GENE SEQUENCE VARIATIONS WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE

Abstract: The present disclosure describes the use of genetic variance information for genes involved in gene pathways in the selection of effective methods of treatment of a disease or condition. The variance information is indicative of the expected response of a patient to a method of treatment. Methods of determining relevant variance information and additional methods of using such variance information are also described.

Description: DESCRIPTION GENE SEQUENCE VARIATIONS WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE BACKGROUND OF THE INVENTION This application concerns the field of mammalian therapeutics and the selection of therapeutic regimens utilizing host genetic information, including gene sequence variances within the human genome in human populations. The information provided below is not admitted to be prior art to the present invention, but is provided solely to assist the understanding of the reader. Many drugs or other treatments are known to have highly variable safety and efficacy in diffe ent individuals. A consequence of such variability is that a given drug or other treatment may be effective in one individual, and ineffective or not well-toler-?ted in another individual. Thus, administration of such a drug to an individual in whom the drug would be ineffective would result in wasted cost and time during which the patient's condition may significantly worsen. Also, administration of a drug to an individual in whom the drug would not be tolerated cculd result in a direct worsening of the patient's condition and could even result in the patient's death. For some drugs, over 90% of the measurable variation in selected pharmacokinetic parameters has been shown to be heritable,. For a limited number of drugs, geneDNA sequence variances have been identified in specific genes that are involved in drug action or metabolism, and these variances have been shown to account for the variable efficacy or safety of the drugs in different individuals. As the sequence of the human genome is completed, and as additional human gene sequence variances are identified, the power of genetic methods for predicting drug response will further increase. In this invention, we address the difficulties that arise in treating the following disease categories: 1 ) neurological and psychiatric disease; 2) pharmacokinetic and dynamic indices including efficacy, absorption, distribution, metabolism, and excretion, as well as safety and toxicity parameters; 3) inflammation and immune disease; 4) endocrine and metabolic disease; 5) cardiovascular and renal disease; and 6) cancer. Neurological and Psychiatric Disease Diseases of the central nervous system (CNS) present unique medical challenges to clinicians, patients, and caregivers These diseases often progress to severely debilitating conditions. Further, the efficacy of available treatments is limited and there are seπous, mostly unpredictable, side effects associated with some drugs The progressive nature of neurological and psychiatric disease makes the passage of time a crucial issue in the treatment process. Specifically, selection of optimal treatment for neurological and psychiatπc diseases is complicated by the fact that it often takes weeks or months to determine if a given therapy is symptomologyproducing a measurable benefit. Thus the current empiπcal approach to prescπbing pharmacotherapy, in which each course of treatment for a given patient is a small expeπment, is unsatisfactory from both a medical and economic perspective. Even when an effective treatment is ultimately identified, it often follows a peπod of ineffective or suboptimal treatment. Pharmacokinetic and Pharmacodynamic Effects The efficacy of a drug is a function of both pharmacodynamic effects and pharmacokinetic effects, or bioavailability. In the present invention, inteφatient vaπabihty in drug safety, tolerabihty and efficacy are discussed in terms of the genetic determinants of inteφatient vaπation in absoφtion, distπbution, metabolism, and excretion, i.e. pharmacokinetic parameters. Adverse drug reactions are a pπncipal cause of the low success rate of drug development programs (less than one in four compounds that enters human clinical testing is ultimately approved for use by the US Food and Drug Administration (FDA)). Adverse drug reactions can be categoπzed as 1 ) mechanism based reactions and 2) idiosyncratic, "unpredictable" effects apparently unrelated to the pπmary pharmacologic action of the compound. Although some side effects appear shortly after administration, in some instances side effects appear only after a latent peπod. Adverse drug reactions can also be categorized into reversible and irreversible effects. The methods of this invention are useful for identifying the genetic basis of both mechanism based and 'idiosyncratic' toxic effects, whether reversible or not. Methods for identifying the genetic sources of inteφatient vaπation in efficacy and mechanism based toxicity may be initially directed to analysis of genes affecting pharmacokinetic parameters, while the genetic causes of idiosyncratic adverse drug reactions are more likely to be attπbutable to genes affecting variation m pharmacodynamic responses or immunological responsiveness. Absoφtion is the first pharmacokinetic parameter to consider when determining the causes of mtersubject vaπation in drug response The relevant genes depend on the route of administration of the compound being evaluated. For orally administered drugs the major steps in absorbtion may occur during exposure to salivary enzymes in the mouth, exposure to the acidic environment of the stomach, exposure to pancreatic digestive enzymes and bile in the small intestine, exposure to enteric bacteria and exposure to cell surface proteins throughout the gastrointestinal tract. For example, uptake of a drug that is absorbed across the gastrointestinal tract by facilitated transport may vary on account of allelic variation in the gene encoding the transporter protein. Many drugs are lipophilic (a property which promotes passive movement across biological membranes). Variation in levels of such drugs may depend, for example, on the enterohepatic circulation of the drug, which may be affected by genetic variation in liver canalicular transporters, or intestinal transporters; alternatively renal reabsorbtion mechanisms may vary among patients as a consequence of gene sequence variances. If a compound is delivered parenterally then absorbtion is not an issue, however transcutaneous administration of a compound may be subject to genetically determined variation in skin absorbtive properties. Once a drug or candidate therapeutic intervention is absorbed, injected or otherwise enters the bloodstream it is distributed to various biological compartments via the blood. The drug may exist free in the blood, or, more commonly, may be bound with varying degrees of affinity to plasma proteins. One classic source of inteφatient variation in drug response is attributable to amino acid polymoφhisms in serum albumin, which affect the binding affinity of drugs such as warfarin. Consequent inteφatient variation in levels of free warfarin have a significant effect on the degree of anticoagulation. From the blood a compound diffuses into and is retained in interstitial and cellular fluids of different organs to different degrees. Inteφatient variation in the levels of a drug in different anatomical compartments may be attributable to variation in the genetically encoded chemical environment of those tissues (cell surface proteins, matrix proteins, cytoplasmic proteins and other factors) Once absorbed by the gastrointestinal tract, compounds encounter detoxifying and metabolizing enzymes in the tissues of the gastrointestinal system. Many of these enzymes are known to be polymoφhic in man and account for well studied variation in pharmacokinetic parameters of many drugs. Subsequently compounds enter the hepatic portal circulation in a process commonly known as first pass. The compounds then encounter a vast array of xenobiotic detoxifying mechanisms in the liver, including enzymes which are expressed solely or at high levels only in liver. These enzymes include the cytochrome P450s, glucuronlytransferases, sulfotransferases, acetyltransferases, methyltransferases, the glutathione conjugating system, flavine monooxygenases, and other enzymes known in the art Polymoφhisms have been detected m all of these metabolizing systems, however the genetic factors responsible for intersubject vanation have only been partially identified, and in some cases not yet identified at all Biotransformation reactions in the liver often have the effect of converting lipophilic compounds into hydrophihc molecules which are then more readily excreted Vaπation in these conjugation reactions may affect half-life and other pharmacokinetic parameters It is important to note that metabolic transformation of a compound not infrequently gives πse to a second or additional compounds that have biological activity greater than, less than, or different from that of the parent compound Metabolic transformation may also be responsible for producing toxic metabolites Biotransformation reactions can be divided into two phases Phase I are oxidation-reduction reactions and phase II are conjugation reactions The enzymes involved in both of these phases are located predominantly in the liver, however biotransformation can also occur in the kidney, gastrointestinal tract, skin, lung and other organs. Phase I reactions occur predominantly m the endoplasmic reticulum, while phase II reactions occur predominantly in the cytosol Both types of reactions can occur in the mitochondπa, nuclear envelope, or plasma membrane One skilled in the art can, for some compounds, make reasonable predictions concerning likely metabolic systems given the structure of the compound Expeπmental means of assessing relevant biotransformation systems are also descπbed Drug-Induced Disease, Disorders or Toxicities Drug-induced disease or toxicity presents a unique senes of challenges to drug developers, as these reactions are often not predictable from prechmcal studies and may not be detected in early clinical tπals involving small numbers of subjects When such effects are detected in later stages of clinical development they often result m termination of a drug development program because, until now, there have been no effective tools to seek the determinants of such reactions When a drug is approved despite some toxicity its clinical use is frequently severely constrained by the possible occurance of adverse reactions in even a small group of patients The likelihood of such a compound becoming first line therapy is small (unless there are no competing products) Thus clinical tπals that lead to detection of genetic causes of adverse events and subsequently to the creation of genetic tests to identify and screen out patients susceptible to such events have the potential to (l) enable approval of compounds for genetically circumscπbed populations or (n) enable repositioning of approved compounds for broader clinical use Similarly, many compounds are not approved due to unimpressive efficacy The identification of genetic determinants of pharmacokinetic vaπation may lead to identification of a genetically defined population in whom a significant response is occuring. Approval of a compound for this population, defined by a genetic diagnostic test, may be the only means of getting regulatory approval for a drug. As healthcare becomes increasingly costly, the ability to allocate healthcare resources effectively becomes increasingly urgent. The use of genetic tests to develop and rationally administer medicines represents a powerful tool for accomplishing more cost effective medical care. Inflammation and Immune Disease In this application, we further address the difficulties that arise in treating inflammatory diseases and other diseases in which modulation of immunologic function provides the basis for therapeutic intervention, including, for example, diseases treated with antiinflammatory, analgesic or antipyretic drugs as well as autacoids, eicosanoids, interleukins, cytokines or their agonists or antagonists. Diseases or conditions involving the inflammatory response or immune system constitute a complex and heterogeneous group of diseases, involving all organ systems from the central nervous system and the circulatory system to the viscera and skin. The diseases may be acute or chronic, or may have an acute stage which later progresses to a chronic condition, or may exhibit a waxing and waning pattern of flare ups and remissions. Due to their wide anatomical distribution, this group of diseases can (collectively) lead to impairment of a wide range of essential physiological functions. The unifying theme in the treatment of these diseases is the modulation of inflammatory mediators or immune function.. The evaluation of long term response to therapy is, for many of these diseases, the most important index of treatment efficacy, due to the progressive nature of inflammatory or immunological diseases. Since it is often difficult to assess the long term effects of treatment over a short observation period (particularly for diseases with a waxing and waning pattern) there is considerable utility in a genetic test that can predict long term outcomes. Many treatments for diseases with significant inflammatory or immunological components are quite costly. Endocine and Metabolic Disease The endocrine system encompasses a number of organs that collectively regulate a wide array of physiologic, metabolic and developmental processes including metabolism, growth, reproduction, development, senescence, behavior, including adaptation to stress, the composition of intracellular and extracellular fluids (e.g. salt and water balance), digestion and wound healing, among other processes. The endocrine organs include the hypothalamus, pituitary gland, thyroid, parathyroid, endocrine pancreas, adrenal gland, gonads, and cells of the gastrointestinal tract, liver, kidneys, heart, pineal gland, and placenta. Endocrine signals can be classified as autocrine, paracrine, or endocrine depending on the distance over which a signal must be transmitted. Endocrine signals are transmitted by hormones including peptides, proteins, steroids and small molecule neuro transmitters. The hormones cany biological signals to target cells. Receptors located on the cell surface (membrane bound) activate intracellular second messenger systems to ultimately alter intracellular metabolism, physiology and cell function. Second messengers systems include adenylate cyclase, guanylate cyclase, phospholipases, and kinases. Some membrane receptors interact with GTP- binding proteins; others produce intracellular signals themselves (for example receptors with tyrosine kinase domains). Other receptors are located intracellularly (for example steroid hormone receptors) and the hormone-receptor complex acts to stimulate intracellular processes such as gene transcription. Regulation in the endocrine system occurs via a complex system of signals transmitted by hormones, neurotransmitters and other small molecules. These signals participate in feedback loops, recruitment of coordinate responses, and cycles or rhythms. The feedback loops function to coordinately stimulate or terminate hormone signals. In this way, communication occurs between cells or tissues that are physically separated. For example, a peripheral endocrine gland may release hormones in response to centrally produced stimulatory hormones, with the peripherally produced substances feeding back on the central nervous system to decrease production of the stimulatory signal. In other systems the action of multiple hormones must be coordinated. For example, female reproductive system requires hypothalamic, pituitary and ovarian signals and also includes effector targets in the breasts, uterus, and vagina. Endocrine signalling systems that are regulated in a coordinated fashion include, for example, the hypothalamic-pituitary- gonadal axis, the hypothalamic-pituitary-adrenal corticotroph axis and the hypothalamic-pituitary-thyroid axis. Within the endocrine system there is integration of endocrine responses that are grouped as. Many hormones are extensively processed prior to secretion. For example in the posterior pituitary gland, a hormone gene encodes a preprohormone that contains several proteins or peptides in contiguous alignment that requires modification prior to becoming an active signaling hormone. The preprohormone after nascent ribosome synthesis then is cut by specific or nonspecific processing proteins to a smaller prohormone within the Golgi apparatus, that then is glycosylated and placed into a secretory granule. Within the secretory granule, the prohormone is then further processed into the active hormone. The active hormone is secreted as a response to physiologic signals and renders the specific biologic function at the target organ or tissue. In this complex protein processing mechanism, there is the possibility of secreting more than one hormones or signaling peptides in the same secretory granule, and as descπbed above, can lead to the delivery of multiple signals to one or more target tissues Assessment of endocπne function can be conducted by quantitation of circulating hormones and metabolic products, stimulation and suppression tests, and anatomic assessment. Aberrations of endocπne disease, disorder, or dysfunction manifests clinically as either a deficiency or a excess of 1 )endocnne function or 2) hormone production, or may be the result of loss of 1) feedback loops, 2) recruitment of hormone signals, or 3) cycles or pulsatile hormone secretion Lastly, there may be genetic determinants of endocπne disease, for example mutations or polymoφhisms in biosynthetic enzymes, hormone receptors, peptide hormone or small molecules, immune surveillance, tumor suppressor genes, and others such that these changes or differences from normally occurnng proteins or molecules alters their functional pattern and the clinical manifestation is then characteπstic of endocπne disease. Endocπne or metabolic disease provide a unique seπes of complications for clinicians, patients, and care givers, the diseases often progress rapidly and disrupts a vast number of major life functions The progressive nature of these disease syndromes makes the passage of time a crucial issue in the treatment process Treatment choices for endocπne or metabolic disorders and their associated pathologies, particularly those affecting major organs, e g coronary, hepatic, renal systems, are often complicated by the fact that it often takes a significant peπod of treatment to determine if a given therapy is effective Accordingly, treatment with the most effective drug or drugs is often delayed while the disease continues to progress. A method that would allow one to predict which patients will respond to a specific therapy would provide physical and psychological benefits As healthcare becomes increasingly inaccessible, the ability to allocate healthcare resources effectively also becomes more important. Cardiovascular and Renal Disease In this application, we address the difficulties that aπse in treating cardiovascular and renal diseases, descπbe methods to enable more effective use of available therapeutics, and methods for developing new therapies Diseases of the cardiovascular and renal systems often progress, over peπods of years to decades, to severely debilitating and life threatening conditions. The efficacy of available treatments is limited and there are side effects associated with many of the drugsused to treat these diseases Due to the progressive nature of many cardiovascular and renal diseases it is of great importance to select an effective therapeutic regimen at the time of diagnosis. The effectiveness of therapy is often assessed by short-term measurements of surrogate markers (e.g. blood pressure, blood lipid levels or blood clotting parameters), however the important endpoints (e.g. myocardial infarction, thromboembolism, renal failure) occur (or are prevented) over the long term. Thus, the tools for selecting optimal therapy for individual patients are currently limited, and as a result some patients receive treatment from which they do not benefit, while other patients may not receive treatment that would produce significant benefit.The current empirical approach to prescribing pharmacotherapy, in which each course of treatment for a given patient is a small experiment (e.g. the selection of effective therapy for blood pressure control), is unsatisfactory from both a medical and economic perspective. Even when an effective treatment is ultimately identified, it often follows a period of ineffective or suboptimal treatment. Methods that would help caregivers predict which patients will exhibit beneficial therapeutic responses to which medications would provide both medical and economic benefits. As healthcare becomes increasingly costly, the ability to rationally allocate healthcare expenditures, and in particular pharmacy resources, becomes increasingly important. The methods of this invention provide a basis for selecting more efficacious pharmacotherapy of cardiovascular and renal diseases. Neoplastic Disorders In this application, we also address the difficulties that arise in treating neoplastic disease. Due to the often rapid progression and life-threatening nature of neoplastic diseases, both early detection and effective treatment are essential. Clearly, there would be great benefit to patients if therapies that will ultimately prove to be ineffective in curbing the progression of disease could be avoided initially, given the cost and often noxious side effects associated with such therapies. Many current therapies for neoplastic disease are targeted against processes such as cell growth and division that occur in both normal and cancerous tissues (albeit at different rates), resulting in pronounced toxicity to normal tissues. Toxic reactions are the most severe in tissues which proliferate rapidly, such as gastrointestinal epithelium and hematopoietic tissues, however serious adverse reactions also occur in other organs occasionally, including heart, kidney, liver, lung and brain. As a consequence of the narrow therapeutic index associated with most antineoplastic treatments, skillful choice of treatments (including the agents used and the dose, if the treatment involves drugs) must be made by the attending physician based not only upon the type of cancer and stage of dissemination, but on a number of additional factors including status of the patient's hematopoietic and myelogenic tissues, hepatic and renal function and age. Knowledge of genetic factors which would impact the choice of treatment based either on optimizing efficacy or minimizing toxicity would greatly benefit cancer patients, because the efficacy of available treatments is limited and there are serious, mostly unpredictable, side effects associated with some drugs. Thus a method that would allow one to predict which patients will exhibit beneficial therapeutic response to a specific medication with minimal adverse effects (often less than half of treated patients, and not infrequently one quarter or less) would provide physical, psychological, and societal benefits. Using such a method, those patients not likely to benefit from aggressive treatment could be offered palliative care. Tumor growth exhibits gompertzian kinetics — growth rate declines with increasing tumor burden. Since chemotherapies are frequently most effective against rapidly growing tumors (low tumor burden), it is imperative that treatment begin immediately after disease detection and that the tumor responds to first-line therapy. Further, selection of optimal treatment for a neoplastic disease is complicated by the fact that it often takes weeks or months to determine if a given therapy is producing a measurable benefit. Thus the current empirical approach to prescribing pharmacotherapy, in which each course of treatment for a given patient is a small experiment, is unsatisfactory from both a medical and economic perspective. Even when an effective treatment is ultimately identified, it often follows a period of ineffective or suboptimal treatment. Neoplastic diseases are related by the fact that they result from the unchecked growth of a previously normal cell, generally thought to be precipitated by one or more mutations in its genetic material. Cancerous cells can undergo gene loss and duplication to become aneuploid or partially polyploid, but usually retain some of the characteristics of their source tissue. Neoplastic cells differ in their ability to form solid tumors, to disseminate from the original site of tumor formation and form metastases, and in their requirements for growth factors, which can include steroid hormones in the case of carcinomas of the prostate or breast. Tumor cells, while having sustained alterations to their genetic material that lead either to a loss of growth inhibition or to a gain of growth function, still produce all the enzymes and other macromolecules required for cell viability. In this regard, they are extremely similar to non-cancerous tissue, and selective poisoning of tumor tissue over normal tissue has for the most part proven elusive. Current chemotherapies mainly target normal cell functions including DNA replication, cell division, RNA transcription, and nucleotide metabolism and are often associated with nausea and vomiting, diarrhea, hair loss, anemia, immune suppression (and consequent increased risk of infection), as well as a host of less common side effects including pulmonary fibrosis, and cardiac, hepatic and renal toxicity. Radiation therapy, often used in the treatment of inoperable tumors such as various brain and laryngeal tumors (but also widely used to treat breast cancer in patients who have had lumpectomies), has the advantage that it can be restricted to a small area, especially when used in conjuction with tissue selective radiosensitizers or radioprotectants. Radiation therapy also targets rapidly proliferating tissues and shares many of the side effects of cytotoxic agents. Minimization of severe toxic reactions to cancer therapy through knowledge of genetic variances in normal tissue that could impact either drug metabolism or cellular repair processes would be an invaluable addition to cancer therapy. Accordingly, a method that would help caregivers predict which patients will exhibit beneficial therapeutic responses to a specific which medication or medications would provide both medical and economic benefits. As healthcare becomes increasingly costly, the ability to rationally allocate healthcare expenditures, and in particular pharmacy resources, also becomes increasingly important. SUMMARY OF THE INVENTION The present invention is concerned generally with the field of identifying an appropriate treatment regimen for a neurological or psychiatric disease, drug- induced disease or disorders, endocrine or metabolic disease, inflammatory disease (or a disease in which modulation of the inflammatory response or the immune system is being tested for therapeutic effect), and cardiovascular and renal diseases, based upon genotype in mammals, particularly in humans. The present invention is additionally concerned generally with the field of pharmacology, specifically pharmacokinetics and toxicology, and more specifically with identifying and predicting inter-patient differences in response to drugs in order to achieve superior efficacy and safety in selected patient populations. It is further concerned with the genetic basis of inter-patient variation in response to therapy, including drug therapy, and with methods for determining and exploiting such differences to improve medical outcomes. Specifically, this invention describes the identification of genes and gene sequence variances useful in the field of therapeutics for optimizing efficacy and safety of drug therapy by allowing prediction of pharmacokinetic and/or toxicologic behavior of specific drugs in specific patients. Relevant pharmacokinetic processes include absoφtion, distribution, metabolism and excretion. Relevant toxicological processes include both dose related and idiosyncratic adverse reactions to drugs, including, for example, hepatotoxicity, blood dyscrasias and immunological reactions. It is further concerned with the genetic basis of inter-patient variation in response to therapy, including drug therapy. Specifically, this invention describes the identification of gene sequence variances useful in the field of therapeutics for optimizing efficacy and safety of drug therapy. These variances may be useful either during the drug development process or in guiding the optimal use of already approved compounds. DNA sequence variances in candidate genes (i.e. genes that may plausibly affect the action of a drug) are tested in clinical trials, leading to the establishment of diagnostic tests useful for improving the development of new pharmaceutical products and/or the more effective use of existing pharmaceutical products. Methods for identifying genetic variances and determining their utility in the selection of optimal therapy for specific patients are also described. In general, the invention relates to methods for identifying patient population subsets that respond to drug therapy with either therapeutic benefit or side effects (i.e. symptomatology prompting concern about safety or other unwanted signs or symptoms). This broad range of pharmacological interactions with receptors, transporters, enzymes and other proteins which are differentially expressed in different populations of cells, e.g., in the CNS, has implications for the design of experiments to identify genetic determinants of drug reponse. In particular, because of the broad pharmacological interactions of compounds being developed as CNS drugs it may be necessary to study the effect of DNA sequence variances in a number of different sets of genes (belonging to different biochemical pathways) in order to identify a sequence variance or set of variances responsible for inteφatient variation in drug response. Methods are described herein for identifying relevant DNA sequence variances and associating them with drug response phenotypes. While the complexity of CNS physiology creates challenges for pharmacogenetic studies, it is also the case that the pharmacological treatment of CNS diseases provides broad scope for the methods of this invention, because (i) the hereditary component of many CNS diseases is well established, indicating a major role of genetic (as opposed to environmental) factors in disease etiology, (ii) the molecular pharmacology of CNS drugs is generally well undertood, providing a rational basis for selecting genes for pharmacogenetic investigation (iii) the heterogeneous responses of patients to CNS drugs suggests that the factors governing response extend beyond presently understood mechanisms; genetic variation can affect virtually all aspects of pharmacology, and is, for the reasons cited above, likely to account for much of the heterogeneity in drug response. In this application we describe methods for improving the treatment of neurological and psychiatric diseases, movement disorders, neurodegenerative diseases, disorders of sensation, and cerebrovascular diseases Specifically, we address the treatment of migraine, pain, epilepsy, schizophrenia, stroke, depression, anxiety, spasticity, Parkinson's disease, dementia, demye nating disease, amyotrophic lateral sclerosis, and Huntington's disease. Specifically, this invention descπbes the identification of genes and gene sequence vaπances useful m the field of therapeutics for optimizing efficacy and safety of drug therapy by allowing prediction of pharmacokinetic and/or toxicologic behavior of specific drugs in specific patients. Relevant pharmacokinetic processes include absoφtion, distribution, metabolism and excretion. Relevant toxicological processes include both dose related and idiosyncratic adverse reactions to drugs, including, for example, hepatotoxicity, blood dyscrasias and immunological reactions The invention also descπbes methods for establishing diagnostic tests useful m (I) the development of, (ii) obtaining regulatory approval for and (in) safe and efficacious clinical use of pharmaceutical products. These vaπances may be useful either duπng the drug development process or in guiding the optimal use of already approved compounds. DNA sequence vaπances in candidate genes (l e. genes that may plausibly affect the action of a drug) are tested in clinical tπals, leading to the establishment of diagnostic tests useful for improving the development of new pharmaceutical products and/or the more effective use of existing pharmaceutical products. Methods for identifying genetic variances and determining their utility in the selection of optimal therapy for specific patients are also descπbed. In general, the invention relates to methods for identifying and dealing effectively with the genetic sources of inteφatient vaπation in drug response, including both variable efficacy as determined by pharmacokinetic vaπability and vaπable toxicity as determined by pharmacokinetic factors or by other genetic factors (e.g. factors responsible for idiosyncratic drug response). This application is directed also to diseases in which abnormal function of the immune system or the inflammatory response is part of the disease process, or m which modulation of immune or inflammatory function is being tested as a therapeutic intervention. Specifically we address the treatment of arthπtis, chronic obstructive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, iflammatory bowel disease, and hepatitis. In this application we further descπbe methods for improving the treatment of endocπne and metabolic diseases. Specifically, we address the treatment of diabetes mellitus and the related metabolic syndrome X, diabetes insipidus, obesity, contraception and infertility, osteoporosis, acne, and alopecia. The methods of this invention are also relevant to devising effective genetic approaches to drug development for endocrine diseases of pituitary, thyroid, parathyroid, adrenal, gonads and secondary sex tissues. While the complexity of cardiovascular and renal physiology creates challenges for pharmacogenetic studies (e.g. selecting the right genes to study, selecting the relevant DNA sequence variances within those genes, constructing sound genetic statistical tests, etc.), it is also the case that the pharmacological treatment of cardiovascular and renal diseases provides broad scope for the methods of this invention, because (i) the hereditary component of many cardiovascular and renal diseases is well established, indicating a major role of genetic (as opposed to environmental) factors in disease etiology, (ii) the molecular pharmacology of cardiovascular and renal drugs is generally well undertood, providing a rational basis for selecting genes for pharmacogenetic investigation (iii) the heterogeneous responses of patients to cardiovascular and renal drugs suggests that the factors governing response extend beyond presently understood mechanisms; genetic variation can affect virtually all aspects of pharmacology, and are, for the reasons cited above, likely to account for much of the heterogeneity in drug response. In this application we describe methods for improving the treatment of cardiovascular and renal diseases. Specifically, we address the treatment of anemia, angina (including coronary artery atherosclerosis), arrhythmias, hypertension, hypotension, myocardial ischemia, heart failure, thrombosis, renal diseases, restenosis, and peripheral vascular disease (including atherosclerosis). The methods of this invention are also relevant to devising effective genetic approaches to drug development for other cardiovascular and renal diseases. Described in the Examples and Tables are pathways, genes and gene sequence variances useful in the genetic analysis of treatment response for each of these diseases, and exemplary compounds being developed to treat each of these diseases, the use of which may be improved by genetic analysis of the type described herein. The inventors have determined that the identification of gene sequence variances in genes that may be involved in drug action are useful for determining whether genetic variances account for variable drug efficacy and safety and for determining whether a given drug or other therapy may be safe and effective in an individual patient. Provided in this invention are identifications of genes and sequence variances which can be useful in connection with predicting differences in response to treatment and selection of appropriate treatment of a disease or condition. A target gene and variances are useful, for example, in pharmacogenetic association studies and diagnostic tests to improve the use of certain drugs or other therapies including, but not limited to, the drug classes and specific drugs identified in the 1999 Physicians' Desk Reference (53rd edition), Medical Economics Data, 1998, the 1995 United States Pharmacopeia -XXIII National Formulary XVIII, Inteφharm Press, 1994, Tables 24-68 or other sources as described below. The terms "disease" or "condition" are commonly recognized in the art and designate the presence of signs and/or symptoms in an individual or patient that are generally recognized as abnormal. Diseases or conditions may be diagnosed and categorized based on pathological changes. Signs may include any objective evidence of a disease such as changes that are evident by physical examination of a patient or the results of diagnostic tests which may include, among others, laboratory tests to determine the presence of DNA sequence variances or variant forms of certain genes in a patient. Symptoms are subjective evidence of disease or a patients condition, i.e. the patients perception of an abnormal condition that differs from normal function, sensation, or appearance, which may include, without limitations, physical disabilities, morbidity, pain, and other changes from the normal condition experienced by an individual. Various diseases or conditions include, but are not limited to; those categorized in standard textbooks of medicine including, without limitation, textbooks of nutrition, allopathic, homeopathic, and osteopathic medicine. In certain aspects of this invention, the disease or condition is selected from the group consisting of the types of diseases listed in standard texts such as Harrison's Principles of Internal Medicine (14th Ed) by Anthony S. Fauci, Eugene Braunwald, Kurt J. Isselbacher, et al. (Editors), McGraw Hill, 1997, or Robbins Pathologic Basis of Disease (6th edition) by Ramzi S. Cotran, Vinay Kumar, Tucker Collins & Stanley L. Robbins, W B Saunders Co., 1998, or the Diagnostic and Statistical Manual of Mental Disorders: DSM-IV (4 th edition), American Psychiatric Press, 1994, or other texts described below. Examples for this invention include, neoplastic disorders such as cancer, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, drug-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstructive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, arrhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease In connection with the methods of this invention, unless otherwise indicated, the term "suffering from a disease or condition" means that a person is either presently subject to the signs and symptoms, or is more likely to develop such signs and symptoms than a normal person in the population. Thus, for example, a person suffering from a condition can include a developing fetus, a person subject to a treatment or environmental condition which enhances the likelihood of developing the signs or symptoms of a condition, or a person who is being given or will be given a treatment which increase the likelihood of the person developing a particular condition. For example, tardive dyskinesia is associated with long-term use of anti- psychotics;dyskinesias, paranoid ideation, psychotic episodes and depression have been associated with use of L-dopa in Parkinson's disease; (and dizziness, diplopia, ataxia, sedation, impaired mentation, weight gain, and other undesired effects have been described for various anticonvulsant therapies. Thus, methods of the present invention which relate to treatments of patients (e.g., methods for selecting a treatment, selecting a patient for a treatment, and methods of treating a disease or condition in a patient) can include primary treatments directed to a presently active disease or condition, secondary treatments which are intended to cause a biological effect relevant to a primary treatment, and prophylactic treatments intended to delay, reduce, or prevent the development of a disease or condition, as well as treatments intended to cause the development of a condition different from that which would have been likely to develop in the absence of the treatment. The term "therapy" refers to a process which is intended to produce a beneficial change in the condition of a mammal, e.g., a human, often referred to as a patient. A beneficial change can, for example, include one or more of: restoration of function, reduction of symptoms, limitation or retardation of progression of a disease, disorder, or condition or prevention, limitation or retardation of deterioration of a patient's condition, disease or disorder. Such therapy can involve, for example, nutritional modifications, administration of radiation, administration of a drug, behavioral modifications, and combinations of these, among others. The term "drug" as used herein refers to a chemical entity or biological product, or combination of chemical entities or biological products, administered to a person to treat or prevent or control a disease or condition. The chemical entity or biological product is preferably, but not necessarily a low molecular weight compound, but may also be a larger compound, for example, an oligomer of nucleic acids, amino acids, or carbohydrates including without limitation proteins, oligonucleotides, ribozymes, DNAzymes, glycoproteins, lipoproteins, and modifications and combinations thereof. A biological product is preferably a monoclonal or polyclonal antibody or fragment thereof such as a variable chain fragment; cells; or an agent or product arising from recombinant technology, such as, without limitation, a recombinant protein, recombinant vaccine, or DNA construct developed for therapeutic, e.g., human therapeutic, use. The term "drug" may include, without limitation, compounds that are approved for sale as pharmaceutical products by government regulatory agencies (e.g., U.S. Food and Drug Administration (USFDA or FDA), European Medicines Evaluation Agency (EMEA), and a world regulatory body governing the International Conference of Harmonization (ICH) rules and guidelines), compounds that do not require approval by government regulatory agencies, food additives or supplements including compounds commonly characterized as vitamins, natural products, and completely or incompletely characterized mixtures of chemical entities including natural compounds or purified or partially purified natural products. The term "drug" as used herein is synonymous with the terms "medicine", "pharmaceutical product", or "product". Most preferably the drug is approved by a government agency for treatment of a specific disease or condition. A "low molecular weight compound" has a molecular weight <5,000 Da, more preferably <2500 Da, still more preferably <1000 Da, and most preferably <700 Da. Those familiar with drug use in medical practice will recognize that regulatory approval for drug use is commonly limited to approved indications, such as to those patients afflicted with a disease or condition for which the drug has been shown to be likely to produce a beneficial effect in a controlled clinical trial. Unfortunately, it has generally not been possible with current knowledge to predict which patients will have a beneficial response, with the exception of certain diseases such as bacterial infections where suitable laboratory methods have been developed. Likewise, it has generally not been possible to determine in advance whether a drug will be safe in a given patient. Regulatory approval for the use of most drugs is limited to the treatment of selected diseases and conditions. The descriptions of approved drug usage, including the suggested diagnostic studies or monitoring studies, and the allowable parameters of such studies, are commonly described in the "label" or "insert" which is distributed with the drug. Such labels or inserts are preferably required by government agencies as a condition for marketing the drug and are listed in common references such as the Physicians Desk Reference (PDR). These and other limitations or considerations on the use of a drug are also found in medical journals, publications such as pharmacology, pharmacy or medical textbooks including, without limitation, textbooks of nutrition, allopathic, homeopathic, and osteopathic medicine. Many widely used drugs are effective in a minority of patients receiving the drug, particularly when one controls for the placebo effect. For example, the PDR shows that about 45% of patients receiving Cognex (tacrine hydrochloride) for Alzheimer's disease show no change or minimal worsening of their disease, as do about 68%o of controls (including about 5%> of controls who were much worse). About 58%> of Alzheimer's patients receiving Cognex were minimally improved, compared to about 33%> of controls, while about 2% of patients receiving Cognex were much improved compared to about 1% of controls. Thus a tiny fraction of patients had a significant benefit. Response to treatments for amyotrophic lateral sclerosis are likewise minimal. Thus, in a first aspect, the invention provides a method for selecting a treatment for a patient suffering from a disease or condition by determining whether or not a gene or genes in cells of the patient (in some cases including both normal and disease cells, such as cancer cells) contain at least one sequence variance which is indicative of the effectiveness of the treatment of the disease or condition. The gene or genes (along with exemplary variances) are specified herein, in Tables 1-6, 12-17, and 18-23. Preferably the at least one variance includes a plurality of variances which may provide a haplotype or haplotypes. Preferably the joint presence of the plurality of variances is indicative of the potential effectiveness or safety of the treatment in a patient having such plurality of vaπances. The plurality of variances may each be indicative of the potential effectiveness of the treatment, and the effects of the individual variances may be independent or additive, or the plurality of variances may be indicative of the potential effectiveness if at least 2, 3, 4, or more appear jointly. The plurality of variances may also be combinations of these relationships. The plurality of variances may include variances from one, two, three or more gene loci. In preferred embodiments of aspects of the invention involving genes relating to psychiatric or neurological disease or related conditions or the other diseases or conditions identified herein, or to phamacological responses to compounds used to treat such diseases or conditions, the gene product is involved in a function as described in the Background of the Invention or otherwise described herein. In some cases, the selection of a method of treatment, i.e., a therapeutic regimen, may incoφorate selection of one or more from a plurality of medical therapies. Thus, the selection may be the selection of a method or methods which is/are more effective or less effective than certain other therapeutic regimens (with either having varying safety parameters). Likewise or in combination with the preceding selection, the selection may be the selection of a method or methods, which is safer than certain other methods of treatment in the patient. The selection may involve either positive selection or negative selection or both, meaning that the selection can involve a choice that a particular method would be an appropriate method to use and/or a choice that a particular method would be an inappropriate method to use. Thus, in certain embodiments, the presence of the at least one variance is indicative that the treatment will be effective or otherwise beneficial (or more likely to be beneficial) in the patient. Stating that the treatment will be effective means that the probability of beneficial therapeutic effect is greater than in a person not having the appropriate presence or absence of particular variances. In other embodiments, the presence of the at least one variance is indicative that the treatment will be ineffective or contra-indicated for the patient. For example, a treatment may be contra-indicated if the treatment results, or is more likely to result, in undesirable side effects, or an excessive level of undesirable side effects. A determination of what constitutes excessive side-effects will vary, for example, depending on the disease or condition being treated, the availability of alternatives, the expected or experienced efficacy of the treatment, and the tolerance of the patient. As for an effective treatment, this means that it is more likely that desired effect will result from the treatment administration in a patient with a particular variance or variances than in a patient who has a different variance or variances. Also in preferred embodiments, the presence of the at least one variance is indicative that the treatment is both effective and unlikely to result in undesirable effects or outcomes, or vice versa (is likely to have undesirable side effects but unlikely to produce desired therapeutic effects). In reference to response to a treatment, the term "tolerance" refers to the ability of a patient to accept a treatment, based, e.g., on deleterious effects and/or effects on lifestyle. Frequently, the term principally concerns the patients perceived magnitude of deleterious effects such as nausea, weakness, dizziness, and diarrhea, among others. Such experienced effects can, for example, be due to general or cell- specific toxicity, activity on non-target cells, cross-reactivity on non-target cellular constituents (non-mechanism based), and/or side effects of activity on the target cellular substituents (mechanism based), or the cause of toxicity may not be understood. In any of these circumstances one may identify an association between the undesirable effects and variances in specific genes. Adverse responses to drugs constitute a major medical problem, as shown in two recent meta-analyses (Lazarou, J. et al, Incidence of adverse drug reactions in hospitalized patients: a meta-analysis of prospective studies, JAMA 279:1200-1205, 1998; Bonn, Adverse drug reactions remain a major cause of death, Lancet 351 :1183, 1998). An estimated 2.2 million hospitalized patients in the United Stated had serious adverse drug reactions in 1994, with an estimated 106,000 deaths (Lazarou et al). To the extent that some of these adverse events are due to genetically encoded biochemical diversity among patients in pathways that effect drug action, the identification of variances that are predictive of such effects will allow for more effective and safer drug use. In embodiments of this invention, the variance or variant form or forms of a gene is/are associated with a specific response to a drug. The frequency of a specific variance or variant form of the gene may correspond to the frequency of an efficacious response to administration of a drug. Alternatively, the frequency of a specific variance or variant form of the gene may correspond to the frequency of an adverse event resulting from administration of a drug. Alternatively the frequency of a specific variance or variant form of a gene may not correspond closely with the frequency of a beneficial or adverse response, yet the variance may still be useful for identifying a patient subset with high response or toxicity incidence because the variance may account for only a fraction of the patients with high response or toxicity. In such a case the preferred course of action is identification of a second or third or additional variances that permit identification of the patient groups not usefully identified by the first variance. Preferably, the drug will be effective in more than 20%> of individuals with one or more specific variances or variant forms of the gene, more preferably in 40% and most preferably in >60%o. In other embodiments, the drug will be toxic or create clinically unacceptable side effects in more than 10%> of individuals with one or more variances or variant forms of the gene, more preferably in >30%, more preferably in >50%, and most preferably in >70%o or in more than 90%. Also in other embodiments, the method of selecting a treatment includes eliminating or excluding a treatment, where the presence or absence of the at least one variance is indicative that the treatment will be ineffective or contra-indicated, e.g., would result in excessive weight gain. In other preferred embodiments, in cases in which undesirable side-effects may occur or are expected to occur from a particular therapeutic treatment, the selection of a method of treatment can include identifying both a first and second treatment, where the first treatment is effective to treat the disease or condition, and the second treatment reduces a deleterious effect or enhance efficacy of the first treatment. The phrase "eliminating a treatment" (similarly for exluding a treatment) refers to removing a possible treatment from consideration, e.g., for use with a particular patient based on the presence or absence of a particular variance(s) in one or more genes in cells of that patient, or to stopping the administration of a treatment. Usually, the treatment will involve the administration of a compound preferentially active or safe in patients with a form or forms of a gene, where the gene is one identified herein. The administration may involve a combination of compounds. Thus, in preferred embodiments, the method involves identifying such an active compound or combination of compounds, where the compound is less active or is less safe or both when administered to a patient having a different form of the gene. Also in preferred embodiments, the method of selecting a treatment involves selecting a method of administration of a compound, combination of compounds, or pharmaceutical composition, for example, selecting a suitable dosage level and/or frequency of administration, and/or mode of administration of a compound. The method of administration can be selected to provide better, preferably maximum therapeutic benefit. In this context, "maximum" refers to an approximate local maximum based on the parameters being considered, not an absolute maximum. Also in this context, a "suitable dosage level" refers to a dosage level which provides a therapeutically reasonable balance between pharmacological effectiveness and deleterious effects. Often this dosage level is related to the peak or average serum levels resulting from administration of a drug at the particular dosage level. Similarly, a "frequency of administration" refers to how often in a specified time period a treatment is administered, e.g., once, twice, or three times per day, every other day, once per week, etc. For a drug or drugs, the frequency of administration is generally selected to achieve a pharmacologically effective average or peak serum level without excessive deleterious effects (and preferably while still being able to have reasonable patient compliance for self-administered drugs). Thus, it is desirable to maintain the serum level of the drug within a therapeutic window of concentrations for the greatest percentage of time possible without such deleterious effects as would cause a prudent physician to reduce the frequency of administration for a particular dosage level. A particular gene or genes can be relevant to the treatment of more than one disease or condition, for example, the gene or genes can have a role in the initiation, development, course, treatment, treatment outcomes, or health-related quality of life outcomes of a number of different diseases, disorders, or conditions. Thus, in preferred embodiments, the disease or condition or treatment of the disease or condition is any which involves a gene from the gene list described herein as Tables 1-6, 12-17, and 18-23. Determining the presence of a particular variance or plurality of variances in a particular gene in a patient can be performed in a variety of ways. In preferred embodiments, the detection of the presence or absence of at least one variance involves amplifying a segment of nucleic acid including at least one of the at least one variances. Preferably a segment of nucleic acid to be amplified is 500 nucleotides or less in length, more preferably 100 nucleotides or less, and most preferably 45 nucleotides or less. Also, preferably the amplified segment or segments includes a plurality of variances, or a plurality of segments of a gene or of a plurality of genes. In other embodiments, e.g., where a haplotype is to be determined, the segment of nucleic acid is at least 500 nucleotides in length, or at least 2 kb in length, or at least 5 kb in length. In preferred embodiments, determining the presence of a set of variances in a specific gene related to treatment of disease, disorders, or dysfunctions or other related genes, or genes listed in Tables 1-6, 12-17, and 18-23, includes a haplotyping test that requires allele specific amplification of a large DNA segment of no greater than 25,000 nucleotides, preferably no greater than 10,000 nucleotides and most preferably no greater than 5.000 nucleotides. Alternatively one allele may be enriched by methods other than amplification prior to determining genotypes at specific variant positions on the enriched allele as a way of determining haplotypes. Preferably the determination of the presence or absence of a haplotype involves determining the sequence of the variant sites by methods such as chain terminating DNA sequencing or minisequencing, or by oligonucleotide hybridization or by mass spectrometry. For the use of mass spectrometry, the method can involve detection of the mass of a fragment or fragments and can further involve inferring the genotype (e.g., the specific variance at a site) from the masses determined. The term "genotype" in the context of this invention refers to the alleles present in DNA from a subject or patient, where an allele can be defined by the particular nucleotide(s) present in a nucleic acid sequence at a particular site(s). Often a genotype is the nucleotide(s) present at a single polymoφhic site known to vary in the human population. In preferred embodiments, the detection of the presence or absence of the at least one variance involves contacting a nucleic acid sequence corresponding to one of the genes identified above or a product of such a gene with a probe. The probe is able to distinguish a particular form of the gene or gene product or the presence or a particular variance or variances, e.g., by differential binding or hybridization. Thus, exemplary probes include nucleic acid hybridization probes, peptide nucleic acid probes, nucleotide-containing probes which also contain at least one nucleotide analog, and antibodies, e.g., monoclonal antibodies, and other probes as discussed herein. Those skilled in the art are familiar with the preparation of probes with particular specificities. Those skilled in the art will recognize that a variety of variables can be adjusted to optimize the discrimination between two variant forms of a gene, including changes in salt concentration, temperature, pH and addition of various compounds that affect the differential affinity of GC vs. AT base pairs, such as tetramethyl ammonium chloride. (See Current Protocols in Molecular Biology by F.M. Ausubel, R. Brent, R.E. Kngston, D.D. Moore, J.D. Seidman, K. Struhl, and V.B. Chanda (editors, John Wiley & Sons.) In other preferred embodiments, determining the presence or absence of the at least one variance involves sequencing at least one nucleic acid sample. The sequencing involves sequencing of a portion or portions of a gene and/or portions of a plurality of genes which includes at least one variance site, and may include a plurality of such sites. Preferably, the portion is 500 nucleotides or less in length, more preferably 100 nucleotides or less, and most preferably 45 nucleotides or less in length. Such sequencing can be carried out by various methods recognized by those skilled in the art, including use of dideoxy termination methods (e.g., using dye-labeled dideoxy nucleotides) and the use of mass spectrometric methods. In addition, mass spectrometric methods may be used to determine the nucleotide present at a variance site. In preferred embodiments in which a plurality of variances is determined, the plurality of variances can constitute a haplotype or collection of haplotypes. Preferably the methods for determining genotypes or haplotypes are designed to be sensitive to all the common genotypes or haplotypes present in the population being studied (for example, a clinical trial population). The terms "variant form of a gene", "form of a gene", or "allele" refer to one specific form of a gene in a population, the specific form differing from other forms of the same gene in the sequence of at least one, and frequently more than one, variant sites within the sequence of the gene. The sequences at these variant sites that differ between different alleles of the gene are termed "gene sequence variances" or "variances" or "variants". The term "alternative form" refers to an allele that can be distinguished from other alleles by having distinct variances at least one, and frequently more than one, variant sites within the gene sequence. Other terms known in the art to be equivalent include mutation and polymoφhism, although mutation is often used to refer to an allele associated with a deleterious phenotype. In preferred aspects of this invention, the variances are selected from the group consisting of the variances listed in the variance tables herein or in a patent or patent application referenced and incoφorated by reference in this disclosure. In the methods utilizing variance presence or absence, reference to the presence of a variance or variances means particular variances, i.e., particular nucleotides at particular polymoφhic sites, rather than just the presence of any variance in the gene. Variances occur in the human genome at approximately one in every 500 - 1 ,000 bases within the human genome when two alleles are compared. When multiple alleles from unrelated individuals are compared the density of variant sites increases as different individuals, when compared to a reference sequence, will often have sequence variances at different sites. At most variant sites there are only two alternative nucleotides involving the substitution of one base for another or the insertion/deletion of one or more nucleotides. Within a gene there may be several variant sites. Variant forms of the gene or alternative alleles can be distinguished by the presence of alternative variances at a single variant site, or a combination of several different variances at different sites (haplotypes). It is estimated that there are 3,300,000,000 bases in the sequence of a single haploid human genome. All human cells except germ cells are normally diploid. Each gene in the genome may span 100-10,000,000 bases of DNA sequence or 100-20,000 bases of mRNA. It is estimated that there are between 60,000 and 150,000 genes in the human genome. The "identification" of genetic variances or variant forms of a gene involves the discovery of variances that are present in a population. The identification of variances is required for development of a diagnostic test to determine whether a patient has a variant form of a gene that is known to be associated with a disease, condition, or predisposition or with the efficacy or safety of the drug. Identification of previously undiscovered genetic variances is distinct from the process of "determining" the status of known variances by a diagnostic test (often referred to as genotyping). The present invention provides exemplary variances in genes listed in the gene tables, as well as methods for discovering additional variances in those genes and a comprehensive written description of such additional possible variances. Also described are methods for DNA diagnostic tests to determine the DNA sequence at a particular variant site or sites. The process of "identifying" or discovering new variances involves comparing the sequence of at least two alleles of a gene, more preferably at least 10 alleles and most preferably at least 50 alleles (keeping in mind that each somatic cell has two alleles). The analysis of large numbers of individuals to discover variances in the gene sequence between individuals in a population will result in detection of a greater fraction of all the variances in the population. Preferably the process of identifying reveals whether there is a variance within the gene; more preferably identifying reveals the location of the variance within the gene; more preferably identifying provides knowledge of the sequence of the nucleic acid sequence of the variance, and most preferably identifying provides knowledge of the combination of different variances that comprise specific variant forms of the gene (referred to as alleles). In identifying new variances it is often useful to screen different population groups based on racial, ethnic, gender, and/or geographic origin because particular variances may differ in frequency between such groups. It may also be useful to screen DNA from individuals with a particular disease or condition of interest because they may have a higher frequency of certain variances than the general population. The process of genotyping involves using diagnostic tests for specific variances that have already been identified. It will be apparent that such diagnostic tests can only be performed after variances and variant forms of the gene have been identified. Identification of new variances can be accomplished by a variety of methods, alone or in combination, including, for example, DNA sequencing, SSCP, heteroduplex analysis, denaturing gradient gel electrophoresis (DGGE), heteroduplex cleavage (either enzymatic as with T4 Endonuclease 7, or chemical as with osmium tetroxide and hydroxylamine), computational methods (described herein), and other methods described herein as well as others known to those skilled in the art. (See, for example: Cotton, R.G.H., Slowly but surely towards better scanning for mutations, Trends in Genetics 13(2): 43-6, 1997 or Current Protocols in Human Genetics by N.C. Dracoli, J.L. Haines, B.R. Korf, D.T. Moir, C.C. Morton, C.E. Seidman, D.R. Smith, and A. Boyle (editors), John Wiley & Sons.) In the context of this invention, the term "analyzing a sequence" refers to determining at least some sequence information about the sequence, e.g., determining the nucleotides present at a particular site or sites in the sequence, particularly sites that are known to vary in a population, or determining the base sequence of all or of a portion of the particular sequence. In the context of this invention, the term "haplotype" refers to a cis arrangement of two or more polymoφhic nucleotides, i.e., variances, on a particular chromosome, e.g., in a particular gene. The haplotype preserves information about the phase of the polymoφhic nucleotides - that is, which set of vaπances were inherited from one parent, and which from the other. A genotyping test does not provide information about phase. For example, an individual heterozygous at nucleotide 25 of a gene (both A and C are present) and also at nucleotide 100 (both G and T are present) could have haplotypes 25 A - 100G and 25C - 100T, or alternatively 25 A - 100T and 25C - 100G. Only a haplotyping test can discriminate these two cases definitively. The terms "variances", "variants" and "polymoφhisms", as used herein, may also refer to a set of variances, haplotypes or a mixture of the two, unless otherwise indicated. Further, the term variance, variant or polymoφhism (singular), as used herein, also encompasses a haplotype unless otherewise indicated. This usage is intended to minimize the need for cumbersome phrases such as: "...measure correlation between drug response and a variance, variances, haplotype, haplotypes or a combination of variances and haplotypes....", throughout the application. Instead, the italicized text in the foregoing sentence can be represented by the word "variance", "variant" or "polymoφhism". Similarly, the term genotype, as used herein, means a procedure for determining the status of one or more variances in a gene, including a set of variances comprising a haplotype. Thus phrases such as "...genotype a patient..." refer to determining the status of one or more variances, including a set of variances for which phase is known (i.e. a haplotype). In preferred embodiments of this invention, the frequency of the variance or variant form of the gene in a population is known. Measures of frequency known in the art include "allele frequency", namely the fraction of genes in a population that have one specific variance or set of variances. The allele frequencies for any gene should sum to 1. Another measure of frequency known in the art is the "heterozygote frequency" namely, the fraction of individuals in a population who carry two alleles, or two forms of a particular variance or variant form of a gene, one inherited from each parent. Alternatively, the number of individuals who are homozygous for a particular form of a gene may be a useful measure. The relationship between allele frequency, heterozygote frequency, and homozygote frequency is described for many genes by the Hardy- Weinberg equation, which provides the relationship between allele frequency, heterozygote frequency and homozygote frequency in a freely breeding population at equilibrium. Most human variances are substantially in Hardy- Weinberg equilibrium. In a preferred aspect of this invention, the allele frequency, heterozygote frequency, and homozygote frequencies are determined experimentally. Preferably a variance has an allele frequency of at least 0.01, more preferably at least 0.05, still more preferably at least 0.10. However, the allele may have a frequency as low as 0.001 if the associated phenotype is, for example, a rare form of toxic reaction to a treatment or drug. Beneficial responses may also be rare. In this regard, "population" refers to a defined group of individuals or a group of individuals with a particular disease or condition or individuals that may be treated with a specific drug identified by, but not limited to geographic, ethnic, race, gender, and/or cultural indices. In most cases a population will preferably encompass at least ten thousand, one hundred thousand, one million, ten million, or more individuals, with the larger numbers being more preferable. In preferred embodiments of this invention, the population refers to individuals with a specific disease or condition that may be treated with a specific drug. In embodiments of this invention, the allele frequency, heterozygote frequency, or homozygote frequency of a specific variance or variant form of a gene is known. In preferred embodiments of this invention, the frequency of one or more variances that may predict response to a treatment is determined in one or more populations using a diagnostic test. It should be emphasized that it is currently not generally practical to study an entire population to establish the association between a specific disease or condition or response to a treatment and a specific variance or variant form of a gene. Such studies are preferably performed in controlled clinical trials using a limited number of patients that are considered to be representative of the population with the disease. Since drug development programs are generally targeted at the largest possible population, the study population will generally consist of men and women, as well as members of various racial and ethnic groups, depending on where the clinical trial is being performed. This is important to establish the efficacy of the treatment in all segments of the population. In the context of this invention, the term "probe" refers to a molecule that detectably distinguishes between target molecules differing in structure. Detection can be accomplished in a variety of different ways depending on the type of probe used and the type of target molecule. Thus, for example, detection may be based on discrimination of activity levels of the target molecule, but preferably is based on detection of specific binding. Examples of such specific binding include antibody binding and nucleic acid probe hybridization. Thus, for example, probes can include enzyme substrates, antibodies and antibody fragments, and nucleic acid hybridization probes. Thus, in preferred embodiments, the detection of the presence or absence of the at least one variance involves contacting a nucleic acid sequence which includes a variance site with a probe, preferably a nucleic acid probe, where the probe preferentially hybridizes with a form of the nucleic acid sequence containing a complementary base at the variance site as compared to hybridization to a form of the nucleic acid sequence having a non-complementary base at the variance site, where the hybridization is carried out under selective hybridization conditions. Such a nucleic acid hybridization probe may span two or more variance sites. Unless otherwise specified, a nucleic acid probe can include one or more nucleic acid analogs, labels or other substituents or moieties so long as the base- pairing function is retained. As is generally understood, administration of a particular treatment, e.g., administration of a therapeutic compound or combination of compounds, is chosen depending on the disease or condition that is to be treated. Thus, in certain preferred embodiments, the disease or condition is one for which administration of a treatment is expected to provide a therapeutic benefit; in certain embodiments, the compound is a compound identified herein, e g , in a drug table (Tables 24-68) As used herein, the terms "effective" and "effectiveness" includes both pharmacological effectiveness and physiological safety Pharmacological effectiveness refers to the ability of the treatment to result m a desired biological effect in the patient. Physiological safety refers to the level of toxicity, or other adverse physiological effects at the cellular, organ and/or organism level (often referred to as side-effects) resulting from administration of the treatment On the other hand, the term "ineffective" indicates that a treatment does not provide sufficient pharmacological effect to be therapeutically useful, even in the absence of deleteπous effects, at least m the unstratified population. (Such a treatment may be ineffective in a subgroup that can be identified by the presence of one or more sequence vaπances or alleles ) "Less effective" means that the treatment results in a therapeutically significant lower level of pharmacological effectiveness and/or a therapeutically greater level of adverse physiological effects, e g , greater liver toxicity Thus, m connection with the administration of a drug, a drug which is "effective against" a disease or condition indicates that administration in a clinically appropπate manner results in a beneficial effect for at least a statistically significant fraction of patients, such as a improvement of symptoms, a cure, a reduction in disease load, reduction in tumor mass or cell numbers, extension of life, improvement in quality of life, or other effect generally recognized as positive by medical doctors familiar with treating the particular type of disease or condition Effectiveness is measured in a particular population. In conventional drug development the population is generally every subject who meets the enrollment cπteπa (I e. has the particular form of the disease or condition being treated) It is an aspect of the present invention that segmentation of a study population by genetic cπteπa can provide the basis for identifying a subpopulation m which a drug is effective against the disease or condition being treated. The term "deletenous effects" refers to physical effects in a patient caused by administration of a treatment which are regarded as medically undesirable Thus, for example, deleteπous effects can include a wide spectrum of toxic effects injuπous to health such as death of normally functioning cells when only death of diseased cells is desired, nausea, fever, inability to retain food, dehydration, damage to cπtical organs such as arrythmias, renal tubular necrosis, fatty liver, or pulmonary fibrosis leading to coronary, renal, hepatic, or pulmonary insufficiency among many others. In this regard, the term "contra-indicated" means that a treatment results in deleterious effects such that a prudent medical doctor treating such a patient would regard the treatment as unsuitable for administration. Major factors in such a determination can include, for example, availability and relative advantages of alternative treatments, consequences of non- treatment, and permanency of deleterious effects of the treatment. It is recognized that many treatment methods, e.g., administration of certain compounds or combinations of compounds, may produce side-effects or other deleterious effects in patients. Such effects can limit or even preclude use of the treatment method in particular patients, or may even result in irreversible injury, dysfunction, or death of the patient. Thus, in certain embodiments, the variance information is used to select both a first method of treatment and a second method of treatment. Usually the first treatment is a primary treatment which provides a physiological effect directed against the disease or condition or its symptoms. The second method is directed to reducing or eliminating one or more deleterious effects or enhancing efficacy of the first treatment, e.g., to reduce a general toxicity or to reduce a side effect of the primary treatment. Thus, for example, the second method can be used to allow use of a greater dose or duration of the first treatment, or to allow use of the first treatment in patients for whom the first treatment would not be tolerated or would be contra-indicated in the absence of a second method to reduce deleterious effects or to potentiate the effectiveness of the first treatment. In a related aspect, the invention concerns a method for providing a correlation between a patient genotype and effectiveness of a treatment, by determining the presence or absence of a particular known variance or variances in cells of a patient for a gene from Tables 1-6, 12-17, and 18-23, or other gene related to neurological disease or other disease identified herein, and providing a result indicating the expected effectiveness of a treatment for a disease or condition. The result may be formulated by comparing the genotype of the patient with a list of variances indicative of the effectiveness of a treatment, e.g., administration of a drug described herein. The determination may be by methods as described herein or other methods known to those skilled in the art. In a related aspect, the invention provides a method for selecting a method of treatment for a patient suffering from a disease or condition as identified herein by comparing at least one variance in at least one gene in the patient, with a list of variances in the gene from Tables 1 -6, 12-17, and 18-23, or other gene related to a disease or condition listed herein, which are indicative of the effectiveness of at least one method of treatment. Preferably the comparison involves a plurality of variances or a haplotype indicative of the effectiveness of at least one method of treatment. Also, preferably the list of variances includes a plurality of variances. Similar to the above aspect, in preferred embodiments the at least one method of treatment involves the administration of a compound effective in at least some patients with a disease or condition; the presence or absence of the at least one variance is indicative that the treatment will be effective in the patient; and/or the presence or absence of the at least one variance is indicative that the treatment will be ineffective or contra-indicated in the patient; and/or the treatment is a first treatment and the presence or absence of the at least one variance is indicative that a second treatment will be beneficial to reduce a deleterious effect of or potentiate the effectiveness of the first treatment; and/or the at least one treatment is a plurality of methods of treatment. For a plurality of treatments, preferably the selecting involves determining whether any of the methods of treatment will be more effective than at least one other of the plurality of methods of treatment. Yet other embodiments are provided as described for the preceding aspect in connection with methods of treatment using administration of a compound; treatment of various diseases, and variances in particular genes. In the context of variance information in the methods of this invention, the term "list" refers to one or more, preferably at least 2, 3, 4, 5, 7, or 10 variances that have been identified for a gene of potential importance in accounting for inter- individual variation in treatment response. Preferably there is a plurality of variances for the gene, preferably a plurality of variances for the particular gene. Preferably, the list is recorded in written or electronic form. For example, identified variances of identified genes are recorded for some of the genes in Tables 12-17 and 18-23; additional variances for genes in Tables 1-6 can be readily identified by one skilled in the art using any of a variety of methods. The list may also contain haplotypes, either alone or with other variances. In addition to the basic method of treatment, often the mode of administration of a given compound as a treatment for a disease or condition in a patient is significant in determining the course and/or outcome of the treatment for the patient. Thus, the invention also provides a method for selecting a method of administration of a compound to a patient suffering from a disease or condition, by determining the presence or absence of at least one variance in cells of the patient in at least one identified gene from Tables 1-6, 12-17, and 18-23, where such presence or absence is indicative of an appropriate method of administration of the compound. Preferably, the selection of a method of treatment (a treatment regimen) involves selecting a dosage level or frequency of administration or route of administration of the compound or combinations of those parameters. In preferred embodiments, two or more compounds are to be administered, and the selecting involves selecting a method of administration for one, two, or more than two of the compounds, jointly, concurrently, or separately. As understood by those skilled in the art, such plurality of compounds may be used in combination therapy, and thus may be formulated in a single drug, or may be separate drugs administered concurrently, serially, or separately. Other embodiments are as indicated above for selection of second treatment methods, methods of identifying variances, and methods of treatment as described for aspects above. In another aspect, the invention provides a method for selecting a patient for administration of a method of treatment for a disease or condition, or of selecting a patient for a method of administration of a treatment, by comparing the presence or absence of at least one variance in a gene as identified above in cells of a patient, with a list of variances in the gene, where the presence or absence of the at least one variance is indicative that the treatment or method of administration will be effective in the patient. If the at least one variance is present in the patient's cells, then the patient is selected for administration of the treatment. In preferred embodiments, the disease or the method of treatment is as described in aspects above, specifically including, for example, those described for selecting a method of treatment. In another aspect, the invention provides a method for identifying a subset of patients with enhanced or diminished response or tolerance to a treatment method or a method of administration of a treatment where the treatment is for a disease or condition in the patient. The method involves correlating one or more variances in one or more genes as identified in aspects above in a plurality of patients with response to a treatment or a method of administration of a treatment. The correlation may be performed by determining the one or more variances in the one or more genes in the plurality of patients and correlating the presence or absence of each of the variances (alone or in various combinations) with the patient's response to treatment. The variances may be previously known to exist or may also be determined in the present method or combinations of prior information and newly determined information may be used. The enhanced or diminished response should be statistically significant, preferably such that p = 0.10 or less, more preferably 0.05 or less, and most preferably 0.02 or less. A positive correlation between the presence of one or more variances and an enhanced response to treatment is indicative that the treatment is particularly effective in the group of patients having those variances. A positive correlation of the presence of the one or more variances with a diminished response to the treatment is indicative that the treatment will be less effective in the group of patients having those variances. Such information is useful, for example, for selecting or de-selecting patients for a particular treatment or method of administration of a treatment, or for demonstrating that a group of patients exists for which the treatment or method of treatment would be particularly beneficial or contra-indicated. Such demonstration can be beneficial, for example, for obtaining government regulatory approval for a new drug or a new use of a drug In preferred embodiments, the variances are in at least one of the identified genes listed on Tables 1-6, 12-17, and 18-23, or are particular variances described herein. Also, preferred embodiments include drugs, treatments, variance identification or determination, determination of effectiveness, and/or diseases as described for aspects above or otherwise described herein. In preferred embodiments, the correlation of patient responses to therapy according to patient genotype is carried out in a clinical trial, e.g., as described herein according to any of the variations described. Detailed description of methods for associating variances with clinical outcomes using clinical trials are provided below. Further, in preferred embodiments the correlation of pharmacological effect (positive or negative) to treatment response according to genotype or haplotype in such a clinical trial is part of a regulatory submission to a government agency leading to approval of the drug. Most preferably the compound or compounds would not be approvable in the absence of the genetic information allowing identification of an optimal responder population. As indicated above, in aspects of this invention involving selection of a patient for a treatment, selection of a method or mode of administration of a treatment, and selection of a patient for a treatment or a method of treatment, the selection may be positive selection or negative selection. Thus, the methods can include eliminating or excluding a treatment for a patient, eliminating or excluding a method or mode of administration of a treatment to a patient, or elimination or exclusion of a patient for a treatment or method of treatment. Also, in methods involving identification and/or comparison of variances present in a gene of a patient, the methods can involve such identification or comparison for a plurality of genes. Preferably, the genes are functionally related to the same disease or condition, or to the aspect of disease pathophysiology that is being subjected to pharmacological manipulation by the treatment (e.g., a drug), or to the activation or inactivation or elimination of the drug, and more preferably the genes are involved in the same biochemical process or pathway. In another aspect, the invention provides a method for identifying the forms of a gene in an individual, where the gene is one specified as for aspects above, by determining the presence or absence of at least one variance in the gene. In preferred embodiments, the at least one variance includes at least one variance selected from the group of variances identified in variance tables herein. Preferably, the presence or absence of the at least one variance is indicative of the effectiveness of a therapeutic treatment in a patient suffering from a disease or condition and having cells containing the at least one variance. The presence or absence of the variances can be determined in any of a variety of ways as recognized by those skilled in the art. For example, the nucleotide sequence of at least one nucleic acid sequence which includes at least one variance site (or a complementary sequence) can be determined, such as by chain termination methods, hybridization methods or by mass spectrometric methods. Likewise, in preferred embodiments, the determining involves contacting a nucleic acid sequence or a gene product of one of one of the genes with a probe that specifically identifies the presence or absence of a form of the gene. For example, a probe, e.g., a nucleic acid probe, can be used which specifically binds, e.g., hybridizes, to a nucleic acid sequence corresponding to a portion of the gene and which includes at least one variance site under selective binding conditions. As described for other aspects, determining the presence or absence of at least two variances and their relationship on the two gene copies present in a patient can constitute determining a haplotype or haplotypes. Other preferred embodiments involve variances related to types of treatment, drug responses, diseases, nucleic acid sequences, and other items related to variances and variance determination as described for aspects above. In yet another aspect, the invention provides a pharmaceutical composition which includes a compound which has a differential effect in patients having at least one copy, or alternatively, two copies of a form of a gene as identified for aspects above and a pharmaceutically acceptable earner, excipient, or diluent. The composition is adapted to be preferentially effective to treat a patient with cells containing the one, two, or more copies of the form of the gene. In preferred embodiments of aspects involving pharmaceutical compositions, active compounds, or drugs, the material is subject to a regulatory limitation or restriction on approved uses or indications, e.g., by the U.S. Food and Drug Administration (FDA), limiting approved use of the composition to patients having at least one copy of the particular form of the gene which contains at least one variance. Alternatively, the composition is subject to a regulatory limitation or restriction on approved uses indicating that the composition is not approved for use or should not be used in patients having at least one copy of a form of the gene including at least one variance. Also in preferred embodiments, the composition is packaged, and the packaging includes a label or insert indicating or suggesting beneficial therapeutic approved use of the composition in patients having one or two copies of a form of the gene including at least one variance. Alternatively, the label or insert limits approved use of the composition to patients having zero or one or two copies of a form of the gene including at least one variance. The latter embodiment would be likely where the presence of the at least one variance in one or two copies in cells of a patient means that the composition would be ineffective or deleterious to the patient. Also in preferred embodiments, the composition is indicated for use in treatment of a disease or condition which is one of those identified for aspects above. Also in preferred embodiments, the at least one variance includes at least one variance from those identified herein. The term "packaged" means that the drug, compound, or composition is prepared in a manner suitable for distribution or shipping with a box, vial, pouch, bubble pack, or other protective container, which may also be used in combination. The packaging may have printing on it and/or printed material may be included in the packaging. In preferred embodiments, the drug is selected from the drug classes or specific exemplary drugs identified in an example, in a table herein, and is subject to a regulatory limitation or suggestion or warning as described above that limits or suggests limiting approved use to patients having specific variances or variant forms of a gene identified in Examples or in the gene list provided below in order to achieve maximal benefit and avoid toxicity or other deleterious effect. A pharmaceutical composition can be adapted to be preferentially effective in a variety of ways. In some cases, an active compound is selected which was not previously known to be differentially active, or which was not previously recognized as a potential therapeutic compound. In some cases, the concentration of an active compound which has differential activity can be adjusted such that the composition is appropriate for administration to a patient with the specified variances. For example, the presence of a specified variance may allow or require the administration of a much larger dose, which would not be practical with a previously utilized composition. Conversely, a patient may require a much lower dose, such that administration of such a dose with a prior composition would be impractical or inaccurate. Thus, the composition may be prepared in a higher or lower unit dose form, or prepared in a higher or lower concentration of the active compound or compounds. In yet other cases, the composition can include additional compounds needed to enable administration of a particular active compound in a patient with the specified variances, which was not in previous compositions, e.g., because the majority of patients did not require or benefit from the added component. The term "differential" or "differentially" generally refers to a statistically significant different level in the specified property or effect. Preferably, the difference is also functionally significant. Thus, "differential binding or hybridization" is sufficient difference in binding or hybridization to allow discrimination using an appropriate detection technique. Likewise, "differential effect" or "differentially active" in connection with a therapeutic treatment or drug refers to a difference in the level of the effect or activity which is distinguishable using relevant parameters and techniques for measuring the effect or activity being considered. Preferably the difference in effect or activity is also sufficient to be clinically significant, such that a corresponding difference in the course of treatment or treatment outcome would be expected, at least on a statistical basis. Also usefully provided in the present invention are probes which specifically recognize a nucleic acid sequence corresponding to a variance or variances in a gene as identified in aspects above or a product expressed from the gene, and are able to distinguish a variant form of the sequence or gene or gene product from one or more other variant forms of that sequence, gene, or gene product under selective conditions. Those skilled in the art recognize and understand the identification or determination of selective conditions for particular probes or types of probes. An exemplary type of probe is a nucleic acid hybridization probe, which will selectively bind under selective binding conditions to a nucleic acid sequence or a gene product corresponding to one of the genes identified for aspects above. Another type of probe is a peptide or protein, e.g., an antibody or antibody fragment which specifically or preferentially binds to a polypeptide expressed from a particular form of a gene as characterized by the presence or absence of at least one variance. Thus, in another aspect, the invention concerns such probes. In the context of this invention, a "probe" is a molecule, commonly a nucleic acid, though also potentially a protein, carbohydrate, polymer, or small molecule, that is capable of binding to one variance or variant form of the gene to a greater extent than to a form of the gene having a different base at one or more variance sites, such that the presence of the variance or variant form of the gene can be determined. Preferably the probe distinguishes at least one variance identified in Examples, tables or lists below or is a variance otherwise identified in a gene identified herein. In preferred embodiments, the probe is a nucleic acid probe at least 15, preferably at least 17 nucleotides in length, more preferably at least 20 or 22 or 25, preferably 500 or fewer nucleotides in length, more preferably 200 or 100 or fewer, still more preferably 50 or fewer, and most preferably 30 or fewer. In preferred embodiments, the probe has a length in a range between from any one of the above lengths to any other of the above lengths (including endpoints). In the case of certain types of probes, e.g., peptide nucleic acid probes, the probe may be shorter, e.g., 6,7, 8, 10, or 12 nucleotides in length. The probe specifically hybridizes under selective hybridization conditions to a nucleic acid sequence corresponding to a portion of one of the genes identified in connection with above aspects. The nucleic acid sequence includes at least one variance site. Also in preferred embodiments, the probe has a detectable label, preferably a fluorescent label. A variety of other detectable labels are known to those skilled in the art. Such a nucleic acid probe can also include one or more nucleic acid analogs. In preferred embodiments, the probe is an antibody or antibody fragment which specifically binds to a gene product expressed from a form of one of the above genes, where the form of the gene has at least one specific variance with a particular base at the variance site, and preferably a plurality of such variances. In connection with nucleic acid probe hybridization, the term "specifically hybridizes" indicates that the probe hybridizes to a sufficiently greater degree to the target sequence than to a sequence having a mismatched base at least one variance site to allow distinguishing such hybridization. The term "specifically hybridizes" thus means that the probe hybridizes to the target sequence, and not to non-target sequences, at a level which allows ready identification of probe/target sequence hybridization under selective hybridization conditions. Thus, "selective hybridization conditions" refer to conditions which allow such differential binding. Similarly, the terms "specifically binds" and "selective binding conditions" refer to such differential binding of any type of probe, e.g., antibody probes, and to the conditions which allow such differential binding. Typically hybridization reactions to determine the status of variant sites in patient samples are carried out with two different probes, one specific for each of the (usually two) possible variant nucleotides. The complementary information derived from the two separate hybridization reactions is useful in corroborating the results. Likewise, the invention provides an isolated, purified or enriched nucleic acid sequence of 15 to 500 nucleotides in length, preferably 15 to 100 nucleotides in length, more preferably 15 to 50 nucleotides in length, and most preferably 15 to 30 nucleotides in length, which has a sequence which corresponds to a portion of one of the genes identified for aspects above. Preferably the lower limit for the preceding ranges is 17, 20, 22, or 25 nucleotides in length. In other embodiments, the nucleic acid sequence is 30 to 300 nucleotides in length, or 45 to 200 nucleotides in length, or 45 to 100 nucleotides in length. The nucleic acid sequence includes at least one variance site. Such sequences can, for example, be amplification products of a sequence which spans or includes a variance site in a gene identified herein. Likewise, such a sequence can be a primer that is able to bind to or extend through a variance site in such a gene. Yet another example is a nucleic acid hybridization probe comprised of such a sequence. In such probes, pπ ers, and amplification products, the nucleotide sequence can contain a sequence or site corresponding to a variance site or sites, for example, a variance site identified herein. Preferably the presence or absence of a particular variant form in the heterozygous or homozygous state is indicative of the effectiveness of a method of treatment in a patient. In reference to nucleic acid sequences which "correspond" to a gene, the term "correspond" refers to a nucleotide sequence relationship, such that the nucleotide sequence has a nucleotide sequence which is the same as the reference gene or an indicated portion thereof, or has a nucleotide sequence which is exactly complementary in normal Watson-Crick base pairing, or is an RNA equivalent of such a sequence, e.g., an mRNA, or is a cDNA derived from an mRNA of the gene. In another aspect, the invention provides a method for determining a genotype of an individual in relation to one or more variances in one or more of the genes identified in above aspects by using mass spectrometric determination of a nucleic acid sequence which is a portion of a gene identified for other aspects of this invention or a complementary sequence. Such mass spectrometric methods are known to those skilled in the art. In preferred embodiments, the method involves determining the presence or absence of a variance in a gene; determining the nucleotide sequence of the nucleic acid sequence; the nucleotide sequence is 100 nucleotides or less in length, preferably 50 or less, more preferably 30 or less, and still more preferably 20 nucleotides or less. In general, such a nucleotide sequence includes at least one variance site, preferably a variance site which is informative with respect to the expected response of a patient to a treatment as described for above aspects. As indicated above, many therapeutic compounds or combinations of compounds or pharmaceutical compositions show variable efficacy and/or safety in various patients in whom the compound or compounds is administered. Thus, it is beneficial to identify variances in relevant genes, e.g., genes related to the action or toxicity of the compound or compounds. Thus, in a further aspect, the invention provides a method for determining whether a compound has a differential effect due to the presence or absence of at least one variance in a gene or a variant form of a gene, where the gene is a gene identified for aspects above. The method involves identifying a first patient or set of patients suffering from a disease or condition whose response to a treatment differs from the response (to the same treatment) of a second patient or set of patients suffering from the same disease or condition, and then determining whether the occurrence or frequency of occurrence of at least one variance in at least one gene differs between the first patient or set of patients and the second patient or set of patients. A correlation or other appropriate statistical test between the presence or absence of the variance or variances and the response of the patient or patients to the treatment indicates that the variance provides information about variable patient response. In general, the method will involve identifying at least one variance in at least one gene. An alternative approach is to identify a first patient or set of patients suffering from a disease or condition and having a particular genotype, haplotype or combination of genotypes or haplotypes, and a second patient or set of patients suffering from the same disease or condition that have a genotype or haplotype or sets of genotypes or haplotypes that differ in a specific way from those of the first set of patients. Subsequently the extent and magnitude of clinical response can be compared between the first patient or set of patients and the second patient or set of patients. A coπelation between the presence or absence of a variance or variances or haplotypes and the response of the patient or patients to the treatment indicates that the variance provides information about variable patient response and is useful for the present invention. The method can utilize a variety of different informative comparisons to identify correlations. For example a plurality of pairwise comparisons of treatment response and the presence or absence of at least one variance can be performed for a plurality of patients. Likewise, the method can involve comparing the response of at least one patient homozygous for at least one variance with at least one patient homozygous for the alternative form of that variance or variances. The method can also involve comparing the response of at least one patient heterozygous for at least one variance with the response of at least one patient homozygous for the at least one variance. Preferably the heterozygous patient response is compared to both alternative homozygous forms, or the response of heterozygous patients is grouped with the response of one class of homozygous patients and said group is compared to the response of the alternative homozygous group. Such methods can utilize either retrospective or prospective information concerning treatment response variability. Thus, in a preferred embodiment, it is previously known that patient response to the method of treatment is variable. Also in prefened embodiments, the disease or condition is as for other aspects of this invention; for example, the treatment involves administration of a compound or pharmaceutical composition. In preferred embodiments, the method involves a clinical trial, e.g., as described herein. Such a trial can be arranged, for example, in any of the ways described herein, e.g., in the Detailed Description. The present invention also provides methods of treatment of a disease or condition as identified herein. Such methods combine identification of the presence or absence of particular variances, preferably in a gene or genes from Tables 1-6, 12-17, and 18-23, with the administration of a compound; identification of the presence of particular variances with selection of a method of treatment and administration of the treatment, and identification of the presence or absence of particular vanances with elimination of a method of treatment based on the vanance information indicating that the treatment is likely to be ineffective or contra- mdicated, and thus selecting and administeπng an alternative treatment effective against the disease or condition Thus, preferred embodiments ot these methods incoφorate preferred embodiments of such methods as descπbed for such sub- aspects As used herein, a "gene" is a sequence of DNA present in a cell that directs the expression of a "biologically active" molecule or "gene pioduct", most commonly by transcnption to produce RNA and translation to produce protein The "gene product' is most commonly a RNA molecule or protein or a RNA or protem that is subsequently modified by reacting with, or combining with, other constituents of the cell Such modifications may include, without limitation, modification of proteins to form glycoproteins, hpoproteins, and phosphoprotems, or other modifications known in the art RNA may be modified without limitation by polyadenylation, splicing, capping or export from the nucleus or by covalent or noncovalent interactions with proteins, The term "gene product" refers to any product directly resulting from transcπption of a gene In particular this includes partial, precursor, and mature transcπption products (l e , pre-mRNA and mRNA), and translation products with or without further processing including, without limitation, hpidation, phosphorylation, glycosylation, or combinations of such processing The term "gene involved in the ongm or pathogenesis of a disease or condition" refers to a gene that harbors mutations or polymoφhisms that contπbute to the cause of disease, or vanances that affect the progression of the disease or expression of specific charactenstics of the disease The term also applies to genes involved in the synthesis, accumulation, or elimination of products that are involved in the oπgin or pathogenesis of a disease or condition including, without limitation, proteins, lipids, carbohydrates, hormones, or small molecules The term "gene involved in the action of a drug" refers to any gene whose gene product affects the efficacy or safety of the drug or affects the disease process being treated by the drug, and includes, without limitation, genes that encode gene products that are targets for drug action, gene products that are involved in the metabolism, activation or degradation of the drug, gene products that are involved in the bioavailability or elimination of the drug to the target, gene products that affect biological pathways that, in turn, affect the action of the drug such as the synthesis or degradation of competitive substrates or allostenc effectors or rate-limiting reaction, or, alternatively, gene products that affect the pathophysiology of the disease process via pathways related or unrelated to those altered by the presence of the drug compound. (Particular vanances in the latter category of genes may be associated with patient groups m whom disease etiology is more or less susceptible to amelioration by the drug The "action" of a drug refers to its effect on biological products withm the body The action of a drug also refers to its effects on the signs or symptoms of a disease or condition, or effects of the drug that are unrelated to the disease or condition leading to unanticipated effects on other processes Such unanticipated processes often lead to adverse events or toxic effects The terms "adverse event" or "toxic" event" are known in the art and include, without limitation, those listed in the FDA reference system for adverse events In accordance with the aspects above and the Detailed Descπption below, there is also descπbed for this invention an approach for developing drugs that are explicitly indicated for, and/or for which approved use is restncted to or recommended to be restncted to individuals in the population with specific vaπances or combinations of vaπances, as determined by diagnostic tests for vaπances or vanant forms of certain genes involved m the disease or condition or involved in the action or metabolism or transport of the drug Such drugs may provide more effective treatment for a disease or condition in a population identified or characteπzed with the use of a diagnostic test for a specific vanance or vanant form of the gene if the gene is involved in the action of the drug or in determining a characteπstic of the disease or condition Such drugs may be developed using the diagnostic tests for specific vanances or vanant forms of a gene to determine the inclusion of patients in a clinical tπal Thus, the invention also provides a method for producing a pharmaceutical composition by identifying a compound which has differential activity or effectiveness against a disease or condition m patients having at least one vanance in a gene, preferably in a gene from Tables 1-6, compounding the pharmaceutical composition by combining the compound with a pharmaceutically acceptable earner, excipient, or diluent such that the composition is preferentially effective m patients who have at least one copy of the vanance or vaπances In some cases, the patient has two copies of the vanance or vanances. In prefened embodiments, the disease or condition, gene or genes, vanances, methods of administration, or method of determining the presence or absence of vanances is as descπbed for other aspects of this invention. In preferred embodiments, the active component of the pharmaceutical composition is a compound listed m the compound tables below (Tables 24 through 68), or a compound chemically related to one of the listed compounds Similarly, the invention provides a method for producing a pharmaceutical agent by identifying a compound which has differential activity against a disease or condition in patients having at least one copy of a form of a gene, preferably a gene from Tables 1 through 6, having at least one vanance and synthesizing the compound m an amount sufficient to provide a pharmaceutical effect m a patient suffenng from the disease or condition The compound can be identified by conventional screening methods and its activity confirmed For example, compound hbraπes can be screened to identify compounds which differentially bind to products of vanant forms of a particular gene product, or which differentially affect expression of vanant forms of the particular gene, or which differentially affect the activity of a product expressed from such gene. Alternatively, the design of a compound can exploit knowledge of the vaπances provided herein to avoid significant allele specific effects, in order to reduce the likelihood of significant pharmacogenetic effects dunng the clinical development process Preferred embodiments are as for the preceding aspect. In another aspect, the invention provides a method of treating a disease or condition in a patient by selecting a patient whose cells have an allele of an identified gene, preferably a gene selected from the genes listed in Tables 1 through 6 The allele contains at least one vanance con-elated with more effective response to a treatment of said disease or condition The method also includes altenng the level of activity in cells of the patient of a product of the allele, where the altenng provides a therapeutic effect Preferably the allele contains a vanance as shown in Tables 1 -6, 12-17, and 18-23, or other vanance table herein, or Table 1 or 3 of Stanton et al, U S Application No 09/300,747 Also preferably, the altenng involves admimsteπng to the patient a compound preferentially active on at least one but less than all alleles of the gene. Preferred embodiments include those as descnbed above for other aspects of treating a disease or condition As recognized by those skilled in the art, all the methods of treating descnbed herein include administration of the treatment to a patient In a further aspect, the invention provides a method for determining a treatment effective to treat a disease or condition by altenng the level of activity of a product of an allele of a gene selected from the genes listed in Tables 1-6, and determining whether that alteration provides a differential effect (with respect to reducing or alleviating a disease or condition, or with respect to vanation m toxicity or tolerance to a treatment) in patients with at least one copy of at least one allele of the gene as compared to patients with at least one copy of one alternative allele., The presence of such a differential effect indicates that altering the level or activity of the gene provides at least part of an effective treatment for the disease or condition. Preferably the method for determining a treatment is carried out in a clinical trial, e.g., as described above and/or in the Detailed Description below. In a further aspect, the invention provides a method for determining a treatment effective to treat a disease or condition by altering the level of activity of a product of an allele of a gene selected from the genes listed in Tables 1-6, and determining whether that alteration provides a differential effect (with respect to reducing or alleviating a disease or condition, or with respect to variation in toxicity or tolerance to a treatment) in patients with at least one copy of at least one allele of the gene as compared to patients with at least one copy of one alternative allele., The presence of such a differential effect indicates that altering the level or activity of the gene provides at least part of an effective treatment for the disease or condition. Preferably the method for determining a method of treatment is carried out in a clinical trial, e.g., as described above and/or in the Detailed Description below. In still another aspect, the invention provides a method for performing a clinical trial or study, which includes selecting or stratifying subjects in the trial or study using a variance or variances or haplotypes from one or more genes specified in Tables 1-6, 12-17, and 18-23. Preferably the differential efficacy, tolerance, or safety of a treatment in a subset of patients who have a particular variance, variances, or haplotype in a gene or genes from Tables 1-6, 12-17, and 18-23 is determined by conducting a clinical trial and using a statistical test to assess whether a relationship exists between efficacy, tolerance, or safety and the presence or absence of any of the variances or haplotype in one or more of the genes. Rresults of the clinical trial or study are indicative of whether a higher or lower efficacy, tolerance, or safety of the treatment in a subset of patients is associated with any of the variance or variances or haplotype in one or more of the genes. In preferred embodiments, the clinical trial or study is a Phase I, II, III, or IV trial or study. Prefened embodiments include the stratifications and/or statistical analyses as described below in the Detailed Description. In preferred embodiments, normal subjects or patients are prospectively stratified by genotype in different genotype-defined groups, including the use of genotype as a enrollment criterion, using a variance, variances or haplotypes from Tables 1-6, 12-17, and 18-23, and subsequently a biological or clinical response vanable is compared between the different genotype-defined groups In preferred embodiments, normal subjects or patients in a clinical tnal or study are stratified by a biological or clinical response vanable in different biologically or c nically- defined groups, and subsequently the frequency of a vanance, vaπances or haplotypes from Tables 1-6, 12-17, and 18-23 is measured m the different biologically or clinically defined groups In preferred embodiments, e g , of the above two analyses, the normal subjects or patients m a clinical tnal or study are stratified by at least one demographic charactenstic selected from the goups consisting of sex, age, racial oπgm, ethnic oπgin, or geographic ongin Generally the method will involve assigning patients to a group to receive the method of treatment or to a control group. In yet another aspect, the invention provides expeπmental methods for finding additional vaπances in a gene provided m Tables 1 -6, 12-17, 18-23 A number of expeπmental methods can also beneficially be used to identify vanances Thus, the invention provides methods for producing cDNA (Example 1) and detecting additional vanances in the genes provided m Tables 1 -6, 12-17, 18-23. using the single strand conformation polymoφhism (SSCP) method (Example 2), the T4 Endonuclease VII method (Example 3) or DNA sequencing (Example 4) or other methods pointed out below The application of these methods to the identified genes will provide identification of additional vanances that can affect mter- mdividual vanation m drug or other treatment response One skilled in the art will recognize that many methods for expeπmental vanance detection have been descπbed (in addition to the exemplary methods of examples 2, 3, 4) and can be utilized These additional methods include chemical cleavage of mismatches (see, e g , Ellis T P., et al., Chemical cleavage of mismatch a new look at an established method Human Mutation 1 1(5) 345-53, 1998), denatuπng gradient gel electrophoresis (see, e.g., Van Orsouw N J , et al., Design and application of 2-D DGGE-based gene mutational scanning tests Genet Anal. 14(5-6) 205-13, 1999) and heteroduplex analysis (see, e g , Ganguly A., et al., Conformation-sensitive gel electrophoresis for rapid detection of single-base differences in double-stranded PCR products and DNA fragments evidence for solvent-induced bends in DNA heteroduplexes. Proc Natl Acad Sci U S A 90 (21).10325-9, 1993) Table 3 of Stanton et al., U.S. Application No 09/300,747, provides a descπption of the additional possible vaπances that could be detected by one skilled in the art by testing an identified gene in Tables 1-6, 12-17, 18-23, using the vanance detection methods descπbed or other methods which are known or are developed The present mvention provides a method for treating a patient at nsk for a disease, disorder, dysfunction or condition (for example to prevent or delay the onset of frank disease) or a patient already diagnosed with a said disease or a disease associated with said disease The methods include identifying such a patient and determining the patient's genotype or haplotype for an identified gene or genes The patient identification can, for example, be based on clinical evaluation using conventional clinical metπcs and/or on evaluation of a genetic vanance or vaπances in one or more genes, preferably a gene or genes from Tables 1-6 The invention provides a method for using the patient's genotype status to determine a treatment protocol that includes a prediction of the efficacy and/or safety of a therapy In another aspect, the invention provides a method for treating a patient at nsk for a drug-mduced disease, disorder or dysfunction by a) identifying a patient with such a nsk, b) determining the genotypic allele status of the patient, and c) converting the data obtained in step b) into a treatment protocol that includes a compaπson of the genotypic allele status determination with the allele frequency of a control population. This compaπson allows for a statistical calculation of the patient's nsk for having drug-induced disease, disorder, or dysfunction, e g , based on correlation of the allele frequencies for a population with response or disease occurrence and/or seventy In prefened embodiments, the method provides a treatment protocol that predicts a patient being heterozygous or homozygous for an identified allele to exhibit signs and or symptoms of drug-induced disease, disorder, or dysfunction and a patient who is wild-type homozygous for the said allele, as responding favorably to these therapies In an another related aspect, the invention provides a method for identifying a patient for participation in a clinical tnal of a therapy for the treatment of a disease or an associated pathological or psychiatnc condition The method for identification of a subjectg of the particiaption in a clmcial tnal of a therapy for a disease descnbed in this invention involves determining the genotype or haplotype of a patient awith (or at nsk for) a disease as identified herein Preferably the genotype is for a vanance in a gene from Tables 1-6 Patients with eligible genotypes are then assigned to a treatment or placebo group, preferably by a blinded randomization procedure In preferred embodiments, the selected patients have at least no copies, one copy or two copies of a wild typespecificallele of identified a gene or genes identified in Tables 1-6 Alternatively, patients selected for the clinical tnal may have zero, one or two copies of an allele belonging to a set of alleles, where the set of alleles compnse a group of related alleles One procedure for ngorously defining a set of alleles is by applying phylogenetic methods to the analysis of haplotypes. (See, for example: Templeton A.R., Crandall K.A and C.F. Sing, A cladistic analysis of phenotypic associations with haplotypes inferred from restπction endonuclease mapping and DNA sequence data III Cladogram estimation. Genetics 1992 Oct. 132(2):619-33.) Regardless of the specific tools used to group alleles, the trial would then test the hypothesis that a statistically significant difference in response to a treatment can be demonstrated between two groups of patients each defined by the presence of zero, one or two alleles (or allele groups) at a gene or genes. Said response may be a desired or an undesired response. In a prefened embodiment, the treatment protocol involves a companson of placebo vs. treatment response rates in two or more genotype-defined groups For example a group with no copies of an allele may be compared to a group with two copies, or a group with no copies may be compared to a group consisting of those with one or two copies. In this manner different genetic models (dominant, co-dominant, recessive) for the transmission of a treatment response trait can be tested. Alternatively, statistical methods that do not posit a specific genetic model, such as contingency tables, can be used to measure the effects of an allele on treatment response. In another preferred embodiment, patients in a clinical tnal can be grouped (at the end of the tnal) according to treatment response, and statistical methods can be used to compare allele (or genotype or haplotype) frequencies in two groups. For example responders can be compared to nonresponders, or patients suffenng adverse events can be compared to those not expenencmg such effects Alternatively response data can be treated as a continuous vanable and the ability of genotype to predict response can be measured. In a preferred embodiments patients who exhibit extreme phenotypes are compared with all other patients or with a group of patients who exhibit a divergent extreme phenotype. For example if there is a continuous or semi-continuous measure of treatment response (for example the Alzheimer's Disease Assessment Scale, the Mini-Mental State Examination or the Hamilton Depression Rating Scale) then the 10%> of patients with the most favorable responses could be compared to the 10% with the least favorable, or the patients one standard deviation above the mean score could be compared to the remainder, or to those one standard deviation below the mean score. One useful way to select the threshold for defining a response is to examine the distribution of responses in a placebo group. If the upper end of the range of placebo responses is used as a lower threshold for an 'outlier response' then the outlier response group should be almost free of placebo responders. This is a useful threshold because the inclusion of placebo responders in a 'true' reponse group decreases the ability of statistical methods to detect a genetic difference between responders and nonresponders. disease. In a related aspect, the invention provides a method for developing a disease management protocol that entails diagnosing a patient with a disease or a disease susceptibility, determining the genotype of the patient at a gene or genes correlated with treatment response and then selecting an optimal treatment based on the disease and the genotype (or genotypes or haplotypes). The disease management protocol may be useful in an education program for physicians, other caregivers or pharmacists; may constitute part of a drug label; or may be useful in a marketing campaign. In a related aspect, the invention provides a method for treating a patient at nsk for or diagnosed with drug-induced disease or pathological condition or dysfunction using the methods of the above aspect and conducting a step c) which involves determining the gene allele load status of the patient. This method further involves converting the data obtained in steps b) and c) into a treatment protocol that includes a comparison of the allele status determinations of these steps with the allele frequency of a control population. This affords a statistical calculation of the patient's risk for having drug-induced disease, disorder or dysfunction. In a prefened embodiment, the method is useful for identifying drug-induced disease, disorder or dysfunction. In addition, in related embodiments, the methods provide a treatment protocol that predicts a patient to be at high risk for drug-induced disease, disorder or dysfunction responding by exhibiting signs and symptoms of drug- induced toxicity, disorders, dysfunction if the patient is determined as having a genotype or allelic difference in the identified gene or genes. Such patients are preferably given alternative therapies. The invention also provides a method for improving the safety of candidate therapies for the identification of a drug-induced disease, disorder, or dysfunction. The method includes the step of comparing the relative safety of the candidate therapeutic intervention in patients having different alleles in one or more than one of the genes listed in Tables 1 -6, 12-17, and 18-23. Preferably, administration of the drug is preferentially provided to those patients with an allele type associated with increased efficacy. In a prefened embodiment, the alleles of identified gene or genes used are wild-type and those associated with altered biological activity. For the aspects above, in connection with any of the listed diseases, disorders, or conditions and treatments thereof, or indeed any disease or disorder, can utilize pharmacogenetic information and determinations of genes and gene pathways involved in the absoφtion, distribution, metabolism, or excretion of said treatment Thus, the presence or the absence of at least vanance or haplotype in such a gene or genes can be indicative of the effectiveness of a treatment for a given disease, disorder, or condition, where the gene or gene pathway is involved in the absoφtion, distnbution, metabolism, or excretion of said treatment, e g , a drug treatment As used herein, by "therapy associated with drug-induced disease" is meant any therapy resulting in pathophysiologic dysfunction or signs and symptoms of failure or dysfunction, or those associated with the pathophysiological manifestations of a disorder. A suitable therapy can be a pharmacological agent, drug, or therapy that alters a pathways identified to affect the molecular structure or function of the parent candidate therapeutic intervention thereby affecting drug- induced disease or disorder progression of any of the descπbed organ system dysfunctions By "drug-induced disease" or "drug-induced syndrome" is meant any physiologic condition that may be conelated with medical therapy by a drug, agent, or candidate therapeutic intervention By "drug-induced dysfunction" is meant a physiologic disorder or syndrome that may be correlated with medical therapy by a drug, agent, or candidate therapeutic intervention m which symptomology is similar to drug-mduced disease Specifically included are a) hemostasis dysfunction, b) cutaneous disorders; c) cardiovascular dysfunction, d) renal dysfunction; e) pulmonary dysfunction, f) hepatic dysfunction, g) systemic reactions; and h) central nervous system dysfunction By "drug associated disorder" is meant a physiologic dysfunction that may be correlated with medical therapy by a drug, agent, or candidate therapeutic intervention. The drug associated disorder may include disease, disorder, or dysfunction. As used herein, by "therapy associated with inflammatory or immunological disease" is meant any therapy resulting in dysfunction or signs and symptoms of a inflammatory or immunologic condition or dysfunction, or those associated with the pathophysiological manifestations of a clinically diagnosed inflammatory or immunologic disorder or syndrome A suitable therapy can be a pharmacological agent or drug that may enhance or inhibit metabolic pathways identified to affect the molecular structure or function of the parent candidate therapeutic intervention thereby affecting inflammatory or immunological disease progression of any of these inflammatory or immunological dysfunctions. By "inflammatory or immunological dysfunction" is meant a disease or syndrome in which symptomology is similar to a inflammatory or immunological disease. Specifically included are:arthritis, asthma, chronic obstructive pulmonary disease, autoimmune disease, inflammatory bowel disease, immunosuppression related to transplantation, pain associated with inflammation, psoriasis, atherosclerosis, and hepatitis. By "pathway" or "gene pathway" is meant the group of biologically relevant genes involved in a pharmacodynamic or pharmacokinetic mechanism of drug, agent, or candidate therapeutic intervention. These mechanisms may further include any physiologic effect the drug or candidate therapeutic intervention renders. By "disease mangement protocol" or "treatment protocol" is meant a means for devising a therapeutic plan for a patient using laboratory, clinical and genetic data, including the patient's diagnosis and genotype. The protocol clarifies therapeutic options and provides information about probable prognoses with different treatments. The treatment protocol may theprovide an estimate of the likelihood that a patient will respond positively or negatively to a therapeutic intervention. The treatment protocol may also provide guidance regarding optimal drug dose and administration, and likely timing of recovery or rehabilitation. A "disease mangement protocol" or "treatment protocol" may also be formulated for asymptomatic and healthy subjects in order to forecast future disease risks based on laboratory, clinical and genetic variables. In this setting the protocol specifies optimal preventive or prophylactic interventions, including use of compounds, changes in diet or behavior, or other measures. The treatment protocol may include the use of a computer program. In another aspect, the invention provides a kit containing at least one probe or at least one primer (or other amplification oligonucleotide) or both (e.g., as described above) corresponding to a gene or genes listed in Tables 1-6, 12- 17, and 18-23 or other gene related to a disease or condition listed in Tables 7-11 or described within the invention. The kit is preferably adapted and configured to be suitable for identification of the presence or absence of a particular variance or variances, which can include or consist of a nucleic acid sequence conesponding to a portion of a gene. A plurality of variances may comprise a haplotype of haplotypes. The kit may also contain a plurality of either or both of such probes and or primers, e.g., 2, 3, 4, 5, 6, or more of such probes and/or primers. Preferably the plurality of probes and/or primers are adapted to provide detection of a plurality of different sequence variances in a gene or plurality of genes, e.g., in 2, 3, 4, 5, or more genes or to amplify and/or sequence a nucleic acid sequence including at least one variance site in a gene or genes. Preferably one or more of the variance or variances to be detected are corcelated with variability in a treatment response or tolerance, and are preferably indicative of an effective response to a treatment. In preferred embodiments, the kit contains components (e.g., probes and/or primers) adapted or useful for detection of a plurality of variances (which may be in one or more genes) indicative of the effectiveness of at least one treatment, preferably of a plurality of different treatments for a particular disease or condition. It may also be desirable to provide a kit containing components adapted or useful to allow detection of a plurality of variances indicative of the effectiveness of a treatment or treatment against a plurality of diseases. The kit may also optionally contain other components, preferably other components adapted for identifying the presence of a particular variance or variances. Such additional components can, for example, independently include a buffer or buffers, e.g., amplification buffers and hybridization buffers, which may be in liquid or dry form, a DNA polymerase, e.g., a polymerase suitable for carrying out PCR (e.g., a thermostable DNA polymerase), and deoxy nucleotide triphosphates (dNTPs). Preferably a probe includes a detectable label, e.g., a fluorescent label, enzyme label, light scattering label, or other label. Preferably the kit includes a nucleic acid or polypeptide anay on a solid phase substrate. The anay may, for example, include a plurality of different antibodies, and/or a plurality of different nucleic acid sequences. Sites in the array can allow capture and/or detection of nucleic acid sequences or gene products conesponding to different variances in one or more different genes. Preferably the arcay is arranged to provide variance detection for a plurality of variances in one or more genes which corcelate with the effectiveness of one or more treatments of one or more diseases, which is preferably a variance as described herein. The kit may also optionally contain instructions for use, which can include a listing of the variances conelating with a particular treatment or treatments for a disease or diseases and/or a statement or listing of the diseases for which a particular variance .or variances conelates with a treatment efficacy and/or safety. Preferably the kit components are selected to allow detection of a variance described herein, and/or detection of a variance indicative of a treatment, e.g., administration of a drug, pointed out herein. Additional configurations for kits of this invention will be apparent to those skilled in the art. The invention also includes the use of such a kit to determine the genotype(s) of one or more individuals with respect to one or more variance sites in one or more genes identified herein. Such use can include providing a result or report indicating the presence and or absence of one or more variant forms or a gene or genes which are indicative of the effectiveness of a treatment or treatments. In another aspect, the invention provides a method for determining whether there is a genetic component to intersubject variation in a sunogate treatment response. The method involves administering the treatment to a group of related (preferably normal) subjects and a group of unrelated (preferably normal) subjects, measuring a surrogate pharmacodynamic or pharmacokinetic drug response variable in the subjects, performing a statistical test measuring the variation in response in the group of related subjects and, separately in the group of unrelated subjects, comparing the magnitude or pattern of variation in response or both between the groups to determine if the responses of the groups are different, using a predetermined statistical measure of difference. A difference in response between the groups is indicative that there is a genetic component to intersubject variation in the surrogate treatment response. In prefened embodiments, the size of the related and unrelated groups is set in order to achieve a predetermined degree of statistical power. In another aspect, the invention provides a method for evaluating the combined contribution of two or more variances to a sunogate drug response phenotype in subjects (preferably normal subjects) by a. genotyping a set of unrelated subjects participating in a Phase I trial of a compound. The genotyping is for two or more variances (which can be a haplotype), thereby identifying subjects with specific genotypes, where the two or more specific genotypes define two or more genotype-defined groups. A drug is administered to subjects with two or more of the specific genotypes, and a sunogate pharmacodynamic or pharmacokinetic drug response variable is measured in the subjects. A statistical test or tests is performed to measure response in the groups separately, where the statistical tests provide a measurement of variation in response with each group. The magnitude or pattern of variation in response or both is compared between the groups to determine if the groups are different using a predetermined statistical measure of difference. In preferred embodiments, the specific genotypes are homozygous genotypes for two variances. In preferred embodiments, the comparison is between groups of subjects differing in three or more variances, e.g., 3, 4, 5, 6, or even more variances. In another aspect, the invention provides a method for providing contract research services to clients (preferably in the pharmaceutical and biotechnology industries), by enrolling subjects (e.g., normal and/or patient subjects) in a clinical drug trial or study unit (preferably a Phase I drug trial or study unit) for the puφose of genotyping the subjects in order to assess the contribution of genetic variation to variation in drug response, genotyping the subjects to determine the status of one or more variances in the subjects, administering a compound to the subjects and measuring a sunogate drug response variable, comparing responses between two or more genotype-defined groups of subjects to determine whether there is a genetic component to the inteφerson variability in response to said compound; and reporting the results of the Phase I drug trial to a contracting entity. Clearly, intermediate results, e.g., response data and/or statistical analysis of response or variation in reponse. In prefened embodiments, at least some of the subjects have disclosed that they are related to each other and the genetic analysis includes comparison of groups of related individuals. To encourage participation of sufficient numbers of related individuals, it can be advantageous to offer or provide compensation to one or more of the related individuals based on the number of subjects related to them who participate in the clinical trial, or on whether at least a minimum number of related subjects participate, e.g., at least 3, 5, 10, 20, or more. In a related aspect, the invention provides a method for recruiting a clinical trial population for studies of the influence of genetic variation on drug response, by soliciting subjects to participate in the clinical trial, obtaining consent of each of a set of subjects for participation in the clinical trial, obtaining additional related subjects for participation in the clinical trial by compensating one or more of the related subjects for participation of their related subjects at a level based on the number of related subjects participating or based on participation of at least a minimum specified number of related subjects, e.g., at minimum levels as specified in the preceding aspect. In all of the aspects herein, the gene (or genes) can be a gene as identified herein (e.g., in the Detailed Description, including examples, or Tables 1-6, 12-17, or 18-23, or is in a pathway as identified herein, e.g., in a Table. By "pathway" or "gene pathway" is meant the goup of biologically relevant genes involved in a pharmacodynamic or pharmacokinetic mechanism of drug, agent, or candidate therapeutic intervention. These mechanisms may further include any physiologic effect the drug or candidate therapeutic intervention renders. Included in this are "biochemical pathways" which is used in its usual sense to refer to a series of related biochemical processes (and the conesponding genes and gene products) involved in carrying out a reaction or series of reactions. Generally in a cell, a pathway performs a significant process in the cell. By "pharmacological activity" used herein is meant a biochemical or physiological effect of drugs, compounds, agents, or candidate therapeutic interventions upon administration and the mechanism of action of that effect. The pharmacological activity is then determined by interactions of drugs, compounds, agents, or candidate therapeutic interventions, or their mechanism of action, on their target proteins or macromolecular components. By "agonist" or "mimetic" or "activators" is meant a drug, agent, or compound that activate physiologic components and mimic the effects of endogenous regulatory compounds. By "antagonists", "blockers" or "inhibitors" is meant drugs, agents, or compounds that bind to physiologic components and do not mimic endogenous regulatory compounds, or interfere with the action of endogenous regulatory compounds at physiologic components. These inhibitory compounds do not have intrinsic regulatory activity, but prevent the action of agonists. By "partial agonist" or "partial antagonist" is meant an agonist or antagonist, respectively, with limited or partial activity. By "negative agonist" or "inverse antagonists" is meant that a drug, compound, or agent that can interact with a physiologic target protein or macromolecular component and stabilizes the protein or component such that agonist-dependent conformational changes of the component do not occur and agonist mediated mechanism of physiological action is prevented. By "modulators" or "factors" is meant a drug, agent, or compound that interacts with a target protein or macromolecular component and modifies the physiological effect of an agonist. As used herein the term "chemical class" refers to a group of compounds that share a common chemical scaffold but which differ in respect to the substituent groups linked to the scaffold. Examples of chemical classes of drugs include, for example, phenothiazines, piperidines, benzodiazepines and aminoglycosides. Members of the phenothiazine class include, for example, compounds such as chloφromazine hydrochoride, mesoridazine besylate, thioridazine hydrochloride, acetophenazine maleate trifluoperazine hydrochloride and others, all of which share a phenothiazine backbone. Members of the piperidine class include, for example, compounds such as meperidine, diphenoxylate and loperamide, as well as phenylpiperidines such as fentanyl, sufentanil and alfentanil, all of which share the piperidine backbone. Chemical classes and their members are recognized by those skilled in the art of medicinal chemistry. As used herein the term "sunogate marker" refers to a biological or clinical parameter that is measured in place of the biologically definitive or clinically most meaningful parameter. In comparison to definitive markers, sunogate markers are generally either more convenient, less expensive, provide earlier information or provide pharmacological or physiological information not directly obtainable with definitive markers. Examples of sunogate biological parameters: (i) testing erythrocye membrane acetylcholinesterase levels in subjects treated with an acetylcholinesterase inhibitor intended for use in Alzheimer's disease patients (where inhibition of brain acetylcholinesterase would be the definitive biological parameter); (ii) measuring levels of CD4 positive lymphocytes as a sunogate marker for response to a treatment for aquired immune deficiency syndrome (AIDS). Examples of sunogate clinical parameters: (i) performing a psychometric test on normal subjects treated for a short period of time with a candidate Alzheimer's compound in order to determine if there is a measurable effect on cognitive function. The definitive clinical test would entail measurring cognitive function in a clinical trial in Alzheimer's disease patients, (ii) Measuring blood pressure as a sunogate marker for myocardial infarction. The measurement of a sunogate marker or parameter may be an endpoint in a clinical study or clinical trial, hence "sunogate endpoint". As used herein the term "related" when used with respect to human subjects indicates that the subjects are known to share a common line of descent; that is, the subjects have a known ancestor in common. Examples of prefened related subjects include sibs (brothers and sisters), parents, grandparents, children, grandchildren, aunts, uncles, cousins, second cousins and third cousins. Subjects less closely related than third cousins are not sufficiently related to be useful as "related" subjects for the methods of this invention, even if they share a known ancestor, unless some related individuals that lie between the distantly related subjects are also included. Thus, for a group of related indivuals, each subject shares a known ancestor within three generations or less with at least one other subject in the group, and preferably with all other subjects in the group or has at least that degree of consanguinity due to multiple known common ancestors. More preferably, subjects share a common ancestor within two generations or less, or otherwise have equivalent level of consanguinity. Conversely, as used herein the term "unrelated", when used in respect to human subjects, refers to subjects who do not share a known ancestor within 3 generations or less, or otherwise have known relatedness at that degree. As used herein the term "pedigree" refers to a group of related individuals, usually comprising at least two generations, such as parents and their children, but often comprising three generations (that is, including grandparents or grandchildren as well). The relation between all the subjects in the pedigree is known and can be represented in a genealogical chart. As used herein the term "hybridization", when used with respect to DNA fragments or polynucleotides encompasses methods including both natural polynucleotides, non-natural polynucleotides or a combination of both. Natural polynucleotides are those that are polymers of the four natural deoxynucleotides (deoxyadenosine triphosphate [dA], deoxycytosine triphosphate [dC], deoxyguanine triphosphate [dG] or deoxythymidine triphosphate [dT], usually designated simply thymidine triphosphate [T]) or polymers of the four natural ribonucleotides (adenosine triphosphate [A], cytosine triphosphate [C], guanine triphosphate [G] or uridine triphosphate [U]). Non-natural polynucleotides are made up in part or entirely of nucleotides that are not natural nucleotides; that is, they have one or more modifications. Also included among non-natural polynucleotides are molecules related to nucleic acids, such as peptide nucleic acid [PNA]). Non-natural polynucleotides may be polymers of non-natural nucleotides, polymers of natural and non-natural nucleotides (in which there is at least one non-natural nucleotide), or otherwise modified polynucleotides. Non-natural polynucleotides may be useful because their hybridization properties differ from those of natural polynucleotides. As used herein the term "complementary", when used in respect to DNA fragments, refers to the base pairing rules established by Watson and Crick: A pairs with T or U; G pairs with C. Complementary DNA fragments have sequences that, when aligned in antiparallel oπentation, conform to the Watson-Crick base pairing rules at all positions or at all positions except one. As used herein, complementary DNA fragments may be natural polynucleotides, non-natural polynucleotides, or a mixture of natural and non-natural polynucleotides. As used herein "amplify" when used with respect to DNA refers to a family of methods for increasing the number of copies of a starting DNA fragment. Amplification of DNA is often performed to simplify subsequent determination of DNA sequence, including genotyping or haplotyping. Amplification methods include the polymerase chain reaction (PCR), the ligase chain reaction (LCR) and methods using Q beta repiicase, as well as transcription-based amplification systems such as the isothermal amplification procedure known as self-sustained sequence replication (3SR, developed by T.R. Gingeras and colleagues), strand displacement amplification (SDA, developed by G.T. Walker and colleagues) and the rolling circle amplification method (developed by P. Lizardi and D. Ward). As used herein "contract research services for a client" refers to a business anangement wherein a client entity pays for services consisting in part or in whole of work performed using the methods described herein. The client entity may include a commercial or non-profit organization whose primary business is in the pharmaceutical, biotechnology, diagnostics, medical device or contract research organization (CRO) sector, or any combination of those sectors. Services provided to such a client may include any of the methods described herein, particularly including clinical trial services, and especially the services described in the Detailed Description relating to a Pharmacogenetic Phase I Unit. Such services are intended to allow the earliest possible assessment of the contribution of a variance or variances or haplotypes, from one or more genes, to variation in a sunogate marker in humans. The sunogate marker is generally selected to provide information on a biological or clinical response, as defined above. As used herein, "comparing the magnitude or pattern of variation in response" between two or more groups refers to the use of a statistical procedure or procedures to measure the difference between two different distributions. For example, consider two genotype-defined groups, AA and aa, each homozygous for a different variance or haplotype in a gene believed likely to affect response to a drug. The subjects in each group are subjected to treatment with the drug and a treatment response is measured in each subject (for example a sunogate treatment response). One can then construct two distributions: the distribution of responses in the AA group and the distribution of responses in the aa group. These distributions may be compared in many ways, and the significance of any difference qualified as to its significance (often expressed as a p value), using methods known to those skilled in the art. For example, one can compare the means, medians or modes of the two distributions, or one can compare the variance or standard deviations of the two distributions. Or, if the form of the distributions is not known, one can use nonparametric statistical tests to test whether the distributions are different, and whether the difference is significant at a specified level (for example, the p<0.05 level, meaning that, by chance, the distributions would differ to the degree measured less than one in 20 similar experiments). The types of comparisons described are similar to the analysis of heritability in quantitative genetics, and would draw on standard methods from quantitative genetics to measure heritability by comparing data from related subjects. Another type of comparison that can be usefully made is between related and unrelated groups of subjects. That is, the comparison of two or more distributions is of particular interest when one distribution is drawn from a population of related subjects and the other distribution is drawn from a group of unrelated subjects, both subjected to the same treatment. (The related subjects may consist of small groups of related subjects, each compared only to their relatives.) A comparison of the distribution of a drug response variable (e.g. a sunogate marker) between two such groups may provide information on whether the drug response variable is under genetic control. For example, a nanow distribution in the group(s) of related subjects (compared to the unrelated subjects) would tend to indicate that the measured variable is under genetic control (i.e. the related subjects, on account of their genetic homogeneity, are more similar than the unrelated individuals). The degree to which the distribution was narrower in the related individuals (compared to the unrelated individuals) would be proportionate to the degree of genetic control. The nanowness of the distribution could be quantified by, for example, computing variance or standard deviation. In other cases the shape of the distribution may not be known and nonparametric tests may be preferable. Nonparametric tests include methods for comparing medians such as the sign test, the slippage test, or the rank conelation coefficient (the nonparametric equivalent of the ordinary correlation coefficient). Pearson's Chi square test for comparing an observed set of frequencies with an expected set of frequencies can also be useful. In addition to and in connection with the determination and utilization of pharmacogenetic information for treatement of proliferative disorders such as 5 cancer, infonnation provided by and genes identified in the following patents and applications are useful: Housman, INHIBITORS OF ALTERNATIVE ALLELES OF GENES ENCODING PROTEINS VITAL FOR CELL VIABILITY OR CELL GROWTH AS A BASIS FOR CANCER THERAPEUTIC AGENTS, U.S. Patent 5,702,890, issued December 30, 1997, and Housman et al., PCT/US98/05419, l o entitled TARGET GENES FOR ALLELE-SPECIFIC DRUGS. Essential and conditionally essential genes identified therein can be utilized as targets for the methods and compositions described in those documents. As an example of the use of the information provided by the listed references, LOH affecting a particular target gene provides information on the effect of a particular variance or variances in 15 that target gene. This can be extended to evaluation of the effects of combinations of variations one or more genes subject to LOH. The utilization of conditionally essential genes is described further herein. For complete description, see the respective patent and application. The inventors have also determined that the loss of chromosomes or 20 chromosome segments that is characteristic of cancer cells (often termed loss of heterozygosity, or LOH) has an important interaction with gene sequence variances, in determining the effect of a treatment on a patients cancer cells. Cancer cells with LOH may have only one copy of a gene that is present in two copies in normal cells. If the two normal copies (one inherited from each parent) differ in activity in a given 25 patient, then the cancer cells will be functionally different from the normal cells on account of having only one of the two copies. For example, consider a patient heterozygous for high and low activity forms of a gene that metabolizes a cancer drug. If LOH involving the chromosome containing the gene has left cancer cells with only one copy of the gene then the metabolism of the drug will be different in 30 cancer cells compared to normal cells. If the gene copy that is lost by LOH is the high activity version then cancer cells may experience higher levels of drug (due to slower metabolism) than normal cells. Provided in this invention are specific chromosomal sites characterized by LOH, and the frequency of LOH in different types of neoplasia at said sites. These LOH sites, in conjuction with the variances 35 described above, may prove more useful in predicting response to treatment than variances alone. Methods for determining the combined impact of LOH and variances are described herein. It was recognized that environmental factors can cause certain genes to be essential that are not essential under other conditions (including usual in vivo and culture conditions). For example, certain genes involved in intermediary metabolism are not essential if the cell or organism is supplemented with high concentrations of a particular nutrient or chemical entity, but if that nutrient or chemical entity is absent or present at low levels, the gene product is essential. In another example, the administration of a drug that inhibits one or more functions within the cell can cause other functions to be essential that are not essential in the absence of the drug. In another example, subjecting a cell to harsh physical agents, such as radiation, can cause certain genes to be essential that are not essential under normal conditions. Such genes are essential under certain conditions associated with the therapy of cancer. The demonstration that such genes are present in the population in more than one allelic form and are subjected to loss of heterozygosity in cancer or noncancer proliferative disorders makes such genes targets for allele specific drugs for the treatment of such disorders. It was found that such genes, similar to generally essential genes, are frequently deleted due to LOH in cells of proliferative disorders such as cancers. Treatment methods involving such genes can provide enhanced sensitivity of cancer cells to a variety of different anti-proliferative treatments, including radiation and administration of various compounds. Unless otherwise indicated, the term "essential" includes both strictly essential and beneficial to cell growth or survival. A gene is said to be "conditionally essential" if it is essential for cell survival or proliferation in a specific environmental condition differing from usual in vivo conditions or usual culture conditions for the type of cell, where the specific environmental condition is caused by the presence or absence of specific environmental constituents, pharmaceutical agents, including small molecules or biologicals, or physical factors such as radiation, or if the gene enhances the growth or survival of the cell under such conditions by at least 2-fold, preferably by at least 4-fold, and more preferably by at least 6-fold, 10-fold or even more. Cancer cells, as well as cells from a number of different non-malignant proliferative disorders, from an individual almost invariably undergo a loss of genetic material (DNA) when compared to normal cells. Frequently, this deletion of genetic material includes the loss of one of the two alleles of genes for which the normal somatic cells of the same individual are heterozygous, meaning that there are differences in the sequence of the gene on each of the parental chromosomes. The loss of one allele in the cancer cells is referred to as "loss of heterozygosity" (LOH). Recognizing that almost all, if not all, varieties of cancer undergo LOH, and that regions of DNA loss are often quite extensive, the genetic content of deleted regions in cancer cells was evaluated and it was found that a variety of different conditionally essential genes are frequently deleted, reducing the cancer cell to only one copy. In this context, the term "deleted" refers to the loss of one of two copies of a chromosome or sub-chromosomal segment. Further investigation demonstrated that the loss of genetic material from cancer cells sometimes results in the selective loss of one of two alleles of a partiuclar gene at a particular locus or loci on a particular chromosome. The term "proliferative disorder" refers to various cancers and disorders characterized by abnormal growth of somatic cells leading to an abnormal mass of tissue which exhibits abnormal proliferation, and consequently, the growth of which exceeds and is uncoordinated with that of the normal tissues. The abnormal mass of cells is refened to as a "tumor", where the term tumor can include both localized cell masses and dispersed cells. The term "cancer" refers to a neoplastic growth and is synonymous with the terms "malignancy", or "malignant tumor". The treatment of cancers and the identification of anticancer agents is the concern of particularly prefened embodiments of the aspects of the present invention. Other abnormal proliferative diseases include "nonmalignant tumors", and "dysplastic" conditions including, but not limited to, leiomyomas, endometriosis, benign prostate hypertrophy, atherosclerotic plagues, and dysplastic epithelium of lung, breast, cervix, or other tissues. Drugs used in treating cancer and other non-cancer proliferative disorders commonly aim to inhibit the proliferation of cells and are commonly refened to as antiproliferative agents. "Loss of heterozygosity", "LOH", or "allele loss" refers to the loss of one of the alleles of a gene from a cell or cell lineage previously having two alleles of that gene. Normal cells contain two copies of each gene, one inherited from each parent. When these two genes differ in their gene sequence, the cell is said to be "heterozygous". The term heterozygous indicates that a cell contains two different allelic forms of a particular gene and thus indicates that the allelic forms differ at at least one sequence variance site. When one allele is lost in a cell, that cell and its progeny cells, comprising its cell lineage, become "hemizygous" for that gene or "partially hemizygous" for a set of genes, and heterozygosity is lost. LOH occurs in all cancers and is a common characteristic of non-malignant, proliferative disorders. In general, many different genes will be affected by loss of heterozygosity in a cell which undergoes loss of heterozygosity. In many cancers 10-40%> of all of the genes in the human genome (there are estimated to be 60.000-100,000 different genes in the genome) will exhibit LOH. In the context of this invention, these terms refer preferably to loss of heterozygosity of a gene that has a particular sequence variance in normal somatic cells of an individual such that there is loss of heterozygosity with respect to that particular sequence variance. Also preferably, these terms refer to loss of heterozygosity of a particular sequence variance that is recognized by an inhibitor that will inhibit one allele of the gene present in normal cells of the individual, but not an alternative allele. The present invention provides a number of advantages. For example, the methods described herein allow for use of a determination of a patient's genotype for the timely administration of the most suitable therapy for that particular patient. The methods of this invention provide a basis for successfully developing and obtaining regulatory approval for a compound even though efficacy or safety of the compound in an unstratified population is not adequate to justify approval. From the point of view of a pharmaceutical or biotechnology company, the information obtained in pharmacogenetic studies of the type described herein could be the basis of a marketing campaign for a drug. For example, a marketing campaign that emphasized the superior efficacy or safety of a compound in a genotype or haplotype restricted patient population, compared to a similar or competing compound used in an undifferentiated population of all patients with the disease. In this respect a marketing campaign could promote the use of a compound in a genetically defined subpopulation, even though the compound was not intrinsically superior to competing compounds when used in the undifferentiated population with the target disease. In fact even a compound with an inferior profile of action in the undifferentiated disease population could become superior when coupled with the appropriate pharmacogenetic test. By "comprising" is meant including, but not limited to, whatever follows the word "comprising". Thus, use of the term "comprising" indicates that the listed elements are required or mandatory, but that other elements are optional and may or may not be present. By "consisting of is meant including, and limited to, whatever follows the phrase "consisting of. Thus, the phrase "consisting of indicates that the listed elements are required or mandatory, and that no other elements may be present. By "consisting essentially of is meant including any elements listed after the phrase, and limited to other elements that do not interfere with or contribute to the activity or action specified in the disclosure for the listed elements. Thus, the phrase "consisting essentially of indicates that the listed elements are required or mandatory, but that other elements are optional and may or may not be present depending upon whether or not they affect the activity or action of the listed elements. Other features and advantages of the invention will be apparent from the following description of the prefened embodiments thereof, and from the claims. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS First a brief description of the Tables is provided. Tables 1-6, Gene Tables, lists genes that may be involved in pharmacological response to cancer or other neoplastic disorders, neurological and psychiatric, adsoφtion, distribution, metaboilism, or excretion of, inflammation and immune, endocrine and metabolism, and cardiovascular and renal therapeutics, respectively, or that may define disease subsets with different prognosis and consequent implications for treatment. These tables have seven columns. Column 1, headed "Class" provides broad groupings of genes relevant to the pharmacology of indication-specific drugs. Column 2, headed "Pathway", provides a more detailed categorization of the different classes of genes by indicating the overall puφose of large groups of genes. These pathways contain genes implicated in the etiology or treatment response of the various diseases detailed in Tables 7-11. Column 3, headed "Function", further categorizes the pathways listed in column 2. Some categories in column 2 (e.g. "Clotting") are not further categorized in column 3. In column 4, headed "Name", lists the genes belonging to the class, pathway and function shown to the left (in columns 1 - 3). The gene names given are generally those used in the OMIM database or in GenBank, however one skilled in the art will recognize that many genes have more than one name, and that it is a straightforward task to identify synonymous names. For example, many alternate gene names are provided in the OMIM record for a gene. In column 5, headed "OMIM", the Online Mendelian Inheritance in Man (OMIM) record number is listed for each gene in column 4. This record number can be entered next to the words: "Enter one or more search keywords:" at the OMIM world wide web site. The url is: http://www3.ncbi.nlm.nih.gov/Omim/searchomim.html. An OMIM record exists for most characterized human genes. The record often has useful information on the chromosome location, function, alleles, and human diseases or disorders associated with each gene. In column 6, headed "GID", provides the GenBank identification number (hence GID) of a genomic, cDNA, or partial sequence of the gene named in column 4. Usually the GID provides the record of a cDNA sequence. Many genes have multiple Genbank accession numbers, representing different versions of a sequence obtained by different research groups, or conected or updated versions of a sequence. As with the gene name, one skilled in the art will recognize that alternative GenBank records related to the named record can be obtained easily. All other GenBank records listing sequences that are alternate versions of the sequences named in the table are equally suitable for the inventions described in this application. (One straightforward way to obtain additional GenBank records for a gene is on the internet. General instructions can be found at the NCBI web site at: http://www3.ncbi.nlm.nih.gov. More specifically, the GenBank record number in column 6 can be entered at the url: http://www3.ncbi.nlm.nih.gov/Entrez/nucleotide.htmI. Once the GenBank record has been retrieved one can click on the "nucleotide neighbors" link and additional GenBank records from the same gene will be listed.action, Column 7, headed "locus", provides the chromosome location of the gene listed on the same row. The chromosome location helps confirm the identity of the named gene if there is any ambiguity. Tables 7-11 are matrix tables showing the intersection of genes and therapeutic indications - that is, which categories of genes are most likely to account for inteφatient variation in reponse to treatments for which diseases. The first two columns provide a framework for organizing the genes listed in Tables 1-6. Column 1 is similar to the 'Class' column in Tables 1-6, while column 2 is a combination of the 'Pathway' and 'Function' columns in Tables 1-6. It is intended that the summary terms listed in columns 1 and 2 be read as referring to all the genes in the conesponding sections of Tables 1-6. The remaining columns in Tables 7-1 1 list the specific indications for a given disease category, for example in Table 7 there are thirteen neurological and psychiatric indications. The information in the Tables lies in the shaded boxes at the intersection of various 'Pathways" (the rows) and treatment indications. An intersection box is shaded when a a row conesponding to a particular pathway (and by extension all the genes listed in that pathway in Tables 1 -6) intersects a column for a specific neurological or psychiatric disease such that the pathway and genes are of possible use in explaining inteφatient differences in response to treatments for the neurological or psychiatric indication.. Thus, the Tables enables one skilled in the art to identify therapeutically relevant genes in patients with one of the listed indications for the puφoses of stratification of these patients based upon genotype and subsequent conelatation of genotype with drug response. The shaded intersections indicate prefened sets of genes for understanding the basis of inteφatient variation in response to therapy of the indicated disease indication, and in that respect are exemplary. Any of the genes in the tables may account for inteφatient variation in response to treatments for any of the diseases listed. Thus, the shaded boxes indicate the gene pathways that one skilled in the art would first investigate in trying to understand inteφatient variation in response to therapy for the listed neurological indications. Tables 12-17 lists the exemplary DNA sequence variances in genes for therelevant to the methods described in the present invention. These variances were discovered by the inventors in studies of selected genes listed in Tables 1 -6, and are provided here as useful for the methods of the present invention. The variances in Tables 12-17 were discovered by one or more of the methods described below in the Detailed Description or Examples. The tables have eight columns. The column headings are spread over two rows, with five headings in the first row and three in the second row. The gene sequence variance listings in the tables have a similar organization to the column headings, with a set of nomenclature data in the first row for each gene entry, and variance data in the second and additional following rows for however many sequence variances are available for a specific gene. Column 1, the "Name" column, contains the Human Genome Organization (HUGO) identifier for the gene. Column 2, the "GID" column provides the GenBank accession number of a genomic, cDNA, or partial sequence of a particular gene. Column 3, the "OMIMJ-D" column contains the record number conesponding to the Online Mendelian Inheritance in Man database for the gene provided in columns 1 and 2. This record number can be entered at the world wide web site http://www3.ncbi.nlm.nih.gov/Omim/searchomim.html to search the OMIM record on the gene. Column 4, the VGX_Symbol column, provides an internal identifier for the gene. Column 5, the "Description" column provides a descriptive name for the gene, when available. Columns 6, 7 and 8 are on the second row of columns. Column 6, the "Variance_Start" column provides the nucleotide location of a variance with respect to the first listed nucleotide in the GenBank accession number provided in column 2. That is, the first nucleotide of the GenBank accession is counted as nucleotide 1 and the variant nucleotide is numbered accordingly. Column 7, the "variance" column provides the nucleotide location of a variance with respect to an ATG codon believed to be the authentic ATG start codon of the gene, where the A of ATG is numbered as one (1) and the immediately preceding nucleotide is numbered as minus one (-1). This reading frame is important because it allows the potential consequence of the variant nucleotide to be inteφreted in the context of the gene anatomy (5' untranslated region, protein coding sequence, 3' untranslated region). Column 7 also provides the identity of the two variant nucleotides at the indicated position. Column 8, the "CDS_Context" column indicates whether the variance is in a coding region but silent (S); in a coding region and results in an amino acid change (e.g., R347C, where the letters are one letter amino acid abbreviations and the number is the amino acid residue in the encoded amino acid sequence which is changed); in a sequence 5' to the coding region (5); or in a sequence 3' to the coding region (3). As indicated above, inteφreting the location of the variance in the gene is contingent on the conect assignment of the initial ATG of the encoded protein (the translation start site). It should be recognized that assignment of the conect ATG may occasionally be inconect in GenBank, but that one skilled in the art will know how to carry out experiments to definitively identify the conect translation initiation codon (which is not always an ATG). In the event of any potential question concerning the proper identification of a gene or part of a gene, due for example, to an enor in recording an identifier or the absence of one or more of the identifiers, the priority for use to resolve the ambiguity is GenBank accession number, OMIM identification number, HUGO identifier, common name identifier. Tables 18-23 lists additional DNA sequence variances (in addition to those in Tables 12-17) in genes relevant to the methods of the present invention (i.e. selected genes from Tables 1-6). These variances were identified by various research groups and published in the scientific literature. The inventors realized that these variances may be useful for understanding inteφatient variation in response to treatment of the diseases listed in Tables 7-1 1, and more generally useful for the methods of the present invention. The layout of Tables 18-23 is identical to that of Tables 12-17, and therefore the descriptions of the rows and columns in Tables 12- 17 (above) pertain to Tables 18-23, as do the caveats and other remarks. Tables 24-68 provide lists of exemplary compounds in clinical development for the various disease indications listed in Tables 7-1 1. The compounds listed in the tables are exemplary; that is, the methods of the invention will apply to other compounds as well. Each table has four columns. The first column is titled "Product Name", the second column is titled "Chemical Name" , the third "Action" and the fourth "Indication". Under these headings are listed rows of compounds. For each compound there is a brief summary of information about the product name, its pharmacological action and potential clinical uses. The first column, "Product Name", provides the generic name and/or alphanumeric designation of the compound, as well as its trade name in some cases (in capital letters). The second column, "Chemical Name" provides the full chemical name of the compound. The listed compounds, or compounds chemically related to those listed (e.g. by modification of one or more chemical moieties of the listed compounds), are suitable for the methods of this invention. The third column, "Action", summarizes in a word or phrase an important pharmacological action of the compound, or what is cunently believed to be an important pharmacological action - in most cases additional pharmacological actions are known but not listed to conserve space; alternatively, subsequent studies may reveal additional or alternative pharmacological actions. (Sources listed in the detailed description will help clarify whether additional pharmacological actions have been discovered.) The fourth column, "Indication", provides an exemplary disease or condition for which the compound is cunently being, or has already been, developed. In many cases the compound is being, has already been, or will likely be developed for other indications. Again, one skilled in the art will know how to identify additional drug development programs for these compounds. For example, a compound in development for one neurodegenerative disease is likely to be evaluated in the treatment of other neurodegenerative diseases. Detailed Description Preferred Embodiments I. Disease Indications A. Neurological and Psychiatric Diseases The treatment of neurological and psychiatric diseases presents a challenge to physicians and other medical practitioners because the available therapeutics are only partially effective in only a fraction of patients. Further, many cunently used medicines produce serious adverse effects. Therapeutic benefits and toxic side effects have to be balanced in each patient. This requires much attention to drug selection, dosage adjustment and monitoring for potential adverse events on the part of care givers - effectively a new pharmacokinetic and pharmacodynamic study must be performed for each patient. These limitations of therapy are especially true of the most debilitating neurological and psychiatric diseases such as psychosis, depression, epilepticepilepsy, the neurodegenerative diseases including Alzheimer's disease and Parkinson's disease, migraine and cerebrovascular disease. Although these diseases have distinct clinical presentations, havethere is extensive overlap in pathogenetic mechanisms and symptoms. Difficulties in treating neurological and psychiatric diseases are attributable to factors such as limited understanding of disease condition pathophysiology, lack of specificity of pathophysiologic changes (i.e. variation in pathophysiologic machanisms in patients with similar clinical presentation) and lack of specificity of therapeutic compounds. Further, most medical therapy is directed to the amelioration of symptoms, not the anest or reversal of underlying pathophysiologic processes. One good example of the difficulty of developing and marketing effective treatments is the history of therapeutic candidates for Alzheimer's disease. Out of dozens of candidate treatments tested in clinical trials only two products have been approved for use in the United Statese, and one of them (tacrine; Cognex) has been withdrawn from marketing due to safety problems. Further, the one marketed product (donezepil; Ancept) is only used by a small fraction of eligible patients because it has a reputation among caregivers and Alzheimer's disease advocacy groups as being ineffective in most patients. Thus a drug that enjoys a monopoly position in a major disease is not a great commercial success because its shortcomings are widely realized. In summary, medical management of neurological and psychiatric diseases is empirical in nature, is only partially effective, and is associated with multiple undesirable side effects. In view of these clinical realities, the use of genetic tests to identify treatment responders, nonresponders, and/or those likely to develop undesirable side effects will have a major impact on use of existing classes of CNS drugs, as well as on the development and use of new drugs to treat diseases of the central nervous system. B. Pharmacokinetic Parameters and Effects on Efficacy The pharmacokinetic parameters with potential effects on efficacy are absoφtion, distribution, metabolism, and excretion. These parameters affect efficacy broadly by modulating the availability of a compound at the site(s) of action. Inteφatient variation in the availability of a compound drug, agent, or candidate therapeutic intervention can result in a reduction of the available compound or more compound at the site of action with a conesponding altered clinical effect. Differences in these parameters, therefore, can be a potential foundation of inteφatient variability to drug response. 1.Pharmacokinetic Parameters that Result in a Reduction of Available Drug a. Absoφtion- Depending on the solubility of the drug, and its ability to passively cross membranes is fundamental to the ability of the drug, agent, or candidate therapeutic intervention to effectively enter the circulation and gain access to the principle site of action. For enteral delivery or administration, absoφtion is a critical first step in the pharmacologic process. Within the gastrointestinal tract, absoφtion of a drug, agent, or candidate therapeutic intervention can be affected by the pH of the contents, speed of gastric emptying, and presence of chelating or binding molecules to the drug, agent or candidate therapeutic intervention. Each of these parameters can effectively reduce the rate of passive absoφtion of the drug across the gastrointestinal mucosal membrane. b. Distribution- Once absorbed, the drug, agent or candidate therapeutic intervention must be delivered or distributed to the primary site of pharmacologic action. Although distribution is dependent on regional blood flow and cardiac output; distribution may be further affected by the rate and extent of sequestration of the drug into biological spaces that render the product unavailable to the principle or primary site of pharmacologic site of action. For example, many drugs are actively transported into biological compartments. These processes, if over- or under active may affect the availability and hence reduce the efficacy of the product. Further, only unbound drug may be effective to a cell, tissue, or physiological process, and bound product may be transported to a space that is physiologically unrelated to the pharmacologic mechanism of action or may be of deleterious adverse or toxic consequence. c. Metabolism- Induction of metabolic enzymes to covalently modify the parent drug, agent or candidate therapeutic intervention may reduce the ability of the parent drug to elicit a pharmacologic action. Metabolism may affect the target active site binding, rate and extent of distribution and excretion, and overall availability of the active molecule. d. Excretion- If the excretion of the drug or drug metabolite is rapid, less drug is available to elicit a pharmacologic effect. 2. Pharmacokinetic Parameters that Result in More Available Drug. a. Absoφtion- Enhanced absoφtion of drugs, agents or candidate therapeutic interventions may result in increased drug availability. For example, in some cases of decreased gastric emptying, there is an enhanced degree of absoφtion by prolonging contact with gastrointestinal mucosal membranes. In others, a change in the solubility of the drug may enhance the passive transport across the gastrointesinal mucosal membrane. b. Distribution- Since free drug is the form that renders pharmacologic action and is metabolised and excreted, drug binding may serve to protect the drug from mechanisms of inactivation. The rate and extent of drug binding affects the free drug concentration relative to the total concentration. c. Metabolism- If drug metabolism induction is occurring and the inducer is rapidly removed without adjustment in the dose of the drug, drug metabolism may be decreased and adverse effects or toxicities may occur. d. Excretion- If inhibition of active transport of the parent drug or metabolite across the bile cannicula or the renal tubule, there is a net result of enhanced drug availability. C. Impaired Drug Tolerability and Drug-Induced Disease, Disorder, Dysfunction or Toxicity In response to chemical substances, drugs, or xenobiotics, drug-induced disease, disorder, dysfunction, or toxicity manifests as cellular damage or organ physiologic dysfunction, with one potentially leading to the other. Adverse drug reactions can be categorized as 1 ) mechanism based reactions which are exaggerations of pharmacologic effects and 2) idiosyncratic, unpredictable effects unrelated to the primary pharmacologic action. Although some side effects appear shortly after administration of a durg, some side effects appear long after drug administration or after cessation of the drug. Furthermore, these reactions can be categorized by reversible or ineversible manifestations of the drug- induced toxicity referring to whether the clinical symptomology subsides or persists upon withdrawal of the offending agent. In the first category, excessive drug effects may result from alterations of pharmacokinetic parameters by either drug-drug interactions, pathophysiologic disease mediated alterations in the organs or processes involved in absoφtion, distribution, metabolism, or excretion, or genetic predisposition to heightened pharmacodynamic effect of the drug. The excessive or heightened response may be receptor or drug target or non-receptor or non-drug target mediated. There are a large number of adverse events that are suspected and or known to occur as a result of administration of a drug, agent, or candidate therapeutic intervention. For example, many antineoplastic agents act by prevention of cell division in dividing cells or promoting cytotoxicity via disruption of DNA synthesis, transcription, and formation of mitotic spindles. These agents, unfortunately, do not distinguish between normal and cancerous cells, e.g. normally dividing cells and cancer cells are equally killed. Therefore, adverse events of antineoplastic agents include bone manow suppression leading to anemia, leukopenia, and thrombocytopenia; immunosuppression rendering the patient susceptible and vulnerable to infectious agents; and initiation of mutagenesis and the formation of alternate forms of cancer, in many cases, acute myeloid leukemia. In another example of predictable adverse events related to drug therapy is immunosuppression as a result of therapy to reduce or ablate immune response. This therapy includes but is not exclusive to prevention of graft vs. host or autoimmune disease. These agents, e.g. corticosteroids, cyclosporine, and azathioprine, all suppress humoral or cell-mediated immunity. Patients taking these agents are rendered susceptible to microbial infections, particular opportunistic infections such as cytomegalovirus, pneumocystis carnii, Candida, and sperigillus. Furthermore, long-term immunosuppressive therapy is associated with increased risk of developing lymphoma. Individual drugs are associated with renal injury (cyclosporine) and interstitial pneumonitis (azathioprine). In the second category of adverse events, idiosyncratic reactions arise often by unpredictable, unknown mechanisms or reactions that evoke immunologic reactions or unanticipated cytotoxicity. Adverse reactions in this category are often found together, because often it is difficult to ascertain the etiology of the offending reaction. These toxic events can be specific for a target organ, e.g. ototoxicity, nephrotoxicity, hepatotoxicity, neurotxicity, etc. or are caused by reactive metabolic intermediates and are toxic or create local damage usually near the site of metabolism. Immunologic reactions to drugs are thought or result from the combination of the drug or agent with a protein to form an antigenic protein-drug complex that stimulates the immune system response. Without the formation of a complex, most small molecular drugs are unable, alone, to elicit an immunological response. First exposure to the offending drug produces a latent reaction, subsequent exposures usually results in heightened and rapid immunological response. These allergic reactions, characterized by immunohypersensitivity, are most dramatic in anaphylaxis. There are other immune responses that result in adverse reactions or toxicities they include but are not limited to : 1) immune response mediated cytotoxicity which occurs when the drug-protein complex binds to the surface of a cell and this cell-complex is then recognized by circulating antibodies; 2) serum sickness which occurs when immune complexes of drug and antibody are found in the circulation; and 3) lupus syndromes in which the drug or reactive intermediate interact with nuclear material to stimulate the formation of antinuclear antibodies. In addition to the immune phenomena described above, there are other drug reactions that are syndromes involving allergic reactions. These reactions include, but are not limited to, skin e rashes, drug induced fever, pulmonary reactions, heaptocellular or cholestatic reactions, interstitial nephritis, and lymphadenopathy. Further, there are some drug reactions that mimic allergic reactions but are not immune related. For example, such reactions are due to direct release of mediators by drugs and are called anaphylactoid reactions. An example of this type of adverse event is reaction to radiocontrast dye. These are common adverse drug reactions that may prevent a candidate therapeutic intervention from use, continued development, and marketing rights. Some of these reactions are reversible, others are not. Adverse drug reactions include, but are not limited to, the following organs systems: a) hemostasis which encompass blood dyscrasias (feature of over half of all drug-related deaths) which are bone manow aplasia, granulocytopenia, aplastic anemia, leukopenia, pancytopenia, lymphoid hypeφlasia, hemolytic anemia, and thrombocytopenia; b) cutaneous which encompass urticaria, macules, papules, angioedema, morbilliform-maculopapular rash, toxic epidermal necrolysis, erythema multiforme, erythema nodosum, contact dermititis, vesicles, petechiae, exfolliative dermititis, fixed drug eruptions, and severe skin rash (Stevens-Johnson syndrome); c) cardiovascular which includes anythmias, QT prolongation, cardiomyopathy, hypotension, or hypertension; d) renal which includes glomerulonephritis and tubular necrosis; e) pulmonary which includes asthma, acute pneumonitis, eosinophilic pneumonitis, fibrotic and pleural reactions, and interstitial fibrosis; f) hepatic which includes steatosis, hepatocellular damage and cholestasis; g) systemic which includes anaphylaxis, vasiculitis, fever, lupus erythematosus syndrome; and h) the central nervous system which includes tinnitus and dizziness, acute dystonic reactions, parkinsonian syndrome, coma, convulsions, depresssion and psychosis, and respiratory depression. In the cases whereby severe, fatal reactions occur after drug administration, there may be a warning label in the product insert. For example, tricyclic antidepressants can cause central nervous system depression, seizures, respiratory anest, cardiac arrythmias and anest. The mechanism for the injury is a result of the increased synaptic concentrations of biogenic amines and inhibition of postsynaptic receptors. Acetominophen can cause hepatic necrosis as a result of prolonged high dose usage or overdose. In the hepatocyte, acetominophen is converted to a toxic metabolite that binds to glutathione. As the concentration of acetominophen increases the levels of glutathione are depleted and the toxic acetominophen metabolite then binds liver macromolecules. Aggregation of polymoφhonuclear neutrophils in hepatic microcirculation may cause ischemia and foster necrotic events. Halothane can cause hepatic necrosis as well as prodrome fever and jaundice. Interestingly, the liver effects of halothane are usually after a first time exposure. The hepatic reaction is thought to occur via a genetic predisposition to deran 'sg-e^d metabolism with the formation of toxic metabolites. D. Pharmacokinetic Parameters as Potential Mechanisms of Drug-Induced Adverse Reactions Leading to Disease, Disorder, Dysfunction or Toxicities 1. Absoφtion Absoφtion is the pharmacokinetic parameter that describes the rate and extent of the drug, agent, or candidate therapeutic intervention leaves the site of administration. Although absoφtion is critical for the drug, agent, or candidate therapeutic intervention to ultimately reach the site of physiologic action, the term bioavailability is the parameter that is clinically relevant. Bioavailability is the term used to define the extent to which the active component of the drug, agent, or candidate therapeutic intervention reaches the its site of physiologic action or a biological fluid to which has access to the site of biological action. Although bioavailability is related to all pharmacokinetic parameters, e.g. absoφtion, distribution, metabolism, and excretion, bioavailability is primarily dependent on the first ability of the drug, agent, or candidate therapeutic intervention to be absorbed from the site of delivery, i.e. cross cellular membranes. There are many factors that influence absoφtion of a drug, agent, or candidate therapeutic intervention. For example, compound solubility, conditions of absoφtion, and route of administration. In the present invention, we concern ourselves with genes that are involved in the active or passive process of drug, agent, or candidate therapeutic intervention absoφtion through a biological membrane. The absoφtion surface is dependent on the route of administration. For example, absoφtion of drugs can occur via 1) oral (enteral); 2) sublingual; 3) injections (parenteral, i.e., intravenous, intramuscular, intraarterial, intrathecal, intraperiotoneal, or subcutaneous); 4) rectal; 5) inhalation (pulmonary); 6) topical application (skin and eye). In each of these routes of administration, the adsoφtion rate and extent is dependent on the concentration of the drug at the site, the patency of the epithelial cells, local biological conditions, and function of the active or passive transport. Absoφtion can affect both the efficacy and safety of a drug, agent, or candidate therapeutic intervention. For example, for a compound to achieve full pharmacologic potential, it must be available at the target site, be active, and be unbound. In regards to safety, absoφtion affects safety in one or more of the following: site of delivery pain, necrosis, or irritation; rate of administration; and enatic available concentrations. 2. Distribution The distribution of the drug, agent, or candidate therapeutic intervention is dependent on the rate and extent the compound enters the bloodstream. Once in the bloodstream, the compound may be distributed to the interstitial and cellular fluids. The distribution of drugs to target tissues can be categorized into two phases. The first distribution phase, is dependent on cardiac output and regional blood flow, both of which are dependent on the health and status of the cardiovascular system. In a second distribution phase, diffusion into tissues is dependent on the level and extent that the drug, agent, or candidate therapeutic intervention is bound. Drug binding by proteins found in the blood can serve to protect the compound from modifications by enzymes, proteins, or compounds in the circulation and or limit the bioavailability of the compound to enter target tissues or individual cells. Drug entry into tissues requires free drug, and drug binding proteins may limit this active or passive transport. Once distributed into tissues, the drug may be sequestered within that tissue, to render full pharmacologic activity or to prevent that drug from reaching the appropriate target tissue. Distribution can affect both the efficacy and safety of a drug, agent, or candidate therapeutic intervention. For example, for a compound to achieve full pharmacologic potential, it must be available at the target site, be active, and be unbound. In regards to safety, distribution affects safety in one or more of the following: distribution to a tissue that is more or less affected by the pharmacologic action of the compound, enatic available concentrations, and tissue specific distribution characteristics. 3. Metabolism Drugs or xenobiotics, are usually found in the circulation bound to plasma proteins, generally but not exclusive to serum albumin. It is the bound form of the drug that is taken up by the hepatocyte. Bile salts in the circulation are taken up via organic anion transporters. Once inside the hepatocyte, the drug or bile salt is a substrate for a series of reactions that are either oxidative or reductive or reactions that are conjugative steps in the metabolism of the substrate. Generally these chemical modifications are a refined process to render the substrate more hydrophilic, or polar, to be more likely excreted in the bile (via the intestinal tract) or urine (via the kidneys). However, there are exceptions whereby the redox reactions produce reactive intermediates or products that retard elimination. Except for their role in detoxification, there is little in common among the enzymes involved in the redox detoxification reactions. For certain enzymes there are specific groups that will act as substrates, for others there are general classes of chemical compounds that will be suitable substrates for a given enzyme or enzymes. In the mammalian liver these mechanisms to detoxify and/or enhance the excretion of metabolic by-products, endogenous substrates, and exogenous molecules. The ability to determine whether hepatic function if inadequate is based upon clinical observation, e.g., the presence of jaundice, right upper quadrant abdominal discomfort or pain, pruritis, or by clinical laboratory analyses, e.g., aspartate transaminase (AST or SGOT) or alanine transferase (ALT or SGPT). The hepatic metabolic and excretory mechanisms are critical for short- and long-term survival and are inheritable characteristics. These hepatic biotransformations mechanisms have broad substrate specificity that have been evolutionarily inherited for the host protection from environmental, biological, and chemical substances. There are two categories of drug, agent, or candidate therapeutic intervention biotransformation (metabolism). In the first, phase I, functionalization reactions occur. Phase I reactions introduce or expose a functional group to the parent compound. In general, phase I reactions render the parent compound pharmacologically inactive, however there are examples of phase I reaction activation or retention of activity. In phase II reactions, biosynthetic reactions occur. Phase II conjugation reactions leads to a covalent linkage between a functional group on the parent compound with glucuronic acid, sulfate, glutathione, amino acids, or acetate. The metabolic conversion of drugs is the liver, however, all tissues have enzymatic activity. Factors affecting drug biotransformation are 1) induction of metabolizing enzymes, 2) inhibition of enzymatic reactions, and 3) genetic polymoφhisms. It is the inteφlay of these factors and the health and well being of the patient or subject that determines the fate of parent drug molecules in the body. The first factor affecting drug biotransformation is induction of metabolizing enzyme activity. The metabolic processes that modify drugs or chemicals (oxidation, reduction, or conjugation) can be induced to significant enzymatic activity. Under physiological conditions, the induction process is in place to coordinately metabolize excess substrates. The induction process can be both at the level of enzymatic activity and increased protein levels of the pertinent enzyme or enzymes. Induction may include one or several of the enzymatic pathways or processes in response to the presence of drugs, xenobiotics, endogenous substrates, or metabolic by-products. There may or may not be increased toxicity as a result of increased concentrations of metabolites. Further, induction of phase I reactive processes (oxidation or reduction reactions) may or may not induce the phase II reactive processes (congujation reactions). The second factor affecting drug biotransformation is the inhibition of metabolic enzymes. Enzymatic inhibition can occur via 1) competition of two or more substrates for the enzymatic active site, 2) suicide inhibitors, or 3) depletion of required cofactors for the enzymatic pathways or processes in phase I or phase II reactions. In competitive inhibition, two or more drugs, xenobiotics, or substrates present can interact with the active site of the enzyme. If one drug binds specifically to the enzymatic active site or to an other intracellular regulatory protein molecule, other compounds are blocked from binding and remain unbound. In this case, unmetabolized parent drug or xenobiotic remains in the circulation, potentially for extended periods of time. Competitive inhibition is dependent on the relative specificity of the substrates for the enzymatic active site and the concentration of the drugs or substrates. An example of competitive drug biotransformation inhibition are cimetidine and ketoconazole which inhibit oxidative drug metabolism by forming a tight complex with the heme iron complex of cytochrome P450, and macrolide antibiotics such as erythromycin and troleandomycin are metabolized to products bind to heme groups on the cytochrome P450 molecules. In the second case, the inhibition of enzymes involved in the drug biotransformation process may also occur by suicide inactivation. In these cases, the drug or xenobiotic may interact and covalently modify or render inactive the enzyme involved in the metabolic pathway. In this way, the parent drug compound or molecule is not metabolized, nor is it free to interact with another molecule. Examples of suicide inactivators are secobarbital and synthetic steroids (norethindrone or ethinyl estradiol) which bind to cytochrome P450 and destroy the heme portion of the enzyme unit. In the third case, inhibition of the enzymes involved in the drug biotransformation pathway can also occur by agents or compounds or physiological status that deplete NADPH or other cofactors required for the enzymatic reactions to occur. In the cases of phase I oxidation or reduction, lack of oxygen or NADPH, may reduce the efficiency and activity of a particular enzyme. In phase II reactions, cofactors provide specific groups for the enzymatic covalent modification of the drug or xenobiotic. These phase II cofactors are required for conjugation biotransformation reactions to occur and depletion of these cofactors would be rate limiting. The third factor that can affect drug biotransformation is genetic polymoφhism. Differences among individuals to metabolize drugs have long been known. Observed phenotypic differences, as determined by amount of drug excreted, through polymoφhically controlled pathway/s has lead to a generalized classification of slow (poor) metabolizers and fast (rapid or extensive) metabolizers. In general, poor metabolizers are those with impaired metabolism of a drug via a polymoφhic pathway have been associated with an increased incidence of adverse effects. In addition, to date all major deficiencies in drug metabolizing activity are inherited as autosomal recessive traits. Fast or rapid metabolizers are those individuals with processes that extensively metabolize a drug via a polymoφhic pathway. The fast or rapid metabolizers have been associated with an increased incidence of ineffective treatment. In these individuals active drug is rapidly metabolized to less active or inactive metabolites such that a reassessment of the pharmacokinetic parameters and dosing regimen may require analysis or readjustment, respectively, for appropriate therapy to occur. The first observed and catalogued genetic polymoφhism associated with drug metabolism was described for isoniazid. Isoniazid is a primary drug prescribed for the chemotherapy of tuberculosis. Marked interindividual variation in the elimination of this drug was observed and genetic studies of families revealed that this vaπation was genetically controlled. Isoniazid is predominantly metabolized via N-acetylation. In the analysis of the phenotypically distinct individuals, it was shown that slow acetylators were homozygous for a recessive gene and fast acetylators were homozygous or heterozygous for the wild type gene It has been determined that the incidence of the slow acetylator phenotype is approximately 50% for U.S. Caucasians and blacks, 60-70%> of Northern Europeans, and 5-10% in Asians. Other drugs have been shown to be polymoφhically acetylated, e.g. sulfonamides (sulfadiazine, sulfamethazine, sulfapyridine, sulfameridine, and sulfadoxine). aminoglutethimide, amonafide, amrinone, dapsone, dipyrone, endralazine, hydralazine, pnzidilol, and procainamide. Other drugs that first undergo metabolism and then polymoφhically acetylated are clonazepam and caffeine Another common genetic polymoφhism associated with oxidative metabolism is exemplified by the drug debπsoquine (a sympatholytic antihypertensive). It was discovered that variable inter-patient hypotensive response was due to differing metabolic rates of debrisoquine 4-hydroxylase. Further analysis of family studies revealed that oxidative metabolic reactions are under monogeneic control. A cytochrome P450 enzyme, CYP2D6, was determined to be the target gene for debπsoquine 4-hydroxylase activity. Poor metabolizers of desbπsoquine are homozygous for a recessive CYP2D6 allele and rapid or fast metabolizers are homozygous or heterozygous for the wild type CYP2D6 allele. Uπnary metabolic ratio can be determined after administration of a probe drug and phenotypic assignments (poor or extensive metabolizer) can be identified. The extent of debπsoquine metabolic analysis achieved clinical importance as it was determined that other drugs were poorly metabolized in individuals that poorly metabolized debπsoquine. For example, anti-anyhthmics such as flecainide, propafenone, and mexiletine; antidepressants such as amitryptiline, clomipramine, desipramine, fluoetine, imipramine, maprotiline, mianserin, paroxetine, and nortnptyline; neuroleptics such as haloperidol, peφhenazine, and thioridazine; antianginals such as perhexilene; opioids such as dextromethoφhan and codeine; and amphetamines such as methylenedioxymethamphetamine. Further, many β-adrenergic antagonists are metabolized and are subject to polymoφhic influence in elimination patterns. Another example of a genetic polymoφhism affecting oxidative metabolism was descπbed for mephenytoin, a drug prescπbed for epilepsy. It was shown that a deficiency in the 4'-hydroxylatιon of S-mephenytoin is inhented as an autosomal recessive trait. The other main metabolic pathway, N-methylation of R- mephenytoin to 5-phenyl-5-ethylhydantoιn remains unaffected. Individuals with poor metabolic rate of mephenytoin are subject to adverse central effects, i.e. sedation. Other drugs can be grouped into the poor mephenytoin metabolizers are mephobarbital, hexobarbital, side-chain oxidization of propanolol, the demethylation of imipramine, and the metabolism of diazepam and desmethyldiazepam. Further analysis of other drugs such as the metabolism of antidepressant drugs (citalopram), the proton pump inhibitor omeprazol, the antimalarial drugs pantoprazole and lansoprazole cosegregate with mephenytoin metabolites. Because the majority of metabolic enzymes for the conduct of drug biotransformation occurs in the liver, impairment of liver function as a result of hepatic pathological conditions or other disease states can lead to alterations of hepatic or other organ metabolic drug biotransformation. Liver disease pathologies such as hepatitis, alcoholic liver disease, fatty liver disease, biliary cinhosis, and hepatocarcinomas can impair function of normal physiological metabolic pathways. Further, decreases in hepatic circulation as a result of cardiac insufficiency, hypertension, vascular obstruction, or vascular insult can affect the rate and extent of drug biotransformation. For example drugs with a high hepatocyte extraction ratio would have different metabolism rates affected by alterations of hepatic circulation. Changes in liver blood flow can affect the rate and extent of the metabolism and the clearance of the parent dnig. In all cases of hepatic pathological conditions, the affect on drug biotransformation and clearance of parent drugs or metabolized products will be dependent on the severity and extent of the liver organ and hepatocellular damage. Although hepatic damage may affect the metabolism and clearance of a parent drug or metabolic by-product, residual concentrations of parent drug or metabolic by-products may be deleterious to the liver and its metabolic functions. Following nonparenteral (enteral) administration of a drug, a significant portion of the drug will be metabolized by intestinal or hepatic enzymes before it reaches the general circulation. This first pass effect may generate active drug (administered drug was a prodrug), inactive drug, or toxic drug. Prior to circulation of the metabolized product, circulation to the kidney, the major organ for excretion of the hydrophilic moiety, and excretion via the urine will occur. Therefore, a metabolic product of hepatic metabolic pathways can affect the liver, kidney, and other organs of the body prior to excretion. a. Phase I Drug Biotransformation: Oxidation and Reduction Reactions Enzymatic Oxidation of Drugs In oxidative metabolism, oxidases catalyze the transfer of electrons from substrate to oxygen, generating either hydrogen peroxide or superoxide anions. There are two oxidases present in hepatocytes; they are aldehyde oxidases and monoamine oxidases. Both of these enzymes have broad substrate specificity and contribute broadly to the metabolism of drugs. A third oxidase, xanthine oxidase, may contribute to the oxidation of drugs, due its ability to catalyze the oxidation of heterocyclic aromatic amines, for example methotrexate and 6-mercaρtopurine. Xanthine oxidase in intact tissues is present as a NAD-dependent dehydrogenase, and is converted to an oxidase when there is disruption of the tissue, for example during hepatic cellular damage. Aldehyde oxidase catalyzes the oxidation of fatty aldehydes to carboxylic acids and the hydroxylation of substituted pyridines, pyrimidines, purines, and pteridines. Generally, xenobiotic aromatic nitrogen heterocycles are metabolized by this enzyme. Monoamine oxidase is present in two forms, A and B. They are dimeric proteins consisting of identical subunits and FAD is covalently linked to the protein through a cysteinyl residue. Catalytic cycles of monoamine oxidases A or B occur in discrete steps that take an amine and convert it to an aldehyde, while in the process creating hydrogen peroxide and ammonia. These oxidases have a broad specificity; they protect mitochondrial proteins from xenobiotic amines and hydrazines. Further neurotransmitters are metabolized through this route, e.g. serotonin, dopamine, and catecholamines. Primary alkylamines containing unsubstituted methylene group or groups adjacent to the nitrogen exhibits activity. Activity increases as the length of a side chain, with optimal side length being C6. These enzymes also catalyze the oxidation of secondary and tertiary amines and acyclic amines. Hydrazines can be oxidized by these oxidases. Substrates for monoamine oxidases include but are not exclusive to the following amines: benzylamine, dopamine, tyramine, epinephrine, N-methylbenzylamine, and N,N- dimethlybenzylamine; and the following hydrazines: procarbazine 1 ,2- dimethylhydrazine. Mono-oxygenases are present in liver cell homogenates and contain two distinct types of xenobiotic mono-oxygenases. They are the cytochrome P450 and the flavin-dependent mono-oxygenases. The liver microsomal P-450 system consists of a flavoprotein, and a family of related, but distinct, hemoproteins. The flavoprotein catalyzes the transfer of the electrons from NADPH to the hemoprotein, and is the mono-oxygenase. The reaction also requires phosphatidylcholine. The reductase is a monomeric flavoprotein that contains both FAD and FMN. The reductase is specific for NADPH as a reductant, but other oxidants can be substituted. In addition to cytochrome P-450, the flavoprotein catalyzes reduction of quinones, nitro, and azo compounds. There are many P450 gene families. Subsequent cloning and sequence determination has afforded the ability to divide this gene family into three main groups, CYP1 , CYP2, and CYP3, that are responsible for the majority of drug biotransformation. There are further subdivisions in each of these families, examples being CYP2D6, CYP3 A4, CYP2E 1 , as well as others. Examples of enzymatic inductive processes that affect biotransformation reactions involve the P450 gene family. Specifically, glucocorticoids and anticonvulsants induce CYP3A4; isoniazid, acetone, and chronic ethanol consumption for CYP2E1. Many inducers of the cyotchrome P450 enzymes also induce conjugation metabolic enzymes, e.g. glucuronosyltransferases. In contrast to the monooxygenases, multiple forms of the terminal oxidase (P-450) are present in the hepatocyte. There are many distinct isoforms characterized in different species including humans. It should be noted that mitochondrial P-450 exhibit little or no activity in the metabolism of drugs, xenobiotics, biological compounds, or chemicals. Representative functional groups oxidated by the microsomal P-450 system are as follows: alkanes (hexane, decane, hexadecane); alkenes (vinyl chloride, aflatoxin-Bl, dieldrin); aromatic hydrocarbons (naphthylene, bromobenzene, benzo(a)pyrene, biphenyl); alipathic amines (aminopyrine, benzphetamine, ethylmoφhine); heterocyclic amines (3- acetylpyridine, 4,4'-bipyridine, quinoline); amides (N-acetlyaminofluorene, urethane); ethers (indemethacin, pheancetin. p-nitroanisole); and sulfides (chloropromazine, thioanisole). There are many P450s that have been identified in human liver. Substrate specificities vary among these P-450 dependent mono-oxygenases. For example, P4501A 1 prefers polycyclic aromatic hydrocarbons; P-4501A2 prefers arylamines, arylamides; P-450A26 prefers coumarin, 7-ethoxycoumarin; P-450 2C8, 2C9, 2C10 prefers tolbutamide, hexobarbital; P-450 2C18 prefers mephenytoin; P-450 mp-1, mp-2 prefers debrisoquine and related amines; P450 2E1 prefers ethanol, N- nitrosoalkylamines, vinyl monomers; P-450 3A3, 3A4, 3A5, 3A7 prefers dihydropyridines, cyclosporin, lovastatin, aflatoxins. The effect of genetic polymoφhism of the P450s has been known for some time. For example, debrisoquine and related drugs; alfentanil, tolbutamide; (S)mephenytoin. Because the P450s can be induced by xenobiotics, an enhanced metabolic rate or efficiency can lead to one drug affecting the potency, efficacy, dosing of another. For example, women taking rifampicin or barbiturates can lead to metabolic inactivation of synthetic oral contraceptives. The flavin-containing mono-oxygenases are the principle enzymes catalyzing the N-oxidation of tertiary amine drugs to N-oxides. The N-oxides are found in abundance in serum. Although isoforms have been identified and the catalytic cycle is similar to the cytochrome P450 system, falvin-containing mono-oxygenases substrate specificity differs. Unlike the other flavin-bearing mono-oxygenases, these flavin-containing mono-oxygenases are present in the cell as very reactive oxygen- activated form. It is believed that particular protein structure stabilizes the nucleophilic molecule. Since the molecule is so highly reactive, precise substrate- to-enzyme fit is unnecessary. The following lists substrate types and examples oxidized by the flavin-containing mono-oxygenases: tertiary amines (trifluroperazine, bromopheniramine, moφhine, nicotine, pargyline); secondary amines (desipramine, methamphetamine, propanolol); hydrazines (1,1- demethlyhydrazine, N-aminopiperidine, 1 -methyl- 1-phenylhydrazine); thiols and disulfides (dithiothreitol, β-mercaptomethanol, thiophenol); thiocarbamides (thiourea, methimazole, propylthiouracil); sulfides (dimethylsulfide, sulindac sulfide). Examples of drugs that undergo oxidative reactions are: N-dealkylation (imipramine, diazepam, codeine, erythromycin, moφhine, tamoxifen, theophylline); O-dealkylation (codeine, indomethacin, dextromethoφhan); alipathic hydroxylation (tolbutamide, ibuprofen, pentobarbital, meprobamate, cyclosporin, midazolam); aromatic hydroxylation (phenytoin, phenobarbital, propanolol, phenylbutazone, ethinyl estradiol); N-oxidation (chloφheniramine, dapsone); S-oxidation (cimetidine, chloφromaziine, thioridazine); deamination (diazepam, amphetamine). b. Enzymatic Reduction of Drugs The reductases are a class of enzymes that are involved in the metabolic reduction of xenobiotics. This class of enzymes includes the aldehyde and ketone reductases, the quinone reductases, the nitro and nitroso reductases, the azoreductases, the N-oxide reductases, and the sulfoxide reductases. These classes of enzymes are involved in sequential one-electron reduction of some functional groups and produce radicals that can produce damage cellular components directly or indirectly. The dehydrogenases consist of alcohol dehydrogenases, aldehyde dehydrogenases, or dihydrodiol dehydrogenases. This class of enzymes is involved in the catalysis of hydrogen transfer to a hydrogen acceptor, usually a pyridine nucleotide. c. Hydrolysis of Drugs Alternative reactions of detoxification and metabolism of drugs and xenobiotics are initial steps of hydrolysis. Esters, amides, imides, or other functional groups that are generated as a result of a hydrolysis reaction can alter the hydophilicity of a molecule and enhance urinary excretion. Hydrolysis occurs both enzymatically and nonenzymatically. Hydrolysis of proteins before they are degraded has been suggested as a step in the process of the aging of intracellular proteins. Antibodies with an affinity for certain esters and certain proteases e.g. 3- phosphoglyceraldehyde dehydrogenase and carbonic anhydrase, have been shown to have esterase activity. Enzymatic hydrolysis of drugs and xenobiotics include the following enzymes: esterases, amidases, imidases, and epoxide hydratases. Examples of drugs undergoing hydrolysis reactions are: procaine, aspirin, clofibrate, lidocaine, procainamide, indomethacin. Other hydrolytic processes include reactions owing to both enzymes in tissues, circulation, and those elaborated by microorganisms in the lower bowel; for example, sulfatases, glucoronidases, and phosphatases. b. Phase II Drug Biotransformation: Conjugation Reactions In addition, to the redox reactions of the hepatocyte to detoxify or metabolize xenobiotics, there are a series of conjugation reactions. The substrates for these reactions are generally the products from the redox reactions described above. These conjugation reactions involve donation of a suitable hydrophilic molecular group to an accepting xenobiotic or its metabolite. The major function of these covalent modifications is to render the parent compound pharmacologically inactive. The covalent addition of such a group to a parent drug or compound not only inactivates the substrate but also renders the recipient molecule more polar and is more readily excreted via the bile ducts into the intestinal tract or via the urine. Lipophilic compounds that have one of the functional groups that can serve as an acceptor undergo enzymatic catalysis with a second, donor substrate. The conjugation reactions include the following broad categories: glucuronidation, sulfation, methylation, N-acetylation, and conjugation with amino acids. The enzymes involved in these reactions are as follows: UDP-glucuronyltransferase, alcohol sulfotransferase, amine N-sulfotransferase, phenol sulfotransferase, glutathione transferase, catechol O-methyltransferase, amine N-methyltransferase, histamine N-methyltransferase, thiol S-methyltransferase, benzoyl-CoA glycine acyltransferase, acetyltransacetylase, cysteine S-conjugate N-acetyltransferase, cysteine S-conjugate N-acetyltransferase, cysteine conjugate β-lyase, thioltransferase, and rhodanese. Each of these enzymes has donor and acceptor specificities. The importance of these reactions in the detoxification and metabolism of drugs and xenobiotics are discussed in the examples Examples of drugs that are known to be conjugated are: glucuronidation (acetominophen, moφhine, diazepam); sulfation (acetominophen, steroids, methyldopa); acetylation (sulfonamides, isoniazid, dapsone, clonazepan). 4. Excretion Excretion of parent drugs and metabolites can occur in the excretory organs, namely the kidneys, liver, lungs, skin, and breasts (milk). The kidneys are the most important organs for the excretion of drugs and metabolites. Renal excretion involves glomerular filtration, active tubular absoφtion, and passive tubule reabsoφtion. The more hydrophilic the compound is the more readily excreted via urine. In addition, many drugs and metabolites are excreted via the bile into the intestinal tract. These metabolites may be excreted in the feces, or may be reabsorbed by the gastrointestinal epithelial cell lining. Organic anions and cations, steroids, fatty acids, and other drugs may be specifically transported into the bile canniculus. In all of the metabolism and excretion routes, the physiologic goal is to detoxify and rid the body of drugs, xenobiotics, endogenous or exogenous chemicals, or compounds that may or may not be deleterious to the major organs of the body. In principle the detoxification mechanisms function to attain this goal, however there are many cases of major organ toxicity upon exposure to drugs or metabolites of drugs. Although drugs and drug metabolites predominantly affect the liver and kidneys due to the circulatory and physiological processes, other organs can be affected. In the present invention, we address specific genes that may have polymoφhic sites affecting metabolic rates to ultimately affect these major organ functions. a. Excretion of Drugs and Drug Metabolites via the Bile After parent drugs or xenobiotics are metabolized by redox and or conjugation reactions, the modified products can then be actively transported into the bile cannicula. The transport occurs in an energy dependent fashion requiring ATP. It has been shown that the transporters involved in the active transport from the basolateral (sinusoidal) to the apical (canalicular) surfaces of hepatocytes are members of the ATP binding cassette (ABC) family. The transmembrane electrical potential required to maintain the chemical and electrical potentials required for this active transport is provided by the Na+/K+ ATPases located on the basolateral membrane. Other ion transporters are the potassium channel, sodium-bicarbonate symporter, chloride-bicarbonate anion exchanger, and the chloride channel. In the cholangiocyte there are other ion transporters, for example chloride-bicarbonate anion exchanger, isoform 2, and other organic-solute transporters. Bile acids, phosphatidyl choline, organic anions, organic cations, and cholesterol are actively transported. Approximately 5% of the transporters is multi-drug resistance protein 1 (MDRl ) and the remaining are the phospholipid transporter multi-drug resistance protein 3 (MDR3), alicular multispecific organic- anion transporter (multi-drug resistance associated protein (MRP2 or cMOAT), canalicular bile-salt-export pump (BSEP or SPGP(sister of p-glycoprotein)), sodium-taurocholate cotransporter, organic anion-transporting polypeptide, glutathione transporter, and a chloride- bicarbonate anion exchanger are also involved in the transport. These transporters have been identified to move specific molecules or compounds across biological membranes. For example, the MDRl protein mediates the canicular excretion of bulky lipophilic cations, e.g. anticancer drugs, calcium channel blockers, cyclosporine A, and various other drugs. In contrast, the MDR3 protein transports phosphatidyl choline from the inner leaflet to the outer leaflet of the canicular membrane. Phosphatidyl choline then can be selectively extracted by intracanicular bile salts and secreted into bile as vesicles or mixed micelles. MRP2 is involved in the transport of amphipathic anionic substrates e.g. leukotriene C4, glutathione-S congujates, glucuronides (bilirubin diglucuronide and estradiol-17b- glucuronide), sulfate conjugates, and is responsible for the generation of bile flow independent of bile salts within the bile cannicula. SPGP is the canicular bile salt export pump in the mammalian liver. The hepatocyte has the ability to recruit the ATP-requiring transporters when faced with excessive metabolites. After synthesis, these transporters are stored in compartments that, in response to c AMP, can be actively moved through the cell to the membrane and fused to the cannicula. The active movement from the intracellular compartment to the membrane requires microtubules, cytoplasmic kinesin, cytoplasmic dynesin, and calcium. It has been shown that peptides activate phophosinositide 3 kinase, and increased turnover of phosphoinostides drives the formation of 3'phophoinositol, which can activate the transporter in the membrane and ultimately increases movement to the cannicular membrane. Signaling pathways via the activation of rab5 stimulate the active movement of the transporters to the internal compartment. b. Excretion of Drugs and Drug Metabolites via the Kidney Excretion of drugs or drug metabolites via the kidney and into the urine involves three processes: 1) glomerular filtration, 2) active tubular secretion, and 3) passive tubular reabsoφtion. The amount of drug or metabolites entering the tubular lumen is dependent on its fractional plasma protein binding and glomerular filtration rate. In the proximal renal tubule anions and cations are actively transported by carrier mediated tubular secretion and bases are transported by a separate system that secretes choline, histamine, and other endogenous bases. In the proximal and distal tubules there is passive reabsoφtion of these molecules. The concentration gradient for back-diffusion is created by sodium and other inorganic ions and water. E. Inflammatory or Immunological Disease, Disorders, or Dysfunctions Inflammatory or immunological diseases and clinical symptoms includes diseases and processes such as: arthritis (including rheumatoid arthritis, osteoarthritis, and other degenerative syndromes of the joints), asthma, chronic obstructive pulmonary disease (including bronchitis, bronchiectasis, emphysema and other pulmonary diseases associated with obstruction to air flow), interstitial or restrictive lung diseases, autoimmune disease (including systemic lupus erythematosus, scleroderma and other diseases characterized by autoantibodies), transplantation (often treated with long term immunosuppressive therapy), pain associated with inflammation, psoriasis and other inflammatory skin diseases, atherosclerosis (for which there is strong data supporting the role of inflammatory pathogenetic mechanisms), and hepatitis, among other diseases. One skilled in the art will recognize that there may be overlap between some of the conditions listed. Challenges in treating diseases with a significant inflammatory or immunological component include: (i) limited understanding of the pathophysiologic basis of these diseases and conditions, , (ii) a complex mix of immune/inflammatory mediators operating simultaneously, with the primary (initiating) events often unclear and the relative importance of different mediators unknown, (iii) medical interventions that rarely produce specifical effects, or address the underlying pathophysiologic basis of the disease or condition. Thus, medical management of inflammatory or immunologic disorders is empirical in nature, is associated with multiple undesirable side effects, and disease progression is common. Based upon these clinical realities and the difficulties drug developers face in developing new treatments for diseases with an inflammatory or immunologic component, the use of genotypebased stratification to identify populations enriched for responders, nonresponders, and/or those likely to develop undesirable side effects will provide clear commercial and medical benefits. Ultimately medical practitioners and patients will also benefit from an enlarged choice of medicines with superior safety and efficacy when used in conjunction with genetic diagnostic tests. Inflammation is a complex process that comprises different cellular and physiologic events that can be initiated by tissue injury, by abnormal immune function, or by a wide variety of other endogenous or exogenous factors, not all of which are understood. The inflammatory process can also escape normal regulatory control and become part of the disease process. Autoimmunity is one aspect of some diseases associated with abnormal immunologic function. Such diseases are characterized by the presence of autoantibodies and oligoclonal B cell populations. Immunological reactions associated with loss of self tolerance may be localized to a specific tissue, or may be systemic. Ultimaltely, in severe cases, the immune system produces life threatening damage to tissues, physiological function is compromised. Autoimmunity can be initiated by a variety of endogenous (genetic predisposition and others) and exogenous (chemicals, drugs, microorganisms, and others) factors. F. Endocrine and Metabolic Diseases The treatment of endocrine and metabolic diseases presents a challenge to physicians and other medical practitioners because the available therapeutics are only partially effective in only a fraction of patients (e.g. antiobesity medications). Further, many cunently used medicines produce serious adverse effects (e.g. long term corticosteroid therapy). Therapeutic benefits and toxic side effects have to be balanced in each patient. This requires much attention to drug selection, dosage adjustment and monitoring for potential adverse events on the part of patients and care givers. These limitations of therapy are especially true for the most debilitating endocnne and metabolic diseases such as diabetes and obesity Difficulties in treating endocrine and metabolic diseases are attributable to factors such as limited understanding of disease pathophysiology, lack of specificity of pathophysiologic changes (e.g. different pathophysiologic machamsms in patients with similar clinical presentation) and lack of specificity of therapeutic compounds. Further, most medical therapy is directed to the amelioration of symptoms or other secondary changes (e.g. achieving effective control of blood sugar), not the anest or reversal of underlying pathophysiologic processes. One good example of the difficulty of developing and marketing effective treatments for metabolic and endocrine diseases is the recent history of obesity therapeutics. Only a few products have been approved for treatment of obesity in the United Statese, and one of them, the anorectic agent dexfenfluramine (d-FF; Redux), a 5-HT reuptake inhibitor and releasing agent, was withdrawn from marketing due to safety problems (pulmonary hypertension, valvular heart disease). Further, a recently marketed antiobesity product (sibutramine; Meridia) with a similar mechanism of action Sibutramine, an inhibitor of serotonin and noradrenaline uptake, reduces appetite (inhibition of serotonin and noradrenaline uptake, reducing appetite) is used by only a small fraction of eligible obese patients because anti-obesity drugs now have a reputation among caregivers and patients as unsafe. Thus approved drugs for the treatment of a disorder that affects many million Americans are only moderately commercially successful because their shortcomings are widely recognized. In summary, medical management of endocrine and metabolic diseases is empirical in nature, is only partially effective, and is associated with multiple undesirable side effects. In view of these clinical realities, the use of genetic tests to identify treatment responders, nonresponders, and/or those likely to develop undesirable side effects will have a major impact on use of existing classes of drugs for treatment of endocrine and metabolic diseases, as well as on the development and use of new drugs to treat these diseases. G.Cardiovascular and Renal Diseases The treatment of cardiovascular and renal diseases presents a challenge to physicians and other medical practitioners because the available therapeutics are only partially effective in only a fraction of patients. Further, many cunently used medicines produce serious adverse effects. Therapeutic benefits and toxic side effects have to be balanced in each patient. This requires much attention to drug selection, dosage adjustment and monitoring for potential adverse events on the part of care givers - in many cases (e.g. antihypertensive therapeutics) effectively a new pharmacokinetic and pharmacodynamic study must be performed for each patient. These limitations of therapy are especially true of the most debilitating cardiovascular and renal diseases. Although these diseases have distinct clinical presentations, there is extensive overlap in pathogenetic mechanisms and symptoms. Difficulties in treating cardiovascular and renal diseases are attributable to factors such as limited understanding of disease pathophysiology, lack of specificity of pathophysiologic changes (i.e. variation in pathophysiologic machanisms in patients with similar clinical presentation) and lack of specificity of therapeutic compounds. Further, most medical therapy is directed to the amelioration of symptoms, not the arrest or reversal of underlying pathophysiologic processes. In summary, medical management of cardiovascular and renal diseases is empirical in nature, is only partially effective, and is associated with multiple undesirable side effects. In view of these clinical realities, the use of genetic tests to identify treatment responders, nonresponders, and/or those likely to develop undesirable side effects will have a major impact on use of existing classes of cardiovascular and renal drugs, as well as on the development and use of new drugs to treat diseases of the cardiovascular and renal systems. H. Neoplastic Diseases The unifying feature of neoplastic disease is uncontrolled proliferation and the bulk of modern chemotherapy targets the rapid growth of cancerous tissue. Effective cancer management must destroy or retard the growth of cancerous tissue and prevent the spread of cancerous cells to secondary locations while sparing normal tissues. Cancer therapy has remarkable parallels to the treatment of parasitic infection in that the causative agent is capable of overwhelming growth and rapid mutation to resistant forms. Cancers can differ greatly in their response to chemotherapy: tumors that proliferate rapidly including melanomas, leukemias, and myelomas tend to respond well to classical chemotherapy using cytotoxic agents; tumors that grow slowly, in contrast, such as lung and colon carcinomas tend to respond poorly; the growth of endocrine tumors such as ones of pancreatic, prostate, testicular, ovarian, adrenal, pituitary, or breast origin can be hormonaly dependent and treatment with agonists of insulin, estrogen, progesterone, testosterone, etc. function can prove valuable; and solid tumors are more apt to respond to treatment with antiangeogenesis agents than fluid tumors. Surgery (for solid tumors) and radiation treatment exist as therapies that are often used in conjuction with chemotherapeutic agents. A clinician must select a therapy (often a combination of agents and including radiation treatment or surgery) based on tumor type in addition to evaluating the possible toxicities associated with proposed therapeutic regimens, taking the patiens cunent hepatic, renal and myeloproliferative function into account. Since cunent practice utilizes high doses of cytotoxic agents to minimize the formation of metastasese as well as the appearance of secondary, resistant neoplasms, avoiding toxicity becomes a serious issue given the nanow therapeutic index of most drugs in this category. Medical management of neoplastic disease is empirical in nature, is associated with severe undesirable side effects, and disease progression is common. Based upon these clinical realities and the difficulties medical practioners face in therapy of neoplastic disease, drug development based upon genotype to identify responders, nonresponders, and or those likely to develop undesirable side effects will be an undeniable beneficial addition to cunent medical practice. II. Identification of interpatient variation in response; identification of genes and variances relevant to drug action; development of diagnostic tests; and use of variance status to determine treatment Development of therapeutics in man follows a course from compound discovery and analysis in a laboratory (preclinical development) to testing the candidate therapeutic intervention in human subjects (clinical development). The preclinical development of candidate therapeutic interventions for use in the treatment of human diseases, disorders, or conditions begins at the discovery stage whereby a candidate therapy is tested in vitro to achieve a desired biochemical alteration of a biochemical or physiological event. If successful, the candidate is generally tested in animals to determine toxicity, adsoφtion, distribution, metabolism and excretion in a living species. Occasionally, there are available animal models that mimic human diseases, disorders, and conditions in which testing the candidate therapeutic intervention can provide supportive data to wanant proceeding to test the compound in humans. It is widely recognized that preclinical data is imperfect in predicting response to a compound in man. Both safety and efficacy have to ultimately be demonstrated in humans. Therefore, given economic constraints, and considering the complexities of human clinical trials, any technical advance that increases the likelihood of successfully developing and registering a compound, or getting new indications for a compound, or marketing a compound successfully against competing compounds or treatment regimens, will find immediate use. Indeed, there has been much written about the potential of pharmacogenetics to change the practice of medicine. In this application we provide descriptions of the methods one skilled in the art would use to advance compounds through clinical trials using genetic stratification as a tool to circumvent some of the difficulties typically encountered in clinical development, such as poor efficacy or toxicity. We also provide specific genes, variation in which may account for inteφatient variation in treatment response, and further we provide specific exemplary variances in those genes that may account for variation in treatment response. The study of sequence variation in genes that mediate and modulate the action of drugs may provide advances at virtually all stages of drug development. For example, identification of amino acid variances in a drug target during preclinical development would allow development of non-allele selective agents. During early clinical development, knowledge of variation in a gene related to drug action could be used to design a clinical trial parametersin which the variances are taken account of by, for example, including secondary endpoints that incoφorate an analysis of response rates in genetic subgroups. In later stages of clinical development the goal might be to first establish retrospectively whether a particular problem, such as liver toxicity, can be understood in terms of genetic subgroups, and thereby controlled using a genetic test to screen patients. Thus genetic analysis of drug reponse can aid successful development of therapeutic products at any stage of clinical development. Even after a compound has achieved regulatory approval its commercialization can be aided by the methods of this invention, for example by allowing identification of genetically defined responder subgroups in new indications (for which approval in the entire disease population could not be achieved) or by providing the basis for a marketing campaign that highlights the superior efficacy and/or safety of a compound coupled with a genetic test to identify preferential responders. Thus the methods of this invention will provide medical, economic and marketing advantages for products, and over the longer term increase therapeutic alternatives for patients. There are some examples whereby there is no direct evidence that a gene or genes are involved in drug response of a candidate therapeutic intervention. In these cases, however, there is genetic data supporting a role of a variance or variances involved in the etiology, progression, or risk of the neurologic or psychiatric disease. These cases, including but excluded to anxiety, Huntington's disease, demyehnating disease, pain,Parkinson's disease, spasticity, and stroke are described below with details of cunent therapies and potential genetic involvment of variances in drug responses. Neurological and Psychiatric Diseases There are some examples whereby there is no direct evidence that a gene or genes are involved in drug response of a candidate therapeutic intervention for the treatment of neurological or psychiatric disease. In these cases, however, there is genetic data supporting a role of a variance or variances involved in the etiology, progression, or risk of the neurologic or psychiatric disease. These cases, including but excluded to anxiety, Huntington's disease, demyehnating disease, pain, Parkinson's disease, spasticity, and stroke are described below with details of cunent therapies and potential genetic involvment of variances in drug responses. A. Anxiety Description of Anxiety Anxiety is a common, nonspecific symptom associated to a greater or lesser degree with many psychiatric diseases, including psychoses, neuroses, mood disorders and personality disorders. It is also an inevitable component of everyday life brought on by stressful events such as medical or surgical procedures. Some prominent nonspecific symptoms of anxiety include tachycardia, chest pains, or inegular heartbeat; epigastric distress; headache, dizzyness, syncope, or parethesias. It is usually some combination of these physical manifestations of anxiety that impels patients to seek medical care. It has been estimated that approximately 13% of primary care visits are substantially attributable to anxiety. There are both acute and chronic anxiety syndromes The acute forms include panic attacks and event-related anxiety Chronic, or generalized anxiety is a pervasive feeling of nervousness that does not subside Because both panic-attack and generalized anxiety lead to desire for being alone or away from public places, many patients adopt agoraphobic tendencies These patients can become housebound because of fear of having a panic attack in a public setting Cunent Therapies for Anxiety The pnncipal treatments for anxiety have been benzodiazepines, monoamine oxidase inhibitors, antidepressants, and β-adrenergic antagonists In all cases, both panic attack and generalized anxiety, concunent continued behavioral and psychological therapy is required to regain a sense of normal life function Limitations of Cunent Therapies for Anxiety The difficulty in determining the efficacy of psycho tropic drugs for the treatment of anxiety is the subjective contπbution of the nonpharmacologic factors that are associated with anxiety However, the relative safety of benzodiazepines, pharmacologic actions, and high demand make these products drugs of choice in the treatment of anxiety The benzodiazepines are associated with side effects due to CNS depression, drowsiness and ataxia Other side effects are increase in hostility or irπtabihty, confusion, weight gam, skin rash, nausea, headache, impairment of sexual function, vertigo, and ghtheadedness Future Drug Development for Anxiety In Tables 2, 13and 19, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be cntical for the identification and stratification of a patient population diagnosed with anxiety based upon genotype Cunent pathways that have possible involvement in the therapeutic benefit of anxiety include, but are not limited to, serontonergic, GABAergic, punnergic, adrenergic, glutammergic, dopaminergic, cholmergic, glycinergic, cholecystokinin, corticotropm releasing factor, histaminergic, opiate, tauπne, oxytocin, neuropeptide Y, estrogen, hemostasis, tachykmin, vasopressmergic and second messenger intracellular cascades gene pathways that are listed m Tables 2, 13 and 19 One skilled m the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of anxiety, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for anxiety Below, Table 26 lists the therapies in development for anxiety categorized by the gene pathway mechanism of action as in Table 7. The listed candidate therapeutic interventions response in patients with anxiety may be affected by polymoφhims in genes as described above. B. Huntington's disease Description of Huntington's Disease Huntington's disease (HD) is an inherited disorder characterized by the gradual onset of motor incoordination and cognitive decline in mid-life. Symptoms develop insidiously either as a movement disorder manifested by brief jerk-like movements of the extremeties, trunk, face, neck (choreas) or as personality changes. Fine motor incoordination and impairment of rapid eye movements are early features. Bradykinesisas and dystonia may predominate if the onset occurs early in life. As the disorder progresses the involuntary movements become more severe and are characterized by: dysarthria, dysphagia, and impaired balance. Cognitive deficits begin by features of slowed mental processing, difficulty in organizing complex tasks, and memory deficits (family, friends, and immediate situation is unaffected). These patients have tendancies to become irritable, anxious, and clinically depressed. In rare cases there may be paranoia or delusional states. There are approximately 25,000 Americans diagnosed with HD. Cunent Therapies of HD Cunent therapies do not include alternatives for the treatment of the progression of the neurodegeneration. Medical management of the associated clinical symptoms includes the following categories: depression, psychosis, and choreas. In the cases of depression and psychoses, the therapies of beneficial therapeutic use are described in this invention. The treatment of choreas generally includes neuroleptic agents that affect dopaminergic pathways by antagonism at the receptor level. Monoamine depleting dru -.g_,s.. can also be used to minimize choreas. Limitations of Cunent Therapies of HD Efficacy Limitations Conventional and atypical neuroleptic agents are not uniformly able to reduce the signs and symptoms of choreas in HD patients. Efficacy varies in the HD population in one or combination of the following ways: 1) patients are only partially responsive or 2) patients are therapy resistant. Unfortunately, limited efficacy in a HD population in light of the presence of undesirable side effects may lead to compliance issues, abenant drug abuse behavior, and further safety issues. Thus, a clinician when presented with a newly diagnosed HD patient, m general, follows standard neurological society or published guidelines for first line therapy. However, when faced with a partially responsive or therapy resistant patient, the clinician can choose from multiple agents, none being completely effective, has limited guidance or rationale to select one agent the other, and follows an empincal medical decision making course of action. Toxicity Limitations Unfortunately, conventional neuroleptic drugs are uniformly, and atypical are latently, associated with undesirable dose-dependent side effects. These include but are not exclusive to sedation, weight gain, cognitive deficits, sexual or reproductive insufficiencies, agranulocytosis, cardiovascular complications, neuroleptic malignant syndrome (parkinsonism with catatonia), jaundice, blood dyscrasias, skin reactions, epithelial keratopathy, seizures, and extrapyramidal effects. The blood dyscrasias include mild leukocytosis, leukopenia, and eosinophiha. The skin reactions include uticana and dermititis and are usually associated with phenothiazmes. Epithelial keratopathy and opacities in the cornea is associated with chloφromazme therapy. In extreme cases these effects may impair vision. These ocular deposits tend to spontaneously disappear upon discontinuation of chloφromazine drug therapy The extrapyramidal side effects of conventional neuroleptics include dystonia (facial gπmacing, torticollis, oculgync crisis), akathesia (feeling of distress or discomfort leading to restlessness or constant movement), and parkinsonian syndrome (πgidity and tremor at rest, flat facial expression). With long term usage of conventional neuroleptic drugs, tardive dyskmesias uniformly appear in HD patients. Tardive dyskinesia is a syndrome of repetitive, painless, involuntary movements. These abnormal involuntary movements are insuppressible, stereotyped, autonomic movements that cease only during sleep, vary in intensity over time, and are dependent on the level of arousal or emotional distress. The syndrome is characterized by quick choreiform (ticlike) movements of the face, eyelids (blinks or spasms), mouth (grimaces), tongue, extremities, or trunk. These movements may have varying degrees of athetosis (twisting movements) and sustained dystonic postures. Increasing the dose of the conventional neuroleptic agent can reverse extrapyramidal effects observed in patients. However, increasing the dose ultimately leads to more severe dyskinesias. Antiparkinson agents tend to exacerbate the tardive dyskinesia symptoms and thus are not used clinically. Because dopaminergic agonists tend to worsen the symptoms and dopaminergic antagonists tend to retard the symptoms of tardive dyskinesias, the optimal alternative is to use a neuroleptic agent that has selective dopaminergic antagonist activity. This alternative therapy would manage both psychosis and dyskinesias. Often a clinician faces the dilemma of a patient with medically managed choreas, but the dose-related tardive dyskinesias, agranulocytosis, or seizures compels the medical care personnel to opt to switch therapies to possibly those agents or drugs with fewer or less severe side effects but with substandard or limited efficacy. Under these conditions, inability to treat the psychotic or chorea symptoms with the backdrop of ineversible dyskinesias leaves the patient with few alternatives. III. Impact of Genotyping on Drug Development for HD There have been reports of polymoφhisms in key genes that affect neuroleptic activity in schizophrenic patients. These polymoφhisms may be further applicable for neuroleptic response in HD patients. For example, within the dopamine D4 receptor subtype, there are known tandem repeats in exon 3. In a recent study, schizophrenic patients on maintenance doses of chloφromazine were stratified into two groups, one having 2 tandem base pair repeats and the other having 4 tandem base pair repeats. Thirty- four percent of group one patients and 62% of group two patients had a favorable response to chloφromazine therapy duπng acute stage treatments. The presence of homogeneous four 48 base pair repeats in both alleles in exon 3 of the dopamine D4 receptor subtype thus appears to be associated with beneficial chloφromazine response. Recently, a study of the serotonin receptor subtype 6, polymoφhism (T267T vs. C267T) in a group of patients refractory to clozapine therapy was reported. In this study, it appeared that the T267T genotype patients were more likely to respond to continued therapy that those patients with C267T genotype patients. A recent report documented a conelation of the serotonin 5HTC2 receptor subtype biallelic polymoφhism and neuroleptic efficacy. A significant number of schizophrenic patients homozygous for the allele C2 responded unsatisfactorily to antipsychotic medication as compared to control. Three polymoφhisms in the serotonergic receptors, i.e. 5HT2A (T102C); 5HT2C (cys23ser); and 5HT2A (his452tyr) have reports of positive or negative conelation with efficacy of antipsychotic therapies. This disparity in the literature will, in the future, be further examined in schizophrenic patient populations and conelation may be discovered V Description of Mechanism of Action Hypotheses for Future Drug Development The genetic basis of the disease has been identified. A gene, huntingtm, whose protein has a mechanism yet to be defined, has a senes of CAG tandem repeats The number of CAG repeats do conelate somewhat with age of onset and the seventy of the disease. Cell death starts in the caudate nucleus by an unknown mechanism The huntingtm protein is essential to life The huntingtm protem undergoes cleavage as cells age The mechanism of cleavage is performed in part by members of the caspase enzymatic family As the huntmgtin protein is cleaved into smaller units, the peptides become toxic, and it has been shown that the smaller fragments tend to migrate into the nuclear compartment. It has been shown that preventing huntingtm cleavage prevents cellular toxicity. Some of the cleaved huntingin fragments form aggregates which may promote or be a by-product of neuronal cell death. The profound loss of neurons in the brams of patients with HD has lead to many development programs for the promotion of neural regeneration These programs broadly include cytokines, growth factors, and agents that promote neural or glial cell growth Further, consideration of preventing neuronal cell death includes apoptosis inhibition and others Other programs include prevention of prolonged excitatory neurotransmission These neurons switch their aerobic metabolism to anaerobic metabolism leading to glycolytic metabolism and excessive production of lactate and metabolic by-products. Excitatory neural inhibition, improvement of energy metabolism, and inhibition of cell death signals may ultimately play a cntical role in preventing, retarding, or halting neurodegeneration in HD patients. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of vaπous drugs or compounds. In Tables 1-6, 12-17, 18-23, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be cntical for the identification and stratification of a patient population diagnosed with HD based upon genotype. Cunent pathways that may have involvement m the therapeutic benefit of HD include glutammergic, serontonergic, dopaminergic, chohnergic, opiates, estrogen, mitochondnal maintenance, growth, differentiation, and apoptosis, secretion gene pathways that are listed in Tables 2, 7, 13, and 19 One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of HD, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for HD. Below in 30 is a list of therapies in development for HD categorized by the gene pathway mechanism of action. The listed candidate therapeutic interventions response in patients with HD may be affected by polymoφhisms in genes as described above. C. The Demyehnating Diseases Description of Demyehnating disease Primary demyehnating diseases result in loss of the myelin sheath that sunounds axons, with preservation of the axons. The main demyehnating diseases are multiple sclerosis, including its variants (Marburg and Balo variants of MS and neuoromyelitis optica), and the perivenous encephalitides, which include acute disseminated encephalomyelitis and acute necrotizing hemonhagic leukoencephalitis.. Due to the paucity of information concerning etiology of these diseases, identification and classification is largely descriptive. The most common and best studied of these diseases is multiple sclerosis. Descπption of Multiple Sclerosis Clinically, MS usually starts as a relapsing illness with episodes of neurological dysfunction lasting several weeks, followed by substantial or complete improvement. This is the relapsing-remitting phase of the disease. Many patients remain in this stage of the disease for years or even decades, while others rapidly progress to the next stage, secondary progressive MS, in which, with repeated relapses, recovery becomes less and less complete. There is also a steadily progressive relapse-independent form of the disease termed primary progressive MS. This form is characterized by a steady worsening of neurological function without any recovery or improvement, and more often affects men. Cunent Therapies for Multiple Sclerosis Although the pathogenesis of MS is not understood, there is accumulating evidence that immunoregulatory mechanisms are involved. Cunent therapy of MS is therefore directed to modulating immune function and thereby halting or retarding myelin degeneration, or facilitating remyelination. Remyelination has been shown to occur spontaneously in response to therapeutic interventions in animals (both normals and MS models). However, in MS animal models remyelination appears to be aborted soon after it begins. For relapsing-remitting MS the following agents are cunently in use : 1 ) interferon beta- 1 β (Betaseron) reduces annual relapse rate and reduces development and progression of new lesions in relapsing-remitting MS as monitored by magnetic resonance imaging (MRI), and has been shown to reduce annual relapse rate, reduce disability progression, and delay increase of lesion volume by MRI in secondary progressive MS; 2) Interferon beta-la (IFN-beta-lα; Avonex) treatment results in reduced disability progression, annual relapse rate, and new brain lesions, as visualized by MRI; 3) Glatiramer acetate (Copaxone; Copolymer- 1; Cop-1) reduces annual relapse rate; 4) Intravenous immunoglobulin, reduces annual relapse rate, and delays disability progression; 5) High-dose methylprednisolone therapy is effective in shortening MS attacks, and may be useful in the long term treatment of secondary-progressive MS; 6) Other agents that have been used with success are mitoxantrone, azathioprine and methotrexate. The latter drug, in particular, has been shown effective in reducing disease activity, both by decreasing the number of exacerbations and by slowing clinical progression. The first four agents are of comparable efficacy in the treatment of relapsing-remitting MS. Not enough trials have been performed to reliably assess the utility of treating nonresponders to one of these treatments with a different treatment, or to assess potential markers of response. III. Limitations of Current Therapies for Multiple Sclerosis The available treatments have both efficacy and toxicity limitations. Further, the cost for one year of interferon treatment is approximately SI 1,000 and parenteral administration is inconvenient. Partial Response to Therapy Cunent therapies reduce, but do not arrest, disease progression, and only a fraction of patients benefit from treatment; approximately 30%> of patients on interferons experience reductions in relapse rates. For primary progressive MS, there are cunently no effective therapies available; interferon beta- lb has in fact been shown to worsen spasticity in primary progressive MS. Undesired Side-Effects or Toxicities as a Therapeutic Limitation All interferons are associated to varying degrees with flu-like symptoms, muscle- ache, fever, chills, and asthenia. There are also side effects that are difficult to distinguish from the course of the demyehnating illness, for example interferons may lower the seizure threshold and exacerbate depressive illnesses, two clinical problems also observed in patients without interferon therapy. Impact of Pharmacogenomics on Drug Development for Multiple Sclerosis Aspects of therapy for demyehnating disease that can be addressed by pharmacogenetic methods include: 1 ) Which patients are most likely to respond to medication? 2) Which drugs are most likely to benefit which patients? 3) What is the optimal dose and duration of treatment? 4) What is the relationship between disease type, stage and manifestations and drug response? 5) Can adverse treatment responses be predicted? As an alternative to directly conelating genetic variants with clinical responses to therapy, one could also use quantitative biochemical, immunological or anatomical measures of disease activity to assess the impact of genetic variation in candidate genes on response to medication. While it is unlikely that all therapeutic responses are under strong genetic control, it is expected that if stratification based upon genotype were performed in clinical trials a conelation between drug response and genotype will be detected for at least some treatment responses. Described below and in Tables 2 and 7 are gene pathways that affect cunent drug therapy as well as drugs cunently in development for MS. Described in the Detailed Description are methods for the identification of candidate genes and gene pathways, patient stratification, clinical trial design and statistical analysis and genotyping for testing the impact of genetic variation on treatment response in multiple sclerosis and other demyehnating diseases. A sample of therapies approved or in development for preventing or treating the progression of symptoms of MS cunently known in the art is shown in Table 32. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Mechanism of Action Hypotheses for Novel Therapies for Multiple Sclerosis: Utility of Genotyping Several possible mechanisms by which intravenous immune globulin (INIG) modulates the course of the disease are related to limiting the inflammatory process and repairing the damage by enhancing remyelination. The efficacy of dexamethasone (DX) and methylprednisolone (MP) at high (HD) and low (LD) dose in acute multiple sclerosis (MS) relapses was evaluated by a double-blind trial in 31 patients followed for 1 year. DX and HDMP were similarly efficacious in promoting recovery, while LDMP was ineffective in the short-term outcome and was followed by an early clinical reactivation. The different outcomes seem to be related to different immunomodulating effects, mainly on cerebrospinal fluid (CSF) IgG synthesis and on peripheral blood and CSF CD4+ lymphocyte subsets. The efficacy of interferon should be investigated in relation to other treatment options, such as immunoglobulin, copolymer I, azathioprine and methotrexate. Other promising therapeutic options (mitoxantrone, intravenous immunoglobulins, drug associations) are under evaluation. Pathogenesis of MS There are three cunent theories for the cause of MS that have been studied to effectively understand the mechanism of disease as well as establish rationale for the development of effective candidate therapeutic interventions. The three cunent theories are 1 ) viral infection, 2) genetic predisposition, 3) inflammation and autoimmunity, and 4) ion channel modulators. Viral Infection Indirect evidence that there is a single unique virus causing MS is the unusual geographic distribution of the disease. There is a documented north-south gradient of disease prevalence, migration studies, and reports of clustering of cases have indicated an environmental influence on disease susceptibility. Despite years of intense research including viral isolation studies from tissue samples of MS patients and controls, has not resulted in identification of an MS specific virus or viral sequence. One virus implicated in the pathogenesis of MS is the human heφes virus type 6 (HHV-6). HHV-6 is a neurotropic virus that can establish a latent infection in man. HHV-6 protein and DNA have been isolated and identified from neuroglial cells in active MS spinal lesions. Further, HHV-6 IgM titers in MS patients and HHV-6 DNA identified in serum samples indicate a recent infection. However, to date there is no evidence that HHV-6 is the causal infectious agent of MS. Instead, a hypothesis of molecular mimicry has been proposed as a likely possibility to explain the indirect immune-mediated injury to otherwise normal tissue in the course of clearing an infectious agent. Besides HHV-6, there are other neuro-specific infectious agents that may damage the CNS through this mechanism. The molecular similarity (mimicry) between virus and myelin antigens may be permissive for immunological cross-reactivity between HHV-6 and myelin antigens. In this model, the T-cells become activated, cross the blood brain barrier and misidentify normal myelin antigens as 'virus' resulting in T-cell mediated cellular and tissue injury. Genetic Susceptibility to MS Although MS is a sporadic disease, studies have pointed to an organized familial clustering, which suggests a genetic predisposition to MS. Equally likely, these studies also suggest that there is a genetic predisposition to an environmental stress or causal event. The most convincing evidence of a genetic predisposition to MS is derived from studies of a population-based study of twins. The risk of MS increases with the degree of shared information within a family. There is further a marked increase in concordance for MS in the comparison of monozygotic and dizygotic twins. Inflammation and Autoimmunity in MS While it is clear there is an inflammatory component to the lesions of MS, is it cunently unclear whether the immune system plays a role in initiation of the characteristic damage of white matter. In experimental studies of animal models of MS, there appears to be T-cell , CD4+ and CD+8, autoreactivity to several putative CNS antigens including myelin basic protein, proteolipid protein, myelin oligodendroglial glycoprotein, 2 ',3 '-cyclic nucleotide phophodiesterases, myelin-associated glycoproteins, and viral antigens. Further, there appears to be down regulation of cytokine production including TNF- α and IL-3. These observations have led to the following proposed mechanism of immune-mediated injury in an MS lesion. Genetic and environmental factors (e.g. viral infection, molecular mimicry, bacterial lipopolysaccharides, superantigens, local metabolic stress, oncogene expression, or reactive metabolites) may potentiate the movement of T-cells through the blood-brain barrier to the CNS. These same genetic and environmental factors may act within the CNS to upregulate the expression of intracellular adhesion molecules on endothelial cells and the circulating T-cells which in turn enhances the rolling, binding, diapedesis, and ultimate migration of the T-cells into the CNS. The same genetic and environmental factors may activate the secretion of αβ-crystallin on the oligodendrocytes rendering these cells more susceptible to T cell recognition. The T-cells once in the CNS then secrete cytokines (TNF-β and INF-γ) activate the antigen presenting cells (astrocytes, microglia, and macrophages) enhancing (macrophage, microglia) or inhibiting (astrocytes) further immune signaling. The activated T cell then encounters the putative MS antigen or antigens in light of the MHC class II molecules on the antigen presenting cells, resulting in T-cell activation. The activated T-cells can then differentiated into Thl or Th2 type CD4+ cells which then results in proinflammatory or anti-inflammatory cytokine signaling, respectively. It has been shown in MS patients that antibody, complement, and antibody-mediated cellular toxicity mechanisms may cause the myelin lesions. Ion Channel Modulations in MS Reduction of the depolarization in postsynaptic membranes by modulation of the ion channels in nerve and muscle tissue has been postulated as a mechanism to ablate abenant neurotransmission in demeylinating neurological disease. Proposed gene targets to produce the membrane depolarization are the nicotinic acetylcholine receptor, voltage gated Na+ channels, and other ion channels. Future Therapeutic Strategies for MS The future strategies for the beneficial therapy of MS are borne out of the existing mechanisms of the etiology of this demyehnating disease as previously described. They are antivirals, cytokine and anticytokine strategies, immune deviation strategies to enhance Th2 cell/cytokine performance, matrix metal loproteinase inhibitors, trimolecular complex strategies, cathepsin B inhibitors, and oxygen radical scavengers. Specifically, antivirals include valcylcovir and acyclovir. Cytokine and anticytokine strategies include TNF inhibitors, antiinflammatory cytokines, and inhibitors of proinflammatory cytokines. Immune-deviation strategies to enhance Th2 cell/cytokine predominance includes pentoxifylline, transforming growth factor-β (TGF-β), and 11-10, 11-4 alone in combination with corticosteroids. Matrix metalloproteinase inhibitors include D-penacillamine, and hydroxyamatate. Trimolecular complex strategies include anti-MHC monoclonal antibodies, MHC class II hypervariable peptide vaccines, anti-T cell monoclonal antibodies, altered peptide ligands, T cell vaccination strategies (myelin basic protein reactive T-cell, T- cell receptor peptide vaccination), co-stimulation strategies (antib7-l , CTLA-4Ig fusion proteins, CD40/CD40 ligand interactions), and adhesion molecule signaling strategies (monoclonal antibodies, or small molecules directed to these adhesion molecules). Neural regeneration development programs will include growth factors including NGF, BDGF, CNTF, NT-3, and other cytokines, as well as other factors that are involved in the support of nerve cell viability, growth, and sustaining neural transmission. Technological advances that reduce difficulties in determining progression of the demyelination by neuroimaging techniques will aid development of new therapies. Estimation of expected clinical and sunogate measures and patterns to identify, screen, and develop statistically derived stopping rules for efficacy and futility. Further, there may be genes within pathways that are either involved in metabolism of neuro transmitters or are involved in metabolism of various drugs or compounds. In Tables 2, 13, 19 there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with MS based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of epilepsy include glutaminergic, GABAergic, opiates, corticotropin releasing hormone, potassium channel, prostaglandin, platelet activating factor, cytokines, clot formation, second messenger cascade, growth, differentiation, and apoptosis, cytoskeleton, adhesion, and myelination gene pathways that are listed in Tables 2, 7, 13, and 19- One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of MS, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for MS. D. Pain Description of Pain Chronic pain can be caused by chronic pathologic processes in somatic structures or viscera, or by prolonged dysfunction of parts the peripheral or central nervous system.. In all there are approximately 70 million Americans that experience chronic pain. Chronic pain may be the result of recunent headache, arthritis, back or spinal injuries, musculoskeletal disorders, cardiac or visceral pathologies. Chronic pain is also part of the clinical manifestation of cancer; many of these cases are medically intractable pain. Chronic pain syndromes include polyarteritis nodosa; systemic lupus erythmatosus; entrapment neuropathy; lumbar plexitis; Bell's palsy; caφal tunnel syndrome. Chronic pain can also result from peripheral neuropathies: diabetic neuropathy (neuropathic complications of diabetes mellitus include distal symmetric, sensory, autonomic, asymetric proximal, cranial and other mononeuropathies); cervical radiculopathy; Guillain-Bane syndrome; brachial plexitis; familial amyloid neuropathy; HIN neuropathy; post spinal cord injury; and post heφetic neuralgia. Cunent therapies for Pain Therapeutic management of chronic pain includes a three step ladder approach: non-opioid analgesics are stepwise prescribed in combination with moderate to potent opiates. The guidelines call for a determination by the patient and the physician of pain relief Broadly speaking, the guidelines are as follows mild pain is treated with non-opioid analgesics, moderate or persisting pain is treated with a weak opioid plus non-opioid analgesics, and severe pam that persists or increases is treated with a potent opioid plus non-opioid analgesics Pain management regimens include not only the use of opioids and non- opioid analgesics, but also benzodiazepines, local anesthetics, anticonvulsants, antichohnergics, serotonin norepmephnne reuptake inhibitors, neuroleptics, and barbiturates These drugs in combination can relieve associated symptoms of chronic pain syndromes such as anxiety, acute on top of chrome pain, seizures, dry mouth, dehnum, and inability to sleep, respectively Treatment options for chronic pain fall into the following categones 1 ) general health promotion and relief from exacerbating factors, 2) nonnarcotic pharmacologic, 3) physical; 4) surgical, and 5) narcotic The nonnarcotic empincal therapies include tπcychc antidepressants (amitπptyhne, nortnptyhne, doxepin, lmipramine), anticonvulsants (carbamazepine, phenytoin), GABAergic agonists (BACLOFEN ® ) and antipsychotics (fluphenazme) Narcotic therapies include opioid agonists (methadone and fentanyl) Devices and surgical therapies can be used in combination with drug therapy In general these therapies have been shown to reduce pain and each are descnbed in detail below Antidepressants The tertiary amines are the most commonly used anti-depressants to manage pain associated with post-SCI Although the exact mechanism is unknown the interference with the re-uptake of neurotransmittters (dopamine, norepmephnne, and serotonin) may reduce pam transmission m the afferent pathways Further, the increased quantities of these neurotransmitters in the areas of the hyperexcitable neurons, descending pain inhibitory pathways that terminate in the substantia gelatmosa of the dorsal horn, may act to reduce pain transmission Interestingly, the dose of the tncychcs for the management of pam is approximately half that required for the management of depression These compounds can be determined to be effective for pain management in approximately two weeks Anticonvulsants Reports exist descnbmg chronic neuropathic pam syndromes as a central neurophysiologic epileptiform activity of the uncontrolled hyperactive neurons leading to a convulsive syndrome in the spinal cord Thus, anticonvulsant therapies are considered to stabilize the threshold against hyperexcitabihty of neurons and inhibiting the spread of epileptiform activity in neurons involved in nociception Further, activation of inhibitory neurons may lead to a pain reduction Although the data is not conclusive, it appears that anticonvulsants are more effective when given in combination with antidepressants. Neuroleptics: The neuroleptics are thought to exert a potentiation of the antidepressants and may impart a dopaminergic antagonism. Neuroleptics are usually given in combination with an antidepressant. GABAergic agonists: Baclofen, a GABAegeic agonist when delivered intrathecally was effective in reducing chronic pain in those patients in which the pain was of musculoskeletal origin (83%> of these patients), but was ineffective in those patients with neurogenic pain (78% experienced no change). Physical treatments: Physical treatments include transcutaneous electrical nerve stimulation (TENS) and spinal cord stimulation devices. Using TENS, some success has been reported to reduce peripheral pain. Upon placing the electrodes, peripheral sensory nerve stimulation is thought to activate pain inhibitory intemeurons in the substantia gelatinosa or dorsal root entry zone of the spinal cord. Spinal cord stimulation devices are programmable multichannel systems with electrodes that may be placed percutaneously, these systems do not require laminectomy. These stimulators have been shown to reduce chronic pain (percieved pain levels requiring intensive therapies: discomforting, distressing, horrible, and excruciating) by 50% long term. The global ratings for quality of life in these patients demonstrated similar long term improvements. The exact mechanism of how spinal cord stimulation results in a reduction of pain is unknown, but it is thought to occur through an antisympathetic effect. Further, it seems to be effective in cases in which the patient has neuropathic or an ischemic component to the pain. In patients with peripheral neuropathies (postheφetic neuralgia, intercostal neuralgia, causalgic pain, diabetic neuropathy, idiophathic neuropathy) spinal cord stimulation is able to reduce chronic pain in approximately 50% of the patients. Surgical treatment: If conservative pharmacologic approaches have failed to relieve pain, neurosurgery can be considered. Neurosurgical treatments consist of nerve blocks, neuroablative and neuroaugmentative procedures. Nerve blocks: Peripheral, epidural, and sympathetic nerve blocks have been attempted. However, the analgesic effect is usually short-lived and ineffective against central mechanisms of pain. Neuroablative procedures. There are surgical procedures that are rarely performed because they have been shown to be ineffective, 1 e sympathectomies. neurolyses, dorsal rhizotomies, cordectomies, anterolateral cordectomies, mesencephalotomies, and cingulotomies These procedures have been superseded by dorsal root entry zone (DREZ) surgery The surgical procedure involves a laminectomy of the appropnate vertebrae, examination of the DREZ and radiofrequency lesions of the DREZ The mechanism of this ablative surgery is thought to be due to the destruction of the secondary pam sensory neurons m the substantia gelatinosa in the dorsal horn Success of this procedure on the reduction of pam has been reported at 60-90% Neuroaugmentative procedures- deep brain stimulation. Electrodes are implanted in the penventncular gray matter, specific sensory thalamic nuclei, or the internal capsule Limitations of Cunent Therapies of Pain Due to Low Efficacy The seventy of pam can be debilitating and significantly interfere with the productivity and quality of life Existing therapies for chronic pam are often inadequate and charactenzed by the tendency to become ineffective with time Potent opiates are part of an analgesic regimen, however, dose-hmitmg side effects and antinociceptive capacity, tolerance and potential for dependence limit their widespread use Surgical intervention is sometimes attempted, but often such procedures are ineffective and at best provide only temporary relief There are many syndromes by which the above combination d g therapy is insufficient to relief symptoms of chronic pain There are common reasons for unrelieved pam associated with the patient or family, i.e. belief that pam in cancer is inevitable and untreatable, failure to contact a physician, patient denial, failure to take medications, noncomphance due to fear of addiction, noncomphance due to a belief that tolerance will rapidly develop and adequate pam relief then will not be available in the advanced stages, and lastly noncomphance due to the adverse side effects Common reasons for unrelieved pain associated with the physician or nurse are. denial of the patient's pam, unawareness of pain intensity, failure to perceive patient denial, failure to treat pam aggressively, fear of patient addiction, failure to prescπbe appropnate doses for analgesia, failure to monitor the patient's progress, failure to understand alternative drug combinations, and finally failure to give psychological support to the patient and family Despite these common reasons for unrelieved chronic pain, even under positive conditions chronic pain can be intractable m a vaπety of diseases. The coexistence of pain and depression in these patients is a dependent relationship, i.e. when the pain is unmanaged the depression becomes more severe, the reverse (increased depression leads to increased pain) relationship is less likely to occur. The characteristic intensity of the pain and psychological impact prompts extreme potential solutions. Some of these pain syndromes are more resistant to analgesic therapy, for example approximately half of the individuals with spinal cord injuries endure chronic pain and 30% experience severe, debilitating chronic pain. Approximately 75%> of advanced stage cancer patients experience moderate to severe pain and approximately half of these individuals are refractory to standard therapy for management of pain. Other efficacy limitations include: slow onset of symptoms (2-3 weeks) before efficacy detection for tricyclic antidepressants. Limitiations of Cunent Therapies of Pain Due to Toxicity or Undesired side effects In the stepwise approach to therapy, physicians are able to monitor and adjust the doses to limit undesired side effects of opioids: sedation, cognitive impairment, myoclonus, addiction, and respiratory depression. Further, opiate tolerance is a well documented effect seen in routine narcotic users and abusers. These side effects may provoke a use of opioid rotation in a pain management schedule. Although the use of opioids in acute and chronic cancer associated pain is well accepted, their use in chronic noncancer pain has been widely considered to be inappropriate due to concerns over efficacy, toxicity and addiction. Other unwanted or undesirable side effects include tardive dyskinesias limit the use of neuroleptics in the management of chronic pain; oral baclofen is associated with drowsiness and confusion. Further, baclofen may cause hepatotoxicity. Complications of radiofrequency lesions of DREZ procedure includes cerebrospinal fluid leaking, loss of sensory/motor functions, exacerbation of bowel, bladder, or sexual dysfunction, and epidural/subcutaneous hematomas. Patients must consider the risks of this procedure, particularly the potential loss of two levels of sensation. Associated with deep brain stimulation are complications due to the release of large amounts of natural opioids leading to deafferenation and nociceptive pain. Impact of Genotyping on Drug Development for Pain As described above, there is evidence to suggest that there are efficacy and safety differences to drug therapy in the pain patient population. Although not all of these responses may be attributable to genotypic differences, it is expected that if stratification based upon genotype were performed, a reasonable conelation between drug response and genotype may become obvious. As described below, there are gene pathways that are involved with cunent drug therapy and those that may be potentially involved in the future. As described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for pain syndromes. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and CNS matrix table 7. For example, optimization of GABAergic, opiate, or ion channel modulation mediated therapy of pain further demonstrates the utility of selection of a potential epilepsy patient that has a predisposing genotype in which selective analgesics or agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine variance or variances within the GABAergic receptor, ion channel or ion channel mediated mechanisms of neurotransmission, or GABAergic receptor mediated intracellular mechanism of action that is preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drug development program for pain. A sample of therapies approved or in development for preventing or treating the progression of symptoms of pain cunently known in the art is shown in Table 33. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Description of Mechanism of Action Hypotheses for Future Drug Development for Pain The persistence of pain most likely involves a cascade of pathological neurochemical events that lead to abnormal sensory hyperexcitability and excitotoxicity. The persistence of hyperexcitability involves a sequence of neuroplastic events in the spinal cord. In particular, the hyperexcitability cascade involves NMDA receptor mediated intracellular calcium-dependent increase of nitric oxide (NO) and cGMP production. These signals facilitate long-term alterations in neuronal excitability and central sensitization. The altered spinal neurochemical environment results in an impairment of neural inhibitory function. In particular, inhibitory gamma-aminobutryic acid (GABA)-ergic intemeurons are suseptible to excessive excitatory amino acid release. Recent studies suggest that abnormal pain sensations may be alleviated by application of GAB A receptor agonists. The analgesic capacity of GABA receptor agonists has been demonstrated in numerous animal models of acute and chronic pain. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of various drugs or compounds. In Tables 2, 13, and 19, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with pain based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of epilepsy include glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, histaminergic, purinergic, GABAergic, glycinergic, melatonin, nitric oxide, peptide protein hormone processing, opiates, cholecystoki in, tachykinin, bradykinin, corticotropin releasing hormone, somatostatin, galanin, calcium or sodium channels, prostaglandin, cytokines, growth, differentiation, apoptosis, lipid transport/metabolism pathways that are listed in Tables 2, 7, 13, and 19. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of pain, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for pain. E. Parkinson's Disease Description of Parkinson's Disease Parkinson's disease (PD) is one of the major neurodegenerative disorders of middle and old age. PD is a clinical syndrome that is dominated by four clinical symptoms: tremor at rest, bradykinesia, rigidity, and postural instability. There are secondary clinical signs and symptoms also associated with PD and are a result of the following manifestations: mood and intellectual disorder, oculomotor control, and autonomic and sensory dysfunction. PD can be generally categorized by the clinically predominant parkinsonian feature: 1) those patients having tremor, or 2) those patients having postural instability and or gait difficulty as the predominant clinical parkinsonian manifestation. In those patients with tremor predominant disease, the onset is earlier in life and exhibits a slower progression that those patients with gait difficulties or postural instability. In the latter case, the age of onset is later in life and is more frequently associated with bradykinesias, dementia, and the movement disorder progresses more rapidly. The stages of PD have been described and are refened to as Hoehn and Ya-hr stages I through V; stage I- signs and symptoms are unilateral, stage II- signs and symptoms are bilateral, stage Ill- signs and symptoms are bilateral and balance is impaired, stage IV- functionally disabled, and stage V- patient is confined to wheelchair or bed. Resting tremor and bradykinesias are the hallmarks of PD. Bradykinesias are primarily responsible for the altered clinical presentation for most PD patients: retardation of activities of daily living and generalized slowing down of movements, lack of facial expression (hypomimia or masked facies), staring expression due to limited ability to blink, impaired swallowing which causes drooling, hypokinetic and hypophonic dysarthria, monotonous speech, micrographia, impaired simultaneous and repetitive movements, difficulty in standing from a chair and turning in bed, shuffling gait with short steps, decreased arm swing and other autonomic movements, start hesitation and sudden freezing of motion. Freezing of motion manifests as a sudden and often unpredictable inability to move and represents the single most disabling parkinsonian symptoms. There are several disorders other than PD that manifests with parkinsonian symptoms. For example, acquired or symptomatic parkinsonism is the result of infectious (postencephalitic and slow virus) disease, side effects from drugs (neuroleptics (antipsychotic and antiemetic drugs), reseφine, tertabenazine, a- methyl dopa, lithium, flunarizine, cinnarizine), toxins (MPTP, carbon dioxide, manganese, mercury, cesium, methanol and ethanol), cerebrovascular insult (multi- infarct, hypotensive shock), trauma (pugilistic encephalopathy), and others (parathyroid abnormalities, hypothyroidism, hepatocerebral degeneration, cerebral tumors, normal pressure hydrocephalus, syringomesencephalia). Parkinsonism can also be the result of heredodegenerative disease, for example autosomal Lewy body disease, Huntington's disease, Wilson's disease, Hallervorden-Spatz disease, olivopontocerebellar and spinocerebellar degenerations, familial basal ganglia calcification, familial parkinsonism with peripheral neuropathy, and neuroacanthocytosis. Lastly, parkinsonism can be the result of multiple-system degenerations and include for example progressive supranuclear palsy, Shy-Drager syndrome, striatonigral degeneration, Parkinsonism-dementia-amyotrophic lateral sclerosis complex, corticobasal ganglionic degeneration, Alzheimer's disease, and hemiatrophy-parkinsonism. These non-PD parkinsonism symptoms can be clinically identified as distinct from PD due to the presence of atypical signs or symptoms of the particular dysfunction or syndrome, absence or paucity of tremor, and poor response to levodopa. Cunent Therapies for PD Pathophysiologically, idiopathic PD cases are almost uniformly identified by the absence of dopaminergic terminals and depigmentation within the substantia nigra and the presence of Lewy bodies (eosinophilic cytoplasmic inclusions in neurons consisting of aggregates of normal filaments). These abnormalities are predominantly found in the ventrolateral region of the substantia nigra which is the region that projects to the putamen. It has been estimated that at least 80% > of dopaminergic neuronal loss within the substantia nigra and an equal degree of dopamine depletion within the striatum is required before signs and symptoms of PD is clinically observed. There are cunently four categories of drug therapies for the treatment of PD: dopaminergic replacement drugs, dopaminergic agonists, anticholinergic drugs, and monoamine oxidase inhibitors. Other therapies include surgical treatment and implantable devices for control of debilitating essential tremor. Dopaminergic Replacement Drugs- therapy of PD is aimed at replacing the lost dopamine that has resulted in the loss of dopaminergic neurons in the substantia nigra and other brain regions. L-dopa is a prodrug that can be converted to dopamine within the exisiting neurons. Generally, L-dopa is beneficial in early PD, because it is effectively metabolized in presynaptic terminals and secreted in an active form. Due to the rapid decarboxylation of L-dopa in the periphery, administration of large doses is required to achieve therapeutic benefit. However, L- dopa is usually administered with carbidopa, an inhibitor of peripheral decarboxylation and thus greater concentrations of L-dopa enters the CNS. The combination of L-dopa and carbidopa reduces by 75% the amount of L-dopa required. Dopaminergic Agonists- dopaminergic agonists can be administered in the early stages of the disease, examples include parlodel and permax. Anticholinergic Drugs- anticholinergic agents are prescribed for the management of tremor or inordinate movements associated with PD, examples include artane, and cogentin. The majority of the anticholinergic therapies for the adjunct treatment of PD are long-acting medications thus relief of symptoms may continue through the night when patients have difficulty turning in their bed, and to rise in the morning. Monoamine Oxidase Inhibitors- inhibition of the metabolism of dopamine by monoamine oxidase can be achieved to increase the synaptic levels of dopamine. An example is selegiline. Others- catechol-o-methyl transferase inhibitors may be prescribed for the adjunctive treatment of PD. example is Tasmar. An antiviral, symmetrel, has been used for the relief of tremors, rigidity, and bradykinesia. Some β-adrenergic antagonists have been shown to reduce tremors, example is inderal. Prior to the advent of levodopa therapy, the most effective means of treating disabling tremors associated with PD were thalamotomy and pallidotomy. These ablative surgical procedures are associated with improved tremor and in certain cases, bradykinesias. Recent advances in neurosurgery, e.g. devices to specifically record from the globus pallidus for enhanced localization, have been employed and there is renewed clinical interest in considering these therapies for the treatment of PD. This therapy has the advantage of single procedure therapeutic intervention of disabling tremors. Another therapeutic alternative for the treatment of essential tremor, a device for deep brain stimulation, is approved for unilateral implantation in the ventral intermediate nucleus of the thalamus. A programmable, implantable pulse generator is implanted just below the clavicle. The implanted device has been shown to be effective in 20%> of the patients, bilateral implantation and stimulation is under investigation. Limitations of Cunent Therapies for PD Although there are therapeutic alternatives for the early intervention of PD, there are few alternatives for the later stages and for the side effects that develop after long term therapy. These limitations are discussed below. Limitations of Cunent Therapies due to Low Efficacy All anti-Parkinson drugs have two qualities that limit the efficiency of treatment regimens. First, the drugs are relatively short acting. A single administration does not relieve symptoms for the duration of waking hours, and multiple administrations are required. The second is that these drugs are all centrally acting drugs and starting dosage is low and slowly increased. Abrupt withdrawal or reductions of any of these medications can lead to deleterious side effects. L-dopa therapy of PD has therapeutic benefit in the early stages of the disease. However, as the movement disorder progresses, the dopaminergic terminals are lost and the prodrug is no longer converted to the active form. The therapeutic benefit is then limited to the level and extent of the intact postsynaptic neurons. Long-term therapy with levodopa is associated with dose dependent side effects including inefficacy, "on-off ' phenomena, and dyskinesias. Response fluctuations occur in approximately 80%> of the patients. These fluctuations consist of wearing-off phenomena, a gradual loss of effectiveness of levodopa related to the timing of administration of the drug, and the on-off phenomena, which is an abrupt loss of the effectiveness of levodopa that is not related to the timing of administration. Dyskinesias, consisting of chorea and dystonia, occur in approximately 40% of patients treated with levodopa. These dyskinesias are most frequently observed when plasma levels of L-dopa are high. For patients with preexisting history of psychiatric illness, anticholinergic therapies are less likely to be administered and further if prescribed are less likely to be effective. Thalamotomy and pallidotomy are two surgical procedures that can only be performed once per side. Thus, refractory cases or cases whereby surgery was not sufficient to alter the essential tremor, additional surgery is unavailable. Deep brain stimulation is only 20% effective, requires extensive follow-up, and is associated with a surgical morbidity of 5%. Animal model studies of growth factors, GDNF, affected sprouting of peripheral neurons and those in the spinal cord. Unregulated neural sprouting can be deleterious to neurological function. Limitation of Cunent Therapies due to Toxicity or Undesired Side Effects Limitations due to toxicity or undesired side effects for the above discussed treatments of PD are as described below for each of the treatment strategies. Dopaminergic replacement drugs- as described above, L-dopa is a prodrug that can be of therapeutic benefit to patients with PD. However there are side effects and toxicities associated with L-dopa therapy, they are choreiform and dystonic dyskinesias and other involuntary movements, adverse mental changes such as paranoid ideation, psychotic episodes, depression, and cognitive impairments (dementia). Dyskinesias associated with levodopa, can be debilitating and as uncomfortable as the rigidity and akinesia of PD. Reductions or withdrawals of L-dopa therapy have been associated with neuroleptic malignant syndrome (NMS). NMS is an uncommon but life-threatening syndrome characterized by fever or hyperthermia, muscle rigidity, involuntary movements, altered consciousness, autonomic dysfunction, tachycardia, tachyapnea, sweating, and hyper- or hypotension. Dopaminergic agonists- as described above, dopaminergic agonists are useful for the activation of post synaptic dopaminergic receptors. The side effects and toxicities associated with dopaminergic agonists are: abnormal involuntary movements, hallucinations, "on-off phenomena, dizziness, fainting, visual disturbances, ataxia, insomnia, depression, hypotension, constipation, vertigo, and shortness of breath. It has been observed clinical laboratory transient elevations of blood sera urea and nitrogen, SGOT, SGPT, GGPT, CPK, alkaline phosphatase, and uric acid. Anticholinergic drugs- the predominant affect afforded by the anticholinergic drugs is to treat the extrapyramidal effects that develop with long-term dopaminergic therapies. This therapy is thus via the anticholinergic and antihistaminergic effects. However, there are adverse reactions that are associated with anticholinergic therapies, they are tachycardia, paralytic ileus, constipation, dry mouth, toxic psychosis (confusion, disorientation, memory impairment, visual hallucinations, possible exacerbation of preexisiting psychiatric symptoms or syndromes, bluned vision, dysuria, and urinary retention. Monoamine oxidase inhibitors- selective inhibition of monoamine oxidase type B (MAO-B) enzyme activity is a useful adjunctive therapy to increase concentrations of dopamine in regions of the brain. Since MAO-B is predominantly found in the brain, fewer systemic side effects occur. Despite this selectivity, there are side effects that are undesirable, they are exacerbation of L-dopa or other dopamine agonist mediated side effects. For example, dyskinesias are enhanced as well as the others listed above. MAO-B inhibition can be deleterious if administered with a tricyclic antidepressant. Further, a combination of MAO-B inhibitor and meφeridine (an opioid narcotic) has lead to stupor, muscle rigidity, severe agitation, and hyperthermia. Thus, concomitant administration of these two types of drugs is avoided. Others- inhibition of COMT as described above is a useful therapeutic alternative to many PD patients. However , there are associated side effects and toxicities associated with this drug family. In some patients there is a clinical liver enzyme elevation that requires monthly monitoring and liver function tests are routinely administered every 6 weeks for the first three months of therapy. Liver impairment can result in the reduction of drug detoxification mechanisms, and clinically as jaundice. Because COMT and monoamine oxidase are the two predominant metabolizing enzymes for catecholamines, concunent therapy of a COMT and a non-selective monoamine oxidase inhibitor may result in abenant neuroexcitoxicity. However, selective monoamine oxidase inhibitors of MAO-B may be administered together. Other side effects include dykinesias, nausea, sleep disorders, dystonia, excessive dreaming, anorexia, muscle cramps, and orthostatic hypotension. Surgical treatment and implantable devices- both pallidotomy and thalamotomy are routinely considered for the treatment of refractory essential tremor. The extent and level of surgical success is dependent on accurate localization of the globus pallidus or the thalamus. Surgery that includes either of these two methods is a one attempt procedure, too much sunounding brain tissue may be lost in subsequent procedures. A side effect may be loss of cerebral function in sunounding areas that may or not result in clinical relevant or observable disease. Impact of Genotyping on Drug Development for PD For Parkinson's disease, there is evidence to suggest that there are efficacy and safety differences to drug therapy in the PD patient population. Although not all of these responses may be attributable to genotypic differences, it is expected that if stratification based upon genotype were performed, a reasonable conelation between drug response and genotype may become obvious. As described below, there are gene pathways that are involved with cunent drug therapy and those that may be potentially involved in the future. As described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for PD. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway table 2 and the matrix table 7. Description of Mechanism of Action Hypotheses for Future Drug Development Motor symptoms of PD result primarily from the degeneration of dopaminergic innervation within the putamen and the caudate nucleus. Further dopaminergic degeneration within the mesocortical and mesolimbic systems may be responsible for the cognitive deficits and neurobehavioral symptoms. Autonomic dysfunction often observed in PD patients may be the result of loss of dopaminergic function in the hypopthalamus. Although dopaminergic pathways have been studied extensively in post mortem PD patients loss of neurotransmitter pathways that may be responsible for additional clinical symptomology. For example, loss of noradrenergic innervation in the locus ceruleus may contribute to the sudden and unpredictable freezing of motion and degeneration of cholinergic neurons in cortical areas may lead to observed dementia in PD patients. There have been recent proposals for the mechanism of selective neuronal cell death and functional loss. The proposed mechanisms involved in the progressive degeneration of dopaminergic neurons are oxidative stress, mitochondrial dysfunction, excitotoxic damage, cell death. Below each is described, with proposed gene targets. Oxidative stress: In oxidative stress, generation of reactive oxygen species, part of the normal cellular metabolism, is abenant and levels exceed the regulated cellular metabolism or scavenging mechanisms. The free radicals are generated by the conversion of superoxide ions to hydrogen peroxide via the enzyme superoxide dismutase and the reaction of hydrogen peroxide with reduced glutathione to produce water under the control of glutathione peroxidase. Since it has been documented a 60%> reduction in the available reduced glutathione as well as a increased generation of iron associated with neuromelanin, there is a potential shift in the balance of the capacity to scavenge hydrogen peroxide radicals. Oxidative stress may also be part of circuitous pathway leading to cell death that is as follows: generated free radicals lead to mitochondrial damage, which leads to neuron excitotoxicity, which leads to increased concentrations of intracellular calcium which increases the generation of free radicals. All four pathways (free radicals, mitochondrial damage, neural excitotoxicity, and increased intracellular calcium) can independently lead to neuron cell death. Neuroprotective agents, antioxidative agents, and those agents having effects of halting, retarding, or preventing progression of neurodegeneration may affect one or more of these pathways leading to therapeutically relevant agents. Mitochondrial damage: In mitochondrial damage, the evidence is born out of the experiments of the specific neurotoxin, MPTP. MPTP is a protoxin, its active form MPP+ has been shown to result form its inhibition of mitochondrial respiration at the level of complex I, the complex that controls the transfer of one electron from NADH to co-enzyme Q and the transfer of two protons to the mitochondrial inner space, both are then used to synthesize ATP from ADP. In addition, MPP+ is thought to increase leakage of electrons at complex I, thereby increasing the generation of superoxide. Since the association of MPTP and the evolution of PD in intravenous drug users, it has been shown that there is a decrease in complex I activity in the substantia nigra in PD patients and is relatively unique to PD than other neurodegenerative disorders. Excitotoxic damage: In excitotoxic damage, the theory posits there is an excess glutaminergic signal from the neocortex and the subthalamic nucleus to the substantia nigra. The excess signal, by acting at NMD A receptors, changes the permeability of the neural cells to calcium which leads to abenant post synaptic membrane potentials, enhanced propensity for depolarization and latent repolarization, and activation of nitric oxide synthase (NOS). Activation of NOS leads to the generation of free oxygen radicals through the peroxynitrite reaction. Since the discovery that output neurons of the subthalamic nucleus provide a glutaminergic excitatory input to the substantia nigra, increased calcium influx into the cells and increased formation of nitric oxide via the acitvation of NOS, may be particularly harmful in PD due to the defect in mitochondiral complex I (see above). Excitotoxic damage to the substantia nigra, thus potentially stems from the integrity of the substantia nigra and or overactivity of the subthalamic nucleus. Thus, strategies aimed at dual actions of enhancing dopaminergic status (dopamine agonism) in the substantia nigra and reducing subthalamic overactivity (glutaminergic antagonism). Cell Death: In neural cell death, neurons in the substantia nigra undergo death signals via necrosis and apoptosis. In studies involving double labeling with the TUNEL assay (apoptosis) to determine DNA fragmentation and cyanine dye labeling to determine cell structural detail, it was shown that DNA fragmentation and chromatin condensation occurs in the same nuclei of neurons in substantia nigra in patients with PD. Therefore, it appears that the number of apoptotic nuclei in the substantia nigra in PD is greater than that seen in normal aging, consistent with the 10-fold higher rate of cell loss observed in patients with PD. Thus, antiapoptotic agents or therapies may halt, retard, or prevent the progression of neurodegeneration. Neuroprotection afforded by growth factors in general or specific to neurons have been considered. Growth factors including but not limited to BDNF, GDNF, bFGF have been studied in preclinical animal models of PD. Furthermore, GDNF has been tested in clinical trials. Alternative neurotrophic agents are a group of ligand called the immunophilins. These ligands have been shown to have neurite growth promoting and neuroprotective effects. Although these effects were first described from results of experiments of the immunosuppressive agents, cyclosporine and FK-506, nonimmunosuppressive analogues have been generated to have neuroprotective capacity while having none of the immunosuppresive qualities. These low molecular weight ligands may hold promise for the medical management of PD. Based upon these varying hypotheses as stated above, there are many products in devleopment for PD. Table 34 below lists cunent therapies that are in development for PD. F. Spasticity Description of Spasticity Spasticity is a complication that occurs in patients with diagnosed neurodegenerative diseases or cerebral insults such as multiple sclerosis, cerebral palsy, tetanus, traumatic brain injury, post traumatic spinal cord injury, amyotrophic lateral sclerosis, dystonic syndromes (axial dystonia), and stroke. Together there are approximately 1.8 million individuals with spasticity in the U.S. Spasticity is a term that generally refers to one of a variety of forms of muscle hypertonicity, hyperactive muscle stretch reflexes, exaggerated tendon reflexes, and clonus and flexor spasms. Spasticity is commonly described as an isokinetic movement disorder distinguished by velocity-dependent increase in muscle tone characterized by hyperactive stretch reflexes. Patients with spasticity have impaired voluntary control of skeletal muscles, difficulty relaxing muscles once movement has stopped, difficulty initiating rapid movements, and an inability to regulate controlled movement. Clinically, there are three types of spasticity 1) mild, characterized by hyperactive reflexes and unsustained myoclonus; 2) moderate, characterized by involuntary, uncontrolled contractions, sustained myoclonus neither of which affects activities of daily living; and 3) marked or severe, characterized by unpredictable, uncontrolled paroxysms of spasm and involuntary clonus; these can throw the patient from a wheelchair and often the patient cannot lie in bed quietly; these patients have difficulties using a wheelchair, and transfers (for example: from bed to chair) are problematic. Broadly speaking there are two groups of spasticity patients: cerebral origin spasticity (etiologies resulting from congenital or acquired injuries such as trauma (traumatic brain injury), anoxia (cerebral palsy), or stroke); spinal origin spasticity (etiologies include spinal cord injury and multiple sclerosis). Uncontrolled spasticity exacerbates physical disabilities, increases the cost of care, and profoundly impacts the quality of life for the patient and family. Cunent Therapies for Spasticity Mild to moderate spasticity is medically managed with the available treatments. Little to no data are available with respect to waning of efficacy or progression of the spasticity to more severe forms. With prolonged marked spasticity, contractures (static muscle shortening due to chronic spasm) may develop so that neither lying nor sitting occurs without undue pressure on bony prominences which lead to chronic pressure sores. As the severity of the spasticity is a continuum, so are the therapies. Spasticity may not require treatment until it becomes painful, bothersome to the patient, or interferes with the activities of daily living. Existing treatments for spasticity may be categorized as systemic or locally acting. Systemic Oral Medications These are dantrolene (interferes with the excitation-contraction coupling mechanism by interfering with Ca^ (dantirum), baclofen (GABA B agonist, lioresal), diazepam (GABA agonist, valium), tizanidine hydrochloride (β 2 -agonist, zanaflex). Back-up medication is the α-agonist, clonidine. Locally Acting Treatments Locally acting treatments include intrathecal baclofen, surgical or chemical rhizotomy, and nerve motor point blocks. Intrathecal baclofen Oral Baclofen is associated with undesirable side effects, however, Baclofen can be delivered to the subarachnoid space attached to a subcutaneous pump. Intrathecal baclofen is a convenient therapy and this form of drug delivery poses fewer central side effects. Further, intrathecal baclofen has shown to reduce spasticity, improve functional capabilities, and increases functional range of passive movement. Surgical intervention This category includes rhizotomy, which has been most successful in the treatment of spasticity in children with cerebral palsy. In elderly patients that may have stroke induced spasticity, rhizotomy is uncommon and virtually not considered. Another surgical procedure, tendon lengthening, can be considered in those patients in which the lower extremities are affected. This procedure can be considered in those stroke patients who have developed spasticity. Chemical Rhizotomy Chemodenervation is performed via injections of phenol (or ethanol) or botulinum toxin. In phenol injections, there is neurolysis of the motor nerve. This nerve block technique is useful for motor neuron associated spasticity, and is generally avoided in cases where sensory and motor neurons are hyperactive. The improvement of spasticity after phenol injections may last for a few weeks to years. Botulinum toxin (BTX) injection into motor neurons has proven useful in the treatment of spasticity. This potent neurotoxin isolated from Clostrium botulinum, acts by binding to receptors at the neuromuscular junctions. The binding to the type A toxin is highly specific. The deactivation of intracellular presynaptic vesicles to release acetylcholine in the synaptic cleft can re-establish normal muscle tone and contractility. Intramuscular delivery of BTX has the advantages of lack of sensory effects, lack of caustic chemicals such as phenol, ability to target specific muscle groups through the use of electromyography, and an ability to weaken muscles in a graded fashion. Limitations of Cunent Therapies for Spasticity: Efficacy and Toxicity Systemic Local Medications With the exception of dantrolene (which acts on directly on muscle), all of the other oral medications act on the central nervous system and there are unwanted effects from the medications, i.e. drowsiness and confusion. Dantrolene and baclofen may cause hepatotoxicity, and dantrolene may cause weakness in other muscle groups. Further, the systemic treatments are highly nonselective. As listed above, there are some indications that these oral medications are less likely reduce the spasticity; outcomes of oral medications in the treatment of cerebral origin spasticity are poor as compared to good outcomes in patients with spinal origin spasticity. Often combination regimens are used to attempt to curb the myoclonus. Locally Acting Treatments Intrathecal Baclofen- The limitations of this method of delivery are numerous: pump failure, infection, catheter migration, and the need to refill the reservoir. The half-life for ITB is 4-5 hours, and the pump must be refilled at least every 90 days. Chemodenervation this technique is dependent on the proficiency of the surgeon and the accuracy of motor stimulation electromyography (EMG). Phenol injection close to a sensory nerve can result in causalgia due to injury of the myelin sheath of the sensory nerve. BTX- There are studies that demonstrate a resistance to the toxin, these studies have shown that an antibody titer to the toxin prevents full potency. Impact of Pharmacogenomics on Drug Development for Spasticity As described above, there is evidence to suggest that there are efficacy and safety differences to drug therapy in the spasticity patient population. Although not all of these responses may be attributable to genotypic differences, it is expected that if stratification based upon genotype were performed, a reasonable conelation between drug response and genotype may become obvious. As described below, there are gene pathways that are involved with cunent drug therapy and those that may be potentially involved in the future. As described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for spasticity. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway table, Table 2, and the gene pathway /indication matrix table, Table 7. Optimization of GABAergic or ion channel modulation mediated therapy of spasticity further demonstrates the utility of selection of a potential spasticity patient that has a predisposing genotype in which selective antispasticity or agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine variance or variances within the GABAergic receptor, ion channel or ion channel mediated mechanisms of neurotransmission, or GABAergic receptor mediated intracellular mechanism of action that is preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drug development program for spasticity. A sample of therapies approved or in development for preventing or treating the progression of symptoms of spasticity cunently known in the art is shown in Table 36. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Description of Mechanism of Action Hypotheses for Future Drug Development for Spasticity Although the exact mechanism of neurodegeneration-induced spasticity is unknown, the pathophysiology centers on the inadequate release of the inhibitory neurotransmitter, GABA within the spinal cord. Cerebral damage or localized damage within the spinal cord can influence the descending neurons that normally release GABA. However, the afferent input to the spinal cord from the muscle spindles is unaffected causing a relative increase of excitatory neurotransmitters, particularly glutamate. The consequence is excessive stimulation of the alpha motor neurons resulting in spasticity. Spasticity arising from cerebral damage may only affect certain modulatory inhibitory signals resulting in a variability of spasticity within each and among patients. Since all muscle groups may not be affected equally, management may be complicated. Spastic paresis or spastic dystonia appear to arise from an imbalance of inhibition and excitation occurring at the level of the motor neuron. The most basic component is the abnormal intraspinal response to sensory input. Since modulation of the local spinal cord activity (peripheral segmental reflex arcs and the anterior horn cells) occurs via the descending pathways, loss of the GABA intemeurons can affect the balance of excitation/inhibition and leads to hyperexcitable cells that result in an increase in activity of by the extrafusal muscle fibers. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of various drugs or compounds. In Tables 2, 13, and 19, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with spasticity based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of epilepsy include glutaminergic, adrenergic, cholinergic, GABAergic, calcium channel, mitochondrial maintenance, adhesion, and myelination gene pathways that are listed in Tables 2, 13, and 19. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of spasticity, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for spasticity. G. Ischemic Cerebrovascular Disease Description of Stroke Ischemic cerebrovascular disease is a result of an imbalance of the oxygen supply and the oxygen demand of brain tissue. Stroke is a series of clinical manifestations of reduction of blood supply to the cerebrovascular bed. The signs and symptoms may be complex and depend on the location and extent of the infarct. Ischemic cerebrovascular disease is divided into thrombotic and hemonhagic stroke. Thrombotic Strokes Strokes are the result of reduced blood flow supplied by one or more or of the major cerebral arteries. Blockage or reduction of blood volume to these main arteries manifests as identifiable neurological symptoms. For example, occlusion of the middle cerebral artery results in contralateral hemiparesis, expressive aphasia, anosognosia and spatial disorientation, contralateral inferior quadrantanopsia, contralateral hemiparesis, sensory loss, contralateral homonymous hemianopsia, or superior quadrantanopsia. Blockage or reduction of the inner carotid artery, anterior cerebral artery, vertebral or basilar arteries, or the posterior artery can result in similarly clinically distinct neurological symptoms. Transient ischemic attacks (TIA) are similar to a thrombotic stroke in that neurological deficit lasts for a brief period and is generally treated with potent platelet aggregation inhibitors. Thrombotic strokes are the result of focal blockage of one or more of the cerebral arteries or branches resulting in neurological signs and symptoms lasting greater than one hour. Artherosclerotic plaques in extracranial or intracranial arteries cause approximately two thirds of thrombotic strokes. Embolization, stenosis, or occlusion of one or more of the cerebral arteries or branches may cause thrombotic strokes. Emboli can be of cardiac origin (e.g. mural thrombi, valvular heart disease, anythmias (atrial fibrillation), cardiac myxoma, and paradoxical emboli (venous origin). Focal ischemia may also be the result of inflammation and necrosis of extracranial or intracranial blood vessels, i.e. vasculitides (e.g. primary cerebral arteritis, giant cell vasculitis, infectious vasculitis) or the result of hematologic abnormalities (hemoglobinopathy, hyperviscosity syndrome, hypercoagulable states, protein C or S deficiency, the presence of antiphospholipid antibodies). Strokes may be drug related, for example illicit drugs (cocaine, "crack", amphetamines, lysergic acid, phencyclidine, methylphenidate, sympathomimetics, heroin, and pentazocine), ethanol, and oral contraceptives. Lastly there are other diseases that may predispose an individual to a stroke, for example fibromuscular dysplasia, arterial dissection, homocystinuria, migraine, subarachnoid hemonhage, vasospasm, emboli of other origin (fat, bone, and air), and moyamoya. Hemonhagic Strokes Approximately 20%> of all strokes are the result of intracranial hemonhage. Approximately half of these cases are into the subarachnoid space and the other half directly in the cerebral tissue. The acute rise in intracerebral pressure generally results in loss of consciousness and many die of cerebral hemiation. Similar to thrombotic strokes, hemonhagic strokes can be considered diffuse or focal, depending on the extent of the vessel disruption. Causes of spontaneous intracranial hemonhage include arterial aneurysms (beny aneurysms, fusiform aneurysm, mycotic aneurysm, and aneurysm with vasculitis), cerebrovascular malformations, hypertensive-artherosclerotic hemonhage, hemonhage into a brain tumor, systemic bleeding diatheses, hemorrhage with vasculopathies, hemmorhage with intracranial venous infarction. Subarachnoid hemonhage is caused by rupture of surface arteries (aneurysms, vascular formations, head trauma) with blood limited to the cerebrospinal fluid space between the pial and the arachnoid membranes. Cunent Therapies for Stroke If a hemonhagic stroke is clear on the CCT, gradual reduction of systemic BP is achieved by standard vascular dilatation medications. Angiography can be useful to identify the source of the hemonhage. Surgical management of the hemonhage may be required. If an ischemic stroke is identified and focal neurological impairments subside over time, a transient ischemic attack (TIA) is suspected. TIA has a high rate of recunent stroke within a short time frame. Platelet aggregation inhibition is standard therapy; aspirin or ticlopidine. Ticlopidine is associated with neutropenia and agranulocytosis which may be life threatening. Because of these severe side effects, Ticlopidine is reserved for patients who are intolerant to aspirin therapy. If angiographic review a clearly defined clot is detected, TIA may be surgically treated with endarterectomy. For the treatment of thrombotic or embolic strokes, each case is independently assessed for surgical management or anticoagulant therapy. The success of thrombotic therapy, e.g. tissue plasminogen activator (tPA), streptokinase, urokinase, relies on timely reperfusion. The therapeutic window for tPA has been shown to be within three hours of onset of symptoms. Hypothermia has been shown to decrease mortality and improve outcomes. Hyperthermia has been shown to worsen both mortality rates and outcomes. Significant neurologic improvement has been shown to occur within the first three months after stroke symptoms. A clear focus on intensive rehabilitation during this critical time frame has been shown to enhance the eventual outcome for survivors of stroke. Limitations of Cunent Therapies for Stroke The single most limiting factor of stroke therapy is the rapid identification of stroke symptoms and urgency of intervention within a short time. Limitations of Stroke Therapy Due to Low Efficacy and Deleterious Side Effects Guidelines for the use of tPA in acute ischemic stroke call for the administration of the thrombolytic agents within the first three hours from the onset of symptoms. After three hours four probable deleterious effects have been proven in animal studies and are as follows: 1) cerebral and extracerebral hemonhage, 2) reperfusion injury, 3) fragmentation of clots, and 4) reocclusion of reperfused vessels. In both animal models and in humans, reperfusion therapy must be administered within three hours of symptom onset. After three hours deleterious reperfusion injury may occur. Mortality at three months was 17% in the tPA group and 21 % in the placebo group (p=0.30). Tissue plasminogen activator (tPA), streptokinase, heparin, and urokinase have specific restrictions: tPA has a 6% > rate of cerebral hemonhage; streptokinase is generally not used for thrombotic strokes because of serious side effects and limited quantifiable efficacy, urokinase is generally delivered near the site of the clot or obstruction. Factors influencing the best medical treatment of ischemic stroke must weigh the benefits and limitations of each o f these therapies . Impact of Genotyping on Drug Development for Stroke As described above, there is evidence to suggest that there are efficacy and safety differences to drug therapy in the stroke patient population. Although not all of these responses may be attributable to genotypic differences, it is expected that if stratification based upon genotype were performed, a reasonable conelation between drug response and genotype may become obvious. As described below, there are gene pathways that are involved with cunent drug therapy and those that may be potentially involved in the future. As described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for stroke patients. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and matrix Table 7. A sample of therapies approved or in development for preventing or treating the progression of symptoms of stroke cunently known in the art is shown in Table 37. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Mechanism of Action Hypotheses for Novel Therapies for Stroke: Utility of Genotyping There are two categories of genotyping that provided insight on the selection of candidate genes for polymoφhic genotypic studies of drug response. One set of likely candidates come from disease etiology or linkage studies. These data may provide input on the genetic etiology or abenant mechanisms of strokes. Another set are those genes involved in the biochemical or molecular mechanisms of drugs, agents, or candidate therapeutic interventions. Genes Involved in the Etiology of Stroke Studies have demonstrated that there is a genetic component to thrombotic stroke. These genetic factors may predispose by an individual to thrombotic stroke by inheriting one or more of the following 1) low threshold for abenant formation of artherosclerotic plaques in intracranial blood vessels; 2) traits that underlie certain specific etiology of stroke; and 3) a disease, disorder, or pathophysiologic process of the CNS in which there are associated molecular or structural disturbances that predispose individuals to strokes. These genetic influences mediating stroke may be candidates for genotyping assays and directly linked to pharmacogenomic programs. Genes Involved in the Mechanism of Drug Action There are also the biochemical, or molecular mechanisms of drug or candidate therapeutic action that may affect drug action. As described above there is an urgent need for the discovery and development of therapeutic alternatives for the medical management of strokes in which therapy commences beyond the therapeutic windows of thrombolytics. Recent research and development programs have included the following pathways: 1) glutamate neurotransmitter pathway has been implicated in abenant excitatory neurotransmission; 2) inflammation is a mechanism that may lead to profound neural cell loss, 3) carnosine pathway, 4) cell adhesion pathways, 5) oxidative stress pathways, 6) growth factor mediated differentiation and rescue of ischemic tissue, and protein maturation and degradation. Ischemic Penumbra, Site of Infarct-Tissue at Risk Ischemic penumbra is the tissue immediately adjacent to the infarct zone that is viable and moφhologically intact but functionally impaired due to the restricted blood flow. Once the blood flow decreases to a certain threshold, this penumbra tissue can be classified as "misery-perfused" because oxygen consumption is preserved and increased oxygen extraction occurs. Ischemic penumbra is, thus, a dynamic process of impaired perfusion and unstable energy metabolism. Since necrosis naturally follows the continued oxygen deprivation, it has been reported that final cerebral infarct size is infarct zone plus the unrecoverable penumbra. Functional imaging of the cerebral infarct can detect the penumbra tissue, and in some reports the penumbra tissue can be identified up to 48 hours. There is controversy whether the penumbra tissue can be rescued and what is the appropriate time from symptom onset to rescue by reperfusion. Rescue and time to rescue by reperfusion is dependent on the extent of occlusion and severity of metabolic disturbances. Based upon the hypothesis that early, immediate reperfusion can restore blood flow, the therapeutic window for successful intervention to restore the metabolic alterations has been postulated and proven to be within the first three hours from symptom onset. Other therapies include restoration of the cytokine, neurotransmitter, and Ca "*"" concentrations within the infarct zone (see therapy for stroke below). Since the therapeutic window for victims of stroke is nanow and the debilitating effects of an ischemic stroke can be both costly and severely impact health-related quality of life, there is demand for candidate therapeutic interventions that can halt, retard, prevent neural destruction. Furthermore, there is a demand to develop further candidate therapeutic interventions that can assist in the rehabilitation and ultimately improve the health-related quality of life indices. Inflammation and Immune Disease. Disorders, or Dysfunctions Exemplary diseases characterized by abnormal inflammatory or immunologic responses (also refened to herein as inflammatory or immune diseases or disorders) are described below. These diseases are suitable for application of the methods described in this invention for identification of variances in a gene or genes involved in therapeutic response, e.g. efficacy, tolerability or toxicity. A. Arthritis Description of Arthritis Arthritis comprises a variety of diseases characterized by pain, swelling, and limited movement in joints and connective tissues. Arthritis is usually chronic and there are three prevalent forms of the disease: rheumatoid arthritis (RA), osteoarthritis (OA), and fibromyalgia. In RA, the synovial joint lining becomes inflamed as a result of hyperactive immune response. There are an estimated 2.1 million Americans with RA; two thirds are women. In OA, the cartilage that covers the ends of the bones within joints deteriorates, causing pain and loss of movement as bone begins to rub against bone. There are an estimated 20.7 million Americans with OA, the majority being over the age of 45. In fibromyalgia, widespread pain affects muscles, attachments of muscles to bone, and the connective tissues, i.e., the ligaments and tendons. There are an estimated 3.7 million individuals diagnosed with fibromyalgia syndrome. Other serious and common forms of arthritis or related disorders include the following: gout, systemic lupus erythmatosus, scleroderma, ankylosing spondylitis, and juvenile arthritis. Rheumatoid arthritis involves the disarthroidal joints and can affect a variety of other organs. The clinical hallmarks of RA include: morning stiffness; swelling of three or more joints; swelling of hand joints (proximal inteφhalangeal, metacaφophalangeal, or wrist); symmetric swelling; subcutaneous nodules; serum rheumatoid factor; and erosions and or penarticular osteopema, in hand or wπst joints, often observed on radiograph Osteoarthritis is a degenerative process in joint tissues that may occur in response to aging, genetic, and environmental factors. It is charactenzed by progressive degeneration of cartilage, bone remodeling, and overgrowth of bone. The clinical hallmarks of OA include: deep aching pain in the afflicted joints (hands, knees spine, and hips), morning stiffness of short duration, vanable joint thickening and effusion. Pathologically OA is charactenzed by breakdown of cartilage. Destruction of joint cartilage involves direct physical injury, enzymatic degradation as a result of the injury to chondrocytes, and subchondral bone stiffening as a result of the bone remodeling. Current Therapies for Arthritis Agents used to treat RA fall into one of the following four categones: analgesics (NSAIDs, salicylates), disease modifying antirheumatic agents (gold compounds, cytotoxic), hormones (glucocorticoids), and skin and mucosal membrane preparations. Therapies for the treatment of OA focus on decreasing pain (analgesics) and physical therapies ro increase joint mobility. Analgesics: Typically, pam associated with arthritis can be controlled with NSAIDs including but not excluded to, salicylates, para-aminophenol denvatives, mdole and indene denvatives, heteroaryl acetic acids, arylpropnomc acids, anthranihc acids, enohc acids, or alkanones. Antiinflammatory agents such as cyclooxygenase inhibitors, hpoxygenase inhibitors, and others can be used to block the inflammation physiological pathway which mediate pain and the progression of the disease. However, because these drugs are limited in their efficacy in advanced or more severe stages of arthritis, these agents are add-on therapies. NSAIDs deπve their pnnciple mechanism of action by the inhibition of prostaglandin and leukotπene synthesis. These compounds inhibit key enzymes in the biosynthetic pathway, i.e. cyclooxygenase. There are d gs that selectively inhibit isoforms of cyclooxygenase 1 and 2 (COX-1, COX-2) which enhances patient tolerance due to the prevalence of COX-2 induction occurs in inflammation mediated by cytokines and others. Further, pynmidine synthesis inhibitors can be used as an antiinflammatory agent m arthritis, e.g. leflunomide. Disease-Modifying Antirheumatic Dmgs or agents Agents involved in the modification of clinical disease manifestation, reduction in inflammation, or slow the progression of the disease are refened to as disease-modifying antirheumatic dmgs (DMARDs) and include gold salts (aurothioglucose, aurothiomalate, auranofin), hypotensives (angiotension converting enzyme inhibitors), anaprox, immunosuppressives (azathioprine, cyclosporine), agents to treat metallic poison (penicillamine), depen, naprosen, immuran, antimalarials (chloroquine, hydroxychloroquine), alkylating agents (cyclophosphamide), absorbable sulfonamides (sulfasalazine), irritants and counter-irritants (capsaicin), antimicrobial agents (tetracyclines), and antimetabolites (methotrexate). Hormones and Growth Factors: Agents acting at hormone receptors or growth factor receptors include steroids (glucocorticoids), adrenocorticotrophic hormone (corticotropin), and tumor necrosis factor inhibitors (soluble TNF receptors (enbrel) and TNF monoclonal antibody (remicade). Since the autoimmunity component of the disease is driven primarily by activated T-cells, which give rise to cytokines IL-1 and TNF at the rheumatoid synovium. These agents are known to interfere with the actions of these cytokines. Corticosteroids affect the inflammation within the joints by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. Skin and mucosal membrane preparations: irritants and counter-irritants can be used to treat arthritic joints and include, but not limited to, Capaicin Chlorambucil, cyclosporine, cyclophosphamide are agents that are available for use in the treatment of refractory RA or with severe extraarticular complications such as vasiculitits, comeal perforation or other severe systemic maladies associated with RA. Low Efficacy Limitations of Therapies for Arthritis The therapies discussed above are limited to the slowing or retarding the progression of arthritis. As degeneration of the joints progresses, and ineversible damage occurs, the options become limited. Thus, therapies for arthritis are aimed at reduction of manifestation of symptoms by controlling the clinical manifestations of inflammation. The reduction of clinical symptoms of arthritis following DMARDs therapy is only evident after several weeks to months after therapy. The slow clinical relevance of these therapies limits the clinician to determine optimal therapy for individuals with arthritis, and provides a risk for selection of optimal therapy for any given stage of the disease. Toxicity or Undesired Side Effects as Therapeutic Limitations of Arthntis There are toxicities and undesired side effects associated with the above cunent therapies for arthntis that require momtonng Dmgs used to treat arthntis may cause death, disability, disease, and place an unborn child at nsk The undesired side effects or toxicities are listed for each d g category as described above. Analgesics associated side effects include dyspepsia, gastπc or small bowel bleeding, ulceration, renal insufficiency, confusion, rash, headache, hepatic toxicity NSAIDs also reversibly inhibit platelet aggregation and prolong bleeding time Antirheumatic agents (DMARDs) associated side effects include antimalaπals retinal or macular damage; sulfonamides hematologic toxicities (leukopenia, thrombocytopenia, hemolysis m patients with glucose 6-phosphate dehydrogenase (G6PD) deficiency); antimetabolites hepatic compromise including hepatic fibrosis, ascites, esophageal vaπces, cmhosis, pneumonitis, myelosuppression, immunosuppressives: myelosuppression, (cyclosponne. renal insufficiency anemia, hypertension), agents to treat metallic poison: rash, stomatitis, dysgeusia or metallic taste, myelosuppression (thrombocytopenia), protemuπa, nephrotic syndrome or renal failure, and induction of autoimmune syndromes (systemic lupus erythmatosus, myesthema gravis, polymyocytis, Goodpasture's syndrome), gold preparations hematologic, renal, pulmonary, and protemuna, chlorambucil. myelosuppression, myeloprohferative disorders, malignancy, hemonhagic cystitis Soluble TNF receptors agents have been shown to induce sepsis and predispose patients to senous infections. Further this product was associated with site of injection reactions, infections, and headache Glucocorticoid associated side effects include increased appetite, weight gam, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebn, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus- pituitary axis, decreased thyroid hormone semm binding protiens, and impaired wound healing. Since the majonty of RA patients are women in their reproductive years, the level and extent the agents used to treat RA affects or has a potential to affect the mother dunng pregnancy, cross the placenta, affect the developing fetus, or be excreted in breast milk duπng lactation are important issues facing the skilled practitioner Clinical medical therapeutic decisions must weigh the use of all of the above cunent therapies for RA against known capacity of these agents to affect both the mother and the child. Description of Mechanism of Action Hypotheses for Future Drug Development for Arthritis Rheumatoid arthritis has been thought to be the result of host genetic factors, immunoregulatory abnormalities and autoimmunity, and triggering or persistent microbial infection. Host genetic factors: the HLA-DR4 antigen (HLA, human leukocyte antigen) is significantly increased in RA patients. Recent studies have determined that a subtype of the HLA-DR4 share similar epitope among several MHC class II molecules and predispose to RA. Autoimmune component: in over 80%> of RA patients autoantibodies to the Fc portion of IgG (rheumatoid factors, RF) are present and can be used to determine diagnosis. The higher the titer of RFs the more severe joint disease and extrarticular manifestations. Related to the autoimmune component of the disease, ICAM-1 inhibitors, or other agents to reduce adhesion have been developed. Microbial Infections: of all the examined pathogens, only the Epstein-Ban vims (EBV) has remained unproven as a cause of RA. EBV has been shown to share a similar epitope as the HLA-DR4 epitopes, but EBV is ubiquitous and has yet to be a proven cause of RA. A gene, genes, or gene pathway involved in the etiology of arthritis or associated disorders or potential sites for targeted dmg therapy of arthritis are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development for the treatment of arthritis are listed in Table 38. B. Chronic Obstmctive Pulmonary Disease Description of Chronic Obstructive Pulmonary Disease Chronic obstmctive pulmonary disease (COPD) is an imperfect term that refers to four pulmonary disorders including simple chronic bronchitis, asthmatic bronchitis, chronic obstmctive bronchitis, and emphysema. A common characteristic of the disease is airway obstmction. Airways obstmction denotes the slowing of forced expiration. A decrease in the forced expiratory volume in 1 second (FEV1) to forced vital capacity (FVC) indicates that airflow is impaired. Forced expiration is determined primarily by intrinsic resistance of the airways, compressibility of the airways, and lung elastic recoil. Reduced maximal expiratory flow results from high airway resistance, reduced lung recoil, or excessive airways collapsibility. The overall cost of these illnesses to society is enormous due to the extent of the number of individuals afflicted with COPD, approximately 15 million Americans, and that COPD is cunently the fourth-leading cause of mortality. The high morbidity and mortality rates associated with COPD are linked to the failure to identify at-risk patients and intervene. The lungs have large reserves of pulmonary function and the slow progressive nature of the disease can often delay the clinical diagnosis and therapeutic intervention. Simple chronic bronchitis is a syndrome predominantly characterized by chronic productive cough and is usually the result of low-grade exposure to bronchial irritants. This syndrome is associated with enhanced mucous secretion, reduced ciliary activity, and impaired resistance to bronchial infection. Bronchitis patients range from those who experience sporadic cough producing mucous to those with a severe, disabling condition manifested by one or more of the following: increased resistance to airflow, hypoxia, hypercapnia, and ineversible nanowing of the small airways, i.e. bronchioles and bronchi (2 mm or less in diameter). Repeated exposure to bronchiole irritants in individuals with hyperactive or sensitive airways can lead to bronchospasm, i.e. bronchial smooth muscle constriction, that is frequently accompanied by excess mucous production and edema of the bronchial walls. Episodic bronchospasm in individuals with chronic bronchitis is termed asthmatic bronchitis and is applied to those individuals with chronic airway constriction, chronic productive cough, and episodic bronchospasm. Emphysema is characterized by abnormal, excessive, permanent enlargement of airway spaces distal to the terminal bronchioles, and is accompanied by destmction of their walls and may or may not be associated with fibrotic tissue. These changes result in a reduction of elastic recoil permitting excessive airway collapse upon expiration and leads to ineversible airway flow obstmction. Emphysema is strongly related to and conelated to inhalation of tobacco smoke, i.e. cigarette or cigar smoking. In emphysema there is a loss of elastic recoil leading to pulmonary hyperinflation. The hyperinflation reaches a limit when the diaphragm is pushed flat and no longer functions effectively. The chest wall is expanded to the point that it pushes inward rather than exerting its normal outward force. These anatomical changes alter inspiration to the point that exertion is nearly impossible. A deficiency in alpha 1- antitrypsin can predispose individuals to signs and symptoms of COPD. In these individuals there is a marked alveolar wall destmction with a non-uniform pattern of air space enlargement. In these patients there may be excessive formation of thick mucous and is often accompanied by persistent cough. Complications of COPD include hypoxemia, cor pulmonale, hypercapnia, and dyspnea. Sustained chronic hypoxemia is a condition that leads to pulmonary vasoconstriction that with time becomes ineversible and leads to cor pulmonale. Current therapies for COPD The current therapies is use for the treatment of subjects with COPD are aimed at reducing the airway obstmction that is reversible, controlling the persistent cough and sputum production, reducing or eliminate airway infections, increasing exercise tolerance to the maximum allowable at the individual's level of physiological deficit, controlling the remedial disease complications, i.e. cardiovascular dysfunction and arterial hypoxemia, and relief of the anxiety and depression or other psychiatric symptoms that accompany patients attempts to cope with the debilitating clinical manifestations. Lastly, all treatment regimens include education and supportive therapy to encourage subjects with COPD to cease behaviors that may exacerbate symptoms such as inhalation of pulmonary irritants, i.e. smoking and others, and substance abuse, i.e. narcotics and sedatives. Bronchodilators Bronchodilators can be inhaled, or by oral, subcutaneous, or intravenous routes. Beta-adrenergic agonists or other sympathomimetic agents are used to produce rapid acute bronchodilation. Anticholinergics agents are used to produce sustained bronchodilation. Nebulized atropine has been supplanted with the advent of a quaternary ammonium salt, ipratropium bromide, which undergoes minimal systemic absoφtion and thus has limited anticholinergic toxicity. Ipratropium has been shown to be effective in patients that have not responded to β-adrenergic agonists and can reduce sputum volume without altering viscosity. Anticholinergics and beta-adrenergic agonist combinations have been used with some success. Such combinations reduce the need to administer high doses, due to additive effects, and therefore reduce the likelihood for adverse effects or toxic side effects. Theophylline is a methylxanthine bronchodilator. Theophylline improves airway flow, decreases dyspnea, reduces pulmonary arterial pressure, increases arterial oxygen tension, improves diaphragmatic strength and endurance, increases right ventricular function (pulmonary vasodilator and cardiac inotropic effects), and may produce antiinflammatory effects. Expectorants Expectorants can be used to increase the secretion clearance in patients with COPD. Although this therapy has not been demonstrated to render clinical benefit, it is as add on therapy that enables the patient to experience an enhanced productive cough. Anti-Inflammatory agents Prolonged use of corticosteroids have been used to retard the rate of decline in FEV1 in COPD subjects. However, it has been determined that systemic corticosteroids are beneficial for acute exacerbations of COPD but are not used for long-term treatment and have not been proven to retard the progression of the disease. Corticosteroids affect the decline of FEV1 in the airways by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. Antiproteases and antioxidants Alpha 1 -protease inhibitor deficiency as a cause of early development of emphysema has increased the awareness of the role of protease-antipro tease and oxidant-antioxidant imbalances in COPD. Intravenous delivery of alpha 1 -protease inhibitor can provide the appropriate levels in those individuals with a genetic deficiency and those whose deficiency is acquired. Mucolvtics and secretion clearance agents can be used to assist in the removal of secretions during productive cough. These agents can thin secretions in patients with chronic bronchitis. Supplemental oxygen therapy is used to treat the deleterious effects of sustained chronic hypoxemia and hypercapnia. Conection of this condition is one of the treatments shown to have a positive effect on the survival rate in patients with COPD. Treatment of cases of cor pulmonale includes the use of diuretics and positive inotropic agents such as digitalis. Careful monitoring is required in these patients due to a development of marked right ventricular hypertrophy. Dyspnea may be severely disabling despite aggressive therapy. Judicious use of opiates to control dyspnea and increase exercise tolerance have been proven to be beneficial. Unfortunately, opiates can have a respiratory depressant effect and care must be taken to deliver the appropriate therapeutic dose. Many patients with COPD find themselves anxious or depressed or both. Appropriate use of psychoactive agents can be used to control the signs and symptoms of anxiety and depression. Surgical procedures can be performed to attempt to restore pulmonary capacity and function. Lung volume reduction surgery is useful to remove a portion of emphysematous lung tissue so that the diaphragm can return to its normal dome shape and the chest wall can reassume its normal configuration, mechanics, and physiology. Bullectomy is a procedure in which large bullae and sunounding lung tissue are removed. This allows for the remaining tissue to expand and once again function normally. Another procedure is lung transplantation. This expensive and aggressive approach is usually reserved for younger patients, particularly those who are alpha 1-antitrypsin deficient. Limitations of Current Therapies for COPD The most common limitations for the use of bronchodilators is the mistaken use of inhalants and inadequate patient education. Beta adrenergic therapy is limited by three factors: 1 ) the density of β2 receptors in the airways decreases with age, 2) despite the selectivity of the β2 receptor agonists, there is cross reactivity to βl receptors and may affect the myocardium and other peripheral tissues, and 3) there is β-adrenergic receptor desensitization. Most of the recommended doses of beta adrenergic agonists provide less than maximal bronchodilation. Beta-adrenergic agonists can cause tremor, reflex tachycardia, tachyphylaxis, cardiomyopathy, and other cardiac toxic effects. Tachycardia is particularly problematic in the elderly or for those individuals who are at cardiac risk. Further, β-adrenergic agonists have been shown to cause hyperkalemia. The majority of patients with COPD are current or former smokers, all of whom are may have coexisting coronary artery disease, thus in the compendium of therapies it is desirable to have alternatives to β-adrenergic agonists. Anticholinergics as bronchodilators have been associated with systemic side effects. In particular, systemic anticholinergic side effects include bradycardia (if pronounced, includes compensatory tachycardia), dry mouth, inhibition of sweating, dilatation of the pupils, and visual blurring. Ipratropium has a slow onset of action and a longer duration of action than β-adrenergic agonists which can be deleterious for acute bronchodilation because patients continue to administer the drug without effect and overdose. Theophylline continues to be a controversial treatment due to misconceptions of its role as a bronchodilator, dmg delivery problems, and conflicting results of comparative studies during acute exacerbations. Further, theophylline has a limited therapeutic window, i.e. the dose required to achieve bronchodilation is close to the dose associated with undesirable or adverse side effects including convulsions, cardiac anhythmias, tachycardia, vasodilation, and diuresis. Further complicating therapy with theophylline is the intra-patient variability in efficacious response. Long-term use of corticosteroids can be useful for patients in which continued symptoms or severe airflow limitations exist despite therapy with other agents. Only 20-30%> of these patients experience therapeutic benefit for long-term use and indiscriminate use often leads to adverse effects without benefits. Unfortunately there have not been identified predictors of responders or nonresponders to long term steroid use in patients with COPD. Therefore, only those patients that attempt long-tem steroid use and have documented clinical improvement should continue steroid therapy. Unfortunately, those patients in which long-term steroid use results in no benefit are subjected to potential adverse effects or toxicities. Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus-pituitary axis, decreased thyroid hormone semm binding protiens, and impaired wound healing. Mucolytic and secretion clearance agents have been shown to improve thinning secretions however, there is little evidence to suggest that these agents render clinical improvement. Further cough suppressants may impair secretion clearance and possible increase the risk of pulmonary infection. Description of Mechanism of Action Hypotheses for Future Drue Development of Candidate Therapeutic Interventions of COPD Since the predominant category of patients with COPD were or are cunent smokers smoking cessation programs and agents used to help patients quit smoking will be a valuable addition to therapeutic regimens. Nicotine replacement therapies such as nicotine patches (transdermal), gum, and transnasal formulations as well as bupropion (an antidepressant or other in this category) should be considered. Other therapies to be considered are novel bronchodilators for inhalation therapy without the use of chorofluorohydrocarbons (CFCs), next generation anticholinergic therapies, alpha 1 antiproteinase augmentation therapies, and refinement of surgical procedures. A gene, genes, or gene pathway involved in the etiology of COPD or associated disorders or potential sites for targeted dmg therapy of COPD are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development for the treatment of COPD are listed in Table 39. C. Autoimmune Disease Description of Autoimmune disease An immune response to "self antigens, or autoimmunity, can vary from minimal to severe depending on the extent of the loss of self tolerance and to the localization of the antigens. There is then a distinction between autoimmune response which may or may not be pathologic and autoimmune disease which does lead to pathologic conditions. In autoimmune disease there is a combination of the following types of evidence, 1) identification of the target antigens, 2) identification and isolation of self-reactive autoantibodies or self-reactive lymphocytes, 3) identification of clinical evidence, i.e. familial hereditary data, lymphocyte infiltration, MHC association and clinical symptomatic improvement with immunosuppressive agents. Initiation of auotimmune disease is thought to require one or more of the following: genetic predisposition to loss of tolerance, environmental factors that stimulate abenant immune response, or loss or dysfunction of cellular or organ physiological processes leading to pathological immune response. Since many autoreactive clones of T and B cells exist and are normally regulated by homeostatic mechanisms, loss or breakdown of this system of checks and balances can lead to activation or enhancement of these autoreactive clones and ultimately lead to autoimmune disease. There are a few autoimmune disease indications whereby inflammation and immune response gene pathways should be considered in the stratification or therapeutic choice of patient groups based upon genotype. There are multiple examples of autoimmune diseases or diseases that have an autoimmune component including: amyotrophic lateral sclerosis, anti-phospholipid syndrome, aplastic anemia, autoimmune hemolytic anemia, diabetes mellitus type 1, Guillan-Bane syndrome, idiopathic thromobocytopenic puφura, Grave's disease, myasthenia gravis, polymyositis, rheumatoid arthritis, Hashimoto's thyroiditis, uveitis, Wegener granulomatosis, periarteritis nodosa, ocular pemphigoid, pemphigus vulgaris, psoriasis, Goodpasture's syndrome, Churg-Strauss vasiculitis, poly-dermatomyositis, Cogan syndrome- autoimmune inner ear disease, hemolytic uremic syndrome, idiopathic glomerulonephritis, inflammatory bowel disease, Crohn's disease, microscopic polyarteritis, and multifocal motomeuron neuropathy. Here we discuss four specific diseases that represent larger patient populations and are representative of diseases in which therapy can be aimed at suppressing the hyperactivity of the immune system. These include multiple sclerosis, systemic lupus erythmatosus, scleroderma, diabetes mellitus type I. sarcoidosis, and nephritis. Multiple Sclerosis Multiple sclerosis (MS) is a disorder of multifocal sites of myelin sheath destmction, perivascular-lymphocytic cuffing and variable degree of oligodendroglial loss. In profound cases, there is gliosis, axonal transection, and neuronal and axonal loss. There are an estimated 300,000 Americans diagnosed with MS. The estimated cost of MS is $5 billion dollars. Clinically, MS begins with a relapsing illness with episodes of neurological dysfunction lasting several weeks, followed by substantial or complete improvement. This is identified as the relapsing-remitting stage of the disease found to be predominantly in females (1.6: 1 ). There are some patients that remain in this stage of the disease for decades; others may rapidly progress to the next stage. As time progresses, and repeated relapses occur, recovery becomes less and less complete or as substantial. In these cases, a gradual relapse independent clinical progression develops and is termed secondary progressive MS. Further, the nonrelapsing-nonremitting form is characterized by a gradual progression and steady worsening of neurological function without any recovery or improvement. A steady but gradual neurological decline and predominately identified in males characterizes the primary progressive form of MS. Clarity in understanding the significance of these varying disease patterns and diagnosis is dependent on quality neurological examination overtime. Systemic Lupus Erythmatosus Systemic lupus erythmatosus (SLE) is a disease characterized by inflammation in many different organ systems associated with the production of antibodies to reactive to nuclear, cytoplasmic, and cell membrane antigens. Clinical manifestations of the disease include reddish rash on the cheeks, fatigue, anemia, rashes, sun sensitivity, alopecia, arthritis, pericarditis, pleurisy, vasiculitis, nephritis, and central nervous system disease. The immune hypereactivity appears to derive from immune hypereactivity and loss of self-tolerance. In these patients antibodies are produced against several nuclear components, notably antinuclear antibodies to native double stranded DNA, single stranded DNA, or nucleohistones. Scleroderma Scleroderma is a chronic disease marked by increases of fibrotic tissue involving the circulatory system, connective tissue (in particular the skin), visceral organs, and the immune system. There are approximately 500-700,000 Americans diagnosed with scleroderma. There are two types of scleroderma, localized and systemic. In localized scleroderma (linear and moφhea) the disorder of the connective tissue is limited to the skin, the tissues just beneath the skin, and muscle. Internal organs are not affected. In systemic scleroderma (sclerosis) vascular, digestive, pulmonary , renal, muscle and joints may be affected. Raynaud's syndrome (frequent spasms of small arteries induced by temperature changes and emotion resulting in deprivation of blood supply to peripheral tissues), CREST syndrome (calcium deposits, Reynaud's syndrome, loss of muscular control of the esophagus, sclerodactylia, and telangiectasia), and Sjogren's syndrome (inflammation of the conductive, cornea, tear, and salivary glands with progressive destmction by lymphocytes and plasma cells) are both subcategories of scleroderma. The clinical manifestations of scleroderma include the following symptoms: fatigue, swelling and numbness of the hands and feet, shiny skin and disappearance of skin folds, ulcers on the fingers, calcium deposits on the fingers, joint inflammation, joints tightening into bend position, muscle weakness, itchy skin, difficulty in swallowing, shortness of breath, fatty dianhea or constipation, and loss of body hair. Although ultimately renal impairment and failure is a common endpoint, therapy affecting the hypertensive phase or renal involvement has changed the mortality rate. Diabetes Mellitus type I This form of diabetes involves the chronic inflammatory destmction of the insulin-producing islet cells of the pancreas. Although this form of diabetes is treated similarly to the type II form (which is not linked to autoimmunity), i.e. insulin replacement therapy, early identification of type I versus type II individuals may be useful to thwart the autoimmune destmction of the β-cells. There are an estimated 500,000 to 1 million Americans that have type I diabetes, it is the seventh leading cause of death, and the following is a list of the progressive complications that are associated with the unregulated carbohydrate balance in tissues: retinopathy leading to blindness, nephropathy (diabetic nephropathy is the leading cause of end- stage renal disease), coronary and cardiovascular disease, neuropathy (severe forms can lead to amputation), impotence (diabetic neuropathy and cardiovascular disease can lead to impotence), and stroke. Sarcoidosis Sarcoidosis is a granulomatous disorder characterized by enhanced cellular immune response at one or more involved sites. The prevalence of sarcoidosis is 5 in 100,000, so approximately 13,000 patients have been diagnosed. Between 80-90% > of patients with sarcoidosis have pulmonary involvement, however, any organ can be affected. Pulmonary involvement includes dyspnea with or without exertion, persistent dry cough, and atypical chest pain. Cor pulmonale can develop as a complication of pulmonary dysfunction and further progress to right atria dilatation and right ventricular hypertrophy. Ocular involvement includes disturbance in visual acuity, and in chronic cases may lead to glaucoma, cataract formation and retinal neovascularization. In 80% of the cases, sarcoidosis is self-limiting and results in minimal symptomology, discomfort, or debilitation. However in the remaining 20%, sarcoidosis patients face potenitally serious debilitation, disfigurement, and can be life threatening. Misdiagnosis is frequent and can limit appropriate therapeutic intervention. Nephritis Inflammation of the kidneys results in impaired renal function. Nephritis can be either interstitial or glomerular. In either case, mononuclear cells infiltrate in the interstitium of the renal cortex. Eosinophils, and in some cases, polymoφhonuclear leukocytes are found in a similar compartment. The infiltrate may be diffuse or patchy and may be accompanied by fibrotic tissue. Membranous nephropathy may develop and lead to impairment of glomerular filtration rate. There is evidence to suggest both cytotoxic T cells and T-cell mediate delayed hypersensitivity are involved. Nephritis is a component of the clinical manifestation of systemic lupus erythmatosis, scleroderma, and other autoimmune diseases and disorders. Current therapy for Autoimmune Diseases and Disorders Agents used to treat autoimmune disease fall into one of the following four categories: analgesics (NSAIDs, salicylates), immunosuppressive agents, hormones (glucocorticoids), and skin and mucosal membrane preparations Analgesics: Typically, pain associated with autoimmune disease can be controlled with NSAIDs including but not excluded to, salicylates, para- aminophenol derivatives, indole and indene derivatives, heteroaryl acetic acids, arylproprionic acids, anthranilic acids, enolic acids, or alkanones. Antiinflammatory agents such as cyclooxygenase inhibitors, lipoxygenase inhibitors, and others can be used to block the inflammation physiological pathway which mediate pain. However, because these dmgs are limited in their efficacy in advanced or more severe stages of autoimmune disease, these agents are add-on therapies. NSAIDs derive their principle mechanism of action by the inhibition of prostaglandin and leukotriene synthesis. These compounds inhibit key enzymes in the biosynthetic pathway, i.e. cyclooxygenase. There are dmgs that selectively inhibit isoforms of cyclooxygenase 1 and 2 (COX-1, COX-2) which enhances patient tolerance due to the prevalence of COX-2 induction occurs in inflammation mediated by cytokines and others. Immunosuppressive dmgs or agents: Agents involved in the modification of the immune system for the treatment of autoimmune disease are immunosuppressive agents Immunosuppressives include azathiopπne, cyclosponne, pemcillamine, antimalaπals (chloroqume, hydroxychloroqume), alkylating agents (cyclophosphamide), and antimetabolites (methotrexate) Hormones and Growth Factors Agents acting at hormone receptors or growth factor receptors include steroids (glucocorticoids), adrenocorticotrophic hormone (corticotropm), and tumor necrosis factor inhibitors (soluble TNF receptors (enbrel) and TNF monoclonal antibody (remicade) Since the autoimmunity component of the disease is dnven pnmaπly by activated T-cells, which give nse to cytokines IL-1 and TNF at the affected areas These agents are known to interfere with the actions of these cytokines Corticosteroids affect the immune response by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcπption of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on- activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitπc oxide synthesis. Plasma Exchange A useful technique for the removal of autoantibodies is a process called plasmaphoresis or plasma exchange In this process, antibodies are removed that mediate humoral immune response to the autoantigen Antioxidants Many of the therapies in use for these auotimmune diseases are aimed at reducing the level and extent of tissue damage mediated by T-cell immune response For example, dimethyl sulfoxide, dimethyl sulfone, para- ammobenzoic acid, and vitamin E are included m this category Limitations Cunent Therapies for Autoimmune Disease based upon Low efficacy The therapies discussed above are limited to the slowing or retarding the progression of autoimmune disease As immune response tissue damage occurs, degeneration of the function progresses, irreversible damage occurs, and therapeutic options become limited Thus, therapies for autoimmune disease are aimed at reduction of manifestation of symptoms by controlling the clinical manifestations of inflammation and the hypersensitive immune response The reduction of clinical symptoms of autoimmune disease following immunosuppressive therapy by one of the agents listed above is only evident after several weeks to months after therapy The slow clinical relevance of these therapies limits the clinician to determine optimal therapy for individuals with autoimmune disease, and provides a nsk for selection of optimal therapy for any given stage of the disease Furthermore, there may be delays in identifying those patients that have an autoimmune hypeneactivity, and this can delay therapeutic intervention. Limitations Cunent Therapies for Autoimmune Disease based upon Toxicity or Undesired side effects There are toxicities and undesired side effects associated with the above cunent therapies for autoimmune disease that require monitoring. Dmgs used to treat autoimmune disease may cause death, disability, disease, and place an unborn child at risk. The undesired side effects or toxicities are listed for each dmg category as described above. Analgesics associated side effects include dyspepsia, gastric or small bowel bleeding, ulceration, renal insufficiency, confusion, rash, headache, hepatic toxicity. NSAIDs also reversibly inhibit platelet aggregation and prolong bleeding time. Immunosuppressive therapies have associated side effects including antimalarials: retinal or macular damage; sulfonamides: hematologic toxicities (leukopenia, thrombocytopenia, hemolysis in patients with glucose 6-phosphate dehydrogenase (G6PD) deficiency); antimetabolites: hepatic compromise including hepatic fibrosis, ascites, esopageal varices, cinhosis, pneumonitis, myelosuppression; immunosuppressives: myelosuppression, (cyclosporine: renal insufficiency anemia, hypertension); penicillamine: rash, stomatitis, dysgeusia or metallic taste, myelosuppression (thrombocytopenia), proteinuria, nephrotic syndrome or renal failure, and induction of autoimmune syndromes (systemic lupus erythmatosus, myesthenia gravis, polymyocytis, Goodpasture's syndrome). Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus- pituitary axis, decreased thyroid hormone semm binding protiens. and impaired wound healing. Since the majority of autoimmune disease patients are women in their reproductive years, the level and extent the agents used to treat autoimmune disease affects or has a potential to affect the mother during pregnancy, cross the placenta, affect the developing fetus, or be excreted in breast milk during lactation are important issues facing the skilled practitioner. Clinical medical therapeutic decisions must weigh the use of all of the above cunent therapies for autoimmune disease against known capacity of these agents to affect both the mother and the child. Description of Mechanism of Action Hypotheses for Future Drus Development for the Treatment of Autoimmune Disease Autoimmune disease has been thought to be the result of host genetic factors, immunoregulatory abnormalities and autoimmunity, and triggering or persistent microbial infection. A gene, genes, or gene pathway involved in the etiology of atuoimmune diseases or disorders or associated disorders or potential sites for targeted dmg therapy of autoimmunity are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development are listed for the treatment of autoimmune disease or disorder, Tables 40 and 42, and for systemic lupus erythmatosus, Table 41. D. Immunosuppression- Transplantation Description of Transplantation There are many different conditions in which medical or surgical therapy is unable to halt, retard, or treat the underlying disease, disorder, or dysfunction. Although many refractory diseases, disorders, or dysfunctions do not lead to severe cases, there are some in which the progression leads to conditions in which the remaining therapeutic alternative is replacement of the diseased tissue with normal donated tissue by transplantation. These end stage conditions include both primary disease or complications from a disease. For example whole organ transplantation is an end- stage therapuetic alternative in the following indications, end-stage cardiomyopathy, end-stage renal disease, pulmonary disease, cinhosis of the liver, as well as other end-stage diseases affecting whole organ function. Besides whole, or partial organ transplantation there are programs aimed at replacing cells in specific tissues to enable or restore physiologic function. For example cellular transplantation includes, but not excluded to, grafting bone manow cells in patients with hematopoeitic or lymphocytic cancers, dopaminergic producing cells in brains of patients with Parkinson's disease, striated muscle cells in patient's with Duchenne's muscular dystrophy, myocytes or cardiomyocytes in patient's with ischemic heart disease or cardiomyopathy, and replacement of neurons or astrocytes or glial cells in neurodegenerative disease including but not excluded to Alzheimer's disease, amyotrophic lateral sclerosis, multiple sclerosis, Huntington's disease, refractory pain, epilepsy, and stroke. In this way, transplantation includes autografts, isografts, allografts or xenografts and can involve whole organ or cellular grafts. With the exception of autologous transplantation, all other transplantation procedures include pre- and post-surgical immunosuppression to blunt graft rejection or graft versus host disease Successful immunosuppression in this setting includes an appropnate balance between the need to prevent the process of graft rejection and the nsk of suppressing the recipient's immune system to the extent that they become vulnerable to infection or other complications Transplantation is immunologically mediated Both T cells and circulating antibodies are induced against allografts or xenografts While the antibodies are responsible for rejection of erythrocytes, T-cells are mainly responsible for the rejection of most other type of tissue The antigens found on grafted tissue which initiate the rapid rejection of an allograft are found on most cell membranes and are encoded by genes in the major histocompatibihty complex (MHC) which are called the HLA The stmctures encoded in these genes, MHC class I and class II molecules, are involved in the determining the discnmination between self and non- self The degree of the histocompatibihty betwee donor and recipient can be determined serologically, by genotypιng,or by a mixed lymphocyte reaction Survival of HLA nonmatched allografts is prolonged by anti-inflammatory agents, cytotoxic agents, antimetabolites, and other modalities aimed at lmmunosuppressmg the recipient These approaches have proven clinical success in terms of graft survival and clinical symptomology Rejection can occur at any time, and is either hyperacute, acute or delayed The rate, extent, and underlying mechanism of transplantation rejection vanes dramatically from individual to individual Physiological factors include patency of blood circulation, lymphatic drainage, expression of antigens on the graft, and others that can influence the rejection rate In hyperacute rejection, preexisting host antibodies to antigens found on the grafted tissue mount an immune response These antibodies activate complement, followed by platelet activation and deposition causing swelling and interstitial hemonhage in a whole organ graft, or specific cell targeting m a cellular transplant Cell mediated immunity is not activated in the hyperacute response In acute rejection, infiltration of lymphocytes and macrophages recognize the foreign antigen on the graft cells, and initiate a cascade of intragraft events that ultimately leads to host cellular and humoral mediated destmction of the grafted tissue and if unchecked will result in ineversible loss of the graft This acute process occurs rapidly and does not in the first stages affect the vital stmctures of a whole organ graft, which allows for identification of the process and implementation of therapy In many cases, an acute rejection episode can be reversed, and approximately 30-50%) of whole organ graft recipients undergo one or more of these episodes in the early transplant penod Delayed or chronic rejection occurs in a slower process than acute rejection and ultimately leads to a gradual loss of function in the grafted tissues. In chronic or delayed rejection, both cell mediated immunity and humoral immunity is activated. Chronic rejection is characterized by arteriosclerosis, in which the smooth muscle cells lining the arteries in the graft organ proliferate to create lesions and lead to fibrosis, with a result of constricting blood flow. As a result of the chronic immune rejection, there is slow and progressive destmction of the grafted organ or cells. If damage to the tissue is extensive, very little can be done to save the graft. Current Immunosuppressive Therapies The goal of clinical immunosuppression in the transplantation setting is to control allograft rejection. Clinical immunosuppression involves the non-specific suppression of both cell-mediated and humoral immune reactivity to the grafted tissue. Although a number of methods have been proposed, successful prolongation of graft survival has been attained through the use of a combination of therapies that suppress both the lymphocytic interaction and proliferation and therapies that deplete the pool of available lymphocytes. Antiproliferative agents These agents are useful to blunt the proliferative phase of lymphocyte activation of the immune response. Purine analogs Azathioprine acts to inhibit the proliferation of T cells. Azathioprine is cleaved to 6-mercaptopurine and it is this active compound that serves to suppress the T-cell mediated antigenic determination and engraftment. Azathioprone is a relatively non-selective immunosuppressive agent. Other agents in the same class as azathioprine, i.e. antimetabolites, include but are not excluded to, mercaptopurine, chlorambucil, and cyclophosphamide. Pyrimidine analogs The agents (cytosine arabinoside) inhibits DNA synthesis and therefore have their greatest effect on the immune response during the proliferative phase of lymphocyte activation. These agents inhibit primary antibody response and have minimal effects on the cell-mediated immunity. Folic acid analogs These agents (methotrexate, aminopterin) inhibit dihydrofolate reductase preventing the conversion of folic acid to tetrahydro folic acid. This conversion is necessary for the production of DNA and RNA. Alkylating Agents These agents (nitrogen mustard, phenylalanine mustard, busulfan, cyclophosphamide) alter the stmcture of the DNA and RNA. These agents have reactive ring stmctures which combine with electron rich groups such as tertiary nitrogen in purines or pyrimidines, or -NH2, -COOH, -SH, -PO3H2 groups. These reactions alter the composition of the DNA , and if not repaired, chromosomal replication will be altered in acitvated proliferating cells. The use of alkylating agents in the setting of transplantation is time dependent and is effective just before or during the activation of the immune system by antigen. Cyclophosphamide has been shown to have a greater effect on B-cells rather than T-cells, thereby inhibiting the humoral response to a greater degree. Antibiotics These agents (actinomycin D, mitomycin C, puramycin, chloramphenicol) inhibit either nucleic acid or protein synthesis. Cyclosporin acts by inhibiting the production of IL-2, which results in an inhibition of the proliferation of T and B lymphocytes. Cyclosporin is widely prescribed for transplantation patients due to the clinical advantage of potent immunosuppression with limited myelosuppression. FK-506 (Tacrolimus) is an agent that acts by inhibiting the production of IL- 2 which prevents the proliferation of T and B lymphocytes. Mycophenolate mofetil is rapidly converted to mycophenolic acid which selectively inhibits T and B cell proliferation. Mycophenolate mofetil has an advantage over azathiprine because it does not damage chromosomes. Lymphocyte Depletion agents A tilymphocvtic globulin (ALG) is an agent that binds to circulating T- lymphocytes and the cells coated with the ALG are lysed and cleared by the reticuloendothelial system. ALG is more commonly used for renal transplantation, showing little to no benefit for liver or bone manow transplantation.. Radiation Total lymphoid inadiation or total body inadiation is based upon the immunosuppression observed after this procedure was used in patients with Hodgkin's lymphoma. The radiation causes breakdown in the nucleic acid stmcture, and the effect is time dependent since there are systems within all cells for the repair of DNA. Since the radiation affects those cells in M or G2 phase, those cells in Gl or S phase are resistant. Monoclonal antibodies A murine monoclonal antibody is available to deplete the circulating CD3 lymphocytes. This antibody reacts with the T3 recognition site of the T- lymphocytes and blocks the recognition of the Class I and II antigens. This leads to prevention of the activation of the effector lymphocytes. This antibody has been useful in the treatment of rejection of renal, pancreatic, hepatic, cardiac, and pulmonary whole organ transplantations. Steroids- such as the glucocorticoids are widely used in transplantation in combination with other dmgs. As well as providing antiinflammatory therapy, corticosteroids suppress immune function by inhibiting the activation of T cells. Corticosteroids affect the inflammation within the airways by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. Steroids are highly effective in the early induction and maintenance regimens and are first line therapy in acute allograft rejection. Blood transfusions can be used to cause allosensitzation if the recipient is exposed to donor antigens in the presence of azathioprine. In this way, induction of a specific degree of hyporeactivity against graft antigens can result by a potential suppressor cell phenomena. Limitations of Immunosuppressive Therapies due to Lack of Efficacy As suggested, the efficacy of immunosuppression is a balance between prevention of graft rejection or graft versus host disease and subjecting a patient unnecessarily to blunted immune defenses to ward off infections. All too often, this balance is not achieved and on one end the patient succumbs to infections or on the other the graft is rejected. It has been estimated that 30% of the transplantation patients are in this category. Limitations of Immunosuppressive Therapies due to Toxicities or Undesired Side Effects Antiproliferative Agents Azathioprine is associated with suppression of bone manow production, and blood disorders including anemia, thrombocytopenia, and leukopenia. Hepatotoxicty ocuns in a dose-independent manner, and is ineversible. Azathioprine is associated with chromosome damage and therefore is mutagenic. Methotrexate and aminopterin are associated with bone manow suppression, mucosal breakdown, gastrointestinal bleeding, megaloblastic hematopoiesis. Alkylating Agents are associated with stomatitis, nausea, vomiting, dianhea, skin rash, anemia, and alopecia. Specifically, cyclophosphamide has been associated with fluid retention, hemonhagic cystitis, and cardiac toxicity. Cyclosporin is associated with gingival hypeφlasia, hirsutism, tremor, hypertension, hyperkalemia, hepatotoxicity, hyperglycemia, hypomagnesiumemia, hypercholesterolemia, hypertriglyceridemia, and hyperuricemia, nausea and gastrointestinal inegularities, and renal dysfunction. Nephro toxicity associated with cyclosporin manifests as tubular necrosis, interstitial fibrosis, and tubular atrophy. FK506 is associated with neurotoxicity, nephrotoxicity, and disturbances of glucose metabolism. The major neurotoxic symptoms are reversible and dose dependent and include headache, tremors, parasthesias, insomnia, increased sensitivity to light, mood changes, aphasia, and seizures. There has been a suggested association of FK-506 with cardiomyopathy and it is contraindicated in pregnancy. Lymphocyte Depletion Agents ALGs are associated with anemia, thrombocytopenia, and allergic reactions including urticaria, anaphylactoid reactions, semm sickness, joint pain, fever, and malaise. Radiation is associated with higher incidence of infections and chromosomal breakage and mutations. Monoclonal antibody therapy has been associated with the production of human anti-mouse antibodies (HAMA) in 80%> of the treated patients and the sensitization rate is 15-40% thus limiting retreatment rates. Side effects are fever, chills, nausea, vomiting, headache, dyspnea, wheezing, pulmonary edema, tachycardia, hypotension, aseptic menigitis, seizures, and coma. These symptoms are related to the inordinate release of cytokines TNF, IL-1 , and interferon-gamma. Although these symptoms can be reduced by pretreatment with steroids, acetominophen, or diphenhydramine the HAMA response precludes repeated use. Steroids- Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus-pituitary axis, decreased thyroid hormone semm binding protiens, and impaired wound healing. Complications of Immunosuppression In addition to the above listed toxicities and undesirable side effects, potent immunosuppression as required in the transplantation setting leads to prolonged immune compromise and predisposes the patient to infections (80%> of the patients) and cancer (ranging between 10-40%> of the patients). This risk has been proposed to result from impaired immune surveillance mechanisms, chronic antigenic stimulation, reactivation of latent oncogenic vimses and the direct oncogenic effects of the immunosuppressive agents. Moreover, 40%> of the deaths of transplant patients are attributable to the complications of infections or a combination of infection and graft rejection. The infections experienced by transplant patients are 50%> bacterial, 30% > viral, 15% fungal. Some of the common bacterial infections are Staphylococcus aureus, Staphylococcus epidermidis, and gram-negative rods in line sepsis. Urinary tract infections, pneumonias, wound infections, and surgical infections (including cholecystitis, appendicitis, diverticular disease, ulcer, etc.). Common viral infections include cytomegalovims, Epstein-Ban vims, Heφes Simplex. Virus, and varicella zoster vims. Further, common fungal or protozoan infections include Candida albicans, Asperigillus flavus, Cryptococcus neoformans, Coccidiodes immitis, Histoplasma capsulatum, Norcardia asteroides, and Pneumocystis carinii. Description of Mechanism of Action Hypotheses for Future Immunosuppressive Drug Development The majority of the hypotheses for future therapeutic interventions for graft rejection and graft immunoreactivity are based upon the understanding the immunologic mechanisms that cause and peφetuate the rejection within the graft. A gene, genes, or gene pathway involved in the etiology of transplantation or immunosuppression or associated disorders or potential sites for targeted dmg therapy of transplantation are depicted in Table 9 with the specific gene list in Table 4. Current candidate therapeutic interventions in development for the treatment of anemia are listed in Tables 42 and 43. E. Pain Associated with Inflammation Description of Pain Associated with Inflammation Pain associated with inflammation can be caused by pathologic processes in somatic stmctures or viscera, or by prolonged dysfunction of parts the peripheral nervous system.. Pain associated with inflammation may be the result of recunent injuries, trauma, headache, arthritis, chronic obstmctive pulmonary disease, psoriasis, or other pathologies. Pain associated with inflammation may be acute or chronic depending on the level and extent of the inflammation. Current therapies for Pain Associated with Inflammation Therapeutic management of pain resulting from inflammation includes a three step ladder approach: non-opioid analgesics are stepwise prescribed in combination with moderate to potent opiates. The guidelines call for a determination by the patient and the physician of pain relief. Broadly speaking, the guidelines are as follows: mild pain is treated with non-opioid analgesics, moderate or persisting pain is treated with a weak opioid plus non-opioid analgesics, and severe pain that persists or increases is treated with a potent opioid plus non-opioid analgesics. Analgesics: Typically, pain associated with inflammation can be controlled with NSAIDs including but not excluded to, salicylates, para-aminophenol derivatives, indole and indene derivatives, heteroaryl acetic acids, arylproprionic acids, anthranilic acids, enolic acids, or alkanones. Antiinflammatory agents such as cyclooxygenase inhibitors, lipoxygenase inhibitors, and others can be used to block the inflammation physiological pathway which mediate pain and the progression of the disease. However, because these dmgs are limited in their efficacy in advanced or more severe stages of arthritis, these agents are add-on therapies. NSAIDs derive their principle mechanism of action by the inhibition of prostaglandin and leukotriene synthesis. These compounds inhibit key enzymes in the biosynthetic pathway, i.e. cyclooxygenase. There are dmgs that selectively inhibit isoforms of cyclooxygenase 1 and 2 (COX-1 , COX-2) which enhances patient tolerance due to the prevalence of COX-2 induction occurs in inflammation mediated by cytokines and others. Further, pyrimidine synthesis inhibitors can be used as an antiinflammatory agent in arthritis, e.g. leflunomide. Limitations of Current Therapies for Pain Associated with Inflammation Limitation of Therapies for Pain Associated with Inflammation due to Low efficacy The therapies discussed above are limited to the slowing or retarding the progression of arthritis. As degeneration of the joints progresses, and ineversible damage occurs, the options become limited. Thus, therapies for arthritis are aimed at reduction of manifestation of symptoms by controlling the clinical manifestations of inflammation. Limitations of Therapies of Pain Associated with Inflammation due too Toxicity or Undesired side effects Analgesics associated side effects include dyspepsia, gastric or small bowel bleeding, ulceration, renal insufficiency, confusion, rash, headache, hepatic toxicity. NSAIDs also reversibly inhibit platelet aggregation and prolong bleeding time. Description of Mechanism of Action Hypotheses for FuturePain Associated with Inflammation Drug Development The persistence of pain most likely involves a cascade of pathological neurochemical events that lead to abnormal sensory hyperexcitability and excitotoxicity. The genes listed in Figure 1 are part of a pathway are all involved in producing prostaglandins or leukotrienes, which are two potent mediators of inflammation. Inordinate levels of prostaglandins have been implicated in pain associated with inflammation, and several dmgs target this branch of the pathway, to inhibit the action of leukotrienes. When a cell receives a pro-inflammatory stimulus, such as tumor necrosis factor, membrane phosphlipids, or interleukin- 1 , as shown in the figure, membrane phospholipases are activated, and arachidonic acid is released from membrane phospholipids into the cell. The liberated arachidonic acid is then metabolized either by the cyclooxgenase enzymes, which leads to the production of prostaglandins, or the lipoxgenase family of enzymes, which leads to the production of leukotrienes. There are several types of prostaglandins and leukotrienes, and many of the enzymes listed here function to convert one form into another. The presence of leukotrienes and prostaglandins can lead to a persistence of neural hyperexcitability involving a sequence of neuroplastic events. A gene, genes, or gene pathway involved in the etiology of pain or associated disorders or potential sites for targeted dmg therapy of pain are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development for the treatment of pain associated with inflammation are listed in Table 44. F. Psoriasis Description of Psoriasis Papulosquamous skin disorders have diverse etiologies and include psoriasis, Reiter's syndrome, pityriasis rosea, lichen planus, oityriasis rubra pilaris, secondary syphilis, mycosis fungoides, and ichthyosiform emptions. Psoriasis is a genetically determined, chronic epidermal proliferative disease with an unpredicatable course. Psoriasis appears as erythematous plaques with silvery, mica-like scales, and is usually nonpruritic. The plaques appear anywhere on the body and almost never involves the mucous membranes. There are variations of psoriasis including guttate psoriasis, inverse psoriasis, pustular psoriasis, erythroderma, and psonatic arthntis. There is an increased prevalence of psonasis m subjects with the HLA antigens BW17, B13, and BW37. Further, 30% of cases have a family history of psonasis. The Koebner phenomena is a hallmark charactenstic of psonasis, e.g. intense trauma (scratches or surgical incisions) to the skm induces new linear papulosquamous lesions. This multifactonal disease is charactenzed by an accelerated cell cycle in an increased number of dividing cells that results in rapid epidermal cell proliferation It is estimated that 4-5 million Americans have psonasis, 100,000 have severe cases, and 1 in 20 have psonatπc arthntis. Current Therapies for Psoriasis The goals of the therapeutic regimens is to limit the epidermal proliferation underlying the dermal inflammation. There are both topical and systemic treatments available, however in either category the treatment suppresses the condition for only as long as is administered. The treatment of psonasis entails a stepwise increase of extent of the therapy ranging from topical applications to phototherapy to systemic interventions to prevent the epidermal proliferation. In the first step topical treatments include corticosteroid ointments, vitamin D containing ointments, preparations containing coal tar or anthralin. salicylic acid containing ointments, and vanous other moistuπzers and bath solutions. These steps are aimed at reducing the itching, scaling, and progression of the lesions. In the second step, phototherapy other than natural sunlight can be used to thwart the epidermal cell proliferation. In these cases, ultarviolet light is administered to affected areas or uniformly to the body. In phototherapy, light delivered to the skin activates poφhyrin molecules. These activated molecules transfer their energy to form cytotoxic singlet oxygen leading to lethal alteration of cellular membranes and subsequent tissue destmction. In UNB therapy, UNB light is administered alone or with ointments containing coal tar, anthralin, or salicylic acid. UVA light is administered with psoralen In the third step of therapeutic regimens for psoriasis, systemic agents are administered to those cases refractory to the previously described first two steps These compounds include retinoids, methotrexate, hydroxyurea, cyclosponn, azthiopnne, 5-fluorouracil, cyclophosphamide, vinblastine, dapsone, and sulfasalazme. Limitations of Current Therapies for Psoriasis The mam limitation of the cunent therapies for psonasis is that the dmgs are only efficacious duπng the administration. Further, peπods of remission and outbreaks are difficult to impossible to predict. It has been shown that patients must rotate their treatments to retain efficacy. This can lead to missed schedules and requires patient education. Lastly, for all the listed therapies there is unreliable efficacy in their ability to stop proliferation and inflammation of the lesions. Toxicities of the cunent therapies include the following: phototherapy can lead to other skin lesions and sunburn. Cytotoxic agents used as immunosuppresive agents including methotrexate, 5-fluorouracil, cyclophospahmide, and vinblastine have associated side effects including hepatic compromise including hepatic fibrosis, ascites, esopageal varices, cinhosis, pneumonitis, myelosuppression, (cyclosporine: renal insuffienciency anemia, hypertension). A gene, genes, or gene pathway involved in the etiology of psoriasis or associated disorders or potential sites for targeted dmg therapy of psoriasis are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development for the treatment of psoriasis are listed in Table 45. G. Atherosclerosis Description and Potential Intervention of Atherosclerosis Atherosclerosis is a complex combination of hyperhpidemia, injury to the endothelium, and inflammation. The interaction of these multiple processes in association with local genetic and hemodynamic influences may promote the formation of atheromatous plaques as a reparative response of the arterial wall. Atherosclerotic plaques are composed of thrombogenic lipid— rich core protected by a fibrous cap comprising smooth muscle cells and inflammatory cells. The inflammatory cells are predominantly macrophages. As atherosclerotic plagues build blood flow is reduced creating ischemia in tissues down stream from the area of the plaque. In another model, the stenosis created by the plaques may be a part of the resulting ischemic event. Frequently, less obstmctive but more vulnerable plaques occur which are characterized by a thinned fibrous cap, marked lipid accumulation, a large number of macrophages, and a smaller amount of smooth muscle cells. It has been proposed that since these plaques are more prone to rupture creating contact with the highly thrombogenic materials of the lipid-rich nucleus of these lesions, thrombosis is stimulated. Advanced atherosclerotic lesions are caused by a series of cellular and molecular events involving replication of smooth muscle cells and macrophages on the vessel wall. The interaction of these cells with the T lymphocytes can lead to a fibφroliferative response. Large amounts of connective tissue produced by these smooth muscle cells consist of macrophages, T lymphocytes, smooth muscle cells, connective tissue, necrotic residues, and varying amounts of lipids and lipoproteins. Endothelial cells maintain the vessel surface in a non-thrombogenic state, preventing platelet and leukocyte adhesion, and act in maintaining the vascular tonus by releasing nitric oxide, prostaglandin, and endothelin. These cells also produce growth factors, cytokines, and chemokines to maintain the integrity of the collagen- and proteoglycan-rich basement membrane. Changes in some of these functions may trigger cell interactions with monocytes, platelets, smooth muscle cells, and lymphocytes. Hyperhpidemia and hypercholesterolemia are sufficient to induce dysfunction of the endothelial modulation of the vasoactive reactions and arteriolar tonus. The inflammatory mechanisms involved in the initial events or atherosclerosis are classic components of a specialized type of chronic inflammatory response that precedes the migration and proliferation of smooth muscle cells of the vessel wall. The foramtion and accumulation of foam cells in the intima leads to the first stage of the atherosclerotic lesion. In this stage, the accumulation of fatty straie consisting of a mixture of macrophages, lipids, and T lymphocytes representing a a purely inflammatory response. If the stimulating agent is maintained, i.e. hyperhpidemia, hypercholesterolemia, or other risk factor, then the protective inflammmatory response will also persist and themay become deleterious to the cells lining the arterial wall. This condition may lead to an intermediate lesion that may contain multiple smooth muscle cell layers, macrophages, and T lymphocytes. A fibrous capsule is formed covering the contents of the lesion. There is evidence to suggest that the inflammatory process and specific immune mechanisms are involved in athergenesis. At sites close to the plaque pture, inflammatory processes are observed resulting from T cell-dependent autoimmune response. This may lead to an inflammatory reactions participating in the destabilization of the fibrous cap. Immunoglobulins, T lymphocytes, and macrophages are found in the plaques. B lymphocytes and plasmocytes amy aslo be detected in the adventitia adjacent to the plaques. Autoimmune reactions against the oxidized lipoproteins have been observed. The macrophages are transformed into foam cells and in the presence of LDL, form immunocomplexes with the LDL by Fc fragments of the immunoglublins. These LDL immunocomplexes can induce numerous metabolic and functional changes iwhich can directly or indirectly damage the endothelial cells leading to the progressin of the atherosclerotic lesion. Despite the evidence of the involvement of the immune system in atherogenesis, the complexity of the immune reactions and response impairs the clarification of the involvement of these machanisms at the various stages of athersclerosis. The sequence of immune response event suggests an initial mechanism to respond to injury. However, this protective inflammatory response in the presence of persistant stimulus and the formation of a fibroprliferative response can be amplified. Attempts to modify the specific cell interactions with growth factor mediators or intracellular signalling molecules has provided a window to the potential prevention or regression of the lesions. A gene, genes, or gene pathway involved in the etiology of athersclerosis or associated disorders or potential sites for targeted dmg therapy of athersclerosis are depicted in Table 9 with the specific gene list in Table 4. Cunent candidate therapeutic interventions in development for the treatment of athersclerosis are listed in Table 46. Endocrine and Metabolic Disease Included in the description below are endocrinologic and/or metabolic diseases, disorders, or syndromes. They include diabetes, diabetes insipidus, obesity, contraception (not a disease but a common reason for taking steroid dmgs), infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction. Application of the methods of this invention to these diseases is described. A. Diabetes Mellitus Carbohydrate metabolism in mammals is controlled by a unique inteφlay of hormones, neurotransmitters, and other physiological influences to ensure a constant supply of metabolic fuel is available to the tissues. The two main hormones that regulate carbohydrate balance are insulin and glucagon. Both hormones are produced in the pancreas; β-cells produce insulin, α-cells produce glucagon. Insulin in the fuel excess state stimulates storage of the available metabolic precursors into glycogen and lipids; glucagon in the fuel deficient state stimulates the movement of the fuel stores to available metabolic precursors. When regulation of insulin or glucagon is abnormal there are pathologic changes. Type II Diabetes (Diabetes Mellitus; DM) is a heterogeneous disorder of carbohydrate metabolism characterized by absolute or relative insulin deficiency alone or in combination with insulin resistance (sensitivity). DM is associate with hyperglycemia and consequent polyuria and polydipsia. There are two forms of the disease, insulin-dependent diabetes mellitus (IDDM) which accounts for approximately 10% > of the DM cases in the United States, and non-insulin-dependent diabetes mellitus (NTDDM) which accounts for the remaining diagnosed cases. The incidence rate for all cases of DM in the U.S. is approximately 440 per 100,000. Type I (juvenile onset) diabetics produce little or no insulin and may be severely hyperglycemic if untreated. They are entirely dependent on exogenous insulin administration.. NIDDM (maturity or adult onset, nonketotic DM) patients retain significant capacity to secrete insulin, do not exhibit ketosis, and are not dependent on exogenous insulin for immediate survival. Within the pancreas, the β-islets cells are lost, stop producing or secreting insulin in patients with IDDM, but remain functional in patients with early stage NIDDM. In both cases of DM, glucagon opposes the effect of insulin on the liver by stimulating glycogenolysis and gluconeogenesis, but glucagon has little if no effect on the peripheral utilization of glucose. In the diabetic patient with insulin deficiency or insulin resistance and hyperglucagonemia, there is an increase in hepatic glucose production, a decrease of peripheral glucose uptake, and a decrease in the conversion of glucose to glycogen in the liver. Broadly, the physiologic changes stimulated by insulin, the primary hormone responsible for specific uptake of glucose from the periphery to tissues, is to increase the available storage of glucose into glycogen stores. In the liver, insulin stimulates the uptake and storage of glucose as glycogen, and inhibits hepatic gluconeogenesis and glycogenolysis. In skeletal muscle, insulin stimulates glucose uptake and storage as glycogen and amino acids in protein and inhibits release of gluconeogenic precursors (e.g., alanine, lactate and pyruvate) to the hepatic circulation. In adipose tissue, insulin stimulates the glucose uptake and metabolism to glycerol (the backbone of triglycerides for storage in fat droplets) and inhibits the flow of gluconeogenic precursors to the hepatic circulation, e.g. glycerol and nonesterified fatty acids. Insulin inhibits the breakdown of triglycerides, glycogen, protein and the conversion of amino acids to glucose (gluconeogenesis). In the intracellular process of storage of glucose as glycogen in the liver, insulin stimulates the glycogen synthase complex and inhibits glycogenolysis. However, in the insulin deficient or insulin resistant patient, glycogen stores are depleted and replaced with stores of ketone bodies (see below). In the intracellular process of storage of amino acids in muscle as protein, insulin stimulates the production of amino acids and their incoφoration into protein. In the absence of insulin, the amino acids stored in the muscle or other tissues, protein manufacture is reduced, and all available amino acids are metabolized to pyruvate, oxaloacetate, and β-ketoglutarate. The pyruvate can be converted to acetyl-CoA which can be further metabolized to acetoacetate, free fatty acid-CoA, or enter the cholesterol synthetic pathway via HMG CoA. In this case, there is production of ketones, fatty acids, and cholesterol. In the intracellular process of storage of metabolic fuel within the adipose tissue, insulin stimulates lipoprotein lipase. Lipoprotein lipase is synthesized primarily in fat and muscle, and when secreted into the extracellular space, the enzyme is associated with the surface of endothelial cells. Lipoprotein lipase hydrolyzes free fatty acids from triglyceride-rich lipoproteins (i.e. chylomicrons, very low density lipoproteins). Free fatty acids liberated from the lipoproteins are then taken up by adipose tissue, esterified into triglycerides for storage in fat droplets or adipocytes. Insulin stimulates the synthesis and secretion of lipoprotein lipase, inhibits lipolysis of triglycerides stored in adipose tissue, and promotes glucose uptake into the fat stores to provide a glycerol substrate within the adipocytes for esterification of the fatty acids. In cases whereby there is limited insulin supply or responsivity, there is an enhanced production of free fatty acids. The excess of free fatty acids stimulates the production of ketones (β-hydroxybutyrate, acetoacetate) and the release of ATP. Diabetic ketoacidosis (DKA) describes a clinical situation whereby there is a severe elevation of ketones in the tissues and peripheral circulation with concomitant hyperglycemia. In hepatocytes, mitochondria produce ketone bodies, which form as the result of β -oxidation of fatty acids. Glucagon further stimulates the hepatic ketogenic state; glucagon lowers malonyl coenzyme A levels (the first enzymatic step in the production of fatty acids) which in -urn stimulates the activity of camitine acyltransferase I, an enzyme the translocates fatty acids from cytosolic to intramitochondrial spaces. The fatty acids once in the mitochondria are converted in the absence of glucose to ketones. The production of excess ketones in DKA is uncontrolled; normally insulin stimulates the ketoacid tissue uptake and the high concentration of ketones themselves saturates tissue uptake. However, in DKA, the only resultant mechanism to remove or excrete excess ketones is via the kidneys. Hyperketonuria causes osmotic diuresis, which in turn causes intravascular volume depletion and dehydration, leading to urinary electrolyte loss. The hyperosmolorarity exaggerates the intracellular dehydration. The hallmark of NIDDM is peripheral tissue insulin resistance. The characteristic post-insulin receptor defect has been difficult to target therapeutically, however, there are working hypotheses to be exploited during dmg development. One theory to explain the how insulin resistance comes about is the single gateway theory. In the liver, it is thought that insulin is acting not directly on the hepatocytes, but through an indirect means. In this theory, insulin resistant fat cells over produce free fatty acids. It is the free fatty acids that circulate to the liver, muscle, and others tissues to mediate insulin resistance by a yet unknown mechanism of action. Another explanation of insulin resistance is free fatty acid response within adipose tissue. In this theory, free fatty acids stimulate the adipocyte production of TNFα and TNFα creates insulin resistance locally and distally within other peπpheral tissues. It is thought that TNFα mediates insulin resistance within adipose tissues by stimulating de-differentiation by inhibiting peroxisome prohferator receptor-γ (PPR-γ) and CAAT-enhancer binding protein α (CEBPα) while activating serine-threonine phosphorylation via the MAP kinase cascade. TNFα has been shown to stimulate lipolysis. Further, TNFα stimulates apoptotic signals by activating capases Withm the skeletal muscle TNFα inhibits insulin stimulated glucose uptake, and directly affects the insulin signaling pathway; it stimulates phosphorylation of the IRS-1 ; and inhibits PPR-γ and CEBPα. An example of the importance of TNFα on the mediation of insulin resistance are recent studies in adipocyte macrophages whereby it has been shown that TNFα has a direct effect on macrophages metabolism (a shift from glucose utilization to free fatty acid production) and a direct effect on PPR-γ and CEBPα. Type II DM is associated with metabolic syndrome X, also refened to as insulin resistance syndrome, or metabolic syndrome. This syndrome is characterized by hypertriglycendemia, low serum high density lipoprotein (HDL) and cholesterol, hypertension, central obesity, defective fibrinolysis, and artherosclerosis. Syndrome X, "the deadly quartet" of obesity, NIDDM, hypertension, and dyslipidemia are common metabolic disorders that have been shown to predispose the patient to early cardiovascular disease, including but not limited to coronary artery disease, heart failure, or congestive heart failure. In these cases, the pancreatic β-cells produce insulin, but the peripheral tissues are physiologically unresponsive to insulin. Thus, the mechanisms of insulin deficiency are active and the resultant hyperglycemia, hyperhpidemia, and others described are present. Clinically, the patient exhibits the signs and symptoms of NIDDM, and unfortunately few therapeutic alternatives are available. Table 50 lists the cunent candidate therapeutic interventions that are in development for the treatment of IDDM and NIDDM. Metabolic Syndrome X- It is well known that individuals who are diagnosed with metabolic syndrome X progress to a diagnosis of IDDM. One explanation of the transition of insulin independent to insulin dependent DM is that the overactive, uncontrolled pancreatic β-cells in NEDDM may generate oxygen free radicals that are deletenous to the β-cells and they undergo apoptosis. Another theory that may explain the loss of β-cells is that free fatty acids produced in adipose, hepatic, and other tissues may compromise the activity of the functioning pancreatic β-cells and ultimately leads to β-cell apoptosis and death. Lastly, the overexpression of TNFα within adipose tissue may activate apoptotic signals within the pancreatic β-cells. Therefore, in cases of NIDDM, it is clinically advantageous to blunt the progression of the disease to syndrome X. Therapeutic alternatives to treat NIDDM are as follows: 1) diet modifications that are aimed at lowering the daily intake of glucose (carbohydrates) and lipids; 2) low doses of exogenous insulin can be used to inhibit the patient's production and secretion of insulin from the pancreatic b- cells; 3) oral hypoglycemic agents, e.g. sulfonylureas (first and second generations), biguanides, thiazolidinediones, and α-glucosidase inhibitors. Once in syndrome X, there are many other therapeutic alternatives that are added to the regimen to treat the "deadly quartet" as described above. Novel therapeutic alternatives are required to be developed to meet the need of the population of NIDDM as well as those individuals in which progression to syndrome X has occuned. Table 56 lists the current candidate therapeutic interventions in development for the treatment of one or more of the deadly quartet that is part of metabolic syndrome X. Many human primary and metastatic tumors express critical proteins required for the maintenance of growth and dedifferentiation along with proteins that may inhibit growth or enhance terminal differentiation. For example, breast adenocarcinomas express at significant levels peroxisome prohferator activated receptor gamma (PPARγ), that when activated by a specific ligand, will induce terminal differentiation of malignant breast epithelial cells. Although, specific activators of PPARγ have been developed for the treatment of NIDDM, the antiproliferative and terminal differentiation effect may be exploited for the development of anti-neoplastic agents. Further, agents affecting the PPARγ pathway may be desirable candidate therapeutic interventions for cancer and DM. Cunent candidate therapeutic interventions for the treatment of cancer are listed in Table 24. Besides metabolic syndrome X, there are other chronic late complications of IDDM and NIDDM including retinopathy (proliferative and nonproliferative), nephropathy, neuropathy (including symmetric distal polyneuropathy, asymetric neuropathy, cranial mononeuropathy and mononeuropathy multiplex), peripheral mononeuropathy and, neuromuscular syndromes and autonomic neuropathy, cardiovascular disease, and skin ulcers due to vascular disease. In cases with loss of sensation in the extremities, there is a predisposition to repeated and undetected trauma. Diabetics are also at increased risk for cardiovascular disease. These complications are only partially reduced by achieving tight control of blood glucose levels. B. Diabetes Insipidus The polyuric syndrome in which there is a dysfunction in the antidiuretic hormone (ADH, often refened to as vasopressin (AVP)) signalling pathway, with an loss of ADH activity, and is termed diabetes insipidus (DI). Since ADH is responsible for the appropriate concentration and water conservation in the body, clinical manifestations of this disorder include: polyuria, near-continuous thirst, nocturia, hypertonic encephalopathy, circulatory collapse, and hypernatremia. These symptoms can lead to life-theatening syndromes. In DI, there is a vasopressinergic deficiency or the target organs are unresponsive to ADH (nephrogenic diabetes insipidus). The etiology of the disorder includes disease processes of the supraoptic nuclei, paraventricular nuclei, the hypothalamohypophysial tract, or the pituitary gland. Although 30% > of the cases are attributed to neoplastic lesions of the hypothalamus, 30% are post-traumatic, and 30%) are idiopathic, with the remaining 10% beign attributed to vascular lesions, infections, systemic diseases such as sarcoidosis that affect the hypothalamic function, and mutations in the ADH gene preprohormone processing pathway. Treatment of DI depends on the level and extent of the vasopressinergic deficiency. In cases, restoration of fluid balance and control of dehydration is paramount. In some cases of partial loss of ADH, relief of symptoms can be attained through the use of vasopressinergic agonists, candidate therapeutic interventions that enhance vasopressin secretion (e.g. clofibrate), or agents that increase the renal response to vasopressin (e.g. chloφropamide). In cases of nephrogenic DI, there is an inability of the renal cells to respond to vasopressin. In one form of this condition, there is congenital defects of the vasopressinergic receptor V2, preventing the ADH stimulation of adenylate cylcase and is an X-linked autosomal dominant genentic condition. In another form of nephrogenic DI, there are mutations in the autsomal gene for aquaporin-2 which produce a nonfunctional versions of this water channel. Although DI is more common, hypersecretion or over-activity of the ADH pathway leads to a syndrome termed inappropriate hypersecretion of ADH (SIADH). In this syndrome there is profound hyponatremia. This syndrome can occur in patients with cerebral disease (cerebral salt wasting) or pulmonary disease (pulmonary salt wasting), in some cases whereby a tumor is hypersecreting vasopressin, or in the absence of complicating disease. In these cases, patients with inappropriate hypersecretion or vasopressin can be successfully treated with agents or candidate therapeutic interventions that interrupt the vasopressinergic signal, for example, meclocycline, an antibiotic that reduces the renal response to vasopressin. C. Obesity According to a commonly accepted definition, obesity refers to a condition by which more than 20% or 25% of body weight is due to fat in men and women, respectively. Another, more reliable, index of fat distribution is the body mass index (BMI) which is calculated as the body weight divided by the square of the height (normal range being 20-25 kg/m " ). Obesity is a serious illness that can lead to many complications including hypertension, diabetes, cancer, degenerative arthritis, elevated cholesterol, gallstones or inhibited bile secretion, heart attacks and other cardiovascular disease, strokes, sleep disorders, and psychiatric illnesses including anxiety and depression. There is a strong genetic component to obesity, as well as strong conelations between obesity and socioeconomic status. Tables 5 and 10 lists the possible genes and gene pathways involved in the manifestation of obesity. Specifically, there are two gene pathways that may be associated with a genetic predisposition to obesity, they are leptin and its receptor, and peroxisome-proliferator-activated receptor γ2 (PPARγ2). In the first, the lipostatic hypothesis of obesity achieved prominence for a potential mechanism of inordinate eating. It was determined in mice lacking a specific gene, the ob gene, did not become sated after eating and ultimately became obese and diabetic. The product of this gene is a 167 amino acid protein called leptin. Leptin acts as a hormone to reduce food intake and increase energy consumption. The leptin recetor is encoded by the db gene. Mice lacking the db gene are also obese, but have high levels of circulating leptin. The leptin receptor is found in two forms, the short and long form which are the result of alternative splicing. The long form is found in the hypothalamus. The mechanism of leptin and leptin receptor dysfunction creating obesity is thought to occur by (i) interfering with the transport of leptin into the ENDOCRINE AND METABOLIC, (ii) impairing leptin receptor signal transduction, (iii) impairing downstream mediators of leptin action, or (iv) causing obesity by a leptin- independent mechanism - for example a mechanism that originates downstream of leptin or that bypasses leptin. Each of these hypotheses invokes a set of candidate genes (with considerable overlap) and implies up or down variation in allele function. The genes with potential affect on leptin and leptin associated activity are leptin receptor (OB-R), melanocortin 4-receptor (MC4-R), pro-opiomelanocortin (POMC; the precursor of α-melanocyte stimulating hormone), and prohormone convertase 1 (PCI). Two lines of evidence suggest that variation in these genes may affect leptin resistance. First, each gene has been strongly implicated in the leptin signaling pathway by in vitro data. Specifically, PCI participates in the processing of the prohormone POMC to the α-melanocyte stimulating hormone (α-MSH), which signals decreased food intake in response to leptin. This signal is transmitted through MC4-R, the receptor for α-MSH. Second, mutations in each of these genes have been associated with obesity in humans and, except PC I, in rodents as well. Leptin signaling could be affected by polymoφhisms that affect protein levels or function. Futhermore, there may be polymoφhisms in the promoters of all four genes as well as the genomic locus of the leptin receptor and three genes implicated in the signal transduction pathway immediately downstream of the leptin receptor. Other genes involved in the leptin signal include Neuropeptide Y. Each gene in this set has the potential to modulate the biological function of leptin. Neuropeptide Y, which stimulates food intake through the Yl and Y5 receptors (and possibly others), is inhibited by leptin. Agouti-related protein inhibits MC4-R signaling and is also down-regulated by leptin. Like NPY, the melanin- concentrating hormone has been shown to stimulate feeding. These genes differ from those above in that mutations have not been associated with obesity in humans (although mutations in the neuropeptide Yl receptor and the agouti -related protein have been associated with obesity in rodents). With the exception of neuropeptide Y (NPY), where the coding region (but not genomic or promoter sequence) has been screened for polymoφhism. these genes have not been studied extensively for variation in humans. In the second gene pathway associated with obesity, PPAR-γ2, is a transcription factor (described above and in Example 1 ) and has been demonstrated to be a key regulator of adipocyte differentiation and energy stroage. PPAR-γ2 is involved in the direction of differentiation of preadipocytes to adipocytes. In in vitro studies, over expression of PPAR-γ2 leads the fibroblast cells to differentiate to adipocytes. Furthermore, phosphorylation of PPAR-γ2 at a serine residue at position 1 14 reduces differentiation process mediated by PPAR-γ2. This serine is contained within a mitogen acitvated protein kinase or related kinase, indicating an intracellular mechanism for the regulated control of adipocyte differentiation. In a recent study, it was determined that 4 of 121 obese subjects were identified as harboring a substitution of proline to a glutamine at amino acid position 115 as compared to none of the normal subjects having the substitution (Ristow et al, NEJM 339(14):953-959). Since the amino acid at position 1 15 is near to the serine phosphorylation site at 1 14, it is sugestive that such a substitution can be predisposing to abenant PPAR-γ2 activity. Other genes that be involved in the genetic differences in obese versus normal weight subjects include signaling genes based on two observations. First, although no human or rodent models are available to assess the affect of mutation on body mass, it has been shown that JAK2 and STAT3 knockouts are embryonic lethals. This would seem to indicate functions beyond regulation of body mass. Second, there is considerable redundancy in most signal transduction pathways, and there may be compensatory mechanisms to overcome any effects of polymoφhism in JAK2 or STAT. As depicted in Table 51 , there are many new candidate therapeutic interventions in development. The targets include galanin, β3-adrenergic receptor, neuropeptide Y, corticotropin releasing factor, and the cholecystokinin receptors. D. Contraception The most widely used oral contraceptives are estrogens and progestins alone or in combination. These agents are taken by women each day to prevent ovulation. The combination therapies are either mono-, bi-, or triphasic which are named as such to indicate the level of estrogen in each of the tablets, i.e. monophasic has the same amount, biphasic has two different doses, and triphasic has three. Progestins are delivered in the same tablet, and the ratio of estrogen to progestin allows for a reduction in the overall amount of steroids delivered to the subject as well as more closely approximates the natural steroid ratio during a mentraal period. The phase delivery of steroids to women wishing to block ovulation has limited the untoward side-effects progestins have on the cardiovascular system. Unfortunately, although very effective, oral contraceptives are associated with undesirable side effects and toxicity. These effects falls into three categories: cardiovascular effects, cancer, and metabolic and endocrinologic effects. Cardiovascular effects seen in response to oral contraceptives include estrogen increasing semm HDL while lowering semm LDL and progestins decreasing HDL and increasing LDL. This inordinate and unregulated change in the lipoφotien balance in women can lead to hypertension. Estrogen is a growth promoting hormone, and the estrogen found in almost all of the oral contraceptives has been studied for effects on or risk of ovarian, cervical, endometiral, and breast cancer as well as hepatocellular adenoma in women. However, studies have not conclusively demonstrated an association of higher rates of these types of cancers in women that have used oral contraception. The metabolic and endocrine effects of oral contraceptives are increased fasting glucose levels, peripheral insulin resistance, higher incidence of gall bladder disease, and estrogen mediated increases of hepatic synthesis of semm proteins. There are other side effects and disease risk that are associated with oral contraceptives that include increased risk of thromboembolism, nausea, vomiting, dizziness, headaches, decreassed libido, visual disturbances, depression, and post- pill ammenorhea. However, there are beneficial effects of oral contraceptives that include reduction of pelvic inflammatory disease, lower incidence of iron deficient anemia, symprtomatic relief of endometriosis, improvement of acne and dysmenonhea, as well as decreasd risk to develop ectopic pregnancies, uterine fibroids, and ovarian cysts. Oral steroid contraceptives also interact with several other dmgs and such interactions can lead to loss of efficacy and include altered dmg absoφtion or metabolism. Any agent or compound that induces hepatic microsomal enzymes or reduces the absoφtion can alter the effectiveness of the oral contraceptives and these include certain antibiotics, anticonvulsants, or antacids. Furthermore, agents that oppose the therapuetic effects of the oral contraceptives include anticoagulants, antidiabetics, and certain antihypertensives (guanethidine, and α-methyldopa). There are other genes that one may conelate to candidate therapeutic responses or safety and these include: blockade of implantation, blockade of sperm penetration into the egg, or blockade of sperm production. As depicted in Table 52, there are many candidate therapeutic interventions that are cunently in development to be of therapeutic benefit in contraception. E. Infertility Infertility is the involuntary inability to concieve a child. Infertility is the result of one or more of the following functions for the male or female including 1 ) adequate production of normal motile sperm, 2) ejaculation of sperm through a patent ductal system, 3) the sperm must be able to traverse an unobstructed female reproductive tract, 4) the female must ovulate and release the ovum, 5) the sperm must be able to enter the ovum, 6) the fertilized ovum must be capable of developing and implanting in the appropriately prepared endometrium. Nearly 40% of the infertility cases, the male has a dysfunction or inadequate function. Couples experiencing infertility have alternatives to alter their reproductive capacity. Although many of the methods are mechanical and require a procedure, such as in vitro fertilization and sperm collection and concentraion, there are agents that help a female to ovulate, such as antiestrogens and gonadotropins. F. Hormonal insufficiency related to aging As individuals age, their androgen and estrogen levels decrease. In some cases, estrogen and androgen replacement therapy has been useful to replenish the deficiency and restore the steroid hormone stasis. In these cases, the deficiency may be the result of a loss of the receptor affinity for the ligand, loss of the receptor levels, reduction in the production of the steroids, or increased metabolic rates of these steroids. As the aging process continues, there may be a natural reduction in the function within the estrogen or androgen target tissues. G. Osteoporosis The condition in which there is bone matrix and mineral loss is termed osteoporosis. The loss of both of these components in bone results in the reduction of strength, and increased incidence of fractures and is characterized by a net excess loss of bone resoφtion over bone formation. Although there are multiple causes, the most common is involutional osteoporosis which is associated with advancing age and menopause. Osteoporosis can also occur as a result of long periods of immobilization, space flight, parathyroid hormone and vitamin D deficiency, as well as in patients with excess glucocorticoids (Cushing's syndrome, or adminstration of glucocortiocids for the therapy of autoimmune disease, transplantation, inflammatory diseases, arthiritis, asthma, Crohn's disease, atherosclerosis, or infections with potent inflammatory responses such as hepatitis). In osteoporosis accelerated normal bone loss can be reversed by estrogens. Estrogens inhibit the secretion of IL-1, IL-6, and TNFα. These cytokines enhance the production of osteoclasts, and in addition, estrogen inhibits the production of TGF-β which is thought to mediate the apoptotic signal within osteoclasts. Although estrogen can reverse bone loss in patients with osteoporosis, the doses of estrogen required are associated with higher risk of myocardial infarctions, stroke, breast and endometrial cancers. However, as described above (under Contraception), estrogen in lower doses and given with progestins can be of therapeutic benefit for osteoporosis and have a reduced toxicity profile. Table 53 lists the cunent candidate therapeutic interventions that are in development for osteoporosis. H. Acne The most common form of noninfectious pustular skin disease is acne. It is an an inflammatory skin condition affecting the the pilosebaceous units and therefore is predominantly found on the face and upper trunk. Several factors can play a role in the progression of acne including 1) androgenic stimulation of the sebaceous glands, and 2) abnormal keratinization and impaction in the pilosebaceous canals causing obstmction of the sebum flow, and 3) proliferation of anaerobic bacteria. Aggravating factors such as oil-based cosmetics, and certain dmgs (androgenic hormones, antiepileptics, progestins (as in oral contraceptives), systemic corticosteroids, and iodide and bromide containing agents. There are also endocrine conditions whereby there is a hypersecretion of androgen, e.g. polycystic ovarian disease, ovarian tumors, or enzymatic hyperactivity for the production of androgens or reduced metabolism of androgens. Treatment of acne is aimed at one or more of these three causes: topical agents that remove the comedomes such as benzoyl peroxide, topical vitamin A preparations enhancing flow of sebum to the surface, and oral 13-c/s-retinoic acid can decrease sebaceous gland secretion and gland size. Oral vitamin A preparations are known teratogens and should be avoided in patients who are or plan to become pregnant. Table 54 lists some cunent candidate therapeutic interventions in development for the treatment of acne and related skin disorders. I. Alopecia Under normal conditions, scalp hair grows between 10- 15mm each month. Under normal conditions, 80-85%> of hair follicles are in the growing anagen stage, and 15-20%) are in the dormant or telogen stage. There are multiple factors that affect the transition of the active to dormant stages and vice versa as well as factors that can affect the rate of growth and condition of hair, including physical, chemical, and emotional events. If severe conditions exists, hair growth can completely stop leading to local or wide spread hair loss. There are two types of hair loss, nonscarring (reversible) and scarring (ineversible). Nonscarring or localized hair loss includes alopecia areata, tinea capitis, trichotillomania, androgenic alopecia, or traction alopecia. Localized hair loss is characterized by well-circumscribed, round, or oval patches of nonscarring hair loss which ususally occurs on the scalp, eyelashes, or eyebrows. Patterns and location of hair loss can define whether there is a poor prognosis for return of hair growth. Alopecia areata may be autoimmune disease and is associated with cases of Hashimoto's thyroiditis. and pernicious anemia; alopecia areata is treated with glucocorticoid topical preparations. Tinea capitis is a an infection predominantly with Trichophyton tonsurans and is treated with griseofulvin. Trichotillomania is a disorder referring to traumatic, self-induced alopecia and usually results from persistent twisting, rubbing and pulling resulting in localized hair loss and is treated with emotional or psychiatric therapy. Androgenic alopecia is the familiar male pattern baldness that occurs slowly as a thinning of the hair shafts and eventual loss. Androgenic alopecia is genetically predetermined and is dependent on androgens. Traction alopecia occurs in subjects that over use or abuse hair styling, curling, or other traumatic devices or procedures that damage hair to the extent of hair loss. Hair loss can be further associated with secondary syphillis. Diffuse or generalized hair loss can occur as a result of a dismption of the normal hair growth cycle. In these cases, full loss of scalp hair may be caused by severe psychological or emotional stress, systemic illness, major surgery with general anesthesia, amphetamines, β-blockers, lithium, probenecid, pregnancy, or discontinuation of oral contraceptives. Dismption of the anagen phase via one or more of these hair growth toxicities may weaken the hair shaft and hair breaks easily. For example, cytotoxic cancer chemotherapeutic agents and radiotherapy to the scalp affect the anagen hair growth phase. Retinoids and hypervitaminosis interferes with the keratinization of the the hair shaft. Diffuse hair loss may occur in cases of hyperthyroidism and nutritional difficiency. Sebonheic dermititis appears as erythema and yellow greasy scales throughout the scalp may be associated with mild diffuse hair loss. Lastly, scarring alopecia may be the result of systemic lupu erythmatosus, discoid lupus erythmatosus, moφhea, and aplasis cutis. In all cases of alopecia, removal or cessation of trauma, agents or procedures that are damaging to the hair follicles or shafts is the first line of therapy. Further, glucocorticoids topical agents can be used to reduce inflammatory or autoimmune components of the localized or diffuse hair loss. Topical Minoxidil, for the treatment of male pattern baldness, has shown to effective in only 30% of the cases. The androgen receptor is encoded by a gene that is known to have a region of polyglutamine repeats (encoded by CAG repeats) in the amino terminal that is responsible for transcriptional activation. In humans, the number of these CAG repeats is polymoφhic. Since androgens can be important in acne, hirsutism, and androgenetic alopecia (AGA), a recent study set out to determine whether these polymorophic repeats were associated with the signs and symptoms of these clinical disorders (Sawaya and Shalita, J Cutan Med Surg 3(1 ):9-15, 1998). The investigators found that normal subjects had a mean of 22 + 4 (n=48) and 21 + 3. (n=60) CAG repeats in this region of their androgen receptor for men and women, respectively. In contrast, men with AGA had 19 + 3 and women with AGA had 17 + 3 CAG repeats. These data are suggestive that CAG repeat length found in a physiologic relevant site in the androgen receptor may be indicative of the role androgens play bin the mediation of adrogenentic alopecia. Table 55 lists the cunent agents, dmgs, or candidate therapeutic interventions that are in development of the therapy of alopecia. J. Adrenal dysfunction The major function of the adrenal cortex is to produce glucocorticoids (cortisol) and mineralocorticoids (aldosterone). Either an excess or deficiency in adrenal cortical hormones can have major physiologic effects. Cortisol is responsible for the regulation of carbohydrate metabolism, intermediate metabolism, hemodynamic functions, and developmental processes. Excess cortisol is termed Cushing's disease and cortisol deficiency is termed Addison's disease. Aldosterone is a hormone primarily involved in the regulation sodium, potassium, and hydrogen ion balance and secondarily in the regulation of blood pressure. Hyperaldosteronism or hypoaldosteromsm are the terms for excess or deficiency of aldosterone. Besides cortisol and aldosterone, there are many other steroids produced in the adrenal cortex; in females the adrenal cortex is the major source of androgens. The biosynthetic steps for the production of steroids compounds in the adrenal cortex proceeds via a series of enzymatic steps, the first molecule to enter the cycle is cholesterol, intermediates steroids (including DHEA sulfate, 17a-OH- progesterone, 1 1-deoxycortisone, testosterone, androstenediones, deoxycortisols, corticosterones), and final products estradiol-17β(E 2 ), estrone (Ei), cortisol, and aldosterone. Under normal condtions, cortisol is the major end-product with aldosterone next, and very little estradiol or estrone. Adrenal cortical steroids are secreted in repsonse to adrenocorticotropic hormone that is secreted from the pituitary in response to stimulation by corticotropm releasing hormone secreted by the hypothalamus. There is a negative feed back loop, in that cortisol inhibits the secretion of ACTH and CRH at the pituitary and the hypothalamus, as well as somatostatin acting in the same manner as cortisol to attnetuate secretion of the hypothalamus and pituitary hormones. Once secreted, cortisol is approximately 90-93% bound by plasma proteins; albumin and the major protein being corticosteroid binding protein (CBG, transcortin). CBG has a high affinity for cortisol and is not required for transport, nor cortisol function. CBG is produced in the liver and the concentrations found in plasma is genetically determined and is regulated by hormone levels. CBG levels are increased during certain physiological conditions including pregnancy, hyperthyroidism, diabetes, in excess estrogen, and during the administration of oral contraceptives. CBG levels can be low or deficient during periods of malnutrition, in liver disease, multiple myeloma, obesity, hypothyroidism, and part of the nephrotic syndrome. In cases whereby there is an increase or decrease in the levels of CBG, bound cortisol levels increase or decrease, respectively, however there is a constant level of free cortisol. Mineralocorticoids, once secreted, are approximately 60% bound to plasma albumin. Nearly 99% of the adrenal cortical steroids are metabolized prior to excretion. Thus, any defect or dysfunction in the enzymes involved or in the metabolic rates can result in elevated levels of cortisol or active metabolites. Further, metabolic enzymatic reactions occur to ensure that products are sufficiently different to not elicit a biological effect in the metabolizing organ. For example, the 1 lβ-hydroxyl group of cortisol can be metabolized in the liver to the ketone form which is devoid of cortisol receptor binding activity. Conversely, cortisol in the kidney can be metabolized to cortisone which prevents cortisol from binding to the mineralocorticoid receptor in the kidney. Cortisol and aldosterone are cleared from the plasma with a half-lifes of 80-120 minutes and 15 minutes, respectively. The changes of metabolic rates can occur via 1) inhibitory influences of plasma binding on clearance rates, 2) enhanced metabolic enzymatic activity. The metabolism of these steroid hormones can be altered by: 1) decreased metabolism, or 2) increased metabolism. Glycyrrhetinic acid, present in licorice, and carbenoxolone block the 1 lβ-hydroxysteroid dehydrogenase activity and thereby prevent the conversion of cortisol to cortisone. Thus alterations as described above can lead to enhanced or decreased adrenal cortical steroid hormone activity and physiologic response. Nearly 80%> of the primary adrenocrotical insufficiency cases are due to autoimmune destmction of the adrenal cortical tissue. Autoimmune adrenocortical insufficiency has some genetic predisposition; 40% of the cases have first or second degree relatives with similar clinical patterns. Nearly all the cases of secondary adrenocortical insufficiency is the result of limited secretion of ACTH. Therapy of adrenocortical insufficiency is treated in the acute setting with intravenous soluble steroids and control of fluid and electrolyte balance. For the maintanence of cortisol levels, these patients are put on a schedule of cortisol administrations that mimic the normal physiologic circadian rhythm. Hypersecretion of cortisol is termed Cushing's syndrome may be caused by adenocortical tumors hypersecreting cortisol, conditions that increase ACTH secretion, and by prolonged administration of corticosteroids. This syndrome is characetized by a moon face, increaased fat pads, red cheeks, pedulous abdomen, abdominal striae, poor muscle development, poor wound healing, and bruisibility with ecchymoses. Therapy of Cushing's syndrome is dependent on the etiology of the disease. Adrenocortical and pituitary tumors can be surgically removed, however in each case dismption of normal glandular function must be avoided. Bilateral removal of adrenal glands can lead to Nelson's syndrome which is thought oto arise due to the loss of cortisol negative feedback on the pituitary gland. In the absence of tumors, dmgs may be used to limit the secretion of ACTH or cortisol thery include: reseφine, bromocriptine, cyproheptadine, and valproate sodium can be used to reduce the secretion of ACTH, however only a minority of patients respond. Ketoconazole inhibits cortisol secretion. Cortisol and the many synthetic congeners are the mainstay dmg or therapy for many inflammatory diseases, conditions, or disorders and in the transplantation setting. Corticosteroids affect the immune response by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. As well as providing antiinflammatory therapy, corticosteroids suppress immune function by inhibiting the activation of T cells. Steroids are highly effective in the early induction and maintenance regimens and are first line therapy in acute allograft rejection. Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus- pituitary axis, decreased thyroid hormone semm binding protiens, and impaired wound healing. Mineralocorticoid hypersecretion occurs due to adrenocortical adenoma, bilateral adrenocortical hypeφlasia, and adrenal carcinoma. Clinically, the symptoms include hypertension, suppression of plasma renin, hypokalemia and associated disorders or syndromes related to each of these dysfunctions. Therapy for these conditions usually entails uni- or bilateral surgical removal of the adrenal adenoma or hypeφlasia. In these cases, cortisol maintainence therapy is initiated as descrbed above. Mineralocorticoid hyposecretion is treated with supplemental mineralocortiocid therapy. K. Thyroid dysfunction The thyroid gland secretes thyroxine (3, 5, 3', 5'-tetraiodothyronine, T 4 ) and 3, 5, 3'-triiodothyronme (T 3 ). The prinicpal role for these two hormones is to regulate tissue metabolism and, in infants and young children, to regulate growth, development, and maturation of the nervous system and bone and joints. The enzymatic pathway for the generation of T and T 3 as well as the conversion of T 4 to T 3 (within the liver and the kidneys) are known and genes involved in these pathways are listed in Table 5. The regulation of thyroid hormone secretion is part of the hypothalamus- pituitary axis; by which thyroid releasing hormone (TRH, secreted from the hypothalamus) acts on the pituitary gland to secrete thyroid-stimulating hormone (TSH) that acts on the thyroid gland to stimulate the secretion of T 4 and T 3 . Somatostatin, and other neuropeptides or neurotransmitters regulate the thyroid gland secretion activity by inhibiting secretion of TSH at the level of the pituitary gland. T3 can directly suppress the the level of pro TRH mRNA in the paraventricular nucleus of the hypothalamus. Circulating thyroid hormones are bound to throxine-binding globulin, transthyretin, or albumin, which are involved in the transport of the thyroid hormones to their target tissues. The concentrations of these binding proteins change under various physiologic conditions and can affect the efficacy and tissue distribution of the thyroid hormones. These condidtions include 1) increased semm thyroid hormone binding proteins: pregnancy, exposure to supraphysiologic levels of estrogen, hepatic cinhosis or acute hepatitis, acute intermittent poφhyria, exposure to heroin or methadone, and clofibrate; 2) decreased semm thyroid hormone binding proteins: protein malnutrition, hepatic failure, chronic illness, nephrotic syndromes, exposure to L-asparaginase, congential abnormality (X-linked) of the binding protein genes, exposure to androgenic steroids of pharmacologic doses of glucocorticoids. The mechanism of action of T3 and T4 on the target tissues is thought to occur via thryroid hormone intracellular receptors that binds the hormone ligand and via a process of entry into the nuclear compartment, the hormone-receptor complex activates DNA transcription genes having a thyroid receptor response element in the promoter region. Dysfunction of thyroid hormone pathway is clinically expressed as either hyperthyroidism or hypothyroidism. In either case, there are multiple levels of possible or potential dusmptions of the thyroid hormone signalling pathway. Hyperthyroidism or Graves' disease is also termed thyroidtoxicosis and may be associated with catecholamine excess, toxic multinodular goiter, toxic adenoma, iodide-induced hyperthyroidism, subacute thyroiditis, factititious (exogenous) thyrotoxicosis, neonatal thyrotoxicosis (mother with Graves' disease), TSH- secreting pituitary tumors, nontumorigenic pituitary-induced hyperthyroidism, choriocarcinoma or hydatiform mole, stmma ovarii, and hyperfunctioning thyroid carcinoma. Clinically, symptoms include marked opthalmopathy (preorbital swelling, exophthalmos, limitation of extraocular movements, protmding eyes and easy tearing), pretibial mxyedema, tachycardia, elevated systolic blood pressure, and increased inotropic activity in the myocardium. Therapy of hyperthyroidism follows two stages, 1 ) reestablishment of the euthyroidism, and 2) induction of a permanent alteration of thyroid function. In the first, reduction of elevated thyroid hormone secretion can be achieved by adminstration of thiourea derivatives (for example, propylthiouracil, methimazole, carbimazole). These agents inhibit the organification of iodine within the thyroid gland and suppress the production of the thyroid hormones. Side effects of these thiourea compounds include maculopapular rash, hepatocellular damage, agranulocytosis, and vasculitis. Other compounds used for the acute therapy of hyperthyroidism include lithium, iopanoic acid, and iopadate. In the second stage of therapy for hyperthyroidism, long-term therapy of propylthiouracil may induce remission of the hypersecretion. If remission is not attained, surgical removal of the thyroid gland, or treatment with 131 I. Unfortunately, radical therapies to remove or ablate function of the thyroid gland can lead to hypothyroidism. In hypothyroidism, there is impaired secretion of the thyroid hormones. Hypothyroidism may be associated with acquired disease (Hashimoto's thyroiditis, idiopathic myxedema, 131 I radiotherapy, external radiation therapy to the neck area, subacute thyroiditis, cystinosis, impaired function of thyroid gland (iodine deficiency or excess, dmg induced (lithium carbonate, para-aminosalicyclic acid, thiourea dmgs, sulfonamides, phenylbutazone, and others)), congential genetic defects (biosynthetic enzymes for the thyroid hormones, thyroid agenesis, thyroid dysgenesis or ectopy, maternal iodide or antithyroid dmgs), hypothalamic dysfunctions (neoplasms, eosinophilic granuloma, therapeutic irradiation), or pituitary dysfunction (neoplasms, pituitary surgery or inadiation, idiopathic hypopituitarism, Sheenan's syndrome, exposure to supraphysiologic levels of dopamine). Clinically, symptoms include weakness, fatigue, lethargy; dry, coarse skin; swelling of the hands, face and extremities; cold intolerance and decreased sweating; modest weight gain; decreased memory; hearing impairment; arthalgia and paresthesias; constipation; and muscle cramps. In infants or young children in which hypothyroidism remains unchecked during the first two years of life, ineversible mental retardation as part of a syndrome called cretinism develops. Therapy of hypothyroidism includes the replacement of synthetic thyroid hormones, T 4 and T 3 . In these cases, hormone replacement therapy is sufficient to restore euthyroidism. Special cases of hypothyroidism, for example those individuals with angina and hypothyroidism require special monitoring since the replacement hormones may stimulate the myocardial oxygen demands in a myocardium that can not produce adequate myocardial blood flow. Another special case are patients with severe mxyedema coma, and event that may arise in patients with severe hypothyroidism and are subjected to additional physiologic stresses. Anthithyroid antibodies can be part of an autoimmune thyroid disease, such as Hashimoto's or Graves' disease. Patients may have semm antibodies formed to thyroid peroxidase (common), semm thyroglobulin, or to the TSH receptor. L. Parathyroid dysfunction Parathyroid hormone is secreted by the parathyroid glands. The hormone is responsible for the regulation of bone resoφtion and calcium mobilization. In addtion to increasing the the plasma Ca+ levels and depressing the plasma phosphate levels, parathyroid hormone increases the excretion of phosphate in the urine. In cases of pseudohypoparathyroidism, patients have normal circulating levels of parathyroid hormone, but lack the GTP-binding protein to allow hormone receptor-G-protein stimulated adenylate cyclase activity and subsequent increases in intracellular cAMP. In another form of pseudohypoparathyroidism, there is an adequate GTP-binding protein, but there is lacking the intracellular messeger system to allow parathyroid hormone mediated phosphaturic action of the hormone within the target tissues. In cases of parathyroidectomy, hypocalcemia, tetnus, and hypeφhophatemia occurs. Administration of parathyroid hormone can restore calcium and phosphate ion stasis. In cases of pararthyroid hormone excess, usually a result of inordinate administration of parathyroid hormone or a tumor hypersecretion of parathyroid hormone, the symptoms include hypercalcemia, hypophosphatemia, and demineralization of the bones, and the formation of calcium containing kidney stones. Removal of the tumor or adjustment of the parathyroid hormone adminstration schedule is the pmdent course of treatment. Secondary hypeφarathyroidism may be the result of chronic renal disease. In nearly 20% of cancer patients there is marked hypercalcemia as result of bone metastases that produce the hypercalcemia as a result of the eroding bone. The bone erosion may be the result of prostaglandin E and the tumor or cancerous cells. Further some cancers cells hypersecrete 1 ,25-dihydroxycholecalciferol, or another bone related hormones. In some cancers, there has been detected hypersecretion of parathyroid hormone-related protein. Tumors in this category include breast, kidney, ovary, and skin. Although the above description includes the hypothalamus-pituitary-target gland axes, there are other orgasn that have endocrine functions. These include the kidneys, the heart, and the pineal gland. The kidneys regulate blood pressure via the renin-angiotensin system. The kidneys produce and secrete renin (in the juxataglomerular apparatus), an acid protease that acts on angiotensinogen to form angiotensin I. The next enzyme in the pathway is angiotensin converting enzyme (ACE, located in the lungs and eslewhere) which converts angiotensin I to angiotensin II. Angiotensin II acts directly on vascular smooth muscle to to arteriolar constriction and leads to an increase in blood pressure, on the adrenal cortex to stimulate secretion of aldsoterone, and in the cerebral cortex to decrease the baroreflex potentiation g the pressor effects. Angiotensin II is metabolized by various peptidases (aminopeptidase) and is sequestered in vascular beds of tissues by as yet unknown molecule trapping mechanism. ACE, angiotensin and renin receptors, and regulation of renin secretion have proven excellent candidate targets for dmg intervention for the treatment of hypertension and other cardiovascular disease. Other likely candidates for the therapuetic intervention of the renin-angiotensin system are listed in Table 5 and Table 11. The kidneys, and to a lesser extent the liver, also produce and secrete erythropoeitin. In adults, erythropoietin is produced by the intersitial cells in the pεritubular capillary bed of the kidneys and the perivenous hepatocytes in the liver. Erythropoietin regulates the production of erythrocytes by stimultatmg the munber of erythropoetin-sensitive committed stem cells in the bone manow that are converted to precursors and ultimately to mature erythrocytes. When erythropoietin levels are low, erythroid stem cells show DNA cleavage followed by programmed cell death (apoptosis). Erythropoeitin reduces the DNA cleavage and stimulates the cells to survive. When the renal mass is reduced in adults by renal disease or nephrectomy, the resultant reduction in the production of erythropoietin, and the inability of the liver production to compensate for this reduction, leads to marked anemia. Synthetic or recombinant erythropoietin has proven to be theφauetically improtant to those individuals in end-stage renal disease and other anemic conditions such as cancer, trauma, surgery, and others. Other genes involved in the erythφoeitin pathway are listed in Table 5. The myocardium produces and secretes atrial natriuretic peptide (ANP). ANP produces natriuresis, in part by stimulating an increase in glomular filtration rate, promotes tubule secretion of sodium, and lowers blood pressure by acting directly on the vascular smooth muscle cells and descreasin rhe responsiveness to pressor substances. In the brain, ANP actions are opposite of those directed by angiotensin II. ANP is metabolized by neutral endopeptidase (inhibited by thioφhan) and has a short half-life. The other endocrine hormone involved in natmiresis is produced and secreted form the adrenal glands and is termed the Na+/K+ ATPase inhibiting factor. This factor produces natmireses by inhibiting the Na+/K+ ATPase and produces an increase in bloo pressure. The pineal gland produces and secretes melatonin. In humans, melatonin is produced and secreted during the dark periods of the day and is maintained at lower concentrations during the daylight hours. Melatonin has been implicated in inducing and maintaining sleep. Melatonin is synthesized from serotonin via two enzymes found in the pineal paremchymal cells. Melatonin is secreted via a neural stimulation to the pineal gland. β-Adrenergic stimulation to the pineal gland results in increased stimulation of the porduction and screretino of melatonin. Metabolism of melatonin occurs via 6-hydorxylation followed by conjugation in the liver and is predominantly excreted in the urine. Cardiovascular and Renal Disease There are some examples whereby there is no direct evidence that a gene or genes are involved in dmg response of a candidate therapeutic intervention. In these cases, however, there is genetic data supporting a role of a variance or variances involved in the etiology, progression, or risk of a cardiovascular or renal disease. These cases, including but excluded to are described below with details of cunent therapies and potential genetic involvment of variances in dmg responses. A. Anemia Anemia is a condition in which the number of red blood cells per cubic mm, the amount of hemoglobin in 100 ml of blood, and the volume of packed red cells per 100 ml of blood are less than normal values. Anemia may be clinically manifested as pallor of the skin and mucus membranes, shortness of breath, palpitations of the heart, soft systolic murmurs, shortness of breath, lethargy, and fatigability or other signs and symptoms. Anemia can be caused by three broad defects 1) bone marrow failure, 2) acute blood loss, and 3) hemolysis, however, anemia may be the result of one or more of these three. Anemia is a common manifestation of many different chronic or acute diseases, toxins, therapeutic dmgs, nutritional status, endocrine disorders, congenital conditions, autoimmune conditions, alcohol, dmg, or substance abuse, trauma, surgery, or any other condition that affects the function or status of the bone manow, blood volume, or erythrocytes. When anemia develops, there are compensatory physiological mechanisms that are available to attempt to restore tissue oxygenation including increases in the erythrocyte glycolytic intermediate 2,3-diphosphoglycerate (2,3- DPG; binds to hemoglobin and decreases the oxygen binding affinity) in erythrocytes, increased peripheral dilation, increased cardiac stroke volume, decrease in blood pressure, or other mechanisms. Anemia may be due to dmg toxicities. Aplastic anemia or hematologic blood disorders may also be due to a proliferative defect and related bone manow failure syndromes. Anemia due to bone manow failure usually results in changes in mean cell volume (MCV) can be categorized as normocytic, microcytic, and macrocytic anemia. Normocytic bone manow failure can be the result of iron deficiency, chronic disease, renal failure, liver disease, endocrine disorders, aplasia, myelodysplasias, myelofibrosis, hematologic or solid tumors, granulomas, human immunodeficiency vims (HIV) infection, and others. Microcytic bone manow failure can be the result of iron deficiency, chronic disease, thalassemias, aluminum toxicity, thyrotoxicosis, hereditary sideroblastic conditions and others. Macrocytic bone manow failure can be the result of megaloblastic conditions (cobalamin and folate deficiencies, and congenital disorders), alcoholism, dmgs, liver disease, aplasia, myelodysplasias, myelofibrosis, hematologica or solid tumors, granulomas, human immunodeficiency vims (HIV) infection, hypothyroidism, splenectomy, and others. Hemolytic anemia primarily due to the destmction of red cells can be the result of congenital conditions (enzyme deficiency, membrane skeletal protein abnormalities, hemoglobinopathies) or acquired conditions (antibody-induced, mechanical fragmentation, and membrane protein anchoring abnormalities). Acute blood loss occurring in trauma, surgery, or acute or chronic disease can lead to excessive blood loss. Dmgs or other agents known to cause anemia include cancer chemotherapeutic agents (antimetabolites, alkylating agents, hydroxyurea, cytosine arabinoside and others), anti-inflammatory agents (aspirin, non-steroid anti- inflammatory agents, phenylbutazone, gold compounds), antibiotics (chloramphenicol, penicillin, cephalosporins, sulfonamides and others), anticonvulsants (phenytoin and others), dihydrofolate reductase inhibitors (methotrexate, pyrimethamine, trimethoprim, triamterene, pentamidene, and others), antiviral agents (zidovudine and others), immunosuppressive agents (azathioprim and others), antianhythmic agents (procainamide, quinidine and others), antihypertensive agents (alpha-methyldopa), antimalarials (primaquine and others), and the anticoagulants (warfarin and heparin and others). Therapy of anemia includes blood transfusion, removal of the agent or toxin causing the anemia, or treating the underlying cause of the anemia. In some cases of anemia, erythropoeitin can be used to stimulate the erythrocyte precursor cells in the bone manow cells to produce mature erythrocytes. A gene, genes, or gene pathway involved in the etiology of anemia or associated disorders or potential sites for targeted dmg therapy of anemia are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of anemia are listed in Table 57. B. Angina Angina pectoris is a common clinical manifestation of coronary artery disease. Angina is a clinical syndrome including chest pain or discomfort brought on by exertional or anxiety, typically lasting several minutes. Patients with angina are at increased risk of myocardial infarction heart failure and death. Angina is a symptom of myocardial ischemia that is the result of myocardial oxygen demand not met by myocardial oxygen supply (for more details see below under Ischemia). Although the most common cause of myocardial ischemia is atherosclerotic coronary artery disease, there are other factors that may lead to this clinical syndrome, including thromboembolic disease and vasospasm. Factors related to myocardial oxygen demand include heart rate, contractility, and wall tension (ventricular volume and ventricular pressure). Unstable angina refers to angina of which occurs at rest or without a specific (exertional or environmental) trigger. Stable angina refers to predictable, event-induced chest pain. Unstable angina has been conelated with progression to acute myocardial infarction in 20% of the cases. More than 50% of the patients with unstable angina have multi-vessel disease with eccentric, inegular, or ulcerated atherosclerotic lesions associated with endothelial dismption and adherent thrombus. Another form of angina is variant angina which is characterized by chest pain accompanied by a transient ST-segment changes (either ST elevation or depression) and ventricular anhythmias. Angina can often be controlled by nitrates, β-adrenergic blockers, calcium channel blockers, antiplatelet and antithrombin therapy, or combination thereof. Genes, and gene pathway involved in the etiology of angina and associated disorders or potential sites for targeted dmg therapy of angina are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of anemia are listed in Table 58. C. Arrhythmia Cardiac anhythmias occur as a result of abnormalities of impulse generation, impulse conduction, and combined abnormalities of impulse generation and conduction. Some cardiac anythmias may lead to asymptomatic conditions, others lead to clinical symptoms and may be life-threatening. Abnormalities of impulse generation includes abnormal automaticity (abnormal pacemakers), triggered activity as a result of early or delayed after-depolarizations. In both alterations of automaticity and triggered activity, generation of impulses in fibers that are normally incapable of normal automaticity, e.g. atrial and ventricular tissue, ensues. Within the myocardium the conduction system can become a cardiac pacemaker. For example, the atrioventricular (AV) node. Abnormalities of impulse conduction occurs via a process called reentry. In reentry, there occurs an area or region that is slow or unable to conduct electrical signals. This defect in conduction permits a wave of excitation to propagate continuously within a closed circuit. In these cases, the sunounding tissue is not at the same pace as the sunounding tissue and the electrical impulse passes through the normal tissue and can spread in a multi -directional manner which leads to marked asynchrony. Heart block is the condition whereby the conduction from the atria to the ventricles is intermpted. Myocardial disease may decrease or stop conduction in one or more regions. Heart block may be complete, incomplete, include a right- or left bundle branch block, hemiblock or fascicular blocks. Ectopic foci of excitation occurs when there is myocardial disease that renders the His-Purkinje fibers or other fibers to discharge electrical activity spontaneously. This condition leads to increased automaticity, potentially leading to extrasystole, premature beats, atrial or ventricular or nodal paroxysmal tachycardia, or atrial flutter. Arrhythmias may also be localized to the atrial or ventricular regions. Atrial anhythmias include atrial tachycardia, or paroxysmal atrial tachycardia with block, atrial flutter, or atrial fibrillation. Ventricular anhythmias can include all of the previous described types of anhythmias but also include paroxysmal ventricular tachyarrhythmia as well and ventricular fibrillation. Accelerated AV conduction (Wolff-Parkinson-White syndrome) or the Lown-Ganong-Levine syndrome are examples or other anhythmias that are characterized by specific electrocardiogram abnormalities. Therapy for anhythmias includes an understanding of the type, underlying mechanism, and treatment targeted to restore normal cardiac function. However, in some cases, mechanisms can only be infened and therapy is based on empirical knowledge. Cunent antianhythmic dmgs can be classified as the following broad categories: Na+ channel blockers, K+ channel blockers, Ca+ channel blockers, β- adrenergic blockers, and digitalis. In each of these categories, there is a blockade of the activity of the specific ion channel or receptor mediated activation of the myocardial activity. Digitalis is the exception, having multiple pharmacologic effects including Ca+ cunent inhibition, stimulation of vagal tone to the myocardium, and a reduction in the K+ cunents within the atrium. A gene, genes, or gene pathway involved in the etiology of anhythmia or associated disorders or potential sites for targeted dmg therapy of anhythmia are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of anhythmias are listed in Table 59. Hypertension Hypertension is the clinical syndrome in which there is sustained elevation of systemic arterial pressure. There may be conditions of specific arterial hypertension to specific organs, including pulmonary, renal, hepatic arterial hypertension. Systemic hypertension is a common abnormality that can be the result of a variety of conditions including: adrenocortical disease ( Conn's syndrome, aldosteronism, hypersecretion of glucocorticoids, hypersecretion of mineralocorticoids, and psuedohyperaldosteronism), pheochromocytoma, justaglomerular carcinoma, renal hypertension, renal disease (glomerulonephritis, pyleonephritis, polycystic disease, Liddle's syndrome, hypokalemic nephropathy, low-renin hypotension), Nanowing of the aorta, oral contraceptives, neurovascular compression of the rostral ventrolateral medulla. However, in most cases, the etiology is unknown (termed essential hypertension). Therapy of hypertension includes α- or β-adrenergic blockers, inhibition of the renin -angiotension system, or converting enzyme, and calcium channel blockers. In cases whereby hypertension is the result of a condition, as listed above, the primary condition is treated with ancillary antihypertensive added. Further, reduction in the intake of sodium in the diet has been shown to assist the reduction of systemic arterial pressure. A gene, genes, or gene pathway involved in the etiology of hypertension or associated disorders or potential sites for targeted dmg therapy of hypertension are depicted in Tablel 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of hypertension are listed in Table 60. E. Hypotension Hypotension is the condition of subnormal blood pressure. Hypotension may be the result of orthostatic hypotension, anemic conditions, fulminant menigococcemica or other infections, blood transfusions, trauma, traumatic brain injury, hepatic or renal failure, and dmg induced. Hypotension is cunently treated with methoamine, peripheral sympathomimetics, and vasopressin. A gene, genes, or gene pathway involved in the etiology of hypotension or associated disorders or potential sites for targeted dmg therapy of hypotension are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of hypotension are listed in Table 61. F. Ischemia Myocardial ischemia develops when the metabolic demands exceed oxygen delivery to the myocardium. Factors that influence the myocardial oxygen supply include the oxygen capacity of the blood, coronary blood flow and vascular resistance. Factors that affect myocardial oxygen demand are heart rate, contractility, and systolic wall tension. Any agent or physiologic factor that decreases myocardial oxygen supply or increases myocardial oxygen demand may potentially lead to myocardial ischemia. There are conditions that lead to myocardial ischemia including hypertension, anhythmias, coronary artery disease, rheumatic fever, congenital heart defects, heart failure, and myocardial infarction. The identification and extent of myocardial damage due to myocardial oxygen demand and reduced supply clinically manifests as myocardial infarction, sudden death, angina pectoris (either uncomplicated or with infarct), and coronary insufficiency. Therapies for myocardial ischemia cunently available are described within other sections of this invention and can be found under the following sections: thrombosis, angina, hypertension, anhythmias, and heart failure. A gene, genes, or gene pathway involved in the etiology of ischemia or associated disorders or potential sites for targeted dmg therapy of ischemia are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of myocardial ischemia are listed in Tables 57, 59, 60, 62, and 64. G. Heart Failure Heart failure is a syndrome in ventricular dysfunction if accompanied by reduced exercise capacity. Heart failure is the final condition from a variety of cardiovascular disorders including coronary heart disease, long-standing hypertension, valve deformities or valvular heart disease, rheumatic heart disease, nutritional cardiac disease and cardiomyopathies. Other diseases or conditions associated with heart failure include infections (systemic or cardiac specific (myocarditis), infiltrative disorders (amyloidosis, hemochromatosis, sarcoidosis), electrolyte disorders, myocardial specific toxins (substances of abuse, cancer chemotherapeutic agents), lupus erythmatosus, rheumatoid arthritis, diabetes mellitus, thyroid disease, hypoparathyroidism, pheochromocytoma, and sustained or prolonged tachycardia. Ultimately, in the failing heart, inotropic action is compromised and the resultant loss in cardiac output renders the myocardium unable to meet the systemic and peripheral metabolic demands leading to various clinical symptoms including cardiac enlargement, weakness, edema, prolonged circulation time, hepatic enlargement, shortness of breath, sensation of suffocation, and distention of peripheral veins. Dyspnea on exertion is a prominent symptom, leading to paroxysmal, and in severe cases, frank pulmonary edema. Physiological compensatory mechanisms of heart failure can be broadly described as increased heart rate, increased preload and afterload, and cardiac hypertrophy. Each of these physiological changes are attempts to increase cardiac output which is dependent on heart rate, blood pressure and contractility. Although the most common form of heart failure is left ventricular failure (70-90%o), there are conditions whereby diastolic dysfunction occurs (10-30%>). Clinically these two are treated differently. For left ventricular (LV) failure, the cunent therapies include a combination of antihypertensives (ACE inhibitors), diuretics, and positive inotropic agents. Refractory cases of LV failure, additional diuretics, vasodilators, and β-adrenergic blockers are added to the regimen. In diastolic dysfunction leading to failure Ca++ channel blockers are the first line of therapy with ACE inhibitors and β-adrenergic blockers added in refractory cases. Heart failure is further associated with a variety of co-morbidities that can worsen the condition and prognosis including septicemia, hypo-osmolarity, primary thrombocytopenia, renal hypertension disorder, myocardial infarction, pulmonary embolism, anhythmias, intracerebral or subdural hemonhage, cerebral thrombosis, hypotension, pneumonia, chronic renal failure, and decubitus ulcers. A gene, genes, or gene pathway involved in the etiology of heart failure or associated disorders or potential sites for targeted dmg therapy of heart failure are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of heart failure are listed in Table 1 1 and complications associated with heart failure in Tables 59, 60, 62, and 64. H Thrombosis Thrombosis is the formation of a blood clot in a blood vessel. If the thrombotic clot is large enough it may occlude the vessel and create tissue hypoxia. If unchecked, thrombosis can be a major medical problem and is associated with vessels that have sluggish blood flow, including in veins of extremities after surgery or delivery, conditions of reduced cardiac output, or in coronary or cerebral arteries where the intima is damaged by atherosclerotic plaques (see below) or damage to the endocardium. Areas of thrombi have a tendency to break off from a vessel wall and can travel to distant sites, termed emboli, and create damage to other organs. The activation of coagulation occurs via a coordinated process of clotting factors leading to the formation of thrombin which then activates the conversion of fibrinogen to fibrin and clot formation ensues. However, in the endothelial cell, when thrombin binds to thrombomodulin, thrombin has anticoagulant activity by first activating protein C. Activated protein C then inactivates an inhibitor of tissue plasminogen activator and conversion of plasminogen to plasmin occurs. Plasminogen is converted to active plasmin when tissue plasminogen activator hydrolyzes the bond between arg560 and val561. Plasmin is responsible for the enzymatic breakdown of clots. Atherosclerosis is a complex combination of hyperhpidemia, injury to the endothelium, and inflammation. The interaction of these multiple processes in association with local genetic and hemodynamic influences may promote the formation of atheromatous plaques as a reparative response of the arterial wall. Atherosclerotic plaques are composed of thrombogenic lipid-rich core protected by a fibrous cap comprising smooth muscle cells and inflammatory cells. The inflammatory cells are predominantly macrophages. As atherosclerotic plagues build blood flow is reduced creating ischemia in tissues down stream from the area of the plaque. In another model, the stenosis created by the plaques may be a part of the resulting ischemic event. Frequently, less obstmctive but more vulnerable plaques occur which are characterized by a thinned fibrous cap, marked lipid accumulation, a large number of macrophages, and a smaller amount of smooth muscle cells. It has been proposed that since these plaques are more prone to rupture creating contact with the highly thrombogenic materials of the lipid-rich nucleus of these lesions, thrombosis is stimulated. Advanced atherosclerotic lesions are caused by a series of cellular and molecular events involving replication of smooth muscle cells and macrophages on the vessel wall. The interaction of these cells with the T lymphocytes can lead to a fibroproliferative response. Large amounts of connective tissue produced by these smooth muscle cells consist of macrophages, T lymphocytes, smooth muscle cells, connective tissue, necrotic residues, and varying amounts of lipids and lipoproteins. Endothelial cells maintain the vessel surface in a non-thrombogenic state, preventing platelet and leukocyte adhesion, and act in maintaining the vascular tonus by releasing nitric oxide, prostaglandin, and endothelin. These cells also produce growth factors, cytokines, and chemokines to maintain the integrity of the collagen- and proteoglycan-rich basement membrane. Changes in some of these functions may trigger cell interactions with monocytes, platelets, smooth muscle cells, and lymphocytes. Hyperhpidemia and hypercholesterolemia are sufficient to induce dysfunction of the endothelial modulation of the vasoactive reactions and arteriolar tonus. Anticlotting therapy includes heparin, strepotokinase, urokinase-type plasminogen activator, and tissue-plasminogen activator. Coumarin derivatives such as dicumarol and warfarin can also be effective anticogulants. These compounds inhibit the action of vitamin K which is a necessary cofactor for the enzyme that converts glutamic acid residues to g-carboxyglutamic acid residues. This mechanism affects the clotting factors II, VII, IX, and X, as well as protein C and protein S. A gene, genes, or gene pathway involved in the etiology of thrombosis or associated disorders or potential sites for targeted dmg therapy of thrombosis are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of thrombosis are listed in Table 64. I. Renal Disease The kidneys are primarily involved in regulating body fluid volume and composition by forming urine. The puφose of urine excretion, composed of ionic solutes, is to remove or eliminate metabolic end-products and maintain fluid volume and composition for the sustenance of physiologic function of the rest of the body. Urine formation and composition is affected by dietary intake of solutes and water as well as endogenous and exogenous carbohydrates, proteins, and nucleic acids. The kidneys also provide the mechanism to excrete dmgs, toxins, and other exogenous substances. Urine formation occurs via a sequence of five steps: 1) the glomerulus filters extracellular fluid across the glomerulus capillaries and the visceral epithelium of Bowman's capsule; the driving force is mean arterial blood pressure; 2) the proximal tubule isotonically reabsorbs approximately two-thirds of the glomerular filtrate; 3) the loop of Henle dissociates the absoφtion of sodium and water; 4) the distal convoluted tubule primarily absorbs sodium under the influence of aldosterone and secretes protons, ammonia, and potassium; and lastly, 5) the collecting duct system regulates the osmolarity of urine under the influence of antidiuretic hormone. In addition to its function of producing urine, the kidney can also serve as an endocrine organ producing and secreting prostaglandins, kallikreinin-kinins, erythropoeitin, and renin The kidney also has a function and role in metabolism. The kidney is a target organ for many hormones including parathyroid hormone, aldosterone, and antidiuretic hormone. Renal dysfunction or disorders often are clinically nonspecific and are characterized by hematuria, azotemia, hypertension, and metabolic acidiosis. Broadly, kidney dysfunction can be categorized as undeφerfusion syndromes, renal parenchymal syndromes, and post-renal syndromes. Renal undeφerfusion syndromes include reduced effective circulating volume (including circulatory collapse, congestive heart failure, and cinhosis of the liver), occlusive renal artery disease (including renal artery atherosclerosis, fibromuscular hypeφlasia), and vasoconstriction of renal microvasculature (including acute transplant rejection, cyclosporin nephrotoxicity, and amophtericin B nephrotoxicity). Renal parenchymal syndromes include acute hypertensive nephropathy, analgesic nephropathy, hemolytic-uremic syndrome, hypercalcemic nephropathy, interstitial nephritis, lupus nephritis, multiple myeloma, oxalate nephropathy, pyelonephritis, glomerulonephritis, renal vein thrombosis, Wegener' s granolumatosis. Renal failure, or the uremic syndrome, occurs when the functional renal mass is sufficiently reduced such that the kidney is longer able to conduct normal functions. Thus, the clinical hallmarks of this disease are related to the loss of urine formation, excretion, and abenant composition of body fluids as well as loss of erythropoeitin and renin and may be treated separately. These related disorders include electrolyte disorders (accumulation of potassium, sodium, phosphate, magnesium and aluminum and hypocalcemia), cardiovascular abnormalities (including accelerated atherosclerosis, hypertension, pericarditis, myocardial dysfunction), hematologic dysfunction (including anemia, leukocyte dysfunction, hemonhagic diathesis), gastrointestinal disorders (including anorexia, nausea, vomiting, gastroparesis, gastrointesinal bleeding), disorders of taste, renal osteodystrophy (including osteomalacia, osteitis fibrosa, osteosclerosis, osteoporosis), neurologic abnornmalities (including insomnia, fatigue, psychological symptoms, asterixis, peripheral neuropathies), myopathy, impaired carbohydrate intolerance (peripheral resistance to insulin)), endocrine and metabolic disorders (including glucose intolerance, insulin resistance, insulin degradation, hypoglycemia, fertility disorders, hypothermia), hyperuricemia, and pruritis, soft tissue calcification and uremic frost. In chronic renal failure, the loss of renal function may be associated with adaptive functional changes in an attempt to restore renal function. These adaptive processes include increased glomemlar filtration rate of the intact nephrons, and increased phosphate excretion. Unfortunately, as the kidney disease and the loss of renal function progresses, these adaptive processes may ultimately create more damage than restore function. In any of the cases for renal disease there are aggravating factors that can affect the progression of the disease including vascular volume depletion (as a result of diuretics, gastrointesinal fluid losses, dehydration, low cardiac output, renal hypoperfusion, atheroembolic disease, ascites, nephrotic syndrome), dmgs (including aminoglycosides, prostaglandin synthesis inhibitors, diuretics), obstmctions (including tubule obstmction via uric acid or Bence Jones protein or posttubular obstmction via prostatic hypertrophy, necrotic papillae, or uretal stones), infections, toxins (including radiographic contract materials), hypertensive crisis, and hypercalcemia or hypeφhosphatemia. Treatments of renal disease are dependent on whether there is an acute or chronic condition. In the acute conditions, stabilization of fluid and electrolyte balance is critical for the sustenance of life. In chronic end-stage failure the patient may have to depend on exogenous dialysis or transplantation. A gene, genes, or gene pathway involved in the etiology of renal disease or associated disorders or potential sites for targeted dmg therapy of renal disease or associated disorders are depicted in Table 11 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of anemia are listed in Table 57, for renal disease in Table 65, and for nephritis in Table 66. J. Restenosis Interventional cardiology includes procedures aimed at mechanically improving coronary blood flow. These procedures include intracoronary stents, coronary artery bypass surgery, and percutaneous transluminal coronary angioplasty (PCTA). Although successful resolution of coronary arterial vessel occlusion has been accomplished with PCTA in as many as two thirds of the patients, cunently nearly 20-30%> of the patients require emergency bypass surgery, there is an associated 4-10%> mortality, 2-5% sustain damage to the vessel including dissection, intimal dismption, perforation, and embolism, and 9% experience Q-wave infarctions. Another PCTA related complication is coronary restenosis. Restenosis, or reocclusion of the coronary vessel, has predisposing factors including male gender, continued smoking after PCTA, diabetes mellitus, elevated insulin levels, absence or previous myocardial infarction, and unstable angina. A gene, genes, or gene pathway involved in the etiology of restenosis or associated disorders or potential sites for targeted dmg therapy of restenosis are depicted in Table 1 1 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of restenosis are listed in Table 67. K. Peripheral vascular disease Peripheral vascular disease (PVD) refers to diseases of any of the blood vessels outside the myocardium and to diseases of the lymph vessels. The disorder is often a nanowing of the blood vessels that cany blood to the arms and legs. There are two types of PVD, functional PVD and organic PVD. Functional PVD is not organic and does not involve defects in the stmcture of the blood vessels. Functional PVD includes Raynaud's syndrome. Organic PVD are caused by stmctural changes in the vessel, such as inflammation and tissue damage, for example Buerger's disease. PVD can result from atheromatous nanowing of the arteries to the legs. Symptoms may range from calf pain on exercise "intermittent claudication", to rest pain and gangrene. Intermittent claudication is the commonest symptom occurring in around up to 5% of men and 2.5% of women aged 60 or over. Peripheral vascular disease may be the result of venous stasis, anemia, dysbetalipoporteinemia, diabetes mellitus, and systemic sclerosis. A gene, genes, or gene pathway involved in the etiology of peripheral vascular disease or associated disorders or potential sites for targeted drag therapy of peripheral vascular disease are depicted in Table 11 with the specific gene list in Table 6. Cunent candidate therapeutic interventions in development for the treatment of peripheral vascular disease are listed in Table 68. Advantages of Pharmaco enomic Clinical Development of Novel Candidate Therapeutic Interventions for the Treatment of Disease The evidence that a variance in a gene involved in a pathway that affects dmg response, indicates and supports the theory that there is a likelihood that other genes have similar qualities to various degrees. As dmg research and development proceeds to identify more lead candidate therapeutic interventions for neurologic and psychiatric disease, there is possible utility in stratifying patients based upon their genotype for these yet to be conelated variances. Further, as described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for patients with neurologic and psychiatric disease. As described below there are likely gene pathways as are those that are outlined in the gene pathway Tables 1-6 as described above and matrix Tables 7-1 1. The advantages of a clinical research and dmg development program that include the use of polymoφhic genotyping for the stratification of patients for the appropriate selection of candidate therapeutic intervention includes 1) identification of patients that may respond earlier to therapy, 2) identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both, 3) identification of pathophysiologic relevant variance or variances and potential therapies affecting those allelic genotypes or haplotypes, and 4) identification of allelic variances or haplotypes in genes that indirectly affects efficacy, safety or both. Based upon these advantages, designing and performing a clinical trial, either prospective or retrospective, which includes a genotype stratification arm will incoφorate analysis of clinical outcomes and potential genetic variation associated with those outcomes, and hypothesis testing of the statistically relevant conelation of the genotypic stratification and therapeutic benefits. If statistical relevance is detectable, these studies will be incoφorated into regulatory filings. Ultimately, these clinical trial data will be considered during the approval for marketing process, as well as, incoφorated into accepted medical management of the described indications. By identifying subsets of patients diagnosed with anxiety that respond earlier to agents, optimal candidate therapeutic interventions may reduce the lag time prior to relief of psychiatric symptoms. Appropriate genotyping and conelation to dosing regimen would be beneficial to the patient, caregivers, medical personnel, and the patient's loved ones. As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select a gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted dmg development program for the clinical indications descibed in this invention. Identification of pathophysiologic relevant variance or variances and potential therapies affecting those allelic genotypes or haplotypes will speed the dmg development. There is a need for therapies that are targeted to the disease and symptom management with limited or no undesirable side effects. Identification of a specific variance or variances within genes involved in the pathophysiologic manifestation of anxiety and specific genetic polymoφhisms of these critical genes can assist the development of novel anxiolytic agents and the identification of those patients that may best benefit from therapy of these candidate therapeutic alternatives. By identifying allelic variances or haplotypes in genes that indirectly affects efficacy, safety or both one could target specific secondary dmg or agent therapeutic actions that affect the overall therapeutic action of conventional, atypical, or novel action. In Tables 12-17 and 18-23, there is a listing of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of an anxiety patient population based upon genotype. In matrix Tables 7-11 one skilled in the art would be able to identify these pathway specific genes or other genes listed in Tables 7-1 1 that may be involved in the manifestation of neurologic or psychiatric disease or are likely candidate targets for therapeutic approaches described in this invention. A sample of therapies approved or in development for preventing or treating the progression of symptoms of cancer currently known in the art are shown in Table 24; for neurologic and psychiatric disease, Tables 25-36; for inflammation and immune disorders, Tables 38-49; for endocrine and metabolic disease, Tables 50-56; and for cardiovacular and renal disease, Tables 57-68. In these tables, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Pharmacogenomics studies for these dmgs, as well as other agents, dmgs, compounds or candidate therapeutic interventions, could be performed by identifying genes that are involved in the function of a dmg including, but not limited to is absoφtion, distribution metabolism, or elimination , the interaction of the dmg with its target as well as potential alternative targets, the response of the cell to the binding of a dmg to a target, the metabolism (including synthesis, biodistribution or elimination) of natural compounds which may alter the activity of the dmg by complementary, competitive or allosteric mechanisms that potentiate or limit the effect of the dmg, and genes involved in the etiology of the disease that alter its response to a particular class of therapeutic agents. It will be recognized to those skilled in the art that this broadly includes proteins involved in pharmacokinetics as well as genes involved in pharmacodynamics. This also includes genes that encode proteins homologous to the proteins believed to cany out the above functions, which are also worth evaluation as they may cany out similar functions. Together the foregoing proteins constitute the candidate genes for affecting response of a patient to the therapeutic intervention. Using the methods described above, variances in these genes can be identified, and research and clinical studies can be performed to establish an association between a dmg response or toxicity and specific variances. For each of the described disease indications one skilled in the art can identify novel candidate therapeutic interventions that may be used to treat the disease or symptoms and/or proceed with a regimen of palliative care. For compounds that have yet to achieve approval, or are still in development one skilled in the art can determine those candidate therapeutic interventions that may be of therapuetic benefit. Exemplary compounds in development for the treatment of disease disorders or dysfunctions There are many sources for obtaining information on dmgs approved for human therapeutic use an for those compounds under clinical or preclinical investigation, as well as for compounds which have been identified as having a particular pharmacological activity. For products, which have been approved, the PDR contains a listing of the package inserts for all of the products available for human therapeutic intervention. The Merck Index can be used as an additional text to supplement information gathered on the candidate therapeutic interventions. For products that are under clinical or preclinical development, there are databases cataloging information on those candidate therapeutic interventions. Generally that information includes aspects of the dmg development process, such as phase of development, identified therapeutic indications, name of manufacturer, mechanistic and pharmacological activities of the product. These databases are available for a fee, and include: PharmaProjects (http://pibpubs.co.u 'pharmamain2/html) and R&D Focus (http.v/wwvv.ims.global.com/products/lifecycle/r and d.htm). One skilled in the art can readily utilize these sources to determine appropriate candidate therapeutic intervention for the identified disease, disorder or condition. Since there are a large number of candidate therapeutic interventions that are either approved for human therapeutic use or under clinical or preclinical investigation, one skilled in the art could search through publicly available or fee- for-access databases for interventions that may be of therapeutic benefit for a particular disease, disorder, or condition, and determine whether variances in particular genes conelate with inteφatient variation in response to one or more of those therapeutic interventions. An example of the results of such searching is provided in Tables 24-68. In these tables, the disease, disorder or condition is listed. In order to generate a table or other compendium of information as listed in the table, one skilled in the art can search, for example as for Table 35, in databases for products having the indication "schizophrenia". Alternatively, one can search for alternative indications or co-morbidities, e.g., pyschoses, neuroleptic, neurological to arrive at a more complete list of the available products. In the table, the candidate therapeutics were sorted and listed by pharmacologic mechanism of action (action). Further, the product name, chemical name (if specified), as well as the indication considered for clinical development. If the candidate therapeutic interventions are approved for therapeutic use, then one skilled in the art can obtain dosing, adverse events, pharmacologic parameters (both pharmacokinetic and pharmacodynamic), and clinical data or information by referring to the PDR. If the candidate therapeutic intervention are in clinical or preclinical stages of dmg development, then one skilled in the art would gather data on dosing, adverse events, pharmacologic parameters (both pharmacokinetic and pharmacodynamic), and clinical data or information for the dmg or product sponsor. In both cases, selection of a candidate therapeutic intervention for retrospective or prospective pharmacogenetic clinical studies would use an analysis of the likelihood that there is a phenomeno logical or statistical support for the review of the data to ascertain whether the candidate therapeutic intervention (approved or in development) efficacy or safety profiles can be grouped based upon the individual's genotype or phenotype. In this way, a gene or genes selected, e.g., from a pathway involving the cellular or more broadly the pharmacological mechanism of actions, can be identified and genotyping can be performed in order to determine the allelic variance, variances, for haplotype. Further, one could group the individuals by such genetic variances and further by the therapeutic outcome determinants. Pharmacogenomics studies for these dmgs, as well as other agents, dmgs, compounds or candidate therapeutic interventions, can be performed by identifying genes that are involved in the the function of a dmg including, but not limited to is absoφtion, distribution metabolism, or elimination , the interaction of the dmg with its target as well as potential alternative targets, the response of the cell to the binding of a dmg to a target, the metabolism (including synthesis, biodistribution or elimination) of natural compounds which may alter the activity of the dmg by complementary, competitive or allosteric mechanisms that potentiate or limit the effect of the dmg, and genes involved in the etiology of the disease that alter its response to a particular class of therapeutic agents. It will be recognized to those skilled in the art that this broadly includes proteins involved in pharmacokinetics as well as genes involved in pharmacodynamics. This also includes genes that encode proteins homologous to the proteins believed to carry out the above functions, which are also worth evaluation as they may cany out similar functions. Together the foregoing proteins constitute the candidate genes for affecting response of a patient to the therapeutic intervention. Using the methods described above, variances in these genes can be identified, and research and clinical studies can be performed to establish an association between a dmg response or toxicity and specific variances. Further, there may be genes within pathways that are either involved in metabolism of dmgs, hormones, compounds, agents, or neurotransmitters or are involved in metabolism of various drugs or compounds. In Tables 1-6 and 12-23, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with neurologic or psychiatric disease based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of described disease indications of this invention are listed as gene pathways and are listed in Tables 1- 23. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of the described neurological or psychiatric disease, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in dmg response to therapies for neurological or psychiatric disease described in the present invention. As indicated in the Summary above, certain aspects of the present invention typically involve the following process, which need not occur separately or in the order stated. Not all of these described processes must be present in a particular method, or need be performed by a single entity or organization or person. Additionally, if certain of the information is available from other sources, that information can be utilized in the present invention. The processes are as follows: a) variability between patients in the response to a particular treatment is observed; b) at least a portion of the variable response is conelated with the presence or absence of at least one variance in at least one gene; c) an analytical or diagnostic test is provided to determine the presence or absence of the at least one variance in individual patients; d) the presence or absence of the variance or variances is used to select a patient for a treatment or to select a treatment for a patient, or the variance information is used in other methods described herein. A. Identification of Inteφatient Variability in Response to a Treatment Inteφatient variability is the mle, not the exception, in clinical therapeutics. One of the best sources of information on inteφatient variability is the nurses and physicians supervising the clinical trial who accumulate a body of first hand observations of physiological responses to the dmg in different normal subjects or patients. Evidence of inteφatient variation in response can also be measured statistically, and may be best assessed by descriptive statistical measures that examine variation in response (beneficial or adverse) across a large number of subjects, including in different patient subgroups (men vs. women; whites vs. blacks; Northern Europeans vs. Southern Europeans, etc.). In accord with the other portions of this description, the present invention concerns DNA sequence variances that can affect one or more of: i. The susceptibility of individuals to a disease; ii. The course or natural history of a disease; iii. The response of a patient with a disease to a medical intervention, such as, for example, a dmg, a biologic substance, physical energy such as radiation therapy, or a specific dietary regimen. (The terms 'dmg', 'compound' or 'treatment' as used herein may refer to any of the foregoing medical interventions.) The ability to predict either beneficial or detrimental responses is medically useful. Thus variation in any of these three parameters may constitute the basis for initiating a pharmacogenetic study directed to the identification of the genetic sources of inteφatient variation. The effect of a DNA sequence variance or variances on disease susceptibility or natural history (i and ii, above) are of particular interest as the variances can be used to define patient subsets which behave differently in response to medical interventions such as those described in (iii). The methods of this invention are also useful in a clinical development program where there is not yet evidence of inteφatient variation (perhaps because the compound is just entering clinical trials) but such variation in response can be reliably anticipated. It is more economical to design pharmacogenetic studies from the beginning of a clinical development program than to start at a later stage when the costs of any delay are likely to be high given the resources typically committed to such a program In other words, a vanance can be useful for customizing medical therapy at least for either of two reasons First, the vanance may be associated with a specific disease subset that behaves differently with respect to one or more therapeutic interventions (I and n above), second, the vanance may affect response to a specific therapeutic intervention (in above) Consider for exemplary puφoses pharmacological therapeutic interventions In the first case, there may be no effect of a particular gene sequence vanance on the observable pharmacological action of a drug, yet the disease subsets defined by the vanance or vaπances differ in their response to the dmg because, for example, the dmg acts on a pathway that is more relevant to disease pathophysiology in one vaπance-defmed patient subset than in another vaπance-defined patient subset The second type of useful gene sequence vanance affects the pharmacological action of a dmg or other treatment Effects on pharmacological responses fall generally into two categoπes; pharmacokinetic and pharmacodynamic effects. These effects have been defined as follows in Goodman and Gilman's Phamacologic Basis of Theiapeutics (ninth edition, McGraw Hill, New York, 1986) "Pharmacokinetics" deals with the absoφtion, distπbution, biotransformations and excretion of dmgs The study of the biochemical and physiological effects of dmgs and their mechanisms of action is termed "pharmacodynamics " Useful gene sequence vanances for this invention can be descπbed as vaπances which partition patients into two or more groups that respond differently to a therapy or that conelate with differences in disease susceptibility or progression, regardless of the reason for the difference, and regardless of whether the reason for the difference is known. The latter is tme because it is possible, with genetic methods, to establish reliable associations even in the absence of a pathophysiological hypothesis linking a gene to a phenotype, such as a pharmacological response, disease susceptibility or disease prognosis B Identification of Specific Genes and Conelation of Vanances in Those Genes with Response to Treatment of Diseases or Conditions It is useful to identify particular genes which do or are likely to mediate the efficacy or safety of a treatment method for a disease or condition, particularly in view of the large number of genes which have been identified and which continue to be identified m humans. As is further discussed in section C below, this conelation can proceed by different paths. One exemplary method utilizes prior information on the pharmacology or pharmacokinetics or pharmacodynamics of a treatment method, e.g., the action of a drag, which indicates that a particular gene is, or is likely to be, involved in the action of the treatment method, and further suggests that variances in the gene may contribute to variable response to the treatment method. For example if a compound is known to be glucuronidated then a glucuronyltransferase is likely involved. If the compound is a phenol, the likely glucuronyltransferase is UGT1 (either the UGT1 *1 or UGT1 *6 transcripts, both of which catalyze the conjugation of planar phenols with glucuronic acid). Similar inferences can be made for many other biotransformation reactions. Alternatively, if such information is not known, variances in a gene can be conelated empirically with treatment response. In this method, variances in a gene which exist in a population can be identified. The presence of the different variances or haplotypes in individuals of a study group, which is preferably representative of a population or populations of known geographic, ethnic and/or racial background, is determined. This variance information is then conelated with treatment response of the various individuals as an indication that genetic variability in the gene is at least partially responsible for differential treatment response. It may be useful to independently analyze variances in the different geographic, ethnic and/or racial groups as the presence of different genetic variances in these groups (i.e. different genetic background) may influence the effect of a specific variance. That is, there may be a gene x gene interaction involving one unstudied gene, however the indicated demographic variables may act as a sunogate for the unstudied allele. Statistical measures known to those skilled in the art are preferably used to measure the fraction of inteφatient variation attributable to any one variance, or to measure the response rates in different subgroups defined genetically or defined by some combination of genetic, demographic and clinical criteria. Useful methods for identifying genes relevant to the pharmacological action of a drag or other treatment are known to those skilled in the art, and include review of the scientific literature combined with inteferential or deductive reasoning that one skilled in the art of molecular pharmacology and molecular biology would be capable of; large scale analysis of gene expression in cells treated with the drug compared to control cells; large scale analysis of the protein expression pattern in treated vs. untreated cells, or the use of techniques for identification of interacting proteins or ligand-protein interactions, such as yeast two-hybrid systems. C. Development of a Diagnostic Test to Determine Variance Status In accordance with the description in the Summary above, the present invention generally concerns the identification of variances in genes which are indicative of the effectiveness of a treatment in a patient. The identification of specific variances, in effect, can be used as a diagnostic or prognostic test. Conelation of treatment efficacy and/or toxicity with particular genes and gene families or pathways is provided in Stanton et al., U.S. Provisional Application 60/093,484, filed July 20, 1998, entitled GENE SEQUENCE VARIANCES WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE (concerns the safety and efficacy of compounds active on folate or pyrimidine metabolism or action) and Stanton, U.S. Provisional Application No. 60/121 ,047, filed February 22, 1999, entitled GENE SEQUENCE VARIANCES WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE (concerning Alzheimer's disease and other dementias and cognitive disorders), which are hereby incoφorated by reference in their entireties including drawings. Genes identified in the examples below and in the Tables can be used in the methods of the present invention. A variety of genes which the inventors realize may account for inteφatient variation in response to treatments for neurological and psychiatric diseases, conditions, disorders, and/or the development of same are listed in Tables 1 -6, and 12-23. Gene sequence variances in said genes are particularly useful for aspects of the present invention. Methods for diagnostic tests are well known in the art. Generally in this invention, the diagnostic test involves determining whether an individual has a variance or variant form of a gene that is involved in the disease or condition or the action of the drug or other treatment or effects of such treatment. Such a variance or variant form of the gene is preferably one of several different variances or forms of the gene that have been identified within the population and are known to be present at a certain frequency. In an exemplary method, the diagnostic test involves determining the sequence of at least one variance in at least one gene after amplifying a segment of said gene using a DNA amplification method such as the polymerase chain reaction (PCR). In this method DNA for analysis is obtained by amplifying a segment of DNA or RNA (generally after converting the RNA to cDNA) spanning one or more variances in the gene sequence. Preferably, the amplified segment is <500 bases in length, in an alternative embodiment the amplified segment is <100 bases in length, most preferably <45 bases in length. In some cases it will be desirable to determine a haplotype instead of a genotype. In such a case the diagnostic test is performed by amplifying a segment of DNA or RNA (cDNA) spanning more than one variance in the gene sequence and preferably maintaining the phase of the variances on each allele. The term "phase" refers to the relationship of variances on a single chromosomal copy of the gene, such as the copy transmitted from the mother (maternal copy or maternal allele) or the father (paternal copy or paternal allele). The haplotyping test may take part in two phases, where first genotyping tests at two or more variant sites reveal which sites are heterozygous in each patient or normal subject. Subsequently the phase of the two or more variant sites can be determined. In performing a haplotyping test preferably the amplified segment is >500 bases in length, more preferably it is >1,000 bases in length, and most preferably it is >2,500 bases in length. One way of preserving phase is to amplify one strand in the PCR reaction. This can be done using one or a pair of oligonucleotide primers that terminate (i.e. have a 3 ' end that stops) opposite the variant site, such that one primer is perfectly complementary to one variant form and the other primer is perfectly complementary to the other variant form. Other than the difference in the 3 ' most nucleotide the two primers are identical (forming an allelic primer pair). Only one of the allelic primers is used in any PCR reaction, depending on which strand is being amplified. The primer for the opposite strand may also be an allelic primer, or it may prime from a non- polymoφhic region of the template. This method exploits the requirement of most polymerases for perfect complementarity at the 3' terminus of the primer in a primer-template complex. See, for example: Lo YM, Patel P, Newton CR, Markham AF, Fleming KA and JS Wainscoat. (1991) Direct haplotype determination by double ARMS: specificity, sensitivity and genetic applications. Nucleic Acids Res July 1 1 ;19(13):3561-7. It is apparent that such diagnostic tests are performed after initial identification of variances within the gene, which allows selection of appropriate allele specific primers. Diagnostic genetic tests useful for practicing this invention belong to two types: genotyping tests and haplotyping tests. A genotyping test simply provides the status of a variance or variances in a subject or patient. For example suppose nucleotide 150 of hypothetical gene X on an autosomal chromosome is an adenine (A) or a guanine (G) base. The possible genotypes in any individual are AA, AG or GG at nucleotide 150 of gene X. In a haplotyping test there is at least one additional variance in gene X, say at nucleotide 810, which varies in the population as cytosine (C) or thymine (T). Thus a particular copy of gene X may have any of the following combinations of nucleotides at positions 150 and 810: 150A-810C, 150A-810T, 150G-810C or 150G-810T. Each of the four possibilities is a unique haplotype. If the two nucleotides interact in either RNA or protein, then knowing the haplotype can be important. The point of a haplotyping test is to determine the haplotypes present in a DNA or cDNA sample (e.g. from a patient). In the example provided there are only four possible haplotypes, but, depending on the number of variances in the gene and their distribution in human populations there may be three, four, five, six or more haplotypes at a given gene. The most useful haplotypes for this invention are those which occur commonly in the population being treated for a disease or condition. Preferably such haplotypes occur in at least 5% of the population, more preferably in at least 10%, still more preferably in at least 20% > of the population and most preferably in at least 30%> or more of the population. Conversely, when the goal of a pharmacogenetic program is to identify a relatively rare population that has an adverse reaction to a treatment, the most useful haplotypes may be rare haplotypes, which may occur in less than 5%, less than 2%, or even in less than 1% of the population. One skilled in the art will recognize that the frequency of the adverse reaction provides a useful guide to the likely frequency of salient causative haplotypes. Based on the identification of variances or variant forms of a gene, a diagnostic test utilizing methods known in the art can be used to determine whether a particular form of the gene, containing specific variances or haplotypes, or combinations of variances and haplotypes, is present in at least one copy, one copy, or more than one copy in an individual. Such tests are commonly performed using DNA or RNA collected from blood, cells, tissue scrapings or other cellular materials, and can be performed by a variety of methods including, but not limited to, PCR based methods, hybridization with allele-specific probes, enzymatic mutation detection, chemical cleavage of mismatches, mass spectrometry or DNA sequencing, including minisequencing. Methods for haplotyping are described above. In particular embodiments, hybridization with allele specific probes can be conducted in two formats: (1) allele specific oligonucleotides bound to a solid phase (glass, silicon, nylon membranes) and the labelled sample in solution, as in many DNA chip applications, or (2) bound sample (often cloned DNA or PCR amplified DNA) and labelled oligonucleotides in solution (either allele specific or short - e.g. 7mers or 8mers - so as to allow sequencing by hybridization). Prefened methods for diagnostic testing of variances are described in four patent applications Stanton et al, entitled A METHOD FOR ANALYZING POLYNUCLEOTIDES, serial numbers 09/394,467; 09/394,457; 09/394,774; and 09/394,387; all filed September 10, 1999. The application of such diagnostic tests is possible after identification of variances that occur in the population. Diagnostic tests may involve a panel of variances from one or more genes, often on a solid support, which enables the simultaneous determination of more than one variance in one or more genes. D. Use of Variance Status to Determine Treatment The present disclosure describes exemplary gene sequence variances in genes identified in a gene table herein (e.g., Tables 12-17 and 18-23), and variant forms of these gene that may be determined using diagnostic tests. As indicated in the Summary, such a variance-based diagnostic test can be used to determine whether or not to administer a specific drag or other treatment to a patient for treatment of a disease or condition. Preferably such diagnostic tests are incoφorated in texts such as are described in Clinical Diagnosis and Management by Laboratory Methods (19th Ed) by John B. Henry (Editor) W B Saunders Company, 1996; Clinical Laboratory Medicine : Clinical Application of Laboratory Data, (6th edition) by R. Ravel, Mosby-Year Book, 1995, or other medical textbooks including, without limitation, textbooks of medicine, laboratory medicine, therapeutics, pharmacy, pharmacology, nutrition, allopathic, homeopathic, and osteopathic medicine; preferably such a test is developed as a 'home brew' method by a certified diagnostic laboratory; most preferably such a diagnostic test is approved by regulatory authorities, e.g., by the U.S. Food and Drag Administration, and is incoφorated in the label or insert for a therapeutic compound, as well as in the Physicians Desk Reference. In such cases, the procedure for using the drag is restricted or limited on the basis of a diagnostic test for determining the presence of a variance or variant form of a gene. Alternatively the use of a genetic test may be advised as best medical practice, but not absolutely required, or it may be required in a subset of patients, e.g. those using one or more other drags, or those with impaired liver or kidney function. The procedure that is dictated or recommended based on genotype may include the route of administration of the drag, the dosage form, dosage, schedule of administration or use with other drugs; any or all of these may require selecting or determination consistent with the results of the diagnostic test or a plurality of such tests. Preferably the use of such diagnostic tests to determine the procedure for administration of a drug is incoφorated in a text such as those listed above, or medical textbooks, for example, textbooks of medicine, laboratory medicine, therapeutics, pharmacy, pharmacology, nutrition, allopathic, homeopathic, and osteopathic medicine. As previously stated, preferably such a diagnostic test or tests are required by regulatory authorities and are incoφorated in the label or insert as well as the Physicians Desk Reference. Variances and variant forms of genes useful in conjunction with treatment methods may be associated with the origin or the pathogenesis of a disease or condition. In many useful cases, the variant form of the gene is associated with a specific charactenstic of the disease or condition that is the target of a treatment, most preferably response to specific drags or other treatments. Examples of diseases or conditions ameliorable by the methods of this mvention are identified in the Examples and tables below; in general treatment of disease with current methods, particularly drag treatment, always involves some unknown element (involving efficacy or toxicity or both) that can be reduced by appropriate diagnostic methods. Alternatively, the gene is involved in drag action, and the vanant forms of the gene are associated with variability in the action of the drug. For example, in some cases, one vanant form of the gene is associated with the action of the drag such that the drug will be effective in an individual who inherits one or two copies of that form of the gene. Alternatively, a vanant form of the gene is associated with the action of the drug such that the drag will be toxic or otherwise contra-indicated in an individual who inhents one or two copies of that form of the gene. In accord with this invention, diagnostic tests for variances and vanant forms of genes as descnbed above can be used clinical trials to demonstrate the safety and efficacy of a drag in a specific population. As a result, in the case of drags which show variability in patient response conelated with the presence or absence of a vanance or variances, it is preferable that such drag is approved for sale or use by regulatory agencies with the recommendation or requirement that a diagnostic test be performed for a specific variance or vanant form of a gene which identifies specific populations in which the drag will be safe and/or effective. For example, the drag may be approved for sale or use by regulatory agencies with the specification that a diagnostic test be performed for a specific vanance or vanant form of a gene which identifies specific populations in which the drag will be toxic. Thus, approved use of the drag, or the procedure for use of the drag, can be limited by a diagnostic test for such variances or vanant forms of a gene; or such a diagnostic test may be considered good medical practice, but not absolutely required for use of the drag. As indicated, diagnostic tests for vaπances as described in this invention may be used in clinical tπals to establish the safety and efficacy of a drag. Methods for such clinical tnals are described below and/or are known in the art and are descπbed in standard textbooks. For example, diagnostic tests for a specific vanance or vanant form of a gene may be incoφorated m the clinical trial protocol as inclusion or exclusion cnteπa for enrollment in the tnal, to allocate certain patients to treatment or control groups within the clinical tnal or to assign patients to different treatment cohorts. Alternatively, diagnostic tests for specific vaπances may be performed on all patients within a clinical tnal, and statistical analysis performed companng and contrasting the efficacy or safety of a drag between individuals with different variances or variant forms of the gene or genes. Prefened embodiments involving clinical trials include the genetic stratification strategies, phases, statistical analyses, sizes, and other parameters as described herein. Similarly, diagnostic tests for variances can be performed on groups of patients known to have efficacious responses to the drag to identify differences in the frequency of variances between responders and non-responders. Likewise, in other cases, diagnostic tests for variance are performed on groups of patients known to have toxic responses to the drag to identify differences in the frequency of the variance between those having adverse events and those not having adverse events. Such outlier analyses may be particularly useful if a limited number of patient samples are available for analysis. It is apparent that such clinical trials can be or are performed after identifying specific variances or variant forms of the gene in the population. In defining outliers it is useful to examine the distribution of responses in the placebo group; outliers should preferably have responses that exceed in magnitude the extreme responses in the placebo group. The identification and confirmation of genetic variances is described in certain patents and patent applications. The description therein is useful in the identification of variances in the present invention. For example, a strategy for the development of anticancer agents having a high therapeutic index is described in Housman, International Application PCT/US94/08473 and Housman, INHIBITORS OF ALTERNATIVE ALLELES OF GENES ENCODING PROTEINS VITAL FOR CELL VIABILITY OR CELL GROWTH AS A BASIS FOR CANCER THERAPEUTIC AGENTS, U.S. Patent 5,702,890, issued December 30, 1997, which are hereby incoφorated by reference in their entireties. Also, a number of gene targets and associated variances are identified in Housman et al., PCT/US98/05419, entitled TARGET ALLELES FOR ALLELE-SPECIFIC DRUGS, filed March 19, 1998, which is hereby incoφorated by reference in its entirety, including drawings. The described approach and techniques are applicable to a variety of other diseases, conditions, and/or treatments and to genes associated with the etiology and pathogenesis of such other diseases and conditions and the efficacy and safety of such other treatments. Useful variances for this invention can be described generally as variances which partition patients into two or more groups that respond differently to a therapy (a therapeutic intervention), regardless of the reason for the difference, and regardless of whether the reason for the difference is known. III. From Variance List to Clinical Trial: Identifying Genes and Gene Variances that Account for Variable Responses to Treatment There are a variety of useful methods for identifying a subset of genes from a large set of candidate genes that should be prioritized for further investigation with respect to their influence on inter-individual variation in disease predisposition or response to a particular drag. These methods include for example, (1 ) searching the biomedical literature to identify genes relevant to a disease or the action of a drag, (2) screening the genes identified in step 1 for variances. A large set of exemplary variances are provided in Tables 12-23. Other methods include (3) using computational tools to predict the functional effects of variances in specific genes, (4) using in vitro or in vivo experiments to identify genes which may participate in the response to a drug or treatment, and to determine the variances which affect gene, RNA or protein function, and may therefore be important genetic variables affecting disease manifestations or drag response, and (5) retrospective or prospective clinical trials. Computational tools are described in U.S. Patent Application, Stanton et al., serial number, attorney docket number 241/034, filed April 26, 1999, entitled GENE SEQUENCE VARIANCES WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE, and in Stanton et al., Serial No. 09/419,705, filed October 14, 1999, entitled VARIANCE SCANNING METHOD FOR IDENTIFYING GENE SEQUENCE VARIANCES, which are hereby incoφorated by reference in their entireties, including drawings. Other methods are considered below in some detail. (1) To begin, one preferably identifies, for a given treatment, a set of candidate genes that are likely to affect disease phenotype or drag response. This can be accomplished most efficiently by first assembling the relevant medical, pharmacological and biological data from available sources (e.g., public databases and publications). One skilled in the art can review the literature (textbooks, monographs, journal articles) and online sources (databases) to identify genes most relevant to the action of a specific drag or other treatment, particularly with respect to its utility for treating a specific disease, as this beneficially allows the set of genes to be analyzed ultimately in clinical trials to be reduced from an initial large set. Specific strategies for conducting such searches are described below. In some instances the literature may provide adequate information to select genes to be studied in a clinical trial, but in other cases additional experimental investigations of the sort described below will be preferable to maximize the likelihood that the salient genes and variances are moved forward into clinical studies. Specific genes relevant to understanding inteφatient variation in response to treatments for major neurological and psychiatric diseases are listed in Tables 1-6. In Tables 7-11 prefened sets of genes for analysis of variable therapeutic response in specific diseases are highlighted. These genes are exemplary; they do not constitute a complete set of genes that may account for variation in clinical response. Experimental data are also useful in establishing a list of candidate genes, as described below. (2) Having assembled a list of candidate genes generally the second step is to screen for variances in each candidate gene. Experimental and computational methods for variance detection are described in this invention, and tables of exemplary variances are provided (Tables 12-23) as well as methods for identifying additional variances and a written description of such possible additional variances in the cDNAs of genes that may affect drag action (see Stanton et al., Application No. 09/300,747, filed April 26, 1999, entitled GENE SEQUENCE VARIANCES WITH UTILITY IN DETERMINING THE TREATMENT OF DISEASE, incoφorated in its entirety. (3) Having identified variances in candidate genes the next step is to assess their likely contribution to clinical variation in patient response to therapy, preferably by using informatics-based approaches such as DNA and protein sequence analysis and protein modeling. The literature and informatics-based approaches provide the basis for prioritization of candidate genes, however it may in some cases be desirable to further nanow the list of candidate genes, or to measure experimentally the phenotype associated with specific variances or sets of variances (e.g. haplotypes). (4) Thus, as a third step in candidate gene analysis, one skilled in the art may elect to perform in vitro or in vivo experiments to assess the functional importance of gene variances, using either biochemical or genetic tests. (Certain kinds of experiments - for example gene expression profiling and proteome analysis - may not only allow refinement of a candidate gene list but may also lead to identification of additional candidate genes.) Combination of two or all of the three above methods will provide sufficient information to nanow and prioritize the set of candidate genes and variances to a number that can be studied in a clinical trial with adequate statistical power. (5) The fourth step is to design retrospective or prospective human clinical trials to test whether the identified allelic variance, variances, or haplotypes or combination thereof influence the efficacy or toxicity profiles for a given drug or other therapeutic intervention. It should be recognized that this fourth step is the crucial step in producing the type of data that would justify introducing a diagnostic test for at least one variance into clinical use. Thus while each of the above four steps are useful in particular instances of the invention, this final step is indispensable. Further guidance and examples of how to perform these five steps are provided below. (6) A fifth (optional) step entails methods for using a genotyping test in the promotion and marketing of a treatment method. It is widely appreciated that there is a tendency in the pharmaceutical industry to develop many compounds for well established therapeutic targets. Examples include beta adrenergic blockers, hydroxymethylglutaryl (HMG) CoA reductase inhibitors (statins), dopamine D2 receptor antagonists and serotonin transporter inhibitors. Frequently the pharmacology of these compounds is quite similar in terms of efficacy and side effects. Therefore the marketing of one compound vs. other members of the class is a challenging problem for drag companies, and is reflected in the lesser success that late products typically achieve compared to the first and second approved products. It occuned to the inventors that genetic stratification can provide the basis for identifying a patient population with a superior response rate or improved safety to one member of a class of drags, and that this information can be the basis for commercialization of that compound. Such a commercialization campaign can be directed at caregivers, particularly physicians, or at patients and their families, or both. 1. Identification of Candidate Genes Relevant to the Action of a Drag Practice of this invention will often begin with identification of a specific pharmaceutical product, for example a drag, that would benefit from improved efficacy or reduced toxicity or both, and the recognition that pharmacogenetic investigations as described herein provide a basis for achieving such improved characteristics. The question then becomes which genes and variances, such as those provided in this application in Tables 1-6, 12-17, and 18-23, would be most relevant to inteφatient variation in response to the drag. As discussed above, the set of relevant genes includes both genes involved in the disease process and genes involved in the interaction of the patient and the treatment - for example genes involved in pharmacokinetic and pharmacodynamic action of a drug. The biological and biomedical literature and online databases provide useful guidance in selecting such genes. Specific guidance in the use of these resources is provided below. Revtevv t/ze literature and online sources One way to find genes that affect response to a drag in a particular disease setting is to review the published literature and available online databases regarding the pathophysiology of the disease and the pharmacology of the drag. Literature or online sources can provide specific genes involved in the disease process or drug response, or describe biochemical pathways involving multiple genes, each of which may affect the disease process or drag response. Alternatively, biochemical or pathological changes characteristic of the disease may be described; such information can be used by one skilled in the art to infer a set of genes that can account for the biochemical or pathologic changes. For example, to understand variation in response to a drag that modulates serotonin levels in a central nervous system (CNS) disorder associated with altered levels of serotonin one would preferably study, at a minimum, variances in genes responsible for serotonin biosynthesis, release from the cell, receptor binding, presynaptic reuptake, and degradation or metabolism. Genes responsible for each of these functions should be examined for variation that may account for inteφatient differences in drug response or disease manifestations. As recognized by those skilled in the art, a comprehensive list of such genes can be obtained from textbooks, monographs and the literature. There are several types of scientific information, described in some detail below, that are valuable for identifying a set of candidate genes to be investigated with respect to a specific disease and therapeutic intervention. First there is the medical literature, which provides basic information on disease pathophysiology and therapeutic interventions. A subset of this literature is devoted to specific description of pathologic conditions. Second there is the pharmacology literature, which will provide additional information on the mechanism of action of a drug (pharmacodynamics) as well as its principal routes of metabolic transformation (pharmacokinetics) and the responsible proteins. Third there is the biomedical literature (principally genetics, physiology, biochemistry and molecular biology), which provides more detailed information on metabolic pathways, protein structure and function and gene structure. Fourth, there are a variety of online databases that provide additional information on metabolic pathways, gene families, protein function and other subjects relevant to selecting a set of genes that are likely to affect the response to a treatment. Medical Literature A good starting place for information on molecular pathophysiology of a specific disease is a general medical textbook such as Harrison's Principles of Internal Medicine, 14th edition, (2 Vol Set) by A.S. Fauci, E. Braunwald, K.J. Isselbacher, et al. (editors), McGraw Hill, 1997, or Cecil Textbook of Medicine (20th Ed) by R. L. Cecil, F. Plum and J. C. Bennett (Editors) W B Saunders Co., 1996. For pediatric diseases texts such as Nelson Textbook of Pediatrics ( 15th edition) by R.E. Behrman, R.M. Kliegman, A.M. Arvin and W.E. Nelson (Editors), W B Saunders Co., 1995 or Oski's Principles and Practice of Pediatrics (3 rd Edition) by J.A. Mamillan & F.A. Oski Lippincott-Raven, 1999 are useful introductions. For obstetrical and gynecological disorders texts such as Williams Obstetrics (20th Ed) by F.G. Cunningham, N.F. Gant, P.C McDonald et al. (Editors), Appleton & Lange, 1997 provide general information on disease pathophysiology. For psychiatric disorders texts such as the Comprehensive Textbook of Psychiatry, VI (2 Vols) by H.I. Kaplan and B.J. Sadock (Editors), Lippincott, Williams & Wilkins, 1995, or The American Psychiatric Press Textbook of Psychiatry (3 rd edition) by R.E. Hales, S.C. Yudofsky and J.A. Talbott (Editors) Amer Psychiatric Press, 1999 provide an overview of disease nosology, pathophysiological mechanisms and treatment regimens. In addition to these general texts, there are a variety of more specialized medical texts that provide greater detail about specific disorders which can be utilized in developing a list of candidate genes and variances relevant to inteφatient variation in response to a treatment. For example, within the field of medicine there are standard textbooks for each of the subspecialties. Some examples include: Heart Disease: A Textbook of Cardiovascular Medicine (2 Volume set) by E. Braunwald (Editor), W B Saunders Co., 1996; Hurst's the Heart, Arteries and Veins (9th Ed) (2 Vol Set) by R.W. Alexander, R.C. Schlant, V. Fuster, W. Alexander and E.H. Sonnenblick (Editors) McGraw Hill, 1998; Principles of Neurology (6th edition) by R.D. Adams, M. Victor (editors), and A.H. Ropper (Contributor), McGraw Hill, 1996; Sleisenger & Fordtran's Gastrointestinal and Liver Disease: Pathophysiology, Diagnosis, Management (6th edition) by M. Feldman, B.F. Scharschmidt and M. Sleisenger (Editors), W B Saunders Co., 1997; Textbook of Rheumatology (5th edition) by W.N. Kelley, S. Ruddy, E.D. Harris Jr. and CB. Sledge (Editors) (2 volume set) W B Saunders Co., 1997; Williams Textbook of Endocrinology (9th edition) by J.D. Wilson, D.W. Foster, H. M. Kronenberg and Larsen (Editors), W B Saunders Co., 1998; Wintrobe's Clinical Hematology (10th Ed) by G.R. Lee, J. Foerster (Editor) and J. Lukens (Editors) (2 Volumes) Lippincott, Williams & Wilkins, 1998; Cancer: Principles & Practice of Oncology (5th edition) by V.T. Devita, S.A. Rosenberg and S. Hellman (editors), Lippincott- Raven Publishers, 1997; Principles of Pulmonary Medicine (3rd edition) by S.E. Weinberger & J Fletcher (Editors), W B Saunders Co., 1998; Diagnosis and Management of Renal Disease and Hypertension (2nd edition) by A.K. Mandal & J.C. Jennette (Editors), Carolina Academic Press, 1994.Massry & Glassock's Textbook of Nephrology (3rd edition) by S.G. Massry & R.J. Glassock (editors) Williams & Wilkins, 1995; The Management of Pain by J.J. Bonica, Lea and Febiger, 1992; Ophthalmology by M. Yanoff & J.S. Duker, Mosby Year Book, 1998; Clinical Ophthalmology: A Systemic Approach by J.J. Kanski, Butterworth- Heineman, 1994; and Essential Otolaryngology by J.K. Lee Appleton and Lange 1998. In addition to these subspecialty texts there are many textbooks and monographs that concern more restricted disease areas, or specific diseases. Such books provide more extensive coverage of pathophysiologic mechanisms and therapeutic options. The number of such books is too great to provide examples for all but a few diseases, however one skilled in the art will be able to readily identify relevant texts. One simple way to search for relevant titles is to use the search engine of an online bookseller such as http://www.amazon.com or http://www.bamesandnoble.com using the disease or drag (or the group of diseases or drags to which they belong) as search terms. For example a search for asthma would turn up titles such as Asthma : Basic Mechanisms and Clinical Management (3rd edition) by P.J. Barnes, I.W. Rodger and N.C. Thomson (Editors), Academic Press, 1998 and Airways and Vascular Remodelling in Asthma and Cardiovascular Disease : Implications for Therapeutic Intervention, by C Page & J. Black (Editors), Academic Press, 1994. Pathology Literature In addition to medical texts there are texts that specifically address disease etiology and pathologic changes associated with disease. A good general pathology text is Robbins Pathologic Basis of Disease (6th edition) by R.S. Cotran, V. Kumar, T. Collins and S.L. Robbins, W B Saunders Co., 1998. Specialized pathology texts exist for each organ system and for specific diseases, similar to medical texts. These texts are useful sources of information for one skilled in the art for developing lists of genes that may account for some of the known pathologic changes in disease tissue. Exemplary texts are as follows: Bone Manow Pathology 2 nd edition, by B.J. Bain, I. Lampert. & D. Clark, Blackwell Science, 1996; Atlas of Renal Pathology bv F.G. Silva, W.B. Saunders, 1999; Fundamentals of Toxicologic Pathology by W.M. Haschek and C.G. Rousseaux, Academic Press, 1997; Gastrointestinal Pathology by P. Chandrasoma, Appleton and Lange, 1998; Ophthalmic Pathology with Clinical Conelations by j. Sassani, Lippincott-Raven, 1997; Pathology of Bone and Joint Disorders by F. McCarthy, F.J. Frassica and A. Ross, W. B. Saunders, 1998; Pulmonary Pathology by M.A. Grippi, Lippicott-Raven, 1995; Neuropathology by D. Ellison, L. Chimelli, B. Harding, S. Love& J. Lowe, Mosby Year Book, 1997; Greenfield's Neuropatholgy 6 th edition by J.G. Greenfield, P.L. Lantos & D.I. Graham, Edward Arnold, 1997. Pharmacology, Pharmacogenetics and Pharmacy Literature There are also both general and specialized texts and monographs on pharmacology that provide data on pharmacokinetics and pharmacodynamics of drugs. The discussion of pharmacodynamics (mechanism of action of the drug) in such texts is often supported by a review of the biochemical pathway or pathways that are affected by the drag. Also, proteins related to the target protein are often listed; it is important to account for variation in such proteins as the related proteins may be involved in drag pharmacology. For example, there are 14 known serotonin receptors. Various pharmacological serotonin agonists or antagonists have different affinities for these different receptors. Variation in a specific receptor may affect the pharmacology not only of drags targeted to that receptor, but also drags that are principally agonists or antagonists of different receptors. Such compounds may produce different effects on two allelic forms of a non-targeted receptor; for example on variant form may bind the compound with higher affinity than the other, or a compound that is principally an antagonist for one allele may be a partial agonist for another allele. Thus genes encoding proteins structurally related to the target protein should be screened for variance in order to successfully realize the methods of the present invention. A good general pharmacology text is Goodman & Gilman's the Pharmacological Basis of Therapeutics (9th Ed) by J.G. Hardman, L.E. Limbird, P.B. Molinoff, R.W. Ruddon and A.G. Gilman (Editors) McGraw Hill, 1996. There are also texts that focus on the pharmacology of drags for specific disease areas, or specific classes of drags (e.g. natural products) or adverse drag interactions, among other subjects. Specific examples include: The -American Psychiatric Press Textbook of Psychopharmacology (2nd edition) by A.F. Schatzberg & CB. Nemeroff (Editors), American Psychiatric Press, 1998; and Essential Psychopharmacology : Neuroscientific Basis and Practical Applications by N. Muntner and S.M. Stahl, Cambridge Univ Press, 1996. There are also texts on pharmacogenetics which are particularly useful for identifying genes which may contribute to variable pharmacokinetic response. In addition there are texts on some of the major xenobiotic metabolizing proteins, such as the cytochrome P450 genes including Pharmacogenetics of Drag Metabolism (International Encyclopedia of Pharmacology and Therapeutics) by Werner Kalow (Editor) Pergamon Press, 1992; Genetic Factors in Drag Therapy : Clinical and Molecular Pharmacogenetics by D.A Price Evans, Cambridge Univ Press, 1993; Pharmacogenetics (Oxford Monographs on Medical Genetics, 32) by W.W. Weber, Oxford Univ Press, 1997; Cytochrome P450 : Structure. Mechanism, and Biochemistry by P.R. Ortiz de Montellano (Editor), Plenum Publishing Coφ, 1995; and Appleton & Lange's Review of Pharmacy, 6 th edition, (Appleton & Lange's Review Series) by G.D. Hall & B.S. Reiss, Appleton & Lange, 1997. Genetics, Biochemistry and Molecular Biology Literature In addition to the medical, pathology, and pharmacology texts listed above there are several information sources that one skilled in the art will turn to for information on the genetic, physiologic, biochemical, and molecular biological aspects of the disease, disorder or condition or the effect of the therapeutic intervention on specific physiologic processes. The biomedical literature may include information on nonhuman organisms that is relevant to understanding the likely disease or pharmacological pathways in man. Also provided below are illustrative texts which will aid in the identification of a pathway or pathways, and a gene or genes that may be relevant to interindividual variation in response to a therapy. Textbooks of biochemistry, genetics and physiology are often useful sources for such pathway information. In order to ascertain the appropriate methods to analyze the effects of an alleleic variance, variances, or haplotypes in vitro, one skilled in the art will review existing information on molecular biology, cell biology, genetics, biochemistry; and physiology. Such texts are useful sources for general and specific information on the genetic and biochemical processes involved in disease and in drag action, as well as experimental procedures that may be useful in performing in vitro research on an allelic variance, variances, or haplotye. Texts on gene structure and function and RNA biochemistry will be useful in evaluating the consequences of variances that do not change the coding sequence (silent variances). Such variances may alter the interaction of RNA with proteins or other regulatory molecules affecting RNA processing, polyadenylation, or export. Molecular and Cellular Biology Molecular Cell Biology by H. Lodish, D. Baltimore, A. Berk, L. Zipurksy & J. Darnell, W H Freeman & Co., 1995; Essentials of Molecular Biology, D. Freifelder and Malacinski, Jones and Bartlett, 1993; Genes and Genomes: A Changing Perspective, M. Singer and P. Berg, University Science Books, 1991 ; Gene Structure and Expression, J.D. Hawkins, 1996. Cambridge University Press; Molecular Biology of the Cell, 2nd edition, B. Alberts et al., Garland Publishing, 1994. Molecular Genetics The Metabolic and Molecular Bases of Inherited Disease by C R. Scriver, A.L. Beaudet, W.S. Sly (Editors), 7th edition, McGraw Hill, 1995; Genetics and Molecular Biology, R. Schleif, 1994. 2nd edition, Johns Hopkins University Press; Genetics, P.J. Russell, 1996. 4th edition, Haφer Collins; An Introduction to Genetic Analysis, Griffiths et al.1993. 5th edition, W.H. Freeman and Company; Understanding Genetics: A molecular approach, Rothwell, 1993. Wiley-Liss General Biochemistry Biochemistry, L. Stryer, 1995. W.H. Freeman and Company; Biochemistry, D. Voet and J.G. Voet, 1995. John Wiley and Sons; Principles of Biochemistry, A.L. Lehninger, D.L. Nelson, and M.M. Cox, 1993. Worth Publishers; Biochemistry, G. Zubay, 1998. Wm. C Brown Communications; Biochemistry, C.K. Mathews and K.E. van Holde, 1990. Benjamin/Cummings Transcription Eukaryotic Transcriptiuon Factors, D.S. Latchman, 1995. Academic Press; Eukaryotic Gene Transcription, S. Goodbourn (ed.), 1996. Oxford University Press; Transcription Factors and DNA Replication, D.S. Pederson and N.H. Heintz, 1994. CRC Press/R.G. Landes Company; Transcriptional Regulation, S.L. McKnight and K. Yamamoto (eds.), 1992. 2 volumes, Cold Spring Harbor Laboratory Press RNA Control of Messenger RNA Stability, J. Belasco and G. Brawerman (eds.), 1993. Academic Press; RNA-Protein Interactions. Nagai and Mattaj (eds.), 1994. Oxford University Press; mRNA Metabolism and Post-transcriptional Gene Regulation. Harford and Morris (eds.), 1997. Wiley-Liss. Translation Translational Control, J.W.B. Hershey, M.B. Mathews, and N. Sonenberg (eds.), 1995. Cold Spring Harbor Laboratory Press General Physiology Textbook of Medical Physiology 9 th Edtion by A.C Guyton and J.E. Hall W.B. Saunders, 1997; Review of Medical Physiology, 18 th Edition by W.F. Ganong, Appleton and Lange, 1997. Online Databases Those skilled in the art are familiar with how to search the biomedical literature, such as, e.g., libraries, online PubMed, abstract listings, and online mutation databases. One particularly useful resource is maintained at the web site of the National Center for Biotechnology Information (ncbi): http://www.ncbi.nlm.nih.gov/. From the ncbi site one can access Online Mendelian Inheritance in Man (OMIM),. OMIM can be found at: http://www3.ncbi.nlm.nih.gov/Omim/searchomim.html. OMIM is a medically oriented database of genetic information with entries for thousands of genes. The OMIM record number is provided for many of the genes in Tables 1-6 and 12-23 (see column 3), and constitutes an excellent entry point for identification of references that point to the broader literature. Another useful site at NCBI is the Entrez browser, located at http://www3. ncbi.nlm.nih.gov/Entrez/. One can search genomes, polynucleotides, proteins, 3D structures, taxonomy or the biomedical literature (PubMed) via the Entrez site. More generally links to a number of useful sites with biomedical or genetic data are maintained at sites such as Med Web at the Emory University Health Sciences Center Library: http://WWW.MedWeb.Emory.Edu MedWeb/; Riken, a Japanese web site at: http://www.rtc.riken.go.ip/othersite.html with links to DNA sequence, structural, molecular biology, bioinformatics, and other databases; at the Oak Ridge National Laboratory web site: http://www.oml.gov/hgmis/links.html; or at the Yahoo website of Diseases and Conditions: http://dir.vahoo.com/healtli/diseases and conditions/index.html. Each of the indicated web sites has additional useful links to other sites. Another type of database with utility in selecting the genes on a biochemical pathway that may affect the response to a drug are databases that provide information on biochemical pathways. Examples of such databases include the Kyoto Encyclopedia of Genes and Genomes (KEGG), which can be found at http://vvww genome.ad.ip/kegg/kegg html. This site has pictures of many biochemical pathways, as well as links to other metabolic databases such as the well known Boehπnger Mannheim biochemical pathways charts: http:/ ''www e pasy cli/cgi-bm search-biochem-index. The metabolic charts at the latter site are comprehensive, and excellent starting points for working out the salient enzymes on any given pathway. Each of the web sites mentioned above has links to other useful web sites, which in turn can lead to additionai sites with useful information.Re-seαrc/z Libraries Those skilled in the art will often require information found only at large libraπes. The National Library of Medicine (http 7. www.nlm.nih.gov/) is the largest medical library in the world and its catalogs can be searched online. Other hbranes, such as university or medical school libraπes are also useful to conduct searches. Biomedical books such as those refened to above can often be obtained from online bookstores as described above. Biomedical Literature To obtain up to date information on drags and their mechanism of action and biotransformation; disease pathophysiology, biochemical pathways relevant to drag action and disease pathophysiology; and genes that encode proteins relevant to drag action and disease one skilled in the art will consult the biomedical literature . A widely used, publically accessible web site for searching published journal articles is PubMed (http-// www ncbi.nlm.nih.gov/PubMedQ. At this site, one can search for the most recent articles (within the last 1-2 months) or older literature (back to 1966). Many Journals also have their own sites on the world wide web and can be searched online. For example see the IDEAL web site at: http • //www apnet.com/www/ap/aboutid.html This site is an online library, featuπng full text journals from Academic Press and selected journals from W B. Saunders and Churchill Livingstone. The site provides access (for a fee) to nearly 2000 scientific, technical, and medical journals Experimental methods for identification of genes involved in the action of a drug There are a number of experimental methods for identifying genes and gene products that mediate or modulate the effects of a drag or other treatment. They encompass analyses of RNA and protein expression as well as methods for detecting protein - protein interactions and protein - ligand interactions. Two prefened experimental methods for identification of genes that may be involved in the action of a drag are (1 ) methods for measuring the expression levels of many mRNA transcripts in cells or organisms treated with the drag (2) methods for measuring the expression levels of many proteins in cells or organisms treated with the drag. RNA transcripts or proteins that are substantially increased or decreased in drag treated cells or tissues relative to control cells or tissues are candidates for mediating the action of the drag. Preferably the level of an mRNA is at least 30% higher or lower in drag treated cells, more preferably at least 50%> higher or lower, and most preferably two fold higher or lower than levels in non-drag treated control cells. The analysis of RNA levels can be performed on total RNA or on polyadenylated RNA selected by oligodT affinity. Further, RNA from different cell compartments can be analyzed independently - for example nuclear vs. cytoplasmic RNA. In addition to RNA levels, RNA kinetics can be examined, or the pool of RNAs cunently being translated can be analyzed by isolation of RNA from polysomes. Other useful experimental methods include protein interaction methods such as the yeast two hybrid system and variants thereof which facilitate the detection of protein - protein interactions. Preferably one of the interacting proteins is the drag target or another protein strongly implicated in the action of the compound being assessed. The pool of RNAs expressed in a cell is sometimes refened to as the transcriptome. Methods for measuring the transcriptome, or some part of it, are known in the art. A recent collection of articles summarizing some cunent methods appeared as a supplement to the journal Nature Genetics. (The Chipping Forecast. Nature Genetics supplement, volume 21, January 1999.) A preferred method for measuring expression levels of mRNAs is to spot PCR products conesponding to a large number of specific genes on a nylon membrane such as Hybond N Plus (Amersham-Pharmacia). Total cellular mRNA is then isolated, labelled by random oligonucleotide priming in the presence of a detectable label (e.g. alpha 33P labelled radionucleotides or dye labelled nucleotides), and hybridized with the filter containing the PCR products. The resulting signals can be analyzed by commercially available software, such as can be obtained from Clontech/Molecular Dynamics or Research Genetics, Inc. Experiments have been described in model systems that demonstrate the utility of measuring changes in the transcriptome before before and after changing the growth conditions of cells, for example by changing the nutrient environment. The changes in gene expression help reveal the network of genes that mediate physiological responses to the altered growth condition. Similarly, the addition of a drag to the cellular or in vivo environment, followed by monitoring the changes in gene expression can aid in identification of gene networks that mediate pharmacological responses. The pool of proteins expressed in a cell is sometimes refened to as the proteome. Studies of the proteome may include not only protein abundance but also protein subcellular localization and protein-protein interaction. Methods for measuring the proteome, or some part of it, are known in the art. One widely used method is to extract total cellular protein and separate it in two dimensions, for example first by size and then by isoelectric point. The resulting protein spots can be stained and quantitated, and individual spots can be excised and analyzed by mass spectrometry to provide definitive identification. The results can be compared from two or more cell lines or tissues, at least one of which has been treated with a drag. The differential up or down modulation of specific proteins in response to drag treatment may indicate their role in mediating the pharmacologic actions of the drag. Another way to identify the network of proteins that mediate the actions of a drag is to exploit methods for identifying interacting proteins. By starting with a protein known to be involved in the action of a drag - for example the drag target - one can use systems such as the yeast two hybrid system and variants thereof (known to those skilled in the art; see Ausubel et al., Cunent Protocols in Molecular Biology, op. cit.) to identify additional proteins in the network of proteins that mediate drug action. The genes encoding such proteins would be useful for screening for DNA sequence variances, which in turn may be useful for analysis of inteφatient variation in response to treatments. For example, the protein 5- lipoxygenase (5LO) is an enzyme which is at the beginning of the leukotriene biosynthetic pathway and is a target for anti-inflammatory drags used to treat asthma and other diseases. In order to detect proteins that interact with 5 -lipoxygenase the two-hybrid system was recently used to isolate three different proteins, none previously known to interact with 5LO. (Provost et al., Interaction of 5- lipoxygenase with cellular proteins. Proc. Natl. Acad. Sci. U.S.A. 96: 1881-1885, 1999.) A recent collection of articles summarizing some cunent methods in proteomics appeared in the August 1998 issue of the journal Electrophoresis (volume 19, number 1 1). Other useful articles include: Blackstock WP, et al. Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol. 17 (3): p. 121-7, 1999, and Patton W.F., Proteome analysis II. Protein subcellular redistribution: linking physiology to genomics via the proteome and separation technologies involved. J Chromatogr B Biomed Sci App. 722(1 -2):203- 23. 1999. Since many of these methods can also be used to assess whether specific polymoφhisms are likely to have biological effects, they are also relevant in section 3, below, concerning methods for assessing the likely contribution of variances in candidate genes to clinical variation in patient responses to therapy. 2. Screen for Variances in Genes that may be Related to Therapeutic Response Having identified a set of genes that may affect response to a drag the next step is to screen the genes for variances that may account for interindividual variation in response to the drug. There are a variety of levels at which a gene can be screened for variances, and a variety of methods for variance screening. The two main levels of variance screening are genomic DNA screening and cDNA screening. Genomic variance detection may include screening the entire genomic segment spanning the gene from 2 kb to 10 kb upstream of the transcription start site to the polyadenylation site, or 2 to 10 kb beyond the polyadenylation site. Alternatively genomic variance detection may (for intron containing genes) include the exons and some region around them containing the splicing signals, for example, but not all of the intronic sequences. In addition to screening introns and exons for variances it is generally desirable to screen regulatory DNA sequences for variances. Promoter, enhancer, silencer and other regulatory elements have been described in human genes. The promoter is generally proximal to the transcription start site, although there may be several promoters and several transcription start sites. Enhancer, silencer and other regulatory elements may be intragenic or may lie outside the introns and exons, possibly at a considerable distance, such as 100 kb away. Variances in such sequences may affect basal gene expression or regulation of gene expression. In either case such variation may affect the response of an individual patient to a therapeutic intervention, for example a drug, as described in the examples. Thus in practicing the present invention it is useful to screen regulatory sequences as well as transcribed sequences, in order to identify variances that may affect gene transcription. Frequently the genomic sequence of a gene can be found in the sources above, particularly by searching GenBank or Medline (PubMed). The name of the gene can be entered at a site such as Entrez: http://www.ncbi.nlm.nih.gov/Entrez/nucleotide.html. Using the genomic sequence and information from the biomedical literature one skilled in the art can perform a variance detection procedure such as those described in examples 2, 3, 4. Variance detection is often first performed on the cDNA of a gene for several reasons. First, available data on functional sequence variances suggests that variances in the transcribed portion of a gene may be most likely to have functional consequences as they can affect the interaction of the transcript with a wide variety of cellular factors during the complex processes of RNA transcription, processing and translation, with consequent effects on RNA splicing, stability, translational efficiency or other processes. Second, as a practical matter the cDNA sequence of a gene is often available before the genomic stmcture is known, although the reverse will be tme in the future as the sequence of the human genome is determined. Third, the cDNA is often compact compared to the genomic locus, and can be screened for variances with much less effort. If the genomic stmcture is not known then only the cDNA seqence can be scanned for variances. Methods for preparing cDNA are described in Example 1. Methods for variance detection on cDNA are described below and in the examples. In general it is preferable to catalog genetic variation at the genomic DNA level because there are an increasing number of well documented instances of functionally important variances that lie outside of transcribed sequence. Also, to properly use optimal genetic methods to assess the contribution of a candidate gene to variation in a phenotype of interest it is desirable to understand the character of sequence variation in the candidate gene: what is the nature of linkage disequilibrium between different variances in the gene; are there sites of recombination within the gene; what is the extent of homoplasy in the gene (i.e. occurance of two variant sites that are identical by state but not identical by descent because the same variance arose at least twice in human evolutionary history on two different haplotypes); what are the different haplotypes and how can they be grouped to increase the power of genetic analysis? Methods for variance screening have been described, including DNA sequencing. See for example: US5698400: Detection of mutation by resolvase cleavage; US5217863: Detection of mutations in nucleic acids; and US5750335: Screening for genetic variation, as well as the examples and references cited therein for examples of useful variance detection procedures. Detailed variance detection procedures are also described in examples 2, 3, 4. One skilled in the art will recognize that depending on the specific aims of a variance detection project (number of genes being screened, number of individuals being screened, total length of DNA being screened) one of the above cited methods may be preferable to the others, or yet another procedure may be optimal. A prefened method of variance detection is chain terminating DNA sequencing using dye labeled primers, cycle sequencing and software for assessing the quality of the DNA sequence as well as specialized software for calling heterozygotes. The use of such procedures has been described by Nickerson and colleagues. See for example: Rieder M.J., et al. Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 26 (4):967-73, 1998, and: Nickerson D.A., et al. PolyPhred: automating the detection and genotyping of single nucleotide substitutions using fluorescence-based resequencing. Nucleic Acids Res. 25 (14):2745-51, 1997. Although the variances provided in Tables 12-17, and 18-23 consist principally of cDNA variances, it is an aspect of this invention that detection of genomic variances is also a useful method for identification of variances that may account for inteφatient variation in response to a therapy. Another important aspect of variance detection is the use of DNA from a panel of human subjects that represents a known population. For example, if the subjects are being screened for variances relevant to a specific drug development program it is desirable to include both subjects with the target disease and healthy subjects in the panel, because certain variances may occur at different frequencies in the healthy and disease populations and can only be reliably detected by screening both populations. Also, for example, if the drag development program is taking place in Japan, it is important to include Japanese individuals in the screening population. In general, it is always desirable to include subjects of known geographic, racial or ethnic identity in a variance screening experiment so the results can be inteφreted appropriately for different patient populations, if necessary. Also, in order to select optimal sets of variances for genetic analysis of a gene locus it is desirable to know which variances have occuned recently - perhaps on multiple different chromosomes - and which are ancient. Inclusion of one or more apes or monkees in the variance screening panel is one way of gaining insight into the evolutionary history of variances. Chimpanzees are prefened subjects for inclusion in a variance screening panel. 3. Assess the Likely Contribution of Variances in Candidate Genes to Clinical Variation in Patient Responses to Therapy Once a set of genes likely to affect disease pathophysiology or drag action has been identified, and those genes have been screened for variances, said variances (e.g., provided in Tables 12-17, and 18-23) can be assessed for their contribution to variation in the pharmacological or toxicological phenotypes of interest. Such studies are useful for reducing a large number of candidate variances to a smaller number of variances to be tested in clinical trials. There are several methods which can be used in the present invention for assessing the medical and pharmaceutical implications of a DNA sequence variance. They range from computational methods to in vitro and/or in vivo experimental methods, to prospective human clinical trials, and also include a variety of other laboratory and clinical measures that can provide evidence of the medical consequences of a variance. In general, human clinical trials constitute the highest standard of proof that a variance or set of variances is useful for selecting a method of treatment, however, computational and in vitro data, or retrospective analysis of human clinical data may provide strong evidence that a particular variance will affect response to a given therapy, often at lower cost and in less time than a prospective clinical trial. Moreover, at an early stage in the analysis when there are many possible hypotheses to explain inteφatient variation in treatment response, the use of informatics-based approaches to evaluate the likely functional effects of specific variances is an efficient way to proceed. Informatics-based approaches to the prediction of the likely functional effects of variances include DNA and protein sequence analysis (phylogenetic approaches and motif searching) and protein modeling (based on coordinates in the protein database, or pdb; see http://www.rcsb.org/pdb/). See, for example: Kawabata et al. The Protein Mutant Database. Nucleic Acids Research 27: 355-357, 1999; also available at: http://pmd.ddbi.nig.ac.jp. Such analyses can be performed quickly and inexpensively, and the results may allow selection of certain genes for more extensive in vitro or in vivo studies or for more variance detection or both. The three dimensional stracture of many medically and pharmaceutically important proteins, or homologs of such proteins in other species, or examples of domains present in such proteins, is known as a result of x-ray crystallography studies and, increasingly, nuclear magnetic resonance studies. Further, there are increasingly powerful tools for modeling the stracture of proteins with unsolved stracture, particularly if there is a related (homologous) protein with known stracture. (For reviews see: Rost et al., Protein fold recognition by prediction-based threading, J. Mol. Biol. 270:471-480, 1997; Firestine et al., Threading your way to protein function, Chem. Biol. 3:779-783, 1996) There are also powerful methods for identifying conserved domains and vital amino acid residues of proteins of unknown stracture by analysis of phylogenetic relationships. (Deleage et al., Protein stracture prediction: Implications for the biologist, Biochimie 79:681-686, 1997; Taylor et al., Multiple protein stracture alignment, Protein Sci. 3: 1858-1870, 1994) These methods can permit the prediction of functionally important variances, either on the basis of stracture or evolutionary conservation. For example, a crystal structure can reveal which amino acids comprise a small molecule binding site. The identification of a polymoφhic amino acid variance in the topological neighborhood of such a site, and, in particular, the demonstration that at least one variant form of the protein has a variant amino acid which impinges on (or which may otherwise affect the chemical environment around) the small molecule binding pocket differently from another variant form, provides strong evidence that the variance may affect the function of the protein. From this it follows that the interaction of the protein with a treatment method, such an administered compound, will likely be variable between different patients. One skilled in the art will recognize that the application of computational tools to the identification of functionally consequential variances involves applying the knowledge and tools of medicinal chemistry and physiology to the analysis. Phylogenetic approaches to understanding sequence variation are also useful. Thus if a sequence variance occurs at a nucleotide or encoded amino acid residue where there is usually little or no variation in homologs of the protein of interest from non-human species, particularly evolutionarily remote species, then the variance is more likely to affect function of the RNA or protein. Computational methods for phylogenetic analysis are known in the art, (see below for citations of some methods). Computational methods are also useful for analyzing DNA polymoφhisms in transcriptional regulatory sequences, including promoters and enhancers. One useful approach is to compare variances in potential or proven transcriptional regulatory sequences to a catalog of all known transcriptional regulatory sequences, including consensus binding domains for all transcription factor binding domains. See, for example, the databases cited in: Burks, C. Molecular Biology Database List. Nucleic Acids Research 27: 1-9, 1999, and links to useful databases on the internet at: http://www.oup.co.uk/nar/Nolume 27/issue 01/summary/gkcl 05 gml.html. In particular see the Transcription Factor Database (Heinemeyer, T., et al. (1999) Expanding the TRANSFAC database towards an expert system of regulatory molecular mechanisms. Nucleic Acids Res. 27: 318-322, or on the internet at: http://193.175.244.40/TRANSFAC/index.html). Any sequence variances in transcriptional regulatory sequences can be assessed for their effects on mRNA levels using standard methods, either by making plasmid constructs with the different allelic forms of the sequence, transfecting them into cells and measuring the output of a reporter transcript, or by assays of cells with different endogenous alleles of variances. One example of a polymoφhism in a transcriptional regulatory element that has a pharmacogenetic effect is described by Drazen et al. ( 1999) Pharmacogenetic association between ALOX5 promoter genotype and the response to anti-asthma treatment. Nature Genetics 22: 168-170. Drazen and co-workers found that a polymoφhism in an Spl -transcription factor binding domain, which varied among subjects from 3-6 tandem copies, accounted for varied expression levels of the 5-lipoxygenase gene when assayed in vitro in reporter construct assays. This effect would have been flagged by an informatics analysis that surveyed the 5- lipoxygenase candidate promoter region for transcriptional regulatory sequences (resulting in discovery of polymoφhism in the Spl motif). 4. Perform in vitro or in vivo Experiments to Assess the Functional Importance of Gene Variances There are two broad types of studies useful for assessing the likely importance of variances: analysis of RNA or protein abundance (as described above in the context of methods for identifying candidate genes for explaining inteφatient variation in treatment response) or analysis of functional differences in different variant forms of a gene, mRNA or protein. Studies of functional differences may involve direct measurements of biochemical activity of different variant forms of an mRNA or protein, or may involve assaying the influence of a variance or variances on various cell properties, including both tissue culture and in vivo studies. The selection of an appropriate experimental program for testing the medical consequences of a variance may differ depending on the nature of the vanance, the gene, and the disease. For example if there is already evidence that a protein is involved in the pharmacologic action of a dmg, then the in vitro or in vivo demonstration that an amino acid variance in the protein affects its biochemical activity is strong evidence that the variance will have an effect on the pharmacology of the drag in patients, and therefore that patients with different variant forms of the gene may have different responses to the same dose of drag. If the variance is silent with respect to protein coding information, or if it lies in a noncoding portion of the gene (e.g., a promoter, an intron, or a 5'- or 3 '-untranslated region) then the appropriate biochemical assay may be to assess mRNA abundance, half life, or translational efficiency. If, on the other hand, there is no substantial evidence that the protein encoded by a particular gene is relevant to dmg pharmacology, but instead is a candidate gene on account of its involvement in disease pathophysiology, then the optimal test may be a clinical study addressing whether two patient groups distinguished on the basis of the variance respond differently to a therapeutic intervention. This approach reflects the cunent reality that biologists do not sufficiently understand gene regulation, gene expression and gene function to consistently make accurate inferences about the consequences of DNA sequence variances for pharmacological responses. In summary, if there is a plausible hypothesis regarding the effect of a protein on the action of a drag, then in vitro and in vivo approaches, including those described below, will be useful to predict whether a given variance is therapeutically consequential. If, on the other hand, there is no evidence of such an effect, then the prefened test is an empirical clinical measure of the impact to the variance on efficacy or toxicity in vivo (which requires no evidence or assumptions regarding the mechanism by which the variance may exert an effect on a therapeutic response). However, given the expense and statistical constraints of clinical trials, it is preferable to limit clinical testing to variances for which there is at least some experimental or computational evidence of a functional effect. Experimental Methods: Genomic DNA Analysis Variances in DNA may affect the basal transcription or regulated transcription of a gene locus. Such variances may be located in any part of the gene but are most likely to be located in the promoter region, the first intron, or in 5' or 3' flanking DNA, where enhancer or silencer elements may be located. Methods for analyzing transcription are well known to those skilled in the art and exemplary methods are briefly described above and in some of the texts cited elsewhere in this application. Transcriptional run off assay is one useful method. Detailed protocols can be found in texts such as: Cunent Protocols in Molecular Biology edited by: F.M. Ausubel, et al. John Wiley & Sons, Inc, 1999, or: Molecular Cloning: A Laboratory Manual by J. Sambrook, E.F. Fritsch and T Maniatis. 1989. 3 vols, 2nd edition, Cold Spring Harbor Laboratory Press Experimental Methods: RNA Analysis RNA variances may affect a wide range of processes including RNA splicing, polyadenylation, capping, export from the nucleus, interaction with translation intiation, elongation or termination factors, or the ribosome, or interaction with cellular factors including regulatory proteins, or factors that may affect mRNA half life. However, the effect of most RNA sequence variances on RNA function, if any, should ultimately be measurable as an effect on RNA or protein levels - either basal levels or regulated levels or levels in some abnormal cell state, such as cells from patients with a disease. Therefore, one prefened method for assessing the effect of RNA variances on RNA function is to measure the levels of RNA produced by different alleles in one or more conditions of cell or tissue growth. Said measuring can be done by conventional methods such as Northern blots or RNAase protection assays (kits available from Ambion, Inc.), or by methods such as the Taqman assay (developed by the Applied Biosystems Division of the Perkin Elmer Coφoration), or by using anays of oligonucleotides or anays of cDNAs attached to solid surfaces. Systems for anaying cDNAs are available commercially from companies such as Nanogen and General Scanning. Complete systems for gene expression analysis are available from companies such as Molecular Dynamics. For recent reviews of systems for high throughput RNA expression analysis see the supplement to volume 21 of Nature Genetics entitled "The Chipping Forecast", especially articles beginning on pages 9, 15, 20 and 25. Additional methods for analyzing the effect of variances on RNA include secondary structure probing, and direct measurement of half life or turnover. Secondary stracture can be determined by techniques such as enzymatic probing (using enzymes such as Tl , T2 and SI nuclease), chemical probing or RNAase H probing using oligonucleotides. Most RNA structural assays are performed in vitro, however some techniques can be performed on cell extracts or even in living cells, using fluorescence resonance energy transfer to monitor the state of RNA probe molecules. Experimental Methods: Protein Analysis There are a variety of experimental methods for investigating the effect of an amino acid variance on response of a patient to a treatment. The prefened method will depend on the availability of cells expressing a particular protein, and the feasibility of a cell-based assay vs. assays on cell extracts, on proteins produced in a foreign host, or on proteins prepared by in vitro translation. For example, the methods and systems listed below can be utilized to demonstrate differential expression, stability and/or activity of different variant forms of a protein, or in phenotype/genotype conelations in a model system. For the determination of protein levels or protein activity a variety of techniques are available. The in vitro protein activity can be determined by transcription or translation in bacteria, yeast, baculovirus, COS cells (transient), Chinese Hamster Ovary (CHO) cells, or studied directly in human cells, or other cell systems can be used. Further, one can perform pulse chase experiments to determine if there are changes in protein stability (half-life). One skilled in the art can construct cell based assays of protein function, and then perform the assays in cells with different genotypes or haplotypes. For example, identification of cells with different genotypes, e.g.cell lines established from families and subsequent determination of relevant protein phenotypes (e.g expression levels, post translational modifications, activity assays) may be performed using standard methods. Assays of protein levels or function can also be performed on cell lines (or extracts from cell lines) derived from pedigrees in order to determine whether there is a genetic component to variation in protein levels or function. The experimental analysis is as above for RNAs, except the assays are different. Experiments can be performed on naive cells or on cells subjected to various treatments, including pharmacological treatments. In another approach to the study of amino acid variances one can express genes conesponding to different alleles in experimental organisms and examine effects on disease phenotype (if relevant in the animal model), or on response to the presence of a compound. Such experiments may be performed in animals that have dismpted copies of the homologous gene (e.g. gene knockout animals engineered to be deficient in a target gene), or variant forms of the human gene may be introduced into germ cells by transgenic methods, or a combination of approaches may be used. To create animal strains with targeted gene disruptions a DNA construct is created (using DNA sequence information from the host animal) that will undergo homologous recombination when inserted into the nucleus of an embryonic stem cell. The targeted gene is effectively inactivated due to the insertion of non-natural sequence - for example a translation stop codon or a marker gene sequence that interrupts the reading frame. Well known PCR based methods are then used to screen for those cells in which the desired homologous recombination event has occuned. Gene knockouts can be accomplished in worms, drosophila, mice or other organisms. Once the knockout cells are created (in whatever species) the candidate therapeutic intervention can be administered to the animal and pharmacological or biological responses measured, including gene expression levels. If variant forms of the gene are useful in explaining inteφatient variation in reponse to the compound in man, then complete absence of the gene in an experimental organism should have a major effect on drag response. As a next step various human forms of the gene can be introduced into the knockout organism (a technique sometimes refened to as a knock-in). Again, pharmacological studies can be performed to assess the impact of different human variances on drag response. Methods relevant to the experimental approaches described above can be found in the following exemplary texts: General Molecular Biology Methods Molecular Biology: A project approach, S.J. Karcher, Fall 1995. Academic Press; DNA Cloning: A Practical Approach, D.M. Glover and B.D. Hayes (eds). 1995. IRL/Oxford University Press. Vol. 1 - Core Techniques; Vol 2 - Expression Systems; Vol. 3 - Complex Genomes; Vol. 4 -Mammalian Systems; Short Protocols in Molecular Biology. Ausubel et al. October 1995. 3rd edition, John Wiley and Sons; Cunent Protocols in Molecular Biology Edited by: F.M. Ausubel, R.Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, K. Strahl, (Series Editior: V.B. Chanda), 1988; Molecular Cloning: A laboratory manual, J. Sambrook, E.F. Fritsch. 1989. 3 vols, 2nd edition, Cold Spring Harbor Laboratory Press. Polymerase chain reaction (PCR) PCR Primer: A laboratory manual, C.W. Diffenbach and G.S. Dveksler (eds.). 1995. Cold Spring Harbor Laboratory Press; The Polymerase Chain Reaction, K.B. Mullis et al. (eds.), 1994. Birkhauser; PCR Strategies. M.A. Innis, D.H. Gelf, and J.J. Sninsky (eds.), 1995. Academic Press. General procedures for discipline specific studies Cunent Protocols in Neuroscience Edited by: J. Crawley, C. Gerfen, R. McKay, M. Rogawski, D. Sibley, P. Skolnick, (Series Editor: G. Taylor), 1997; Cunent Protocols in Pharmacology Edited by: S. J. Enna / M. Williams, J.W. Ferkany, T. Kenakin, R.E. Porsolt, J.P. Sullivan, (Series Editor: G. Taylor), 1998; Cunent Protocols in Protein Science Edited by: J.E. Coligan, B.M. Dunn, H.L. Ploegh, D.W. Speicher, P.T. Wingfield, (Series Editor: Virginia Benson Chanda), 1995; Cunent Protocols in Cell Biology Edited by: J.S. Bonifacino, M. Dasso, J. Lippincott-Schwartz, J.B. Harford, K.M. Yamada, (Series Editor: K. Morgan) 1999; Cunent Protocols in Cytometry Managing Editor: J.P. Robinson, Z. Darzynkiewicz (ed) / P. Dean (ed), A. Orfao (ed), P. Rabinovitch (ed), C. Stewart (ed), H. Tanke (ed), L. Wheeless (ed), (Series Editor: J. Paul Robinson), 1997; Cunent Protocols in Human Genetics Edited by: N.C Dracopoli, J.L. Haines, B.R. Korf, et al., (Series Editor: A. Boyle), 1994; Current Protocols in Immunology Edited by: J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, (Series Editor: R. Coico), 1991. IV. Clinical Trials A clinical trial is the definitive test of the utility of a variance or variances for the selection of optimal therapy. A clinical trial in which an interaction of gene variances and clinical outcomes (desired or undesired) is explored will be refened to herein as a "pharmacogenetic clinical trial". Pharmacogenetic clinical trials require no knowledge of the biological function of the gene containing the variance or variances to be assessed, nor any knowledge of how the therapeutic intervention to be assessed works at a biochemical level. The pharmacogenetics effects of a variance can be addressed at a purely statistical level: either a particular variance or set of variances is consistently associated with a significant difference in a salient dmg response parameter (e.g. response rate, effective dose, side effect rate, etc.) or not. On the other hand, if there is information about either the biochemical basis of a therapeutic intervention or the biochemical effects of a variance, then a pharmacogenetic clinical trial can be designed to test a specific hypothesis. In prefened embodiments of the methods of this application the mechanism of action of the compound to be genetically analyzed is at least partially understood. Methods for performing clinical trials are well known in the art. (see e.g. Guide to Clinical Trials by Bert Spilker, Raven Press, 1991 ; The Randomized Clinical Trial and Therapeutic Decisions by Niels Tygstmp (Editor), Marcel Dekker; Recent Advances in Clinical Trial Design and Analysis (Cancer Treatment and Research, Ctar 75) by Peter F. Thall (Editor) Kluwer Academic Pub, 1995. Clinical Trials: A Methodologic Perspective by Steven Piantadosi, Wiley Series in Probability and Statistics, 1997). However, performing a clinical trial to test the genetic contribution to inteφatient variation in drag response entails additional design considerations, including (i) defining the genetic hypothesis or hypotheses, (ii) devising an analytical strategy for testing the hypothesis, including determination of how many patients will need to be enrolled to have adequate statistical power to measure an effect of a specified magnitude (power analysis), (iii) definition of any primary or secondary genetic endpoints, and (iv) definition of methods of statistical genetic analysis, as well as other aspects. In the outline below some of the major types of genetic hypothesis testing, power analysis and statistical testing and their application in different stages of the drag development process are reviewed. One skilled in the art will recognize that certain of the methods will be best suited to specific clinical situations, and that additional methods are known and can be used in particular instances. A. Performing a Clinical Trial: Overview As used herein, a "clinical trial" is the testing of a therapeutic intervention in a volunteer human population for the puφose of determining whether it is safe and/or efficacious in the treatment of a disease, disorder, or condition. The present invention describes methods for achieving superior efficacy and/or safety in a genetically defined subgroup defined by the presence or absence of at least one gene sequence variance, compared to the effect that could be obtained in a conventional trial (without genetic stratification). A "clinical study" is that part of a clinical trial that involves determination of the effect of a candidate therapeutic intervention on human subjects. It includes clinical evaluation of physiologic responses including pharmacokinetic (bioavailability as affected by drag absoφtion, distribution, metabolism and excretion) and pharmacodynamic (physiologic response and efficacy) parameters. A pharmacogenetic clinical study (or clinical trial) is a clinical study that involves testing of one or more specific hypotheses regarding the interaction of a genetic variance or variances (or set of variances, i.e. haplotype or haplotypes) on response to a therapeutic intervention. Pharmacogenetic hypotheses are formulated before the study, and may be articulated in the study protocol in the form of primary or secondary endpoints. For example an endpoint may be that in a particular genetic subgroup the rate of objectively defined responses exceeds the response rate in a control group (either the entire control group or the subgroup of controls with the same genetic signature as the treatment subgroup they are being compared to) or exceeds that in the whole treatment group (i.e. without genetic stratification) by some predefined relative or absolute amount. For a clinical study to commence enrollment and proceed to treat subjects at an institution that receives any federal support (most medical institutions in the US), an application that describes in detail the scientific premise for the therapeutic intervention and the procedures involved in the study, including the endpoints and analytical methods to be used in evaluating the data, must be reviewed and accepted by a review panel, often termed an Institutional Review Board (IRB). Similarly any clinical study that will ultimately be evaluated by the FDA as part of a new dmg or product application (or other application as described below), must be reviewed and approved by an IRB. The IRB is responsible for determining that the trial protocol is safe, conforms to established ethical principles and guidelines, has risks proportional to any expected benefits, assures equitable selection of patients, provides sufficient information to patients (via a consent form) to insure that they can make an informed decision about participation, and insures the privacy of participants and the confidentiality of any data collected. (See the report of the National Commission for Protection of Human Subjects of Biomedical and Behavioral Research (1978). The Belmont Report: Ethical Principles and Guidelines for the Protection of Human Subjects of Research. Washington, D.C: DHEW Publication Number (OS) 78-0012. For a recent review see: Coughlin, S.S. (ed.) (1995) Ethics in Epidemiology and Clinical Research. Epidemiology Resources, Newton, MA.) The European counteφart of the US FDA is the European Medicines Evaluation Agency (EMEA). Similar agencies exist in other countries and are responsible for insuring, via the regulatory process, that clinical trials conform to similar standards as are required in the US. The documents reviewed by an IRB include a clinical protocol containing the information described above, and a consent form. It is also customary, but not required, to prepare an investigator's brochure which describes the scientific hypothesis for the proposed therapeutic intervention, the preclinical data, and the clinical protocol. The brochure is made available to any physician participating in the proposed or ongoing trial. The supporting preclinical data is a report of all the in vitro, in vivo animal or previous human trial or other data that supports the safety and/or efficacy of a given therapeutic intervention. In a pharmacogenetic clinical trial the preclinical data may also include a description of the effect of a specific genetic variance or variances on biochemical or physiologic experimental variables in vitro or in vivo, or on treatment outcomes, as determined by in vivo studies in animals or humans (for example in an earlier trial), or by retrospective genetic analysis of clinical trial or other medical data (see below) used to formulate or strengthen a pharmacogenetic hypothesis. For example, case reports of unusual pharmacological responses in individuals with rare alleles (e.g. mutant alleles), or the observation of clustering of pharmacological responses in family members may provide the rationale for a pharmacogenetic clinical trial. The clinical protocol provides the relevant scientific and therapeutic introductory information, describes the inclusion and exclusion criteria for human subject enrollment, including genetic criteria if relevant (e.g. if genotype is to be among the enrollment criteria), describes in detail the exact procedure or procedures for treatment using the candidate therapeutic intervention, describes laboratory analyses to be performed during the study period, and further describes the risks (both known and possible) involving the use of the experimental candidate therapeutic intervention. In a clinical protocol for a pharmacogenetic clinical trial, the clinical protocol will further describe the genetic variance and/or variances hypothesized to account for differential responses in the normal human subjects or patients and supporting preclinical data, if any, a description of the methods for genotyping, genetic data collection and data handling as well as a description of the genetic statistical analysis to be performed to measure the interaction of the variance or variances with treatment response. Further, the clinical protocol for a pharmacogenetic clinical trial will include a description of the genetic study design. For example patients may be stratified by genotype and the response rates in the different groups compared, or patients may be segregated by response and the genotype frequencies in the different responder or nonresponder groups measured. One or more gene sequence variances or a combination of variances and/or haplotypes may be studied. The informed consent document is a description of the therapeutic intervention and the clinical protocol in simple language (e.g. third grade level) for the patient to read, understand, and, if willing, agree to participate in the study by signing the document. In a pharmacogenetic clinical study the informed consent document will describe, in simple language, the use of a genetic test or a limited set of genetic tests to determine the subject or patient's genotype at a particular gene variance or variances, and to further ascertain whether, in the study population, particular variances are associated with particular clinical or physiological responses. The consent form should also describe procedures for assuring privacy and confidentiality of genetic information. The US FDA reviews proposed clinical trials through the process of an Investigational New Drag Application (IND). The IND is composed of the investigator's brochure, the supporting in vitro and in vivo animal or previous human data, the clinical protocol, and the informed consent forms. In each of the sections of the IND, a specific description of a single allelic variance or a number of variances to be tested in the clinical study will be included. For example, in the investigator's brochure a description of the gene or genes hypothesized to account, at least in part, for differential responses will be included as well as a description of a genetic variance or variances in one or more candidate genes. Further, the preclinical data may include a description of in vivo, in vitro or in silico studies of the biochemical or physiologic effects of a variance or variances (e.g., haplotype) in a candidate gene or genes, as well as the predicted effects of the variance or variances on efficacy or toxicology of the candidate therapeutic intervention. The results of retrospective genetic analysis of response data in patients treated with the candidate therapy may be the basis for formulating the genetic hypotheses to be tested in the prospective trial. The US FDA reviews applications with particular attention to safety and toxicological data to ascertain whether candidate compounds should be tested in humans. The established phases of clinical development are Phase I, II, III, and IV. The fundamental objectives for each phase become increasingly complex as the stages of clinical development progress. In Phase I, safety in humans is the primary focus. In these studies, dose-ranging designs establish whether the candidate therapeutic intervention is safe in the suspected therapeutic concentration range. However, it is common practice to obtain information about sunogate markers of efficacy even in phase I clinical trials. In a pharmacogenetic clinical trial there may be an analysis of the effect of a variance or variances on Phase I safety or sunogate efficacy parameters. At the same time, evaluation of pharmacokinetic parameters (e.g., adsoφtion, distribution, metabolism, and excretion) may be a secondary objective; again, in a pharmacogenetic clinical study there may be an analysis of the effect of sequence variation in genes that affect absorbtion, distribution, metabolism and excretion of the candidate compound on pharmacokinetic parameters such as peak blood levels, half life or tissue distribution of the compound. As clinical development stages progress, trial objectives focus on the appropriate dose and method of administration required to elicit a clinically relevant therapeutic response. In a pharmacogenetic clinical trial, there may be a comparison of the effectiveness of several doses of a comp ound in patients with different genotypes, in order to identify interactions between genotype and optimal dose. For this puφose the doses selected for late stage clinical testing may be greater, equal or less than those chosen based upon preclinical safety and efficacy determinations. Data on the function of different alleles of genes affecting pharmacokinetic parameters could provide the basis for selecting an optimal dose or range or doses of a compound or biological. Genes involved in drag metabolism may be particularly useful to study in relation to understanding inteφatient variation in optimal dose. Genes involved in drug metabolism include the cytochrome P450s, especially 2D6, 3A4, 2C9, 2E1, 2A6 and 1A1 ; the glucuronyltransferases; the acetyltransferases; the methyltransferases; the sulfotransferases; the glutathione system; the flavine monooxygenases and other enzymes known in the art. An additional objective in the latter stages of clinical development is demonstration of the effect of the therapeutic intervention on a broad population. In phase III trials, the number of individuals enrolled is dictated by a power analysis. The number of patients required for a given pharmacogenetic clinical trial will be determined by prior knowledge of variance or haplotype frequency in the study population, likely response rate in the treated population, expected magnitude of pharmacogenetic effect (for example, the ratio of response rates between a genetic subgroup and the unfractionated population, or between two different genetic subgroups); nature of the genetic effect, if known (e.g. dominant effect, codominant effect, recessive effect); and number of genetic hypotheses to be evaluated (including number of genes and/or variances to be studied, number of gene or variance interactions to be studied). Other considerations will likely arise in the design of specific trials. Clinical trials should be designed to blind both human subjects and study coordinators from biasing that may otherwise occur during the testing of a candidate therapeutic invention. Often the candidate therapeutic intervention is compared to best medical treatment, or a placebo (a compound, agent, device, or procedure that appears identical to the candidate therapeutic intervention but is therapeutically inert). The combination of a placebo group and blind controls for potentially confounding factors such as prejudice on the part of study participants or investigators, insures that real, rather than perceived or expected, effects of the candidate therapeutic intervention are measured in the trials. Ideally blinding extends not only to trial subjects and investigators but also to data review committees, ancillary personnel, statisticians, and clinical trial monitors. In pharmacogenetic clinical studies, a placebo arm or best medical control group may be required in order to ascertain the effect of the allelic variance or variances on the efficacy or toxicology of the candidate therapeutic intervention as well as placebo or best medical therapy. It will be important to assure that the composition of the control and test populations are matched, to the degree possible, with respect to genetic background and allele frequencies. This is particularly trae if the variances being investigated may have an effect on disease manifestations (in addition to a hypothesized effect on response to treatment). It is likely that standard clinical trial procedures such as insuring that treatment and control groups are balanced for race, sex and age composition and other non-genetic factors relevant to disease will be sufficient to assure that genetic background is controlled, however a prefened practice is to explicitly test for genetic stratification between test and control groups. Methods for minimizing the possibility of spurious results attributable to genetic stratification between two comparison groups include the use of sunogate markers of geographic, racial and/or ethnic background, such as have been described by Rannala and coworkers. (See, for example: Rannala B, and JL Mountain. 1997 Detecting immigration by using multilocus genotypes. Proc Natl Acad Sci USA Aug 19;94(17):9197-201.) One procedure would be to assure that sunogate markers of genetic background (such as those described by Rannala and Mountain) occur at comparable frequency in two comparison groups. Open label trials are unblinded; in single blind trials patients are kept unaware of treatment assignments; in double blind trials both patients and investigators are unaware of the treatment groups; a combination of these procedures may be instituted during the trial period. Pharmacogenetic clinical trial design may include one or a combination of open label, single blind, or double blind clinical trial designs. Reduction of biases attributable to the knowledge of either the type of treatment or the genotype of the normal subjects or patients is an important aspect of study design. So, for example, even in a study that is single blind with respect to treatment, it should be possible to keep both patients and caregivers blinded to genotype during the study. In designing a clinical trial it is important to include termination endpoints such as adverse clinical events, inadequate study participation either in the form of lack of adherence to the clinical protocol or loss to follow up, (e.g. such that adequate power is no longer assured), lack of adherence on the part of trial investigators to the trial protocol, or lack of efficacy or positive response within the test group. In a pharmacogenetic clinical trial these considerations obtain not only in the entire treatment group, but also in the genetically defined subgroups. That is, if a dangerous toxic effect manifests itself predominantly or exclusively in a genetically defined subpopulation of the total treatment population it may be deemed inappropriate to continue treating that genetically defined subgroup. Such decisions are typically made by a data safety monitoring committee, a group of experts not including the investigators, and generally not blinded to the analysis, who review the data from an ongoing trial on a regular basis. It is important to note that medicine is a conservative field, and clinicians are unlikely to change their behavior on the basis of a single clinical trial. Thus it is likely that, in most instances, two or more clinical trials will be required to convince physicians that they should change their prescribing habits in view of genetic information. Large scale trials represent one approach to providing increased data supporting the utility of a genetic stratification. In such trials the stringent clinical and laboratory data collection characteristic of traditional trials is often relaxed in exchange for a larger patient population. Important goals in large scale pharmacogenetic trials will include establishing whether a pharmacogenetic effect is detectable in all segments of a population. For example, in the North American population one might seek to demonstrate a pharmacogenetic effect in people of African, Asian, European and Hispanic (i.e. Mexican and Puerto Rican) origin, as well as in native American people. (It generally will not be practical to segment patients by geographical origin in a standard clinical trial, due to loss of power.) Another goal of a large scale clinical trial may be to measure more precisely, and with greater confidence, the magnitude of a pharmacogenetic effect first identified in a smaller trial. Yet another undertaking in a large scale clinical trial may be to examine the interaction of an established pharmacogenetic variable (e.g. a variance in gene A, shown to affect treatment response in a smaller trial) with other genetic variances (either in gene A or in other candidate genes). A large scale trial provides the statistical power necessary to test such interactions. In designing all of the above stages of clinical testing investigators must be attentive to the statistical problems raised by testing multiple different hypotheses, including multiple genetic hypotheses, in subsets of patients. Bonfenoni's conection or other suitable statistical methods for taking account of multiple hypothesis testing will need to be judiciously applied. However, in the early stages of clinical testing, when the main goal is to reduce the large number of potential hypotheses that could be tested to a few that will be tested, based on limited data, it may be impractical to rigidly apply the multiple testing conection. R. Phase I Clinical Trials X . Introduction Phase I of clinical development is generally focused on safety, although drag companies are increasingly obtaining information on pharmacokinetics and sunogate pharmacodynamic markers in early trials. Phase I studies are typically performed with a small number (< 60) of normal, healthy volunteers usually at single institutions. The primary endpoints in these studies usually relate to pharmacokinetic parameters (i.e. adsoφtion, distribution, metabolism and bioavailability), and dose-related side effects. In a Phase I pharmacogenetic clinical trial, stratification based upon allelic variance or variances of a candidate gene or genes related to pharmacokinetic parameters may allow early assessment of potential genetic interactions with treatment. Phase I studies of some diseases (e.g. cancer or other medically intractable diseases for which no effective medical alternative exists) may include patients who satisfy specified inclusion criteria. These safety/limited-efficacy studies can be conducted at multiple institutions to ensure rapid enrollment of patients. In a pharmacogenetic Phase I study that includes patients, or a mixture of patients and normals, the status of a variance or variances suspected to affect the efficacy of the candidate therapeutic intervention may be used as part of the inclusion criteria. Alternatively, analysis of variances or haplotypes in patients with different treatment responses may be among the the endpoints. It is not unusual for such a Phase I study design to include a double-blind, balanced, random-order, crossover sequence (separated by washout periods), with multiple doses on separate occasions and both pharmacokinetic and pharmacodynamic endpoints. 2. Phase I trials with subjects drawn from large populations and/or from related volunteer subjects: the Pharmacogenetic Phase I Unit concept In general it is useful to be able to assess the contribution of genetic variation to treatment response at the earliest possible stage of clinical development. Such an assessment, if accurate, will allow efficient prioritization of candidate compounds for subsequent detailed pharmacogenetic studies; only those treatments where there is early evidence of a significant interaction of genetic variation with treatment response would be advanced to pharmacogenetic studies in later stages of development. In this invention we describe methods for achieving early insight - in Phase I - into the contribution of genetic variation to variation in sunogate treatment response variables. It occuned to the inventors that this can be accomplished by bringing the power of genetic linkage analysis and outlier analysis to Phase I testing via the recmitment of a very large Phase I population including a large number of individuals who have consented in advance to genetic studies (occasionally refened to hereinafter as a Pharmacogenetic Phase I Unit). In one embodiment of a Pharmacogenetic Phase I Unit many of the subjects are related to each other by blood. (Cunently Phase I trials are performed in unrelated individuals, and there is no consideration of genetic recruitment criteria, or of genetic analysis of sunogate markers.) There are several novel ways in which a large population, or a population comprised at least in part of related individuals, could be useful in early clinical trials. Some of the most attractive applications depend on the availability of sunogate markers for pharmacodynamic drag action which can be used early in clinical development, preferably in normal subjects in Phase I. Such sunogate markers are increasingly used in Phase I, as drag development companies seek to make early yes/no decisions about compounds. Recruitment of a population optimized for clinical genetic investigation may entail utilization of methods in statistical genetics to select the size and composition of the population. For example powerful methods for detecting and mapping quantitative trait loci in sibpairs have been developed. These methods can provide some estimate of the statistical power derived from a given number of groups of closely related individuals. Ideally subjects in the pharmacogenetic Phase I unit are of known ethnic/racial/geographic background and willing to participate in Phase I studies, for pay, over a period of years. The population is preferably selected to achieve a specified degree of statistical power for genetic association studies, or is selected in order to be able to reliably identify a certain number of individuals with rare genotypes, as discussed below. Family participation could be encouraged by appropriate incentive compensation. For example, individual subjects might be paid $200 for participation in a study; two sibs participating in the same study might each be paid $300; if they could encourage another sib (or cousin) to participate the three related individuals might each be paid $350, and so forth. This type of compensation would encourage subjects to recruit their relatives to participate in Phase I studies. (It would also increase the cost of studies, however the type of data that can be obtained can not be duplicated with conventional approaches.) The optimal location to establish such a Phase I unit is a city with a stable population, many large families, and a positive attitide about gene technology. The Pharmacogenetic Phase I Unit population can then be used to test for the existence of genetic variation in response to any drag as a first step in deciding whether to proceed with extensive pharmacogenetic studies in later stages of clinical development. Specific uses of a large Phase I unit in which some or all subjects are related include: a. It should be possible, for virtually any compound, to assess the magnitude of the genetic contribution to variation in drag response (if any) by comparing variation in dmg response traits among related vs. non-related individuals. The rationale is as follows: if a sunogate drug response trait (i.e.a sunogate marker of pharmacodynamic effect that can be measured in normal subjects) is under strong genetic control then related individuals, who share 25%> (cousins) or 50%> (sibs) of their alleles, should have less divergent responses (less intragroup variance) than unrelated individuals, who share a much smaller fraction of alleles. That is, individuals who share alleles at the genes that affect drag response should be more similar to each other (i.e. have a nanower distribution of responses, whether measured by variance, standard deviation or other means) than individuals who, on average, share very few alleles. By using statistical methods known in the art the degree of variation in a set of data from related individuals (each individual would only be compared with his/her relatives, but such comparisons would be performed within each group of relatives and a summary statistic developed) could be compared to the degree of variation in a set of unrelated individuals (the same subjects could be used, but the second comparison would be across related groups). Account would be taken of the degree of similarity expected between related individuals, based on the fraction of the genome they shared by descent. Thus the extent of variation in the sunogate response marker between identical twins should be less than between sibs, which should be less than between first cousins, which should be less than that between second cousins, and so forth, //"there is a genetic component to the variation. It is well known from twin studies (in which, for example, variation between identical twins is compared to variation between fraternal twins) that pharmacokinetic variables (e.g. compound half life, peak concentration) are frequently over 90%> heritable; the type of study proposed here (comparison of variation within groups of sibs and cousins to variation between unrelated subjects) would also show this genetic effect, without requiring the recruitment of monozygotic twins. For a summary of pharmacokinetic studies in twins see: Propping, Paul (1978) Pharmacogenetics. Rev. Physiol. Biochem. Pharmacol. 83: 123-173. It may be that the pattern of drag responses that distinguishes related individuals from non-related individuals is more complex than, for example, variance or standard deviation. For example, there may be two discrete phenotypes characteristic of intrafamilial variation (a bimodal distribution) that are not a feature of variation between unrelated individuals (where, for example, variation might be more nearly continuous). Such a pattern could be attributable to Mendelian inheritance operating on a restricted set of alleles in a family (or families) with, for example, AA homozygotes giving one phenotype and AB heterozygotes and BB homozygotes giving a second phenotype, all in the context of a relatively homogeneous genetic background. In contrast, variation among non-related subjects would be less discrete due to a greater degree of variation in genetic background and the presence of additional alleles C, D and E at the candidate locus. Statistical measures of the significance of such differences in distribution, including nonparametric methods such as chi square and contingency tables, are known in the art. The methods described herein for measuring whether pharmacodynamic traits are under genetic control, using sunogate markers of drag efficacy in phase I studies which include groups of related individuals, will be useful in obtaining an early assessment of the extent of genetically determined variation in drag response for a given therapeutic compound. Such information provides an informed basis for either stopping development at the earliest possible stage or, preferably, continuing with development but with a plan for identifying and controlling for genetic variation so as to allow rapid progression through the regulatory approval process. For example, it is well known that Alzheimers trials are long and expensive, and most drags are only effective in a fraction of patients. Using sunogate measures of response in normals drawn from a population of related individuals would help to assess the contribution of genetic variation to variation in treatment response. For an acetylcholinesterase inhibitor, relevant sunogate pharmacodynamic measures could include testing erythrocye membrane acetylcholinesterase levels in drug treated normal subjects, or performing psychometric tests that are affected by treatment (and ideally that conelate with clinical efficacy) and measuring the effect of treatment. As another example, antidepressant drags can produce a variety of effects on mood in normal subjects - or no effect at all. Careful monitoring and measurement of such responses in related vs. unrelated normal subjects, and statistical comparison of the degree of variation in each group, could provide an early readout on whether there is a genetic component to drag response (and hence clinical efficacy). The observation of similar effects in family members, and comparatively dissimilar effects in unrelated subjects would provide compelling evidence of a pharmacogenetic effect and justify the substantial expenditure necessary for a full pharmacogenetic drag development program. Conversely, the absence of any significant family influence on drag response would provide an early termination point for pharmacogenetic studies. Note that the proposed studies do not require any knowledge of candidate genes, nor is DNA collection or genotyping required - simply a reliable surrogate pharmacodynamic assay and small groups of related normal individuals. Refined statistical methods should permit the magnitude of the pharmacogenetic effect to be measured, which could be a further criteria for deciding whether to proceed with pharmacogenetic analysis. The greater the differential in magnitude or pattern of variance between the related and the unrelated subjects, the greater the extent of genetic control of the trait. Not all drug response traits are under the predominant control of one locus. Many such traits are under the control of multiple genes, and may be refened to as quantitative trait loci. It is then desirable to identify the major loci contributing to variation in the drag response trait. This can be done for example, to map quantitative trait loci in a population of drug treated related normals. Either a candidate gene approach or a genome wide scanning approach can be used. (For review of some relevant methods see: Hsu L, Aragaki C, Quiaoit F. (1999) A genome-wide scan for a simulated data set using two newly developed methods. Genet Epidemiol 17 Suppl 1.S621-6; Zhao LP, Aragaki C, Hsu L, Quiaoit F. (1998) Mapping of complex traits by single-nucleotide polymoφhisms. Am J Hum Genet 63(l):225-40; Stoesz MR, Cohen JC, Mooser V, et al. ( 1997) Extension of the Haseman-Elston method to multiple alleles and multiple loci: theory and practice for candidate genes. Ann Hum Genet 61 (Pt 3):263-74.)) However, this method would require at least 100 patients (preferably 200, and still more preferably >300) to have adequate statistical power, and each patient would have to be genotyped at a few polymoφhic loci (candidate gene approach) or hundreds of polymoφhic loci (genome scanning approach). b. With a large Phase I population of normal subjects that need not be related (a second type of Pharmacogenetic Phase I Unit) it is possible to efficiently identify and recruit for any Phase I trial a set of individuals comprising virtually any combination of genotypes present in a population (for example, all common genotypes, or a group of genotypes expected to represent outliers for a drag response trait of interest). This method preferably entails obtaining blood or other tissue (e.g. buccal smear) in advance from a large number of the subjects in the Phase I unit. Ideally consent for genotyping would be obtained at the same time. It would be most efficient if blanket consent for genotyping any polymoφhic site or sites could be obtained. Second best would be consent for testing any site relevant to any customer project (not specific at the time of initial consent). Third best would be consent to genotype polymoφhic sites relevant to specific disease areas. Another, less desirable, solution would be to obtain consent for genotyping on a project by project basis (for example by mailing out reply cards), after the specific polymoφhic sites to be genotyped are known. One useful way to screen for pharmacogenetic effects in Phase I is to recruit homozygotes for a variance or variances of interest in one or more candidate genes. For example, consider a compound for which there are two genes that are strong candidates for influencing response to treatment. Gene X has alleles A and A', while gene Y has alleles B and B'. If these genes do in fact contribute significantly to response then one would expect that, regardless of the mode of inheritance (recessive, codominant, dominant, polygenic) homozygotes would exhibit the most extreme responses. One would also expect epistatic interactions, if any, to be most extreme in double homozygotes. Thus one would ideally perform a sunogate drag response test in Phase I volunteers doubly homozygous at both X and Y. That is, test AA/BB, A'A'/BB, AA/B'B' and A'A'/B'B' subjects. If the allele frequencies for A and A' are .15 and .85, and for B and B' .2 and .8 then the frequency of AA homozygotes is expected to be 2.25% and BB homozygotes 4%. In the absence of any linkage between the genes, the frequency of AA/BB double homozygotes is expected to be 0.0225 x 0.04 = 0.0009 or .09%, or about 1 subject in 1000. Ideally at least 5 subjects of each genotype are recruited for the Phase I study, and preferably at least 10 subject. Thus, even for variances of moderately low allele frequency (15%>, 20%), the identification of potential outliers (i.e. homozygotes) for the candidate genes of interest will require a large population. Preferably the Phase I unit has enrolled at least 1 ,000 normal individuals, more preferably 2,000, still more preferably 5,000 and most preferably 10,000 or more. In another application of the large, genotyped Phase I population it may be useful to identify individuals with rare variances in candidates genes (either homozygous or heterozygous), in order to determine whether those variances are predisposing to extreme pharmacological responses to the compound. For example, variances occurring at 5% allele frequency are expected to occur in homozygous form in 0.25%> of the population (0.05 x 0.05), and therefore may rarely, if ever, be encountered in early clinical development. Yet it may be serious adverse effects occuring in just such a small group that create problems in later stages of drag development. In yet another application of the large genotyped Phase I population, subjects may be selected to represent the known common variances in one or more genes that are candidates for influencing the response to treatment. By insuring that all common genotypes are represented in a Phase I trial the likelihood of misleading results due to genetic stratification (resulting in discrepancy with results of later, larger trials can be reduced. It would be useful to prospectively genotype the large Phase I population for variances that are commonly the source of inteφatient variation in drug response, since demand for genotyped groups of such patients can be anticipated from pharmaceutical companies and contract research organizations (CROs). For example, genotyping might initially focus on common pharmacological targets such as estrogen receptors, adrenergic receptors, or serotonin receptors. The pre- genotyped Phase I population could be part of a package of services (along with genotyping assay development capability, high throughput genotyping capacity and software and expertise in statistical genetics) designed to accelerate pharmacogenetic Phase I studies. Eventually, as the databank of genotypes built up, individuals with virtually any genotype or combination of genotypes could be called in for precisely designed physiological or toxicological studies designed to test for pharmacogenetic effects. One of the most useful aspects of the Pharmacogenetic Phase I Unit is that subjects with rare genotypes can be pharmacologically assessed in a small study. This addresses a serious limitation of conventional clinical trials with respect to the investigation of polygenic traits or the effect of rare alleles. Unfortunately even Phase III studies, as cunently performed, are often barely powered to address simple one variance hypotheses about efficacy or toxicity. The problem, of course, is that each time a new genetic variable is introduced the comparison groups are cut in halves or thirds (or even smaller groups if there are multiple haplotypes at each gene). It is therefore a challenging problem to test the interaction of several genes in determining drag response. Yet the character of drag response data in populations - there is often a continuous distribution of responses among different individuals - suggests that drag responses may often be mediated by several genes. (On the other hand, there are an increasing number of well documented single gene, or even single variance, pharmacogenetic effects in the literature, showing that it is possible to detect the effect of a single variance.) One approach to identifying pharmacogenetic effects is to focus on finding the single gene variances that have the largest effects. This approach can be undertaken within the scale of cunent clinical trials. However, in order to develop a test which predicts a large fraction of the quantitative variation in a drag response trait it may be desirable to test the effect of multiple genes, including the interaction of variances at different genes, which may be non-additive (refened to as epistasis). The Pharmacogenetic Phase I Unit provides a way to efficiently test for gene interactions or multigene effects by, for example, allowing easy identification of individuals who, on account of being homozygous at several loci of interest, should be outliers for the drag response phenotypes of interest if there is a gene x gene interaction. Testing drag response in a small number of such individuals will provide a quick read on gene interaction. Obtaining genetic data on the pharmacodynamic action of a compound in Phase I should also provide a crude measure of allele affects - which variances or haplotypes increase pharmacological responses and which decrease them. This information is of great value in designing subsequent trials, as it constrains the number of hypotheses to be tested, thereby enabling powerful statistical designs. This is because when the effect of variances on drag response measures is unknown one is forced to statistically test all the possible effects of each allele (e.g. two tailed tests). As the number of genetically defined groups increases (e.g. as a result of multiple variances or haplotypes) there is a loss of statistical power due to multiple testing conection. On the other hand, if the relative phenotypic effect of each allele at a locus is known (or can be hypothesized) from Phase I data then each individual in a subsequent clinical trial contributes useful information - there is a specific prediction of response based on that individuals combination of genotypes or haplotypes, and testing the fit of the actual data to those predictions provides for powerful statistical designs. (It is also possible to measure allele effects biochemically, of course, to establish which alleles have positive and which negative effects, but at considerable cost.) It is important to note that Phase I trials can provide useful information at almost any stage of clinical development. It is not unusual, for example, for a product in Phase II or even Phase III testing to be remanded to Phase I in order to clarify some aspect of toxicology or physiology. In this context a Pharmacogenetic Phase I Unit would be extremely useful to a drug development company. Phase I studies in defined genetic subgroups drawn from a large genotyped population, or in groups of related individuals, would be the most economical and efficient way to clarify the existence of pharmacogenetic effects, if any, paving the way for future rational development of the product. C. Phase II Clinical Trials Phase II studies generally include a limited number of patients (<100) who satisfy a set of predefined inclusion criteria and do not satisfy any predefined exclusion criteria of the trial protocol. Phase II studies can be conducted at single or multiple institutions. Inclusion/exclusion criteria may include historical, clinical and laboratory parameters for a disease, disorder, or condition; age; gender; reproductive status (i.e. pre- or postmenopausal); coexisting medical conditions; psychological, emotional or cognitive state, or other objective measures known to those skilled in the art. In a pharmacogenetic Phase II trial the inclusion/exclusion criteria may include one or more genotypes or haplotypes. Alternatively, genetic analysis may be performed at the end of the trial. The primary goals in Phase II testing may include (i) identification of the optimal medical indication for the compound, (ii) definition of an optimal dose or range or doses, balancing safety and efficacy considerations (dose-finding studies), (iii) extended safety studies (complementing Phase I safety studies), (iv) evaluation of efficacy in patients with the targeted disease or condition, either in comparison to placebo or to cunent best therapy. To some extent these goals may be achieved by performing multiple trials with different goals. Likewise, Phase II trials may be designed specifically to evaluate pharmacogenetic aspects of the drag candidate. Primary efficacy endpoints typically focus on clinical benefit, while sunogate endpoints may measure treatment response variables such as clinical or laboratory parameters that track the progress or extent of disease, often at lesser time, cost or difficulty than the definitive endpoints. A good sunogate marker must be convincingly associated with the definitive outcome. Examples of sunogate endpoints include tumor size as a sunogate for survival in cancer trials, and cholesterol levels as a sunogate for heart disease (e.g. myocardial infarction) in trials of lipid lowering cardiovascular drugs. Secondary endpoints supplement the primary endpoint and may be selected to help guide further clinical studies. In a pharmacogenetic Phase II clinical trial, retrospective or prospective design will include the stratification of patients based upon a variance or variances in a gene or genes suspected of affecting treatment response. The gene or genes may be involved in mediating pharmacodynamic or pharmacokinetic response to the candidate therapeutic intervention. The parameters evaluated in the genetically stratified trial population may include primary, secondary or surrogate endpoints. Pharmacokinetic parameters - for example, dosage, absorbtion, toxicity, metabolism, or excretion - may also be evaluated in genetically stratified groups.. Other parameters that may be assessed in parallel with genetic stratification include gender, race, ethnic or geographic origin (population history) or other demographic factors. While it is optimal to initiate pharmacogenetic studies in phase I, as described above, it may be the case that pharmacogenetic studies are not considered until phase II, when problems relating either to efficacy or toxicity are first encountered. It is highly desirable to initiate pharmacogenetic studies no later than Phase II of a clinical development plan because (1 ) phase III studies tend to be large and expensive - not an optimal setting in which to explore untested pharmacogenetic hypotheses; (2) phase III studies are typically designed to test one fairly nanow hypothesis regarding efficacy of one or a few dose levels in a specific disease or condition. Phase II studies are often numerous, and are intended to provide a broad picture of the pharmacology of the candidate compound. This is a good setting for initial pharmacogenetic studies. Several pharmacogenetic hypotheses may be tested in phase II, with the goal of eliminating all but one or two. D. Phase III Clinical Trials Phase III studies are generally designed to measure efficacy of a new treatment in comparision to placebo or to an established treatment method. Phase II studies are often performed at multiple sites. The design of this type of trial includes power analysis to ensure the sufficient data will be gathered to demonstrate the anticipated effect, making assumptions about reponse rate based on earlier trials. As a result Phase III trials frequently include large numbers of patients (up to 5,000). Primary endpoints in Phase III studies may include reduction or anest of disease progression, improvement of symptoms, increased longevity or increased disease- free longevity, or other clinical measures known in the art. In a pharmacogenetic Phase III clinical study, the endpoints may include determination of efficacy or toxicity in genetically defined subgroups. Preferably the genetic analysis of outcomes will be confined to an assessment of the impact of a small number of variances or haplotypes at a small number of genes, said variances having already- been statistically associated with outcomes in earlier trials. Most preferably variances at only one or two genes will be assessed. After successful completion of one or more Phase III studies, the data and information from all trials conducted to test a new treatment method are compiled into a New Drag Application (NDA) and submitted for review by the US FDA, which has authority to grant marketing approval in the US and its territories. The NDA includes the raw (unanalyzed) clinical data, i.e. the patient by patient measurements of primary and secondary endpoints, a statistical analysis of all of the included data, a document describing in detail any observed side effects, tabulation of all patients who dropped-out of trials and detailed reasons for their termination, and any other available data pertaining to ongoing in vitro or in vivo studies since the submission of the investigational new drug (IND) application. If pharmacoeconomic objectives are a part of the clinical trial design then data supporting cost or economic analyses are included in the NDA. In a pharmacogenetic clinical study, the pharmacoeconomic analyses may include genetically stratified assessment of the candidate therapeutic intervention in a cost benefit analysis, cost of illness study, cost minimization study, or cost utility analysis. The analysis may also be simultaneously stratified by standard criteria such as race/ethnicity/geographic origin, sex, age or other criteria. Data from a genetically stratified analysis may be used to support an application for approval for marketing of the candidate therapeutic intervention. E. Phase IV Clinical Trials Phase IV studies occur after a therapeutic intervention has been approved for marketing, and are typically conducted for suveillance of safety, particularly occurance of rare side effects. The other principal reason for Phase IV studies is to produce information and relationships useful for marketing a drug. In this regard pharmacogenetic analysis may be very useful in Phase IV trials. Consider, for example, a drag that is the fourth or fifth member of a drag class (say statins, or thiazidinediones or fluoropyrimidines) to obtain marketing approval, and which does not differ significantly in clinical effects - efficacy or safety - from other members of the drag class. The first, second and third drags in the class will likely have a dominant market position (based on their earlier introduction into the marketplace) that is difficult to overcome, particularly in the absence of differentiating clinical effects. However, it is possible that the new drag produces a superior clinical effect - for example, higher response rate, greater magnitude of response or fewer side effects - in a genetically defined subgroup. The genetic subgroup with superior response may constitute a larger fraction of the total patient population than the new drag would likely achieve otherwise. In this instance, there is a clear rationale for performing a Phase IV pharmacogenetic trial to identify a variance or variances that mark a patient population with superior clinical response. Subsequently a marketing campaign can be designed to alert patients, physicians, pharmacy managers, managed care organizations and other parties that, with the use of a rapid and inexpensive genetic test to identify eligible patients, the new drag is superior to other members of the class (including the market leading first, second and third drugs introduced). The high responder subgroup defined by a variance or variances may also exhibit a superior response to other drags in the class (a class pharmacogenetic effect), or the superior efficacy in the genetic subgroup may be specific to the dmg tested (a compound-specific pharmacogenetic effect). In a Phase IV pharmacogenetic clinical trial, both retrospective and prospective analysis can be performed. In both cases, the key element is genetic stratification based on a variance or variances or haplotype. Phase IV trials will often have adequate sample size to test more than one pharmacogenetic hypothesis in a statistically sound way. F. Unconventional Clinical Development Although the above listed phases of clinical development are well- established, there are cases where strict Phase I, II, III development does not occur, for example, in the clinical development of candidate therapeutic interventions for debilitating or life threatening diseases, or for diseases where there is presently no available treatment. Some of the mechanisms established by the FDA for such studies include Treatment INDs, Fast-Track or Accelerated reviews, and Oφhan Drag Status. In a clinical development program for a candidate therapeutic of this type there is a useful role for pharmacogenetic analysis, in that the candidate therapeutic may not produce a sufficient benefit in all patients to justify FDA approval, however analysis of outcome in genetic subgroups may lead to identification of a variance or variances that predict a response rate sufficient for FDA approval. As used herein, "supplemental applications" are those in which a candidate therapeutic intervention is tested in a human clinical trial in order to gain an expanded label indication, expanding recommended use to new medical indications. In these applications, previous clinical studies of the therapeutic intervention, i.e. preclinical safety and Phase I human safety studies can be used to support the testing of the therapeutic intervention in a new indication. Pharmacogenetic analysis is also useful in the context of clinical trials to support supplemental applications. Since these are, by defininition, focused on diseases not selected for initial development the overall efficacy may not be as great as for the leading indication(s). The identification of genetic subgroups with high response rates may enable the rapid approval of supplemental applications for expanded label indications. In such instances part of the label indication may be a description of the variance or variances that define the group with superior response. As used herein, "outcomes" or "therapeutic outcomes" describe the results and value of healthcare intervention. Outcomes can be multi-dimensional, and may include improvement of symptoms; regression of a disease, disorder, or condition; prevention of a disease or symptom; cost savings or other measures. Pharmacoeconomics is the analysis of a therapeutic intervention in a population of patients diagnosed with a disease, disorder, or condition that includes at least one of the following studies: cost of illness study (COI); cost benefit analysis (CBA), cost minimization analysis (CMA), or cost utility analysis (CUA), or an analysis comparing the relative costs of a therapeutic intervention with one or a group of other therapeutic interventions. In each of these studies, the cost of the treatment of a disease, disorder, or condition is compared among treatment groups. Costs have both direct (therapeutic interventions, hospitalization) and indirect (loss of productivity) components. Pharmacoeconomic factors may provide the motivation for pharmacogenetic analysis, particularly for expensive therapies that benefit only a fraction of patients. For example, interferon alpha is the only treatment that can cure hepatitis C virus infection, however viral infection is completely and permanently eliminated in less than a quarter of patients. Nearly half of patients receive virtually no benefit from alfa interferon, but may suffer significant side effects. Treatment costs are ~S 10,000 per course. A pharmacogenetic test that could predict responders would save much of the cost of treating patients not able to benefit from interferon alpha therapy, and could provide the rationale for treating a population in a cost efficient manner, where treatment would otherwise be unaffordable. As used herein, "health-related quality of life" is a measure of the impact of a disease, disorder, or condition on a patient's activities of daily living. An analysis of the health-related quality of life is often included in pharmacoeconomic studies. As used herein, the term "stratification" refers to the partitioning of patients into groups on the basis of clinical or laboratory characteristics of the patient. "Genetic stratification" refers to the partitioning of patients or normal subjects into groups based on the presence or absence of a variance or variances in one or more genes. The stratification may be performed at the end of the trial, as part of the data analysis, or may come at the beginning of a trial, resulting in creation of distinct groups for statistical or other puφoses. G Power analysis in pharmacogenetic clinical trials The basic goal of power calculations in clinical trial design is to insure that trials have adequate patients and controls to fairly assess, with statistical significance, whether the candidate therapeutic intervention produces a clinically significant benefit. Power calculations in clinical trials are related to the degree of variability of the drag response phenotypes measured and the treatment difference expected between comparison groups (e.g. between a treatment group and a control group). The smaller the variance within each group being compared, and the greater the difference in response between the two groups, the fewer patients are required to produce convincing evidence of an effect of treatment. These two factors (variance and treatment difference) determine the degree of precision required to answer a specific clinical question. The degree of precision may be expressed in terms of the maximal acceptable standard enor of a measurement, the magnitude of variation in which the 95% confidence interval must be confined or the minimal magnitude of difference in a clinical or laboratory value that must be detectable (at a statistically significant level, and with a specified power for detection) in a comparison to be performed at the end of the trial (hypothesis test). The minimal magnitude is generally set at the level that represents the minimal difference that would be considered of clinical importance. In pharmacogenetic clinical trials there are two countervailing effects with respect to power. First, the comparison groups are reduced in size (compared to a conventional trial) due to genetic partitioning of both the treatment and control groups into two or more subgroups. However, it is reasonable to expect that variability for a trait is smaller within groups that are genetically homogeneous with respect to gene variances affecting the trait. If this is the case then power is increased as a function of the reduction in variability within (genetically defined) groups. In general it is preferable to power a pharmacogenetic clinical trial to see an effect in the largest genetically defined subgroups. For example, for a variance with allele frequencies of 0.7 and 0.3 the common homozygote group will comprise 49% of all patients (0.7 x 0.7 x 100). It is most desirable to power the trial to observe an effect (either positive or a negative) in this group. If it is desirable to measure an effect of therapy in a small genetic group (for example, the 9% of patients homozygous for the rare allele) then genotyping should be considered as an enrollment criterion to insure a sufficient number of patients are enrolled to perform an adequately powered study. Statistical methods for powering clinical trials are known in the art. See, for example: Shuster, J.J. (1990) Handbook of Sample Size Guidelines for Clinical Trials. CRC Press, Boca Raton, FL; Machin, D. and M.J. Campbell ( 1987) Statistical Tables for the Design of Clinical Trials. Blackwell, Oxford, UK; Dormer, A. ( 1984) Approaches to Sample Size Estimation in the Design of Clinical Trials - A Review. Statistics in Medicine 3: 199-214. H. Statistical analysis of clinical trial data There are a variety of statistical methods for measuring the difference between two or more groups in a clinical trial. One skilled in the art will recognize that different methods are suited to different data sets. In general, there is a family of methods customarily used in clinical trials, and another family of methods customarily used in genetic epidemiological studies. Methods in quantitative and population genetics designed to measure the association betweeen genotypes and phenotypes, and to map and measure the effect of quantitative trait loci are also relevant to the task of measuring the impact of a variance on response to a treatment. Methods from any of these disciplines may be suitable for performing statistical analysis of pharmacogenetic clinical trial data, as is known to those skilled in the art. Conventional clinical trial statistics include hypothesis testing and descriptive methods, as elaborated below. Guidance in the selection of appropriate statistical tests for a particular data set is provided in texts such as: Biostatistics: A Foundation for Analysis in the Health Sciences, 7th edition (Wiley Series in Probability and Mathematical Statistics. Applied Probability and statistics) by Wayne W. Daniel, John Wiley & Sons. 1998; Bayesian Methods and Ethics in a Clinical Trial Design (Wiley Series in Probability and Mathematical Statistics. Applied Probability Section) by J. B. Kadane (Editor), John Wiley & Sons, 1996. Examples of specific hypothesis testing and descriptive statistical procedures that may be useful in analyzing clinical trial data are listed below. A. Hypothesis testing statistical procedures ( 1 ) One-sample procedures (binomial confidence interval, Wilcoxon signed rank test, permutation test with general scores, generation of exact permutational distributions) (2) Two-sample procedures (t-test, Wilcoxon-Mann- Whitney test, Normal score test, Median test, Van der Waerden test, Savage test, Logrank test for censored survival data, Wilcoxon-Gehan test for censored survival data, Cochran- Armitage trend test, permutation test with general scores, generation of exact permutational distributions) (3) R x C contingency tables (Fisher's exact test, Pearson's chi-squared test. Likelihood ratio test, Kruskal-Wallis test, Jonckheere-Teφstra test, Linear-by linear association test, McNemar's test, marginal homogeneity test for matched pairs) (4) Stratified 2 x 2 contingency tables (test of homogeneity for odds ratio, test of unity for the common odds ratio, confidence interval for the common odds ratio) (5) Stratified 2 x C contingency tables (all two-sample procedures listed above with stratification, confidence intervals for the odds ratios and trend, generation of exact permutational distributions) (6) General linear models (simple regression, multiple regression, analysis of variance -ANOVA-, analysis of covariance, response-surface models, weighted regression, polynomial regression, partial conelation, multiple analysis of variance -MANOVA-, repeated measures analysis of variance). (7) Analysis of variance and covariance with a nested (hierarchical) stracture. (8) Designs and randomized plans for nested and crossed experiments (completely randomized design for two treatment, split-splot design, hierarchical design, incomplete block design, latin square design) (9) Nonlinear regression models (10) Logistic regression for unstratified or stratified data, for binary or ordinal response data, using the logit link function, the normit function or the complementary log-log function. (11) Probit, logit, ordinal logistic and gompit regression models. (12) Fitting parametric models to failure time data that may be right-, left-, or interval-censored. Tested distributions can include extreme value, normal and logistic distributions, and, by using a log transformation, exponential, Weibull, lognormal, loglogistic and gamma distributions. (13) Compute non-parametric estimates of survival distribution with right- censored data and compute rank tests for association of the response variable with other variables. B. Descriptive statistical methods • Factor analysis with rotations • Canonical conelation • Principal component analysis for quantitative variables. • Principal component analysis for qualitative data. • Hierarchical and dynamic clustering methods to create tree stracture, dendrogram or phenogram. • Simple and multiple conespondence analysis using a contingency table as input or raw categorical data. Specific instructions and computer programs for performing the above calculations can be obtained from companies such as: SAS/STAT Software, SAS Institute Inc., Cary, NC, USA; BMDP Statistical Software, BMDP Statistical Software Inc., Los Angeles, CA, USA; SYSTAT software, SPSS Inc., Chicago, IL, USA; StatXact & LogXact, CYTEL Software Coφoration, Cambridge, MA, USA. C. Statistical Genetic Methods Useful for Analysis of Pharmacogenetic Data A wide spectrum of mathematical and statistical tools may be useful in the analysis of data produced in pharmacogenetic clinical trials, including methods employed in molecular, population, and quantitative genetics, as well as genetic epidemiology. Methods developed for plant and animal breeding may be useful as well, particularly methods relating to the genetic analysis of quantitative traits. Analytical methods useful in the analysis of genetic variation among individuals, populations and species of various organisms are described in the following texts: Molecular Evolution, by W- H. Li, Sinauer Associates, Inc., 1997; Principles of Population Genetics, by D. L. Haiti and A. G. Clark, 1996; Genetics and Analysis of Quantitative Traits, By M. Lynch and B. Walsh, Sinauer Associates, Inc., Principles of Quantitative Genetics, by D. S. Falconer and T.F.C Mackay, Longman, 1996; Genetic Variation and Human Disease, by K. M. Weiss, Cambridge University Press, 1993; Fundamentals of Genetic Epidemiology, by M. J. Khoury, T. H. Beaty, and B. H. Cohen, Oxford University Press, 1993; Handbook of Genetic Linkage, by J. Terwilliger J. Ott, Johns Hopkins University Press, 1994. The types of statistical analysis performed in different branches of genetics are outlined below as a guide to the relevant literature and publicly available software, some of which is cited. Molecular evolutionary gen etics • Patterns of nucleotide variation among individuals, families/populations and across species and genera, • Alignment of sequences and description of variation/polymoφhisms among the aligned sequences, amounts of similarities and dissimilarities, • Measurement of molecular variation among various regions of a gene, testing of neutrality models, • Rates of nucleotide changes among coding and the non-coding regions within and among populations, • Construction of phylogenetic trees using methods such as neighborhood joining and maximum parsimony; estimation of ages of variances using coalescent models, Population genetics • Patterns of distribution of genes among genotypes and populations. Hardy- Weinberg equilibrium, departures form the equilibrium • Genotype and haplotype frequencies, levels of heterozygosities, polymoφhism information contents of genes, estimation of haplotypes from genotypes; the E- M algorithm, and parsimony methods • Estimation of linkage disequilibrium and recombination • Hierarchical stmcture of populations, the F-statistics, estimation of inbreeding, selection and drift • Genetic admixture/migration and mutation frequencies • Spatial distribution of genotypes using spatial autoconelation methods • Kin- structured maintainance of variation and migration Quantitative genetics • Phenotype as the product of the interaction between genotype and environment • Additive, dominance and epistatic variance on the phenotype • Effects of homozygosity, heterozygosity and developmental homeostasis • Estimation of heritability: broad sense and nanow sense • Determination of number of genes governing a character • Determination of quantitative trait loci (QTLs) using family information or population information, and using linkage and/or association studies • Determination of quantitative trait nucleotide (QTN) using a combination linkage disequilibrium methods and cladistic approaches • Determination of individual causal nucleotide in the diploid or haploid state on the phenotype using the method of measured genotype approaches, and combined effects or synergistic interaction of the causal mutations on the phenotype • Determination of relative importance of each of the mutations on a given phenotype using multivariate methods, such as discriminant function, principal component and step- wise regression methods • Determination of direct and indirect effect of polymoφhisms on a complex phenotype using path analysis (partial regression ) methods • Determination of the effects of specific environment on a given genotype - genotype x environment interactions using joint regression and additive and multiplicative parameter methods. Genetic epidemiology • Determination of sample size based on the disease and the marker frequency in the "case" and in the "control" populations • Stratification of study population based on gender, ethnic, socio-economic variation • Establishing a "causal relationship" between genotype and disease, using , using various association and linkage approaches - viz., case-control designs, family studies (if available), transmission disequilibrium tests etc., • Linkage analysis between markers and a candidate locus using two-point and multipoint approaches. Computer programs used for genetic analysis are: Dna SP version 3.0, by Juilo Rozas, University of Barcelona, Spain. Http://www.bio.ub.cs/-Julio; Arlequin 1.1 by S. Schnieder, J-M Kueffer, D. Roessli and L. Excoffϊer. University of Geneva, Switzerland, http://ant-hropologie.unige.ch/arlequin. PAUP*4, by D. L. Swofford, Sinauer Associates, Inc., 1999. SYSTAT software, SPSS Inc., Chicago, IL, 1998; . Linkage User's Guide, by J. Ott, Rockefeller University, Http://Linkage.rockefeller.edu/soft/linkage Guidance in the selection of appropriate genetic statistical tests for analysis of data can be obtained from texts such as: Fundamentals of Genetic Epidemiology (Monographs in Epidemiology and Biostatistics, Vol 22) by M. J. Khoury, B. H. Cohen & T. H. Beaty, Oxford Univ Press, 1993; Methods in Genetic Epidemiology by Newton E. Morton, S. Karger Publishing, 1983; Methods in Observational Epidemiology, 2nd edition (Monographs in Epidemiology and Biostatistics, V. 26) by J. L. Kelsey (Editor), A. S. Whittemore & A. S. Evans, 1996; Clinical Trials : Design, Conduct, and Analysis (Monographs in Epidemiology and Biostatistics, Vol 8) by C L. Meinert & S. Tonascia, 1986) I. Retrospective clinical trials. In general the goal of retrospective clinical trials is to test and refine hypotheses regarding genetic factors that are associated with drag responses. The best supported hypotheses can subsequently be tested in prospective clinical trials, and data from the prospective trials will likely comprise the main basis for an application to register the drag and predictive genetic test with the appropriate regulatory body. In some cases, however, it may become acceptable to use data from retrospective trials to support regulatory filings. Exemplary strategies and criteria for stratifying patients in a retrospective clinical trial are provided below. Clinical trials to study the effect of one gene locus on drag response A. Stratify patients by genotype at one candidate variance in the candidate gene locus. 1. Genetic stratification of patients can be accomplished in several ways, including the following (where 'A ' is the more frequent form of the variance being assessed and 'a' is the less frequent form): (a) AA vs. aa (b) AA vs. Aa vs. aa (c) AA vs. (Aa + aa) (d) (AA + Aa) vs. aa. 2. The effect of genotype on drag response phenotype may be affected by a variety of nongenetic factors. Therefore it may be beneficial to measure the effect of genetic stratification in a subgroup of the overall clinical trial population. Subgroups can be defined in a number of ways including, for example, biological, clinical, pathological or environmental criteria. For example, the predictive value of genetic stratification can be assessed in a subgroup or subgroups defined by: a. Biological criteria: i. gender (males vs. females) ii. age (for example above 60 years of age). Two, three or more age groups may be useful for defining subgroups for the genetic analysis, iii. hormonal status and reproductive history, including pre- vs. post- menopausal status of women, or multiparous vs. nulliparous women iv. ethnic, racial or geographic origin, or surrogate markers of ethnic, racial or geographic origin. (For a description of genetic markers that serve as sunogates of racial/thnic origin see, for example: Rannala, B. and J.L. Mountain, Detecting immigration by using multilocus genotypes. Proc Natl Acad Sci USA , 94 (17): 9197-9201, 1997. Other sunogate markers could be used, including biochemical markers.) b. Clinical criteria: i. Disease status. There are clinical grading scales for many diseases. For example, the status of Alzheimer's Disease patients is often measured by cognitive assessment scales such as the mini-mental status exam (MMSE) or the Alzheimer's Disease Assessment Scale (ADAS), which includes a cognitive component (ADAS-COG). There are also clinical assessment scales for many other diseases, including cancer. ii. Disease manifestations (clinical presentation), iii. Radiological staging criteria. c. Pathological criteria: i. Histopathologic features of disease tissue, or pathological diagnosis. (For example there are many varieties of lung cancer: squamous cell carcinoma, adenocarcinoma, small cell carcinoma, bronchoalveolar carcinoma, etc., each of which may - which, in combination with genetic variation, may correlate with ii. Pathological stage. A variety of diseases, particularly cancer, have pathological staging schemes iii. Loss of heterozygosity (LOH) iv. Pathology studies such as measuring levels of a marker protein v. Laboratory studies such as hormone levels, protein levels, small molecule levels 3. Measure frequency of responders in each genetic subgroup. Subgroups may be defined in several ways. i. more than two age groups ii. reproductive status such as pre or post-menopausal 4. Stratify by haplotype at one candidate locus where the haplotype is made up of two variances, three variances or greater than three variances. Data from already completed clinical trials can be retrospectively reanalyzed. Since the questions are new, the data can be treated as if it were a prospective trial, with identified variances or haplotypes as stratification criteria or endpoints in clinically stratified data (e.g. what is the frequency of a particular variance in a response group compared to nonresponsders). Care should be taken to in studying a population in which there may be a link between drag-related genes and disease-related genes. Retrospective pharmacogenetic trials can be conducted at each of the phases of clinical development, if sufficient data is available to conelate the physiologic effect of the candidate therapeutic intervention and the allelic variance or variances within the treatment population. In the case of a retrospective trial, the data collected from the trial can be re-analyzed by imposing the additional stratification on groups of patients by specific allelic variances that may exist in the treatment groups. Retrospective trials can be useful to ascertain whether a hypothesis that a specific variance has a significant effect on the efficacy or toxicity profile for a candidate therapeutic intervention. A prospective clinical trial has the advantage that the trial can be designed to ensure the trial objectives can be met with statistical certainty. In these cases, power analysis, which includes the parameters of allelic variance frequency, number of treatment groups, and ability to detect positive outcomes can ensure that the trial objectives are met. In designing a pharmacogenetic trial, retrospective analysis of Phase II or Phase III clinical data can indicate trial variables for which further analysis is beneficial. For example, sunogate endpoints, pharmacokinetic parameters, dosage, efficacy endpoints, ethnic and gender differences, and toxicological parameters may result in data that would require further analysis and re-examination through the design of an additional trial. In these cases, analysis involving statistics, genetics, clinical outcomes, and economic parameters may be considered prior to proceeding to the stage of designing any additional trials. Factors involved in the consideration of statistical significance may include Bonfenoni analysis, permutation testing, with multiple testing conection resulting in a difference among the treatment groups that has occuned as a result of a chance of no greater than 20% > , i.e. p< 0.20. Factors included in determining clinical outcomes to be relevant for additional testing may include, for example, consideration of the target indication, the trial endpoints, progression of the disease, disorder, or condition during the trial study period, biochemical or pathophysiologic relevance of the candidate therapeutic intervention, and other variables that were not included or anticipated in the initial study design or clinical protocol. Factors to be included in the economic significance in determining additional testing parameters include sample size, accrual rate, number of clinical sites or institutions required, additional or other available medical or therapeutic interventions approved for human use, and additional or other available medical or therapeutic interventions concurrently or anticipated to enter human clinical testing. Further, there may be patients within the treatment categories that present data that fall outside of the average or mean values, or there may be an indication of multiple allelic loci that are involved in the responses to the candidate therapeutic intervention. In these cases, one could propose a prospective clinical trial having an objective to determine the significance of the variable or parameter and its effect on the outcome of the parent Phase II trial. In the case of a pharmacogenetic difference, i.e. a single or multiple allelic difference, a population could be selected based upon the distribution of genotypes. The candidate therapeutic intervention could then be tested in this group of volunteers to test for efficacy or toxicity. The repeat prospective study could be a Phase I limited study in which the subjects would be healthy human volunteers, or a Phase II limited efficacy study in which patients which satisfy the inclusion criteria could be enrolled. In either case, the second, confirmatory trial could then be used to systematically ensure an adequate number of patients with appropriate phenotype is enrolled in a Phase III trial. A placebo controlled pharmacogenetics clinical trial design will be one in which target allelic variance or variances will be identified and a diagnostic test will be performed to stratify the patients based upon presence, absence, or combination thereof of these variances. In the Phase II or Phase III stage of clinical development, determination of a specific sample size of a prospective trial will be described to include factors such as expected differences between a placebo and treatment on the primary or secondary endpoints and a consideration of the allelic frequencies. The design of a pharmacogenetics clinical trial will include a description of the allelic variance impact on the observed efficacy between the treatment groups. Using this type of design, the type of genetic and phenotypic relationship display of the efficacy response to a candidate therapeutic intervention will be analyzed. For example, a genotypically dominant allelic variance or variances will be those in which both heterozygotes and homozygotes will demonstrate a specific phenotypic efficacy response different from the homozygous recessive genotypic group. A pharmacogenetic approach is useful for clinicians and public health professionals to include or eliminate small groups of responders or non-responders from treatment in order to avoid unjustified side-effects. Further, adjustment of dosages when clear clinical difference between heterozygous and homozygous individuals may be beneficial for therapy with the candidate therapeutic intervention In another example, a reccesive allelic variance or variances will be those in which only the homozygote recessive for that or those variances will demonstrate a specific phenotypic efficacy response different from the heterozygotes or homozygous dominants. An extension of these examples may include allelic variance or variances organized by haplotypes from additional gene or genes. V. Variance Identification and Use A. Initial Identification of variances in genes Selection of population size and composition Prior to testing to identify the presence of sequence variances in a particular gene or genes, it is useful to understand how many individuals should be screened to provide confidence that most or nearly all pharmacogenetically relevant variances will be found. The answer depends on the frequencies of the phenotypes of interest and what assumptions we make about heterogeneity and magnitude of genetic effects. Prior to testing to identify the presence of sequence variances in a particular gene or genes, it is useful to understand how many individuals should be screened to provide confidence that most or nearly all pharmacogenetically relevant variances will be found. The answer depends on the frequencies of the phenotypes of interest and what assumptions we make about heterogeneity and magnitude of genetic effects. At the beginning we only know phenotype frequencies (e.g. responders vs. nonresponders, frequency of various side effects, etc.). The most conservative assumption (resulting in the lowest estimate of allele frequency, and consequently the largest suggested screening population) is (i) that the phenotype (e.g. toxicity or efficacy) is multifactorial (i.e. can be caused by two or more variances or combinations of variances), (ii) that the variance of interest has a high degree of penetrance (i.e. is consistently associated with the phenotype), and (iii) that the mode of transmission is Mendelian dominant. Consider a pharmacogenetic study designed to identify predictors of efficacy for a compound that produces a 15% response rate in a nonstratified population. If half the response is sustantially attributable to a given variance, and the variance is consistently associated with a positive response (in 80% of cases) and the variance need only be present in one copy to produce a positive result then ~10%> of the subjects are likely heterozygotes for the variance that produces the response. The Hardy- Weinberg equation can be used to infer an allele frequency in the range of 5%> from these assumptions (given allele frequencies of 5%/95%> then: 2 x .05 x .95 = .095, or 9.5% heterozygotes are expected, and 0.05 x 0.05 = 0.0025, or 0.25%o homozygotes are expected. They sum to 9.5% + 0.25% = 9.75%> likely responders, 80%> of whom, or 7.6%, are likely real responders due to presence of the positive response allele. Thus about half of the 15%> responders are accounted for.). From the Table it can be seen that, in order to have a 99% chance of detecting an allele present at a frequency of 5%> nearly 50 subjects should be screened for variances, assuming that the variances occur in the screening population at the same frequency as they occur in the patient population. Similar analyses can be performed for other assumptions regarding likely magnitude of effect, penetrance and mode of genetic transmission. At the beginning we only know phenotype frequencies (e.g. responders vs. nonresponders, frequency of various side effects, etc.). As an example, the occunence of serious 5-FU/FA toxicity - e.g. toxicity requiring hospitalization is often >10%. The occunence of life threatening toxicity is in the 1-3% range (Buroker et al. 1994). The occunence of complete remissions is on the order of 2- 8%. The lowest frequency phenotypes are thus on the order of -2%. If we assume that (i) homogeneous genetic effects are responsible for half the phenotypes of interest and (ii) for the most part the extreme phenotypes represent recessive genotypes, then we need to detect alleles that will be present at -10% frequency (.1 x .1 = .01, or 1%) frequency of homozygotes) if the population is at Hardy- Weinberg equilibrium. To have a ~99%o chance of identifying such alleles would require searching a population of 22 individuals (see Table below). If the major phenotypes are associated with heterozygous genotypes then we need to detect alleles present at -.5% frequency (2 x .005 x .995 = .00995, or ~1%> frequency of heterozygotes). A 99% chance of detecting such alleles would require -40 individuals (Table below). Given the heterogeneity of the North American population we cannot assume that all genotypes are present in Hardy- Weinberg proportions, therefore a substantial oversampling may be done to increase the chances of detecting relevant variances: For our initial screening, usually, 62 individuals of known race/ethnicity are screened for variance. Variance detection studies can be extended to outliers for the phenotypes of interest to cover the possibility that important variances were missed in the normal population screening. Likelihood of Detecting Polymorphism in a Population as a Function of Allele Frequency & Number of Individuals Genotyped The table above shows the probability (expressed as percent) of detecting both alleles (i.e. detecting heterozygotes) at a biallelic locus as a function of (i) the allele frequencies and (ii) the number of individuals genotyped. The chances of detecting heterozygotes increases as the frequencies of the two alleles approach 0.5 (down a column), and as the number of individuals genotyped increases (to the right along a row). The numbers in the table are given by the formula: 1 - (p)~ n - (q) . Allele frequencies are designated p and q and the number of individuals tested is designated n. (Since humans are diploid, the number of alleles tested is twice the number of individuals, or 2n.) While it is preferable that numbers of individuals, or independent sequence samples, are screened to identify variances in a gene, it is also very beneficial to identify variances using smaller numbers of individuals or sequence samples. For example, even a comparison between the sequences of two samples or individuals can reveal sequence variances between them. Preferably, 5, 10, or more samples or individuals are screened. Source of nucleic acid samples Nucleic acid samples, for example for use in variance identification, can be obtained from a variety of sources as known to those skilled in the art, or can be obtained from genomic or cDNA sources by known methods. For example, the Coriell Cell Repository (Camden, NJ.) maintains over 6,000 human cell cultures, mostly fibroblast and lymphoblast cell lines comprising the NIGMS Human Genetic Mutant Cell Repository. A catalog (http://locus.umdnj.edu/nigms) provides racial or ethnic identifiers for many of the cell lines. It is preferable to perform polymoφhism discovery on a population that mimics the population to be evaluated in a clinical trial, both in terms of racial/ethnic/geographic background and in terms of disease status. Otherwise, it is generally preferable to include a broad population sample including, for example, (for trials in the United States): Caucasians of Northern, Central and Southern European origin, Africans or African- Americans, Hispanics or Mexicans, Chinese, Japanese, American Indian, East Indian, Arabs and Koreans. Source of human DNA, RNA and cDNA samples PCR based screening for DNA polymoφhism can be carried out using either genomic DNA or cDNA produced from mRNA. For many genes, only cDNA sequences have been published, therefore the analysis of those genes is, at least initially, at the cDNA level since the determination of intron-exon boundaries and the isolation of flanking sequences is a laborious process. However, screening genomic DNA has the advantage that vaπances can be identified m promoter, intron and flanking regions Such vaπances may be biologically relevant Therefore preferably, when vanance analysis of patients with outlier responses is performed, analysis of selected loci at the genomic level is also performed Such analysis would 3 be contingent on the availability of a genomic sequence or mtron-exon boundary sequences, and would also depend on the anticipated biological importance of the gene in connection with the particular response When cDNA is to be analyzed it is very beneficial to establish a tissue source in which the genes of interest are expressed at sufficient levels that cDNA can be 10 readily produced by RT-PCR Preliminary PCR optimization efforts for 19 of the 29 genes m Table 2 reveal that all 19 can be amplified from lymphoblastoid cell mRNA The 7 untested genes belong on the same pathways and are expected to also be PCR amphfiable l ; PCR Optimization Pπmers for amplifying a particular sequence can be designed by methods known to those skilled in the art, including by the use of computer programs such as the PRIMER software available from Whitehead Institute/MIT Genome Center In some cases it is preferable to optimize the amplification process according to 20 parameters and methods known to those skilled in the art, optimization of PCR reactions based on a limited anay of temperature, buffer and pnmer concentration conditions is utilized New pπmers are obtained if optimization fails with a particular pnmer set 25 Variance detection using T4 endonuclease VII mismatch cleavage method Any of a vanety of different methods for detecting vaπances in a particular gene can be utilized, such as those descnbed m the patents and applications cited m section A above An exemplary method is a T4 EndoVII method The enzyme T4 ^0 endonuclease VII (T4E7) is denved from the bacteriophage T4 T4E7 specifically cleaves heteroduplex DNA containing single base mismatches, deletions or insertions The site of cleavage is 1 to 6 nucleotides 3' of the mismatch. This activity has been exploited to develop a general method for detecting DNA sequence vanances (Youil et al 1995, Mashal and Sklar, 1995) A quality controlled T4E7 ι-> vanance detection procedure based on the T4E7 patent of R G H Cotton and co- workers (Del Tito et al , in press) is preferably utilized T4E7 has the advantages of being rapid, inexpensive, sensitive and selective Further, since the enzyme pinpoints the site of sequence variation, sequencing effort can be confined to a 25 - 30 nucleotide segment. The major steps in identifying sequence variations in candidate genes using T4E7 are: (1) PCR amplify 400-600 bp segments from a panel of DNA samples; (2) mix a fluorescently-labeled probe DNA with the sample DNA; (3) heat and cool the samples to allow the formation of heteroduplexes; (4) add T4E7 enzyme to the samples and incubate for 30 minutes at 37°C, during which cleavage occurs at sequence variance mismatches; (5) ran the samples on an ABI 377 sequencing apparatus to identify cleavage bands, which indicate the presence and location of variances in the sequence; (6) a subset of PCR fragments showing cleavage are sequenced to identify the exact location and identity of each variance. The T4E7 Variance Imaging procedure has been used to screen particular genes. The efficiency of the T4E7 enzyme to recognize and cleave at all mismatches has been tested and reported in the literature. One group reported detection of 81 of 81 known mutations (Youil et al. 1995) while another group reported detection of 16 of 17 known mutations (Mashal and Sklar, 1995). Thus, the T4E7 method provides highly efficient variance detection. DNA sequencing A subset of the samples containing each unique T4E7 cleavage site is selected for sequencing. DNA sequencing can, for example, be performed on ABI 377 automated DNA sequencers using BigDye chemistry and cycle sequencing. Analysis of the sequencing runs will be limited to the 30-40 bases pinpointed by the T4E7 procedure as containing the variance. This provides the rapid identification of the altered base or bases. In some cases, the presence of variances can be infened from published articles which describe Restriction Fragment Length Polymoφhisms (RFLP). The sequence variances or polymoφhisms creating those RFLPs can be readily determined using convention techniques, for example in the following manner. If the RFLP was initially discovered by the hybridization of a cDNA, then the molecular sequence of the RFLP can be determined by restricting the cDNA probe into fragments and separately hybridizing to a Southern blot consisting of the restriction digestion with the enzyme which reveals the polymoφhic site, identifying the sub-fragment which hybridizes to the polymoφhic restriction fragment, obtaining a genomic clone of the gene (e.g., from commercial services such as Genome Systems (Saint Louis, Missouri) or Research Genetics (Alabama) which will provide appropriate genomic clones on receipt of appropriate primer pairs). Using the genomic clone, restrict the genomic clone with the restriction enzyme which revealed the polymoφhism and isolate the fragment which contains the polymoφhism, e.g., identifying by hybridization to the cDNA which detected the polymoφhism. The fragment is then sequenced across the polymoφhic site. A copy of the other allele can be obtained by PCT from addition samples. Variance detection using sequence scanning In addition to the physical methods, e.g., those described above and others known to those skilled in the art (see, e.g., Housman, U.S. Patent 5,702,890; Housman et al., U.S. Patent Application 09/045,053), variances can be detected using computational methods, involving computer comparison of sequences from two or more different biological sources, which can be obtained in various ways, for example from public sequence databases. The term "variance scanning" refers to a process of identifying sequence variances using computer-based comparison and analysis of multiple representations of at least a portion of one or more genes. Computational variance detection involves a process to distinguish trae variances from sequencing enors or other artifacts, and thus does not require perfectly accurate sequences. Such scanning can be performed in a variety of ways, preferably, for example, as described in Stanton et al., filed October 14, 1999, serial number 09/419,705, attorney docket number 246/128. While the utilization of complete cDNA sequences is highly prefened, it is also possible to utilize genomic sequences. Such analysis may be desired where the detection of variances in or near splice sites is sought. Such sequences may represent full or partial genomic DNA sequences for a gene or genes. Also, as previously indicated, partial cDNA sequences can also be utilized although this is less preferred. As described below, the variance scanning analysis can simply utilize sequence overlap regions, even from partial sequences. Also, while the present description is provided by reference to DNA, e.g., cDNA, some sequences may be provided as RNA sequences, e.g., mRNA sequences. Such RNA sequences may be converted to the conesponding DNA sequences, or the analysis may use the RNA sequences directly. B. Determination of Presence or Absence of Known Variances The identification of the presence of previously identified variances in cells of an individual, usually a particular patient, can be performed by a number of different techniques as indicated in the Summary above. Such methods include methods utilizing a probe which specifically recognizes the presence of a particular nucleic acid or amino acid sequence in a sample. Common types of probes include nucleic acid hybridization probes and antibodies, for example, monoclonal antibodies, which can differentially bind to nucleic acid sequences differing in one or more variance sites or to polypeptides which differ in one or more amino acid residues as a result of the nucleic acid sequence variance or variances. Generation and use of such probes is well-known in the art and so is not described in detail herein. Preferably, however, the presence or absence of a variance is determined using nucleotide sequencing of a short sequence spanning a previously identified variance site. This will utilize validated genotyping assays for the polymoφhisms previously identified. Since both normal and tumor cell genotypes can be measured, and since tumor material will frequently only be available as paraffin embedded sections (from which RNA cannot be isolated), it will be necessary to utilize genotyping assays that will work on genomic DNA. Thus PCR reactions will be designed, optimized, and validated to accommodate the intron-exon stracture of each of the genes. If the gene structure has been published (as it has for some of the listed genes), PCR primers can be designed directly. However, if the gene stmcture is unknown, the PCR primers may need to be moved around in order to both span the variance and avoid exon-intron boundaries. In some cases one-sided PCR methods such as bubble PCR (Ausubel et al. 1997) may be useful to obtain flanking intronic DNA for sequence analysis. Using such amplification procedures, the standard method used to genotype normal and tumor tissues will be DNA sequencing. PCR fragments encompassing the variances will be cycle sequenced on ABI 377 automated sequencers using Big Dye chemistry C. Conelation of the Presence or Absence of Specific Variances with Differential Treatment Response Prior to establishment of a diagnostic test for use in the selection of a treatment method or elimination of a treatment method, the presence or absence of one or more specific variances in a gene or in multiple genes is conelated with a differential treatment response. (As discussed above, usually the existence of a variable response and the conelation of such a response to a particular gene is performed first.) Such a differential response can be determined using prospective and/or retrospective data. Thus, in some cases, published reports will indicate that the course of treatment will vary depending on the presence or absence of particular variances. That information can be utilized to create a diagnostic test and/or incoφorated in a treatment method as an efficacy or safety determination step. Usually, however, the effect of one or more variances is separately determined. The determination can be performed by analyzing the presence or absence of particular vanances m patients who have previously been treated with a particular treatment method, and conelating the vanance presence or absence with the observed course, outcome, and/or development of adverse events in those patients This approach is useful in cases in which observation of treatment effects was clearly recorded and cell samples are available or can be obtained Alternatively, the analysis can be performed prospectively, where the presence or absence of the vanance or vanances in an individual is determined and the course, outcome, and/or development of adverse events m those patients is subsequently or concunently observed and then conelated with the vanance determination Analysis of Haplotypes Increases Power of Genetic Analysis In some cases, vaπation in activity due to a single gene or a single genetic vanance in a single gene may not be sufficient to account for a clinically significant fraction of the observed vanation m patient response to a treatment, e g , a drug, there may be other factors that account for some of the vanation in patient response Drag response phenotypes may vary continuously, and such (quantitative) traits may be influenced by a number of genes (Falconer and Mackay, Quantitative Genetics, 1997) Although it is impossible to determine a priori the number of genes influencing a quantitative trait, potentially only one or a few loci have large effects, where a large effect is 5-20%> of total vaπation in the phenotype (Mackay, 1995) Ha\ ing identified genetic vaπation in enzymes that may affect action of a specific drag, it is useful to efficiently address its relation to phenotypic vanation. The sequential testing for conelation between phenotypes of interest and single nucleotide polymoφhisms may be adequate to detect associations if there are major effects associated with single nucleotide changes, certainly it is useful to this type of analysis However there is no way to know in advance whether there are major phenotypic effects associated with single nucleotide changes and, even if there are, there is no way to be sure that the salient vanance has been identified by screening cDNAs A more powerful way to address the question of genotype-phenotype conelation is to assort genotypes into haplotypes (A haplotype is the cis anangement of polymoφhic nucleotides on a particular chromosome ) Haplotype analysis has several advantages compared to the senal analysis of individual polymoφfnsms at a locus with multiple polymoφhic sites (1) Of all the possible haplotypes at a locus (2 π haplotypes are theoretically possible at a locus with n binary polymoφhic sites) only a small fraction will generally occur at a significant frequency in human populations. Thus, association studies of haplotypes and phenotypes will involve testing fewer hypotheses. As a result there is a smaller probability of Type I enors, that is, false inferences that a particular variant is associated with a given phenotype. (2) The biological effect of each variance at a locus may be different both in magnitude and direction. For example, a polymoφhism in the 5' UTR may affect translational efficiency, a coding sequence polymoφhism may affect protein activity, a polymoφhism in the 3' UTR may affect mRNA folding and half life, and so on. Further, there may be interactions between variances: two neighboring polymoφhic amino acids in the same domain - say cys/arg at residue 29 and met/val at residue 166 - may, when combined in one sequence, for example, 29cys-166val, have a deleterious effect, whereas 29cys-166met, 29arg-166met and 29arg-166val proteins may be nearly equal in activity. Haplotype analysis is the best method for assessing the interaction of variances at a locus. (3) Templeton and colleagues have developed powerful methods for assorting haplotypes and analyzing haplotype/phenotype associations (Templeton et al., 1987). Alleles which share common ancestry are ananged into a tree stracture (cladogram) according to their (infened) time of origin in a population (that is, according to the principle of parsimony). Haplotypes that are evolutionarily ancient will be at the center of the branching stracture and new ones (reflecting recent mutations) will be represented at the periphery, with the links representing intermediate steps in evolution. The cladogram defines which haplotype-phenotype association tests should be performed to most efficiently exploit the available degrees of freedom, focusing attention on those comparisons most likely to define functionally different haplotypes (Haviland et al., 1995). This type of analysis has been used to define interactions between heart disease and the apolipoprotein gene cluster (Haviland et al 1995) and Alzheimer's Disease and the Apo-E locus (Templeton 1995) among other studies, using populations as small as 50 to 100 individuals. The methods of Templeton have also been applied to meaure the genetic determinants of variation in the angiotensin-I converting enzyme gene. (Keavney, B., McKenzie, C A., Connoll, J.M.C, et al. Measured haplotype analysis of the angiotensin-I converting enzyme gene. Human Molecular Genetics 7: 1745- 1751.) Methods for determining haplotypes The goal of haplotyping is to identify the common haplotypes at selected loci that have multiple sites of variance. Haplotypes are usually determined at the cDNA level. Several general approaches to identification of haplotyes can be employed. Haplotypes may also be estimated using computational methods or determined definitively using experimental approaches. Computational approachs generally include an expectation maximization (E-M) algorithm (see, for example: Excoffier and Slatkin, Mol. Biol. Evol. 1995) or a combination of Parsimony (see below) and E-M methods. Haplotypes can be determined experimentally without requirement of a haplotyping method by genotyping samples from a set of pedigrees and observing the segregation of haplotypes. For example families collected by the Centre d'Etude du Polymoφhisme Humaine (CEPH) can be used. Cell lines from these families are available from the Coriell Repository. This approach will be useful for cataloging common haplotypes and for validating methods on samples with known haplotypes. The set of haplotypes determined by pedigree analysis can be useful in computational methods, including those utilizing the E-M algorithm. Haplotypes can also be determined directly from cDNA using the T4E7 procedure. T4E7 cleaves mismatched heteroduplex DNA at the site of the mismatch. If a heteroduplex contains only one mismatch, cleavage will result in the generation of two fragments. However, if a single heteroduplex (allele) contains two mismatches, cleavage will occur at two different sites resulting in the generation of three fragments. The appearance of a fragment whose size conesponds to the distance between the two cleavage sites is diagnostic of the two mismatches being present on the same strand (allele). Thus, T4E7 can be used to determine haplotypes in diploid cells. An alternative method, allele specific PCR, may be used for haplotyping. The utility of allele specific PCR for haplotyping has already been established (Michalatos-Beloin et al., 1996; Chang et al. 1997). Opposing PCR primers are designed to cover two sites of variance (either adjacent sites or sites spanning one or more internal variances). Two versions of each primer are synthesized, identical to each other except for the 3' terminal nucleotide. The 3' terminal nucleotide is designed so that it will hybridize to one but not the other variant base. PCR amplification is then attempted with all four possible primer combinations in separate wells. Because Taq polymerase is very inefficient at extending 3' mismatches, the only samples which will be amplified will be the ones in which the two primers are perfectly matched for sequences on the same strand (allele). The presence or absence of PCR product allows haplotyping of diploid cell lines. At most two of four possible reactions should yield products. This procedure has been successfully applied, for example, to haplotype the DPD amino acid polymoφhisms. Parsimony methods are also useful for classifying DNA sequences, haplotypes or phenotypic characters. Parsimony pπnciple maintains that the best explanation for the observed differences among sequences, phenotypes (individuals, species) etc., is provided by the smallest number of evolutionary changes. Alternatively, simpler hypotheses are preferable to explain a set of data or patterns, than more complicated ones, and ad hoc hypotheses should be avoided whenever possible (Molecular Systematics, Hilhs et al., 1996). Parsimony methods thus operate by minimizing the number of evolutionary steps or mutations (changes from one sequence/character) required to account for a given set of data. For example, supposing we want to obtain relationships among a set of sequences and construct a stracture (tree/topology), we first count the minimum number of mutations that are required for explaining the observed evolutionary changes among a set of sequences A structure (topology) is constructed based on this number. When once this number is obtained, another stracture is tned. This process is continued for all reasonable number of structures. Finally, the stracture that required the smallest number of mutational steps is chosen as the likely structure/evolutionary tree for the sequences studied. D Selection of Treatment Method Using Vanance Information 1. General Once the presence or absence of a vanance or vanances in a gene or genes is shown to conelate with the efficacy or safety of a treatment method, that information can be used to select an appropnate treatment method for a particular patient. In the case of a treatment which is more likely to be effective when administered to a patient who has at least one copy of a gene with a particular vanance or variances (in some cases the conelation with effective treatment is for patients who are homozygous for a vanance or set of vanances in a gene) than in patients with a different vanance or set of variances, a method of treatment is selected (and/or a method of administration) which conelates positively with the particular variance presence or absence which provides the indication of effectiveness. As indicated in the Summary, such selection can involve a vanety of different choices, and the conelation can involve a vanety of different types of treatments, or choices of methods of treatment. In some cases, the selection may include choices between treatments or methods of administration where more than one method is likely to be effective, or where there is a range of expected effectiveness or different expected levels of contra-indication or deletenous effects. In such cases the selection is preferably performed to select a treatment which will be as effective or more effective than other methods, while having a comparatively low level of deleterious effects. Similarly, where the selection is between method with differing levels of deleterious effects, preferably a method is selected which has low such effects but which is expected to be effective in the patient. Alternatively, in cases where the presence or absence of the particular variance or variances is indicative that a treatment or method of administration is more likely to be ineffective or contra-indicated in a patient with that variance or variances, then such treatment or method of administration is generally eliminated for use in that patient. 2. Diagnostic Methods Once a conelation between the presence and absence of at least one variance in a gene or genes and an indication of the effectiveness of a treatment, the determination of the presence or absence of that at least one variance provides diagnostic methods, which can be used as indicated in the Summary above to select methods of treatment, methods of administration of a treatment, methods of selecting a patient or patients for a treatment and others aspects in which the determination of the presence or absence of those variances provides useful information for selecting or designing or preparing methods or materials for medical use in the aspects of this invention. As previously stated, such variance determination or diagnostic methods can be performed in various ways as understood by those skilled in the art. In certain variance determination methods, it is necessary or advantageous to amplify one or more nucleotide sequences in one or more of the genes identified herein. Such amplification can be performed by conventional methods, e.g., using polymerase chain reaction (PCR) amplification. Such amplification methods are well-known to those skilled in the art and will not be specifically described herein. For most applications relevant to the present invention, a sequence to be amplified includes at least one variance site, which is preferably a site or sites which provide variance information indicative of the effectiveness of a method of treatment or method of administration of a treatment, or effectiveness of a second method of treatment which reduces a deleterious effect of a first treatment method, or which enhances the effectiveness of a first method of treatment. Thus, for PCR, such amplification generally utilizes primer oligonucleotides which bind to or extent through at least one such variance site under amplification conditions. For convenient use of the amplified sequence, e.g., for sequencing, it is beneficial that the amplified sequence be of limited length, but still long enough to allow convenient and specific amplification Thus, preferably the amplified sequence has a length as descnbed in the Summary. Also, in certain vanance determination, it is useful to sequence one or more portions of a gene or genes, in particular, portions of the genes identified in this disclosure As understood by persons familiar with nucleic acid sequencing, there are a vanety of effective methods In particular, sequencing can utilize dye termination methods and mass spectrometnc methods The sequencing generally involves a nucleic acid sequence which includes a vanance site as indicated above m connection with amplification Such sequencing can directly provide determination of the presence or absence of a particular vanance or set of vaπances, e g., a haplotype, by inspection of the sequence (visually or by computer) Such sequencing is generally conducted on PCR amplified sequences in order to provide sufficient signal for practical or reliable sequence determination Likewise, m certain vanance determinations, it is useful to utilize a probe or probes As previously descnbed, such probes can be of a vanety of different types VII. Loss of Heterozygosity and Conditionally Essential Genes Different environmental, pharmacological, and physical changes in the environment that result in homeostatic or compensatory responses in which genes that are not normally essential for cell survival or proliferation become essential are known in the art. When LOH results in a difference m normal cell genotype vs cancer cell genotype that affects a locus encoding a product affecting the cells' ability to survive in the presence of an environmental change, or a pharmaceutical or biological agent, or a physical factor, there is an opportunity to exploit a therapeutic window between cancer cells and normal cells Below we descπbe specific examples of genes that ( 1 ) affect cell responses to altered environments, (2) are located on chromosomes that undergo LOH in cancer and (3) exist in two or more vanant forms. These examples have been selected to illustrate how the therapeutic strategy descnbed m this application would work with a vanety of different alterations in chemical or physical environment Example 20 descnbes a gene (Dihydropyπmidme Dehydrogenase) that mediates response to an altered chemical environment (presence of the toxic chemical 5-floxuπdιne) by specifically transforming the chemical to an inactive metabolite Example 27 descπbes a gene (Methyl guanine methyltransferase) that mediates response to an altered chemical environment (presence of toxic chemicals such as mtrosourea or other alkylating agents) by removing methyl or alkyl adducts to DNA, the pπncipal toxic lesion of these agents. Example 21 describes a set of genes (Fanconi Anemia genes A,B,C,D,E,F,G and H) which mediate response to an altered chemical environment (presence of chemicals which cause DNA crosslinking, such as diepoxybutane, mitomycin C and cisplatinum) by repairing the crosslinks. Example 25 describes a set of genes (the DNA Dependent Protein Kinase Complex, including the DNA Dependent Protein Kinase catalytic subunit (DNA-PKcs), the DNA binding component (called Ku), made up of Ku-70 and Ku-86 kDa subunits, and the Ku-86 related protein Kaφ-1) that mediates repair of double stranded DNA breaks, such as occurs after x-inadiation. Example 22 describes a gene (asparagine synthase) that mediates response to an altered nutritional environment (absence of extracellular asparagine) which can be produced by an enzyme such as asparaginase, which hydrolyzes semm asparagine. Example 26 describes the Ataxia Telangiectasia gene, which is involved in response to ionizing radiation and radiomimetic chemicals. Other detailed examples include methionine synthase (Ex. 23) and methylthioadenosine phosphorylase (Ex. 24). Other examples include Poly (ADP) Ribose Polymerase (PARP), Glutathione-S- Transferase pi (GST-pi), NF-kappa B, Abl Kinase, 3-alkaylguanine alkyltransferase, N-methylpurine DNA glycosylase (hydrolyzes the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7-methylguanine from alkylating agent-damaged DNA polymers), OGG-1, MDR-1. In addition to the direct use of conditionally essential (or essential) genes in allele-specific inhibitor applications, the information provided by the LOH status of a gene. For example, in some cases, the effect of LOH can be a gene dosage effeect. This can additionally be combined with a reduced activity associated with particular forms of the gene. Either or both types of information can be used to identify patients who would be expected to respond differently to a treatment targeting that gene than would patients with two copies of the gene, or with at least one copy of a different form of the gene than remained after LOH. To illustrate, a patient may be heterozygous for a high activity allele and a low activity allele. LOH in cancer cells could remove either the high activity allele or the low activity allele, leaving only the other allele in cancer cells in the patient, while the normal cells would have intermediate activity due the presenece of both alleles. As a result, a therapy targeting or otherwise involving that gene in the response to treatment would be expected to result in variation in response between the normal cells and the cancer cells in the patient. If the low activity allele conelated with high response to the therapy, then it would be expected that the anti-cancer treatment would be more effective in a patient with such LOH than in a patient in whom cancer cells had not undergone LOH with respect to that gene. Indeed, LOH assays for particular genes can also be used as sunogate assays for other LOH of other genes located near the marker gene. Thus, the marker gene can, for example, be used in connection with LOH-related effects or evaluations of other nearby genes. Such genes can include genes in the same pathway, as those genes are often located in close proximity on the same chromosome. In has been shown that LOH at tumor suppressor genes conelates with anticancer chemotherapy response. Thus, LOH information on tumor suppressor genes can also be used in connection with LOH and/or pharmacogenetic information about other genes. As a result, it is beneficial to determine both the LOH status of the tumor suppressor gene or genes and one or more additional genes. Together, or separately, the LOH information and the variance-based pharmacogenetic information can be used to identifiy patient subset that will respond differently to a particular therapy related to particular genes and/or to select appropriate therapies for patients based on the forms of the gene or genes in disease cells and normal cells. VII. Pharmaceutical Compositions, Including Pharmaceutical Compositions Adapted to be Preferentially Effective in Patients Having Particular Genetic Characteristics A. General The methods of the present invention, in many cases will utilize conventional pharmaceutical compositions, but will allow more advantageous and beneficial use of those compositions due to the ability to identify patients who are likely to benefit from a particular treatment or to identify patients for whom a particular treatment is less likely to be effective or for whom a particular treatment is likely to produce undesirable or intolerable effects. However, in some cases, it is advantageous to utilize compositions which are adapted to be preferentially effective in patients who possess particular genetic characteristics, i.e., in whom a particular variance or variances in one or more genes is present or absent (depending on whether the presence or the absence of the variance or variances in a patient is conelated with an increased expectation of beneficial response). Thus, for example, the presence of a particular variance or variances may indicate that a patient can beneficially receive a significantly higher dosage of a drug than a patient having a different B. Regulatory Indications and Restrictions The sale and use of drags and the use of other treatment methods usually are subject to certain restrictions by a government regulatory agency charged with ensuring the safety and efficacy of drags and treatment methods for medical use, and approval is based on particular indications. In the present invention it is found that variability in patient response or patient tolerance of a drag or other treatment often conelates with the presence or absence of particular variances in particular genes. Thus, it is expected that such a regulatory agency may indicate that the approved indications for use of a drag with a variance-related variable response or toleration include use only in patients in whom the drug will be effective, and/or for whom the administration of the drag will not have intolerable deleterious effects, such as excessive toxicity or unacceptable side-effects. Conversely, the drug may be given for an indication that it may be used in the treatment of a particular disease or condition where the patient has at least one copy of a particular variance, variances, or variant form of a gene. Even if the approved indications are not nanowed to such groups, the regulatory agency may suggest use limited to particular groups or excluding particular groups or may state advantages of use or exclusion of such groups or may state a warning on the use of the drag in certain groups. Consistent with such suggestions and indications, such an agency may suggest or recommend the use of a diagnostic test to identify the presence or absence of the relevant variances in the prospective patient. Such diagnostic methods are described in this description. Generally, such regulatory suggestion or indication is provided in a product insert or label, and is generally reproduced in references such as the Physician's Desk Reference (PDR). Thus, this invention also includes drags or pharmaceutical compositions which cany such a suggestion or statement of indication or warning or suggestion for a diagnostic test, and which may also be packaged with an insert or label stating the suggestion or indication or warning or suggestion for a diagnostic test. In accord with the possible variable treatment responses, an indication or suggestion can specify that a patient be heterozygous, or alternatively, homozygous for a particular variance or variances or variant form of a gene. Alternatively, an indication or suggestion may specify that a patient have no more than one copy, or zero copies, of a particular variance, variances, or variant form of a gene. A regulatory indication or suggestion may concern the variances or variant forms of a gene in normal cells of a patient and/or in cells involved in the disease or condition. For example, in the case of a cancer treatment, the response of the cancer cells can depend on the form of a gene remaining in cancer cells following loss of heterozygosity affecting that gene. Thus, even though normal cells of the patient may contain a form of the gene which conelates with effective treatment response, the absence of that form in cancer cells will mean that the treatment would be less likely to be effective in that patient than in another patient who retained in cancer cells the form of the gene which conelated with effective treatment response. Those skilled in the art will understand whether the variances or gene forms in normal or disease cells are most indicative of the expected treatment response, and will generally utilize a diagnostic test with respect to the appropriate cells. Such a cell type indication or suggestion may also be contained in a regulatory statement, e.g., on a label or in a product insert. C. Preparation and Administration of Drags and Pharmaceutical Compositions Including Pharmaceutical Compositions Adapted to be Preferentially Effective in Patients Having Particular Genetic Characteristics A particular compound useful in this invention can be administered to a patient either by itself, or in pharmaceutical compositions where it is mixed with suitable carriers or excipient(s). In treating a patient exhibiting a disorder of interest, a therapeutically effective amount of a agent or agents such as these is administered. A therapeutically effective dose refers to that amount of the compound that results in amelioration of one or more symptoms or a prolongation of survival in a patient. Toxicity and therapeutic efficacy of such compounds can be determined by standard pharmaceutical procedures in cell cultures or experimental animals, e.g., for determining the LD o (the dose lethal to 50% of the population) and the ED 5 o (the dose therapeutically effective in 50% of the population). The dose ratio between toxic and therapeutic effects is the therapeutic index and it can be expressed as the ratio LD 5 o/ED 5 o. Compounds which exhibit large therapeutic indices are prefened. The data obtained from these cell culture assays and animal studies can be used in formulating a range of dosage for use in human. The dosage of such compounds lies preferably within a range of circulating concentrations that include the ED 5 o with little or no toxicity. The dosage may vary within this range depending upon the dosage form employed and the route of administration utilized. For any compound used in the method of the invention, the therapeutically effective dose can be estimated initially from cell culture assays. For example, a dose can be formulated in animal models to achieve a circulating plasma concentration range that includes the IC50 as determined in cell culture. Such information can be used to more accurately determine useful doses in humans. Levels in plasma may be measured, for example, by HPLC. The exact formulation, route of administration and dosage can be chosen by the individual physician in view of the patient's condition. (See e.g. Fingl et. al., in The Pharmacological Basis of Therapeutics. 1975, Ch. 1 p.l). It should be noted that the attending physician would know how to and when to terminate, interrupt, or adjust administration due to toxicity, or to organ dysfunctions. Conversely, the attending physician would also know to adjust treatment to higher levels if the clinical response were not adequate (precluding toxicity). The magnitude of an administrated dose in the management of disorder of interest will vary with the severity of the condition to be treated and the route of administration. The severity of the condition may, for example, be evaluated, in part, by standard prognostic evaluation methods. Further, the dose and perhaps dose frequency, will also vary according to the age, body weight, and response of the individual patient. A program comparable to that discussed above may be used in veterinary medicine. Depending on the specific conditions being treated, such agents may be formulated and administered systemically or locally. Techniques for formulation and administration may be found in Remington's Pharmaceutical Sciences, 18th ed., Mack Publishing Co., Easton, PA (1990). Suitable routes may include oral, rectal, transdermal, vaginal, transmucosal, or intestinal administration; parenteral delivery, including intramuscular, subcutaneous, intramedullary injections, as well as intrathecal, direct intraventricular, intravenous, intraperitoneal, intranasal, or intraocular injections, just to name a few. For injection, the agents of the invention may be formulated in aqueous solutions, preferably in physiologically compatible buffers such as Hanks's solution, Ringer's solution, or physiological saline buffer. For such transmucosal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art. Use of pharmaceutically acceptable carriers to formulate the compounds herein disclosed for the practice of the invention into dosages suitable for systemic administration is within the scope of the invention. With proper choice of carrier and suitable manufacturing practice, the compositions of the present invention, in particular, those formulated as solutions, may be administered parenterally, such as by intravenous injection. The compounds can be formulated readily using pharmaceutically acceptable carriers well known in the art into dosages suitable for oral administration. Such carriers enable the compounds of the invention to be formulated as tablets, pills, capsules, liquids, gels, syrups, slurries, suspensions and the like, for oral ingestion by a patient to be treated. Agents intended to be administered intracellularly may be administered using techniques well known to those of ordinary skill in the art. For example, such agents may be encapsulated into liposomes, then administered as described above. Liposomes are spherical lipid bilayers with aqueous interiors. All molecules present in an aqueous solution at the time of liposome formation are incoφorated into the aqueous interior. The liposomal contents are both protected from the external microenvironment and, because liposomes fuse with cell membranes, are efficiently delivered into the cell cytoplasm. Additionally, due to their hydrophobicity, small organic molecules may be directly administered intracellularly. Pharmaceutical compositions suitable for use in the present invention include compositions wherein the active ingredients are contained in an effective amount to achieve its intended puφose. Determination of the effective amounts is well within the capability of those skilled in the art, especially in light of the detailed disclosure provided herein. In addition to the active ingredients, these pharmaceutical compositions may contain suitable pharmaceutically acceptable carriers comprising excipients and auxiliaries which facilitate processing of the active compounds into preparations which can be used pharmaceutically. The preparations formulated for oral administration may be in the form of tablets, dragees, capsules, or solutions. The pharmaceutical compositions of the present invention may be manufactured in a manner that is itself known, e.g., by means of conventional mixing, dissolving, granulating, dragee-making, levitating, emulsifying, encapsulating, entrapping or lyophilizing processes. Pharmaceutical formulations for parenteral administration include aqueous solutions of the active compounds in water-soluble form. Additionally, suspensions of the active compounds may be prepared as appropriate oily injection suspensions. Suitable lipophilic solvents or vehicles include fatty oils such as sesame oil, or synthetic fatty acid esters, such as ethyl oleate or triglyceπdes, or liposomes. Aqueous injection suspensions may contain substances which increase the viscosity of the suspension, such as sodium carboxymethyl cellulose, sorbitol, or dextran. Optionally, the suspension may also contain suitable stabilizers or agents which increase the solubility of the compounds to allow for the preparation of highly concentrated solutions. Pharmaceutical preparations for oral use can be obtained by combining the active compounds with solid excipient, optionally grinding a resulting mixture, and processing the mixture of granules, after adding suitable auxiliaries, if desired, to obtain tablets or dragee cores. Suitable excipients are, in particular, fillers such as sugars, including lactose, sucrose, mannitol, or sorbitol; cellulose preparations such as, for example, maize starch, wheat starch, rice starch, potato starch, gelatin, gum tragacanth, methyl cellulose, hydroxypropylmethyl-cellulose, sodium carboxymethylcellulose, and/or polyvinylpyrrolidone (PVP). If desired, disintegrating agents may be added, such as the cross-linked polyvinyl pynolidone, agar, or alginic acid or a salt thereof such as sodium alginate. Dragee cores are provided with suitable coatings. For this puφose, concentrated sugar solutions may be used, which may optionally contain gum arabic, talc, polyvinyl pynolidone, carbopol gel, polyethylene glycol, and/or titanium dioxide, lacquer solutions, and suitable organic solvents or solvent mixtures. Dyestuffs or pigments may be added to the tablets or dragee coatings for identification or to characterize different combinations of active compound doses. Pharmaceutical preparations which can be used orally include push-fit capsules made of gelatin, as well as soft, sealed capsules made of gelatin and a plasticizer, such as glycerol or sorbitol. The push-fit capsules can contain the active ingredients in admixture with filler such as lactose, binders such as starches, and/or lubricants such as talc or magnesium stearate and, optionally, stabilizers. In soft capsules, the active compounds may be dissolved or suspended in suitable liquids, such as fatty oils, liquid paraffin, or liquid polyethylene glycols. In addition, stabilizers may be added. The invention described herein features methods for determining the appropriate identification of a patient diagnosed with a neurolgical disease or neurolgical dysfunction based on an analysis of the patient's allele status for a gene listed in Tables 1-6, 12-17, and 18-23. Specifically, the presence of at least one allele indicates that a patient will respond to a candidate therapeutic intervention aimed at treating clinical symptoms. In a prefened approach, the patient's allele status is rapidly diagnosed using a sensitive PCR assay and a treatment protocol is rendered. The invention also provides a method for forecasting patient outcome and the suitability of the patient for entering a clinical drag trial for the testing of a candidate therapeutic intervention for a disease, condition, or dysfunction as identified herein. The findings described herein indicate the predictive value of the target allele in identifying patients at risk for a disease or disorder as identified for aspects herein. In addition, because the underlying mechanism influenced by the allele status is not disease-specific, the allele status is suitable for making patient predictions for diseases not affected by the pathway as well. The following examples, which describe exemplary techniques and experimental results, are provided for the puφose of illustrating the invention, and should not be construed as limiting. Example 1 Method for Producing cDNA In order to identify sequence variances in a gene by laboratory methods it is in some instances useful to produce cDNA(s) from multiple human subjects. (In other instances it may be preferable to study genomic DNA.). Methods for producing cDNA are known to those skilled in the art, as are methods for amplifying and sequencing the cDNA or portions thereof. An example of a useful cDNA production protocol is provided below. As recognized by those skilled in the art, other specific protocols can also be used. cDNA Production ** Make sure that all tubes and pipette tips are RNase-free. (Bake them overnight at 100°C in a vacuum oven to make them RNase-free.) 1. Add the following to a RNase-free 0.2 ml micro-amp tube and mix gently: 24 ul water (DEPC treated) 12 ul RNA (lug/ul) 12 ul random hexamers(50 ng/ul) 2. Heat the mixture to 70°C for ten minutes. 3. Incubate on ice for 1 minute. 4. Add the following: 16 ul 5 X Synthesis Buffer 8 ul 0.1 M DTT 4 ul 10 mM dNTP mix ( 10 mM each dNTP) 4 ul Superscript RT II enzyme Pipette gently to mix. 5. Incubate at 42°C for 50 minutes. 6. Heat to 70°C for ten minutes to kill the enzyme, then place it on ice. 7. Add 160 ul of water to the reaction so that the final volume is 240 ul. 8. Use PCR to check the quality of the cDNA. Use primer pairs that will give a -800 base pair long piece. See "PCR Optimization" for the PCR protocol. The following chart shows the reagent amounts for a 20 ul reaction, a 80 ul reaction, and a batch of 39 (which makes enough mix for 36) reactions: 20 ul X 1 tube 80 ul X 1 tube 80ul X 39 tubes Example 2 Method for Detecting Variances by Single Strand Conformation Polymoφhism (SSCP) Analysis This example describes the SSCP technique for identification of sequence variances of genes. SSCP is usually paired with a DNA sequencing method, since the SSCP method does not provide the nucleotide identity of variances. One useful sequencing method, for example, is DNA cycle sequencing of 32 P labeled PCR products using the Femtomole DNA cycle sequencing kit from Promega (Wl) and the instructions provided with the kit. Fragments are selected for DNA sequencing based on their behavior in the SSCP assay. Single strand conformation polymoφhism screening is a widely used technique for identifying an discriminating DNA fragments which differ from each other by as little as a single nucleotide. As originally developed by Orita et al. (Detection of polymoφhisms of human DNA by gel electrophoresis as single-strand conformation polymoφhisms. Proc Natl Acad Sci USA. 86(8):2766-70, 1989), the technique was used on genomic DNA, however the same group showed that the technique works very well on PCR amplified DNA as well. In the last 10 years the technique has been used in hundreds of published papers, and modifications of the technique have been described in dozens of papers. The enduring popularity of the technique is due to (1) a high degree of sensitivity to single base differences (>90%) (2) a high degree of selectivity, measured as a low frequency of false positives, and (3) technical ease. SSCP is almost always used together with DNA sequencing because SSCP does not directly provide the sequence basis of differential fragment mobility. The basic steps of the SSCP procdure are described below. When the intent of SSCP screening is to identify a large number of gene variances it is useful to screen a relatively large number of individuals of different racial, ethnic and/or geographic origins. For example, 32 or 48 or 96 individuals is a convenient number to screen because gel electrophoresis apparatus are available with 96 wells (Applied Biosystems Division of Perkin Elmer Coφoration), allowing 3 X 32, 2 X 48 or 96 samples to be loaded per gel. The 32 (or more) individuals screened should be representative of most of the worlds major populations. For example, an equal distribution of Africans, Europeans and Asians constitutes a reasonable screening set. One useful source of cell lines from different populations is the Coriell Cell Repository (Camden, NJ), which sells EBV immortalized lyphoblastoid cells obtained from several thousand subjects, and includes the racial ethnic/geographic background of cell line donors in its catalog. Alternatively, a panel of cDNAs can be isolated from any specific target population. SSCP can be used to analyze cDNAs or genomic DNAs. For many genes cDNA analysis is preferable because for many genes the full genomic sequence of the target gene is not available, however, this circumstance will change over the next few years. To produce cDNA requires RNA. Therefore each cell lines is grown to mass culture and RNA is isolated using an acid/phenol protocol, sold in kit form as Trizol by Life Technologies (Gaithersberg, MD). The unfractionated RNA is used to produce cDNA by the action of a modified Maloney Murine Leukemia Virus Reverse Transcriptase, purchased in kit form from Life Technologies (Superscript II kit). The reverse transcriptase is primed with random hexamer primers to initiate cDNA synthesis along the whole length of the RNAs. This proved useful later in obtaining good PCR products from the 5' ends of some genes. Alternatively, oligodT can be used to prime cDNA synthesis. Material for SSCP analysis can be prepared by PCR amplification of the cDNA in the presence of one α 32 P labeled dNTP (usually α 32 P dCTP). Usually the concentration of nonradioactive dCTP is dropped from 200 uM (the standard concentration for each of the four dNTPs) to about 100 uM, and 32 P dCTP is added to a concentration of about 0.1-0.3 uM. This involves adding a 0.3- 1 ul (3-10 uCi) of 32 P cCTP to a 10 ul PCR reaction. Radioactive nucleotides can be purchased from DuPont/New England Nuclear. The customary practice is to amplify about 200 base pair PCR products for SSCP, however, an alternative approach is to amplify about 0.8-1.4 kb fragments and then use several cocktails of restriction endonucleases to digest those into smaller fragments of about 0.1-0.4kb, aiming to have as many fragments as possible between .15 and .3 kb. The digestion strategy has the advantage that less PCR is required, reducing both time and costs. Also, several different restriction enzyme digests can be performed on each set of samples (for example 96 cDNAs), and then each of the digests can be ran separately on SSCP gels. This redundant method (where each nucleotide is surveyed in three different fragments) reduces both the false negative and false positive rates. For example: a site of variance might lie within 2 bases of the end of a fragment in one digest, and as a result not affect the conformation of that strand; the same variance, in a second or third digest, would likely lie in a location more prone to affect strand folding, and therefore be detected by SSCP. After digestion, the radiolabelled PCR products are diluted 1 :5 by adding formamide load buffer (80%> formamide, IX SSCP gel buffer) and then denatured by heating to 90%>C for 10 minutes, and then allowed to renature by quickly chilling on ice. This procedure (both the dilution and the quick chilling) promotes intra- (rather than inter-) strand association and secondary stmcture formation. The secondary stmcture of the single strands influences their mobility on nondenaturing gels, presumably by influencing the number of collisions between the molecule and the gel matrix (i.e., gel sieving). Even single base differences consistently produce changes in intrastrand folding sufficient to register as mobility differences on SSCP. The single strands were then resolved on two gels, one a 5.5% acrylamide, 0.5X TBE gel, the other an 8% acrylamide, 10% glycerol, IX TTE gel. (Other gel recipes are known to those skilled in the art.) The use of two gels provides a greater opportunity to recognize mobility differences. Both glycerol and acrylamide concentration have been shown to influence SSCP performance. By routinely analyzing three different digests under two gel conditions (effectively 6 conditions), and by looking at both strands under all 6 conditions, one can achieve a 12-fold sampling of each base pair of cDNA. However, if the goal is to rapidly survey many genes or cDNAs then a less redundant procedure would be optimal. Example 3 Method for Detecting Variances by T4 endonuclease VII (T4E7) mismatch cleavage method The enzyme T4 endonuclease VII is derived from the bacteriophage T4. T4 endonuclease VII is used by the bacteriophage to cleave branched DNA intermediates which form during replication so the DNA can be processed and packaged. T4 endonuclease can also recognize and cleave heteroduplex DNA containing single base mismatches as well as deletions and insertions. This activity of the T4 endonuclease VII enzyme can be exploited to detect sequence variances present in the general population. The following are the major steps involved in identifying sequence variations in a candidate gene by T4 endonuclease VII mismatch cleavage: 1. Amplification by the polymerase chain reaction (PCR) of 400-600 bp regions of the candidate gene from a panel of DNA samples The DNA samples can either be cDNA or genomic DNA and will represent some cross section of the world population. 2. Mixing of a fluorescently labeled probe DNA with the sample DNA. Heating and cooling the mixtures causing heteroduplex formation between the probe DNA and the sample DNA. 3. Addition of T4 endonuclease VII to the heteroduplex DNA samples. T4 endonuclease will recognize and cleave at sequence variance mismatches formed in the heteroduplex DNA. 4. Electrophoresis of the cleaved fragments on an ABI sequencer to determine the site of cleavage. 5. Sequencing of a subset of PCR fragments identified by T4 endonuclease VI to contain variances to establish the specific base variation at that location. A more detailed description of the procedure is as follows: A candidate gene sequence is downloaded from an appropriate database. Primers for PCR amplification are designed which will result in the target sequence being divided into amplification products of between 400 and 600 bp. There will be a minimum of a 50 bp of overlap not including the primer sequences between the 5' and 3' ends of adjacent fragments to ensure the detection of variances which are located close to one of the primers. Optimal PCR conditions for each of the primer pairs is determined experimentally. Parameters including but not limited to annealing temperature, pH, MgCL concentration, and KCl concentration will be varied until conditions for optimal PCR amplification are established. The PCR conditions derived for each primer pair is then used to amplify a panel of DNA samples (cDNA or genomic DNA) which is chosen to best represent the various ethnic backgrounds of the world population or some designated subset of that population. One of the DNA samples is chosen to be used as a probe. The same PCR conditions used to amplify the panel are used to amplify the probe DNA. However, a flourescently labeled nucleotide is included in the deoxy-nucleotide mix so that a percentage of the incoφorated nucleotides will be fluorescently labeled. The labeled probe is mixed with the conesponding PCR products from each of the DNA samples and then heated and cooled rapidly. This allows the formation of heteroduplexes between the probe and the PCR fragments from each of the DNA samples. T4 endonuclease VII is added directly to these reactions and allowed to incubate for 30 min. at 37 C. 10 ul of the Formamide loading buffer is added directly to each of the samples and then denatured by heating and cooling. A portion of each of these samples is electrophoresed on an ABI 377 sequencer. If there is a sequence variance between the probe DNA and the sample DNA a mismatch will be present in the heteroduplex fragment formed. The enzyme T4 endonuclease VII will recognize the mismatch and cleave at the site of the mismatch. This will result in the appearance of two peaks conesponding to the two cleavage products when mn on the ABI 377 sequencer. Fragments identified as containing sequencing variances are subsequently sequenced using conventional methods to establish the exact location and sequence variance. Example 4 Method for Detecting Variances by DNA sequencing. Sequencing by the Sanger dideoxy method or the Maxim Gilbert chemical cleavage method is widely used to determine the nucleotide sequence of genes. Presently, a worldwide effort is being put forward to sequence the entire human genome. The Human Genome Project as it is called has already resulted in the identification and sequencing of many new human genes. Sequencing can not only be used to identify new genes, but can also be used to identify variations between individuals in the sequence of those genes. The following are the major steps involved in identifying sequence variations in a candidate gene by sequencing: 1. Amplification by the polymerase chain reaction (PCR) of 400-700 bp regions of the candidate gene from a panel of DNA samples The DNA samples can either be cDNA or genomic DNA and will represent some cross section of the world population. 2. Sequencing of the resulting PCR fragments using the Sanger dideoxy method. Sequencing reactions are performed using flourescently labeled dideoxy terminators and fragments are separated by electrophoresis on an ABI 377 sequencer or its equivalent. 3. Analysis of the resulting data from the ABI 377 sequencer using software programs designed to identify sequence variations between the different samples analyzed. A more detailed description of the procedure is as follows: A candidate gene sequence is downloaded from an appropriate database. Primers for PCR amplification are designed which will result in the target sequence being divided into amplification products of between 400 and 700 bp. There will be a minimum of a 50 bp of overlap not including the primer sequences between the 5' and 3' ends of adjacent fragments to ensure the detection of variances which are located close to one of the primers. Optimal PCR conditions for each of the primer pairs is determined experimentally. Parameters including but not limited to annealing temperature, pH, MgCl 2 concentration, and KCl concentration will be varied until conditions for optimal PCR amplification are established. The PCR conditions derived for each primer pair is then used to amplify a panel of DNA samples (cDNA or genomic DNA) which is chosen to best represent the various ethnic backgrounds of the world population or some designated subset of that population. PCR reactions are purified using the QIAquick 8 PCR purification kit (Qiagen cat# 28142) to remove nucleotides, proteins and buffers. The PCR reactions are mixed with 5 volumes of Buffer PB and applied to the wells of the QIAquick strips. The liquid is pulled through the strips by applying a vacuum. The wells are then washed two times with 1 ml of buffer PE and allowed to dry for 5 minutes under vacuum. The PCR products are eluted from the strips using 60 ul of elution buffer. The purified PCR fragments are sequenced in both directions using the Perkin Elmer ABI Prism r ' Big Dye terminator Cycle Sequencing Ready Reaction Kit (Cat# 4303150). The following sequencing reaction is set up: 8.0 ul Terminator Ready Reaction Mix, 6.0 ul of purified PCR fragment, 20 picomoles of primer, deionized water to 20 ul. The reactions are mn through the following cycles 25 times: 96°C for 10 second, annealing temperature for that particular PCR product for 5 seconds, 60°C for 4 minutes. The above sequencing reactions are ethanol precipitated directly in the PCR plate, washed with 70% ethanol, and brought up in a volume of 6 ul of formamide dye. The reactions are heated to 90°C for 2 minutes and then quickly cooled to 4°C 1 ul of each sequencing reaction is then loaded and ran on an ABI 377 sequencer. The output for the ABI sequencer appears as a series of peaks where each of the different nucleotides. A, C, G, and T appear as a different color. The nucleotide at each position in the sequence is determined by the most prominent peak at each location. Comparison of each of the sequencing outputs for each sample can be examined using software programs to determine the presence of a variance in the sequence. One example of heterozygote detection using sequencing with dye labeled terminators is described by Kwok et. al (Kwok, P.-Y.; Carlson, C; Yager, T.D., Ankener, W.,and D. A. Nickerson, Genomics 23, 138-144, 1994). The software compares each of the normalized peaks between all the samples base by base and looks for a 40%> decrease in peak height and the concomitant appearance of a new peak underneath. Possible variances flagged by the software are further analyzed visually to confirm their validity. Example 5 Hardy- Weinberg equilibrium Evolution is the process of change and diversification of organisms through time, and evolutionary change affects moφhology, physiology and reproduction of organisms, including humans. These evolutionary changes are the result of changes in the underlying genetic or hereditary material. Evolutionary changes in a group of interbreeding individuals or Mendelian population, or simply populations, are described in terms of changes in the frequency of genotypes and their constituent alleles. Genotype frequencies for any given generation is the result of the mating among members (genotypes) of their previous generation. Thus, the expected proportion of genotypes from a random union of individuals in a given population is essential for describing the total genetic variation for a population of any species. For example, the expected number of genotypes that could form from the random union of two alleles, A and a, of a gene are AA, Aa and aa. The expected frequency of genotypes in a large, random mating population was discovered to remain constant from generation to generation; or achieve Hardy- Weinberg equilibrium, named after its discoverers. The expected genotypic frequencies of alleles A and a (AA, 2Aa, aa) are conventionally described in terms of p 2 + 2pq + q 2 in which p and q are the allele frequencies of A and a. In this equation (p 2 + 2pq + q 2 = 1 ), p is defined as the frequency of one allele and q as the frequency of another allele for a trait controlled by a pair of alleles (A and a). In other words, p equals all of the alleles in individuals who are homozygous dominant (AA) and half of the alleles in individuals who are heterozygous (Aa) for this trait. In mathematical terms, this is p = AA + '/ 2 Aa Likewise, q equals the other half of the alleles for the trait in the population, or q = aa + 1 Aa Because there are only two alleles in this case, the frequency of one plus the frequency of the other must equal 100%, which is to say p + q = l Alternatively, p = 1 - q OR q = 1 - p All possible combinations of two alleles can be expressed as: (p + q) 2 = ι or more simply, p 2 + 2pq + q 2 = 1 In this equation, if p is assumed to be dominant, then p 2 is the frequency of homozygous dominant (AA) individuals in a population, 2pq is the frequency of heterozygous (Aa) individuals, and q 2 is the frequency of homozygous recessive (aa) individuals. From observations of phenotypes, it is usually only possible to know the frequency of homozygous dominant or recessive individuals, because both dominant and recessives will express the distinguishable traits. However, the Hardy- Weinberg equation allows us to determine the expected frequencies of all the genotypes, if only p or q is known. Knowing p and q, it is a simple matter to plug these values into the Hardy- Weinberg equation (p 2 + 2pq + q 2 = 1). This then provides the frequencies of all three genotypes for the selected trait within the population. This illustration shows Hardy- Weinberg frequency distributions for the genotypes AA, Aa, and aa at all values for frequencies of the alleles, p and q. It should be noted that the proportion of heterozygotes increases as the values of p and q approach 0.5. Linkage disequilibirum Linkage is the tendency of genes or DNA sequences (e.g. SNPs) to be inherited together as a consequence of their physical proximity on a single chromosome. The closer together the markers are, the lower the probability that they will be separated during DNA crossing over, and hence the greater the probability that they will be inherited together. Suppose a mutational event introduces a "new" allele in the close proximity of a gene or an allele. The new allele will tend to be inherited together with the alleles present on the "ancestral," chromosome or haplotype. However, the resulting association, called linkage disequilibrium, will decline over time due to recombination. Linkage disequilibrium has been used to map disease genes. In general, both allele and haplotype frequencies differ among populations. Linkage disequilibrium is varied among the populations, being absent in some and highly significant in others. Quantification of the relative risk of observable outcomes of a Pharmacogenetics Trial Let PlaR be the placebo response rate (0% ( PlaR ( 100%) and TntR be the treatment response rate (0% ( TntR ( 100%>) of a classical clinical trial. ObsRR is defined as the relative risk between TntR and PlaR: ObsRR = TntR / PlaR. Suppose that in the treatment group there is a polymoφhism in relation to drag metabolism such as the treatment response rate is different for each genotypic subgroup of patients. Let q be the allele a frequency of a recessive biallelic locus (e.g. SNP) and p = 1 - q the allele A frequency. Following Hardy- Weinberg equilibrium, the relative frequency of homozygous and heterozygous patients are as follow: AA: p2 Aa: 2pq aa: q2 with (p2+2pq+q2) = l . Let's define AAR, AaR, aaR as respectively the response rates of the AA, Aa and aa patients. We have the following relationship: TntR = AAR*p2 + AaR*2pq + aaR*q2. Suppose that the aa genotypic group of patients has the lowest response rate, i.e. a response rate equal to the placebo response rate (which means that the polymoφhism has no impact on natural disease evolution but only on drag action) and let's define ExpRR as the relative risk between AAR and aaR, as ExpRR = AAR / aaR. From the previous equations, we have the following relationships: ObsRR ( ExpRR ( 1 /PlaR TntR / PlaR = (AAR*p2 + AaR*2pq + aaR*q2) / PlaR The maximum of the expected relative risk, max (ExpRR), conesponding to the case of heterozygous patients having the same response rate as the placebo rate, is such that: ObsRR = ExpRR*p2 + 2pq + q2 <=> ExpRR = (ObsRR - 2pq -q2) / p2 The minimum of the expected relative risk, min(ExpRR), conesponding to the case of heterozygous patients having the same response rate as the homozygous non- affected patients, is such that: ObsRR = ExpRR*(p2 + 2pq) +q2 t=> ExpRR = (ObsRR -q2) / (p2 + 2pq) For example, if q = 0.4, PlaR = 40% and ObsRR = 1.5 (i.e. TntR = 60%), then 1.6 ( ExpRR ( 2.4. This means that the best treatment response rate we can expect in a genotypic subgroup of patients in these conditions would be 95.6% instead of 60%. This can also be expressed in terms of maximum potential gain between the observed difference in response rates (TntR - PlaR) without any pharmacogenetic hypothesis and the maximum expected difference in response rates (max(ExpRR)*PlaR - TntR) with a strong pharmacogenetic hypothesis: (max(ExpRR)*PlaR - TntR) = [(ObsRR - 2pq -q2) / p2] * PlaR - TntR (max(ExpRR)*PlaR - TntR) = [TntR - PlaR*(2pq + q2) -TntR*p2]/p2 (max(ExpRR)*PlaR - TntR) = [TntR*( 1 - p2)- PlaR*(2pq + q2)]/p2 = (max(ExpRR)*PlaR - TntR) = [( 1 - p2) / p2] * (TntR - PlaR) that is for the previous example, (95.6% - 60%) = [(1 - 0.62V0.62]* (60% -40%) = 35.6% Suppose that, instead of one SNP, we have p loci of SNPs for one gene. This means that we have 2p possible haplotypes for this gene and (2p)(2p-l )/2 possible genotypes. And with 2 genes with pi and p2 SNP loci, we have [(2p l )(2pl- l )/2]*[(2p2)(2p2-l)/2] possibilities; and so on. Examining haplotypes instead of combinations of SNPs is especially useful when there is linkage disequilibrium enough to reduce the number of combinations to test, but not complete since in this latest case one SNP would be sufficient. Yet the problem of frequency above still remains with haplotypes instead of SNPs since the frequency of a haplotype cannot be higher than the highest SNP frequency involved. Statistical Methods to be used in Objective Analyses The statistical significance of the differences between variance frequencies can be assessed by a Pearson chi-squared test of homogeneity of proportions with n- 1 degrees of freedom. Then, in order to determine which variance(s) is(are) responsible for an eventual significance, we can consider each variance individually against the rest, up to n comparisons, each based on a 2x2 table. This should result in chi -squared tests that are individually valid, but taking the most significant of these tests is a form of multiple testing. A Bonfenoni's adjustment for multiple testing will thus be made to the P-values, such as p*=l-(l-p) n . The statistical significance of the difference between genotype frequencies associated to every variance can be assessed by a Pearson chi-squared test of homogeneity of proportions with 2 degrees of freedom, using the same Bonfenoni's adjustment as above. Testing for unequal haplotype frequencies between cases and controls can be considered in the same framework as testing for unequal variance frequencies since a single variance can be considered as a haplotype of a single locus. The relevant likelihood ratio test compares a model where two seqarate sets of haplotype frequencies apply to the cases and controls, to one where the entire sample is characterized by a single common set of haplotype frequencies. This can be performed by repeated use of a computer program (Terwilliger and Ott, 1994, Handbook of Human Linkage Analysis, Baltimore, John Hopkins University Press) to successively obtain the log-likelihood conesponding to the set of haplotpe frequency estimates on the cases (XnL case ), on the controls (XnLco r ot), and on the overall (XnL combi „ e( t). The test statistic 2((lnZ, cnie )+ (ln--.co-.--ro/)- Qn combmed)) is then chi-squared with r-1 degrees of freedom (where r is the number of haplotypes). To test for potentially confounding effects or effect-modifiers, such as sex, age, etc., logistic regression can be used with case-control status as the outcome variable, and genotypes and covariates (plus possible interactions) as predictor variables. Example 6 Exemplary Pharmacogenetic Analysis Steps In accordance with the discussion of distribution frequencies for variances, alleles, and haplotypes, variance detection, and conelation of variances or haplotypes with treatment response variability, the points below list major items which will typically be performed in an analysis of the pharmacogenetic determination of the effects of variances in the treatment of a disease and the selection/optimization of treatment. 1) List candidate gene/genes for a known genetic disease, and assign them to the respective metabolic pathways. 2) Determine their alleles, observed and expected frequencies, and their relative distributions among various ethnic groups, gender, both in the control and in the study (case) groups. 3) Measure the relevant clinical/phenotypic (biochemical / physiological) variables of the disease. 4) If the causal variance/allele in the candidate gene is unknown, then determine linkage disequilibria among variances of the candidate gene(s). 5) Divide the regions of the candidate genes into regions of high linkage disequilibrium and low disequilibrium. 6) Develop haplotypes among variances that show strong linkage disequilibrium using the computation methods. 7) Determine the presence of rare haplotypes experimentally. Confirm if the computationally determined rare haplotypes agree with the experimentally determined haplotypes. 8) If there is a disagreement between the experimentally determined haplotypes and the computationally derived haplotypes, drop the computationally derived rare haplotypes, construct cladograms from these haplotypes using the Templeton (1987) algorithm. 9) Note regions of high recombination. Divide regions of high recombination further to see patterns of linkage disequilibria. 10) Establish association between cladograms and clinical variables using the nested analysis of variance as presented by Templeton (1995), and assign causal variance to a specific haplotype. 11) For variances in the regions of high recombination, use permutation tests for establishing associations between variances and the phenotypic variables. 12) If two or more genes are found to affect a clinical variable determine the relative contribution of each of the genes or variances in relation to the clinical variable, using step-wise regression or discriminant function or principal component analysis. 13) Determine the relative magnitudes of the effects of any of the two variances on the clinical variable due to their genetic (additive, dominant or epistasis) interaction. 14) Using the frequency of an allele or haplotypes, as well as biochemical/clinical variables determined in the in vitro or in vivo studies, determine the effect of that gene or allele on the expression of the clinical variable, according to the measured genotype approach of Boerwinkle et al (Ann. Hum. Genet 1986). 15) Stratify ethnic/ clinical populations based on the presence or absence of a given allele or a haplotype. 16) Optimize drag dosages based on the frequency of alleles and haplotypes as well as their effects using the measured genotype approach as a guide. Example 7 Exemplary Pharmacogenetic Analysis Steps - biological function analysis In many cases when a gene which may affect drag action is found to exhibit variances in the gene, RNA, or protein sequence, it is preferable to perform biological experiments to determine the biological impact of the variances on the stracture and function of the gene or its expressed product and on drag action. Such experiments may be performed in vitro or in vivo using methods known in the art. The points below list major items which may typically be performed in an analysis of the effects of variances in the treatment of a disease and the selection/optimization of treatment using biological studies to determine the stracture and function of variant forms of a gene or its expressed product.. 1) List candidate gene/genes for a known genetic disease, and assign them to the respective metabolic pathways. 2) Identify variances in the gene sequence, the expressed mRNA sequence or expressed protein sequence. 3) Match the position of variances to regions of the gene, mRNA, or protein with known biological functions. For example, specific sequences in the promotor of a gene are known to be responsible for determining the level of expression of the gene; specific sequences in the mRNA are known to be involved in the processing of nuclear mRNA into cytoplasmic mRNA including splicing and polyadenylation; and certain sequences in proteins are known to direct the trafficking of proteins to specific locations within a cell and to constitute active sites of biological functions including the binding of proteins to other biological consituents or catalytic functions. Variances in sites such as these, and others known in the art, are candidates for biological effects on drag action. 4) Model the effect of the variance on mRNA or protein stracture. Computational methods for predicting the stracture of mRNA are known and can be used to assess whether a specific variance is likely to cause a substantial change in the stracture of mRNA. Computational methods can also be used to predict the stracture of peptide sequences enabling predictions to be made concerning the potential impact of the variance on protein function. Most useful are structures of proteins determined by X-ray diffraction, NMR or other methods known in the art which provide the atomic stracture of the protein. Computational methods can be used to consider the effect of changing an amino acid within such a stmcture to determine whether such a change would dismpt the stracture and/or funciton of the protein. Those skilled in the art will recognize that this analysis can be performed on crystal structures of the protein known to have a variance as well as homologous proteins expressed from different loci in the human genome, or homologous proteins from other species, or non-homologous but analogous proteins with similar functions from humans or other species. 5) Produce the gene, mRNA or protein in amounts sufficient to experimentally characterize the structure and function of the gene, mRNA or protein. It will be apparent to those skilled in the art that by comparing the activity of two genes or their products which differ by a single variance, the effect of the variance can be determined. Methods for producing genes or gene products which differ by one or more bases for the puφose of experimental analysis are known in the art. 6) Experimental methods known in the art can be used to determine whether a specific variance alters the transcription of a gene and translation into a gene product. This involves producing amounts of the gene by molecular cloning sufficient for in vitro or in vivo studies. Methods for producing genes and gene products are known in the art and include cloning of segments of genetic material in prokaryotes or eukarotic hosts, ran off transcription and cell-free translation assays that can be performed in cell free extracts, transfection of DNA into cultured cells, introduction of genes into live animals or embryos by direct injection or using vehicles for gene delivery including transfection mixtures or viral vectors. 7) Experimental methods known in the art can be used to determine whether a specific variance alters the ability of a gene to be transcribed into RNA. For example, run off transcription assays can be performed in vitro or expression can be characterized in transfected cells or transgenic animals. 8) Experimental methods known in the art can be used to determine whether a specific variance alters the processing, stability, or translation of RNA into protein. For example, reticulocyte lysate assays can be used to study the production of protein in cell free systems, transfection assays can be designed to study the production of protein in cultured cells, and the production of gene products can be measured in transgenic animals. 9) Experimental methods known in the art can be used to determine whether a specific variant alters the activity of an expressed protein product. For example, protein can be producted by reticulocyte lystae systems or by introducing the gene into prokaryotic organisms such as bacteria or lowre eukaryotic organisms such as yeast or fungus), or by introducing the gene into cultured cells or transgenic animals. Protein produced in such systems can be extracted or purified and subjected to bioassays known to those in the art as measures of the notion of that particular protein. Bioassays may involve, but are not limited to, binding, inhibiton, or catalytic functions. 10) Those skilled m the art will recognize that it is sometimes prefened to perform the above expenments in the presence of a specific drug to determine whether the drag has differential effects on the activity being measured Alternatively, studies may be performed in the presence of an analogue or metabolite of the drag 11) Using methods descnbed above, specific vanances which alter the biological function of a gene or its gene product that could have an impact on drag action can be identified Such vaπances are then studied in clinical tnal populations to determine whether the presence or absence of a specific vanance conelates with observed clinical outcomes such as efficacy or toxicity. 12) It will be further recognized that there may be more than one vanance within a gene that is capable of altenng the biological function of the gene or gene product. These vanances may exhibit similar, synergistic effects, or may have opposite effects on gene function In such cases, it is necessary to consider the haplotype of the gene, namely the combination of vanances that are present within a single allele, to assess the composite function of the gene or gene product. 13) Perform clinical tnals with stratification of patients based on presence or absence of a given vanance, allele or haplotype of a gene Establish associations between observed drag responses such as toxicity, efficacy, drag response, or dose toleration and the presence or absense of a specific vanance, allele, or haplotype 14) Optimize drag dosage or drag usage based on the presence of the vanant Example 8 Stratification of patients by genotype in prospective clinical tπals In a prospective clinical tnal, patients will be stratified by genotype to determine whether the observed outcomes are different in patients having different genotypes A cntical issue is the design of such tπals to assure that a sufficient number of patients are studied to observe genetic effects The number of patients required to achieve statistical significance in a conventional clinical tnal is calculated from 1 1 N=2(z α +z 2β ) 2 / (δ/σ) 2 (two tailed test) From this equation it may be mfened that the size of a genetically defined subgroup N, required to achieve statistical significance for an observed outcome associated with vanance or haplotype "I" can be calculated as: 1.2 N,=2(z α +z 2β ) 2 / (δ,/σ,) 2 If P, is the prevalence of the genotype "ι"ιn the population, the total number of patients that need to be incoφorated in a clinical trial N g to identify a population with haplotype "i" of size N, is given by- 1 3 N„=N, P, It should be noted that N g descnbes the total number of patients that need to be genotyped in order to identify a subset of N, patients with genotype "i". If genotyping is used as means for statistical stratification of patients, N g represents the number of patients that would need to be enrolled in a trial to achieve statistical significance for subgroup "i". If genotyping is used as a means for inclusion, it represents the number of patients that need to screened to identify a population of N, individuals for an appropnately powered clinical tnal. Thus, N g is a cntical determinant of the scope of the clinical trial as well as N,. A clinical tnal can also be designed to test associations for multiple genetic subgroups "j" defined by a single allele in which case: 1.4 N g = max ( N g , ) for ι=l ...j If more than one subgroup is tested, but there is no overlap m the patients contained within the subgroups, these can be considered to be independent hypotheses and no multiple testing conection should be required. If consideration of more than one subgroup constitutes multiple testing, or if individual patients are included in multiple subgroups, then statistical conections may required in the values of z α or z 2β which would increase the number of patients required. It should be emphasized that a clinical tnal of this nature may not provide statistically significant data concerning associations with any genotype other than "1". The total number of patients that would be required in a clinical tnal to test more than one genetically defined subgroup would be determined by the maximum value of N g for any single subgroup. The power of pharmacogenomics to improve the efficiency of clinical trials arises from the fact it is possible to have N g <N. The goal of pharmacogenomic analysis is to identify a genetically define subgroup in which the magnitude of the clinical response is greater and the variability in response is reduced. These observations conespond to an increase in the magnitude of the (mean) observed response δ or a decrease the degree of variability σ. Since the value of N, calculated in equation 1.2 decreases non-linearly as the square of these changes, the total number of patients N g can also decrease non-linearly, resulting in a clinical trial that requires fewer patients to achieve statistical significance. If δ,and σ, are not different than δ and σ, then N g is greater than N as given by N g =N , /P,. Values of δ,and σ, that give N g <N can be calculated: 1.5 N g <N if: P,> [(δ/σ) 2 ]/[(δ,/σ,) ] It is apparent from this analysis that N g is not uniformly less than N, even with modest improvements in the values for δ,and σ,. As with a conventional clinical trial, the incoφoration of an appropriate control group in the study design is critical for achieving success. In the case of a prospective clinical trial, the control group commonly is selected on the basis of the same inclusion criteria as the treatment group, but is treated with placebo or a standard therapeutic regimen rather than the investigational drag. In the case of a study with subgroups that are defined by haplotype, the ideal control group for a treatment subgroup with hapotype "i" is a placebo-treated subgroup with haplotype "i". This is often a critical control, since haplotypes which may be associated with the response to treatment may also affect the natural course of the disease. A critical issue in considering control groups is that σ for the control group placebo treated population with haplotype "i" may not be equivalent to that of the control population. If so, 1.5 may overestimate the benefits of any reduction in σ, in the treatment response group if there is not also a reduction in σ, in the control group. If σ of the treatment and control groups are not equivalent, δ would be still calculated as the difference in the response of the two groups, but σ would be different in the two groups with values of σ 0 or σi respectively. In this case, the number of patients in the genetically defined subgroup N, would be defined by: The total number of patients that would need to be enrolled in such a trial would be the maximium of 2.2 N or N/Pi It will be apparent that such an analysis remains sensitive to increases in δ, but is less sensitive to changes in σ which are not also reflected in the control group. Certain analysis may be performed by comparing individuals with one haplotype against the entire normal population. Such an analysis may be used to establish the selectivity of the response associated with a specific haplotype. For example, it may be desirable to establish that the response or toxicity observed in a specific subgroup is greater than that associated observed with the entire population. It may also be of interest to compare the response to treatment between two different subgroups. If σ differs between the groups, then the estimate of the number of patients that need to be enrolled in the trial must be calculated using equations 2.1 with N being the maximum of N P, for the different subgroups. Another issue in controls is the relative size of the treatment and control groups. In a prospectively designed clinical trial which selectively incoφorates patients with haplotype "i"the number of patients in the control and treatment group will be essentially equivalent. If the control group is different, or if haplotypes are used for stratification but not inclusion, statistical conections may need to be made for having populations of different size. Example 9 Stratification of patients by phenotype. The identification of genetic associations in Phase II or retrospective studies can be performed by stratifying patients by phenotype and analyzing the distribution of genotypes/haplotypes in the separate populations. A particularly important aspect of this analysis is that any gene may have only a partial effect on the observed outcome, meaning that there will be an association value (A) conesponding to the fraction of patients in a phenotypically-defined subgroup who exhibit that phenotype due to a specific genotype/phenotype. It will be recognized to those skilled in the art that the fraction of individuals who exhibit a phenotype due to any specific allele will be less than 1 (i.e. A<1). This is trae for several reasons. The observed phenotype may occur by random chance. The observed phenotype may be associated with environmental influences, or the observed phenotype may be due to different genetic effects in differen tindividuals.Furthermore, the onstraction of haplotypes and analysis of recombination may not group all alleles with pheontypically-significant variances within a single haplotype or haplotype cluster. In this case, causative variances at a single locus may be associated with more than one haplotype or haplotype cluster and the association constant A for the locus would be A=Aι+A 2 +...+A n <l . It is likely that many phenotypes will be associated with multiple alleles at a given locus, and it is particularly important that statistical methods be sufficiently robust to identify association with a locus even if A; is reduced by the presence of several causative alleles. Statistical methods can be used to identify genetic effects on an observed outcome in patient groups stratified by phenotype, eg the presence or absence of the observed response. One such method entails determining the allele frequencies in two populations of patients stratified by an observed clinical outcome, for example efficacy or toxicity and performing a maximum likelihood analysis for the association between a given gene and the observed phenotype based on the allele frequencies and a range of values for A (the association constant between a specific allele and the observed outcome used to stratify patients). This analysis is performed by comparing the observed gene frequencies in a patient population with an observed outcome to gene frequencies in a table in which the predicted frequencies of different alleles of the gene assuming different values of the association constant A for that allele. This table of predicted gene frequencies can be constructed by those skilled in the art based on the frequency of any specific allele in the normal population, the predicted inheritance of the effect (e.g. dominant or recessive) and the fraction of a subgroup with a specific outcome who would have that allele based on the association constant A. For example, if a specific outcome was only observed in the presence of a specific allele of a gene, the expected frequency would be 1. If a specific outcome was never observed in the presence of a specific allele of a gene, the expected fequency would be 0. If there was no association between the allele and the observed outcome, the frequency of that allele among individuals with an observed outcome would be the same as in the general population. A statistical analysis can be performed to compare the observed allele frequencies with the predicted allele frequencies and determine the best fit or maximum likeihood of the association. For example, a chi square analysis will determine whether the observed outcome is statistically similar to predicted outcomes calculated for different modes of inheritance and different potential values of A. P values can then be calculated to determine the likelihood that any specific association is statistically significant. A curve can be calculated based on different values of A, and the maximal likelihood of an association determined from the peak of such a curve. Methods for chi square analysis are known to those in the art. A multidimensional analysis can also be performed to determine whether an observed outcome is associated with more than one allele at a specific genetic locus. An example of this analysis considering the potential effects of two different alleles of a single gene is shown. It will be apparent to those skilled in the art that this analysis can be extended to n dimensions using computer programs. This analysis can be used to determine the maximum likelihood that one or more alleles at a given locus are associated with a specific clinical outcome. It will be apparent to those skilled in the art that critical issues in this analysis include the fidelity of the phenotypic association and identification of a control group. In particular, it may be useful to perform an identical analysis in patients receiving a placebo to eliminate other forms of bias which may contribute to statistical enors. Example 10 Amyotrophic Lateral Sclerosis I. Description of Amyotrophic Lateral Sclerosis Amyotrophic Lateral Sclerosis (ALS) is a degenerative neurological disease that primarily involves the motor neuron system. The disease is characterized by muscular atrophy, progressive weakness, fasciculations, spasticity, disarthria, dysphagia, and repiratory compromise. Sensory, cognitive, oculomotor, and autonomic functions are spared. There are approximately 30,000 individuals with ALS in the U.S. with an estimated annual cost of $300 million dollars. The majority of cases are sporadic and of unknown etiology, however approximately 5%-10% of ALS cases are inherited as an autosomal dominant trait (familial ALS). Superoxide dismutase 1 (SOD 1 ) gene mutations are responsible for about 20% of familial ALS cases. II. Current therapies for ALS There are no compounds that halt or prevent the progressive neurodegeneration of ALS. Riluzole (RILUTEK ® ) , a benzothiazole derivative, is approved for treatment of ALS based on data that it slows disease progression and modestly increases survival time and ventilator-free time.. Riluzole's mechanism of action is not completely understood, however pharmacological properties include: 1 ) an inhibitory effect on glutamate release, 2) inactivation of voltage dependent sodium channels, 3) downmodulation of signalling via excitatory amino acid receptors, particularly glutamate receptors. Unfortunately riluzole, which was introduced in 1996, produces a benefit in only a fraction of patients, and the effect is modest. For example, despite the increase in longevity there is no consistent increase in muscular strenght or pulmonary function. Thus patients do not experience significant relief from symptoms. Patients and care givers quickly understood these limitations, and consequently the use of the drag has been limited. A 1997 study, conducted during the first 8 months after commercialization of riluzole, found that only 37%> of patients (17 of 46) eligible for riluzole were interested in trying the drag. The most common reason given for not wanting to try riluzole was insufficient benefit. III. Limitations of Current Therapies for ALS As noted above, despite therapy with riluzole, in most ALS patients the disease progresses to debilitating and ultimately life-threatening symptoms. However, since there are no therapeutic alternatives, riluzole is frequently administered despite the modest efficacy. This practice increases the cost of ALS care significantly. In addition to unimpressive efficacy, riluzole therapy has been associated with elevation of serum ALT levels. Thus patients on riluzole should be monitored bimonthly for elevated liver enzymes, at significant cost. Other side effects, which occur infrequently, include neutropenia, asthenia, nausea, dizziness, decreased lung function, dianhea, abdominal pain, pneumonia, vomiting, vertigo, paresthesia, anorexia, and somnolence. Attending to these iatrogenic effects further increases the costs associated with rizulin therapy. IN. Potential Impact of Genotyping on Drug Development for ALS There is already a well established genetic cause of some familial ALS cases: mutation of the SOD-1 gene. It is likely that genetic factors play a role in the pathogenesis of sporadic ALS and non-SODl linked familial ALS. Strong candidate genes include, for example, other scavengers of superoxide, the entire glutamate signal transduction pathway, calcium channels and genes involved in the production and degradation of neurofilaments. Stratification of clinical trial patients by allelic variation in these or other candidate genes may reveal differences in response rate, duration or quality of response, or adverse events that would be useful in the development of a compound. Provided in this invention are additional genetic pathways implicated in the disease process or response to candidate therapies. Variation in these genes may account for the observed variability in treatment response. Exemplary variations in the candidate genes are provided in Tables 12-17 and 18-23. The Detailed Description above describes how one skilled in the art would identify a candidate gene or genes, identify sequence variances, stratify patients, design clinical trials, and obtain regulatory approval of a pharmacogenetic test for optimal responders to an ALS treatment.Gene pathways including most preferably, but not limited to, those genes that are listed in the gene pathway Table 2, and pathway matrix Table 7 and discussed in Section V. below are candidates for the genetic analysis and product development strategies described above. Advantages of Pharmacogenetic Clinical Development of Agents for ALS In view of the limitations of present therapy, the advantages of an ALS clinical development program that includes genetic stratification of patients in the analysis of response to candidate therapeutic interventions are numerous. First, it may be possible to identify a subpopulation that responds to a treatment at a higher rate than the whole ALS population. This would address the demonstrated disinclination of ALS patients to expose themselves to therapies of limited effectiveness. It might also allow regulatory approval of therapies that do not produce a sufficient response in the unstratified population to justify approval. Second, it may be possible to identify patients who respond to a treatment only at higher doses than most patients require, or respond preferentially to an altered dosing route or schedule. Such customization of therapy to individual genetic and biochemical differences may allow a higher overall response rate to be achieved, without requiring totally empirical dose adjustment in each patient. Third, it may be possible to identify patients in whom side effects are likely to occur. Such patients could be offered alternative treatments. It is also worth noting that the type of benefit afforded by drags such as RILUTEK ® - a slowing of deterioration - will likely be most useful if the drug is started very early, before large numbers of neurons are gone. However the long term prophylactic use of medicines in well, or nearly well, individuals entails a different cost-benefit analysis than in already sick individuals. Identification of patients that respond well to early neuroprotective therapy may be aided by the analysis of genetic determinants of treatment response. Additional uses of genetic stratification in clinical development have been described above. As an example of a candidate gene with DNA sequence variances potentially relevant to drag efficacy, safety, or both consider the glutamate aspartate receptor NMDA 2C, a member of the glutamate pathway. Described in this application are novel NMDA 2C DNA sequence variances that the inventors have recognized may affect response to drugs. (Diseases in which the glutamate pathway is likely to play a role are summarized in Table 7) Six DNA sequence variances have been identified in the NMDA 2C gene, five of which alter the encoded amino acid sequence. Several of the amino acid variances are nonconservative, including phenylalanine-valine, glycine-arginine and arginine-serine (see Table 13 for details). Seven DNA sequence variances are described in the NMDA 2A receptor (Table 13). The effect of one or more of these genetic polymoφhisms on efficacy or safety of an ALS treatment could be tested in a clinical trial. For example, the goal could be optimization of patient selection for glutamate channel antagonist therapy of ALS by determining whether an ALS patient has a NMDA 2A or 2C receptor genotype against which a glutamate antagonist is more effective or safer. Similarly, for genes belonging to the other pathways relevant to treatment of ALS (see tables 2 and 7) and polymoφhisms in those genes (tables 13 and 19) a strong argument can be made that said polymoφhisms (or sets of polymoφhisms, or haplotypes) may affect efficacy or safety of drags active against ALS, including, but not limited to, drugs listed below in Table 25 and related compounds. The candidate genes include, but are not limited to, modulators of glutaminergic, serotonergic, GABAergic, melatonergic and opiate pathways, as well as calcium channels, cytokines, factors that mediate growth, differentiation and apoptosis, the coagulation cascade, second messenger systems, detoxification genes, particularly relating to superoxide, protein degradation and cytoskeleton genes. V. Therapeutic Strategies for ALS The etiology of most ALS cases is unknown but may involve autoimmune responses, for example to calcium channels, injury due to excessive excitotoxic stimulation (especially via aspartate, glutamate and GABA receptors), impaired clearance of free radicals, imbalance of neurofilament turnover or possiblly viral mediated destruction of motor neurons (e.g. heφes vims). A number of drug development programs are aimed at these postulated pathophysiologic mechanisms. For example, there are candidate therapeutic agents that down modulate immune reactivity, block or dampen excitatory neurotransmitter signalling, alleviate free radical injury, and interfere with a hypothesized viral infection of motor neurons. Beyond the specific mechanisms of action enumerated above, there are many compounds in development that are intended to halt, retard, or prevent neural cell degeneration, or promote neural cell regeneration. Many such compounds are in clinical development programs for multiple neurological diseases. For example, gabapentin is a compound with complex and incompletely understood pharmacology, but its shows anticonvulsant, antinociceptive, anxiolytic and neuroprotective activity in animal models. In ALS animal models gabapentin prevents neuronal death. One of its actions may be inhibition of glutamate synthesis by branched-chain amino acid aminotransferase (BCAA-t). Other compounds in development for ALS target proteins involved in growth control and differentiation, protein processing, intracellular second messenger cascades and cytoskeletal proteins (see 25 below for specific compounds and Table 1 for the candidate genes that may affect response to those compounds). Below in Table 25 the therapies in development for ALS catagorized by mechanism of action. The listed candidate therapeutic intervention response in patients with ALS may be affected by polymoφhisms in genes as described above in the Detailed Description. Example 11 Dementia I. Description of Dementia Dementia is a general term for mental deterioration, clinical state characterized by a significant loss of function in multiple cognitive domains, not due to an impaired level of confusion. Diagnosis of dementia requires 1) assessment of an individual's cunent level of cognitive function with the ability to compare to past intellectual function, and 2) documenting a decline in intellectual function by serial examinations over time. A comprehensive, reliable, and universally accepted clinical classification of the clinical and neuropathological characteristics of senile dementia has been described. However, definitive diagnosis is obtainable only with pathological findings upon autopsy. Based upon these diagnoses, there are an estimated 4 million Americans with Alzheimer's disease (AD) and 10 million Americans with dementia of all types. Besides AD, there are categories of dementia that include vascular dementia, lewy body disease, frontal lobe dementia, mixed dementia, and post-traumatic dementia. A number of different diseases or conditions are characterized by or involve loss of cholinergic function and/or defects in neuronal remodeling repair and may result in clinical symptoms of dementia. Among these are diseases such as Alzheimer's disease (AD), Huntington's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). Dementia can further be a complication of the following: depression, drag intoxication, metabolic disorders, normal pressure hydrocephalus, subdural hematomas, and cerebrovascular insufficiency. II. Current Therapies for Dementia Cunent therapies for the treatment of dementia include enhancement of cortical cholinergic function. In general, approaches to replacement of cholinergic function can be characterized as either: 1 ) therapies that compensate for existing damage; and 2) therapies that halt, retard, or prevent cerebral damage. Ideally, a therapy targeting both mechanisms could potentially reverse existing damage. There are two broad mechanisms to enhance cerebral cholinergic function; 1 ) to block metabolism of acetylcholine via an acetylcholinesterase inhibitor, or 2) agonists at muscarinic or nicotinic receptors. Acetylcholinesterase inhibitors have recently been approved for the use in patients with mild to moderate Alzheimer's disease. These agents (donepezil, Tacrine) selectively inhibit the acetylcholinesterase enzyme and increases levels of cortical acetylcholine. In randomized controlled clinical trials, donepezil was shown to improve both cognitive performance and global functioning. The improvements are modest and may not be apparent until up to three months after commencement of treatment. III. Limitations of Current Therapies for Dementia Despite the introduction of pharmacologic agents for the treatment of dementia, the mainstay of therapeutic management continues to be education, and support for caregivers, and treatment of complications. This is in part because the available acetylcholinesterase inhibitor (donepezil) has limited efficacy and has undesirable side effects. Thus, the clinician is faced with the dilemma of limited therapeutic alternatives and weighing the benefits against the side effects. Limitations of Acetylcholinesterase Therapy due to Low Efficacy Acetylcholinesterase inhibitors have limited efficacy; only a fraction (modest improvement in 40-50%>) of patients respond to therapy. The extent and progression of loss of cortical cholinergic neurons limit the therapeutic benefit of acetylcholinesterase inhibitors. Long-term benefit of inhibition of acetylcholinesterase activity is unproven. Further, there is no clinical evidence supporting the use of acetylcholinesterase inhibitors in the prevention of AD or in the treatment of more severe stages. An additional efficacy concern of the acetylcholinesterase inhibitor is the latent period before demonstrable clinical benefit. In the same period there may be concunent neurodegeneration. Thus, the clinician has limited therapeutic alternatives, the patient may have limited response to therapy, and the disease progresses. In many cases, medical management of dementia is reduced to treatment of complications or supportive care. Limitation of Acetylcholinesterase Therapy due to Toxicity or Undesired Side Effects Toxicities associated with the use of acetylcholinesterase inhibitors are 1) vagotonic effect on the myocardium resulting in bradycardia and complicationsof other myocardial syndormes, 2) gastrointestinal complications such as nausea, vomiting, dianhea, 3) lowering of seizure threshold (since seizures can be a complication of AD, this side effect may be confused with the progression of the disease). Other acetylcholinesterase inhibitors have been shown to have a severe hepatotoxic effect, those products have been removed from the market or clinical development programs. IV. Impact of Genotyping on Drug Development for Dementia As previously indicated, the pathways and genes emphasize the relationship with Alzheimer's disease. In connection with the development of Alzheimers, it had been found that the presence of the ApoE4 allele was associated with an earlier development of the disease than other alleles, and further was associated with a decreased response to present acetylcholinesterase inhibitors, such as tacrine. The ε4 allele of Apolipoprotein E (ApoE) is a well-established risk factor for late onset Alzheimer's disease. The work of Poirier (1995) and Farlow (1998) suggests there are significant interactions between sex, ApoE genotype, and therapeutic response (ADAS-Cog scores) to the acetylcholinesterase inhibitor tacrine, with the ε4 allele generally associated with poor response and the effect being more notable in women than in men. ApoE is only part of the brain lipid transport pathway, however, and the interaction of allelic variation at other components of this pathway with drag response can also contribute to variation in therapeutic responses. Sequence variance in the butyrylcholinesterase (BCHE) gene has been found to conelate with the development of Alzheimer's disease, as well as with treatment efficacy of both cholinomimetic and non-cholinomimetic drag therapies. In this case, the presence of at least one BCHE-k allele is predictive of the development of Alzheimer's disease and is negatively conelated with treatment efficacy of tacrine (a colinestrase inhibitor) and an experimental vasopressinergic drag (a non- cholinomimetic drug). The BCHE-k allele has a point mutation at nucleotide 1828 (a G to A subsitution) which results in an ala539thr change. This polymoφhism can be readily detected by PCR amplifying a region sunounding the variance site and sequencing the amplification product to determine the nucleotide at the particular site. A group of patients was treated with an experimental vasopressinergic drug (n = 91 ) and compared to patients administered a placebo (n = 108) without segregation or stratification by BCHE or other allelic status. As evaluated using the Mini Mental State Examination (MMSE) over a twelve-week treatment period, no statistically significant improvement was shown for the treatment group. However, when the treatment group was stratified according to the presence or absence of a BCHE-k allele, those patients without such an allele showed a statistically significant improvement while those having at least one of the BCHE-k alleles did not. Thus, the analysis provides an example of a gene where a patient sub- population was identified where a treatment showed a positive response even though no such positive response was found for the overall patient population. Indeed, those patients not having a k-allele are approximately three times more likely to respond to the vasopressinergic drug than are patients having at least one k-allele. The response of Alzheimer's disease patients treated with the cholinomimetic drag, tactrine, was also determined. Similar to the above, the MMSE test was utilized as an indicator of a positive response. The positive response rate was approximately two- fold higher in those patients not having a k- allele than in those patients having at least one k-allele. In addition, it was found that the presence of either or both of a BCHE-k allele and an apoE-4 allele was positively conelated with the development of Alzheimer's disease. For example, in patients over 75 years of age, the odds ratio of a patient having a BCHE-k allele was 2.3, the odds ratio for having a apoE-4 allele was 2.0, and the odds ratio for the joint occunence of both alleles was 17.5. Thus, the BCHE-k allele is an example where the presence of a variant allele is negatively conelated with the efficacy of treatment with drags from multiple drag categories, and which is further postively conelated with the development of a particular disease. Thus, the variance status of such a gene is useful both as a prognostic tool for disease risk, as well as for identifying likely drag responders versus nonresponders for drug development and/or treatment selection. The evidence that a variance in a gene involved in a pathway that affects drag response in patients with dementia, indicates and supports the theory that there is a likelihood that other genes have similar qualities to various degrees. As drag research and development proceeds to identify more lead candidate therapeutic interventions for dementia, there is possible utility in stratifying patients based upon their genotype for these yet to be conelated variances. Further, as described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for dementia. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and matrix Table 7. Advantages of Pharmacogenomic Clinical Development of Therapies for Dementia The advantages of a clinical research and drag development program that includes the use of polymoφhic genotyping for the stratification of patients for the appropriate selection of candidate therapeutic intervention includes 1) identification of patients that may respond earlier to therapy, 2) identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both, 3) identification of pathophysiologic relevant variance or variances and potential therapies affecting those allelic genotypes or haplotypes, and 4) identification of allelic variances or haplotypes in genes that indirectly affects efficacy, safety or both. Based upon these advantages, designing and performing a clinical trial, either prospective or retrospective, which includes a genotype stratification arm will incoφorate analysis of clinical outcomes and genetic variation associated with those outcomes, and hypothesis testing of the statistically relevant conelation of the genotypic stratification and therapeutic benefits. If statistical relevance is detectable, these studies will be incoφorated into regulatory filings. Ultimately, these clinical trial data will be considered during the approval for marketing process, as well as, incoφorated into accepted medical management of dementia. By identifying subsets of patients with mild to moderate dementia that respond earlier to drags or agents or experience enhanced efficacy, optimal candidate therapeutic interventions may reduce the period of time prior to relief of cognitive impairments. Appropriate genotyping and conelation to dosing regimen would be beneficial to the patient, caregivers, medical personnel, and the patient's loved ones. Optimization of cholinomimetic mediated therapy of dementia further demonstrates the utility of selection of a potential dementia patient that has a predisposing genotype in which selective cholinomimetic are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine variance or variances within the muscarinic cholinergic receptor, nicotinic cholinergic receptor, modulatory mechanisms of cholinergic neurotransmission, or cholinergic receptor mediated intracellular mechanism of action that is preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drag development program for dementia. V. Description of Mechanism of Action Hypotheses for Future Drug Development or the Therapy of Dementia Drag development programs for the identification of novel drag or candidate therapeutic interventions are aimed at the underlying pathophysiologic mechanisms of the disease leading to clinical signs and symptoms of dementia. Cunent hypotheses include, but are not limited to, therapeutic development in one of the following areas: 1) replacement of cholinergic function, 2) acetylcholine pathway: biosynthesis, secretion, degradation, reuptake, and receptor binding, 3) CNS lipid transport/membrane repair pathway and gene identification, 4) inflammatory mediators, e.g. prostaglandin, prostacylin, and thromboxane pathway, and 5) constituents of AD lesions and AD genes. These are described in detail below. A- Therapeutic Approaches for Replacement of Cholinergic Function Because dementia is apparently related to a loss of cholinergic function in the neocortex and forebrain arising from death or atrophy of basal forebrain cholinergic neurons, replacement of cholinergic function has been shown to have therapeutic benefit. In general, novel approaches for the replacement of cholinergic function can be characterized as either: 1 ) therapies that compensate for existing damage; and 2) therapies that halt, retard, or prevent cerebral damage. B. Therapeutic approaches that compensate for existing damage The therapeutic approaches that may compensate for existing damage include modulating cholinergic deficit, modulating other neurotransmitter deficits, modulating immune or inflammatory mechanisms of neural damage, and modulation of metabolism of specific neurotransmitters. Although these novel therapies are aimed at existing or damage yet to occur, the underlying course of the disease will remain. Potential therapies for the compensation for cholinergic deficit are 1) increase presynaptic production of acetylcholine, 2) enhance release of acetylcholine, 3) stimulate choline reuptake, 4) selective muscarinic agonists, 5) antichohnesterase inhibitors, 6) mixed action anticholmesterases and muscanmc receptor ligands, and 6) mcotmic receptor agonists Potential therapies for the compensation for modulating other neurotransmitters are 1) selective NMDA agonists, and 2) other disorders of neurotransmitter function. Potential therapies for the compensation for modulating immune or inflammatory mechanisms of neural damage are 1) antiinflammatory agents that suppress inflammation and 2) inhibition of amyloid precursor protein (APP) degradation. Potential therapies that compensate for monoamine metabolite deficits are agents that affect monoamine oxidase type B enzyme activity, therapy for behavioral symptoms of neurotransmitter function in dementia, and compensate for immune or inflammatory mechanisms involved in neural cell destruction C Therapeutic approaches that halt, retard, or prevent cerebral damage In general therapeutic approaches that halt, retard, or prevent cerebral neural damage are cunently either growth factors or modulation of the deposition of abenent pathological depositions of metabolic by-products These approaches include promotion of the growth and regeneration of cholinergic neurons and generally include growth factors that act on neurons, neural precursors, or glial cells Growth factors mcludebut are not limited to nerve growth factor (NGF), bram- deπved growth factor (BDGF), neurotrophms, and leukemia inhibitory factor (LIF) Prevention of amyloid plaque deposition includes modulation of APP gene expression, prevention of the development of amyloidogemc peptide, inhibition of amyloid aggregation/secretion, and APP antagonists. Prevention of the formation of neurofibnllary tangles includes modulation of the phosphorylation of tau proteins D CNS Lipid Transport/Membrane Repair Pathway and Gene Identification Bram Apohpoprotems The six apohpoprotems known to be expressed in the brain are listed below They are present on the surface of three major types of lipoproteins, one class enriched in A-I, but also containing most of the D,E, and J protein in the brain; one class composed pnncipally of E with minor amounts of A-I, A-IV, D, and J; and a third minor class containing the majonty of A-IV Vanation in the stmcture or expression of these apohpoprotems can modulate lipid transport and bram remodeling Lipoprotein Receptors Six bram receptors for lipoproteins have been identified in man. These include the low density lipoprotein receptor (LDL-R), the LDL receptor-related protem (LRP), the very low density lipoprotein receptor (VLDL-R), and the class A macrophage scavenger receptor, all of which are also expressed outside the brain. Two new protein with LDL receptor-like domains have recently been identified in human brain: Apolipoprotein E receptor type 2, and the SorLA-1 receptor. Alterations in the stmcture or expression of those receptors can affect binding of ApoE alleles (ApoE2, for example, has reduced affinity for the LDL receptor), and more generally will modulate the biology of lipid transport. Lipoprotein docking and lipid mobilization: Heparin sulfate proteoglyans (HSPG) are responsible for initial binding of ApoE-bearing lipoproteins to cells. Removal of HSPGs with heparinase blocks binding, even in the presence of receptor (LDL-R or LRP). Therefore variations in biosynthetic enzymes of the HSPG pathway will influence lipoprotein uptake. Lipid hydrolysis by cholesterol ester transfer protein (CETP) effects the transport of lipids from lipoproteins into cells. Cholesterol Metabolism: Acyl CoAxholesterol acyltransferase and HMG CoA reductase are responsible for the metabolism of cholesterol, therefore variations in the metabolic pathway of cholesterol will influence availability of cholesterol. Hormonal control of lipoproteins and lipoprotein receptors: The expression of lipoproteins and their receptors is under hormonal control. Clinical studies of tacrine for Alzheimer's disease have also shown reduced incidence of AD in women taking estrogen supplements post menopausally. Therefore, variation in hormone levels, hormone receptors, or hormone receptor signaling pathways will modulate response to acetylcholinesterase inhibitors, e.g., by affecting lipid transport and cholinergic remodeling or by other means. Hormone receptors that bind their physiologic ligand within the cytoplasm then become activated and cross the nuclear membrane include but are not limited to growth hormone, prolactin, estrogen, retinoic acid receptor, thyrotropin releasing hormone. Associated transcriptional co- activators include but are not limited to SRC-1, SRC-2 (TIF-2), SRC-3 (p/CIP:AIBl), P/CAF, CBP, E6-AP, TRIP230, SMRT, SRA, and N-CoR. E. Prostaglandin, Prostacylin, and Thromboxane Pathway Inflammatory mediators, and in particular the products of arachidonic acid metabolism, play a role in the development of AD neuropathology. There are several lines of evidence supporting the role of inflammatory or immunological processes in the pathogenesis of Alzheimer's disease. First, neurodegeneration in AD is accompanied by manifestations of immune reaction including activation of the complement cascade, accumulation and activation of microglia and presence of inflammatory cytokines and acute phase reactants in tissue of AD brains. Second, epidemiological studies suggest that use of non- steroidal anti-inflammatory drugs (NSAIDs) delays the clinical expression of Alzheimer's disease. The development of selective COX inhibitors has led to renewed interest in the therapeutic potential of NSAIDs in AD. Arachidonic acid formation pathway genes include phospholipase A2, phospholipase C β3, and diacylglycerol lipase. PGG2 formation pathway genes include cyclooxygenase I, cyclooxygenase II. PGH2 formation pathway genes include PGG2 reductase. PGH2 metabolizing enzymes include PGH2 reductase, PGD2 reductase, PGH-PGE isomerase, and thromboxane A2 synthase. Receptors include PGFla receptor, PGD2 receptor, PGE2 receptor, PG12 receptor, and thromboxane A receptor. Exemplary variances for genes above are shown in Tables 13 and 19. F. Constituents of Alzheimer's Disease Lesions and AD Genes The relative contribution of different pathogenetic mechanisms to the development of AD in specific patients can affect the degree of cholinergic impairment and hence the response to acetylcholinesterase inhibitors. There is clear evidence that different pathogenetic mechanisms affect the onset and rate of progression of AD. The possible effects of such are several lines of evidence supporting the role of inflammatory or immunological processes in the pathogenesis of Alzheimer's disease. First, neurodegeneration in AD is accompanied by manifestations of immune reaction including activation of the complement cascade, accumulation and activation of microglia and presence of inflammatory cytokines and acute phase reactants in tissue of AD brains. Second, epidemiological studies suggest that use of non-steroidal anti-inflammatory drags (NSAIDs) delays the clinical expression of Alzheimer's disease. The development of selective COX inhibitors has led to renewed interest in the theφaeutic potential of NSAIDS in AD. Pathway genes include Tau protein, amyloid precursor protein, presenilin 1, and presenilin 2. In Tables 13 and 19, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with dementia based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of dementia include, but are not limited to, glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, histaminergic, purinergic, GABAergic, glycinergic, nitric oxide, peptide protein processing, opiates, cholecystokinin, corticotropin releasing factor, thyroid stimulating hormone, somatostatin, adrenocorticotropic hormone, vasoactive intestinal peptide, calsium or potassium channels, prostaglandin, cytokines, estrogen, clot formation, hemostasis, oxygenstress, mitochondrial maintenance, protein maturation and degradation, second messenger cascade, growth, differentiation and apoptosis, cytoskeleton, secretion, amyloid processing, and lipid transport or metabolism gene pathways that are listed in Tables 1 -6, 12-17 and 18-23. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of dementia, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drag response to therapies for dementia. A sample of therapies approved or in development for preventing or treating the progression of symptoms of dementia cunently known in the art is shown in Table 27. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Based upon these varying approaches there are many products in development for dementia. In Table 27 below lists current therapies that are in development for U.S. marketing approval. Identification of genes in specific pathways and the link to specific agents or drugs may be useful to conduct clinical trials and achieve higher degrees of safety and efficacy. The listed candidate therapeutic interventions response in patients with dementia may be affected by polymoφhisms in genes as described above. Example 12 Depression /. Description of Depression Major depression is a psychiatric disorder distinguishable from normal grief, sadness, and disappointment as well as the dysphoria and demoralization often associated with medical illness. Depressive disorders are characterized by abnormally long term depressed mood and may be accompanied by delusions and hallucinations. Individuals suffering from depression have feelings of despair and intense sadness, exhibit mental slowing and loss of concentration, are preoccupied with pessimistic worry and inner self, and are agitated and tend toward self- deprecation. In some depressive disorders, mania is present usually in episodic intervals and in these cases depressed mood is replaced with feelings of grandiosity and may be accompanied by incoherent speech. Clinically, unipolar or bipolar depression are terms used to describe the two broad categories of depressive disorders characterized by the absence or presence of episodic mania, respectively. II. Current Medical Management Strategies for Depression Unipolar Depression Depression is a wide-spread disease that requires improved therapeutic alternatives to the conventional agents that have been available since the 1960s. Cunent therapeutic candidates of unipolar or bipolar depression are as follows: tricyclic antidepressants, tetracyclic antidepressants, lithium, monoamine oxidase (MAO) inhibitors, electroconvulsive therapy (ECT) and atypical agents such as PROZAC ® , WELLBUTRTN ® , and trazodone. Bipolar Depression Despite the difficulties of medical management of bipolar depression, advances have changed therapeutic outcomes. Therapies such as lithium, valproate, and carbamazepine, clozapine, and ECT have made a positive impact on the patient outcomes. Further, the importance of psychosocial issues for understanding patients illnesses and factors affecting treatment compliance are more fully realized. For bipolar depression, mood stabilizers are the first line therapy and include: lithium, valproate, and carbamazepine. Adjunct therapies are used for the treatment of agitation, insomnia, or aggressive behaviors and include benzidiazepines and antipyschotics. ECT is useful as an alternative therapy in patients who are pregnant or are trying to conceive, unresponsive to standard therapy, unable to tolerate first line therapies, or are refractory to first line or adjunct therapies. ECT has been shown to be effective as stated above, as well as 54% effective in refractory patients. There are additional therapies that have been used for the treatment of bipolar depression. For example, off-label use of clozapine, Ca++ channel antagonists, gabapentin, and lamotrigine in diagnosed bipolar patients have been demonstrated to be effective at stabilizing mood. Gabapentin, has a higher safety profile during pregnancy, but has side effects of ataxia, fatigue and somnolence. Lamotrigine, by effectively lowering glutamine release is effective at stabilizing mood, but is associated with dizziness, headache, double vision, somnolence, headache, and rash. Other medications include valproate for euphoric mania, valproate for dysphoric mania or mixed mania, and clozapine with lithium or valproate for patients with rapid-cycling episodes. III. Limitation of Current Therapies for Depression Frequently, depression is undiagnosed and if detected, treatment often is inadequate. Therapy of depression is associated with undesirable side effects and/or simply fails to adequately manage the symptoms of the condition. Thus, there is a need for ongoing improved development of antidepressant therapeutic alternatives to the cunently available products. Limitations of Cunent Therapies for Unipolar Depression Although these agents or therapies are efficacious (e.g. 80%o improvement following ECT; lithium effectively prevents relapses in 60%> of patients) there are significant limitations to their use and are 1) the onset of action of antidepressant drags is latent, 2) responsivity and efficacy is not uniform, 3) long-term treatment can lead to symptoms of drag resistance, 4) there is perceived inhibition of creativity and decreased energy, and 5) there are patients with refractory depression with no therapeutic alternatives. Limitations of Cunent Therapies for Bipolar Depression Bipolar depression patients have additional therapeutic concerns as compared to unipolar depression patients. For bipolar patients there is the added difficulty of treating depression episodes. The efficacy of antidepressants is not well founded or documented in bipolar depression. Further, antidepressants have been documented to induce manic or hypomanic symptoms. Therefore, mood stabilizers are the first line therapy with adjunct therapies during manic or depression episodes. An additional therapeutic issue associated with bipolar patients is that many comorbid psychiatric disorders occur within the same patient not only hindering a diagnosis, but also therapy. For example, substance abuse disorders, panic disorders, obsessive-compulsive disorders, and impulsive control disorders are often present and potentially mask symptoms of bipolar depression. IV. Impact of Pharmacogenomics on Drug Development for Depression There are two genes that have been described having polymoφhisms that affect antidepression drag response, the serotonin transporter gene and the angiotension converting enzyme that affects the metabolism of substance P. These two examples are described below. The Serotonin Transporter Gene The serotonin transporter gene (5-HTT) polymoφhism provides an example of a recessive SNP polymoφhism in the non-coding region with an impact on inefficacy of a 5-HTT selective drag. The serotonin transporter (5-HTT) plays a critical role in the termination of the serotonin (5-HT) neurotransmission and represent the prime target for selective serotonin reuptake inhibitors (SSRIs). A functional polymoφhism in the transcriptional control region upstream of the 5-HTT coding sequence has been reported. It consists of a 44 -base pair insertion (long variant) or deletion (short variant). It has been demonstrated that the long (1) and short (s) variants of this 5- HTT gene-linked polymoφhic region had different transcriptional efficiencies. In vitro studies showed that the difference in 5-HTT mRNA synthesis result in different 5-HTT expression and 5-HT cellular uptake (Lesch et al. Science 1996 274: 1527-153). Recently, it has been shown that an SSRI (fluvoxamine) efficacy in delusional depression seems to be related to allelic variation within the promoter of the 5-HTT gene (Smeraldi et al. Mol. Psychiatry 1998; 3:508-51 1). Both homozygotes for the long variant (1/1) of the 5-HTT promoter and heterozygotes (1 s) showed a better response to fluvoxamine than homozygotes for the short variant (s/s). Interestingly, the addition of pindolol (a mixed adrenoreceptor and 5-HT 1 A antagonist) has been proposed as an augmentation therapy for non-responders or partial responders to SSRIs, and it appears that in the group treated with fluvoxamine plus pindolol all the genotypes acted like 1 1 treated with fluvoxamine alone. This supports the hypothesis that the effect of pindolol is related to its ability to block 5-HT 1 A autoreceptors, thus preventing a negative feed-back of 5-HT at somatodendritic level. Furthermore, the activation of 5-HT1A autoreceptors could modulate the clinical effect of the SSRIs-induced 5-HTT blockade. The 5-HTT polymoφhism represents an example of a gene allelic variance that affects the transcriptional control, and ultimately, the amount of available transporter protein. In these cases, the gene product concentration or protein availability affects the function of the native mechanism and ultimately the ability of the drug to intervene with physiological function. One skilled in the art, upon utilizing the techniques described in the detailed description, would be able to identify known variances within a candidate gene, provide a diagnostic test to identify individuals with that variance or variances, group the individuals based upon the identified genotype, and design and implement a clinical study to test the effect a candidate drag has on the the groups. In this example, the allelic differences may affect transcriptional or translational control of the 5-HTT gene. A skilled practitioner will be able to utilize the techniques known in the art to determine the effects of a variance or variances within a gene promoter region to be able to study the impact those allelic differences have on the safety or efficacy of SSRIs or any other candidate drags affecting the 5-HT pathway. Further, this example underscores the ability of a skilled practitioner to be able to utilize methods known in the art to design a pharmacogenomics clinical trial when the allelic difference is within the gene promoter region. The Angiotensin Converting Enzyme Gene and Substance P The localization of substance P in brain regions that coordinate stress responses and receive convergent monoaminergic innervation suggested that substance P antagonists might have psychotherapeutic properties. Similar to clinically used antidepressant and anxiolytic drags, substance P antagonists suppress isolation-induced vocalizations in guinea pigs. In a placebo-controlled trial in patients with moderate to severe major depression, robust antidepressant effects of the substance P antagonist MK-869 were consistently observed. In preclinical studies, substance P antagonists did not interact with monoamine systems in the manner seen with established antidepressant drags. These findings suggest that substance P may play an important role in psychiatric disorders. Substance P is highly metabolized by ACE (angiotensin converting enzyme) which is a good actual example of pharmacogenetics: It has a high allele frequency in normal individuals (D: 34%>, I: 66%>) and there are clinical studies clearly demonstrating its impact on ACE inhibitors. Moreover, it has been shown that DD homozygous patients ( 1 1 %>) have a higher brain level of substance P than II homozygous patients (43%>), with an intermediate level for heterozygous patients (46%). Using results of the initial phase II trial, we expect that a substance P antagonist will have more impact on patients with high brain level of substance P (actually, the DD patients who are more at risk for affective disorders). As measure of response rate, starting with the standard measure of response defined as >50% change from baseline to week 6 in total HAM-D21 score, 54%> of the patients improved with MK-869 and 28%o patients improved with placebo in the phase II trial. In a recent clinical trial of MK-869 versus placebo, a similar response rate was observed for both groups (54%o and 48% respectively). If the ACE variance is considered as a dominant SNP with regard to substance P metabolism, calculation of an unequivocal positive response rate in the DD subgroup (i.e., 100%>) would require an equally similar response rate in the II subgroup, while assuming the DI subgroup response rate remains similar to placebo (i.e., 48%). In this case, MK-869 would be positive (100%>) only in a fraction of the patients, e.g., one out of every five. Approximately 25% of the responders should be DD homozygous; if not, the hypothesis is not valid. Then, if 25% are DD, the number of patients included in the failed trial should be enough to see a statistically significant difference between the DD subgroup and other patients, since we would need at least 56 patients to test for such a high relative risk (100%, / 48% = 2). This approach exemplifies the utility of high allele frequency polymoφhisms. Further, when the treatment is not efficacious for all individuals (i.e. response rates vary between treatment groups is less than 15%) the allele frequency of a potentially interacting recessive SNP polymoφhism should be relatively high (e.g. from 30% for a 15% difference in response rate to 60%). This conesponds to 16% or less of total patients (see example 18 and table below). The evidence that a variance in a gene involved in a pathway affects antidepressive drug response, indicates and supports the idea that other genes have similar qualities to various degrees. As drag research and development proceeds to identify more lead candidate therapeutic interventions for depression, there is utility in stratifying patients based upon their genotype for these yet to be conelated variances. Further, as described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily utilized for depression. As described below in section V. below there are likely gene pathways such as those outlined in the gene pathway Table 2 and matrix Table 7. Optimization of adrenergic control or ion channel modulation mediated therapy of epilepsy further demonstrates the utility of selection of a potential epilepsy patient that has a predisposing genotype in which selective adrenergic or agents are more effective and or are safer. In considering an optimization protocol, one can potentially predetermine variance or variances within the adrenergic receptor, ion channel or ion channel mediated mechanisms of neurotransmission, or adrenergic receptor mediated intracellular mechanism of action that is preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drag development program for depression. A sample of therapies in development for preventing or treating the progression of symptoms of depression cunently known in the art is shown in table 28. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. V. Mechanism of Action Hypotheses for Novel Therapies for Depression: Utility of Genotyping Unipolar Depression Unfortunately, to date the biological mechanism of major unipolar depression is unclear. However, studies of endocrine systems, neurotransmission, and neuroelectrophysiology have provided the basis for the generation of pathophysiologic hypotheses. These hypotheses have been supported by clinical data stemming from the success of conventional treatment of depression. One such hypothesis is that there is pituitary-hypothalamic dysfunction in depressed patients. It has been observed that depressed patients commonly have elevated levels of cortical steroids in their urine and blood. Further, 50%> of the patients with clinical depression will not secrete cortisol when subjected to the dexamethasone suppression test. Additionally, thyrotropin releasing hormone (TRH) stimulation of thyrotropin stimulating hormone (TSH) release is abenant in depressed patients without an alteration of serum T3 or T4 concentrations and growth hormone, prolactin, gonadal hormones, corticotropin releasing factor (CRF), and melatonin have diminished physiologic responses. Another hypothesis of the biological dysfunction of depression is that there is a neurotransmitter dysfunction due to a catecholamine-indolamine imbalance. This theory postulates that there is a required level of catecholamines and receptor sensitivity required for normal mood. In depression, there may be abenant receptor insensitivity, depletion of amines, or a depletion of their synthesis or storage that leads to depression. Supporting this theory is that monoamine oxidase inhibitors increase the availability of catecholamines and indolamines and have been used clinically for the management of depression. The cholinergic neurotransmitter system has been implicated in the manifestation of depression. In has been postulated that there is an imbalance of adrenergic and cholinergic control of neural transmission in patients with depression. Electrophysiologic studies have shown that patients with depression have altered rapid eye movement (REM) sleep patterns, i.e. shortened REM latency, than non-depressed patients. Other studies have documented a conelation of the circadian rhythm and precipitation of depressive episodes during autumn and winter months and diminished ambient light during those times during the year. In each of the theories posited and described above, satisfactory conclusions are limited. Conventional therapy of depression with tricyclic antidepressants has demonstrated that this treatment affects more than one neurotransmitter system due to either modification or alteration of the regulation of neurotransmitter receptors signaling pathways rather than acting solely at neurotransmitter receptor binding. Novel therapies of unipolar depression include venlafaxine and mirtazapine. Both of these compounds show promise in clinical trials for the treatment of depression. Venlafaxine is a mixed serotonergic and noradrenergic reuptake inhibitor. Mirtazapine has noradrenergic and serotonergic antidepressant mechanism of action. These two products have what looks to be superior action over tricyclic antidepressants or selective serotonergic inhibitors (SSRIs). Bipolar Depression Theories for the mechanism have been described. In one model, electrophysiological kindling and behavior sensitization underlie bipolar disorders and further increasing frequencies of episodes over time. In another model, there appears to be a desynchronization of circadian rhythm in bipolar patients. As for depression, the catecholamine hypothesis presumes that mania is due to an excess of catecholamines and depression is due to their depletion. Noradrenergic and dopaminergic dysfunction have both been linked to depression. In both cases of dysfunction, there appears to be causal links, i.e. abenant noradrenergic neurotransmission and L-dopa induced hypomania among bipolar patients, respectively. Amphetamines can produce hypomania in bipolar patients and dopaminergic antagonists are effective for severe mania. The serotonergic hypothesis generalizes that low serotonergic transmission is responsible for mania and depression because low serotonergic inputs may result in defective neuromodulation. Other hypotheses include neurotransmitters, enzymes, neuropeptides, and theories involving endocrine and immunological systems. As in many other complex disorders of psychological function, these models fall short of adequately describing the disturbance. Future studies and drag development may provide insights to refined biological mechanism of bipolar depression. In Tables 13, and 19, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with depression based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of depression include glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, purinergic, GABAergic, melatonin, peptide protein processing, opiates, oxytocin, neuropeptide Y, calcitonin/calcitonin gene related peptide, tachykinin, corticotropin releasing factor, vasopressin, calcium or potassium channels, prostaglandin, testosterone, oxygen stress, second messenger cascade, folate metabolism pathways that are listed in Tables 2, 7, 13, and 19. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of depression, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drag response to therapies for depression. In Table 28 below is a list of the available candidate therapeutic alternatives available or in development for depression. There are listed by therapeutic approach are defined and listed in Table 2. The listed candidate therapeutic interventions response in patients with depression may be affected by polymoφhims in genes as described above. Example 13 Epilepsy I. Description of Epilepsy Epilepsy is a neurological disorder affecting an estimated 1.8 million Americans with estimated direct and indirect costs of illness to be approximately $3 billion dollars. Epilepsy is characterized by the behavioral consequences of recunent, spontaneous, transient paroxysms of abnormal brain activity. An epileptic attack or seizure may result in impaired consciousness, involuntary movements, autonomic disturbances, psychic or sensory disturbances. The fundamental etiology of epilepsy is thought to occur within the cerebral cortex or limbic cortex (hippocampus). Chronic epilepsy is the syndrome in which recurrent neuronal paroxysms that underlie ictal events are transient expression of more permanently physiological disordered cortex. In ascertaining the location and the diagnosis of epilepsy, one can determine patterns of uncoordinated cortex by examination of ictal and interictal EEG recordings. Interictal recordings of epilepsy patients have an appearance of brief discharges that can be recorded from the scalp. There is a noticeable spike-wave complex that is evident and is characterized by shaφ negative transients followed by a slower wave. The EEG spike-wave complex reflects a summation of highly synchronized abnormal neuronal membrane potentials that upon inspection appear as large paroxsymal depolarization shifts followed by prolonged after depolarizations. Epilepsy can be divided into the following categories based upon etiology: 1) primary epilepsy which is an intrinsic, nonprogressive, hereditary group of cerebral disturbances, 2) secondary epilepsy which is symptomatic of some know pathologic processes affecting the brain, and 3) reactive seizures which are characterized by natural reaction to physiologic stress or transient ischemic injury. Epilepsy can be categorized into the following categories: partial seizures, generalized seizures, and seizures of unknown origin. Partial seizures are initiated (uni- or bilaterally) in discrete focal areas in the cortex and remain focal lesions. Generalized seizures begin either uni- or bilaterally and spread throughout the cortical tissue. In either case the mechanism of epileptogenic activity is to date unknown. However, there is evidence suggesting the etiology of epilepsy. Partial seizures can be further subcategorized into: 1 ) simple partial seizure disorders, consciousness not impaired (with motor signs or symptoms, with somatosensory or special sensory symptoms (e.g. simple hallucinations, such as tingling, light flashes, buzzing), with autonomic signs and symptoms (e.g. epigastric sensation, pallor, sweating, flushing, piloerection and pupilary dilation), with psychic symptoms (e.g. disturbances of higher cerebral function (deja vu, fear, distortion of time perception)); or 2) complex partial seizure disorders (simple partial onset following impairment of consciousness, impairment of consciousness at onset); or 3) partial seizures evolving to generalized tonic clonic seizures (simple partial seizures evolving to generalized seizures, complex partial seizures evolving to generalized seizures, and simple partial seizures evolving to complex partial seizures and further evolving to generalized seizures). A key feature of partial epilepsy is auras. These somatosensory or special sensory symptoms manifest as sensations described above and precede the seizure. There are cases whereby pharmacotherapy reduces the frequency and severity of partial seizures but may have little to no effect on aura sensation in partial epilepsy patients. Generalized seizures are divided into 1) nonconvulsive seizures (absence seizures, atypical seizures, myoclonic seizures, or atonic seizures), or 22) convulsive seizures (tonic-clonic seizures, tonic seizures, or clonic seizures). Other seizure disorders that do not fit into the above categories are some cases of neonatal and infantile seizures. There are other factors that one must consider when diagnosing seizure disorders. A generalized seizure may be the result sleep deprivation, alcohol or sedative drag withdrawal, use of convulsant drags, fever, or acute head trauma. Furthermore, reversible toxic, infectious, or metabolic processes may induce recunent generalized convulsions. Infantile febrile convulsions are an example of infancy and early childhood seizures that may or may not be indicative of a future epilepsy diagnosis. Acquired epilepsy may be the result of congenital lesions, head trauma, infectious processes, brain tumors, cerebrovascular disease, systemic toxic and metabolic disturbances, hippocampal sclerosis, and miscellaneous disorders (collagen vascular disease, blood dyscrasias, cerebral gray matter degenerating diseases (allergic encephalopathy), presenile or senile dementias). Epilepsy may be confused with clinical signs and symptoms of syncope, migraine, or pseudoseizures (nonepileptic psychogenic seizures). Usually, video/EEG monitoring of the patient during ictal and interictal periods allows trained personnel to distinguish epilepsy from these other clinical presentations. II. Current Medical Management of Epilepsy For the majority of patients, epileptic seizures can be controlled with antiepileptic drag therapy (in many cases, monotherapy) and may be withdrawn if the patient is seizure free for an extended period, usually 2 years. Some patients do not become free of seizures, despite therapy compliance. Persistent epilepsy, aside from deleterious effects on health, has psychosocial, behavioral, and cognitive consequences, which often impose financial burdens to patients, their loved ones, and society. Based upon accurate diagnosis of the seizure type and seizure-associated physiology, appropriate therapy to reduce seizure frequency, severity, and epilepsy- associated behaviors can be identified. Diagnosis of epilepsy involves both identification of the epileptic syndrome and the type of seizure. Syndromes are identified based upon age of onset, EEG recording analysis, location of the epileptic region or site of epileptogenesis, type of seizure. The drags available for medical management of epilepsy are divided by their use in the clinic; common forms of epilepsy are treated differently that partial or secondarily generalized tonic-clonic seizures disorders. The cunent pharmacotherapy has three main mechanisms of action: 1) reduction of sustained repetitive firing of a neuron by promoting the inactivation state of voltage- activated Na+ channels; 2) enhanced GABAergic mediated presynaptic or postsynaptic inhibition of neural transmission; or 3) limiting the activation of specific voltage-activated Ca++ channels (T cunent). Following these general mechanism of action, current anticonvulsant drugs act by 1) prolonging the inactivation of the Na+ channels thereby reducing the ability of neurons to fire at high frequencies, 2) affecting GABAergic neurotransmission by reducing the metabolism of GABA, acting at the GABA receptor, enhancing the Cl " influx in response to GABA postsynaptically, or promoting presynaptic GABA release, or 3) reducing the flow Ca++ T-type calcium channels reducing the pacemaker cunent that underlies the thalmic rhythm in spikes and waves in generalized absence seizures. There are generally accepted first- and second-line drags for each of the types of epilepsies and associated syndromes. For partial seizures they are carbamazepine and phenytoin (first-line) and gabapentin, lamotrigine, phenobarbital, primidone, tagabine, topiramate and valproic acid (second-line). For generalized seizures they are: absence seizures ethosuximide and valproic acid (first-line); lamotrigine (second-line); myoclonic seizures, valproic acid (first-line), acetazolamide, clonazepam, lamotrigine, or primidone (second-line)); tonic-clonic seizures valproic acid, carbamazepine, phenytoin (first-line), lamotrigine, phenobarbital, primidone (second-line); absence epilepsy with onset in childhood ethosuximide (first-line), valproic acid, lamotrigine (second-line); absence seizures with onset in adolescence valproic acid (first-line), ethosuximide, lamotrigine (second-line)); juvenile myoclonic epilepsy valproic acid (first-line), acetazolamide, clonazepam, primidone, lamotrigine (second-line); infantile spasms (West's syndrome corticotropin (first-line), clonazepam, valproic acid)); Lennox-Gastaut syndrome valproic acid, lamotrigine (first-line), carbamazepine (second-line). Because there is greater risk for refractory epilepsy in partial epilepsy patients, there has been greater demand for the development of novel treatment alternatives. Since 1993 and as stated above, the introduction of lamotrigine, topiramate, tiagabine, and gabapentin have changed the medical management of partial epilepsy. Although carbamazepine and phenytoin remain the mainstay therapies, these additions to the antiepileptic arsenal have provided therapeutic alternatives to this subset population of epilepsy patients. In addition to AEDs, refractory epilepsy may benefit from surgical therapy to remove the site of epileptogenesis or implantation of a device to stimulate the vagus nerve. Surgical removal of cortical tissue can be successful therapy in up to two thirds of certain selected epilepsy and can reduce the seizure frequency and severity in others. However, surgical therapy of refractory epilepsy is underused, and is often a delayed procedure. It has been estimated that there are approximately 50,000 epilepsy patients that could benefit from resective surgery, however, there are only an estimated 1,500 surgeries performed each year. Potential reasons for the profound difference in the potential number of surgical candidates and the number of procedures include: limited number of surgical teams performing the resective surgery; failure of primary physicians to identify potential candidates and to refer them to surgical centers; reluctance of third party payers to provide coverage for the costly presurgical diagnostic testing and procedures; and further, a reluctance on the part of the patient to voluntarily elect removal of cortical tissue. Vagal nerve stimulation for the treatment of some patients with epilepsy has proven to be safe and well tolerated. A device is implanted in the upper quadrant that can be programmed to directly stimulate the vagal nerve. Stimulation of this autonomic nerve has lead to a documented 25%) reduction of seizure frequency in refractory patients. The device does not appear to have similar efficacy when implanted in a partial epilepsy patient population. The use of the surgically implanted device has recently only been approved in the U.S. (June, 1997) for patients over 12 years of age with known refractory partial epilepsy. Transient hoarseness is a frequent side-effect of this device as a result of over-stimulation of the vagal nerve. -777- Limitations of Current Therapies for Epilepsy The limitations of cunent medical management of epilepsy are 1) partial response to therapy or refractory epilepsy, 2) undesired side effects, 3) continuing medical management of refractory or partial response in epilepsy patients, and 4) noncomphance. Partial Response to Therapy and Refractory Epilepsy as a Therapeutic Limitation Approximately 80%> of patients with epilepsy are medically managed with cunent pharmacotherapy. In the remaining 20%>, epileptic seizure frequency and severity are refractory to cunently available medications. Medical personnel are left with attempting combination therapy of available anti-convulsive therapy. Standard regimens of multiple anticonvulsant therapy are fraught with greater tendency towards unwanted side effects. Interestingly, 20%> of the primary generalized epilepsy patients and 35% of partial epilepsy patients are refractory. A poor response to anti-epileptic therapy may be result of many different therapeutic or diagnostic causes. Since the focus of therapeutic management of refractory epilepsy is combination antiepileptic drug therapy, the balance of beneficial therapy and the patient's intolerance of the adverse effects of the AEDs must be appropriately monitored. Undesired Side Effects or Toxicities as a Therapeutic Limitation All of the anti-epilepsy agents or compounds have undesired side effects. For example, nausea, dizziness, diplopia, ataxia, sedation, impaired mentation, hyperactivity, folic acid deficiency, leukopenia, elevated serum alkaline phosphatase levels, pruritis, blood dyscrasias, hirsutism, gingival hypeφlasia, coarsening features, weight gain, and alopecia have been described for various anticonvulsant therapies. Individuals with epilepsy have an increased rate of mortality as compared to the general population. Mortality is associated with treatment and with seizures and may include one or more of the following: trauma, bums, and drowning, habitual seizures with cardiopulmonary disease, severe aspiration, food bolus, and sudden unexplained death. Sudden unexplained death in epilepsy patients (SUDEP) has been reported as high as 1 in 270 patients that are refractory to anti epilepsy drags, and is a statistic that does not include suicides. Additional concern of combination therapy besides increased propensity to experience undesirable side effects is the effect of metabolic rates and blood levels of the combinations. There is ample literature on the effect one antiepileptic agent has on another, for example carbamazepine decreases the blood levels of clanzepam, ethosuximide, methsuximide, primidone, tiagabine, topiramate, and valproic acid while increasing phenobarbital blood levels. Clonazepam decreases the blood levels of carbamazepine while decreasing primidone blood levels. Continuous Medical Management as a Therapeutic Limitation Antiepileptic drag (AED) therapy of epilepsy requires continuous medical monitoring. Factors involving lifestyle may trigger seizures in a patient diagnosed with epilepsy who have seemingly medically managed disease. For example, emotional stress, sleep deprivation, menstrual cycle, flickering lights and other sensory stimuli, alcohol use or withdrawal, or comorbidities (i.e. infections) may exacerbate seizures. Noncomphance as a Limitation of Cunent Therapies Noncomphance or partial compliance is a major concern in both monotherapy or combination therapy. Many patients who are in what appears to be remission , tend to noncomphance of their prescribed therapy. Determining plasma levels of the drag or drags can monitor compliance, but this places an added burden on the patient and family members. Noncomphance can result from additional factors: missed medication, failure to refill the medication, a complicated dosing regimen, problems with memory or vision, postictal confusion, denial of medical condition, fear of teratogenic effects of the drug or drugs during pregnancy, concerns about the effects (both short and long-term) of the medication, and inability to afford the medication. Clearly, for some patients, refined therapeutic management of seizure frequency and severity would have benefits above and beyond the clinical setting. Without many therapeutic alternatives to refine combination antiepileptic agent regimens, epilepsy poses a continued impact on health-related quality of life for each patient. IV. Impact of Pharmacogenomics on Drug Development for Epilepsy Genetic mechanisms of epilepsy have recently been described. However, the clinical genetics of seizure disorders has been a relatively slowly progressing field. Molecular genetic approaches have been useful to identify genes or gene clusters involved in linkage analysis. Genetic polymoφhism analysis and effects of antiepileptic drag therapy was recently described for the cytochrome P450 2C9 and 2C19 genes and these variance differences on the metabolic rates of phenytoin. The polymoφhisms considered in this study were the argl44cys and the ile3591eu of the CYP2C9 gene and the *1, *2, and *3 polymoφhisms of CYP2C19. In this study of 134 Japanese patients, the mean maximal metabolic rates of phenytoin were 42%> lower in individuals having the ile3591eu genotype. From this analysis, the authors conclude that patients with the ile3591eu genotype may not tolerate higher daily doses of phenytoin and may require genetic identification prior to implementation of medical strategies. The evidence that a variance in a gene involved in a pathway that affects antiepilepsy drug response, indicates and supports the expectation that there is a likelihood that other genes have similar qualities to various degrees. As drug research and development proceeds to identify more lead candidate therapeutic interventions for epilepsy, there is possible utility in stratifying patients based upon their genotype for these yet to be conelated variances. Further, as described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for epilepsy. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and in the gene pathway and indication matrix Table 7. Optimization of GABAergic or ion channel modulation mediated therapy of epilepsy further demonstrates the utility of selection of a potential epilepsy patient that has a predisposing genotype in which selective AED or agents are more effective and or are safer. In considering an optimization protocol, one could potentially predetermine variance or variances within the GABAergic receptor, ion channel or ion channel mediated mechanisms of neurotransmission, or GABAergic receptor mediated intracellular mechanism of action that is preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drag development program for epilepsy. A sample of therapies approved or in development for preventing or treating the progression of symptoms of epilepy cunently known in the art is shown in table 29. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. V. Mechanism of Action Hypotheses for Novel Therapies for Epilepsy: Utility of Genotyping Further studies have demonstrated that there is a genetic component to epilepsy. These genetic factors may predispose by an individual to epilepsy by inheriting one or more of the following 1) low threshold for abenant seizure activity; 2) traits that underlie certain specific primary epilepsy disorders; and 3) a disease of the CNS in which there are associated structural disturbances that produce seizures. As described above there is an urgent need for the discovery and development of therapeutic alternatives for the medical management of epilepsy. Recent research and development programs have included the following exemplary hypothesis testing programs. In a first hypothesis, glutamate neurotransmitter pathway has been implicated in abenant excitatory neurotransmission. Glutamate and aspartate are ligands for the N-methyl-D-aspartate receptors and ionophore receptors (AMPA and Glu 1-4). Research efforts have been dedicated to eliciting glutaminergic specific antagonists that may be productive inhibitors of abenent exicitatory neural signals or may be effective to attentuate neural modulatory mechanisms that are defective in epileptogenic tissue. Another hypothesis includes the glycinergic pathway. Because glycine is an additional excitatory neurotransmitter, efforts to identify glycinergic specific ligands that may be of therapeutic benefit to prevent, reduce, or ablate seizure activity in cortical tissue. A third hypothesis is the histamine receptor ligands and tachykinin receptor ligands may be useful for neuromodulation of excitatory neurotransmission. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of various drags or compounds. In Tables 1-6, 12-17 and 18-23, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with epilepsy based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of epilepsy include glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, purinergic, GABAergic, glycinergic, taurine, oxytocin, vasopressin, calcium, potassium, or sodium channels, mitochondrial maintenance, protein maturation and degradation, and second messenger cascade gene pathways that are listed in Tables 1-6, 12-17, 18-23. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of epilepsy, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drag response to therapies for epilepsy. Based upon these varying hypotheses there are many products in development for epilepsy. Table 29 below lists current therapies that have not yet received U.S. marketing approval. The listed candidate therapeutic interventions response in patients with epilepsy may be affected by polymoφhims in genes as described above. Example 14 Migraine I. Description of Migraine Migraine is a neurological syndrome that has multiple, complex manifestations. Migraine with auras, unilateral throbbing, and associated nausea is the basic clinical symptomatic presentation. The premonitory phase may be up to 24 hours and may be associated with auras or alterations of mood, appetite, visual, sensory, or motor functions. Migraine headache is a unilateral throbbing that is associated with photophobia, hypacusis, polyuria, and diarrhea. There are many clinical subtypes of migraine. Broadly, these subtypes can be distinguished by the presence or absence of auras. Migraines without auras are defined as the classic type. Migraines with auras can be further classified as 1) migraine with typical auras, 2) migraine with prolonged auras, 3) familial hemiplegic migraine, 4) basilar migraine, 5) migraine without headache, and 6) migraine with acute-onset aura. Additional migraine types include ophthalmologic migraine and retinal migraine. II. Current therapies for Migraine Migraine medical therapy depends on the acute or prophylactic nature of the therapy and whether the migraine is diagnosed as mild, moderate, or severe. Many patients will take a step approach to each separate migraine attack, starting with weakly acting agents and progressing to more potent drags. For patients with severe migraine, therapy includes prophylactic management. Therapy for Acute Migraine Mild migraine is a headache that may accompanied by nausea, is unilaterally throbbing, and can be treated by nonprescription analgesics. Patients infrequently consult a neurologist for care of mild migraines because the level of impairment imparted by the headache portion is not debilitating and is relatively short lived. Mild migraine is thus treated with aspirin, acetominophen, ibuprophen, indomethacin, naproxen sulfate, and in some cases antiemetic drugs (diphenhyrdamine, prochloφerazine, promethazine, and metchloφramide). Moderate migraine is generally characterized by similar symptoms of mild migraine, however the frequency and or severity are increased. Patients with moderate migraine are generally not relieved with non-narcotic analgesics, and require medications that combine aspirin or acetominophen with a mild sedative or α and β adrenergic receptor mediated vasoconstriction. Severe migraine is characterized by similar symptoms as mild and moderate migraine. However, the severity and frequency of headache is debilitating. Patients seek relief from the headache pain in the acute stage and frequently require prophylactic maintenance therapy. The drugs used for the therapy of acute migraine are members of the ergot alkaloid family or sumitriptan. The ergot alkaloids are partial agonists and antagonists for a variety of receptor types; serotoninergic, adrenergic, dopaminergic, muscarinic, and GABAergic. Synthetic products with similar chemical structures to ergotamine predominantly are agonists at the serotonin subtype ID or IB. Both of these two subtypes act by inhibiting adenylyl cyclase activity in cortical neurons. Ergotamine is also a vasoconstrictor; this activity is thought to occur through activation of the αl adrenergic receptor system. Ergotamine is metabolized by undefined pathways and metabolites are excreted primarily in the bile. The bioavailability of ergotamine is approximately 1%> due the potent first pass effect after parenteral delivery of the drag and enatic absoφtion between individuals. Sumitripan is another drug used for the acute, severe migraine attacks. Sumitripan is a serotonin IB, ID selective receptor agonist. Because these receptor subtypes are auto receptors, activation of 5HT1B and 5HT1D receptors can act by controlling the release of the serotonin and other neurotransmitter release. Sumitriptan may also be efficacious in the treatment of migraine because it may block proinflammatory receptors at the level of nerve terminal in the perivascular space. Other drugs used as adjunct therapy for acute, severe migraine attacks are corticosteroids and opioid analgesics. Due to their addictive qualities, opioid or narcotic analgesics are limited to acute, infrequent attacks. Prophylactic Therapy of Migraine There are currently six classes of standard treatments for the prophylactic therapy of migraine. They are 1) tricyclic antidepressants (amytriptylline), 2) 5HT antagonists (methylsergide), 3) β adrenergic receptor antagonists (propanolol, timolol, atenolol, metropolol, nadolol), 4) monoamine oxidase inhibitors (depranil), 5) calcium channel blockers (verapamil, flunarizine), and 6) anticonvulsants (divalproex sodium, chloφromazine). The criteria for the selection of prophylactic therapy are 1) patient has 6 or more headaches each month, 2) symptomatic medications are contraindicated or ineffective, 3) medication is necessary more than twice each week, and 4) there is an expressed need on the part of the patient to prevent infrequent attacks, e.g. hemiplegic migraine, those headaches producing profound disruption, or those associated with a risk of stroke. The ultimate choice of the prophylactic medication is based upon the measured effect on the type of migraine and the patient's willingness to withstand the associated side effects. III. Limitations of Current Therapies for Migraine The cunent therapy of migraine includes management of acute attacks of the mild, moderate and severe categories. Therapies of severe migraine further include prophylactic therapies. Regardless of the acute or prophylactic nature of the therapy, there are both efficacy and toxicity limitations in which migraine remains problematic for medical management. Toxicity or Undesired side effects of Acute Migraine Therapy Ergotamine and its derivatives are useful drags for the management of acute severe migraine attacks, however there are side effects associated with administration of the drug. Ergotamine is an activator of the CNS emetic centers, and nausea and vomiting are a frequent side effect that can be confused with a manifestation of the migraine attack. Other undesirable side effects are weakness of the legs, muscle pains, numbness and tingling of toes, and transient tachy- or bradycardia. A known side effect of sumitriptan is coronary vasospasm and it is thus contraindicated in patients with ischemic heart disease or Prinzmetal's angina. Limitations of Prophylactic Migraine Therapy Although prophylactic therapy for migraine can reduce the -frequency and intensity of the migraine attack, there are patients that achieve dramatic improvement and there are those that achieve only a 50%) reduction, indicating a limited efficacy and benefit for a significant population subgroup. In those patients, the severity and intensity must be significant to require daily prophylactic medication. Of the six categories of prophylactic agents all have associated side effects that may or may not be tolerable to each individual patient. They are 1) tricyclic antidepressants: sedation, dry mouth, weight gain, tremor, cardiac arrythmias, aggravation of angle-closure glaucoma, and difficulty in urinating; 2) 5HT antagonist: weight gain, muscle cramps, vasoconstriction, and retroperitoneal pleuroperitoneal and subendocaridal fibrosis; 3) β adrenergic receptor antagonists: aggravation of asthma, bradycardia, hypotension, fatigue, depression, masking the symtpoms of diabetes mellitus; 4) monoamine oxidase inhibitors: orthostatic hypotension, insomnia, and nausea; 5) calcium channel blockers: are not frequently used, however are associated with constipationa and orthostatic hypotension; and 6) anticonvulsants: nausea, fatigue, weight gain, alopecia, tremor, liver dysfunction, and neural tube defects in developing embryos. The least desired effect of prolonged prophylactic therapy of migraine is the associated increased frequency of headaches. Headaches, not of the migraine type, can occur daily and are related to rebound withdrawal from frequent use of the acute antimigraine medication. Patients experiencing this type of headache pattern are said to have transformed migraine and often experience episodic migraine attacks superimposed on their daily headaches. Ergotamines are frequently associated with chronic daily headaches, as are the triptans. Unfortunately, patients experiencing daily headaches are less likely to respond to acute therapy or any other preventative medications. Withdrawal of other migraine medications further render the patient more susceptible to daily headaches. Therefore, it is beneficial to prevent transformed migraine and chronic daily headaches. Drags known to be associated with transformed migraine are generally limited to occasional use in patients that have greater than two migraines each month. It is additionally recommended for patients that experience more frequent headaches requiring over-the-counter or prescription medications be put on a rotating schedule. IV. Impact of Pharmacogenomics on Drug Development for Migraine As described above, there is evidence to suggest that there are efficacy and safety different responses to drag therapy within the migraine patient population. Although not all of these responses may be attributable to genotypic differences, it is expected that if stratification based upon genotype were performed, a reasonable conelation between drag response and genotype may become obvious. As described below, there are gene pathways that are involved with cunent drug therapy and those that may be potentially involved in the future. As described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for migraine and patients diagnosed with migraine. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and matrix Table 7. Optimization of serontonergic, nonsteroidal antiinflammatory, or cerebral vasoconstrictor mediated mechanism of therapy of migraine further demonstrates the utility of selection of a potential migraine patient that has a predisposing genotype in which selective anitmigraine or agents may be more effective and or have an more desirable safety profile. In considering an optimization protocol, one could potentially predetermine variance or variances within the serotonergic receptor pathway, nonsteroidal aninflammatory pathway, or serotonergic receptor or nonsteroidal antiinflammatory mediated intracellular mechanism of action that is preeminently responsible for antimigraine drug response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drag development program for migraine. A sample of therapies approved or in development for preventing or treating the progression of migraine cunently known in the art is shown in Table 31. In this table, the candidate therapeutics were sorted and listed by mechamsm of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Pharmacogenomics studies for these drags, as well as other agents, drags, compounds or candidate therapeutic interventions, could be performed by identifying genes that are involved in the function of a drug including, but not limited to is absoφtion, distribution metabolism, or elimination , the interaction of the drag with its target as well as potential alternative targets, the response of the cell to the binding of a drag to a target, the metabolism (including synthesis, biodistribution or elimination) of natural compounds which may alter the activity of the drug by complementary, competitive or allosteric mechanisms that potentiate or limit the effect of the drag, and genes involved in the etiology of the disease that alter its response to a particular class of therapeutic agents. It will be recognized to those skilled in the art that this broadly includes proteins involved in pharmacokinetics as well as genes involved in pharmacodynamics. This also includes genes that encode proteins homologous to the proteins believed to carry out the above functions, which are also worth evaluation as they may carry out similar functions. Together the foregoing proteins constitute the candidate genes for affecting response of a patient to the therapeutic intervention. Using the methods described above, variances in these genes can be identified, and research and clinical studies can be performed to establish an association between a drag response or toxicity and specific variances. V. Description of Mechanism of Action Hypotheses for Future Migraine Drug Development The pathogenesis of migraine includes the following theories: vascular, depression of cortical electrical activity, serotonergic abnormalities, alteration of neurotransmitter modulation, and modulation of neuroendocrine mechanisms. These are described briefly below. The vascular theory of migraine posits that there is abnormal cerebral blood flow and it apparently plays a pivotal role in the clinical symptoms of migraine. Studies have shown that a decrease in cerebral blood flow during an aura and an increase in blood flow during headache occur in migraine patients. This theory is somewhat substantiated indirectly by the pharmacologic action of therapies for acute migraine and prophylaxis, as previously described. There have been additional studies that point to a mechanism of spreading depression of cortical electrical activity and a concunent alteration of blood flow. This theory suggests that focal reduction of electrical activity and concunent increase in blood flow occurs focally and spreads across the hemisphere at a rate of 2-3 mm each minute. This spreading hypothesis has been refined to a description of migraine as an evolving process in the cerebral cortex that occurs secondarily to decreased cortical function, decreased coritcal metabolism, and or vasoconstriction of cortical arterioles. Many studies have addressed the effect of serotonergic mechanism of the pathogenesis of migraine. These studies used the following premises: 1) there have been reports of decreased concentrations of serotonin in platelets and plasma, 2) increased levels of serotonin and serotonergic metabolites in urine, 3) lastly, migraine may be precipitated by abnormal release of biogenic amines, a theory bome out of the fact that reseφine and fenfluramine can precipitate a migraine attack. Other theories propose that alteration s of neurotransmitter systems e.g. nitric oxide, glutamate, and opioid receptors may be part of the pathogenesis of migraine. Further, Some studies have included anatomical differences in the raphe system and within the cerebral vasculature as well as alterations of the autonomic nervous system. Therapy of migraine is dependent on the appropriate diagnosis, as well as the type, frequency, and severity of the throbbing headache. Upon diagnosis, patient education to identify and avoid trigger factors is a critical first step in all patients. Trigger factors may include but are not exclusive to alcohol (red wine), foods (chocolate, certain cheeses), irregular sleep patterns, and acute changes in stress levels. Triggers may also come from environmental factors, such as time-zone shifts, high altitudes, or barometric changes. In women, menstrual cycles may trigger a migraine attack. These trigger factors suggest that there are complicating factors to include in any pathophysiologic hypothesis of migraine, and that these hypotheses may include neuroendocrine, endocrine, and other metabolic factors. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of various drags or compounds. In Tables -6, 12-17 and 18-23, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with epilepsy based upon genotype. Cunent pathways that may have involvement in the therapeutic benefit of migraine include glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, GABAergic, nitric oxide, peptide hormone processing, opiates, tachykinin, bradykinin, corticotropin releasing hormone, calcitonin calcitonin gene related peptide, calcium channel, hemostasis, and second messenger cascade gene pathways that are listed in Tables -6, 12-17 and 18-23. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of migraine, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drug response to therapies for migraine. Based upon these varying hypotheses as stated above, there are many products in development for migraine. Table 31 below lists current therapies that have not yet received U.S. marketing approval. Example 15 Psychosis Psychosis is a general term for major mental disorder characterized by loss of contact with reality, often manifested by disordered thought, delusions or hallucinations. Psychosis can be part of several distinct psychiatric diseases, including schizophrenia, manic-depressive disease, severe depression with psychotic features, organic psychotic disorders, as well as in alcohol or drug intoxication and acute idiopathic psychotic illnesses. The most common of these is schizophrenia. The antipsychotic drags are also used to treat non-psychiatric conditions such as, for example, nausea and vomiting, movement disorders associated with neurodenerative diseases such as Huntington's disease and Tourette's syndrome, pruritis and chronic hiccough. Example 11 focuses predominantly on schizophrenia, however similar analysis, in terms of the relevant pathways, genes, polymoφhisms and analytical methods for establishing relationships between polymoφhisms and drug responses, would obtain in all the other diseases treated with antipsychotic drags. Criteria for the diagnosis of schizophrenia and other psychoses, as well as diagnostic criteria for the other disorders treated with antipsychotics, are well established. (Diagnostic and Statistical Manual of Mental Disorders, 4th ed., American Psychiatric Association Press, Washington, D.C, 1994.) II. Cunent Medical Management of Schizophrenia Over 15 drugs are approved for treatment of psychosis in the US. They include the so-called conventional or typical antipsychotic drugs and the more recently introduced atypical antipsychotic drugs. The former class includes phenothiazines (e.g. chloφromazine, the first antipsychotic to be widely used), thioxanthenes (e.g. thiothixene), butyrophenones (e.g. haloperidol, one of the most useful conventional antipsychotics) and other heterocyclic compounds. The atypical antipsychotics include compounds such as clozaril (the first, and best studied member of the class), risperidone, olanzapine, quetiapine, ziprasidone and iloperidone. Some drags, such as loxapine, have pharmacology intermediate between that of the typical and atypical drugs. The typical antipsychotics are believed to act predominantly by antagonizing dopamine receptors, particularly D2-dopamine receptors. These medications can be effective in reducing the positive symptoms of schizophrenia (hallucinations, delusions) but are generally not effective at alleviating the negative symptoms (withdrawal, flat affect, anhedonia, lack of will), nor do they generally result in improved cognitive function. In fact, negative symptoms and cognitive function may worsen on typical antipsychotics. Typical antipsychotics exhibit dose dependent efficacy, and the optimal dose for a given patient must be determined empirically by gradually increasing the dose until adequate control of symptoms is achieved (without unacceptable side effects - see below). A therapeutic dose is usually reached within 2-3 weeks of initiating therapy. The atypical antipsychotic drugs have replaced the typical agents as front line therapy for schizophrenia and other psychoses because they have a beneficial impact on the negative symptoms as well as the positive symptoms of schizophrenia, and because, based on recent research, they may also improve cognitive function. The atypical drags affect a number of neurotransmitter systems, with modulation of serotonergic neurotransmission - particularly 5HT2C receptor antagonism, a prominent effect in addition to modulation of dopaminergic function.. The best studied of this class of drugs is clozapine, which binds dopamine receptors with low affinity, and also interacts with muscarinic, adrenergic, serotonergic, and histaminergic receptors. The table below depicts the relative receptor affinity (0-5 on a scale of 5, where 5 indicates a high affinity interaction) of a conventional drug (haloperidol) and an atypical drag (clozapine). Relative Receptor Affinities of Haloperidol and Clozapine The effectiveness of the atypical antipsychotic drags has revealed the inadequacy of a simplistic dopamine excess hypothesis of schizphrenia. The clinical effects of the atypical antipsychotic drags are likely to reflect the summation of a complex set of interactions with a variety of neurotransmitter receptors. Inteφatient differences in the function, levels or anatomical distribution of these different receptors are likely to account for a substantial fraction of inteφatient variation in response to atypical antipsychotic drags. Further, the function, levels and anatomical distribution of receptors is largely under genetic control, as is the associated biosynthetic, catabolic, recycling and signal transduction machinery. An understanding of the specific genetic variants that have major effects on drug efficacy would allow a far more sophisticated selection of appropriate therapy and dose than is possible cunently. III. Limitations of Current Therapies The chief limitations of antipsychotic medicines are (i) conventional and atypical neuroleptic agents do not reduce the signs and symptoms of schizophrenia in all patients (an estimated one third to one quarter of psychotic patients are resistant to therapy); (ii) a wide range of serious adverse effects. Further, it is impossible to predict the response of any given patient, particularly the mix of drug effects on positive symptoms, negative symptoms, cognitive deficits and side effects. As a result, selection of therapy is at present completely empirical. This approach is costly, as (i) multiple physician visits may be required before an optimal dose of an effective agent is attained; (ii) even after determining an effective drag regiment, the long term effects of therapy in specific patients generally remain unknown, particularly with respect to side effects; (iii) these problems result in low rates of compliance with therapy. Hence there is a need for tools that would allow the prospective identification of patients likely to be responsive to - and free from short or long term side effects from - a particular drug. Efficacy Limitations The dilemma confronting psychiatrists and other clinicians selecting therapy for psychotic patients has been described by Baldessarini in Goodman and Gi nan's The Pharmacological Basis of Therapeutics (9th edition) as follows: "No one drug or combination of drugs has a selective effect on a particular symptom complex in groups of psychotic patients; although individual patients may appear to do better with one agent than another, this can be determined only by trial and ernor". Thus, a clinician selecting therapy for a newly diagnosed psychotic patient, generally selects a compound with which he is comfortable, based on past experience. If that agent is not effective, or is producing a side effect, then a second agent is selected, again, entirely based on the physicians clinical judgement, and so on. This approach to optimization of pharmacotherapy has both medical and economic drawbacks. From the medical point of view, it does not always result in the selection of optimal treatment, with the attendant drawbacks in patient compliance. From an economic viewpoint the number of physician visits required to reach an effective dose of an effective drag are greater than necessary, and some patients may require hospitalization during the period when various drag regimens are being tested. There are other costs of using less than optimal therapy: (i) a patient might experience an improvement in cognitive symptoms on an optimal drag that would allow performance of a regular job; suboptimal therapy, even while adequately controlling positive symptoms, might not be sufficient to enable job performance, (ii) An optimal drug would minimize side effects, and thereby reduce physician visits, while also resulting in greater compliance. (Noncomphance is likely to ultimately lead to more hospitalization.)Determination of an optimal dose of an antipsychotic is another challenging aspect of therapy with these agents. Baldessarini (Goodman and Gilman, 9th ed.) writes: "Optimal dosage of antipsychotic drugs requires individualization to determine doses that are effective, well-tolerated, and accepted by a patient. Careful observation of the patients changing response is the best guide to dosage." As with selection of an optimal agent, discussed above, the determination of an optimal dose presently requires multiple physician visits. Clearly some fraction of inteφatient variation in optimal dose level is likely due to genetic, and consequent biochemical differences between patients. Such differences may involve drag metabolizing enzymes or proteins that mediate pharmacodynamic effects. A list of such proteins is provided in Tables 1-6. Many typical antipsychotic drags are metabolised by cytochrome P450 enzymes, with consequent wide inteφatient variation in pharmacokinetic parameters. Further, many antipsychotic drugs are converted to active metabolites which can have therapeutic effects or side effects. The metabolism of the tricyclic atypical drags (clozapine, olanzapine, and quetiapine) occurs via N+-oxidation, N-glucuronidation, and phases 1 and 2 metabolism with final glucuronidation before renal excretion. The non-tricyclic atypical antipsychotic drugs (e.g. risperidone, sertindole and ziprasidone) have diverse chemical structures and there is less data on their metabolism, but it appears to include diverse phase 1 biotransformation reactions. As a rale, conventional antipsychotics are mainly effective against positive symptoms (hallucinations, delusions, illusions), while not significantly ameliorating negative symptoms (withdrawal and flat affect). They are also associated with a high incidence of adverse effects, particularly extrapyramidal symptoms (EPS) and tardive dyskinesia. Atypical antipsychotics constitute a significant improvement, in that they are at least as effective as conventional drags against positive symptoms, they show at least some effectiveness against negative symptoms and, according to recent studies, they may also produce improvement in the cognitive deficits associated with schizophrenia (e.g. attention, executive function, short and long term memory), while causing substantially fewer extrapyramidal symptoms. Toxicity Limitations Unfortunately, conventional anti-psychotic drags are uniformly associated with undesirable dose-dependent side effects. These include (but are not limited to) extrapyramidal effects, electrocardiogram abnormalities, sedation, weight gain, cognitive deficits, sexual or reproductive dysfunction, blood dyscrasias (particularly agranulocytosis associated with clozapine), , neuroleptic malignant syndrome (parkinsonism with catatonia), jaundice, skin reactions, epithelial keratopathy andseizures. Skin reactions include uticaria and dermititis and are usually associated with phenothiazines. Epithelial keratopathy and comeal opacities are associated with chloφromazine therapy. In extreme cases these effects impair vision, but they tend to spontaneously disappear upon discontinuation of chloφromazine. The extrapyramidal side effects of conventional neuroleptics include dystonia (facial grimacing, torticollis, oculgyric crisis), akathesia (feeling of distress or discomfort leading to restlessness or constant movement), and parkinsonian syndrome (rigidity and tremor at rest, flat facial expression). Tardive dyskinesia is a common side effect of long term usage of conventional neuroleptic drugs.Tardive dyskinesia is a syndrome of abnormal involuntary repetitive, painless movements. These movements vary in intensity over time, dependent on the level of arousal or emotional distress. Typically there are quick choreiform (ticlike) movements of the face, eyelids (blinks or spasms), mouth (grimaces), tongue, extremities, or trunk. Increasing the dose of the conventional neuroleptic agent can reverse extrapyramidal effectsshort term, but at the cost of more severe dyskinesia long term. Not infrequently a clinician is compelled to change medication for a patient with adequately controlled schizophrenia because of dose related tardive dyskinesia or other extrapyramidal side effects.. Another important side effect of many antipsychotic drags is QT wave prolongation, which has recently resulted in the withdrawal of an atypical antipsychotic compound. Cardiac conduction abnormalities associated with antipsychotic therapy have resulted in patient deaths, presumably as a consequence of ventricular tachycardias. The mechanism of the conduction abnormalities appears to involve drag binding to cardiac potassium channels and consequent interference with repolarization cunent. Sertindole, for example, is a new antipsychotic agent that binds with high affinity (3-14 nM, depending on conditions) to and antagonizes HERG, a cardiac potassium channel. The degree of inteφatient variation in these effects is not well characterized. Genes likely to account for these differences encode potassium channels (which may also have some role in the central actions of these compounds), sodium channels and the genes associated with inherited forms of long QT wave syndrome (QT1, QT2, QT3, QT4, QT5 and QT6). Yet another important side effect of antipsychotic drags is weight gain which can lead to obesity. IV. Impact of Genotyping on Drug Development for Schizophrenia Most traditional neuroleptics have a narrow therapeutic-to-toxic index, and thus, the novel antipsychotics are the result of a search to substantially widen the distance between the dose that treats psychosis and the one that produces adverse effects. In vitro binding profiles have been created for the atypical antipsychotics that have been approved by the U.S. Food and Drag Administration (FDA)- clozapine, olanzapine, and risperidone and those that are under FDA review- quetiapine and sertindole. These profiles, which were compared with that of the typical neuroleptic haloperidol, provide guidance for predicting the adverse effects produced by these drags. Most conventional antipsychotics have central nervous system effects, particularly extrapyramidal symptoms (EPS) and tardive dyskinesia, sedation, and dulling of cognition. Other adverse effects of the typical antipsychotics include the neuroleptic malignant syndrome, orthostatic hypotension, changes in liver function, anticholinergic and antiadrenergic side effects, sexual dysfunction, and weight gain. The newer agents have a lower incidence of EPS and tardive dyskinesia, while weight gain and changes in blood pressure and liver function tests are adverse effects that have been associated with the use of the newer agents. The favorable side effect profile of these new antipsychotics is likely to make patients more willing to continue treatment, and thus these agents represent a step forward in the treatment of patients with severe, chronic mental illness. This paper reviews the cunent literature describing the metabolism of both multi-receptor clozapine analogue atypical antipsychotic drags (clozapine, olanzapine, and quetiapine) and serotonin-dop amine antagonist atypical antipsychotic drags (risperidone, sertindole and ziprasidone), to highlight the significance of those data in the context of clinical practice. The former group of atypical antipsychotic drags shares a similar tricyclic structural nucleus and are metabolized through three major categorical metabolic pathways~N+-oxidation, N- glucuronidation, and phases 1 and 2 biotransformation with final glucuronidation before renal excretion. There have been reports of polymoφhisms in key genes that affect neuroleptic activity in schizophrenic patients. For example, within the dopamine D4 receptor subtype, there are known tandem repeats in exon 3. In a recent study, schizophrenic patients on maintenance doses of chloφromazine were stratified into two groups, one having 2 tandem base pair repeats and the other having 4 tandem base pair repeats. Thirty- four percent of group one patients and 62%> of group two patients had a favorable response to chloφromazine therapy during acute stage treatments. The presence of homogeneous four 48 base pair repeats in both alleles in exon 3 of the dopamine D4 receptor subtype thus appears to be associated with beneficial chloφromazine response. Recently, a study of the serotonin receptor subtype 6, polymoφhism (T267T vs. C267T) in a group of patients refractory to clozapine therapy was reported. In this study, it appeared that the T267T genotype patients were more likely to respond to continued therapy that those patients with C267T genotype patients. A recent report documented a conelation of the serotonin 5HTC2 receptor subtype biallelic polymoφhism and neuroleptic efficacy. A significant number of schizophrenic patients homozygous for the allele C2 who responded unsatisfactorily to antipsychotic medication as compared to control. Three polymoφhisms in the serotonergic receptors, i.e. 5HT2A (T102C); 5HT2C (cys23ser); and 5HT2A (his452tyr) have reports of positive or negative conelation with efficacy of antipsychotic therapies. This disparity in the literature will, in the future, be further examined in schizophrenic patient populations and conelation may be discovered. The evidence that a variance in a gene involved in a pathway that affects neuroleptic drag response, indicates and supports the theory that there is a likelihood that other genes have similar qualities to various degrees. As drag research and development proceeds to identify more lead candidate therapeutic interventions for schizophrenia, there is possible utility in stratifying patients based upon their genotype for these yet to be conelated variances. Further, as described in the Detailed Description, methods for the identification of candidate genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease is easily translated for schizophrenia. As described below in section V. below there are likely gene pathways as are those that are outlined in the gene pathway Table 2 and matrix table 7. Identification of pathophysiologic relevant variance or variances and potential therapies affecting those allelic genotypes or haplotypes will speed the drug development. There is a need for therapies that are targeted to the disease and symptom management with limited or no undesirable side effects. Identification of a specific variance or variances within genes involved in the pathophysiologic manifestation of schizophrenia and specific genetic polymoφhisms of these critical genes may assist the development of novel neuroleptic agents and the identification of those patients that may best benefit from therapy of these candidate therapeutic alternatives. By identifying allelic variances or haplotypes in genes that indirectly affects efficacy, safety or both one could target specific secondary drug or agent therapeutic actions that affect the overall therapeutic action of conventional, atypical, or novel neuroleptic action. A sample of therapies approved or in development for preventing or treating the progression of symptoms of schizophrenia cunently known in the art is shown in Table 35. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. V. Mechanism of Action Hypotheses for Novel Therapies for Schizophrenia: Utility of Genotyping The underlying etiology of schizophrenia is not established, however there is compelling evidence that modulation of several neurotransmitter systems has an impact on the disease. As discussed above, conventional anti-psychotic drugs, effective in the management of schizophrenia, are dopamine antagonists, specifically D2-receptor antagonists, which block dopaminergic neurotransmission in the forebrain. Additionally, drags such as mescaline and amphetamines, which are known to stimulate dopaminergic pathways, have been shown to induce psychotic symptoms. Evidence of dysfunctional serotonergic neurotransmission in schizophrenia includes evidence of altered serotonin receptor density, altered serotonin metabolism, and the evidence that serotonin receptors appear to be important targets for the atypical neuroleptics. Based on cunent knowledge, there are three hypotheses that underscore the utility of polymoφhic genotype analysis within the schizophrenic population. In the first, it could be considered that endogenous dopamine levels and consequential dopaminergic tone varies among schizophrenic patients, affecting response to receptor antagonists. These genetic DNA variations may affect brain neurotransmitter modulation of dopaminergic transmission and dopaminergic receptor mediated intracellular mechanisms among schizophrenic patients. In the second hypothesis, genetic DNA variations may affect the level of expression and brain distribution of dopamine receptors, imparting a variation in drag response among schizophrenia patients. Further, consideration of other endogenous neurotransmitters, i.e. serotonin, levels and consequential endogenous neurotransmitter tone varies among schizophrenic patients, affecting response to neurotransmitter receptor ligands or neurotransmitter receptor mediated intracellular mechanisms. Further, there may be genes within pathways that are either involved in metabolism of neurotransmitters or are involved in metabolism of various drags or compounds. In Tablesl-6, 12-17, and 18-23, there are listings of candidate genes and specific single nucleotide polymoφhisms that may be critical for the identification and stratification of a patient population diagnosed with epilepsy based upon genotype. Current pathways that may have involvement in the therapeutic benefit of schizophrenia include glutaminergic, serontonergic, dopaminergic, adrenergic, cholinergic, histaminergic, GABAergic, glycinergic, opiates, cholecystokinin, neurotensin, tachykinin, calcium channels, and second messenger cascade gene pathways that are listed in Tables 1-6, 12-17, and 18-23. One skilled in the art would be able to identify these pathway specific gene or genes that may be involved in the manifestation of schizophrenia, are likely candidate targets for novel therapeutic approaches, or are involved in mediating patient population differences in drag response to therapies for schizophrenia. Example 16 Effect of Pharmacokinetic parameters on Efficacy of Drags and Candidate Therapeutic Interventions The efficacy of a compound is determined by a combination of pharmacodynamic and pharmacokinetic effects. Both types of effect are under genetic control. In the present invention, the genetic determinants of efficacy are discussed in terms of variation in the genes that encode proteins responsible for absoφtion, distribution, metabolism, and excretion of compounds, i.e. pharmacokinetic parameters. The pharmacokinetic parameters with potential effects on efficacy include absoφtion, distribution, metabolism, and excretion. These parameters affect efficacy broadly by controlling the availability of a compound at the site(s) of action. Inteφatient variability in the availability of a compound can result in undertreatment or overtreatment, or in adverse reactions due to levels of a compound or its metabolite(s). Differences in the genes responsible for pharmacokinetic variation, therefore, can be a potential source of inteφatient variability in drag response. Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions that may Efficacy Clozapine induced agranulocytosis has been associated in some reports with specific HLA haplotypes or with HSP70 variants. These reports suggest that a gene within the HLA region is associated with agranulocytosis in response to clozapine therapy. In a recent study, two ethnic groups were analyzed for genetic markers for agranulocytosis. Tumor necrosis factor microsatellites d3 and b4 were found in higher frequencies in patients that experience clozapine-induced agranulocytosis. These data, while they need to be confirmed by additional studies, are suggestive that tumor necrosis factor polymoφhisms may also be associated with clozapine- induced agranulocytosis. In this invention we provide additional genes and gene sequence variances that may account for variability in toxic reponses. The Detailed Description above demonstrates how identification of a candidate gene or genes (e.g. gene pathways), genetic stratification, clinical trial design, and diagnostic genotyping can lead to improved medical management of a disease and/or approval of a drag, or broader use of an already approved drug. Gene pathways including, but not limited to, those that are outlined in the gene pathway, Tables 1-6, preferably Table 3, are useful in identifying the sources of inteφatient variation in efficacy as well as in the adverse events summarized in the column headings of Table 8. Discussed in detail below are exemplary candidate genes for the analysis of pharmacokinetic variability in clinical development, using the methods described above. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents: Impact on Efficacy As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in absoφtion and distribution, phase I and phase II metabolism, and excretion the optimization of therapy of by an agent known to have an efficacious effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Example 17 Drag-Induced Toxicity: Blood Dyscrasias I. Description of Blood Dyscrasias Blood dyscrasias are a feature of over half of all drag-related deaths and include, but are not limited to, bone manow aplasia, granulocytopenia, aplastic anemia, leukopenia, lymphoid hypeφlasia, hemolytic anemia, and thrombocytopenia. All of these syndromes include pancytopenia to some degree. Bone marrow aplasia- is defined as a profound loss of bone marrow resulting in pancytopenia. Drags known to cause bone marrow aplasia include, but are not limited to, chloramphemicol, gold salts, mephenytoin, penicillamine, phenylbutazone, and trimethadione. In general these drags are not first line therapy due to the rare occurance of manow aplasia. Specific forms of aplasia include: Granulocytopenia- is defined as a loss of polymoφhonuclear neutrophils to a count lower than 500. Granulocytopenia primarily predisposes the patient to bacterial and fungal infections. Drugs known to cause granulocytopenia include, but are not limited to, captopril, cephalosporins, choral hydrate, chloφropamide, penicillins, phenothiazines, phenylbutazone, phenytoin, procainamide, propranolol, and tolbutamide. Aplastic anemia- is a disorder involving an inability of the hematologic cells to regenerate and thus there is a dramatic depletion of one or more of the following cell types: neutrophils, platelets, or reticulocytes. Drugs associated with producing aplastic anemia are: 1) agents or compounds that produce bone marrow depression, for example cytotoxic drags used in cancer chemotherapy; 2) agents or compounds that frequently, but inevitably, produce manow aplasia, for example benzene; 3) agents or compounds that are associated with aplastic anemia, for example chloramphenicol, antiprotozoals, and sulfonamides. Aplastic anemia is almost always a result of damage to the hematopoietic stem cells. There are two possible routes for the destruction of these cells: 1) direct damage to the stem cell DNA, and 2) cell cycle dependant depletion of later stage progenitor cells. In the first case, drugs or agents bind to and randomly damage the genetic material. This type of aplasia is associated with both early aplasia (immediate or direct cytotoxcity) or later myelodysplasia and leukemia. In the latter case, mitotically and metabohcally active progenitor cells are preferentially affected and progenitor cell depletion may lead to unregulated proliferation of spared stem cells. Leukopenia- is defined when the circulating peripheral white cell count falls below 5-10 x 10 9 cells per liter. Circulating leukocytes consist of neutrophils, monocytes, basophils, eosinophils, and lymphocytes. Neutropenia is defined when the peripheral neutrophil count falls below 2 X 10 9 cells per liter. There are a number of drags families that can cause neutropenia including, but not exclusive to, antiarrythmics (procainamide, propanolol, quinidine), antibiotics (chloramphenicol, penicillins, sulfonamides, trimethoφim- methoxazole, para-aminosalicyclic acid, rifampin, vancomycin, isoniazid, nitrofurantoin), anti-malarials (dapsone, qunine, pyrimethamine), anticonvulsants ( phenytoin, mephenytoin, trimethadione, ethosuximide, carbamazepine), hypoglycemic agents (tolbutamide, chloφropamide), antihistamines (cimetadine, brompheniramine, tripelennamine), antihypertensives (methydopa, captopril), antiinflammatory agents (aminopyrine, phenylbutazone, gold salts, ibuprofen, indomethacin), diuretics (acetazolamide, hydrochlorothiazide, chlorthalidone), phenothiazines (chloφormazine, promazine, prochloφerazine), antimetabolite immunosuppresive agents, cytotoxic agents (alkylating agents, antimetabolites, anthracyclines, vinca alkyloids, cis-platinum, hydroxyurea, actinomycin D), and other agents (alpha and gamma interferon, allopurinol, ethanol, levamisole, penicillamine). Lymphoid hyperplasia- is characterized by reactive changes within the T-cell regions of the lymph node that encroach on, and at times appear to efface, the germinal follicles. In these regions, the T-cells undergo progressive transformation to immunoblasts. These reactions are encountered particularly in response to drag- induced immunoreactivity. Drags known to cause lymphoid hypeφlasia are phenytoin, and mephenytoin. Hemolytic anemia- is characterized by the premature destruction of red cells, accumulation of hemoglobin metabolic by-products, and a marked increase in erythroporesis within the bone manow. Drags know to cause hemolytic anemia include, but are not excluded to, methyldopa, penicillin, sulfonamides, and vitamin E deficiency. Thrombocytopenia- is characterized by a marked reduction in the number of circulating platelets to a level below 100,000/mm 3 . Drag-induced thrombocytopenia may result from decreased production of platelets or decreased platelet survival or both. Drugs known to cause thrombocytopenia include, but are not excluded to, ethanol, acetominophen, acetazolamide, acetylsalicyclic acid, 5-aminosalicylic acid, carbamazepine, chloφheniramine, cimetadine, digitoxin, diltiazem, ethychlorynol, gold salts, heparin, hydantoins, isoniazid, levodopa, meprobamate, methyldopa, penicillamine, phenylbutazone, procainamide, quinidine, quinine, ranitidine, Rauwolfa alkaloids, rifampin, sulfonamides, sulfonylureas, cytotoxic drugs, and thiazide diuretics. II. Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions that may Induce Blood Dyscrasias Clozapine induced agranulocytosis is associated with differing HLA types and HSP70 variants in patients for whom responded to clozapine therapy but developed agranulocytosis. This is suggestive that a gene within the MHC region is associated with the manifestation of agranulocytosis in response to clozapine therapy. In a recent study, two ethnic groups were analyzed for genetic markers for the agranulocytosis. Tumor necrosis factor microsattelites d3 and b4 were found in higher frequencies in patients that experience clozapine-induced agranulocytosis. These data are suggestive that there is an involvement of tumor necrosis factor constellation polymoφhism and clozapine-induced agranulocytosis. There is evidence to suggest that there are safety response differences to drag therapy in reference to development of blood dyscrasias which may be attributable to genotypic differences between individuals. There is provided in this invention examples of gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this disorder, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1-6, preferably Table 3, and pathway matrix Table 8 and discussed below are candidates for the genetic analysis and product development using the methods described above. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause Blood Dyscrasias As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drag transport, phase I and phase II metabolism, protection from reactive intermediate damage, and immune responsiveness the optimization of therapy of by an agent known to have a blood dyscrasia side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drug development program. Example 18 Drug-Induced Toxicity: Cutaneous Toxicity Drug-induced cutaneous toxicity includes, but is not excluded to, eczematous: photodermititis (phototoxic and photoallergic), exfoliative dermititis; maculopapular eruption; papulosquamous reactions: psoriaform, lichus planus, or pityriasis rosea-like; vesiculobullous reactions; txic epidermal necrolysis; pustular- acneform reactions; urticaria and erythemas: urticaria, erythema multiforme; nodular lesions: erythema nodosum, vasiculitis reaction; telangiectatic and LE reactions; pigementary reaction; other cutaneous reactions: fixed drag reactions, alopecia, hypertrichosis, macules, papules, angioedema, morbilliform-maculopapular rash, toxic epidermal necrolysis, erythema multiforme, erythema nodosum, contact dermititis, vesicles, petechiae, exfolliative dermititis, fixed drag eruptions, and severe skin rash (Stevens- Johnson syndrome). Drags known to be associated with cutaneous toxicities include, but are not exclusive of, antineoplastic agents, sulfonamides, hydantoins and others listed for each type of toxicity. Uticaria and angioedema- is defined as the transient apprearance of elevated, erythematous pruitic wheals (hives) or seφiginous exanthem. The apprearance of uticaria is percieved as ongoing immediate hypersensitivity reaction. Angioedema is defined as uticaria, but involving deeper dermal and subdermal sites. Uticaria and angioedema appear to result from dilation of local postcapillary venules. Degranulation of cutaneous mast cells may be involved. Drugs associated with uticaria and angioedema include, but are not excluded to, antimicrobials include, but not exclusive of, 5-aminosalicylic acid, aminoglycosides, cephalosporins, ethambutol, isoniazid, metronidazole, miconazole, nalidixic acid, penicillins, quinine, rifampin, spectinomycin, sulfonamides, and other drugs: asparaginase, aspirin and other non-steroidal antiinflammatory agenets, calcitonin, chloral hydrate, chlorambucil, cimetidine, cyclophosphamide, daunorubicin, ergotamine, ethchlorvynol, doxorubicin, ethosuximide, ethylenediamine, glucocorticoids, melphalan, penicillamine, phenothiazines, procainamide, procarbazine, quinidine, tartazine, thiazide diuretics, thiotepa. Morbilliform-maculopapular rash- are rashes that result in eruptions or are morbilliform in nature. Drugs associated with rashes include, but are not limited to, 5- aminosalicyclic acid, cephalosporins, erythromycin, gentamicin, penicillins, streptomycin, sulfonamides, allopurinol, barbiturates, captopril, coumarin, gold salts, hydantoins, thiazide diuretics. Toxic epidermal necrolysis and erythroderma and exfoliative dermititis- Cutaneous erythroderma, edema, scaling, and fissuring may occur in response to certain drugs. Drags associated with these types of cutaneous reactions include, but are limited to, allopurinol, amikacin, captopril, carbamazepine, chloral hydrate, chlorambucil, chloroquine, chloφromazine, cyclosporine, diltiazem, ethambutol, ethylenediamine, glutethimide, gold salts, griseofulvin, hydantoins, hydroxychloroquine, minoxidil, nifedipine, nonsteroid antiinflammatory agents, penicillin, phenobarbital, rifampin, spironolactone, sulfonamides, trimethadione, trimethoprim, tocainamide, tocainide, vancomycin, veφamil. Erythema mutliforme- is characterized by a hypersensitivity reaction in blood vessels of the dermis. The hypersensitivity is the result of immune complexes formed by small molecules interacting with proteinaceous components of the blood vessels. In cases whereby the mucosal membranes of the mouth and eye are involved, is referred to as Stevens-Johnson syndrome. Typically the cutaneous lesions, blisters and painful erosions occur in the mout and eye. Drags associated with erythema mulitforme include, but are not limited to, allopurinol, acetominophen, amikacin, barbiturates, carbamazepine, chloroquine, chloφoramide, clindamycin, ethambutol, ethosuximide, gold salts, glucocorticoids, hydantoins, hydralazine, hydroxyurea, mechlorethamine, meclofenamate, penicillins, phenothiazides, phenophthalein, phenylbutazone, rifampin, streptomycin, sulfonamides, sulfonylureas, sulindac, vaccines. Fixed drug eruptions- Drug associated with fixed drag eruptions include, but are not excluded to, acetominophen, 5-aminosalicyclic acid, aspirin, barbiturates, benzodiazepines, barbiturates, chloroquine, dapsone, dimethylhydrinate, gold salts, hydralazine, hyoscine, ibuprofen, iodides, meprobamate, methanamine, metronidazole, penicillins, phenobarbital, phenolphthalein, phenothiazides, phenylbutazone, procarbazine, pseudoephedrine, quinine, saccharin, streptomycin, sulfonamides, and tetracyclines. Erythema nodosum- is an innflammatory reaction in subcutaneous fat which represents a hypersentivity reaction to a number of antigenic stimuli. Multiple red, painful nodules do not ulcerate but involute and leave a yeloow-puφle braises. Small molecules intreracting with proteinaceous components forma asenstitizing antigen. Drugs associated with producing erythema nododum include, but are not excluded to, bromides, oral contraceptives, penicillins, and sulfonamides. Contact dermititis- is characterized by eruptions on histological analysis to epidermal intercellular edema (spongiosis). Contact dermititis can be caused by allergic or irritant mechanisms. Allergic contact dermititis is a delayed hypersensitivity reaction that can occur in response to a variety of small molecules that when bound to proteinaceous components of the skin form a sensitizing antigen. The antigen is processed by Langerhans' cells in the epidermis, presenting the antigen to the circulating T lymphocytes. Irritant dermititis is produced by substances that irritate or have a direct toxic effect on the skin. Drugs associated with contact dermititis side effects include, but are not limited to, ambroxol, amikacin, antihistamines, bacitracin, benzalkonium chloride, benzocaine, benzyl chloride, cetl alcohol, chloramphenicol, chloφormazine, clioquinol, colophony, ethylenediamine, fluorouracil, formaldehyde, gentamycin, glucocorticoids, glutaraldehyde, heparin, hexachlorophene, iodochlorhydroxyquin, lanolin, local anesthestics, minoxidil, naftin, neimycin, nitrofurazone, opiates, para- aminobenzoic acid, parabens, penicillins, phenothiazines, prolflavine, propylene glycol, streptomycin, sulfonamides, thimerosal, timolol. Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions that May Induce Cutaneous Reactions Recently, it has been decribed that there is a deletion polymoφhism in the B2 bradykinin receptor gene (B2BKR). It was revealed that there is a 9 base pair deletion in exon 1 of the B2BKR gene and upon inspection of patients experienceing angioedema, patients with immunochemical evidence of angioedema were homozygous for no deletion at that site. These results were suggestive of B2BKR genotype influence on the clinical status and manifestation angioedema. There is evidence to suggest that there are safety response differences to drag therapy in reference to development of cutaneous reactions which may be attributable to genotypic differences between individuals. There is provided in this invention examples of gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this disorder, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1-6, more preferably Table 3, and pathway matrix Table 8 and discussed below are candidates for the genetic analysis and product development using the methods described above. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause Cutaneous Reactions As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drag transport, phase I and phase II metabolism, protection from reactive intermediate damage, and immune responsiveness, the optimization of therapy of by an agent known to have a cutaneous side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Example 19 Drug-Induced CNS Toxicity Drag-induced central nervous system toxicity includes CNS stimulation or CNS depression. Characteristics of CNS toxicity include, but are not limited to, tinnitus and dizziness, acute dystonic reactions, parkinsonian syndrome, coma, convulsions, depression and psychosis, sweating, mydriasis, hypeφyrexia, centrally mediated cardiovascular involvement (hypertension, tachycardia, extrasystoles, arrythmias, circulatory collapse) and respiratory depression or tachypnea. Drags known to be associated with CNS toxicity include, but are not exclusive of, salicylates, antipsychotics, sedatives, cholinergics, Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions that May Induce CNS Toxicity There is evidence to suggest that there are safety response differences to drug therapy in reference to development of CNS toxicities which may be attributable to genotypic differences between individuals. There is provided in this invention examples of gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this undesirable adverse effect, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1-6, more preferably Table 3, and pathway matrix Table 8 and discussed below are candidates for the genetic analysis and product development using the methods described above. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause CNS Toxicities As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drug transport, phase I and phase II metabolism, protection from reactive intermediate damage, the optimization of therapy of by an agent known to inpart CNS toxic or undesirable side effect or effects by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drug development program. Example 20 Drug-Induced Liver Toxicity Drag-induced liver disease or drag-induced liver toxicity can manifest as zonal necrosis, nonspecific focal hepatitis, viral hepatitis-like reactions, inflammatory or noninflammatory cholestasis, small or large droplet fatty liver, granulomas, chronic hepatitis, fibrosis, tumors, or vascular lesions. In the majority of the cases of known drug-induced liver toxicity, the drug is metabolized to a form that is deleterious to hepatic, or extrahepatic function. There are many endogenous or exogenous compounds that may be considered to attenuate or ablate toxic hepatocyte-produced metabolite mechanisms or effects of hepatic or extrahepatic damage. In hepatocellular damage, free oxygen radicals may be generated in the hepatic metabolic processes that are deleterious to intracellular organelles, DNA, or metabolic pathways. There are endogenous cytoprotective agents that may prevent free radical-mediated damage such as retinoids, flavins, reduced glutathione, vitamin E, S-adenylylmethionine, and the enzyme superoxide dismutase (SOD). In animal models in which SOD activity is diminished or absent, the liver function was normal, but the sensitivity to toxin challenge was heightened. In cholestatic damage, the bile salt uptake, metabolism, secretion, or transport is compromised and the residual increased bile salt concentrations are deleterious to hepatocyte function. The increase in bile salts is the main metabolic disturbance that initially leads to jaundice and pruritis and can progress to pancreatitis, hyperbilirabinemia, biliary cinhosis, and hepatic encephalopathy. In both cases of drag-induced liver toxicity, the drag must first be absorbed and enter in the hepatic circulation. Further, clinically it is often difficult to determine whether cholestatic damage leads to hepatocellular damage or whether hepatocellular damage leads to cholestatic damage. In many cases, until the patient is symptomatic, the underlying damage mechanisms may be clinically overlooked. By the time the drag-induced liver disease is symptomatic, the damage, be it hepatocellular or cholestatic or both, may be ineversible. Identification of Genes involved in Drug-Induced Liver Toxicity Thus, in the process of identifying drag- or xenobiotic-induced liver toxicity, one skilled in the art would identify key metabolic enzymes or bile cannicula transport processes that would be linked with either hepatocellular damage or cholestasis or combination of hepatocellular damage or cholestasis. Hepatocellular damage may be the result of direct chemical mediated effects, may be severe, and usually is associated with damage within organelles, DNA and membranes. Clinically there is a marked elevation of SGOT and SGPT as well as other enzymes. In cases of cholestasis there is jaundice, pruritis, a marked elevation of bile salts and alkaline phosphatase activity, but not an elevation of SGOT or SGPT. In cases of toxic liver disease there is difficulty, at least initially to determine the underlying etiology. Clinically, symptoms may not appear as clear as described above. Further, depending on the rate and extent of the damage, hepatocellular damage may be masked or asymptomatic until liver impairment has induced cholestasis. Potentially hepatotoxic agents can be divided broadly into two groups: intrinsic hepatotoxins and idiosyncratic hepatotoxins. Intrinsic hepatotoxins produce acute liver damage in a predictable, dose-dependent fashion shortly after ingestion or exposure. Generally, all subjects exposed will uniformly exhibit signs and symptoms. In this category, the effects seen in humans can be mimicked in animal models. Examples of intrinsic hepatotoxins are carbon tetrachloride, 2-nitropropane, trichloroethane, the octapeptide toxins of the Amanita mushroom species, and the antipyretic, acetominophen. In some of these cases, toxic metabolites result in covalent modification of hepatocyte macromolecules or reactive oxygen intermediates leads to peroxidation of cell membrane lipids or other intracellular molecules. In contrast, idiosyncratic hepatotoxins produce liver damage in an unpredictable, dose-independent manner after a latent period of ingestion or exposure. Animal models or experimental data is generally incapable of predicting the effect in humans. Further, idiosyncratic hepatotoxins do not uniformly affect a population; a subset of the group exposed may or may not exhibit signs or symptoms. Range of symptoms are from mild to severe and is thought to coincide with differences in the pathways of drag or xenobiotic biotransformation or immune-mediated drag sensitivity (drug allergy). In idiosyncratic drag-induced liver disease, fever, arthralgias, rash, eosinophilia, are often prominent and indicate a hypersensitivity reaction. Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions that may Induce Hepatotoxicity Genes encoding proteins with catalytic function that are involved in the metabolism of drags or xenobiotics are listed in Tables 3 and 8 below. Further listed are those proteins that are involved in the uptake, transport, or secretion into the bile cannicula. Below are further specific example of drug-specific effects on the liver. Acetaminophen-Induced Liver Disease Acetominophen is a readily available, easy to administer analgesic that is an example of a intrinsic hepatotoxin. This hepatotoxin causes zonal necrosis and acute liver failure and is associated with renal failure. Although a high dose (10-15 grams) is required for significant liver injury to occur, the onset of initial symptoms does not occur until hours after ingestion. The progression of symptoms occurs including progressive liver failure with hepatic encephalopathy, prolongation of prothrombin time, hypoglycemia, and lactic acidosis. The liver injury is caused by a toxic metabolite of acetominophen via the P450 metabolizing system. This toxic intermediate at low concentrations is conjugated with glutathione. However, in toxic doses, the conjugating enzymes stores are exhausted and the reactive intermediate reacts with intracellular proteins and results in cellular dysfunction and ultimately death. The rate of metabolism is dependent on the concentrations of both P450 and glutathione. Speeding this toxic pathway may include increasing the available P450 or reducing the availablility of glutathione, e.g. using known inducers of P450 such as ethanol and and phenobarbital; and known inhibitors of glutathione concentrations, e.g., ethanol and fasting. Acetominophen toxicity is completely reversed if the drug is removed. Chronic ingestion may produce subclinical liver injury, centrilobular necrosis, or chronic hepatitis; however all reversible if the drag is removed. Amiodarone-Induced Liver Disease Amiodarone is used in treatment of refractory arrythmias. In some patients amiodarone produces mild to moderate increases of serum transaminases which are generally accompanied by engorgement of lysosomes with phospho lipid. In a fraction of the patients, a more severe liver injury develops which histologically resembles alcoholic hepatitis: fat infiltration of hepatocytes, focal necrosis, fibrosis, polymoφhonuclear leukocyte infiltrates, and Mallory bodies. The lesion may progress to micronodular cinhosis, with portal hypertension and liver failure. Hepatomegaly is seen, but jaundice is rare. Amiodarone accumulates in lysosomes and inhibits lysosomal phopholipases, however the connection between this mechanism and alcoholic hepatitis histopathology is unknown. Unfortunately, rapid discontinuation of amiodarone increases the risk of cardiac arrythmias. Chlopromazine-Induced Liver Disease Chloφromazine is an anti-psychotic agent which, in a small portion of the patient population can produce a cholestatic reaction. Symptoms include fever, anorexia, arthalgias, pruritis, jaundice, and eosinophilia is common. This idiosyncratic type of liver toxicity suggests a hypersensitivity type reaction. The symptoms subside over a period of weeks following discontinuation, Rarely, residual cholestatic disease occurs, treatment for pruritis and fat-soluble vitamin supplementation may be required, but eventual recovery almost always occurs. Erythromycin-Induced Liver Disease Erythromycin, a broad spectrum antibiotic, can be accompanied by a cholestatic reaction. Inflammatory cell infiltration and liver cell necrosis may occur. The hepatoptoxicity presents as right upper quadrant pain, fever, and variable cholestatic symptoms. The prognosis is uniform and will occur after readminstration of the drag, The mechanism of action is unknown. Halothane-Induced Liver Disease Halothane is a gaseous anthesthetic and can, in rare instances, cause a viral- like hepatitis syndrome. In severe cases, this hepatotoxicity, may cause fatal massive heaptic necrosis. Severe reactions seem to appear after previous or multiple exposure to halothane. It is known that the P450 metabolites of this xenobiotic are responsible for the mechanism of hepatic injury. Isoniazid (INH)-Induced Liver Disease Isoniazid is used as a single drag in the prophylaxis of tuberculosis. In 10- 20%) of of the persons taking INH, subclinical liver injury occurs. The conversion of INH to acetylhydrazine is via acetylation. In slow acetylators, INH is more hepatotoxic. The conversion of INH to acetylhydrazine to diacetylhydrazine is impaired. In slow acetylators, the acetylhydrazine is not well metabolized and is further oxidized by one of the P450 enzymes to a toxic, reactive molecule that is responsible for the liver disease. Discontinuation of the drug returns the enzymatic levels to normal and the liver is able to restore activity. Sodium Valproate-Induced Liver Disease Sodium valproate is an anti-epileptic agent that is routinely prescribed for petit mal epilepsy and in some cases produces severe hepatotoxicity. Similar to INH, sodium valproate is accompanied by a high incidence of transient, slight and asymptomatic increases in semm transaminases. Usually the increased enzyme activity appears after weeks of treatment. In rare cases of severe liver toxicity, the nonspecific systemic and digestive symptoms are followed by jaundice, evidence of liver failure, as well as encephalopathy and coagulopathy. The mechanism of hepatotoxicity is unknown, however there are theories that there is impairment of mitochondiral oxidation of long-chain fatty acids by a metabolite of the parent drag. Symptoms subside with little to no residual liver dysfunction after discontinuing the drag. Oral Contraceptive Induced Liver Disease Estrogen, progesterone, and combination oral contraceptives can produce several adverse effects on the heptobiliary system. They are 1) hepatocellular cholestasis, 2) liver cell neoplasias, 3) increased predisposition to cholesterol and gall stone fomation, 4) hepatic vein thrombosis. These cholestatic hepatotoxic effects are attributed to estrogen's direct effect on bile formation. The mechanism of action is unknown. There is evidence to suggest that there are safety response differences to drag therapy in reference to development of drag-induced liver toxicity which may be attributable to genotypic differences between individuals. There is provided in this invention examples of gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this disorder, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1-6, more preferably Table 3, and pathway matrix Table 8 and discussed below are candidates for the genetic analysis and product development using the methods described above. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause Liver Toxicity As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drag transport, phase I and phase II metabolism, excretion, hepatic cannicular uptake and concentration, and protection from reactive intermediate damage the optimization of therapy by an agent known to have a hepatic side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Example 21 Drag-Induced Cardiovascular Toxicity Drag induced cardiovascular toxicities include but are not excluded to anhythmias, tachycardia, extrasystoles, circulatory collapse, QT prolongation, cardiomyopathy, hypotension, or hypertension. Drags known to elicit these type of responses include but are not excluded to theophylline, hydantoins, doxorabicin, daunorubicin. Arrythmias-If the normal sequence of electrical impulse and propagation through myocardial tissue is perturbed, an arrythmia occurs. Broadly, arrythmias fall into one of three categories: bradyarrythmias (slowing or failure of the initiating impulse), heart block (an impaired propagation through node tissue or atrial or ventricular muscle), and tachyarrythmias (abnormal rapid heart rhythms). Subcategories include: sinus bradycardia, atrioventricular block (AN block), sinus tachycardia, ventricular tachycardia, atrial flutter, multifocal atrial tachycardia, polymoφhic ventricular tachycardia with or without QT prolongation, frequent or difficult to terminate ventricular tachycardia, atrial tachycardia with or without AV block, ventricular bigeminy, and ventricular fibrillation. Drugs known to induce these types of arrythmias include, but are not excluded to, digitalis, verapamil, diltiazem, b-adrenergic blockers, clonidine, methyldopa, quinidine, flecainide, propafenone, theophylline, sotalol, procainamide, disopyramide, certain non- cardioactive drugs ( ), and amiodarone. Heart Rate, Tachycardia-Heart rate is under both sympathetic and parasympathic control. The influence of heart rate on cardiac output is paramount. Drugs affecting heart rate include, but are not limited to, sympathomimetics, parasympathomimetics, and agents or compounds affecting these two central inputs. Extasystoles- is defined as premature myocardial excitation. Extrasystoles can include atrial, nodal, or ventricular. Other asynchronous pathologies may result from these systoles. Drugs known to be associated with extra systoles include, but are not excluded to, agents that prolong the depolarization time, agents that leave a residual available intracellular calcium, or agents that alter the function of the K+ or Na+ channel activity. QT Prolongation- is the interval on an electrocardiogram that indicates ventricular action potential duration. QT prolongation can lead to uncoordinated atrial and ventricular action potentials. In these circumstances of delayed or prolonged polymoφhic ventricular afterdepolarizations, resultant abnormal triggering of secondary, uncoordinated depolarizations can occur. Two of these conditions are explained as follows and may be associated with underlying rapid or slow heart rate: 1) under conditions of residual excess intracellular calcium (myocardial ischemia, adrenergic stress, digitalis intoxication), and 2) under conditions of marked prolongation of cardiac action potential (agents (antiarrythmics or others) that prolong action potential duration). Cardiomyopathy-There are broadly three categories of cardiomyopathies: dilated, hypertrophic, and restrictive. These cardiac muscular diseases can be of mechanical or acquired origin. Dilated cardiomyopathies are generally caused by myocardial injury that results in depressed systolic function and progressive ventricular dilatation. Drug induced dilated cardiomyopathy can occur in the presence of, but are not excluded to, ethanol, chenotherapeutic agents, elemental compounds, and catecholamimetics. Hypertrophic cardiomyopathy is the presentation of grossly assymetric (eccentric) or symmetric (concentric) hyoertrophy of the left ventricle in the absence of another cardiac or systemic disease capable of producing the disproportionate increase in ventricle mass. In drag induced hypertrophic cardiomyopathy, there may be compensatory hypertrophy of the left ventricle in response to inordinate and or sustained hypertension or prolonged reduced or insufficient cardiac output as a result of myocardial injury or noncardiac mediated physiological events. Restrictive cardiomyopathies are the result of a primary abnormality of diastolic function (impaired filling). Impaired diastolic function can occur as a result of moφho logically detectable myocardial or endomyocardial disease, interstitial deposition of deposition of abnormal substances (infiltrative), intracellular accumulation of abnormal substances (strage diseases), or as a result of endomyocardial disease. In the last category, anthracyclines have been associated with both dilated and restrictive cardiomyopathies. Blood Pressure-Blood pressure is regulated in a complex inteφlay of neural and endocrine mechanisms. These mechanisms are aimed at the physiologic contorl of cardiac output, delivery of blood components to the tissues, and removal of metabolic by-products from the tissues. Hypertension is defined as the elevated arterial blood pressure either an increase of systolic or diastolic pressure or both. Secondary hypertension can be associated with drugs and chemicals including, but not limited to, cyclosporine, oral contraceptives, glucocorticoids, mineralocorticoids, sympathomimetics, tyramine, and MAO inhibitors. Hypotension is defined as the reduction in blood pressure that is associated with orthostatic hypotension, syncope, head injury, hepatic failure, antidiuresis, myocardial infarction and cardiogenic shock. Drag-induced hypotension is associated drags including, but not exclusive of, parasympathomimetics, diuretics, and direct acting cardiac agents. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause Cardiovascular Toxicitv As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drug transport, phase I and phase II metabolism, and protection from reactive intermediate damage the optimization of therapy of by an agent known to have a cardiovascular side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drug response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Example 22 Drag-Induced Pulmonary Toxicity Drag induced pulmonary toxicity includes, but is not excluded to, asthma, acute pneumonitis, eosinophilic pneumonitis, fibrotic and pleural reactions, and interstitial fibrosis. Drag know to elicit pulmonary toxicity include, but are not excluded to, salicylates, nitrofuratoin, busulfan, nitrofurantoin, and bleomycin. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause Pulmonary Toxicities As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drug transport, phase I and phase II metabolism, excretion, protection from reactive intermediate damage, and immune responsiveness, the optimization of therapy of by an agent known to have a pulmonary side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Example 24 Drug-Induced Renal Toxicity Drag-induced renal toxicity includes, but is not exclusived to, glomerulonephritis and tubular necrosis. Drags associated with eliciting renal toxicity include, but are not excluded to, penicillamine, aminoglycoside antibiotics, cyclosporine, amphotericin B, phenacetin, and salicylates. Advantages of Inclusion of Pharmacogenetic Stratification in Clinical Development of Agents that May Cause or are Associated with Renal Toxicity As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 8, genes involved in drug transport, phase I and phase II metabolism, and renal tubular uptake and concentration the optimization of therapy of by an agent known to have a renal side effect by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drug development program. Example 24 Asthma I. Description of Asthma Asthma can be an acute or chronic condition associated with inflammation of the lower airways and variable levels of airflow obstruction. Asthma symptoms vary among individuals and may include wheezing, shortness of breadth, tightness of the chest, trouble controlling a cough, persistent cough at night, difficulty breathing during or soon after physical exertion or exercise, or waking up at night due to one of these symptoms. Episodes of these symptoms (refened to as asthma attacks, flare-ups, or exacerbations) occur when there is sufficiently severe airway constriction to render a patient almost unable or unable to breathe. There can be warning signs , however, many attacks are sudden and unanticipated. Individuals with asthma have inflamed airways that are supersensitive to inducers of asthma which exacerbate asthma and enhance underlying inflammation such as allergens, respiratory infections, or industrial pollutants. Provokers of asthma leading to bronchospasm include exercise or physical activities, irritants, emotions and aspirin. Asthma attacks are associated with swollen and inflamed linings of the airways, excess mucus in the airways, and bronchospasm which are reversible. In chronic asthma, there is persistent activation of resident cells (e.g. basophils, eosinophils, neutrophils) lining the airway leading to chronic inflammation which can result in ineversible changes in the airway pasages. These permanent changes are part of a remodeling process. Recent evidence has suggested that airway inflammation is a major factor in the pathogenesis and in the severity of the disease. One theory holds that asthsma is a T helper 2 (Th2) cell-driven chronic eosinophilia mediated via dendritic and other antigen-presenting cells. The inflammatory nature of the disease is multicellular in nature, with mast cells, eosinophils, macrophages, basophils, lymphocytes, neutrophils, and epithelial cells participating and therefore immunoglobins, cytokines, chemokines, adhesion molecules, proteinases, inflammatory mediators, and growth factors are involved in various stages and interact to maintain and amplify the inflammatory response. The net result of these interactions is persistent inflammation and repair, ultimately leading to ineversible airway remodeling. II. Current therapies for Asthma Because asthma results from a complex combination of mediators of inflammation, most useful anti-asthma agents affect pathways for these mediators. In acute or chronic asthma, the therapeutic categories include: immunosuppressive agents including glucocorticoids, antiinflammatory agents including leukotriene receptor agonists and mast cell stabilizers (cromolyn sulfate); bronchodilators including β-adrenergic agonists, sympathomimetic agents, and xanthines; and agents to treat cough and excess mucus including expectorants and mucolytics. Corticosteroids affect the inflammation within the airways by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. β-Adrenergic agonists and sympathomimetics affect the pulmonary airway lining in a well-characterized mechanism of β-adrenergic receptor activation of adenylyl cyclase as well as cAMP independent mechanisms. Bronchodilation is the immediate clinical effect. Leukotriene modifiers affect the airway by inhibition of 5-lipoxygenase, the initial enzyme of leukotriene biosynthesis, and exert their effect by decreasing leukotriene production, thereby interferring with eosinophil migration and other processes. Corticosteroids affect the inflammation within the airways by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. Corticosteroids in combination with long-acting β-adrenegic agonists work well as combination therapy. Cromones are believed to act on the airway by modifying mediator release, and inhibiting mast cell degranulation. Xanthines are believed to act on the airway in asthma by inhibiting eosinophil cell migration, and enhancing β-adrenergic pathway mediated bronchodilation via the inhibition of phosphodiesterase. Difficult to treat or therapy-resistant asthma syndromes present a challenge to clinicians. They include difficult acute and chronic, as well as chronic severe, acute severe, therapy-resistant, difficult to control and corticosteroid-dependent asthma. III. Limitations of Current Therapies for Asthma Limitations Involving Efficacy The therapies discussed above do not reverse the underlying pathological process in asthma; they merely slow or retard the progression of asthma. As thickening of the airways occurs and becomes ineversible the therapeutic options become limited. Thus, therapies for asthma are aimed at reduction of inflammatory processes and control of symptoms starting at the earliest date (frequently in the pediatric setting). The limitations of the adrenegic agonist compounds used for the treatment of asthma include short duration of action and ligand desensitization. Excessive use of short acting β-adrenergic agonists has been proposed to lead to loss of asthma control and consequent increases in morbidity and mortality. Long acting bronchoactive/bronchoprotective agonists acting at adrenergic receptors have supplanted short duration β-agonists. Short-acting β-adrenergic agonists are primarily used for the relief of acute asthma symptoms. Excessive reliance on these agents is generally not advisable because 1) β-adrenergic receptors undergo a rapid desenitization and the agonist becomes an ineffective bronchodilator, and 2) repetitive high doses of short acting β-adrenergic agonists may be detrimental to to the control of asthma by potentially interfering with corticosteroid action. This desensitization occurs through a process involving G-protein receptor coupled-kinases and or cAMP dependent protein kinase or by enhanced degradation of cAMP by phosphodiesterase activity. Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of Cushingoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus-pituitary axis, decreased thyroid hormone serum binding protiens, and impaired wound healing. Theophylline or other phosphodiesterase inhibitors have been shown to have a nanow therapeutic window and can result in life-threatening cardiac arrythmias. Difficult to treat asthma involves a spectrum of disease that responds suboptimally to doses of glucocorticoids. In the face of partial response to inhaled or oral steroids, higher doses are administered risking steroid associated side-effects. The reduction of clinical symptoms of asthma following antiinflammatory therapy may only become evident after several weeks to months of therapy. The slow action of these therapies creates problems for the clinician seeking to expeditiously determine optimal therapy for an individual patient. The development of genetic tests to predict response to different agets will allow selection of optimal therapy with less of the time consuming empirical clinical decision making required presently. Limitations Involving Toxicity or Undesired Side Effects There are toxicities and undesired side effects associated with the above cunent therapies for asthma that require monitoring. Drugs used to treat asthma may cause death, disability, disease, and place a fetus at risk. The undesired side effects or toxicities are listed for each drag category as described above. IV. Impact of Stratification Based Upon Genotype in Drug Development for Drugs, Compounds, or Candidate Therapeutic Interventions for Asthma In a recent report, it was demonstrated that the 5-lipoxygenase (5-LO) gene promoter variation among asthma patients is linked to drug response to 5-LO inhibitors (Drazen et al., Nature Genetics 22: 1999). In a clinical trial to test efficacy of a potent, selective 5-LO inhibitor (ABT-761), the trial was abruptly closed due to inordinate event rate of abnormal liver function tests. Although the projected enrollment was not reached, the interim data suggested superior efficacy regarding forced expiratory volume in the high dose relative to low dose or placebo groups. The investigators chose to stratify the high dose and placebo group of the enrolled patients based upon genotype of the 5-LO gene promoter. The 5-LO gene promoter has been found to contain 3-6 tandem repeats of the Spl -binding motif. The wild-type allele was designated as 5 tandem repeats and had a frequency of 0.772 in the study population. The forced expiratory volume data indicated that heterozygous patients on high-dose active treatment had, on average, an improvement of forced expiratory volume within one week (23.3 + 6.0%o) and was similar to the wild-type patients (18.8 + 3.6%>). In contrast, the patients with mutant genotype had no benefit from active 5-LO inhibitor treatment (-1.2 + 2.9%>). In the table below, the trial outcome data is described for two periods following treatment with high dose or placebo. a Data extrapolated from published data Approximately 6%> of asthma patients do not carry a wild-type allele at the 5- LO core promoter locus, and this data indicates that these patients would not benefit from 5-LO inhibitor drag therapy. Further, these data indicate that there is evidence to reasonably identify patients, i.e. stratification based upon 5-LO genotype, to appropriately treat patients with asthma. A recent double blind, placebo controlled crossover designed pharmacogenetic restrospective clinical trial of a β2-adrenoreceρtor polymoφhism was implemented to analyze the significance of β2-adrenoreceptor polymoφhisms (Tan et al. Lancet 350:995-999). In vitro studies have suggested that polymoφhism of the β2-adrenergic receptor may influence the desensitization induced by β2 agonists. Twenty two moderately severe asthmatics were enrolled into a placebo controlled cross-over study of formeterol (a β2-adrenergic agonist). The patients were divided into groups by allelic variances: 1) at codon 16, homozygous arginine (n=4), heterozygous arginine/glycine (n=8), and homozygous glycine (n=10); and 2) at codon 27, homozygous glutamine (n=5), heterozygous glutatmine/glutamic acid (n=l 1), and homozygous glutamic acid (n=6). Genotypic analysis determined that individuals who were homozygous for glycine at codon 16 were also homozygous for glutamic acid at codon 27. The results were as follows: Data extrapolated from published graphs. 2 A11 individuals homozygous for Glu27 were also homozygous for Gly 16. The homozygous glycine at position 16 was associated with individuals who were prone to bronchodilator desensitization than at arginine at position 16: the mean FEVi desensitisation was 80%o for Gly 16 homozygotes versus 28% for the Arg 16 homozygotes. Similar results were observed for the 6 hour FEVi and the FEF. For the polymoφhism at codon 27, the mean for the Glu27 homozygous individuals demonstrated greater desensitization than those who were homozygous for Gln27. The allelic variance, glycine at position 16 appeared to dominate over the putative protective effects of the mutation of glutamic acid at position 27. The effects of the codon 16 and 27 polymoφhism in the β2-adrenoreceptor on β2-agonist desensitization, as observed in the above data, suggest that there may be an identifiable subset of patients for whom β2-adrenergic receptor desensitization occurs in the presence of long-acting or repeated use of β2-agonists. Thus, one skilled in the art, will be able to utilize the presently described pharmacogenetic techniques to identify the allelic variances with the coding region of the β -adrenergic receptor or other receptor proteins that are similar to the β - adrenergic receptor, including but not limited to those variances for those genes listed in Tables 4, 15, and 21 and those 7-membrane spanning receptor G-protein coupled receptors. In this way, a skilled practitioner will be able to utilize the methods, protocols, and techniques that are described in the detailed description and those known in the art to identify the gene targets, allelic variance or variances, and candidate drugs that affect these pathways. Further, one can design and implement a strategy that incoφorates a diagnostic test to genotype the individual for a given allele or alleles or halpotype, grouping these candidates by genotype, and testing a β-adrenergic agonist or other candidate therapeutic product for the affect of the pharmacogenomic difference between or among the groups. As described above, there is evidence to suggest that there are safety response differences to drag therapy in asthma which may be attributable to genotypic differences between individuals. There is provided in this invention examples of gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this disorder, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1-6, preferably Table 4, and pathway matrix Table 9 and discussed below are candidates for the genetic analysis and product development using the methods described above. As an example of identification of the primary gene and relevant polymoφhic variance that directly affects efficacy, safety, or both one could select an gene pathway as described in the Detailed Description, and determine the effect of genetic polymoφhism and therapy efficacy, safety, or both within that given pathway. For example, referring to Table 9, genes involved in cytokine-mediated immune regulation, non-cytokine mediated immune regulation (including, but not excluded to, cyclophilins, corticosteroids), cell mediated inflammation involving apoptosis, adhesion and migration, protease and protease inhibitors, complement, degranulation (platelets, mast cells, neutrophils, ans eosinophils), release of inflammatory modulators (including membrane lipids, prostaglandin, platelet activating factor, leukotrienes, histamine, nitric oxide), vascularization mediators (including endothelin and vascular endothelial cell growth factor), neurotransmitters and peptide hormone inflammation modulators (including adrenergic, purinergic, cholinergic, ion channels, tachykinin, neurokinin, substance P, bradykinin, parathyroid hormone, melanocortin and adrenocorticotrophic hormones, and modulators of general cell growth pathways the optimization of therapy of by an agent can be achieved by determining whether the patient has a predisposing genotype in which the selected agents are more effective and or are more safe. In considering an optimization protocol, one could potentially predetermine the genotypic profile of these genes involved in the manifestation of the adverse effect, or those genes preeminently responsible for drag response. By embarking on the previously described gene pathway approach, it is technical feasibility to determine the relevant genes within such a targeted drag development program. Description of Mechanism of Action Hypotheses for Future Drug Development There are many potential mechanisms that may serve as targets for candidate therapeutic interventions. For example, phosphodiesterase inhibitors to PDE4; T- lymphocyte-eosinophil interactions inhibition: targeting the factors involved in the regulation of the TH2(CD+4) differentiation and/or activation by soluble factors (cytokines (IL-4, IL-5); co-stimulatory molecules (B7-2/CD86); and transcritpion factors (GATA-3, AP-1). These targets may be available to limit the TH2 cell involvement in the initiation of asthmatic inflammation. Suppression of eosinophil adhesion with consequent inhibition of influx into the lung is a strategy to suppress asthmatic airway inflammation. Such inhibition may be mediated through inhibitors directed towards very late antigen-4 (VLA-4), monoclonal antibodies directed towards VLA-4, intracellular adhesion molecule 1 (ICAMl), and alpha 1,3-fucosyltransferase VII (an enzyme which regulates sekectin function). Furthermore, molecules may be targeted to suppress the expression of adhesion molecules (e-selectin, vascular cell-adhesion molecule 1 (VCAM-1), and ICAMl). There are a group of chemokines that contain a cysteine-X-cysteine motif, such as IL-8 that are effectors of acute inflammatory episodes, whereas cysteine- cysteine chemokines, such as macrophage inhibitory peptide 1 (MIP-1), eotaxin, RANTES, or macrophage chemotactic peptide 1 (MCP-1) act as chronic mediators of inflammation. These molecules may be appropriate targets for inhibiting either the acute or chronic inflammatory pathway. Cysteinyl leukotrienes have a central role in the development of chronic asthma, and antagonists (i.e., CysLTi) may be able to ablate the actions of this ligand. These novel leukotriene receptor agonists may have potential for anti- inflammatory effects. Endothelin receptors may also be a target, with endothelin antagonists to specific receptor subtypes ET A or ETβ. Other receptors known to be involved in the inflammatory process that may be potential targets are the tachykinin NK1 receptors and selective ligands to the NK1/NK2 receptors. Induction of cyclooxygenase and the consequent increase in prostaglandin release is associated with the development of inflammation. Antisense oligonucleotides directed against the receptor types NK-kB, major basic protein, 5- lipoxygenase, leukotriene C4(LTC4 synthetase, IL-4, IL-5, IL-8 and adenosine have been developed that are inhalable products that can directly block the expression of these mediators of the inflammatory response. Other areas of drag target development include immunobiology of the airways i.e., THl and TH2 and their involvement in the immune response, synthesis of immunoglobulin, IgE, integrins, inhibition of αIL5 and αIL5 monoclonal antibody, soluble IL4 receptor, neurokinin receptor antagonist, chemokine inhibitors. The inflammatory response is also being evaluated in terms of the effects of NO2, SO2, and ozone on the subsequent effect on airway response to these potential allergens. As well as adhesion molecule expression, cytokine production, and cytokine gene transcription factors. Optimization of nonsteroidal or steroidal antiinflammatory agents , or agents aimed at a mechanism of therapy of the underlying etiology of asthma further demonstrates the utility of selection of a potential asthma patient that has a predisposing genotype in which selective antiasthmatic or other agents may be more effective and or have an more desirable safety profile. In considering an optimization protocol, one could potentially predetermine variance or variances within the nonsteroidal antiinflammatory pathway, steroid antiinflammatory pathway, or antiinflammatory mediated intracellular mechanism of action that is preeminently responsible for antiasthmatic drag response. By embarking on the previously described gene pathway approach, it is technically feasible to determine the relevant genes within such a targeted drug development program for asthma. A sample of therapies approved or in development for preventing or treating the progression of asthma cunently known in the art is shown in Table 47. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Example 25 Inflammatory Bowel Disease Description of Inflammatory Bowel Disease Inflammatory bowel disease (IBD) is a broad clinical term that includes idiopathic chronic inflammatory bowel diseases including Crohn's disease (CD) and ulcerative colitis (UC) which can be distinguished from inflammatory bowel disease of known origin including diverticulitis, radiation enteritis, colitits, drag or toxin- induced enterocolitis, or vasiculitis of the intestinal tract. UC is a term that encompasses a broad category of diffuse, continuous, and superficial inflammation of the colon, which begins within the rectum and extends proximally. The condition is limited to the colon and large intestine, with limited involvement of the small intestine. In UC, the inflammation primarily affects the mucosal process and is not transluminal within these anatomical regions. CD is characterized by focal, asymetric, transmural inflammation affecting any portion of the gastrintestinal tract, i.e. from the mouth to the anus. The focal localization and possible extent of the inflammation distinguishes UC from CD. There are cunently approximately 35-100 and 10-100 CD per 100,000 Americans diagnosed with UC or CD, respectively. Clinically, patients with UC experience variable stool consistencies from constipation to dianhea, low-grade fever, malaise, nausea, vomiting associated with defecation, night sweats, arthalgias, dehydration, tachycardia, and symptoms of abdominal tenderness. There can be rectal bleeding, tenemus, and passage of mucopus. Patients with Crohn's disease experience symptoms of peptic ulcer disease, nausea, vomiting, and epigastric pain. Transmural inflammation leads to fibrosis and transluminal nanowing. In some cases, the narrowing leads to signs and symptoms of intestinal obstruction including nausea, vomiting, waves of abdominal pain, and a reduced output of stool. Patients with colonic CD are likely to experience abdominal pain, cramping or localized pain, rectal bleeding, and dianhea. Weight loss is common among CD patients due to malabsoφtion of nutrients and reduced food intake due to minimization of postprandial symptoms. There are extraintestinal manifestations of inflammatory bowel disease affecting the following processes including: nutritional and metabolic abnormalities, hematologic abnormalities, skin and mucous membranes, musculoskeletal, hepatic and biliary abnormalities, renal complications, and optic complications. These complications are associated when the colon or intestinal tract is inflammed. These complications are clinically menifset as joint swelling or pain, erythema nodosum, pyoderma gangenosum, sclerosing cholangitis, conjunctivitis, or uveitis. There is an increased risk for the development of gastrointestinal cancer in patients with IBD. In both UC and CD, there is an increased risk of adenocarcinoma of the intestine. This is not conelated to the intensity of the first attack, subsequent course, or and specific medical therapeutic approach. Therefore routine screenig for dysplasia and neoplasia is wananted. Current Therapy of Inflammatory Bowel Disease Strategies for the therapy of inflammatory bowel disease includes antiinflammatory agents, and immunomodulation. Antiinflammatory agents include the use of glucocorticoids and the aminosalicylates. Glucocorticoids act by modulation of the immune response. Corticosteroids affect the inflammation within the gastrointestinal tract by decreasing growth and development of mast cells, inducing apoptosis, suppressing lymphocyte generation of IL-5 and other cytokines, inhibiting some mediator release, inhibiting cytokine production, inhibiting the transcription of cytokines (for example IL-8, TNF-α, prototypic antiviral chemokine (regulated-on-activation normal T-expressed and secreted, RANTES), and GM-CSF), and inhibiting nitric oxide synthesis. 5-aminosalicyclic acid (5 ASA) is a salicylate that is used for the treatment of IBD, is not orally active, is poorly absorbed and is inactivated by intestinal bacteria, and is delivered as a suppository or rectal suspension enema. Oral formulations can be used to deliver active drug to the lower intestine which are cogeners of 5 AS A. The aminosalicylates are potent antiinflammatory agents that inhibit cyclooxygenase (COX), arate limiting enzyme in the protaglandin and leukotriene pathway. Immunosuppressive agents are also used to modulate the inflammatory/immune response. There are four broad categories of immunosuppresive agents that have distinct mechanisms of action: inhibition of ribonucleotide synthesis which acts to inhibit the proliferation of T-cell clones (6- mercaptopurine), inhibition of folic acid which acts to inhibit T-cell and B-cell function as well as decrease IL-1 and IL-6 activity (methotrexate), inhibition of T- cell receptor stimulated transcription of lymphokine genes which act to ihibit the production of IL-2 and IL-2 receptors as well as inhibit certain cytokines (TNF-α, IFN-γ) (cyclosporin and FK506), and inhibition of guanosine nucleotide synthesis which acts as cytostatic effects on lymphocytes (mycophenolate). Each of these catgoiies of agents have been employed for the therapy of IBD. Recently a chimeric monoclonal antibody was approved for use in the treatment of moderately to severe active Crohn's disease for those patients that are unresponsive to conventional therapy. This monoclonal antibody is specific for TNF-α and can remove TNF from the bloodstream before it reaches the site of inflammation. Crohn's disease may progress to a level and extent in which surgical removal of the localized inflammation is warranted. Surgery has been indicated for recunent intestianl obstruction, complicated fistulas, intractable hemonhage, disease refractory to medical therapy, growth retardation refractory to therapies, or cancer. The surgical procedures vary from excision of a localized, diseased portion of the gastrointestinal tract to removal of large portions, i.e. the entire colon (colectomy). Surgical excision of the inflammed region or to conect complications such as blockage, perforation, abscess, or bleeding can result in a substantial relief of symptoms. Limitations to Current Therapies for IBD Salicylate associated side effects include dyspepsia, gastric or small bowel bleeding, ulceration, renal insufficiency, confusion, rash, headache, hepatic toxicity. NSAIDs also reversibly inhibit platelet aggregation and prolong bleeding time. Glucocorticoid associated side effects include increased appetite, weight gain, fluid retention, acne, ecchymosis, development of cushoid facies, hypertension, hyperkalemia, diabetes, hyperglycemia, hyperosmolar state, hyperhpidemia, hepatic steatosis, atherosclerosis, myopathy, aseptic necrosis, osteoporosis, ulcers, pancreatitis, psuedotumor cerebri, pyschosis, glaucoma, cataract formation, vascular necrosis, increased suseptibihty to infection, impairment of the hypothalamus- pituitary axis, decreased thyroid hormone serum binding protiens, and impaired wound healing. Agents involved in immunomodulation have the following undesirable side effects including antimetabolites: hepatic compromise including hepatic fibrosis, ascites, esopageal varices, cinhosis, pneumonitis, myelosuppression; immunosuppressives: myelosuppression, (cyclosporine: renal insuffienciency anemia, hypertension. Monoclonal antibody to TNF proteins therapies have been shown to generate a human-antimouse antibody response (HAMA). However, patients on immunosuppressive agents such as glucocorticoids and others are less likely to generate antibodies to the treatment antibody. Delayed hypersensitivty is demonstrable 2 to 4 years after initial treatment in 25% of the patients treated with the chimeric antibody. Further, there are patients that develop a serum sickness reaction which includes fever, and joint swelling that requiring hospital admission. A positive antinuclear antibody (ANA) occurred in 24-36% of the patients analyzed. Nine percent of the patients developed anti-DNA antibodies, less than 1%> developed a lupus-like reaction requiring steroid therapy. In surgical therapy of IBD, reccurring inflammation and relapse, after excision procedures occurs in 75% of the patients. Attempts have been made to include salicylate therapy after resective surgery, however, the inflammation reccunance rate in that group was 52%>. Impact of Stratification Based Upon Genotype in Drug Development for Drugs. Compounds, or Candidate Tlxerapeutic Interventions for Autoimmune Disease Thiopurine methyltransferase (TPMT) The thiopurine S -methyltransferase (TPMT) is a cytosolic enzyme whose precise physiological role is unknown. This enzyme catalyzes the S-methylation of widely used immunosuppressive or cytotoxic thiopurine drags such as 6- thioguanine, 6-mercaptopurine and azathioprine.8 The in vivo activity of this cytosolic enzyme is characterized by interindividual and interethnic variability caused by the genetic polymoφhism of the TPMT gene, which was discovered, using pharmacogenetic techniques, by the existence of three major phenotypes, high (HM), intermediate (IM) and deficient (DM) methylation. As a consequence, individuals greatly differ in detoxication of thiopurine drags to 6- methylmercaptopurine as well as the occurrence of side effects or therapeutic efficacy. Using genomic techniques, PCR-SSCP (polymerase chain reaction - single strand conformation polymoφhism), Spire- Vayron de la Moureyre et al. 9 have defined the mutational and allelic spectrum of TPMT in a group of 191 Europeans. In this analysis, PCR-SSCP techniques identified allelic variances in the entire coding sequence, the exon-intron boundaries, the promoter region and the 3'- flanking region of the genes. Six mutations were detected throughout the ten exons and seven TPMT alleles were characterized. Within the promoter region, six alleles conesponding to a variable number of repeats (VNTR) were identified. The TPMT phenotype was conectly predicted by genotyping for 87% of individuals. A clear negative conelation between the total number of repeats from both alleles and the TPMT activity level was observed, indicating that VNTRs contribute to inter- individual variations of TPMT activity. This VNTR polymoφhism can be considered responsible for shifts to lower or higher TPMT activities observed among discordant individuals. Seven out of the nine phenotyped HMs but genotyped IMs were carrier of a total of eight VNTR repeats. This low number of repeat can account for the switch to high TMPT activities of these samples. One in 300 patients with IBD are homozygous-deficient for TPMT. The clinical relevance for this deficiency is that TPMT is the enzyme responsible for the conversion of 6-MP to 6-MMP, and the AZA compounds to 6-TG. In TPMT deficient patients, higher levels of 6-TG and 6-MMP are then produced and are associated with significant leukopenia. In general, patients produce variable levels of 6-TG and 6-MMP as determined by their intrinsic enzyme systems. Higher 6-TG levels are conelated with good therapuetic response, but produce leukopenia. Higher 6-MMP levels conelate with hepatotoxicity and in recent studies with leukopenia. There is evidence to suggest that there are safety response differences to drag therapy in IBD which may be attributable to genotypic differences between individuals, one example being the TPMT gene described above. There is provided in this invention examples of other gene pathways that are implicated in the disease process or its therapy and those that potentially cause this variability. The Detailed Description above demonstrates how identification of a candidate gene or genes and gene pathways, stratification, clinical trial design, and implementation of genotyping for appropriate medical management of a given disease can be used to identify the genetic cause of variations in clinical response to therapy, new diagnostic tests, new therapeutic approaches for treating this disorder, and new pharmacuetical products or formulations for therapy. Gene pathways including, but not limited to, those that are outlined in the gene pathway Tables 1 -6, preferably Table 4, and Table 9 and discussed below are candidates for the genetic analysis and product development using the methods described above. V. Description of Mechanism of Action Hypotheses for Future Drug Development The majority of the hypotheses for future therapuetic interventions for inflammatory bowel disease are based upon the understanding the immunologic mechanisms that cause and peφetuate the inflammation within the gastrointestinal tract. Although the initiating event is elusive, the resulting immunologic events have been studied. All of the gastrointestinal enterocytes have immunologic function. Under physiologic conditions, these enterocytes selectively activate CD8+ nonspecific suppressor cells, in response to inflammation. In patients with IBD, these enterocytes selectively stimulate the development of CD4+ helper T cells which can respond in two ways 1) the Thl response which involves the activation of IL-2 and IFN-g and leads to delayed hypersensitivity and cellular immunity and 2) the Th2 response which involves IL-4, IL-5, IL-6, and IL-10 and leads to antibody response and humoral immunity. Both Thl and Th2 responses are genetically controlled and are coordinately regulated, i.e. Thl response stimulation results in down regulation of Th2 response and vice versa. It has been demonstrated that in UC patients the Th2 response is favored and in CD patients the Thl response is favored. A humanized (95% human, 5%> mouse) version of the chimeric antibody (75% human, 25%> mouse) to TNF is cunently under development. Some antiidiotypic antibodies are generated, but it doesn't appear to stimulate a delayed hypersensitivity, no stimulation of anti-DNA antibodies, or lupus-like reactions. Mediators of the immune response including intracellular adhesion molecule (ICAM-1) inhibitors (antisense molecules or others), IL-10, IL-11 have been tested in humans. Further, and anti-CD4 monoclonal antibody which has been shown to interfere with the interaction of the CD4 molecule and the HLA class II molecules leading to an inhibition of antigen presentation has been tested. Thalidomide (inhibitor of TNF, acceleration of the degradation of the TNF mRNA) is also under consideration. It has been noted that individuals who smoke tobacco products have a lower incidence of IBD. Therefore, understanding the immune response and conelation with nicotinic chloinergic pathways is under investigation. A sample of therapies approved or in development for preventing or treating the progression of EBD cunently known in the art is shown in Table 48. In this table, the candidate therapeutics were sorted and listed by mechanism of action. Further, the product name, the pharmacologic mechanism of action, chemical name (if specified), and the indication is listed as well. Example Hepatitis C Selecting Optimal Therapy for HCV Patients Genetically Determined Variation in Response to Interferon α Treatment of hepatitis C vims (HCV) infection with interferon α is expensive, benefits a minority of patients, and produces side effects in a significant fraction of patients. Addition of ribavirin increases efficacy, but combination therapy remains expensive and still falls well short of providing a lasting benefit to most patients. It would therefore be desirable to identify prospectively those patients likely to have a sustained response to treatment. Ideally a diagnostic test would also predict what dose of interferon and ribavirin, administered for what length of time, will afford to each patient the best chance of a sustained response. Pre-treatment identification of patients likely to suffer serious toxic side effects would also be desirable. The best characterized predictors of response to interferon α therapy are viral load and HCV genotype. Low viral load before therapy is predictive of a positive response. However, demonstration of decreased viral load after initiation of therapy is cunently the best predictor of response to therapy. There is no consensus on the optimal time after irritation of therapy for measuring viral levels; periods ranging from 2 weeks to four months have been proposed. The viral load test is not very effective at discriminating long term responders from those patients who suffer rebound of HCV infection within 6 months after treatment. Also, the ideal test would be performed in advance of any treatment, thereby saving the considerable costs associated with even short term therapy. In search of other predictive indices, over 100 controlled clinical studies have examined a variety of viral and host factors in responders and nonresponders. Genetic variation in both HCV and host genes has been shown to independently influence patient response to interferon α treatment. A consensus has emerged regarding the interaction of viral genotype and treatment response, however the contribution of host factors to treatment response has not been as well investigated. There are a number of promising recent findings suggesting that polymoφhisms in regulators of human immune function are conelated with response to interferon α. Viral genome variation Comparison of sequenced HCV genomes reveals considerable variation in viral sequence, with at least 6 major types and well over a dozen minor types recognized. The geographical distribution of viral types is nonrandom, perhaps accounting for some of the apparent racial heterogeneity in the natural history of HCV infection. HCV is present in each patient as a heterogeneous population of viral quasispecies, with the degree of heterogeneity differing among patients. Despite these complexities, there are strong conelations between predominant viral type and treatment response. In general, patients with genotype 1 (especially lb) respond poorly to interferon α, with many studies showing response rates under 10 percent. Patients with genotype 2 or 3 do well, with response rates typically greater than 40 percent. Most viral genotyping is based on a short variable segment, however there are multiple segments of the viral genome that vary, and some studies have found that more detailed viral genotyping, for example of the 5' untranslated region, provides stronger conelations with treatment response. Human genome variation A recent study suggests that there is significant variation in response to interferon α treatment among racial groups in the US, even after controlling for the effect of different HCV types. This finding suggests that host genetic variation may be an important factor in response. A number of candidate genes have recently been tested for correlation with interferon α response. The best studied genes are regulators of immune function such as IL-6, IL-10 and TNFα. One study, for example, found that patients with high expression of IL-10 (attributable to a specific haplotype) tend to respond poorly to interferon, perhaps due to impaired immune response. IL-4, IL-12 and TGF-β levels have been correlated with treatment response in some (but not all) studies, however no genetic analysis has been performed. Similarly, hepatic levels of interferon α-β receptor have been conelated with response to interferon, but no genetic analysis has been performed to determine whether polymoφhism affects receptor levels. HLA alleles have also been conelated with response to interferon, particularly the A24-B54-DR2 haplotype. A number of other compelling candidate genes have not been investigated. For example, a recent report shows that HCV can enter cells via the low density lipoprotein receptor. If so, the well studied amino acid polymoφhisms of the LDL- R should be investigated for effects on disease course and response to treatment. There are also likely to be genetic factors that influence response to ribavirin; for example, the drag must be transported across the plasma membrane and then phosphorylated before becoming a substrate for viral enzymes. The transporters and kinases responsible for these processes may be worth genetic investigation. An optimal test for selecting treatment for HCV infection would (i) suggest the optimal therapeutic regimen (interferon alone, interferon and ribavirin, or some other combination), (ii) suggest the optimal dose and duration of treatment, (iii) predict sustained responders vs. short term responders, and (iv) predict patients likely to suffer serious adverse effects. At least three areas should be further investigated to better predict the reponse to interferon α treatment. First, it is not clear that conventional viral genotyping methods, focusing on the 5' untranslated region, capture all of the aspects of viral sequence variation that affect viral biology. Additional genetic determinants of viral pathogenicity should be investigated. Second, the human gene variants that have been associated with response need to be more thoroughly investigated, and interactions between human candidate gene alleles, as well as perhaps between human genes and viral genes, should be tested. Third, recent work suggests a number of new host proteins that may affect response to interferon, and proteins that mediate response to ribavirin have not yet been investigated. The genes encoding these proteins should be thoroughly investigated. With additional information on candidate genes available it should be possible to constmct a plan, ideally via retrospective analysis of clinical trial data, for first assesing the impact of variation in each of the candidate genes, then examining gene x gene interactions, and finally reducing the number of tests to a much smaller number for confirmatory prospective trials. In Table 49, there a list of the candidate therapeutic interventions that in development for Hepatitis. One skilled in the art could apply, as described in the text, the methods of this invention to ascertain whether there is a gene in the inflammatory pathway that may be involved in the efficacy, safety, or toxicities of these candidate interventions. Example 27 Pro 12 Ala Substitution in PPARγ2 Affects Insulin Sensitivity Peroxisome proliferator-activated receptors (PPARs) are members of the nuclear hormone receptor family of DNA binding transcription factors. PPARs form heterodimers with retinoid X receptors and the resultant heterodimers, in coordination with coactivators and corepressors,bind to DNA and activate transcription of various genes. The PPAR superfamily includes receptors that mediate the size and number of peroxisomes in response to a diverse group of chemicals both naturally occurring and xenobiotics. Endogenous ligands thought to activate the PPARs are arachidonic acid, oleic acids, andogenous molecules (fatty acids or steroids), C18 unsaturated fatty acids, peroxisome proliferation activators, and others (see Table 5). Diverse chemicals can activate the PPARs: herbicides, leukotriene antagonists, plasticizers (phthalate ester plasticizers used in the production of vinyl plastics), the fibrate class of hypolipidemic agents, thiazolidinediones. Overstimulation of these receptors can result in heptomegaly, liver hypeφlasia, and possibly heptocellular carcinoma. There are three known PPARs, α, γ, δ. PPARα is believed to be involved in the regulation and control of fatty acid oxidation enzymes. PPARα is has been shown to have high expression rates in heart, adipose, and liver. PPARγ is believed to be involved in adipocyte differentiation. PPARγ is expressed in high levels in adipocyte tissues. PPARδ (NUC1) is believed to be involved in a family of DNA binding proteins that are involved in adipogenesis and may be involved in early development. PPARδ has been has been shown to have high expression in heart, kidney, and lung. PPARα is involved in the metabolic control of the expression of genes encoding fatty acid oxidation enzymes. Data from several experimental strategies have supported the hypothesis of the mechanism of action of PPARa: 1) PPARa is necessary for the induction of peroxisomal biogenesis in response to peroxisomal proliferating agents; 2) the target genes of PPARs are enzymes involved in cellular fatty acid oxidation which include mitochondrial, peroxisomal, and cytochrome P450 pathways; 3) PPARα is activated by fatty acids or inhibitors of mitochondrial long-chain fatty acid import. It has been shown that PPARα modulates the expression of genes encoding lipid metabolism enzymes, lipid transporters, or apolipoproteins. In an animal model of hyperhpidemia, activators of PPARα was shown to decrease the lipid production in hepatocytes, however PPARα activation also demonstrated tumor promotion within the same animals. Ligands that can specifically activate the lipostat enzymes while not turning on tumor production would be advantageous. PPARγ is thought to be involved in the differentiation of preadipocytes to adipocytes. Overexpression of PPARg in a non-adipose cell, i.e. nonadipogenic fibroblasts, results in the conversion to fat-laden adipocyte-like cells after exposure to a PPARγ ligand. Another transcription factor family involved in adipogenesis is the CAAT/enhance binding protein, CEBP. CEBPa is expressed in high abundance in adipose tissue and may play a direct role in establishing and maintaining the fully differentiated adipocyte phenotype. This hypothesis is based mainly on the data that indicates CEBPα is expressed late in adipogenesis and after key enzymes are induced. In other studies it has been shown that PPARγ and CEBPα expression can both be induced by CEBPβ and CEBPδ. PPARγ and CEBPα both induce the expression of each other as well as activate and maintain the adipocyte proliferative and growth differentiation program. The PPARγ gene has two transcription start sites and translation results in two distinct proteins PPARγl and PPARγ2. Both are highly expressed in adipose tissue. As in other nuclear hormone receptors, PPARγ is dependent on ligand activation. Cunently, known biological ligands are 15-deoxy-Δ 12 ' 14 prostaglandin J, other prostanoids, and products from the linoleic acid pathway, i.e. oxLDL, HETE, 13-HODE and 9-HODE. Xenobiotics from the thiazolidinedione group, i.e. troglitazone, ciglitazone, and pioglitazone can directly activate PPARγ. Modulation of PPR activities are thought to be effective strategies for the development of products for therapy of cancers (breast, prostate, and acute promyleocytic leukemia), metabolic diseases including thyroid disease and diabetes mellitus. PPARγ is expressed at significant levels in human primary and metastatic breast adenocarcinomas. Experimental evidence has suggested that the PPARγ transcriptional pathway can induce terminal differentiation of malignant breast epithelial cells. Ligands known to activate PPARγ have been shown to cause lipid accumulation, reduction of growth rate, and a reversion to a differentiated, less malignant state in studies of cultured breast cancer cells. Further, inhibition of MAP kinase, a negative regulator of PPARg, enhances the activation by a PPARγ ligand (i.e. thiazolidinedione) sensitivity. In studies of an animal model of diabetes, ligands that specifically activate PPARγ (i.e. troglitazone), normalization of elevated glucose levels in obese animals was demonstrated. Studies have been conducted to ascertain the efficacy of thiazolidinediones to treat NIDDM. One product troglitazone (Rizulin) has achieved approval for human therapeutic use in the U.S. In a recent study, it was determined whether genetic variation in the PPARγ coding region was associated with obesity and insulin sensitivity or resistance, as well as type II diabetes mellitus (Deeb et al., Nature Genetics, 1998). It was determined that there was a single polynucleotide base substitution (C/G) which lead to a substitution in the coding sequence of proline to alanine at amino acid position 12 (Pro 12 Ala). The study included two human populations, Finns and Japanese- Americans. It was determined that the relative frequency of the the alanine alle frequency in the Finn study population (nondiabetic, including some with impaired glucose tolerance) was 0.12 whereas the Japanese- American frequency was 0.022 in type II DM patients, 0.039 in patients with impaired glucose tolerance, and 0.093 in normal subjects. In both populations there was an association of the Ala allele frequency and lower fasting insulin levels and body mass index, as well as higher insulin sensitivity; in the Finn population the values achieved statistical significance. The study further demonstrated a functional conelation of the population data with in vitro PPARγ transcription factor binding affinities. In these experiments, it was shown that the Ala-isoform demonstrated a two- to five-fold decrease in relative affinity for the identified peroxisome prohferator response element, as well as a 36%> faster off rate in comparison with the values detected for the PPARγ Pro isoform. Confirmatory data in the form of reduced detectable transactivation by the PPARγ ligand in the case of the PPARγ Ala isoform. In addition, there is data to suggest that PPARγ mRNA expression levels are reduced in obese individuals and that the the ratio of mRNA encoding PPARγ is positively conelated with body mass index. These data suggest that there is an association of reduced trasnscription activation by the Ala PPARγ allelic variant. Further suggesting, that there is a molecular mechanism for the observed body mass index and insulin sensitivity in the individuals having these allele polymoφhisms. The data reported suggests that via reduced transcription of target genes that are involved in regulation of glucose homeostasis. Example 28 Sulfonylurea receptor silent polvmoφhism and insulin levels In a sub-population that is approximately three times more likely to acquire type II DM, Mexican- Americans have higher insulin concentrations, and are more likely to exhibit insulin resistance. It has further been determined that in this population of Americans, hypeinsulinemia is a risk factor for the development of type II DM. The high affinity sulfonylurea receptor (SURl) is known to be involved in the reguilation of insulin secretion. This receptor may be involved in type II DM. The SURl gene product is a functional part of the pancreatic β-cell KATP ion channel. The channel complex is composed of a two subunits, the sulfonylurea binding domain and the b-cell KATP channel responsible for conducting an inward rectifying potassium cunent. With the β-cell, metabolism of glucose produces changes in the relative concentrations of ADP and ATP which leads to a reduction of the KATP channel activation, causing a depolarization of the β-cell membrane and exocytosis of insulin. Within the nucleotide-binding fold region (NBF) of the SURl, mutations have been shown to be autosomal recessive and lead to clinical familial hyper insulinemia. Other mutations in the SURl have been associated with Beckwith-Waldemann-syndrome associated malignant insulinomas. In exon 31, there is a silent polymoφhism (AGG/ AGA) that encodes an arginine residue at position 1272. In the Mexican American study population that had the AGA genotype, there were higher fasting and 2 hr. insulin levels as well as a higher proinsulin to insulin ratio than those observed in the wild-type genotype subgroup. Between the two groups there were similar values for fasting glucose, body mass index, and waist circumference measurements. *values in pmol/1 These data taken togethere suggests that there is an association between the SURl allelic variant and hyperinsulinemia in normal individuals from a high DM risk ethnic group. Example 29 Vitamin D Receptor and Estrogen Receptor Polymoφhisms and Response to Hormone Replacement Therapy Bone mineral density (BMD), a predictor of risk of bone fractures, decreases rapidly in postmenopausal women. Hormore replacement therapy (estrogen) reduces the rate of or prevents the decrease in BMD. Genetic factors contribute to 60-80% of BMD variation. In a recent study (Deng et al., Hum Genet 103:576-585), it was shown that hormone receptor polymoφhisms affect BMD in elderly women and that genotype should be considered when prescribing hormone relacement therapy (HRT) to preserve bone mass in elderly Caucasian women. A population of 108 women participated in the study. They were genotyped for polymoφhic differences in their vitamin D (VDR) and estrogen (ER) receptors. Using restriction endonuclease specific sites within these genes, it was determined that the VDR has a polymoφhic Bsml site (B or b) and the ER has two polymoφhic sites, Xbal (X or x) and RvwII (P or p). In the placebo and HRT groups, the VDR and ER genotype groups had significant affect on the BMD measurements. An analysis of the gene-by-gene interaction revealed that the level of significance was reduced. The amount of variation in BMD attributable to the VDR and ER polymoφhisms varied from approximately 1 %> (for the total body bone mineral content changes in the placebo or HRT groups) to approximately 18.7% (for the spine bone mineral density changes occuring in the HRT group). Significant genotype effects were observed in the xx, PP, or bb groups having a larger decrease of bone mass during the study period, whereas a genotype of XX, pp, or BB is associated with smaller decreases (or larger increase) of bone mass. This study demonstrates and interaction of drug response with genotype with age/reproductive status. Example 30 Cholesterol ethyl-transferase (CETP) A well studied polymoφhism in the first intron of the gene encoding cholesterol ester transfer protein (CETP) provides an example of a polymoφhism in the non-coding region of a gene that has with an impact on drag efficacy via a recessive genetic mechanism. The high-density lipoprotein (HDL) cholesterol concentration is inversely related to the risk of coronary artery disease. CETP has a central role in the metabolism of HDL and may therefore alter the susceptibility to atherosclerosis. The DNA of 807 men with angiographically documented coronary atherosclerosis was analyzed for the presence of a polymoφhism in the gene coding for CETP. The presence of a DNA variation in a Taq I restriction enzyme site was refened to as Bl, and its absence as B2. All patients participated in a cholesterol-lowering trial of the drag pravastatin designed to reduce cholesterol synthesis by inhibiting HMGCoA Reductase, and thereby anest progression of, or induce the regression of coronary atherosclerosis and were randomly assigned to treatment with either pravastatin or placebo for two years. The Bl variant of the CETP gene was associated with both higher plasma CETP concentrations (mean [±SD], 2.29±0.62 μg per milliliter for the B1B1 genotype vs. 1.76+0.51 μg per milliliter for the B2B2 genotype) and lower HDL cholesterol concentrations (34+8 vs. 39+10 mg per deciliter). In addition, a significant dose-dependent association between CETP genotype and the progression of coronary atherosclerosis in the placebo group (decrease in mean luminal diameter: 0.14+0.21 mm for the BIB 1 genotype, 0.10+0.20 mm for the B1B2 genotype, and 0.05+0.22 mm for the B2B2 genotype). This association was abolished by pravastatin. Pravastatin therapy slowed the progression of coronary atherosclerosis in BIB 1 carriers but not in B2B2 carriers (representing 16 percent of the patients taking pravastatin). There was a significant interaction between pravastatin treatment and decreases in the mean luminal diameter (P = 0.01) and the minimal luminal diameter (P = 0.05). The association of the B 1 allele with greater progression of diffuse atherosclerosis (i.e., greater decreases in the mean luminal diameter), as observed in the placebo group, was influenced by the use of pravastatin. In fact, the B 1 allele appeared to be associated with less progression in the patients who were receiving pravastatin. There was a co-dominant relation between the Bl allele and the efficacy of pravastatin in retarding the progression of coronary atherosclerosis. Carriers of two B 1 alleles benefited most from treatment with pravastatin: they had significantly less progression of coronary atherosclerosis, as evidenced by smaller decreases in both the mean luminal diameter (P = 0.001) and the minimal luminal diameter (P = 0.002), than their BlBl counteφarts in the placebo group. Furthermore, carriers of only one Bl allele (B1B2) who were receiving pravastatin had significantly less focal atherosclerosis (P = 0.01) than their counteφarts in the placebo group. Finally, B2B2 homozygotes had a nonsignificantly greater progression at the end of the study than their counteφarts in the placebo group. Both the association of the CETP TaqlB genotype with the decrease in either the mean luminal diameter or the minimal luminal diameter in the placebo group and the interaction between the genotype and pravastatin treatment remained significant after adjustments were made for the mean luminal diameter (or minimal luminal diameter) at base line, the base-line HDL cholesterol concentration, changes in HDL cholesterol concentrations, and activities of both hepatic lipase and lipoprotein lipase. The precise molecular mechanism that underlies the relation between the CETP gene variant and the angiographic response to pravastatin treatment cannot be deduced from this study. However, it may be related to plasma concentrations of CETP. The observations suggest that high CETP concentrations, and therefore high levels of CETP activity, result in an enhanced transfer of cholesteryl esters to atherogenic lipoproteins and have negative effects on the stmcture and function of the HDL pool, which increases the risk of coronary artery disease. This inference is in agreement with the observation that the pravastatin-induced reduction in CETP concentrations was associated with beneficial angiographic effects in patients who had high CETP concentrations - that is, those who were homozygous for the Bl allele. In contrast, the reduction in CETP concentrations induced by pravastatin in patients with genetically determined low plasma concentrations of CETP — that is, those who were homozygous for the B2 allele ~ was associated with a lack of retardation of the progression of coronary atherosclerosis. On the basis of these results and the finding of an increased risk of coronary artery disease in subjects who are heterozygous for CETP deficiency, it is believed that a critical concentration of CETP is required for normal reverse cholesterol transport. In contrast, high plasma concentrations of CETP, as seen in placebo-treated BlBl patients, may promote atherosclerosis by increasing the cholesterol component of atherogenic lipoproteins. One skilled in the art can apply the knowledge of the CETP allelic differences by applying the techniques as described in the detailed summary section. In this way, one could identify the known allelic differences as described above to identify other allelic differences within the CETP gene. One would then be able to utilize molecular biological techniques to provide a diagnostic test to identify the genotypic differences within a selected group of volunteers or patients. In this way, using the methods for designing and implementing a clinical study described in the detailed description, one could implement a clinical trial to further test the significance of allelic variances on the response to pravastatin, other statins, other cholesterol lowering drags or other candidates drags that are known to interact with or affect the CETP gene pathway. Example 31 Angiotensin converting enzyme (ACE) The ACE polymoφhism provides an example of a variance in the non- coding region of a gene with an impact on drag efficacy. Angiotensin-converting enzyme (ACE) inhibitors, initially developed as antihypertensives, have been shown to reduce mortality in trials of patients with both symptomatic and asymptomatic left ventricular dysfunction and after acute myocardial infarction. An insertion/deletion polymoφhism, consisting of a 287- base pair Alu repeat sequence, in intron 16 of the ACE gene, has been shown to predict approximately half of the variance in serum ACE levels between individuals. Homozygotes for the deletion allele (DD) have serum ACE levels twice as high on average as those homozygous for the insertion allele (II), whereas heterozygous (ID) have intermediate levels. It has been demonstrated that genotype continues to predict residual ACE activity even after acute ACE inhibition with enalapril (Todd et al. Br J Clin Pharmacol 1995; 39:131-4). In a typical pharmacogenetic phase I design, comparing two groups of homozygotes healthy males, DD (n=12) and II (n=l 1) after genotyping 200 healthy normotensive men, the effect of enalapril, an ACE inhibitor drug, was significantly greater and lasted longer in the men homozygous for the II ACE genotype (Ueda et al. Circulation 1998; 98:2148-2153 ). Example 32 Glycoprotein Integπn beta-3 subunit and Glycoprotein Integπn alpha-2 subunit (GPIIIa/GPIIb) Glycoproteins Ilia (GPIIIa) and lib (GPIIb) form the GPIIIa/GPIIb complex that belongs to a class of multisubunit integrin receptors that bind cell adhesion molecules. These receptors are composed of alpha and beta subunits refened to as GPIIb and GPIIIa, respectively. Together the GPIIIa beta and GPIIb alpha subunits form part of the platelet complex receptor, fibronectin receptor, and vitronectin receptor, and play a role in clotting. The GPIIIa gene encodes a 788 amino acid polypeptide with a 26 residue signal peptide, a 29 residue transmembrane domain near the carboxyterminus and four cysteine rich domains of 33-38 residues each. (Zymrin et al., J. Clin. Invest. 81.-1470- 1475 (1988)). Two different antigenic forms of GPIIIa, alloantigens P1A1 and P1A2 (Platelet Antigen 1 and 2) have been described and can be distinguished using a monoclonal antibody. The most common form of GPIIIa, P1A1, is carried by 98%o of the Caucasian population. The rarer form of GPIIIa, P1A2, carries a point mutation or single nucleotide polymoφhism at base 192, changing a codon from CTG to CCG thereby causing a leucine to proline substitution at amino acid position 33 (Newman et al., J. Clin. Invest. 55:1778-1781 (1989)). The GPIIb polypeptide is the larger component of the GPIIIa/GPIIb complex and includes two disulfide-linked subunits of 137 amino acids and 871 amino acids respectively. Two antigenic forms of GPIIb, Bak a and Bak b , have been described and can be distinguished using specific antisera. The rarer form of GPIIb, Bak , has been shown to have a T to G point mutation that results in an isolucine to serine substitution at amino acid position 843 (Lyman et al., Blood 75:2343-2348 (1990)). The presence of the C-nucleotide at position 192 of GPIIIa DNA can be readily detected by PCR amplification of a region bracketing position 192, followed by Mspl digestion of the amplification products, as the C-substitution at that site creates a new Mspl restriction site. Alternatively, the sequence at the variance site can be determined using sequencing of the amplification products to identify the nucleotide at the specified position. The variant GPIIb forms can be detected using similar techniques as for GPIIIa variants by determining the nucleotide at position 2622 (corresponding to amino acid position 843). It was found that each of the rarer variant sequences described above for GPIIIa and GPIIb conelated with the development of Alzheimer's disease, both separately and together. The variant GPIIIa and GPIIb alleles were found in Alzheimer's patients with an odds ratio of 1.82 and 1.45 respectively as compared to the wild-type alleles. Further, the two variant alleles were found to occur together in Alzheimer's patients as compared to normal subjects with an odds ratio of 3.74. GPIIIa and GPIIb thus provide examples of variant sequences which result in amino acid substitutions in encoded polypeptides, where the variant sequences are conelated with the development of a disease or condition. Similarly, other sequence variances in GPIIIa and GPIIb can be anlyzed. In GPIIIa, these include for example, arg62term, leul 17tφ, as l 19tyr, serl621eu, arg214gln, arg214tip, cys374tyr, tro407ala, arg636cys, and ser752tro. For GPIIb, the additional variance include leul83tro, gly242asp, the289ser, glu3241ys, erg327his, gly418asp, arg553trm, ile565thr, gln747tip, and ser870term. The possible conelation of these variances with the development of cardiovascular disease can also be determined as for the previously identified variances. Example 33 β2-adrenergic Receptor Polvmoφhisms and Affects on Outcomes of Congestive Heart Failure Several variances have been identifies in the gene encoding β-adrenergic receptor. Some of the variances have been shown to affect receptor physiology, and may account, in part, for inteφatient variation in the development, progression, and treatment outcomes of congestive heart failure. In a recent study, β-adrenergic receptor polymoφhisms were conelated with clinical course of congestive heart failure (CHF) patients. Three amino acid polymoφhisms identified in the β- adrenergic receptor were used to stratify patients diagnosed with CHF: Gln27Glu (Glu27 is associated with reduced receptor down-regulation), ArglόGly (Gly 16 is associated with increased down-regulation), and Thrl64Ile (Ile 164 is associated with decreased coupling of the receptor with its GTP-binding protein). The allele frequencies of these polymoφhisms were similar in normal and CHF patients, suggesting that the polymoφhisms are not important in the etiology of CHF. In a comparison of patients with the 164Ile variance versus the 164Thr variance (more common allele), the investigators determined that survival was greater for the 164Thr variance groupover the study period; unadjusted relative risk was 4.81 as compared to 3.69. The follow-up survival for individuals with the 164Ile genotype was 42% as compared with 76%> for the 164Thr individuals. Although at the time of enrollment the two groups had similar clinical symptoms and other characteristics, there appeared to have been speedier decline in the patients with the Ile 164 genotype. An analysis of the other two polymoφhic sites (positions 16 and 27), revealed no detectable difference. These data taken together suggest that certain polymoφhisms in pharmacologically and/or physiologically relevant proteins may influence the course of disease progression, and establishes the importance of determining genotypic differences to be able to identify individuals with specific genotypes in which earlier aggressive therapy would be wananted. Example 34 Anthracvcline Antibiotics I. Description of Anthracycline Antibiotics The anthracyclines are among the most important cancer drags due to their broad effectiveness against various carcinomas, sarcomas, leukemias and lymphomas.The anthracycline antibiotics, daunorubicin and doxorubicin, were initially isolated from Streptomyces peucetiousand have been in clinical use for decades. As a result of the effectiveness of these compounds hundreds of analogs have been produced synthetically or isolated from various microorganisms, including the recently developed compound idarubicin. Other recently isolated anthracyclines include DA- 125, moflomycin, SM-5887, IT-62-B, WP631, KRN8602, AD198 and MX2 (all of which show antitumor activity), as well as 3'-O- demethyl mutactimycin, 4-0,3 '-O-didemethyl mutactimycin and nothramicin (isolated from non-Streptomyces species). Many other compounds are known to those skilled in the art. These compounds can intercalate into DNA, and interfere with DNA replication and RNA transcription by steric action and by interfering with topoisomerase II function. The anthracyclines are associated with single- and double-stranded DNA strand scission, as well as production of radicals including superoxide, which induce damage to cellular components, including indirect DNA and protein alkylation. Free radical generation is dependent on cellular cytochrome p450 and quinone or hydroxyquinone moieties on adjacent rings in the anthracene backbone. Anthracyclines also bind membranes and alter membrane fluidity and transport, perhaps by radical formation. The anthracyclines are metabolized via hepatic oxidation to polyalcohols , with subsequent deglycosylation, formation of glucuronides and excretion into both bile and urine. II. Current Indications for Anthracycline Antibiotics and Derivatives Anthracycline antibiotics and derivatives are cunently used to treat a broad spectrum of neoplastic diseases including, leukemias, lymphomas, sarcomas, neuroblastomas and cancers of the breast, thyroid, lung, stomach, and urogenital tract (endometrium, ovary, testicle). The synthetic, less cardiotoxic anthracyline derivative, mitoxantrone is indicated for acute nonlymphocytic leukemia (ANLL), and is also active against non-Hodgkins lymphomas and breast cancer. III. Limitations of Current Therapies Utilizing Anthracycline Derivative Antibiotics The clinical use of anthracycline derivatives is circumscribed by dose- limiting neutropenia and mucositis, and by cardiac toxicity, including an acute syndrome characterized by conduction and rhythm abnormalities or pump failure, and a chronic syndrome of cardiomyopathythat can lead to congestive heart failure. Anthracyclines are administered intravenously on various schedules. In the past dosing was by iv bolus every 3 or 4 weeks, but it has come to be appreciated that repeated small doses or continuous iv infusion is safer, especially in terms of cardiac toxicity, with no evident loss of efficacy. A major limitation of this family of compounds is that a cumulative dose in excess of 550 mg/square meter puts patients at risk of cardiomyopathy and resulting congestive heart failure. In the range of 1 to 10%) of patients receiving a cumulative dose of at least 550 mg/square meter develop cardiomyopathy. Cariomyopathy develops in a smaller fraction of patients receiving lower cumulative doses.All clinically tested anthracyclines are effective against some lymphomas and leukemias. Doxorubicin is also effective against certain solid tumors, such as those of the breast and lung, and a wide range of sarcomas. Doxorubicin is the drug of choice for the treatment of metastatic thyroid tumors. It is known to produce severe local toxicity to previously inadiated tissues, even when the two therapies are not administered contemporaneously. Although mitoxantrone treatment produces less nausea, vomiting, and alopecia than doxorubicin, acute myelosuppression and mucositis are frequently observed. IV. Impact of Genotyping on Drug Development for Anthracyclines The effectiveness of the anthracycline class of chemo therapeutics is believed to be related to its ability to cause DNA damage, either by direct free-radical damage or through the disruption of topoisomerase II function. Other effects of free radicals, which attack a wide range of important biological targets, are also likely to be important. Resistance to treatment can occur through several mechanisms, some of which are well studied. For example, (1) decreased levels of Topoisomerase II are frequently observed in anthracyline resistant cells. Levels of Topoisomerase II (including TOP2 alpha and TOP2 beta genes) could be influenced by sequence variation or (in cancer tissue) by loss of heterozygosity , affecting inteφatient variation in response or toxicity. (2) Topoisomerase III and Topoisomerase III beta levels or function may modulate response to anthracyclines. Anthracyline resistance in experimental systems is often mediated by drag efflux proteins, including the multidrug resistance transporter MDRl and the multidrag resistance associated protein 1, as well a possibly other members of the ATP -binding cassette family (MRPs 1 through 6). (3) Variation in levels or function of phase I oxidative metabolism, glutathione-S-transferase and peroxidase, , lung resistance related protein (LRP), breast cancer resistance protein (BCRP), and topoisomerase II. As anthracyclin action is exerted through DNA damage, enzymes involved in the detection and repair of DNA damage (such as members of the xeroderma pigmentosum complementation groups (XP), the excision repair cross- complementation groups (ERCC), p53, the ataxia telangiectasia pathway could also affect efficacy and toxicity. Polymoφhisms in any of these gene pathways that affect the enzymatic activity of a gene product, the amount of a gene product, or the interaction of a gene product with anthracycline derivatives would be expected to affect either the initial response to treatment or systemic toxicity. There is also evidence that anthracyclines are probably less effective in MSI tumors; resistance attributable to impaired ability to detect DNA damage and thence activate apoptosis, and to increased mutation rate. Impairment of essential free fatty acid metabolism is believed to play a role in therapeutic effect, as well as cardiac toxicity since administration of L-carnitine has been shown to partially reverse cardiac toxicity. The levels of iron, which serves as a mediator of free-radical damage, are also an important factor in cardiac toxicity, since treatment with the iron chelator , ADR-529 is protective. The levels of enzymes controlling oxidative stress, such as superoxide dismutase, are also known to be important determinants of anthracycline toxicity. Doxorubicin and its metabolite doxorabicinol are known to inhibit the action of ion pumps known to be involved in cardiac muscle contraction such as the sarcoplasmic reticulum calcium- dependent ATPase, SERCA1. Polymoφhisms gene products involved in fatty acid metabolism, iron metabolism, calcium concentration, and free radical quenching that alter total enzymatic activity would all be expected to be predictive of toxicity, particularly if the polymoφhism is in a gene product whose expression is restricted to or enriched in cardiac tissue (i.e. SERCA1). As an extension, any polymoφhism conelated with reduced cardiac function, either manifest or occult, might predispose patients receiving anthracycline antibiotics or derivatives to cardiac toxicity. Example 35 Antimicrotubule Agents I. Description of Vinca and Taxus Alkaloids and Derivatives The vinca alkaloids, originally extracted from the periwinkle, Vinca rosea, and the taxus alkaloid, taxol, isolated from the Western yew, Taxus brevifolia, exert their pharmaceutical effects by promoting the destabilization or polymerization, respectively, of microtubule structures involved in cell architecture and division. The vinca alkaloids, and vinorelbine, a newer, better tolerated derivative, share a heterodimeric, heterocyclic stracture and bind tubulin with a 1 : 1 stoichiometry. Binding prevents mitotic spindle function and normal chromosome segregation, leading to apoptotic cell death. Colchicine, an alkaloid extracted from the autumn crocus, Colchicum autumnale, shares this mechanism of action, but its use is restricted to the treatment of gout.. Taxol, and its more potent derivative, docetaxel, are complex teφenoid compounds that contains a taxane ring nucleus. Treatment with taxus alkaloids causes the accumulation of microtubule aggregates, leading to abnormal cell moφhology and anest of cell division during mitosis. Prior treatment with doxorubicin, which antagonizes cell cycle progression, can reduce therapeutic benefit and increase toxicity. Discodermolide, a polyhydroxylated alkatetraene lactone, binds tubulin at the same location as taxol, causing tubule aggregation in an analogous manner. Epothilone A and B, isolated from the myxobacterium Sorangium cellulosum, and desoxyepothilone B, a less toxic derivative, are also known to exert their antiproliferative effects through microtubule stabilization. Rhizoxin, combretastatin A4, and amphethinile are other recently identified natural product microtubule inhibitors. II. Current Indications for Antimicrotubule Agents The vinca alkaloids differ significantly in their antitumor effects as well as actions on normal tissues. Nincristine is a standard component of regimens for treating pediatric leukemias and solid tumors and is frequently used to treat adult lymphomas. Vinblastine is utilized primarily for the treatment of lymphomas, neuroblastoma, breast and choriocarcinomas, and as a second-line therapy for various solid tumors. The most important use of vinblastine is conjunction with bleomycin and cisplatin in the curative therapyt of testicular cancer. Vinorelbine has been successfully used as a monotherapy to treat non-small cell lung cancer and breast cancer. Treatment is via weekly intravenous infusion until dose-limiting toxicity is observed or triweekly during vinblastine treatment of testicular cancer. III. Limitations of Current Therapies Utilizing Antimicrotubule Agents Vinblastine and vinrelbine cause leukopenia and vincristine can cause hypertension through inappropriate vasopressin secretion. Alopecia occurs in approximately 20% of patients receiving vincristine, but is reversible, often without cessation of treatment. All three vinca alkaloids can cause neurotoxicity, but vincristine has predictable cumulative effects. Neurotoxic symptoms include numbness and tingling of the extremities, loss of deep tendon reflexes, and muscle weakness, the latter prompting suspension or reduction of dosing. Neutropenia and mucositis are frequently observed during taxol treatment, with peripheral stocking-glove sensory neuropathy seen as the dose-limiting toxicity. Many patients experience myalgia for several days after dosing. Dosing can be via short (1-6 hour) or long (72-96 hour) infusions. Pretreatment with corticosteroids or antihistamines has been used to avert hypersensitivity reactions seen with shorter dosing schedules and mucositis is a frequent complication of longer schedules. Paclitaxel and docetaxel undergo oxidative hepatic metabolism via CYP2C8 and 3 A4 and are particularly toxic in patients with reduced liver function. IV. Impact of Genotyping on Drug Development for Antimicrotubule Agents The effectiveness of antitubule agents is related to their ability to prevent mitosis by affecting spindle assembly and disassembly, by preventing secretory vesicle translocation, and by perturbing normal cellular architecture . Resistance to treatment can occur through alterations in microtubule-associated protein 4 (MAP4), beta tubulin (TUBB), multidrag resistance transporter (MDRl), Bcl-X/Bcl-2 binding protein (BAD), and tyrosine kinase type receptor HER2/NEU. Polymoφhisms in any of these gene pathways that affect the enzymatic activity of gene product, amount of gene product, or interaction between gene product and antimicrotubule agent would be expected to affect initial response to treatment. Since the vinca and taxol classes of antimicrotubule agents have opposing effects on microtubule polymerization state, resistance to one class of agents is often associated with collateral sensitization to the other. Analogously, tubulin or MAP4 polymoφhisms that stabilize microtubules would be expected to respond better to taxol therapy than to vinca alkaloid therapy. Microtubules are composed of alpha and beta tubulin subunits and each is encoded by a 15-20 member, dispersed, pseudogene-containing, multigene family restricted in expression to a subset of tissues. For instance, alpha- 1 and beta-2 tubulins are restricted to the testis. Polymoφhisms in these subunits would be expected to affect primarily the efficacy of antimicrotubule agents for the treatment of testicular cancers. Taxol derivatives are metabolized primarily by cytochrome P450s CYP2C8 and 3A4. Polymoφhisms that affect the enzymatic activity or amount of these gene products would be expected to be predictive of toxicity, especially hepatic and neural. Alpha-3, beta-4, and beta-5 tubulin subunits are restricted to differentiated neural tissues and polymoφhisms in these genes affecting protein levels or microtubule agent binding might be predictive of neural toxicity. Example 36 Topoisomerase Inhibitors I. Description of Topoisomerase Inhibitors Etoposide and teniposide are two semisynthetic glycoside derivatives of podophyllotoxin, a toxic alkaloid from the mayapple, Podophyllum peltatum. These compounds have a similar spectrum of antitumor activity and exert their cytotoxic effects by their interaction with cellular topoisomerase II, an enzyme required during DNA replication. The complex between DNA topoisomerase II and etoposide or teniposide is capable of double stranded DNA strand scission, but not strand exchange or ligation. The resulting DNA damage initiates apoptotic cell death. The bulk of administered etoposide is excreted via the kidney unchanged whereas approximately 80% of teniposide is recovered from urine as metabolites. Amsacrine, 4-(9-acridinylamino)-N-(methanesulfonyl)-m-anisidine, is an additional inhibitor of DNA topoisomerase II in clinical trials as part of multiagent induction chemotherapeutic regimen for acute myelogenic leukemias. Topotecan and irinotecan, derivatives of camptothecin, originally isolated from the bark of Camptotheca acuminata, bind DNA topoisomerase I and cause DNA fragmentation and apototic cell death in a manner entirely analogous to the podophyllotoxins. Topotecan is also oxidized by liver cytochromes prior to being excreted via the kidneys. Irinotecan is a prodrug and requires activation by a carboxylesterase to its active metabolite, SN-38. Elimination after hepatic oxidation is via biliary excretion. II. Current Indications for Topoisomerase Inhibitors Etoposide and teniposide are active against a broad spectrum of tumor types including testicular, small cell lung, various lymphomas, acute granulocytic leukemia, and Kaposi's sarcoma. When combined with cisplatin and bleomycin for testicular tumors and with cisplatin for small cell lung carcinomas, these compounds become the treatment of choice. Administration can be achieved orally (etoposide), but the prefened route is intravenous, with dosing repeated at 2 to 3 day intervals. Teniposide is better tolerated in patients with compromised renal function than is etoposide. Topotecan is used primarily for the treatment of ovarian and small cell lung carcinomas and is administered via daily intravenous infusion for 3 or more days. Irinotecan is indicated for the treatment of colorectal cancer and is administered by slow intravenous infusion once weekly for 4 weeks, followed by a two week recovery period. This dosing cycle is repeated until the desired therapeutic endpoint is reached. III. Limitations of Current Therapies Utilizing Topoisomerase Inhibitors The dose-limiting toxicity for etoposide is leukopenia which peaks approximately two weeks after the onset of treatment. Nausea, vomiting, stomatitis, and dianhea occur in about 15%> of patients receiving etoposide intravenously and 55%o who receive it orally. Hepatic toxicity, phlebitis, dermatitis, and reversible alopecia are also observed. Etoposide treatment of childhood acute lymphoblastic leukemia (ALL) has been linked with a secondary myeloid/lymphoid or mixed- lineage leukemia involving a translocation event at 1 lq23, a region involved in pluripotent stem cell differentiation, that appears 1 to 3 years subsequent to therapy. Teniposide is also used for the treatment of refractory ALL and is associated with myelosuppression, nausea, and vomiting. Undesired effects of topotecan and irinotecan treatment are similar to those of topoisomerase II inhibitors. Nausea associated with irinotecan is often severe enough to require treatment. IV. Impact of Genotyping on Drug Development for Topoisomerase Inhibitors Resistance to topoisomerase I and II inhibitor therapy can be caused by alterations in topoisomerase activity, topoisomerase levels, or in inhibitor accumulation (MDRl). Multiple amino acid polymoφhisms have been reported for both topoisomerases (Table 3) that could potentially affect enzyme activity, drag binding, or protein levels. It has also been shown that cell lines lacking functional Ku86, a protein involved in double-stranded DNA break repair, are hypersensitive to etoposide, suggesting that polymoφhisms affecting the levels or activity of this protein in normal tissues or tumor might also be an important determinants of toxicity and efficacy, respectively. A serious undesired outcome of etoposide treatment of ALL is the development of therapy-related, secondary nonlymphocytic leukemia. Studies have shown that even though etoposide is a known mutagen, mutation rates are not significantly enhanced during treatment, suggesting that patients that acquire secondary leukemia have a natural predisposition . The appearance of secondary acute myelomonocytic or promyelocytic leukemia is related to DNA translocations involving the 1 lq23 region that contains the Drosophila trithorax homeobox transcription factor homo log MLL or thel5q22 region that contains the PML gene, whose product contains transcription factor consensus elements. The latter translocation produces a hybrid protein containing the DNA binding portion of the PML protein fused to the hormone binding portion of the retinoic acid receptor alpha protein. The 1 lq23 region is known to the contain folate-sensitive fragile site FRA1 IB, suggesting that polymoφhisms in genes involved in folate metabolism may play a contributing role to the appearance of secondary leukemia. Polymoφhisms in genes involved in non-pathological DNA rearrangements such as immunoglobulin and T-cell receptor reanangements (i.e. ataxia telangiectasia, DNA ligase, Ku86, Ku70, etc.), that alter the amount or activity of their gene product, represent candidate genes for association with susceptibility to etoposide treatment- related, secondary leukemia. Example 37 Platinum Coordination Complexes I. Description of Platinum Coordination Complexes The cytotoxic nature of platinum compounds was first observed in E. coli in 1965 and traced to inorganic platinum adducts with ammonium and chloride ions. Of the thousands of platinum derivatives that have been synthesized and tested, cisplatin (cis-diaminodichloroplatinum II) and carboplatin (diaminocyclobutanediacarboxylatoplatinum II), have proven most valuable in the clinic. These platinum complexes seem to enter cells by diffusion and are activated by hydrolysis to a hydrated, cationic diaminoplatinum II species believed to react with nucleic acids and proteins. The N7 position of guanine is particularly prone to modification and intrastrand and interstrand DNA cross-links between proximal guanine bases and adenine and guanine bases are formed. These adducts inhibit DNA replication and transcription, leading to apoptotic cell death. The bulk of compound is excreted unchanged in the urine. II. Current Indications for Platinum Coordination Complexes Cisplatin produces good response in a broad range of cancers including those of the bladder, head and neck, endometrium, and small cell lung carcinoma. It has been used alone, or in combination with paclitaxel , cyclophosphamide, or doxombicin for the treatment of ovarian cancers and is curative in combination with bleomycin, etoposide, and vincristine in about 85% > of testicular cancers. Platinum compounds are also used as sensitizers for radiation therapy. Administration is via intravenous infusion subsequent to hydration with saline to minimize renal toxicity. Dosing regimens are 20 mg/m 2 for five consecutive days or 100 mg/m 2 given once every four weeks. III. Limitations of Current Therapies Utilizing Platinum Coordination Complexes Marked nausea and vomiting occur in almost all treated patients, but can be controlled with ondasteron or corticosteroids. Renal electrolyte wasting is a frequent occurrence and may lead to tetany and/or seizures. As a result, it is recommended that plasma magnesium levels in patients receiving platinum compounds are routinely monitored. The most serious adverse effects of platinum coordination compound therapy are neurological. Tinnitus and hearing loss in the high frequency range become more frequent and severe with repeated doses and tend to be more pronounced in children. Cisplatin induced neuropathies were first recognized in the early 1980s. Early indications are reduced decreased vibratory sensibility in toes, loss of ankle jerks, and loss of sural nerve response. Peripheral nerves may show axonal degeneration and secondary myelin breakdown. Cisplatin- induced peripheral neuropathy may worsen after discontinuation of treatment, can linger for months to years after cessation of treatment, and can result in death. IV. Impact of Genotyping on Drug Development for Platinum Coordination Complexes Resistance to platinum compound therapy is generally acquired through the selection of mutant forms of the tumor suppressor protein p53. This protein is involved in the detection of DNA damage and DNA damage-related cell-cycle anest and apoptosis. Tissue culture studies have shown that these mutants appear to arise spontaneously and become enriched only after platinum treatment. Numerous polymoφhisms in the p53 gene have been reported and any that reduce protein amounts or DNA binding activity would be expected to conelate with lower treatment efficacy. As the cytotoxicity of platinum coordination complexes are directly related to their charge and ability to alkylate DNA, enzymes involved in the detection and repair of DNA damage (such as members of the xeroderma pigmentosum complementation groups (XP), the excision repair cross- complementation groups (ERCC), Ku86/70, etc.) could also affect efficacy and toxicity. Elevated levels of some of these enzymes has been found in platinum- resistant ovarian tumor samples. Polymoφhisms in any of these gene pathways that affect the enzymatic activity of gene product, the amount of gene product, or the interaction of gene product with platinum-induced DNA adducts would be expected to affect either the initial response to treatment or systemic toxicity. Neural platinum toxicity appears to be mediated by free, inorganic platinum. Platinum accumulation is greatest in dorsal root ganglia and lowest in neural tissues protected by the blood-brain barrier, consistent with primarily peripheral toxicity. Several agents including glutathione, metallothionein, nerve growth factor, neurotrophin 3, glutamate, and S-2-(3-aminopropylamino)-ethylphosporothioic acid (WR 2721) have shown promise in animal models as a neuroprotectants. Glutathione is synthesized from the amino acids cysteine, glutamate, and glycine by the consecutive action of gamma-glutamylcysteine synthetase and glutathione synthetase, encoded by single-copy genes and expressed ubiquitously. Polymoφhisms in the genes required for glutathione synthesis would be expected to affect primarily the efficacy of platinum compounds. In contrast, metallothioneins are encoded by a 10 to 12 member multigene family. Metallothionein 3 expression is restricted to neural tissue and polymoφhisms could be associated with neural toxicity. Polymoφhisms in these genes influencing protein levels or activity would be expected to be important predictors of neural toxicity. Example 38 Steroid Hormone Derivatives I. Description of Steroid Hormone Derivatives and Related Agents Steroidal agents include adrenocorticosteroids and analogs, agents such as aminoglutethimide that regulate the levels of adrenocorticotropic hormone (ACTH), antiestrogens such as tamoxifen, progestins such as hydroxyprogesterone caproate and megestrol acetate, antiandrogens such as flutamide, and gonadotropin releasing hormone (GNRH) and analogs such as goserelin and leuprolide, that decrease secretion of leutenizing hormone (LH) and follicle stimulating hormone (FSH) by the pituitary after long term administration. Depression of FSH and LH levels, in turn, decreases circulating levels of testosterone to castration levels in men and estrogen levels in women to postmenopausal. Flutamide, tamoxifen, panomifene, and raloxifene are recently developed androgen and estrogen receptor modulators that block the activation of transcription required for the maintenance and function of hormone-responsive tissues. In the absence of androgen- or estrogen-stimulated transcription, proliferation of metastatic prostate and breast cancers is greatly reduced. These agents are usually used in conjunction with cytotoxic chemotherapeutic agents such as alkylating agents, platinum compounds, anthracylines, topoisomerase inhibitors, and microtubule polymerization/depolymerization modulators. Tamoxifen, cyclosporin A, and verapamil, have all received great clinical attention due to their ability to reverse MDRl -associated drag resistance. II. Current Indications Steroid Hormone Derivatives and Related Agents Steroidal agents and agents that indirectly affect steroid levels are used against a rather limited number of neoplastic diseases. Corticosteroids such as dexamethasone and prednisone are used alone or in combination with vincristine and anthracylines, with or without methotrexate and asparginase, for the treatment of acute and undifferentiated lymphoblastic leukemia, due to their ability to block lymphocyte proliferation. Amino glutathimide treatment of metastatic breast cancer with concomitant hydrocortisone supplementation has been largely supplanted by tamoxifen, which acts directly to limit estrogen receptor signaling. The orally available aromatase inhibitors vorozole, letrozole, exemestane, formestane, and anastrozole are cunently in development as second-line therapies for the treatment of advanced breast cancer. Tumors stemming from endocrine tissues and steroid-responsive tissues frequently retain steroid hormone responsiveness initially. This is trae for tumors of breast, prostate, testicular, ovarian, and endometrial origin, as well as other less frequent cancers. Localized prostate cancer is often curable with surgery and/or radiation therapy, but androgen-deprivation therapy becomes the primary hormonal treatment for metastatic disease. Treatment leads to a reduction in symptoms, but is considered palliative since tumors eventually become insensitive. Reduction in serum androgen can be achieved by bilateral orchiectomy, generally reserved for older patients, GNRH analog treatment, and flutamide treatment alone or in conjunction with GNRH analogs. Flutamide decreases the original flare of prostate tumor growth as a result of transient LH increase in GNRH analog monotherapy. Leuprolide and goserelin are administered via intramuscular and subcutaneous injection and are released slowly into the bloodstream; both agents are also indicated for the treatment of breast and endometrial cancers. Flutamide is administered orally, generally three times daily and is cunently approved only for use in combination therapy. Tamoxifen has replaced diethylstilbesterol as the hormonal treatment of choice for estrogen receptor-bearing breast cancers. Both tamoxifen and raloxifene have found recent application for the prevention of postmenopausal decreases in bone density. Tamoxifen is administered by mouth twice daily and is often used for prolonged periods in the context of adjuvant therapy following the initial treatment of primary breast cancers. The drag is metabolized by oxidation and formation of glucuronides and excreted into the stool via bile. III. Limitations of Current Therapies Utilizing Steroid Hormone Derivatives and Related Agents As a class, the hormonal agents are extremely well tolerated. Leuprolide, goserelin and flutamide treatment can produce some of the symptoms of menopause including hot flashes, as well as a loss of libido and impotence, but none of these complications is dose limiting. Doses of tamoxifen 20-times the recommended dose are associated with retinal degeneration, but standard doses produce symptoms similar to menopause, weight gain, and gastrointestinal disturbances, none of which is dose limiting. The aromatase inhibitors produce similar side effects. Prolonged use of tamoxifen, such as during adjunct treatment, chemoprevention, or for prevention of postmenopausal osteoporosis, has been linked to the development of endometrial cancers. Patients receiving the standard dose of tamoxifen for two years are twice as likely to develop endometrial cancer than untreated controls. IV. Impact of Genotyping on Drug Development for Steroid Hormone Derivatives Antiestrogen therapy in the context of chemotherapy is generally indicated only for estrogen-receptor bearing tumors. Estrogen receptor polymoφhisms that affect protein levels, DNA or estrogen binding, or interaction with other transcription factors would be expected to conelate with treatment outcome. More- specifically, decreases in any of these parameters should decrease efficacy. Expression of epidermal growth factor receptor (EGFR) and tyrosine kinase-type cell surface receptor HER2/NEU conelates with poor response to tamoxifen even in estrogen receptor positive tumors, but neither EGFR or HER2/NEU appear to be amplified during the course of treatment. As noted above, HER2/NEU expression also conelates with poor prognosis during treatment with antimicrotubule agents, suggesting that ectopic or enhanced expression of growth factor receptors can overcome the growth inhibition caused by cytotoxic agents. Steroid hormone derivatives are metabolizes via cytochrome P450 and flavin containing monooxygenases and by conjugation to sulfates and glucuronates for elimination. Oxidative metabolism of tamoxifen by liver microsomal fractions has been well characterized and involves the formation of 4-hydroxyl, 4 '-hydroxyl, N- oxide, N-desmethyl, 3,4-dihydroxyl, and 3,4-epoxyl derivatives. The latter, reactive epoxide species is formed in large amounts in rats, but not mice or humans, and is thought to account for increased liver carcinogenesis in this species. Formation of the N-oxide is believed to be mediated by a flavin containing monooxygenase (FMO), while other reactions appear to be carried out by cytochromes, especially CYP3A4 (N-demethylation) and 2D6 (4-hydroxylation). Polymoφhisms in genes encoding FMO enzymes 1 and 3-5 (FMO2 is inactive), or CYP3A4 and 2D6, or sulfotransferases, or glycosyltransferases that affect protein amount or activity would be expected to influence efficacy by increasing or decreasing elimination. Polymoφhisms in the gene(s) encoding the enzyme(s) responsible for 3,4- epoxide formation that affect protein amount or activity would be expected to conelate with the mutagenic effects of tamoxifen, especially with the occunence of treatment-related endometrial cancers. Example 39 Inhibitors of Signal Transduction I. Description of Signal Transduction Inhibitors Signal transduction is the processes whereby external cellular stimuli are converted into changes in protein expression. The usual chain of events is (1) interaction of a ligand with a cell surface receptor, (2) ligand-induced changes in the three-dimensional stracture of the receptor, including dimerization, that are transmitted to the cytoplasmic face of the plasma membrane, (3) transmission of these changes to transcription factors in a complex, multienzyme cascade that generally involves a change in the phosphorylation state of enzymes in the cascade, modulating their activity or ability to interact with other proteins in the cascade, and (4) modulation of the availability or activity of gene specific transcription factors through changes in phosphorylation status, oligomeric state, cellular localization, synthesis, or degradation. Changes in the signal transduction process play a pivotal role in the etiology of neoplastic transformation and disease. The enzymes involved are usually members of a closely-related, multienzyme family, that display complex temporal regulation during development and are differentially expressed in normal tissues. Recent advances in understanding the molecular biology of these pathways and technical breakthroughs in both combinatorial chemistry and high-throughput screening have added novel, synthetic agents to the small number of known, naturally occurring signal transduction inhibitors. Cunent signal transduction inhibitors affect phosphorylation and dephosphorylation steps associated with receptor and soluble kinases as well as protein phosphatases. Many subtype selective and nonselective inhibitors of protein kinase C (PKC) were initially isolated from natural sources. These include the protein kinase C inhibitors staurosporin , herbimycin A, lavendustin A, and erbstatin, originally isolated from various Stremptomyces species; the tyrosine kinase inhibitors emodin, cytovaricin B, angelmicin B, geldanamycin, and genistein isolated from Talaromyces, Streptomyces, and Lupinus species; the the phosphatidylinositol 3 -kinase inhibitor wortmannin isolated from Talaromyce flavus; and the protein phosphatase inhibitor okadaic acid isolated from the black sponge, Prorocentrum oncauum. Erbstatins, which bind the ATP -binding site of PKC, also have activity against topoisomerases I and II. Numerous synthetic derivatives of these compounds that enhance stability and availibility, as well as novel compounds, have been produced and assayed in biological systems more recently. These include the protein kinase C inhibitors L86-8275, H7, LY333531 (Eli Lilly), safignol (Sphinx/Eli Lilly) and CGP41251(Ciba-Geigy); the tyrosine kinase inhibitors SU5416 (Sugen), specific for VEGF receptor-associated tyrosine kinase; ZM 252868, ZD1839 (Zeneca), PD153035 (Parke-Davis), and CGP 52411 (Ciba-Geigy), specific for EGF receptor-associated tyrosine kinase, CEP-701 (KT- 5555) and K252a, specific for TRK-type receptor-associated tyrosine kinase, KN- 62, specific for CaN'calmodulin-dependent protein kinase II; tyrosine kinase inhibitors of the tyφhostin class, as exemplified by AG1714 (4-nitrobenzylidene malononitrile ); the phosphatidylinositol 3 kinase inhibitors of the 3-deoxy-D- myo inositol 1 -phosphate/ 1-phosphonate class; the protein serine/threonine phosphatase inhibitor endothall; and the tyrosine phosphatase inhibitor bis(maltolato)oxovanadium(IV). Bryostatin, a macrolactone originally isolated from marine sponges, inhibits signal transduction through an as yet unknown mechanism, but likely to involve PKC isozymes. The growth factor 1 family of transmembrane receptors, including epidermal growth factor receptor (EGFR) and members of the ERB-B family, are overexpressed in a wide variety of solid tumors, particularily squamous cell carcinomas of the head and neck, lung, and cervix. The oncogene CBL, implicated in pre/pro B-cell lymphomas, and its cellular counteφart C-CBL, mediate the recycling/degradation of EGFR members. EGFR members are already important therapeutic targets and C-CBL represents an important future drag target. Mutations in members of the RAS G protein superfamily are the most common initiators of neoplastic transformation, occurring in approximately 40% of colorectal cancers, 90%> of pancreatic cancers, 30%> of lung adenocarcinomas, and 25%o of acute myeloid leukemias. Inhibitors of RAS farnesylation are cunently in clinical trials. RAS control of cell cycle decisions and of transcription factor phosphorylation by Janus kinase (JUNK) is mediated by at least four distinct signaling pathways including the mitogen-activated protein kinases (MAPKs) and phosphatidyl inositol 3 kinases (PIK3s). Inhibitors designed to members of these multigene families are in early development, show great promise. Silymarin, a flavonoid antioxidant isolated from milk thistle, is a MAPK modulator and has shown great efficacy in the chemoprevention of skin cancer in a mouse model. II. Current Indications for Signal Transduction Inhibitors Many of the signal transduction inhibitors listed above show promising antineoplastic activity in tissue culture and animal models, but only a few compound are cunently in early clinical development. The staurosporine derivative UCN-01 is being tested for activity in advanced or refractory solid tumors, lymphoproliferative disorders, and lymphoid malignancies and SU5416 is being tested in combination therapy with 5-fluorouracil and leucovorin for metastatic colorectal cancer. Bryostatin is in early clinical trials alone, or in combination with cisplatin and paclitaxel for refractory and advanced malignancies including unresectable stomach, esophagus, anus, prostate, or non-small cell lung cancer. It is anticipated that upon further development, members of this class of agents will be indicated for the treatment of a broad range of neoplastic diseases. The phosphatidylinositol 3 kinase inhibitor, wortmannin, has been shown to be active as a radiosensitizer in vitro, suggesting potential utility in the radiation therapy of tumors. III. Impact of Genotyping on Drug Development for Signal Transduction Inhibitors Activation of the MAPK pathway has been shown to conelate with poor prognosis for prostate cancers as well as resistance to androgen ablation therapy. In both colorectal and breast tumors, expression in malignant tissue was elevated while expression in sunounding tissues was normal. The oncogenic potential of MAPKs has been demonstrated in a mouse model, where a lysine to glutamate mutation appears to cause cellular transformation. These findings all highlight the important role of the MAPK pathway in the initiation and progression neoplastic disease. There is also evidence for the direct involvement of the PKC pathway in neoplastic disease: a point mutation at position 294 of alpha-protein kinase C, leading to an aspartic acid to glycine substitution, has been linked to pituitary tumor invasiveness. Overexpression of EGFR has been strongly associated with the transition from superficial to invasive bladder cancers. Enhanced cellular motility is a prerequisite to invasion and can be inhibited in an in vitro model by wortmannin, a specific inhibitor of phosphatidylinositol 3 kinase, implicating this class of enzymes in bladder cancer progression. The structurally related ataxia telangiectasia gene product, when mutated, causes a predisposition to malignancy. Polymoφhisms in genes encoding receptors and proteins of the signal transduction pathway as detailed above and in Tables 1-3, or related proteins yet to be discovered, which influence protein amounts, activity, interaction with other proteins or drugs, would be expected to have prognostic value for risk assessment, treatment efficacy, and toxicity. Example 40 Inhibitors of Cell Cycle Control a) Description of Cell Cycle Control Inhibitors The control of cell cycle progression and division is through a complex signaling pathway, such as described above, at the heart of which are the cell division cycle (CDC) proteins, CDC kinases (CDCKs), cyclins, cyclin-dependent kinases (CDKs), and cyclin-dependent kinase inhibitors. All exist as members of multigene families that show temporally regulated and tissue-specific expression. Ubiquitin ligases and the ubiquitinated protein proteolysis pathway are involved in modulating cyclin levels during the cell cycle. Interest in this class of macromolecules as drug development targets was sparked by the observation that the level of various cyclin-dependent kinases and cyclin-dependent kinase inhibitors differed between normal tissues and a wide variety of tumor types and could be prognostic of treatment outcome. Low to absent levels of the cyclin-dependent kinase inhibitor IB (p27, KIP1) has been shown to be predictive of unfavorable prognosis in a variety of tumors. Ectopic expression of KIP 1 in human brain tumor cells has been shown to reverse some of the changes of neoplastic transformation. In contrast, elevated levels of the cyclin-dependent kinase inhibitor 2A (pl6, INK4, MTS1), is associated with progression and unfavorable prognosis in prostate and ovarian cancers. This protein is also the target of frequent somatic mutation. Several natural and synthetic inhibitors of CDK and CDCK function have been isolated. These include flavopiridol, butyrolactone I, and the purine derivatives aminopurvalanol, olomoucine, and roscovitine. II. Current Indications for Cell Cycle Control Inhibitors The CDK and CDCK inhibitors listed above have demonstrated efficacy in a number of transformed cell types in tissue culture, but only flavopiridol is advanced clinical development for refractory and recunent colorectal cancer, adenocarcinoma of the prostate, lymphocytic leukemia, and non-Hodkin's and mantle cell lymphomas, either as a monotherapy or in combination with taxol and cisplatinum compounds. It is anticipated that upon further development, members of this class of agents will be indicated for the treatment of a broad range of neoplastic diseases and hypeφroliferative disorders such as psoriasis and restenosis. III. Impact of Genotyping on Drug Development for Cell Cycle Control Inhibitors Expression of cyclin-dependent kinase inhibitor 1 A (p21/WAFl) is induced by the tumor suppressor protein p53 in response to DNA damage, thereby playing a direct role in mediating p53-induced Gl anest. Two polymoφhisms in the p21 gene, a serine to argenine change at codon 31 a C toT transition in non-coding sequence, show increased prevalence in prostate adenocarcinoma and squamous cell carcinoma of the head and neck. Similarly, low to absent levels of the cyclin-dependent kinase inhibitor, p27/KIPlare associated with poor clinical outcome in gastric and colorectal cancers. Cyclin DI expression levels have also been shown to correlate with progression and prognosis in non-small cell lung cancers, estrogen receptor-positive breast cancers, esophageal cancer, and gastric cancers. However, the conelation can be positive or negative, depending upon cancer type, making it likely that cyclin DI levels are not the directly responsible for neoplastic transformation in these tumors, and that they are a poor prognostic indicator for tumors in general. However, analysis of patients diagnosed with squamous cell carcinomas showed that G/G homozygotes of the silent G/A polymoφhism in exon 4 of cyclin DI tend to exhibit less differentiated tumors and have shorter remission times than G/A heterozygotes and A/A homozygotes. These findings carried over to various tumor subtypes, including laryngeal and pharyngeal. Polymoφhisms in genes encoding cell cycle checkpoint proteins, and proteins involved in cell cycle progress as detailed above and in Tables 1-3, or related proteins yet to be discovered, which influence protein amounts, activity, interaction with other proteins or drugs, would be expected to have prognostic value for risk assessment, treatment efficacy, and toxicity. Example 41 Angio genesis Inhibitors i. Description of Angiogenesis Inhibitors The utility of angiogenesis inhibitors for the treatment of solid tumors was first recognized by Folkman and colleagues in 1980. Angiogenesis, the creation of vasculature, is a process that insures that tissues and organs are adequately supplied with oxygen and nutrients and that toxic metabolites are efficiently removed. Angiogenesis involves the release of growth factor gradients by inadequately supplied tissue, response to these factors mediated by receptors in sunounding vasculature, and proteases and adhesion molecules involved in tissue remodelling. Angiogenesis and neovascularization, inappropriate or abnormal angiogenesis, can be induced by a number of pathological conditions, usually in the context of hypoxia or inflammation. As rapidly growing cell masses, solid tumors require a constant, plentiful supply of oxygen and nutrients. In larger tumors, perfusion is often inadequate, causing hypoxia and central necrosis. Various classes of compounds including inhibitors of signal transduction (i.e. LY333531), inhibitors of growth factor receptors (i.e. SU5416), protease inhibitors (i.e. KB-R7785, marimastat), and adhesion inhibitors (castanospermine) have shown activity in various models of angiogenesis and against multiple solid tumor types. Compounds showing promise in model systems or cunently in development include the peptides aplidine, vascular endothelial growth inhibitor (VEGI), brain-specific angiogenesis inhibitor (BAH), Kl-5 (kringles 1-5 of plasminogen), U-995 (shark cartilage derived), endostatin, angiostatin, an antibody against vascular endothelial growth factor, and macrophage inflammatory protein 2 (MIP2, GRO2); the steroids and teφenoids squalamine, vitamin D3, and retinoic acid; the antibiotics clarithromycin and combretastatin A4; and the synthetic compounds SU5416 (Sugen), TNP-470, COL-3, IM862, PTK787/ZK222584 (Zeneca), CT-2584, KB-R7785, LY333531 (Eli Lilly), BPHA (Shionogi), carboxyamidotriazole, 5,6-dimethylxanthenone-4-acetic acid, and alpha- difluoromethylornithine, an inhibitor of polyamine synthesis. II. Current Indications for Angiogenesis Inhibitors Clinical trials of antiangiogenesis agents are underway for a wide variety of refractory and recunent solid tumor types including Kaposi's sarcoma, non- Hodgkin's lymphoma, astrocytoma, glioblastoma, oligodendroglioma, ovarian, prostate, and renal tumors. III. Impact of Genotyping on Drug Development for Angiogenesis Inhibitors Vascular endothelial growth factor (VEGF) gene expression is increased in k-RAS transformed colorectal cells and VEGF expression is required for efficient tumor formation in nude mice but not for cell immortality. VEGF expression is associated with the progression, invasion and metastasis of colorectal cancer and overexpression of VEGF mRNA in the primary tumour is closely conelated with poor prognosis. High pretreatment serum VEGF is associated with poor response to treatment and unfavorable survival in patients with small cell lung cancer treated with cisplatin and etoposide combination chemotherapy. These findings suggest the importance of this growth factor in tumor proliferation and implicate polymoφhisms in VEGF proteins and VEGF receptor as potentially important determinants of prognosis, treatment efficacy, and toxicity. The plasminogen-derived antiangiogenic peptide, angiostatin binds vitronectin and induces focal adhesion kinase (FAK1) activity in cell culture. FAK1 normally becomes phosphorylated only in response to cell-cell contact or treatment with peptide hormones including cholecystokinin, bombesin, and vasopressin. This observation suggests that the biological effects of angiostatin may relate to subversion of adhesion plaque formation in endothelial cells. The collagen XVIII- derived antiangiogenic peptide, endostatin binds fibulins 1 and 2 and also induces FAK1 activity. Macrophage metalloproteinase (HME/MMP12) expression levels in hepatocellular tumors conelate well with angiostatin levels, which in turn were inversely correlated with poor survival. Transforming growth factor-beta 1, a key mediator of tumor angiogenesis, inhibits the generation of angiostatin in a pancreatic carcinoma cell line through modulation of the plasminogen activator/plasminogen activator inhibitor system. Generation of angiostatin may also involve an as yet unidentified, secreted disulfide reductase. Polymoφhisms in genes listed above or in Tables 1-3 and including similar genes not yet discovered that encode vascular growth factors, their receptors, and in enzymes involved in their processing that affect enzyme amounts, activity, or interaction with drag molecules could potentially affect neoplastic disease risk and prognosis as well as antiangiogenic treatment efficacy and toxicity. Example 42 Protease Inhibitors I. Description of Protease Inhibitors Extracellular proteases play a crucial role in normal tissue remodeling during embryogenesis, growth, and wound healing by modulating the maturation and degradation of growth factors and extracellular matrix components such as elastin and collagen. Proteases play a role in angiogenesis — the potent inhibitors angiostatin and endostatin are proteolytic fragments of plaminogen and collagen 18 Al , respectively. Extracellular proteases are involved in the progression of multiple pathological conditions such as osteoporosis and multiple inflammatory disorders including rheumatoid arthritis, multiple sclerosis, and nephritis. Tumor metastasis, the migration of cells from the primary tumor to distal sites via the lymph or blood vessels, is mechanistically similar to the migration of lymphocytes from the lymph nodes to sites of inflammation, a process known to rely on the action of zinc requiring matrix metalloproteases (MMPs) and to be regulated by conesponding tissue inhibitors of metalloproteinases (TIMPs). Both matrix metalloproteases and their inhibitors occur in large, dispersed multigene families. Levels of MMP 1 and TIMP 1 conelate with metastatic potential and poor treatment outcome in breast, gastric, and colorectal cancers; levels of MMP 2 and TIMP 2 conelate with metastatic potential and poor treatment outcome in renal, urothelial, bladder, and colorectal cancers. Invasion of smooth muscle cell layers by tumor cells is inhibited by TIMPs and transfection of human breast cancer cells with TIMP4 reduces their growth and metastatic potential, suggesting direct involvement of metalloproteases in metastasis. Several matrix metalloprotease have shown promising activity in tissue culture and in vivo models of metastasis including biphenyl sulfonyl-phenylalanine hydroxiamic acid (BPHA), KB-R7785, and R-94138; several inhibitors including marimastat, batimastat, and AG3340 (Agouron) are in various stages of clinical development. II. Current Indications for Protease Inhibitors Clinical trials of protease inhibitors in progress target advanced lung cancers including small cell and non-small cell; supratentorial glioblastoma multiforme; gliosarcoma; gastric, pancreatic, and metastatic breast cancers; and combination therapy with mitoxantrone and prednisone for hormone refractory prostate cancer. Batimastat has shown promise for the treatment of malignant pleural effusion. Because proteinase inhibitors are not cytotoxic, their use in anticancer therapies has been in combination with cytotoxic agents such as anthracycline antibiotics, microtubule inhibitors, topoisomerase inhibitors, etc., where they inhibit tumor growth indirectly through their antiangiogenic effects and tumor metastasis directly by inhibition of enzymes required for tumor dispersion. As metalloproteases have been implicated in tumor metastasis, protease inhibitors may find widespread application for the prophylactic treatment of primary tumors during standard chemotherapeutic regimens to prevent the migration of (resistant) tumor cells to secondary sites. III. Limitations of Current Therapies Utilizing Protease Inhibitors Symptoms reported by patients with various malignancies during trials of marimastat included severe joint and muscle pain which were debilitating in >60% of patients at doses >50 mg twice daily. These symptoms were reversible on discontinuation of the drag, and their incidence was been decreased by reducing the dose to 10 mg twice daily. IV. Impact of Genotyping on Drug Development for Protease Inhibitors Protease inhibitors have great potential in the treatment of neoplastic disease through their apparent ability to inhibit tumor invasion and dispersion. The protease/protease inhibitor systems that have been implicated in this process include the matrix metalloproteinases (MMPs) and their conesponding tissue inhibitors of metalloproteinase (TIMPs), the cathepsins (CTSs), and plasminogen activator (PLAU), plasminogen activator receptor (PLAUR), and plasminogen activator inhibitor (PAH). As proteases are also involved in the inhibition of the angiogenesis required for tumor growth by releasing the potent inhibitors of angiogenesis, endostatin and angiostatin from collagen and plasminogen, greater understanding of the protease biology involved in these opposing processes will be required before protease inhibitor therapy can realize its full potential. Serum levels of PLAU, PAH, and PLAUR are predictors of progression and prognosis in prostate and gastric cancers: higher levels correlate with poor outcome and prophylactic chemotherapy after resection may be warranted for patients displaying high levels. Similarly, the five year relapse rate of patients having node- negative breast cancer with low PAH and low cathepsin D (CSTD) was 13% > while patients who had greater than the median value for both of these molecules had a 5 year relapse rate of 40%. These data would indicate that at least two different protease systems are active in spread of node negative breast cancer and that measurement of CSTD and PAH levels may aid in the decisions to be made when offering adjuvant treatment to these patients. Cathepsin B (CTSB) is overexpressed in tumors of the lung, prostate, colon, breast, and stomach. Abundant extracellular expression of CTSB protein was found in 29 of 40 (72.5%) of esophageal adenocarcinoma specimens by use of immunohistochemical analysis. A single nucleotide insertional polymoφhism at -1607 in the promoter of matrix metalloproteinase 1 (MMP1), where an additional guanine (G) creates an Ets transcription factor binding site, creates an allele that displays significantly higher transcription in normal fibroblasts and in melanoma cells. This polymoφhism occurs in the normal population with a frequency of 30%>. In contrast, in eight tumor cell lines, this frequency increased to 62.5% (P < 0.0001), perhaps because increased levels of MMP 1 allow more aggressive matrix degradation, thereby facilitating cancer progression. Polymoφhisms in genes listed above or in Tables 1-3 and including similar genes not yet discovered that encode proteases, their substrates (including adhesion proteins), their inhibitors, and in enzymes involved in their processing that affect enzyme amounts, activity, or interaction with drag molecules could potentially affect neoplastic disease risk and prognosis as well as protease inhibitor treatment efficacy and toxicity. Example 43 Use of Genotype Information for the Identification of Candidates for Prophylactic Therapy i) Occult Disease Detection and Prophylaxis The early detection and treatment of neoplastic disease greatly improves prognosis — the prognosis for breast cancer chemotherapy is inversely related to lymph node involvement. Genotyping of polymoφhisms known to be associated with increased risk for neoplastic disease would warrant careful monitoring or prophylactic treatment. Patients and practitioners must carefully weigh the benefits and associated undesired toxicities of prophylactic treatment against the risk of disease onset and response to conventional therapies. Great advances in linking genetic polymoφhisms to cancer risk have been made in recent years. Most link polymoφhisms in genes involved in drag and xenobiotic metabolism (primarily phase I metabolism) to the appearance of various cancers. As environmental risk factors can be controlled, they can be viewed as modulators of genetic polymoφhisms involved in innate risk. These include, but are not restricted to, the genes in the table below, which are known to be polymoφbic and polymoφhisms have been linked to innate or environmentally induced cancer risk in the scientific literature. Table: Polymoφhic Genes Linked to Cancer Risk. Column 1, labelled "Cancer" shows commonly observed neoplastic diseases classified by organ or cell-type. Genes for which polymoφhisms are linked to cancers listed in column 1 are under the broad heading "Associated Polymoφhic Gene." These genes are identified by systematic name, "Name;" Genebank identifier, "GID;" Online Mendelian Inheritance in Man identifier, "OMIM_ID;" and internal, Variagenics, Inc. identifier, "NGX_Symbol." In addition, the PubMed database identifier, "PMID," allowing identification of pertinent literature is also given. Worldwide web addresses for the databases mentioned are in the "DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS" section under the subheading "Online Databases." It is likely that the inteφlay of multiple polymoφhic and non-polymoφhic genes is involved in the process of neoplastic transformation with both positive and negative risk associations. But, a patient having several predisposing factors for a given cancer type listed in column 1 of the table above will be at greater risk than a patient having fewer. For example, patients with polymoφhisms in glutathione-S- transferase (GST) M3 that reduce expressed levels are more likely to develop lung cancer if they also express low levels of GST Ml. One skilled in the art will recognize that knowledge of risk ratios associated with various gene polymoφhisms and neoplastic diseases will allow medical practitioners to determine whether prophylactic treatment , including change of habits or environment, preventative chemotherapy, careful monitoring for signs of disease, and prophylactic surgery, are wananted and advisable. Multiple risk-associated allelic loci can be genotyped to direct a course of prophylactic treatment in much the same manner as a high cholesterol count in a blood test carries an increased risk of heart disease and may wanant treatment with a statin-type drag (HMGCoA inhibitor). It will also be recognized by one skilled in the art that factors including age, sex (in the case of non-gender specific cancers), ethnic background, and environment (including diet, smoking, alcohol consumption, and diet) impact risk determinations and great care must be exercised in extrapolating from one population to another. II. Post-Treatment Prophylaxis Notes: Aim is to forestall onset of new disease after successful initial therapy-conelation of tumor genotype with metastatic potential. KIPl polymoφhisms, WAFl polymoφhisms, EGFR polymoφhisms, ERBB2 polymoφhisms Other Embodiments The invention described herein provides a method for identifying patients with a risk of developing neurological disease or dysfunction by determining the patients allele status for a gene listed in Tables 1-6, 11-17, and 18-23 and providing a forecast of the patients ability to respond to or tolerate a given drug treatment. In particular, the invention provides a method for determining, based on the presence or absence of a polymoφhism, a patient's likely response to drug therapies of neurological disease or dysfunction. Given the predictive value of the described polymoφhisms a candidate polymoφhism is likely to have a similar predictive value for other drags acting through other pharmacological mechanisms. Thus, the methods of the invention may be used to determine a patient's response to other drags including, without limitation, antihypertensives, anti-obesity, anti- hyperlipidemic, or anti-proliferative, antioxidants, or enhancers of terminal differentiation. In addition, while determining the presence or absence of the candidate allele is a clear predictor determining the efficacy of a drag on a given patient, other allelic variants of reduced catalytic activity are envisioned as predicting drug efficacy using the methods described herein. In particular, the methods of the invention may be used to treat patients with any of the possible variances, e.g., as described in Table 3 of Stanton et al, U.S. Application No. 09/300,747. In addition, while the methods described herein are preferably used for the treatment of human patients, non-human animals (e.g., dogs, cats, sheep, cattle and other bovines, swine, and apes and other non-human primates) may also be treated using the methods of the invention. It will be readily apparent to one skilled in the art that varying substitutions and modifications may be made to the invention disclosed herein without departing from the scope and spirit of the invention. For example, using other compounds, and/or methods of administration are all within the scope of the present invention. Thus, such additional embodiments are within the scope of the present invention and the following claims. The invention illustratively described herein suitably may be practiced in the absence of any element or elements, limitation or limitations which is not specifically disclosed herein. Thus, for example, in each instance herein any of the terms "comprising", "consisting essentially of and "consisting of may be replaced with either of the other two terms. The terms and expressions which have been employed are used as terms of description and not of limitation, and there is no intention that in the use of such terms and expressions of excluding any equivalents 405/1 of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the invention claimed. Thus, it should be understood that although the present invention has been specifically disclosed by prefened embodiments and optional features, modification and variation of the concepts herein disclosed may be resorted to by those skilled in the art, and that such modifications and variations are considered to be within the scope of this invention as defined by the appended claims. In addition, where features or aspects of the invention are described in terms of Markush groups or other grouping of alternatives, those skilled in the art will recognize that the invention is also thereby described in terms of any individual member or subgroup of members of the Markush group or other group. 4czf01 .xls Page 406 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page Inflammatio n (additional genes in Immunology ) 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag WO 00/50639 PCT/USOO/01392 CO co 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page CD voltage-dependent calcium channel, P/Q type, alpha 1 A 601011 NM 000068 19pl3 calcium channel, voltage-dependent, L type, alpha IB subunit/CACNAlB 601012 NM 000718 9q34 calcium channel, voltage-dependent, L type, alpha 1C subunit/CACNAlC 114205 NM 000719 12pl3.3 calcium channel, voltage-dependent, L type, alpha ID subunit/CACNAlD 114206 NM 000720 3pl4.3 L-type voltage dependent calcium channel alpha IS subunit/CACNAlS 114208 NM 000069 lq32 calcium channel, voltage-dependent, beta 1 subunit/CACNBl 114207 NM 000723 17q21-q22 voltage dependent calcium channel beta 2 subunit/CACNB2 600003 U07139 10pl2 voltage dependent calcium channel beta 3 subunit/CACNB3 601958 NM 000723 12ql3 Calcium voltage dependent calcium channel Channels beta 4 subunit/CACNB4 601949 2q22-q23 calcium channel, voltage-dependent, alpha 2/delta subunit/CACNA2Dl 114204 Z28613 7q21-q22 calcium channel, voltage-dependent, gamma subunit/CACNG 114209 NM 000727 17q24 neuronal voltage dependent calcium channel gamma subunit/CACNG2 602911 NM 006078 ATPase, Ca++ transporting, plasma membrane 1/ATP2B1 108731 NM 001682 12q21-q23 ATPase, Ca++ transporting, plasma membrane 2/ATP2B2 108733 NM 001683 3p26-p25 ATPase, Ca++ transporting, plasma membrane 3/ATP2B3 300014 AF060497 Xq28 4czf01 .xis Page 4czf01 .xls Pag 4czf01 .xls Page 4czf0i .xls Page 465 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page Cellular Maintainanc e 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .XlS Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Page Phase I Dru Metabolism (oxidation and 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page rt o 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page Multidrug resistance protein MDR3/P- 602347 X06181 7q21.1 glycoprotein 3/PGY3 Familial intrahepatic cholestasis 1 , NM_00560 (progressive, Byler disease and benign 602397 18q21 3 recurrent) /FIC 1 NM_00374 Bile salt export pump/BSEP 603201 2q24 2 Microsomal triglyceride transfer NM_00025 157147 4q22-q24 protein large subunit/MTP 3 Solute carrier family 6, member 186854 U16120 3p25-q24 6/SLC6A6 (taurine) Solute carrier family 10, member NM_00304 182396 chr. 14 1/SLClOAl (taurocholate) 9 Solute carrier family 10, member NM_00045 Transporters 601295 13q33 2/SLC10A2 (taurocholate) 2 Solute carrier family 13, member NM_00398 17pl l.l- 604148 2/SLC13A2 (dicarboxylic acids) 4 ql l .l Solute carrier family 19, member 600424 U19720 21q22.3 1/SLC19A1 (reduced folate) Solute carrier family 21, member NM_00507 602883 12pl2 3/SLC21A3 (organic anion) 5 Solute carrier family 22, member NM_00305 602607 6q26 1/SLC22A2 (organic cation) 8 multidrug resistance protein MDRl 171050 X96395 7q21.1 multidrug resistance associated protein NM_00039 601107 10q24 MRP2/CMOAT 2 multidrug resistance protein MDR3/P- 602347 X06181 7q21.1 glycoprotein 3/PGY3 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag Immune Response (additional genes in Immunology) 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Table 4. Inflammation Gene List Class I Pathway | Function JName I OMIM I GID I Locus 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag Immune Discriminati on (Self vs Non- Self) 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Cell- Mediated Inflammatio n 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag LO 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag Defense Proteins and Peptides 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Neurotrans itter and Peptide Hormone Inflammetor y Modulation 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag General Cell Growth 4czf01 .xls Pag 4czf01 .xls Pag o O 4czf01 .xls Pag Peptide Hormones Control of Metabolism 4czf01 .xls Pag Gonadotropi c Hormones 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Metabolism Carbohydrat e Metabolism and Storage 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Inflammatio n (additional genes in Inflammation ) 4czf01 .xls Page Table 6. Cardiovascular and Renal Gene List 4czf01 .xls Page 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag LO m 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Page 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag D -a — α ^ -. o a -~ >- © ts ^ 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xis Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag O CO CD 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag Inflammaror y Response 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag 4czf01 .xls Pag VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 707 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 708 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 709 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 710 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 711 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 712 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 713 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 714 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 715 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 716 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 717 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 718 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 719 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 720 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 721 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 722 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 723 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 724 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 725 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 726 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 727 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_.xls Page 728 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 729 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 730 VARIAGENICS 01/20/2000 CONFIDENTIAL 4ctq01_ xls Page 731 Table 12. Identified Variances In Genes for Pathways Identified in Cancer and Related Disorders AB00235 AB00235 603584 GEIM- Human mRNA for 269 82G>A V28M 6 6 1 CL KIAA0358 gene, complete eds AB00235 AB00235 603584 GEN- Human mRNA for 1567 1380G>A S 6 6 1 CL KIAA0358 gene, complete eds AB00235 AB00235 603584 GEN- Human mRNA for 1627 1440OT s 6 6 1CL KIAA0358 gene, complete eds AB00235 AB00235 603584 GEN- Human mRNA for 2438 2251 G>A V751 M 6 6 1 CL KIAA0358 gene, complete eds AB00714 AB00714 603289 GEN-13J Homo sapiens mRNA for 360 267G>T S 4 4 ZIP-kinase, complete eds AB00714 AB00714 603289 GEN-13J Homo sapiens mRNA for 1765 1672G>A 3 4 4 ZIP-kinase, complete eds AB00787 AB00787 602233 GEN-104 Homo sapiens KIAA0413 5024 5024G>A 3 3 3 mRNA, complete eds AB00787 AB00787 602233 GEN-104 Homo sapiens KIAA0413 5045 5045G>A 3 3 3 mRNA, complete eds AB00787 AB00787 602233 GEN-104 Homo sapiens KIAA0413 5265 5265T>C 3 3 3 mRNA, complete eds AB02068 AB02068 None GEN- Homo sapiens mRNA for 3854 3854A>G 3 0 0 LAX KIAA0873 protein, partial eds AF001174 AF001174 602898 GEN- Homo sapiens p38beta2 1044 1038T>C S 18T MAP kinase mRNA, complete eds AF001433 AF001433 601671 GEN- Human requiem (HREQ) 2378 2337T>C 3 SD-144146.1 Page 18D mRNA, complete eds AF001900 AF001900 None GEN- Homo sapiens secreted 782 480G>C 17W frizzled-related protein mRNA, complete eds AF001900 AF001900 None GEN- Homo sapiens secreted 1668 1366G>A 17W frizzled-related protein mRNA, complete eds AF004709 AF004709 602899 GEN-UX Homo sapiens stress- 432 384G>A activated protein kinase 4 mRNA, complete eds AF006689 AF006689 603014 GEN-YA Homo sapiens MAP kinase 75 (-1 )G>A kinase Jnkk2 mRNA, complete eds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 808 808OG H270D 1 HV caspase Mch5-beta mRNA, alternatively spliced, complete eds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 915 915G>A 1HV caspase Mch5-beta mRNA, alternatively spliced, complete eds AF012535 AF012535 None GEN- Homo sapiens death 234 95T>C L32P 1Z2 receptor 5 (DR5) mRNA, complete eds AF012535 AF012535 None GEN- Homo sapiens death 339 200OT A67V 1Z2 receptor 5 (DR5) mRNA, complete eds AF012535 AF012535 None GEN- Homo sapiens death 1397 1258G>C 3 1Z2 receptor 5 (DR5) mRNA, complete eds AF013988 AF013988 602652 GEN- Homo sapiens serine 271 1250T S42L 20E protease mRNA, complete eds AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 781 781 G>A 3 2A5 binding protein (BAD) mRNA, partial eds AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 883 8830A 3 2A5 binding protein (BAD) mRNA, partial eds AF026070 AF026070 None GEN- Homo sapiens death 455 387A>G 26S receptor 3 beta (DR3) SD-144146 1 Page 7 mRNA, complete eds AF026070 AF026070 None GEN- Homo sapiens death 1202 1134T>C 26S receptor 3 beta (DR3) mRNA, complete eds AF026070 AF026070 None GEN- Homo sapiens death 1204 1136T>G L379R 26S receptor 3 beta (DR3) mRNA, complete eds AF026070 AF026070 None GEN- Homo sapiens death 1237 26S receptor 3 beta (DR3) mRNA, complete eds AF027706 AF027706 None GEN- Homo sapiens 1424 1200T>A S L9F serine/threonine kinase RICK (RICK) mRNA, complete eds AF029761 AF029761 None GEN- Homo sapiens decoy 1011 929C>T S310L MND receptor 2 mRNA, complete eds AF030227 AF030227 164875 GEN- untitled 2702 2605G>A 3 MM5 ITGA7 AF032108 600536 GEN- Homo sapiens integrin 527 366G>A S 2NO alpha-7 mRNA, complete eds AF035606 AF035606 None GEN- Homo sapiens calcium 564 438C>T LCZ binding protein (ALG-2) mRNA, complete eds AF035606 AF035606 None GEN- Homo sapiens calcium 1006 880T>C LCZ binding protein (ALG-2) mRNA, complete eds AF036892 AF036892 601937 GEN-7W Nuclear receptor 842 659G>T R220I coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 1971 1788G>C Q596H coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 3048 2865A>G S coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 3909 3726A>G S coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 4483 4300T>C 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 5644 5461A>G 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 5675 5492T>A 3 SD-144146.1 Page 7 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 6051 5868T>G 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 6664 6481G>A 3 coactivator (ACTR) AF053712 AF053712 None GEN- Homo sapiens 2086 1902T>G 3 MM2 osteoprotegerin ligand mRNA, complete eds AF093771 AF093771 None GEN-LTJ Homo sapiens 528 529G>A mitoxantrone resistance protein 1 mRNA, partial sequence AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 65 (-39)G>C 17S maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 197 94A>G K32E 17S maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 227 124G>A G42R 17S maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 348 245C>T T82M 17S maleylacetoacetate isomerase D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 149 100G>A D34N D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 341 292G>T V98L D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 479 430A>T N144Y D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 1288 1239G>A 3 D12614 D12614 153440 GEN-QD Human mRNA for 319 179C>A T60N lymphotoxin (TNF-beta), complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 46 (-21)OT 5 1T5 complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 409 343A>C 3 1T5 complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 464 398G>C 3 1T5 complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 500 434A>G 3 1T5 complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 654 588T>C 3 SD-144146.1 Page 1T5 complete eds D15057 D15057 600243 GEN- Human mRNA for DAD-1 , 686 620A>C 3 1T5 complete eds D25418 D25418 600022 GEN-78 Prostaglandin 12 726 635G>A R212H (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1047 956C>G S319W (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1075 984A>C S (prostacyclin) receptor (IP) D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 25 (-47)G>A 5 transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1332 1261A>G 1421V transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1855 1784G>C 3 transformylase PTGIR D38128 600022 GEN- Human IP gene for 203 204C>G 3 4DH prostacyclin receptor, exon 3 PTGIR D38128 600022 GEN- Human IP gene for 231 232C>A 3 4DH prostacyclin receptor, exon 3 D38145 D38145 601699 GEN- Human mRNA for 1646 1619T>C 3 4E3 prostacyclin synthase, complete eds NT5 D38524 129190 GEN- Human mRNA for 5- 3075 2992C>T 3 2PF nucleotidase D50840 D50840 602874 GEN-314 Human mRNA for 638 348T>C S ceramide glucosyltransferase, complete eds D50840 D50840 602874 GEN-314 Human mRNA for 1151 861A>G S ceramide glucosyltransferase, complete eds D78586 D78586 114010 GEN-BR CAD PROTEIN 5308 5282C>A P1761 H D87461 D87461 601931 GEN- Human mRNA for 2432 2256C>A 3 43N KIAA0271 gene, complete eds AAC2 D90040 243400 GEN-465 Human mRNA for 232 191G>A R64Q arylamme N- acetyltransferase (EC SD-144146 1 Page 7 2.3.1.5) AAC2 D90040 243400 GEN-465 Human mRNA for 323 282C>T arylamine N- acetyltransferase (EC 2.3.1.5) AAC2 D90040 243400 GEN-465 Human mRNA for 844 803A>G K268R arylamine N- acetyltransferase (EC 2 3.1.5) D90041 D90041 108345 GEN-464 Human liver arylamine N- 591 445G>A V149I acetyltransferase (EC 2.3.1 5) gene D90041 D90041 108345 GEN-464 Human liver arylamine N- 1240 1094C>A acetyltransferase (EC 2.3.1.5) gene DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 829 7870T 3 4E9 reductase gene J00277 J00277 190020 GEN- Human (genomic clones 81 81T>C S MH8 lambda-[SK2-T2, HS578T]; cDNA clones RS-[3,4, 6]) c-Ha-ras1 proto-oncogene, complete coding sequence J03143 J03143 107470 GEN-ZK Human interferon-gamma 1098 1050T>G receptor mRNA, complete eds J03209 J03209 185250 GEN-PK Human matrix 133 133G>A E45K metalloproteinase-3 (MMP- 3) mRNA, complete eds J03209 J03209 185250 GEN-PK Human matrix 288 288C>T metalloproteinase-3 (MMP- 3) mRNA, complete eds J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 932 380G>A R127H J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1063 511G>A A171T J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1190 638C>G 3 J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1201 649C>T 3 J03250 J03250 172420 GEN-C4 DNA topoisomerase I 160 (-52)C>T 5 SD-144146.1 Page 7 J03250 J03250 172420 GEN-C4 DNA topoisomerase I 590 379G>A V127I J03250 J03250 172420 GEN-C4 DNA topoisomerase I 1984 1773G>A S J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 172 57C>T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 559 444C>T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1704 1589C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1833 1718C>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1959 1844A>C 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3301 3186C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3991 3876A>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 55 21 C>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 959 925C>A P309T lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 1762 1728A>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- 3 lipoxygenase (leukocytes) 2043AC>AC SD-144146.1 Page 7 J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- F lipoxygenase (leukocytes) 2043delAC J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2328 2294C>T 3 lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2376 2342T>G 3 lipoxygenase (leukocytes) J03626 J03626 258900 GEN-C6 Uridine monophosphate 742 638G>C G213A synthetase (orotate phosphoribosyl transferase and orotidine-5- decarboxylase) J03626 J03626 258900 GEN-C6 Uridine monophosphate 742 638G>C G213A synthetase (orotate phosphoribosyl transferase and orotidine-5- decarboxylase) J03626 J03626 258900 GEN-C6 Uridine monophosphate 1424 1320C>T synthetase (orotate phosphoribosyl transferase and orotidine-5- decarboxylase) J03626 J03626 258900 GEN-C6 Uridine monophosphate 1575 1471A>G synthetase (orotate phosphoribosyl transferase and orotidine-5- decarboxylase) J03626 J03626 258900 GEN-C6 Uridine monophosphate 1603 1499delT synthetase (orotate phosphoribosyl transferase and orotidine-5- decarboxylase) J03746 J03746 138330 GEN- Human glutathione S- 560 487A>G 3 11Z transferase mRNA, complete eds J03746 J03746 138330 GEN- Human glutathione S- 598 525T>G 3 11Z transferase mRNA, complete eds J03817 J03817 138350 GEN-9D Glutathione S-transferase 99 84T>C S M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 543 528C>T S M1 SD-144146.1 Page 7 J03817 J03817 138350 GEN-9D Glutathione S-transferase 643 628T>A S210T M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 728 713C>G 3 M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 902 887C>T 3 M1 J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 454 401 G>A R134K cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 969 916C>G Q306E cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 1614 1561T>C S cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2011 1958G>A R653Q cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2335 2282C>T T761 M cyclohydrolase J04088 J04088 126430 GEN-8C Topoisomerase II alpha 543 507G>A S J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1385 1349G>A R450Q J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1474 1438A>G K480E J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1496 1460G>A R487K J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1517 1481G>A R494Q J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1520 1484A>G E495G J04088 J04088 126430 GEN-8C Topoisomerase II alpha 1594 1558A>T F J04088 J04088 126430 GEN-8C Topoisomerase II alpha 2443 2407C>T P803S J04088 J04088 126430 GEN-8C Topoisomerase II alpha 4008 3972A>C S J04088 J04088 126430 GEN-8C Topoisomerase II alpha 4446 4410T>G S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 206 206G>A R69H J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 1780 1780C>T S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 2478 2478G>A S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 2978 2978C>A T993N J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3415 3415C>T P1139S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3661 3661 C>T 3 J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3804 3804A>G 3 J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 4071 4071 G>A 3 GSTM3 J05459 138390 GEN- Human glutathione 687 670G>A V224I 170 transferase M3 (GSTM3) mRNA, complete eds J05594 J05594 601688 GEN-E Prostaglandin 15-OH 173 156A>G S SD-144146.1 Page dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 913 896C>G 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 950 933G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1448 1431 G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 260 260C>G A87G end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 449 449G>C +150S end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 887 887A>G Y296C end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 902 902C>A P301 H end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 905 905A>G N302S end K02581 K02581 188300 GEN-CI Thymidine kinase 1 90 33C>T S K02581 K02581 188300 GEN-CI Thymidine kinase 1 90 33C>T S K02581 K02581 188300 GEN-CI Thymidine kinase 1 112 55G>A G19R K02581 K02581 188300 GEN-CI Thymidine kinase 1 279 222G>A S K02581 K02581 188300 GEN-CI Thymidine kinase 1 282 225G>A S K02581 K02581 188300 GEN-CI Thymidine kinase 1 313 256C>T F K02581 K02581 188300 GEN-CI Thymidine kinase 1 329 272- S 278TGGCTG T>TGGCTGT K02581 K02581 188300 GEN-CI Thymidine kinase 1 329 272- 278delTGGC TGT K02581 K02581 188300 GEN-CI Thymidine kinase 1 334 277G>T V93F K02581 K02581 188300 GEN-CI Thymidine kinase 1 445 388A>G R130G K02581 K02581 188300 GEN-CI Thymidine kinase 1 479 422C>T P141 L K02581 K02581 188300 GEN-CI Thymidine kinase 1 487 430G>A E144K K02581 K02581 188300 GEN-CI Thymidine kinase 1 772 715A>G 3 K02581 K02581 188300 GEN-CI Thymidine kinase 1 867 810G>A 3 SD-144146.1 Page 7 K02581 K02581 188300 GEN-CI Thymidine kinase 1 867 810G>A 3 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 19 (-68)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 26 (-61 )A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 48 (-39)C>T 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 114 28G>A E10K K02770 K02770 147720 GEN-5M Interleukin 1 , beta 119 33G>A M11 I L00634 L00634 134635 GEN-CK Farnesyltransferase, CAAX 182 166G>T V56L box, alpha L00634 L00634 134635 GEN-CK Farnesyltransferase, CAAX 184 168G>A S box, alpha L01087 L01087 600448 GEN-CM Protein kinase C-theta 1940 1846C>A s L01087 L01087 600448 GEN-CM Protein kinase C-theta 1943 1849G>A E617K GSTM5 L02321 138385 GEN- Human glutathione S- 1406 1349T>C 3 WO transferase (GSTM5) mRNA, complete eds L05628 L05628 158343 GEN- Human multidrug 3369 3173G>A R1058Q 4D9 resistance-associated protein (MRP) mRNA, complete eds L05628 L05628 158343 GEN- Human multidrug 4198 4002G>A s 4D9 resistance-associated protein (MRP) mRNA, complete eds " GFBR3 L07594 600742 GEN- Human transforming 3966 3618G>C 3 1 EA growth factor-beta type III receptor (TGF-beta) mRNA, complete eds L07861 L07861 176977 GEN-DO Protein kinase C, delta 445 387G>A s L07861 L07861 176977 GEN-DO Protein kinase C, delta 1835 1777G>A V593M L11284 L11284 176872 GEN- Homosapiens ERK 1763 1764T>C 3 1 K8 activator kinase (MEK1 ) mRNA L1 1284 L11284 176872 GEN- Homosapiens ERK 1914 1915G>A 3 1 K8 activator kinase (MEK1 ) mRNA L11285 L1 1285 601263 GEN- Homosapiens ERK 252 253C>A 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 276 277T>C 3 1 K7 activator kinase (MEK2) SD-144146- 1 Page 7 mRNA L11285 L11285 601263 GEN- Homosapiens ERK 537 538C>T 3 1 K7 activator kinase (MEK2) mRNA L1 1285 L11285 601263 GEN- Homosapiens ERK 613 614G>C 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 744 745A>C 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1156 1157G>T 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1311 1312C>T 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1457 1458C>A 3 1 K7 activator kinase (MEK2) mRNA L1 1285 L11285 601263 GEN- Homosapiens ERK 1459 1460A>C 3 1 K7 activator kinase (MEK2) mRNA L12002 L12002 192975 GEN-I Leukocyte integrin alpha-4 1208 798T>C S L19182 L19182 602867 GEN- Human MAC25 mRNA, 297 284G>A R95K 21Z complete eds L22473 L22473 600040 GEN- Human Bax alpha mRNA, 552 552G>A S L9D complete eds L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1422 1185T>C 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1490 1253C>T 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1517 1280A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2244 2007A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2299 2062A>G 3 RECEPTOR CDA L27943 123920 GEN- Homo sapiens cytidine 552 435T>C S 4E4 deaminase (CDA) mRNA, complete eds 'TGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 547 159C>T S SD-144146.1 Page 7 (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 611 223G>A V75M (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 1725 1337A>G Q446R (subtype EP2), 53kD L32866 L32866 603352 GEN- Human effector cell 308 306A>G 3 2JC protease receptor-1 (EPR- 1) gene, partial eds L36719 L36719 602315 GEN- Homo sapiens MAP kinase 1227 890C>A T297N 2NE kinase 3 (MKK3) mRNA, complete eds L36719 L36719 602315 GEN- Homo sapiens MAP kinase 1271 934A>G K312E 2NE kinase 3 (MKK3) mRNA, complete eds GSTT2 L38503 600437 GEN- Homo sapiens glutathione 203 203OT S68L 2PC S-transferase theta 2 (GSTT2) mRNA, complete eds GSTT2 L38503 600437 GEN- Homo sapiens glutathione 543 5430T 2PC S-transferase theta 2 (GSTT2) mRNA, complete eds L41690 L41690 None GEN- Homo sapiens TNF 399 399G>T E133D 2T4 receptor-1 associated protein (TRADD) mRNA, 3 end of eds L41690 L41690 None GEN- Homo sapiens TNF 417 417G>T E139D 2T4 receptor-1 associated protein (TRADD) mRNA, 3 end of eds L78207 L78207 600509 GEN-5Q Cell surface receptor for 4019 3981A>G sulfonylureas on pancreatic b cells M10901 M10901 138040 GEN-2W Corticosteroid nuclear 1220 1088A>G N363S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- S receptor b 1893AG>AG M10901 M10901 138040 GEN-2VV Corticosteroid nuclear 2024 1892- F receptor b 1893delAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2054 1922A>T D641V receptor b SD-144146.1 Page 7 M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2372 2240T>G I747S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>C L753F receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>T L753F receptor b M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 2166 2034C>T S M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3353 3221T>G 3 M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3398 3266T>G 3 ETS2 M11922 164740 GEN- Human Hu-ets-2 gene, 54 54A>G S 1 LG homologous to avian erythroblastosis virus transforming gene, partial eds M12674 M12674 133430 GEN-7Z Estrogen receptor 1267 975C>G S M12783 M12783 190040 GEN-QF Human c-sis/platelet- 1896 804T>C 3 derived growth factor 2 (SIS/PDGF2) mRNA, complete eds M12783 M12783 190040 GEN-QF Human c-sis/platelet- 2148 1056T>C 3 derived growth factor 2 (SIS/PDGF2) mRNA, complete eds M12783 M12783 190040 GEN-QF Human c-sis/platelet- 2250 1158G>A 3 derived growth factor 2 (SIS/PDGF2) mRNA, complete eds M13194 M13194 126380 GEN-EA DNA EXCISION REPAIR 496 354C>T S PROTEIN ERCC-1 M13194 M13194 126380 GEN-EA DNA EXCISION REPAIR 1078 936C>T 3 PROTEIN ERCC-1 M13509 M13509 120353 GEN-QJ Human skin collagenase 383 315A>G S mRNA, complete eds M13509 M13509 120353 GEN-QJ Human skin collagenase 899 831G>A S mRNA, complete eds M13509 M13509 120353 GEN-QJ Human skin collagenase 1522 1454A>G 3 mRNA, complete eds M13509 M13509 120353 GEN-QJ Human skin collagenase 1747 1679C>T 3 mRNA, complete eds BCL2 M13994 151430 GEN- Human B-cell 1744 286G>A A96T 1Q9 leukemia/lymphoma 2 (bcl- SD-144146. Page 7 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete eds BCL2 M13994 151430 GEN- Human B-cell 1786 328G>C G1 10R 1 Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete eds BCL2 M13994 151430 GEN- Human B-cell 2959 1501A>G 1 Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 184 (-11 )T>C proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 270 76G>C V26L proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 446 252C>T S proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1254 1060C>G 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1306 1112G>A 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1336 1142T>A 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1338 1144C>T 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1451 1257G>A 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1462 1268C>T 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1522 1328G>C 3 SD- 144146. Page 7 M14221 M14221 161565 GEN-QM Human cathepsin B 1712 1518C>G 3 proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1898 1704A>G 3 proteinase mRNA, complete eds ARG1 M14502 207800 GEN- Human liver arginase 800 744C>T S IRE mRNA, complete eds ABL1 M14752 189980 GEN- Human c-abl gene, 2233 1869G>A S 1S7 complete eds ABL1 M14752 189980 GEN- Human c-abl gene, 3826 3462A>G 3 1S7 complete eds M14758 M14758 171050 GEN- P glycoprotein 1 978 554- V185G 1 S6 555TT>GA>G A M14758 M14758 171050 GEN- P glycoprotein 1 978 554- S 1 S6 555TT>TT M14758 M14758 171050 GEN- P glycoprotein 1 1623 1199G>A S400N 1 S6 M14758 M14758 171050 GEN- P glycoprotein 1 3101 2677G>A A893T 1 S6 M14758 M14758 171050 GEN- P glycoprotein 1 3101 2677G>T A893S 1S6 M14758 M14758 171050 GEN- P glycoprotein 1 3859 3435C>T S 1 S6 M14758 M14758 171050 GEN- P glycoprotein 1 4460 4036A>G 3 1 S6 SD-144146.1 Page 7 NGFR M14764 162010 GEN- Human nerve growth factor 2716 2603C>T 1S8 receptor mRNA, complete eds NGFR M14764 162010 GEN- 1 S8 NGFR M 14764 162010 GEN- 1 S8 NGFR M14764 162010 GEN- Human nerve growth factor 3252 3139C>G 3 1S8 receptor mRNA, complete eds M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 890 818G>A G273E M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 978 906A>G S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1 173 1101 C>A S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1395 1323T>C S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1614 1542C>T S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1965 1893C>T S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2505 2433G>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2505 2433G>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2528 24560A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2528 2456C>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2553 2481G>C 3 PCNA M15796 176740 GEN- Human cyclin protein gene, 1063 945C>G 3 1 UE complete eds 15872 M15872 138360 GEN-QS Human glutathione S- 16 (-40)G>A transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 54 (-2)T>C transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 84 29T>C F10S transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 111 56C>T T19I transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 170 115G>T transferase 2 (GST) SD-144146.1 Page 7 mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 321 266G>A R89K transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 376 321 C>T S transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 430 375G>A S transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 622 567C>T S transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 684 629A>C E210A transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 701 646G>T A216S transferase 2 (GST) mRNA, complete eds M15990 M15990 164880 GEN- Human c-yes-1 mRNA 3403 3196G>A 3 1 UR M15990 M15990 164880 GEN- Human c-yes-1 mRNA 3864 3657G>A 3 1 UR M15990 M15990 164880 GEN- Human c-yes-1 mRNA 3969 3762A>C 3 1 UR M15990 M15990 164880 GEN- Human c-yes-1 mRNA 4148 3941 T>C 3 1 UR M16650 M16650 165640 GEN-EH Omithine decarboxylase 1 1330 1243G>C E415Q M16650 M16650 165640 GEN-EH Omithine decarboxylase 1 1356 1269C>T S M20132 M20132 313700 GEN-38 Androgen receptor 995 633G>A (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1385 1023T>C (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1786 1424G>A G475E (dihydrotestosterone receptor) M20137 M20137 147740 GEN- Human interleukin 3 (IL-3) 132 79C>T P27S CCJ mRNA, complete eds, clone pcD-SR-alpha SD-144146.1 Page 74 M20566 M20566 147880 GEN-3A Interleukin 6A 3058 2621A>T 3 M21154 M21154 180980 GEN-EM S-adenosylmethionine 1050 802A>G I268V decarboxylase 1 M21154 M21154 180980 GEN-EM S-adenosylmethionine 1139 891T>G S decarboxylase 1 M24857 M24857 180190 GEN-80 Retinoic acid receptor, 1694 1280C>T S427L gamma 1 SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 32 (-52)T>C 5 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 67 (-17)G>A 5 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 110 27T>C S 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 153 70T>C S24P 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 203 120G>A S 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 263 180C>T S 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 264 181 G>A G61 S 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 285 202C>A S 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 288 205A>G S69G 29M 464) potential SD-144146.1 Page 75 lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 291 208C>G R70G 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 335 252T>C 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 341 258C>T 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 395 312G>A 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 452 369C>T 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 479 396G>A 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 549 466G>A 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 561 478C>T 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 617 534C>G 29M 464) potential lymphokine/cytokine mRNA, complete eds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 660 577A>G 29M 464) potential lymphokine/cytokine SD-144146.1 Page 751 mRNA, complete eds M25753 M25753 123836 GEN-ET Cyclin B1 167 168C>T 3 M25753 M25753 123836 GEN-ET Cyclin B1 1055 1056OA 3 M26383 M26383 146930 GEN-3E Interleukin 8 259 185C>G A62G M26383 M26383 146930 GEN-3E Interleukin 8 1237 1163A>T 3 M26383 M26383 146930 GEN-3E Interleukin 8 1281 1207A>G 3 M27396 M27396 108370 GEN-EX Asparagine Synthase 807 629T>A V210E M27396 M27396 108370 GEN-EX Asparagine Synthase 1387 1209C>G S M27492 M27492 147810 GEN-3F INTERLEUKIN 1 4686 4604T>G 3 RECEPTOR, TYPE I PRECURSOR M29696 M29696 146661 GEN-3H Interleukin 7 receptor 1088 1066G>A V356I M31145 M31145 146730 GEN-3J Insulin-like growth factor 923 759A>G I253M binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1048 884T>C 3 binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1260 1096C>G 3 binding protein 1 precursor M31159 M31159 146732 GEN- Human growth hormone- 204 95G>C G32A 2GD dependent insulin-like growth factor-binding protein mRNA, complete eds M31159 M31159 146732 GEN- Human growth hormone- 2178 2069A>T 3 2GD dependent insulin-like growth factor-binding protein mRNA, complete eds M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1271 1241C>T 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1344 1314G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1489 1459G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1780 1750T>C 3 1 M32315 M32315 191191 GEN-3M Tumor necrosis factor 676 587T>G M196R receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 1176 1087G>A A363T receptor 2 (75kD) SD-144146.1 Page 752 M32315 M32315 191191 GEN-3M Tumor necrosis factor 1668 1579G>T 3 receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 2898 2809G>A 3 receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 3671 3582G>A 3 receptor 2 (75kD) VEGF M32977 192240 GEN-2JF Human heparin-binding 50 (-7)OT 5 vascular endothelial growth factor (VEGF) mRNA, complete eds VEGF M32977 192240 GEN-2JF Human heparin-binding 92 36C>T vascular endothelial growth factor (VEGF) mRNA, complete eds RB1 M33647 180200 GEN- Human retinoblastoma 1105 1102G>A V368I 2K1 associated (RB1 ) mRNA, complete eds M35011 M35011 147561 GEN- Human integrin beta-5 1448 1419C>T 2LV subunit mRNA, complete eds M35011 M35011 147561 GEN- Human integrin beta-5 2778 2749A>C 2LV subunit mRNA, complete eds M35011 M35011 147561 GEN- Human integrin beta-5 2904 2875T>C 2LV subunit mRNA, complete eds M35011 M3501 1 147561 GEN- Human integrin beta-5 3077 3048G>A 3 2LV subunit mRNA, complete eds M3501 1 M3501 1 147561 GEN- Human integrin beta-5 3095 3066T>A 3 2LV subunit mRNA, complete eds MET M35074 164860 GEN- Human met oncogene 60 60C>T S 2LU mRNA, 3 end MET M35074 164860 GEN- Human met oncogene 294 294G>A S 2LU mRNA, 3 end M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 53 35T>C V12A M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 900 882T>C S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S SD-144146.1 Page 7 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2226 2208C>T S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2426 2408G>C 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3056 3038C>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3098 3080A>G 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3403 3385A>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3927 3909C>T 3 M37825 M37825 165190 GEN- Human fibroblast growth 787 648T>G S 20M factor-5 (FGF-5) mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 711 519T>C 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 936 744G>T 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 1270 1078T>C 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 3268 3076T>G 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 4529 4337A>C 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 4555 4363A>G 35G protein mRNA, complete eds M54968 M54968 190070 GEN- Human K-ras oncogene 4672 4480A>C 35G protein mRNA, complete eds SNK2A1 M55265 115440 GEN- Human casein kinase II 193 45T>C 35Y alpha subunit mRNA, complete eds SNK2A1 M55265 115440 GEN- Human casein kinase II 1007 859A>C S287R 35Y alpha subunit mRNA, complete eds SD-144146.1 Page 7 CSNK2A1 M55265 115440 GEN- Human casein kinase II 1180 1032G>A S 35Y alpha subunit mRNA, complete eds CSNK2A1 M55265 115440 GEN- Human casein kinase II 1199 1051A>G M351V 35Y alpha subunit mRNA, complete eds CSNK2A2 M55268 115442 GEN- Human casein kinase II 1532 1369C>A 3 35X alpha subunit mRNA, complete eds M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 644 639C>A S M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 1892 1887C>A 3 M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 2030 2025G>A 3 M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 159C>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 159C>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 159C>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 210 195G>C W65C methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 264 249A>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 265 250C>T L84F methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 265 250C>T L84F methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 442 427A>G 1143V methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 442 427A>G 1143V methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 493 478G>A G160R methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 548 533A>G K178R methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 582 567G>A S methyltransferase FGF7 M60828 148180 GEN- Human keratinocyte 323 (-123)G>C 5 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1180 735T>C 3BE growth factor mRNA, SD-144146.1 Page 7 complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1201 756A>G 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1216 771A>G 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1218 773G>C 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1266 821 A>C 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1306 861 C>T 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1654 1209A>T 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1657 1212T>C 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1799 1354A>T 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1801 1356C>T 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1867 1422A>G 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1945 1500C>A 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 1973 1528G>A 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 2167 1722G>A 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 2186 1741A>G SD-144146.1 Page 7 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 2302 1857T>A 3 3BE growth factor mRNA, complete eds FGF7 M60828 148180 GEN- Human keratinocyte 2328 1883G>A 3 3BE growth factor mRNA, complete eds M61764 M61764 191135 GEN-FO Tubulin, gamma 693 669A>G S polypeptide M61764 M61764 191 135 GEN-FO Tubulm, gamma 723 699T>C S polypeptide M61764 M61764 191135 GEN-FO Tubulin gamma 849 825T>G S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 858 834G>A S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1033 1009T>C S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1053 1029OG s polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1131 1107G>A s polypeptide M61764 M61764 191135 GEN-FO Tubulin gamma 1 188 1 164C>T s polypeptide IGFBP4 M62403 146733 GEN- Human insulin-like growth 859 776G>A s 3CJ factor binding protein 4 (IGFBP4) mRNA, complete eds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1403 1320G>T 3 3CJ factor binding protein 4 (IGFBP4) mRNA, complete eds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1443 1360G>A 3 3CJ factor binding protein 4 (IGFBP4) mRNA, complete eds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1446 1363G>A 3 3CJ factor binding protein 4 (IGFBP4) mRNA complete eds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1485 1402A>T 3 SD-144146 1 Page 7 3CJ factor binding protein 4 (IGFBP4) mRNA, complete eds M62782 M62782 146734 GEN- Homo sapiens insulin-like 908 852C>T 3CU growth factor binding protein 5 (IGFBP-5) mRNA, complete eds M62982 M62982 152391 GEN-12 Lipoxygenases 12- 1018 965G>A S322N lipoxygenase (platelet) M62982 M62982 152391 GEN-12 Lipoxygenases 12- 1145 1092T>G S hpoxygenase (platelet) AKT1 M63167 164730 GEN- Human rac protein kinase 934 736T>G S246A 3D7 alpha mRNA, complete eds AKT1 M63167 164730 GEN- Human rac protein kinase 1964 1766G>A 3 3D7 alpha mRNA, complete eds M63509 M63509 138380 GEN-9G Glutathione S-transferase 644 628A>T T210S M2 (muscle) FGFR3 M64347 134934 GEN- Human novel growth factor 3108 3108C>A 3 SEX receptor mRNA, 3 eds FGFR3 M64347 134934 GEN- Human novel growth factor 3715 3715G>A 3 SEX receptor mRNA, 3 eds M68892 M68892 147559 GEN-15 Leukocyte integrin beta-7 1327 1176C>T S IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 751 751A>C 3 factor binding protein 6 (IGFBP6) mRNA, complete mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 835 835A>C factor binding protein 6 (IGFBP6) mRNA, complete mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 850 850G>A factor binding protein 6 (IGFBP6) mRNA, complete mature peptide M73554 M73554 168461 GEN-FY Cyclin D1 864 723G>A S M73554 M73554 168461 GEN-FY Cyclin D1 1094 953A>C 3 M73554 M73554 168461 GEN-FY Cyclin D1 1094 953A>C 3 M73554 M73554 168461 GEN-FY Cyclin D1 1367 1226T>G 3 M73554 M73554 168461 GEN-FY Cyclin D1 3899 3758T>G 3 M73554 M73554 168461 GEN-FY Cyclin D1 4013 3872A>G 3 SD-144146 1 Page 7 SRD5A2 M74047 264600 GEN- Human steroid 5-alpha- 2379 2352A>G CDC reductase 2 (SRD5A2) mRNA, complete eds M74091 M74091 123838 GEN-FZ G1/S-SPECIFIC CYCLIN C 41 42C>G 3 CCNE M74093 123837 GEN- Human cyclin mRNA 1195 1196C>T 3 3MX CCNE M74093 123837 GEN- Human cyclin mRNA 1641 1642C>A 3 3MX M74782 M74782 308385 GEN-64 Interleukin 3 receptor.alpha 1396 1250C>T 3 (low affininty) MPG M74905 156565 GEN- Human 3-alkyladenine 254 108C>T S 3NL DNA glycosylase (HAAG) mRNA, complete eds MPG M74905 156565 GEN- Human 3-alkyladenine 350 204G>A 3NL DNA glycosylase (HAAG) mRNA, complete eds MPG M74905 156565 GEN- Human 3-alkyladenine 413 267G>A 3NL DNA glycosylase (HAAG) mRNA, complete eds MPG M74905 156565 GEN- Human 3-alkyladenine 416 270C>T 3NL DNA glycosylase (HAAG) mRNA, complete eds MPG M74905 156565 GEN- Human 3-alkyladenine 546 400C>G P134A 3NL DNA glycosylase (HAAG) mRNA, complete eds MPG M74905 156565 GEN- Human 3-alkyladenine 743 597C>T 3NL DNA glycosylase (HAAG) mRNA, complete eds M80646 M80646 274180 GEN-40 Thromboxane synthase 756 585G>C S M80646 M80646 274180 GEN-40 Thromboxane synthase 1240 1069C>G L357V M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 1834 1770G>C S M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 3282 3218C>T T1073M M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 4213 4149C>G 3 M84747 M84747 300007 GEN-45 Interleukin 9 receptor 1273 1094G>A R365H TGFBR2 M85079 190182 GEN- Human TGF-beta type II 2045 1710A>C 3 3ZS receptor mRNA, complete eds M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2159 2062G>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094ATATTA SD-144146.1 Page 7 >ATATTA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 C0X2 2186 2089- 3 2094delATAT TA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2230 2133A>G 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2339 2242T>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2409 2312G>A 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2726 2629C>T 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2983 2886C>T 3 M90814 M90814 123834 GEN-GK Cyclin D3 1648 1548G>A 3 IL8RB M94582 146928 GEN- Interleukin 8 receptor 838 786T>C S 49G IL8RB M94582 146928 GEN- Interleukin 8 receptor 1262 1210C>T 3 49G IL8RB M94582 146928 GEN- Interleukin 8 receptor 1494 1442A>G 3 49G BRAF M95712 164757 GEN- Human B-raf mRNA, 284 223T>G S75A 4AD complete eds M96234 M96234 138333 GEN-9J Glutathione S-transferase 797 534T>C S M4 M96652 M96652 147851 GEN-65 Interleukin 5 receptor alpha 883 634T>G S212A M98045 M98045 136510 GEN- Homo sapiens 802 732C>T S 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1747 1677G>T 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1912 1842G>A 3 4C3 folylpolyglutamate synthetase mRNA, SD-144146.1 Page 7 complete eds M98045 M98045 136510 GEN- Homo sapiens 1995 1925C>G 4C3 folylpolyglutamate synthetase mRNA, complete eds M98539 M98539 176803 GEN-SW prostaglandin D2 synthase 157 158C>A 3 gene S72487 S72487 131222 GEN- orf1 5 to PD- 183 19G>A D7N 3LD ECGF/TP...orf2 5 to PD- ECGF TP [human, epidermoid carcinoma cell line A431 , mRNA, 3 genes, 1718 nt] S72487 S72487 131222 GEN- orfl 5 to PD- 483 319C>T 3LD ECGF/TP...orf2 5 to PD- ECGF/TP [human, epidermoid carcinoma cell line A431 , mRNA, 3 genes, 1718 nt] S72487 S72487 131222 GEN- orfl 5 to PD- 601 437G>C 3LD ECGF/TP...orf2 5 to PD- ECGF/TP [human, epidermoid carcinoma cell line A431 , mRNA, 3 genes, 1718 nt] S72487 S72487 131222 GEN- orfl 5 to PD- 1299 1135G>A 3LD ECGF/TP...orf2 5 to PD- ECGF/TP [human, epidermoid carcinoma cell line A431 , mRNA, 3 genes, 1718 nt] PDCD2 S78085 600866 GEN- PDCD2=programmed cell 1180 1151 G>A 3 3QQ death-2/Rp8 homolog [human, fetal lung, mRNA, 1282 nt] U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3377 3316A>C 3 U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3524 3463A>G 3 U03858 U03858 600007 GEN- Fms-related tyrosine 683 600C>T S MDM kinase 3 ligand U03858 U03858 600007 GEN- Fms-related tyrosine 1016 933T>C MDM kinase 3 ligand SD-144146. Page 7 PI5 U04313 154790 GEN- Human maspin mRNA, 2496 2421 G>C 3 MA complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 364 209G>A S70N 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 728 573C>T S 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1613 1458C>T S 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1643 1488G>C S 16V kinase TrkC (NTRK3) mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 38 15C>T S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 282 259A>T S87C dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 350 327C>T S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 365 342T>C S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 464 441 G>A S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 474 451A>G M151V dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 532 509A>G H170R dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 538 515T>A L172Q dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 689 666T>C S dehydrogenase mRNA, complete eds SD-144146. Page 7 DDH1 U05598 600450 GEN-184 Human dihydrodiol 806 783G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 872 849G>T dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 952 929T>G I310S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1020 997G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1035 1012G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1 1 12 1089C>T dehydrogenase mRNA, complete eds U05875 U05875 147569 GEN-18J Human clone pSK1 2047 1399C>G interferon gamma receptor accessory factor- 1 (AF-1 ) mRNA, complete eds U05875 U05875 147569 GEN-18J Human clone pSK1 2087 1439T>C interferon gamma receptor accessory factor- 1 (AF-1 ) mRNA, complete eds XDH U06117 278300 GEN-194 Human xanthine 3951 3888C>G dehydrogenase (XDH) mRNA, complete eds U09178 U09178 274270 GEN-HA Dihydropyrimidine 166 85T>C C29R Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 166 85T>C C29R Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 577 496A>G M166V Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 638 557A>G Y186C Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 1708 1627A>G I543V Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3432 3351T>C 3 Dehydrogenase SD-144146.1 Page 7 U09178 U09178 274270 GEN-HA Dihydropyrimidine 3730 3649G>A 3 Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3925 3844A>G 3 Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3937 3856T>C 3 Dehydrogenase U09579 U09579 116899 GEN- Human melanoma 609 515C>T 3 1GZ U09579 U09579 116899 GEN- Human melanoma 1875 1781G>A 3 1 GZ differentiation associated (mda-6) mRNA, complete eds U09579 U09579 1 16899 GEN- Human melanoma 1877 1783C>G 3 1 GZ differentiation associated (mda-6) mRNA, complete eds U09759 U09759 602896 GEN- Human protein kinase 303 152A>G N51 S 1 HA (JNK2) mRNA, complete eds U09759 U09759 602896 GEN- Human protein kinase 1079 928A>G 1310V 1HA (JNK2) mRNA, complete eds U09759 U09759 602896 GEN- Human protein kinase 1280 1129C>T P377S 1 HA (JNK2) mRNA, complete eds U09759 U09759 602896 GEN- Human protein kinase 1559 1408C>T 3 1 HA (JNK2) mRNA, complete eds U09806 U09806 None GEN- Human 120 120T>C S 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 473 473G>A R158Q 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 550 550C>T F 4FZ methylenetetrahydrofolate reductase mRNA, partial SD-144146.1 Page 7 <υ oo > CO < Q co 0- -xi o CT> co CC < LU ϋ -- o < O < h- CD < O O Λ Λ o < O 1- O 1- CD O σ> < CD H -- H CD σ> co co co ^ r-. oo o o co o • * co o ro co σ> o "*— oo σ> σ- co co ----- o co o r- o co co N N > Q Q Q LL 2 U- z N UJ X 2 5 J l-U X 2 z Q -2 D UJ l-U UJ X UJ X -z LU X X 2 Q UJ LU LU LU ^ CD CD CD CD CD CD CD CD CD CD CD CD Φ co co co co co c c c c co o o o o o 2 2 -z z co oo co co co co o o σ o o o o o co o o σ o o o o o m oo co oo oo oo co oo o o σ> cn σ> σ- n σ> σ> σ> σ> σ> o o o σ o σ o o o o 3 3 3 r- 3 3 n =) 3 3 3 3 o σ o o o o o o o σ m m m o o co oo co co oo oo co D- α- σ- σ- σ> σ> cn σ- σ> σ> X X o o o o o σ o o o 1— 1— 3 3 3 3 3 -D Z) Z> 3 3 Q factor (MGDF) mRNA, complete eds THPO U11025 600044 GEN- Human megakaryocyte 382 347G>A G116E 1JW growth and development factor (MGDF) mRNA, complete eds THPO U11025 600044 GEN- Human megakaryocyte 674 639T>A 1JW growth and development factor (MGDF) mRNA, complete eds THPO U11025 600044 GEN- Human megakaryocyte 132 1097G>A 3 1JW growth and development factor (MGDF) mRNA, complete eds U11791 U11791 601953 GEN-HF Cyclin H 823 763A>G M255V TPMT U12387 187680 GEN- Human thiopurine 536 460G>A A154T 1LY methyltransferase (TPMT) mRNA, complete eds TPMT U12387 187680 GEN- Human thiopurine 795 719A>G Y240C 1LY methyltransferase (TPMT) mRNA, complete eds TPMT U12387 187680 GEN- Human thiopurine 1085 1009T>C 1LY methyltransferase (TPMT) mRNA, complete eds TPMT U12387 187680 GEN- Human thiopurine 1336 1260C>T 1LY methyltransferase (TPMT) mRNA, complete eds TPMT U12387 187680 GEN- Human thiopurine 1373 1297G>A 1LY methyltransferase (TPMT) mRNA, complete eds U13737 U13737 600636 GEN- Human cysteine protease 2356 2132A>C 1PC CPP32 isoform alpha mRNA, complete eds U13737 U13737 600636 GEN- Human cysteine protease 2535 2311 C>T 1PC CPP32 isoform alpha mRNA, complete eds BRCA1 U14680 113705 GEN- Human breast and ovarian 4427 4308T>C 1S1 cancer susceptibility (BRCA1 ) mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 2223 1932T>G F644L SD-144146.1 Page 76 apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 3046 2755C>T P919S apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 5503 5212A>G 3 apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 5634 5343A>G 3 apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 5644 5353A>G 3 apoptosis inhibitory protein mRNA, complete eds U19487 U19487 176804 GEN-4I PROSTAGLANDIN E2 231 75A>T S RECEPTOR, EP2 SUBTYPE U19720 U19720 600424 GEN-11 Folate Transporter 53 (-43)T>C 5 (SLC19A1 ) U 19720 U19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 341 246C>G S (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 791 696C>T S (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 1067 972G>A S (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 2100 2005 Λ 2006ins F (SLC19A1 ) G U19720 U19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 (SLC19A1 ) U 19720 U 19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 2652 2557T>C 3 (SLC19A1 ) SD-144146. Page 7 U19775 U19775 600289 GEN- Human MAP kinase Mxi2 731 688G>A D230N 22C (MXI2) mRNA, complete eds U20536 U20536 601532 GEN- Human cysteine protease 982 904C>T 23K Mch2 isoform alpha (Mch2) mRNA, complete eds U20536 U20536 601532 GEN- Human cysteine protease 1117 1039G>A 3 23K Mch2 isoform alpha (Mch2) mRNA, complete eds U20536 U20536 601532 GEN- Human cysteine protease 1322 1244T>C 3 23K Mch2 isoform alpha (Mch2) mRNA, complete eds U20536 U20536 601532 GEN- Human cysteine protease 1363 1285T>C 3 23K Mch2 isoform alpha (Mch2) mRNA, complete eds U24231 U24231 None GEN-289 Human Fas-associating 1312 1183G>A 3 death domain-containing protein mRNA, complete eds U25029 U25029 138040 GEN-82 Glucocorticoid receptor 335 335C>T 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 386 386T>C 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 1069 1069C>T 3 alpha CDKN2A U26727 600160 GEN- Human p16INK4/MTS1 311 284C>A T95N 2BC mRNA, complete eds CDKN2A U26727 600160 GEN- Human p16INK4/MTS1 570 543G>C 3 2BC mRNA, complete eds CDKN2A U26727 600160 GEN- Human p16INK4/MTS1 643 616C>T 3 2BC mRNA, complete eds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 476 442T>C F148L 2BX mRNA, complete eds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 481 447A>G S 2BX mRNA, complete eds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 542 508C>G L170V 2BX mRNA, complete eds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 578 544C>T 3 2BX mRNA, complete eds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 614 580T>C 3 2BX mRNA, complete eds SD-144146.1 Page 76 U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 616 582G>A 3 2BX mRNA, complete eds CSNK1 D U29171 600864 GEN- Human casein kinase I 1612 1435C>A 3 2E2 delta mRNA, complete eds U31628 U31628 601070 GEN-4J Interleukin 15 receptor 1250 1168G>T 3 alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1266 1205C>A P402Q alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1513 1452C>T 3 alpha chain U33286 U33286 601342 GEN-IM Chromosome segregation 54 (-70)A>G 5 gene homolog CAS U33286 U33286 601342 GEN-IM Chromosome segregation 821 698G>A G233D gene homolog CAS U33286 U33286 601342 GEN-IM Chromosome segregation 3127 3004T>C 3 gene homolog CAS FGF8 U36223 600483 GEN- Human fibroblast growth 300 291T>C S 2MX factor 8 (FGF-8) mRNA, complete eds FGF8 U36223 600483 GEN- Human fibroblast growth 645 636G>C 2MX factor 8 (FGF-8) mRNA, complete eds FGF8 U36223 600483 GEN- Human fibroblast growth 648 639A>G 2MX factor 8 (FGF-8) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 736 693G>A 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1285 1242T>C 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1294 1251T>C 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1580 1537A>T 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1621 1578G>T 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1715 1672G>A SD-144146.1 Page 76 20C alpha (Mch3) mRNA, complete eds U37448 U37448 601761 GEN- Human Mch3 isoform 1764 1721G>A 20C alpha (Mch3) mRNA, complete eds U37518 U37518 None GEN- Human TNF-related 912 825C>T 20G apoptosis inducing ligand TRAIL mRNA, complete eds U37518 U37518 None GEN- Human TNF-related 1140 1053A>G 20G apoptosis inducing ligand TRAIL mRNA complete eds U37518 U37518 None GEN- Human TNF-related 1289 1202C>A 20G apoptosis inducing ligand TRAIL mRNA complete eds U37518 U37518 None GEN- Human TNF-related 1525 1438G>A 20G apoptosis inducing ligand TRAIL mRNA, complete eds U37518 U37518 None GEN- Human TNF-related 1588 1501G>A 20G apoptosis inducing ligand TRAIL mRNA complete eds U37518 U37518 None GEN- Human TNF-related 1595 1508C>T 20G apoptosis inducing ligand TRAIL mRNA complete eds U39656 U39656 601254 GEN- Human MAP kinase kinase 431 91A>C 2Q8 6 (MKK6) mRNA, complete eds U39656 U39656 601254 GEN- Human MAP kinase kinase 713 373G>A V125M 2Q8 6 (MKK6) mRNA, complete eds U43030 U43030 600435 GEN-LFI Human cardιotrophιn-1 1404 1372C>T (CTFI ) mRNA complete eds U43142 U43142 601528 GEN- Human vascular 1499 1128C>T 2UM endothelial growth factor related protein VRP 144146 Page 7 mRNA, complete eds U45878 U45878 601721 GEN- Human inhibitor of 2281 1833G>A 2WJ apoptosis protein 1 mRNA, complete eds U45878 U45878 601721 GEN- Human inhibitor of 2820 2372C>G 2WJ apoptosis protein 1 mRNA, complete eds U45879 U45879 601712 GEN- Human inhibitor of 748 511T>G S171A 2WI apoptosis protein 2 mRNA, complete eds U45879 U45879 601712 GEN- Human inhibitor of 835 598T>G S200A 2WI apoptosis protein 2 mRNA, complete eds U47634 U47634 None GEN- Human beta-tubulin class 1005 1005C>T 2XR III isotype (beta-3) mRNA, complete eds U47634 U47634 None GEN- Human beta-tubulin class 1035 1035C>T 2XR III isotype (beta-3) mRNA, complete eds U47634 U47634 None GEN- Human beta-tubulin class 1431 1431T>C 3 2XR III isotype (beta-3) mRNA, complete eds U47634 U47634 None GEN- Human beta-tubulin class 1502 1502G>A 3 2XR III isotype (beta-3) mRNA, complete eds U54831 U54831 126431 GEN-8W Topoisomerase II beta 127 127A>G T43A U54831 U54831 126431 GEN-8W Topoisomerase II beta 1002 1002T>C S U55206 U55206 None GEN- Homo sapiens human 75 16T>C C6R 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 150 91 G>A A31T 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 511 452C>T T151 I 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 1161 1102A>G 35Z gamma-glutamyl hydrolase SD-144146.1 Page 7 (hGH) mRNA, complete eds U56390 U56390 602234 GEN- Human cysteine protease 411 408C>T S 36X ICE-LAP6 mRNA, complete eds U60519 U60519 601762 GEN- Human apoptotic cysteine 304 157G>A E53K 3AZ protease Mch4 (Mch4) mRNA, complete eds U60519 U60519 601762 GEN- Human apoptotic cysteine 324 177A>G S 3AZ protease Mch4 (Mch4) mRNA, complete eds U70136 U70136 600044 GEN-4R Thrombopoietin 4138 4105G>T A1369S U70136 U70136 600044 GEN-4R Thrombopoietin 4141 4108T>A F1370I U70321 U70321 None GEN- Human herpesvirus entry 343 50G>A R17K 3K9 mediator mRNA, complete eds U70321 U70321 None GEN- Human herpesvirus entry 1014 721G>A V241 I 3K9 mediator mRNA, complete eds U70321 U70321 None GEN- Human herpesvirus entry 1218 925A>G 3 3K9 mediator mRNA, complete eds U70321 U70321 None GEN- Human herpesvirus entry 1249 956C>T 3K9 mediator mRNA, complete eds U70321 U70321 None GEN- Human herpesvirus entry 1453 1160G>A 3K9 mediator mRNA, complete eds U77088 U77088 188250 GEN-K4 Thymidine kinase 2 1480 1472T>C U79269 U79269 123829 GEN-K7 Cyclin-Dependent Protein 1281 972A>T Kinase U81375 U81375 602193 GEN- Human placental 1989 1811G>A 3VO equilibrative nucleoside transporter 1 (hENT1 ) mRNA, complete eds U81375 U81375 602193 GEN- Human placental 1996 1818C>T 3VO equilibrative nucleoside transporter 1 (hENT1 ) mRNA, complete eds U81375 U81375 602193 GEN- Human placental 2045 1867T>C 3VO equilibrative nucleoside SD-144146. Page 7 transporter 1 (hENTI) mRNA, complete eds IFNB1 V00546 147640 GEN-TV Messenger RNA for human 474 410T>G L137R fibroblast interferon V00548 V00548 147562 GEN-P2 Human messenger RNA 119 119G>A R40K for leukocyte (alpha-2) interferon V00594 V00594 156360 GEN-P6 Human mRNA for 320 263G>C 3 metallothionein from cadmium-treated cells EGFR X00663 131550 GEN-U4 Human mRNA fragment for 1 136 1 136G>A R379K epidermal growth factor (EGF) receptor EGFR X00663 131550 GEN-U4 Human mRNA fragment for 1935 1935A>G epidermal growth factor (EGF) receptor EGFR X00663 131550 GEN-U4 Human mRNA fragment for 2283 2283C>T epidermal growth factor (EGF) receptor X00734 X00734 None GEN- Human beta-tubulin gene 1059 1059G>T S MST (5-beta) with ten Alu family members X00737 X00737 164050 GEN-P8 Human mRNA for purine 59 (-51)T>G 5 nucleoside phosphorylase (PNP; EC 2.4.2.1 ) X00737 X00737 164050 GEN-P8 Human mRNA for purine 169 60T>C S nucleoside phosphorylase (PNP; EC 2.4.2.1 ) X00737 X00737 164050 GEN-P8 Human mRNA for purine 260 151A>G S51 G nucleoside phosphorylase (PNP; EC 2.4.2.1) X00737 X00737 164050 GEN-P8 Human mRNA for purine 280 171T>C S nucleoside phosphorylase (PNP; EC 2.4.2.1 ) X00737 X00737 164050 GEN-P8 Human mRNA for purine 1254 1145G>A 3 nucleoside phosphorylase (PNP; EC 2.4.2.1 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 687 424A>G S142G CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 2823 2560delT F CD71 ) SD-144146.1 Page 7 X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 3766 3503T>G 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4122 3859A>C 3 CD71) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4147 3884G>A 3 CD71) X01060 X01060 190010 GEN-6C Transferrin receptor 90, 4247 3984T>C 3 X01060 X01060 190010 GEN-6C Transferrin recepto X01060 X01060 190010 GEN-6C Transferrin recepto X01060 X01060 190010 GEN-6C Transferrin recepto CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4619 4356T>G 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4726 4463A>T 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4766 4503C>T 3 CD71 ) X01394 X01394 191160 GEN-4Y Tumor necrosis factor 125 (-28)C>T 5 X01586 X01586 147680 GEN-PC Interleukin 2 332 225T>G H75Q X01586 X01586 147680 GEN-PC Interleukin 2 563 456G>A S X02308 X02308 188350 GEN-KL Thymidylate synthetase 1066 961T>C 3 X02308 X02308 188350 GEN-KL Thymidylate synthetase 1066 961T>C 3 X02308 X02308 188350 GEN-KL Thymidylate synthetase 1136 1031A>G 3 X02308 X02308 188350 GEN-KL Thymidylate synthetase 1136 1031A>G 3 X02308 X02308 188350 GEN-KL Thymidylate synthetase 1497 1392T>A 3 X02469 X02469 191170 GEN-PF Human mRNA for p53 350 215C>G P72R cellular tumor antigen X02469 X02469 191170 GEN-PF Human mRNA for p53 953 818G>A R273H cellular tumor antigen NRAS X02751 164790 GEN-XG Human N-ras mRNA and 221 (-506)A>G 5 flanking regions NRAS X02751 164790 GEN-XG Human N-ras mRNA and 390 (-337)OA 5 flanking regions X02812 X02812 190180 GEN-XR Human mRNA for 870 29C>T P10L transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 979 138C>G I46M SD-144146 1 Page 7 transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1632 791 C>T T264I transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1807 966C>T transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1930 1089G>A transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1942 1101 C>T transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 2013 1172G>A S391 N transforming growth factor- beta (TGF-beta) X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 424 64G>C E22Q X03635 X03635 133430 GEN-50 estrogen receptors 617 257C>T A86V X03635 X03635 133430 GEN-50 estrogen receptors 621 261G>C S X03635 X03635 133430 GEN-50 estrogen receptors 829 469C>T F X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1451 1091T>A V364E X03635 X03635 133430 GEN-50 estrogen receptors 1674 1314G>A M438I X03635 X03635 133430 GEN-50 estrogen receptors 2142 1782A>G S X03635 X03635 133430 GEN-50 estrogen receptors 2354 1994A>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 2550 2190A>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 2733 2373C>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 3181 2821T>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 3338 2978C>T 3 X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3 3294CCT>CC T X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3 3294delCCT X03635 X03635 133430 GEN-50 estrogen receptors 3896 35360A 3 SD-144146.1 Page X03635 X03635 133430 GEN-50 estrogen receptors 4378 4018T>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 6287 5927T>C 3 X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3732 3432T>C 3 receptor X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3951 3651 C>A 3 receptor X04571 X04571 131530 GEN- Human mRNA for kidney 4507 4071 G>A 3 KYO epidermal growth factor (EGF) precursor X04707 X04707 190160 GEN- Human c erb-A mRNA for 1295 995T>C I332T CCA thyroid hormone receptor ARAF1 X04790 311010 GEN- Human mRNA for A-raf-1 1659 1465C>T F 15C oncogene KIT X06182 164920 GEN-198 Human c-kit proto- 4656 4635G>T 3 oncogene mRNA ITGA5 X06256 135620 GEN- Human mRNA for 2562 25390A L847I 19B fibronectin receptor alpha subunit X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 83 (-54)G>C 5 X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 940 804G>A S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1327 1191T>C S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1906 1770OT S RAF1 X06409 164760 GEN- Human mRNA fragment for 486 487T>C 3 19K activated c raf-1 (exons 8- 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1947 1948C>T 19K activated c-raf-1 (exons 8- 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1992 1993C>A 19K activated c-raf-1 (exons 8- 17) GSTP1 X06547 134660 GEN- Human mRNA for class Pi 319 313A>G 1105V 19N glutathione S-transferase (GST-Pi, E C 2 5 1 18) GSTP1 X06547 134660 GEN- Human mRNA for class Pi 347 341 C>T A114V 19N glutathione S-transferase (GST-Pi, E C 2 5 1 18) GSTP1 X06547 134660 GEN- Human mRNA for class Pi 561 555C>T 19N glutathione S-transferase (GST-Pi, E C 2 5 1 18) SD-144146 1 Page 7 ITGB1 X07979 135630 GEN- Human mRNA for 1189 1086A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 1279 1176A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2713 2610T>C 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2878 2775T>A 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3339 3236A>G 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3531 3428G>A 3 4E5 fibronectin receptor beta subunit ANX5 X12454 131230 GEN- Human mRNA for vascular 128 (-1 )OT 5 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1413 1285T>G 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1431 1303C>T 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1518 1390G>A 3 1 M2 anticoagulant X12556 X12556 311030 GEN- Human mRNA for dbl 2670 2496T>G F832L 1 M8 proto-oncogene X13589 X13589 107910 GEN-56 Cytochrome P450, 364 240A>G S subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790OT R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790OT R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1655 1531 C>T 3 SD-144146.1 Page 7 subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1796 1672G>T subfamily XIX (aromatization of androgens) LIF X13967 159540 GEN- Human mRNA for 3710 3666T>G 1PZ leukaemia inhibitory factor (LIF/HILDA) CLU X14723 185430 GEN- Human SP-40,40 mRNA 131 84C>T 1SB for complement-associated protein SP-40,40 alpha- 1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 429 382G>T V128F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 836 789C>T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1234 1187C>T S396L 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1372 1325A>T Y442F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1482 14350T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1548 1501 C>T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1645 1598A>T 1SB for complement-associated protein SP-40,40 alpha-1 SD-144146.1 Page 7 and beta-1 chain CSNK2B X16312 115441 GEN- Human mRNA for 271 138T>C 1XW phosvitm/casein kinase II beta subunit CSNK2B X16312 115441 GEN- Human mRNA for 812 679A>T 1XW phosvitm/casein kinase II beta subunit CSNK2B X16312 1 15441 GEN- Human mRNA for 885 752T>C 1 XW phosvitm/casein kinase II beta subunit X17033 X17033 192974 GEN-LG Integrin, alpha 2 (CD49B, 4193 4145T>G alpha 2 subunit of VLA-2 receptor) X17033 X17033 192974 GEN-LG Integrin, alpha 2 (CD49B, 4849 4801A>G alpha 2 subunit of VLA-2 receptor) X17033 X17033 192974 GEN-LG Integrin, alpha 2 (CD49B, 4897 4849A>G alpha 2 subunit of VLA-2 receptor) FGFR1 X51803 136350 GEN- Human mRNA for 276 159T>G 32G fibroblast growth factor (FGF) receptor X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 4425 4299G>A S X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 4437 4311 G>C s X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 4528 4402G>A A1468T X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 4821 4695C>T S X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 5157 5031C>T s X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 5184 5058G>A s X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 5252 5126C>T P1709L X51841 X51841 147557 GEN-21 Leukocyte integrin beta-4 5410 5284T>C 3 SPI1 X52056 165170 GEN- Human mRNA for spι-1 1328 1117C>T 3 33A proto-oncogene X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3044 2869G>A 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3289 3114A>G 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3391 3216C>T 3 X52479 X52479 176960 GEN-LM Protein kinase C alpha 908 881 A>C D294A FGFR2 X52832 176943 GEN-341 Human bek mRNA for 338 159A>G S fibroblast growth factor receptor-BEK SD-144146 1 Page 7 FGFR2 X52832 176943 GEN-341 Human bek mRNA for 2903 2724A>T fibroblast growth factor receptor-BEK X54199 X54199 138440 GEN-LS Phosphoribosylglycinamide 168 90G>A formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimida zole synthetase X54315 X54315 114020 GEN-351 Human mRNA for N- 2549 2448T>C S cadherin X55005 X55005 190120 GEN- Human c-erbA-1 mRNA for 493 27A>G S 35S thyroid hormone receptor alpha X55005 X55005 190120 GEN- Human c-erbA-1 mRNA for 1523 1057G>A V353I 35S thyroid hormone receptor alpha X55740 X55740 129190 GEN- Human placental cDNA 3373 3324T>G 36H coding for δnucleotidase (EC 3.1.3.5) X57110 X57110 165360 GEN- Cas-Br-M (murine) 2695 2547T>A MKX ecotropic retroviral transforming sequence FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 83 28G>A V10I 37M fibroblast growth factor receptor (FGFR-4) FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 217 162T>G 37M fibroblast growth factor receptor (FGFR-4) GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 821 773C>T 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 979 931 G>A 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1187 1139T>G 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1354 1306C>T 38S plasma glutathione peroxidase SD-144146.1 Page 7 GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1443 1395C>T 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1516 14680A 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1581 1533C>T 3 38S plasma glutathione peroxidase X58377 X58377 147681 GEN- Interleukin 11 807 744A>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 927 864T>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 1964 1901T>C 3 38V ITGA6 X59512 147556 GEN- H. sapiens mRNA for 186 186C>G S 39W integrin alphaδ subunit ITGA6 X59512 147556 GEN- H. sapiens mRNA for 188 188G>C G63A 39W integrin alphaθ subunit X59543 X59543 180410 GEN-M2 Ribonucleoside 1037 850C S diphosphate reductase X59543 X59543 180410 GEN-M2 Ribonucleoside 2410 2223G>A S diphosphate reductase X59543 X59543 180410 GEN-M2 Ribonucleoside 2410 2223G>A S diphosphate reductase X59543 X59543 180410 GEN-M2 Ribonucleoside 2419 2232A>G S diphosphate reductase X59543 X59543 180410 GEN-M2 Ribonucleoside 2717 2530T>A 3 diphosphate reductase X59543 X59543 180410 GEN-M2 Ribonucleoside 2724 2537 Λ 2538ins F diphosphate reductase T X59543 X59543 180410 GEN-M2 Ribonucleoside 2882 2695A>C 3 diphosphate reductase X59618 X59618 180390 GEN-M3 Ribonucleotide reductase 189 (-6)T>G 5 M2 polypeptide X59618 X59618 180390 GEN-M3 Ribonucleotide reductase 524 330C>G S M2 polypeptide X59618 X59618 180390 GEN-M3 Ribonucleotide reductase 1636 1442C>T 3 M2 polypeptide X59618 X59618 180390 GEN-M3 Ribonucleotide reductase 2259 2065T>C 3 M2 polypeptide SD-144146.1 Page 7 NFKB2 X61498 164012 GEN- H-sapiens mRNA for NF- 2457 2294C>T P765L 3BW kB subunit KDR X61656 191306 GEN- H.sapiens mRNA for 2308 2308A>G T770A 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2353 2353G>C G785R 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2499 2499C>G N833K 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2537 2537A>T E846V 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 4123 4123G>C 3 3BZ growth factor receptor tyrosine kinase DNMT X63692 126375 GEN- H.sapiens mRNA for DNA 4507 4270C>T R1424C 3E4 (cytosin-5)- methyltransferase DNMT X63692 126375 GEN- H.sapiens mRNA for DNA 4692 4455C>T S 3E4 (cytosin-5)- methyltransferase DNMT X63692 126375 GEN- H-sapiens mRNA for DNA 4922 4685C>A T1562N 3E4 (cytosin-5)- methyltransferase DNMT X63692 126375 GEN- H-sapiens mRNA for DNA 235 4998C>T 3 3E4 (cytosin-5)- methyltransferase X64177 X64177 156351 GEN- H-sapiens mRNA for 63 40G>A A14T 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 90 67A>G K23E 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 125 102C>T S 3EQ metallothionein X64177 X64177 156351 GEN- H-sapiens mRNA for 131 108T>C S 3EQ metallothionein X64177 X64177 156351 GEN- H-sapiens mRNA for 168 145A>G I49V 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 182 159G>A S 3EQ metallothionein SD-144146- 1 Page 7 X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 51 44G>A R15H CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 116 109A>C K37Q CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 261 254G>A G85E CONVERTASE PRECURSOR X66364 X66364 123831 GEN- H-sapiens mRNA 495 471T>G C157W 3GM PSSALRE for serine/threonine protein kinase NTRK1 X66397 191315 GEN- H.sapiens tpr mRNA 2632 2335G>A V779I 3GN X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 112 21T>C S squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 292 201 C>T S squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1436 1345T>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H-sapiens mRNA for 1579 1488T>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H-sapiens mRNA for 1621 1530C>T 3 squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1719 1628A>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1904 1813G>C 3 squalene synthase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 718 638T>C 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 837 757C>A 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 882 802A>C 3 for phospholipid hydroperoxide glutathione peroxidase SD-144146.1 Page 7 X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 30 (-68)C>G 5 30E protein-tyrosine kinase X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 2010 1913A>G 3 30E protein-tyrosine kinase X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 2101 2004C>T 3 30E protein-tyrosine kinase X75962 X75962 600315 GEN- H.sapiens mRNA for OX40 836 831 C>T S MNA homologue X76061 X76061 180203 GEN- H-sapiens p130 mRNA for 685 616G>A V206M 30K 130K protein X76061 X76061 180203 GEN- H-sapiens p130 mRNA for 2659 2590T>C S 30K 130K protein X76061 X76061 180203 GEN- H.sapiens p130 mRNA for 3585 3516G>C 3 30K 130K protein X76104 X76104 600831 GEN- H.sapiens DAP-kinase 4376 4040A>G N1347S 300 mRNA X76105 X76105 600954 GEN- H.sapiens DAP-1 mRNA 887 728C>T 3 SON X76105 X76105 600954 GEN- H.sapiens DAP-1 mRNA 1089 930A>G 3 SON X76105 X76105 600954 GEN- H.sapiens DAP-1 mRNA 1890 1731A>G 3 SON X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 253 28G>T V10F omega) receptor 2 (splice variant) X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 1 128 903A>G S omega) receptor 2 (splice variant) X77794 X77794 601578 GEN-N8 Cyclin G1 1133 1013G>A 3 X79389 X79389 600436 GEN- H.sapiens GSTT1 mRNA 824 824T>C 3 3T7 X79483 X79483 602399 GEN- H.sapiens ERK6 mRNA for 1287 1254T>G 3 LPR extracellular signal regulated kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 25 (-74)C>T 5 SUM 2k) mRNA for serine/threonine protein X80230 X80230 603251 serine/threonine protein SD-144146.1 Page 7 kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 1516 1418G>A 3 SUM 2k) mRNA for serine/threonine protein kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 1574 1476A>G 3 SUM 2k) mRNA for serine/threonine protein kinase X83544 X83544 602074 GEN- H.sapiens DAP-3 mRNA 41 (-33)G>T 5 3Y6 X83544 X83544 602074 GEN- H.sapiens DAP-3 mRNA 285 212C>T S71 F 3Y6 X83544 X83544 602074 GEN- H.sapiens DAP-3 mRNA 294 221A>G D74G 3Y6 X83544 X83544 602074 GEN- H.sapiens DAP-3 mRNA 877 804T>C S 3Y6 X83544 X83544 602074 GEN- H.sapiens DAP-3 mRNA 1106 1033G>A V345I 3Y6 X83861 X83861 176806 GEN-5H Prostaglandin E receptor 3 387 180C>G S (subtype EP3) {alternative products} X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 32 (-161 )C>T 5 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 317 125G>A R42H 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 435 243C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 616 424G>A V142I 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 663 471 C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 900 708T>C 3 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 974 782C>T 3 3ZC BCI-2 homologue X86681 X86681 602110 GEN- H.sapiens mRNA for 1725 1340G>A 3 41 E nucleolar protein, HNP36 X90858 X90858 191730 GEN-NQ Uridine phosphorylase 309 (-44)C>T 5 X90858 X90858 191730 GEN-NQ Uridine phosphorylase 824 472G>A A158T X92106 X92106 602403 GEN- H.sapiens mRNA for 1405 1327A>G I443V SD-144146.1 Page 7 47S bleomycin hydrolase X96395 X96395 601107 GEN- H.sapiens mRNA for 848 811G>T A271S 4AM canalicular multidrug resistance protein Y00285 Y00285 147280 GEN-6I IGF-2 receptor 4613 4466G>A S1489N Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6371 6224C>T T2075M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6813 6666C>T Y00285 Y00285 147280 GEN-6I IGF-2 receptor 7150 7003G>A Y00285 Y00285 147280 GEN-6I IGF-2 receptor 8685 8538C>A 3 GPX1 Y00433 138320 GEN-TJ Human mRNA for 504 186G>A S glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 610 292C>G R98G glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 911 593C>T P198L glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1048 730A>C glutathione peroxidase (EC 1.1 1.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1 1 10 792A>C glutathione peroxidase (EC 1.11.1.9.) Y00486 Y00486 102600 GEN- Human APRT gene for 503 432C>A MGW adenine phosphoribosyltransferase Y00486 Y00486 102600 GEN- Human APRT gene for 505 434G>C R145P MGW adenine phosphoribosyltransferase Y00486 Y00486 102600 GEN- Human APRT gene for 792 721 A>G MGW adenine phosphoribosyltransferase PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 430 358A>G N120D Serpin (plasminogen activator-inhibitor 2, PAI-2) PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 1251 1179T>G Serpin (plasminogen activator-inhibitor 2, PAI-2) PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 1762 1690G>A SD-144146.1 Page 7 Serpin (plasminogen activator-inhibitor 2, PAI-2) OAT Y07511 258870 GEN- Human mRNA for kidney 1174 1134C>T 1E3 omithine aminotransferase (EC 2 6 1 13) OAT Y07511 258870 GEN- Human mRNA for kidney 1545 1505C>T 1E3 omithine aminotransferase (EC 2 6 1 13) Y08200 Y08200 601905 GEN- Homo sapiens mRNA for 1696 1422C>T 1FT rab geranylgeranyl transferase, alpha-subunit Y08201 Y08201 179080 GEN-9B Geranylgeranyl transferase 54 51T>A type II beta-subunit Y10659 Y10659 300119 GEN-1J6 H sapiens IL-13Ra mRNA 1116 1073G>A G358D Z11695 Z11695 176948 GEN-1L1 H sapiens 40 kDa protein 1287 1153G>A 3 kinase related to rat ERK2 Z11696 Z11696 601795 GEN-1L0 H sapiens 44kDa protein 449 449T>G I150S kinase related to rat ERK1 Z14138 Z14138 603259 GEN- H sapiens (Ewings 394 234T>C S 1QS sarcoma cell line) mRNA encoding open reading frame Z15108 Z15108 176982 GEN- H sapiens mRNA for 246 240T>C S 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H sapiens mRNA for 1694 1688A>C D563A 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H sapiens mRNA for 2033 2027G>A 3 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H sapiens mRNA for 2086 2080T>G 3 1TE protein kinase C zeta Z35491 Z35491 601497 GEN- H sapiens mRNA for novel 315 37G>A E13K 2ME glucocorticoid receptor- associated protein Z35491 Z35491 601497 GEN- H sapiens mRNA for novel 333 55G>A E19K 2ME glucocorticoid receptor- associated protein Z35491 Z35491 601497 GEN- H sapiens mRNA for novel 1297 1019A>C 3 2ME glucocorticoid receptor- associated protein CCNF Z36714 600227 GEN- H sapiens mRNA for cyclin 4062 4019C>A 3 2NB F SD-144146 1 Page 7 Z48810 Z48810 602664 GEN- H.sapiens mRNA for TX 1280 1239A>C 2YJ protease precursor Table 13. Identified Variances In Genes for Pathways Identified in Neurologi cal and Psychiatri c Diseases AB00026 AB00026 602784 GEN- Human mRNA for prepro 215 210T>C 3 3 16N cortistatin like peptide, complete eds AB00063 AB00063 601646 GEN-169 Homo sapiens mRNA for 1423 1409T>C L470P 4 4 protein phosphatase 2A delta (B) regulatory subunit, deltal isoform, complete eds AB00063 AB00063 601646 GEN-169 Homo sapiens mRNA for 2163 2149T>A 4 4 protein phosphatase 2A delta (B) regulatory subunit, deltal isoform, complete eds AB00234 AB00234 601581 GEN- Human mRNA for 2562 2148G>C S 1 1 1 CR KIAA0343 gene, complete eds AB00255 AB00255 601717 GEN- Human mRNA for 1467 1443T>C S 9 9 1AA hunc18b2, complete eds AB00255 AB00255 601717 GEN- Human mRNA for 1600 1576G>A V526I 9 9 1AA hunc18b2, complete eds AB00255 AB00255 601717 GEN- Human mRNA for 1669 1645G>A A549T 9 9 1AA hunc18b2, complete eds AB00591 AB00591 602758 GEN-VC Homo sapiens mRNA for 891 822C>T S 0 0 phosphatidylinositol 4- SD-144146, 1 Page 7 kinase, complete eds AB01071 ABO1071 602601 GEN- Homo sapiens mRNA for 1071 1010T>A 0 0 1SQ lectin-like oxidized LDL receptor, complete eds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 0 0 1SQ lectin-like oxidized LDL receptor, complete eds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 0 0 1SQ lectin-like oxidized LDL receptor, complete eds AB01071 ABO1071 602601 GEN- Homo sapiens mRNA for 1801 1740A>G 3 0 0 1SQ lectin-like oxidized LDL receptor, complete eds AB01071 ABO1071 602601 GEN- Homo sapiens mRNA for 2199 2138G>A 3 0 0 1SQ lectin-like oxidized LDL receptor, complete eds AB01388 AB01388 603208 GEN- Inward rectifier potassium 1469 1218A>G 3 9 9 CBP channel Kir 1.4 AB01531 ABO1531 None GEN- Homo sapiens mRNA for 377 332A>G D111G 8 8 L2T gamma2-adaptin, complete eds AB01531 AB01531 None GEN- Homo sapiens mRNA for 534 489G>A 8 8 L2T gamma2-adaptin, complete eds AB01531 ABO1531 None GEN- Homo sapiens mRNA for 2444 23990A 8 8 L2T gamma2-adaptin, complete eds AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 365 365C>T P122L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 381 381 G>A P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 624 624A>G P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 641 641 OT P214L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 1161 1161T>C P2X, LIGAND-GATED ION SD-144146.1 Page 7 CHANNEL, 4, P2RX4 AF004562 AF004562 602926 GEN-UK Homo sapiens hUNC18a 1830 1710A>T alternatively-spliced mRNA, complete eds AF004562 AF004562 602926 GEN-UK Homo sapiens hUNC18a 3322 3202T>C alternatively-spliced mRNA, complete eds AF004562 AF004562 602926 GEN-UK Homo sapiens hUNC18a 3673 3553C>G alternatively-spliced mRNA, complete eds AF006823 AF006823 603220 GEN-WS Homo sapiens TWIK- 1160 1035G>A related acid-sensitive K+ channel (TASK) mRNA, complete eds AF007548 AF007548 None GEN- Homo sapiens golgi 200 200G>A R67K 12G SNARE (GS27) mRNA, complete eds AF010126 AF010126 602998 GEN- Homo sapiens breast 206 195C>G 1 SR cancer-specific protein 1 (BCSG1 ) mRNA, complete eds AF010126 AF010126 602998 GEN- Homo sapiens breast 340 329A>T E110V 1SR cancer-specific protein 1 (BCSG1 ) mRNA, complete eds AF010126 AF010126 602998 GEN- Homo sapiens breast 518 507C>T 1 SR cancer-specific protein 1 (BCSG1 ) mRNA, complete eds AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1023 987T>C 1 NE P2X, LIGAND-GATED ION CHANNEL, 5, P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1025 989T>C F330S 1 NE P2X, LIGAND-GATED ION CHANNEL, 5, P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1090 1054G>C E352Q 1 NE P2X, LIGAND-GATED ION CHANNEL, 5, P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1321 1285G>A 1 NE P2X, LIGAND-GATED ION CHANNEL, 5, P2RX5 SD- 144146 1 Page 79 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1424 1388C>G 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1512 1476G>A 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1743 1707A>G 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1858 1822A>G 3 1NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016903 AF016903 None GEN- Homo sapiens agrin 516 516C>G S 1 M7 precursor mRNA, partial eds AF016903 AF016903 None GEN- Homo sapiens agrin 518 518G>C R173P 1 M7 precursor mRNA, partial eds AF016903 AF016903 None GEN- Homo sapiens agrin 3501 3501 C>T S 1 M7 precursor mRNA, partial eds AF016903 AF016903 None GEN- Homo sapiens agrin 6422 6422A>G 3 1 M7 precursor mRNA, partial eds AF016903 AF016903 None GEN- Homo sapiens agrin 6704 6704A>G 3 1 M7 precursor mRNA, partial eds HRH1 AF026261 600167 GEN- Histamine receptor H1 1068 1068A>G S 26W AVPR1B AF030512 600264 GEN- Homo sapiens small cell 273 150G>A S 4FF vasopressin subtype 1 b receptor mRNA, complete eds AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 314 291 C>T S AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 431 408T>C S AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 506 483A>G S AF033382 AF033382 603787 GEN- potassium channel 476 476G>T G159V 20T AF033382 AF033382 603787 GEN- potassium channel 1083 1083C>T S 20T AF034795 AF034795 116935 GEN- Homo sapiens cell matrix 1404 853G>A 3 SD-144146.1 Page 7 2GB adhesion regulator variant (CMAR) mRNA, complete eds AF034795 AF034795 116935 GEN- Homo sapiens cell matrix 1411 860C>T 2GB adhesion regulator variant (CMAR) mRNA, complete eds AF034795 AF034795 116935 GEN- Homo sapiens cell matrix 1811 1260G>A 2GB adhesion regulator variant (CMAR) mRNA, complete eds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 273 273G>A F mRNA, partial eds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 295 295G>C A99P mRNA, partial eds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 302 302C>T T101 I mRNA, partial eds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 1059 1059G>A 3 mRNA, partial eds AF036892 AF036892 601937 GEN-7W Nuclear receptor 842 659G>T R220I coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 1971 1788G>C Q596H coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 3048 2865A>G S coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 3909 3726A>G S coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 4483 4300T>C 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 5644 5461A>G 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 5675 5492T>A 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 6051 5868T>G 3 coactivator (ACTR) AF036892 AF036892 601937 GEN-7W Nuclear receptor 6664 6481G>A 3 coactivator (ACTR) AF038173 AF038173 601255 GEN- Homo sapiens clone 23723 1368 1368T>C 3 2QH axonal transporter of synaptic vesicles (ATSV) mRNA, partial eds SD-144146.1 Page 7 AF038173 AF038173 601255 GEN- Homo sapiens clone 23723 1387 1387A>G 3 2QH axonal transporter of synaptic vesicles (ATSV) mRNA, partial eds AF038173 AF038173 601255 GEN- Homo sapiens clone 23723 1501 1501 G>C 3 2QH axonal transporter of synaptic vesicles (ATSV) mRNA, partial eds AF039400 AF039400 603906 GEN- Homo sapiens calcium- 2787 2436T>C S MQY dependent chloride channel-1 (hCLCAI ) mRNA, complete eds AF043472 AF043472 603888 GEN- Homo sapiens Shab- 1840 1709T>G 3 2XX related delayed-rectifier K+ channel alpha subunit (KCNS3) mRNA complete eds AF043473 AF043473 602905 GEN- POTASSIUM CHANNEL 1308 1308G>T S 2XW PROTEIN KV2 1 AF046873 AF046873 602705 GEN- Homo sapiens synapsin 1364 1328G>A R443H LFF Ilia mRNA, complete eds AF047442 AF047442 None GEN- Homo sapiens vesicle 160 96G>A S LFO trafficking protein sec22b mRNA, complete eds AF048837 AF048837 602973 GEN- Homo sapiens cGMP- 1551 1491T>C S LGG specific phosphodiesterase (PDE9A2) mRNA complete eds AF052224 AF052224 None GEN- Homo sapiens neuronal 15480 15365T>G 3 MR1 double zinc finger protein (ZNF231 ) mRNA complete eds AF052224 AF052224 None GEN- Homo sapiens neuronal 15560 15445C>T 3 MR1 double zinc finger protein (ZNF231 ) mRNA, complete eds AF052224 AF052224 None GEN- Homo sapiens neuronal 15745 15630C>T 3 MR1 double zinc finger protein (ZNF231 ) mRNA, complete eds AF053233 AF053233 None GEN- Homo sapiens endobrevin 225 201A>G S SD-1441461 Page 79 38F mRNA, complete eds AF058921 AF058921 None GEN- LJY ph AF058921 AF058921 None GEN- LJY ph AF060538 AF060538 185880 GEN-LL4 proteιn-1 B mRNA, alternatively spliced, complete eds AF064548 AF064548 603506 GEN- Homo sapiens low-density 1695 16470T KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete eds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4037 3989C>T A1330V KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete eds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4683 4635C>A KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete eds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4802 4754C>T S1585L KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete eds AF077671 AF077671 600755 GEN- Homo sapiens synapsin Ha 1246 1225T>C LMT (SYN2) mRNA complete eds AJ130763 AJ130763 254780 GEN- Homo sapiens mRNA for 161 159G>A LDP LAFPTPase, isoform 1 , partial AJ130763 AJ130763 254780 GEN- Homo sapiens mRNA for 287 285T>A LDP LAFPTPase, isoform 1 , partial D12614 D12614 153440 GEN-QD Human mRNA for 319 179C>A T60N lymphotoxin (TNF-beta), complete eds D13388 D13388 602837 GEN-A7 DNAJ PROTEIN 207 90C>T SD-144146 1 Page 7 HOMOLOG 2 CYP11 B2 D13752 124080 GEN- Human CYP11 B2 gene for 1600 1593G>A 3 CCD steroid 18-hydroxylase, complete eds D13811 D13811 238310 GEN-AA Glycine cleavage system: 277 148G>T V50L Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1073 944G>A R315K Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1083 954G>A S Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1773 1644C>T 3 Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 2037 1908C>T 3 Protein T D16469 D16469 300197 GEN- Human mRNA for ORF, Xq 2294 941A>G 3 1Y2 terminal portion D16469 D16469 300197 GEN- Human mRNA for ORF, Xq 2460 1107A>G 3 1Y2 terminal portion D16469 D16469 300197 GEN- Human mRNA for ORF, Xq 2660 1307C>A 3 1Y2 terminal portion D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1035 599T>G I200S 1c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039C>T R347C 1 c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039C>T R347C 1c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 2048 1612C>T 3 1c D25418 D25418 600022 GEN-78 Prostaglandin 12 726 635G>A R212H (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1047 956C>G S319W (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1075 984A>C S (prostacyclin) receptor (IP) D28538 D28538 604102 GEN- Metabotropic glutamate 531 381A>G S 2DC receptor type 5 D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 25 (-47)G>A 5 transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1332 1261A>G 1421V transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1855 1784G>C 3 SD-144146.1 Page 7 transformylase PTGIR D38128 600022 GEN- Human IP gene for 203 204C>G 4DH prostacyclin receptor, exon 3 PTGIR D38128 600022 GEN- Human IP gene for 231 232C>A 4DH prostacyclin receptor, exon 3 D38145 D38145 601699 GEN- Human mRNA for 1646 1619T>C 4E3 prostacyclin synthase, complete eds D45887 D45887 114182 GEN-BA Calmodulin 1 34 (-35)G>T (phosphorylase kinase, delta) D49394 D49394 182139 GEN-5 Serotonin 5-HT receptors 1914 1695C>G 5-HT3 D50678 D50678 602600 GEN- Human mRNA for 3378 3276G>A SOY apolipoprotein E receptor 2, complete eds D50678 D50678 602600 GEN- Human mRNA for 3755 3653G>A SOY apolipoprotein E receptor 2, complete eds D50678 D50678 602600 GEN- Human mRNA for 3949 3847G>C SOY apolipoprotein E receptor 2, complete eds D50678 D50678 602600 GEN- Human mRNA for 43684266T>A SOY apolipoprotein E receptor 2, complete eds D50678 D50678 602600 GEN- Human mRNA for 44554353G>A SOY apolipoprotein E receptor 2, complete eds D87673 D87673 602438 GEN-444 Human mRNA for heat 274 270C>T shock transcription factor 4, complete eds D87673 D87673 602438 GEN-444 Human mRNA for heat 1463 1459G>C shock transcription factor 4, complete eds D87845 D87845 602344 GEN- Human mRNA for platelet- 2299 2096G>A 44C activating factor acetylhydrolase 2, complete eds D87845 D87845 602344 GEN- Human mRNA for platelet- 2332 2129A>G SD-144146.1 Page 79 44C activating factor acetylhydrolase 2, complete eds D89052 D89052 603717 GEN- Human mRNA for proton- 56 (-27)G>T 5 45C ATPase-like protein, complete eds D89052 D89052 603717 GEN- Human mRNA for proton- 719 637G>A 3 45C ATPase-like protein, complete eds D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 434 (-1284)A>T 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 889 (-829)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 1 156 (-562)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2644 927T>C S D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2920 1203A>G 3 LRP1 D90070 107770 GEN-466 Human ATL-derived PMA- 686 513T>G 3 responsive (APR) peptide mRNA EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2228 1748G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2376 1896G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2840 2360G>C 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2935 2455G>A 3 SD-144146.1 Page 7 4DX EDNRA D90348 131243 GEN- Endothelin Receptor Type 3294 2814A>G 3 4DX A J00123 J00123 131330 GEN- Human enkephalm gene 81 81C>T S MK4 FGA J00127 134820 GEN-T3 Human fibrinogen alpha- 560 530T>A I177N chain mRNA, complete eds FGA J00127 134820 GEN-T3 Human fibrinogen alpha- 1138 1108G>T A370S chain mRNA, complete eds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 543 543C>T S chain mRNA partial eds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 1101 1101C>T S chain mRNA partial eds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 1409 1409G>A R470K chain mRNA, partial eds J00137 J00137 306900 GEN-OX COAGULATION FACTOR 581 580A>G T194A IX DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 829 787C>T 3 4E9 reductase gene J02611 J02611 107740 GEN-60 Human apolipoprotein D 676 615T>G 3 mRNA, complete eds J02611 J02611 107740 GEN-60 Human apolipoprotein D 683 622T>G 3 mRNA complete eds J02611 J02611 107740 GEN-60 Human apolipoprotein D 701 640C>G 3 mRNA, complete eds J02611 J0261 1 107740 GEN-60 Human apolipoprotein D 745 684A>G 3 mRNA, complete eds CBG J02943 122500 GEN-Y2 Human corticosteroid 106 71A>T D24V binding globulin mRNA, complete eds CBG J02943 122500 GEN-Y2 Human corticosteroid 971 936T>C binding globulin mRNA, complete eds CBG J02943 122500 GEN-Y2 Human corticosteroid 1229 11 4G>A binding globulin mRNA, complete eds J03143 J03143 107470 GEN-ZK Human interferon-gamma 1098 1050T>G SD-144146 1 Page 7 receptor mRNA, complete eds J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 932 380G>A R127H J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1063 511G>A A171T J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1190 638C>G 3 J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1201 649C>T 3 J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 172 57C>T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 559 444C>T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1704 1589C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1833 1718C>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1959 1844A>C 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3301 3186C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3991 3876A>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor CHGA J03483 118910 GEN- Human chromogranin A 583 501T>G N167K HE mRNA, complete eds CHGA J03483 118910 GEN- Human chromogranin A 1405 1323A>G S H E mRNA, complete eds CHGA J03483 118910 GEN- Human chromogranin A 1543 1461C>T 3 H E mRNA, complete eds SD-144146.1 Page 7 J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1569 1493A>C N498T dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1624 1548T>A dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1813 1737A>G dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 2096 2020T>C dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03778 J03778 157140 GEN-C7 MICROTUBULE- 391 354G>A S ASSOCIATED PROTEIN TAU J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1202 1164C>T s 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1237 1199T>G I400S 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1372 1334C>G P445R 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1379 1341C>T S 2c J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 454 401 G>A R134K cyclohydrolase SD-144146.1 Page 8 J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 969 916C>G Q306E cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 1614 1561T>C S cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2011 1958G>A R653Q cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2335 2282C>T T761 M cyclohydrolase J04046 J04046 114183 GEN- Human calmodulin mRNA, 791 688C>T 3 13N complete eds J04046 J04046 114183 GEN- Human calmodulin mRNA, 881 778T>C 3 13N complete eds J04046 J04046 114183 GEN- Human calmodulin mRNA, 1927 1824T>C 3 13N complete eds J04144 J04144 106180 GEN-2L Angiotensin-converting 803 781 G>T A261S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1042 1020C>T S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- S enzyme (ACE) 1515CCT>CC T J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- [P505V;50 enzyme (ACE) 1515delCCT 6-505del] J04144 J04144 106180 GEN-2L Angiotensin-converting 1797 1775A>G D592G enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2215 2193G>A S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2350 2328A>G S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2505 2483T>C M828T enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S enzyme (ACE) J05158 J05158 603104 GEN-173 Human carboxypeptidase 2314 2314C>T 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2316 2316G>T 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2332 2332G>T 3 N mRNA, 3 end SD-144146.1 Page 80 J05158 J05158 603104 GEN-173 Human carboxypeptidase 2541 2541 G>A 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2651 2651 C>T 3 N mRNA, 3 end J05176 J05176 107280 GEN-PT Human alpha-1 - 240 240A>G S antichymotrypsin mRNA, 3 end J05176 J05176 107280 GEN-PT Human alpha-1- 327 327C>T S antichymotrypsin mRNA, 3 end J05176 J05176 107280 GEN-PT Human alpha-1- 554 554T>C V185A antichymotrypsin mRNA, 3 end J05200 J05200 180901 GEN- Human ryanodine receptor 14981 14876G>T G4959V 17B mRNA, complete eds J05594 J05594 601688 GEN-E Prostaglandin 15-OH 173 156A>G S dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 913 896C>G 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 950 933G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1448 1431G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) K00396 K00396 107741 GEN-PO Human apolipoprotein E 121 61G>A E21K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 151 91G>A E31K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 197 137T>C L46P (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 204 144delG F (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 238 178A>G T60A (epsilon 2 and 3 alleles) SD-144146.1 Page 80 mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 365 305C>G P102R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 409 349G>A A117T (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Httrπan apolipoprotein E 448 388T>C C130R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 494434G>A G145D (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 515455G>A R152Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 520460C>A R154S (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 538 478C>T R160C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 547487C>T R163C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 548488G>A R163H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 550490A>G K164E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 743 683G>A F (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 785725G>A R242Q SD-144146.1 Page 80 (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 796 736C>T R246C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 821 761T>A V254E (epsilon 2 and 3 alleles) K00396 K00396 107741 GEN-PO Human apolipop (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 935 875G>A R292H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 1000 940A>C S314R (epsilon 2 and 3 alleles) mRNA K00557 K00557 602529 GEN-TY human alpha-tubulin 126 126G>C mRNA, 3 end K01911 K01911 162640 GEN-20 Neuropeptide Y 236 150G>A S K01911 K01911 162640 GEN-20 Neuropeptide Y 290204C>T S AGT K02215 106150 GEN-WK Human angiotensinogen 659 620C>T T207M mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 842803T>C M268T mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1155 1116G>A S mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1476 1437C>A S mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1821 1782G>A 3 mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 2053 2014A>C 3 mRNA, complete CDS KNG K02566 228960 GEN-X2 Human alpha-2-thiol 1248 1199C>A T400K proteinase inhibitor mRNA, complete coding sequence K02770 K02770 147720 GEN-5M Interleukin 1 , beta 19 (-68)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 26 (-61 )A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 48 (-39)OT 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 114 28G>A E10K SD-144146. Page 80 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 119 33G>A M11 I L03558 L03558 601145 GEN- Homo sapiens cystatin B 485 390A>G 3 110 mRNA, complete eds L05597 L05597 None GEN- Serotonin 5-HT receptors 824 600T>C S 4EV 5-HT1 F L05597 L05597 None GEN- Serotonin 5-HT receptors 1010 786 Λ 787insA [H262Q;2 4EV 5-HT1 F ATAAAATTC 2 Λ 263ins EDNRB L06623 131244 GEN- Endothelin Receptor Type 88 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 332 99C>T S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B TGFBR3 L07594 600742 GEN- Human transforming 3966 3618G>C 3 1 EA growth factor-beta type III receptor (TGF-beta) mRNA, complete eds L07861 L07861 176977 GEN-DO Protein kinase C, delta 445 387G>A S L07861 L07861 176977 GEN-DO Protein kinase C, delta 1835 1777G>A V593M GNRHR L07949 138850 GEN- Gonadotropin releasing 1371 1347C>A 3 1 F1 hormone agonist CCKBR L08112 118445 GEN- Cholecystokinin (CCKb) 456 456G>A S 1 FL L08485 L08485 137142 GEN-G Gamma-aminobutyric acid 1646 1341G>T S (GABA) A receptor, alpha 5 L08485 L08485 137142 GEN-G Gamma-aminobutyric acid 2113 1808C>T 3 (GABA) A receptor, alpha 5 INPP1 L08488 147263 GEN- Human inositol 185 (-142)T>G 5 1 FY polyphosphate 1- phosphatase mRNA, complete eds INPP1 L08488 147263 GEN- Human inositol 479 153T>G S 1 FY polyphosphate 1- phosphatase mRNA, complete eds INPP1 L08488 147263 GEN- Human inositol 674 348A>G S SD-144146.1 Page 80 1 FY polyphosphate 1- phosphatase mRNA, complete eds INPP1 L08488 147263 GEN- Human inositol 806 480G>A 1 FY polyphosphate 1- phosphatase mRNA, complete eds MIF L10612 153620 GEN-1J8 Human glycosylation- 170 96C>G inhibiting factor mRNA, complete eds MIF L10612 153620 GEN-1J8 Human glycosylation- 221 1470G inhibiting factor mRNA, complete eds MIF L10612 153620 GEN-1J8 Human glycosylation- 227 153C>G inhibiting factor mRNA, complete eds MIF L10612 153620 GEN-1 J8 Human glycosylation- 239 165G>A inhibiting factor mRNA, complete eds MIF L10612 153620 GEN-1J8 Human glycosylation- 329 255C>A inhibiting factor mRNA, complete eds MIF L10612 153620 GEN-1J8 Human glycosylation- 445 371 C>T inhibiting factor mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 191 153C>T LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 200 162G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 230 192T>C LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 242 204G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 295 257C>T A86V LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 330 292G>A D98N SD-144146.1 Page 80 LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 338 300G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 638 600C>G LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 676 638A>G H213R LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 940 902G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 1011 973T>C LVD sulfotransferase mRNA, complete eds L11005 L11005 602841 GEN- Human aldehyde oxidase 4284 4154C>A 1JU (hAOX) mRNA, complete eds L11005 L11005 602841 GEN- Human aldehyde oxidase 4447 4317G>C 1JU (hAOX) mRNA, complete eds L11005 L11005 602841 GEN- Human aldehyde oxidase 4525 4395T>G 1JU (hAOX) mRNA, complete eds L11005 L11005 602841 GEN- Human aldehyde oxidase 4675 4545G>A 1JU (hAOX) mRNA, complete eds L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1003 904C>A L302I L11667 L1 1667 601753 GEN-H Cyclophilin D 40kDa 1283 1184A>G 3 L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1479 1380T>A 3 L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1519 1420T>C 3 L11931 L11931 182144 GEN- Human cytosolic serine 1444 1420C>T L474F 4DT hydroxymethyltransferase (SHMT) mRNA, complete eds L11931 L11931 182144 GEN- Human cytosolic serine 1541 15170T 4DT hydroxymethyltransferase (SHMT) mRNA, complete eds SD-144146. Page 80 L12052 L12052 171885 GEN- Human cAMP 1707 1707G>A 3 I LK phosphodiesterase mRNA, 3 end L13266 L13266 138249 GEN-J Glutamate Aspartate 1618 525G>C S receptor NMDA 1 L13266 L13266 138249 GEN-J Glutamate Aspartate 1792 699C>A s receptor NMDA 1 L13266 L13266 138249 GEN-J Glutamate Aspartate 1948 855G>A s receptor NMDA 1 L13266 L13266 138249 GEN-J Glutamate Aspartate 2713 1620T>G I540M receptor NMDA 1 L13266 L13266 138249 GEN-J Glutamate Aspartate 3137 2044G>T A682S receptor NMDA 1 L13266 L13266 138249 GEN-J Glutamate Aspartate 3241 2148G>A S receptor NMDA 1 MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1467 1250C>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete eds MDCR L13385 601545 GEN- Homo sapiens(clone 71) 1868 1651C>T 3 106 Miller-Dieker lissencephaly protein (LIS1) mRNA, complete eds MDCR L13385 601545 GEN- Homo sapiens(clone 71) 1917 1700C>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete eds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 2962 2745G>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete eds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 4589 4372G>A 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete eds L13436 L13436 108961 GEN-2Q guanylate cyclase 2222 2223C>T 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 2444 2445C>T 3 L13977 L13977 176785 GEN- Human 2009 1980T>C 3 I PX prolylcarboxypeptidase mRNA, complete eds CAMK4 L17000 114080 GEN- Homo sapiens 1381 1340C>T A447V SD-144146.1 Page 80 1ZR calcium/calmodulin- dependent protein kinase mRNA, complete eds L17075 L17075 601284 GEN- Human TGF-b superfamily 838 747G>A S 1ZQ receptor type I mRNA, complete eds PRKCI L18964 300094 GEN- Human protein kinase C 573 309T>G S 21 N iota isoform (PRKCI) mRNA, complete eds L19760 L19760 600322 GEN- Human nerve-terminal 259 171 C>G S 22D protein (isoform SNAP25A) mRNA, complete eds L19760 L19760 600322 GEN- Human nerve-terminal 418 330T>C S 22D protein (isoform SNAP25A) mRNA, complete eds L19760 L19760 600322 GEN- Human nerve-terminal 629 541A>T I181 F 22D protein (isoform SNAP25A) mRNA, complete eds L19956 L19956 600641 GEN- Human aryl 243 105A>G S LVE sulfotransferase mRNA, complete eds L19956 L19956 600641 GEN- Human aryl 284 146C>T S49F LVE sulfotransferase mRNA, complete eds HD L20431 143100 GEN- Homo sapiens Huntington 1536 1535T>G I512S 23G disease-associated protein (HD) mRNA, complete eds HD L20431 143100 GEN- Homo sapiens Huntington 2112 21110G 3 23G disease-associated protein (HD) mRNA, complete eds HD L20431 143100 GEN- Homo sapiens Huntington 3788 3787G>A 3 23G disease-associated protein (HD) mRNA, complete eds HD L20431 143100 GEN- Homo sapiens Huntington 4912 4911 G>A 3 23G disease-associated protein (HD) mRNA, complete eds HD L20431 143100 GEN- Homo sapiens Huntington 5454 5453C>T 3 23G disease-associated protein (HD) mRNA, complete eds L20463 L20463 600445 GEN-M G-protein coupled 1671 1380A>G 3 adenosine A3 receptor SD-144146.1 Page 80 VLDLR L20470 192977 GEN- Human very low density 336 (-56)C>T 23D lipoprotein receptor mRNA, complete eds VLDLR L20470 192977 GEN- Human very low density 3566 3175T>C 23D lipoprotein receptor mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 676 (-721)T>G 25C Axholesterol acyltransferase mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 814 (-583)C>T 25C Axholesterol acyltransferase mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 1993 597C>T 25C Axholesterol acyltransferase mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 2365 9690T 25C Axholesterol acyltransferase mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 2821 1425G>C 25C Axholesterol acyltransferase mRNA, complete eds SOAT L21934 102642 GEN- Human acyl coenzyme 3537 2141T>C 25C Axholesterol acyltransferase mRNA, complete eds L22214 L22214 102775 GEN-2S Adenosine A1 receptor 557 147G>C s (ADORA1 ) L22214 L22214 102775 GEN-2S Adenosine A1 receptor 2622 2212G>A 3 (ADORA1) SLC6A3 L24178 126455 GEN-283 Homo sapiens dopamine 1917 1898C>T 3 transporter mRNA, complete eds L24470 L24470 600563 GEN-O PROSTAGLANDIN F 1422 1185T>C RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1490 1253C>T RECEPTOR SD-144146.1 Page 81 L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1517 1280A>G 3 RECEPTOR L24470 L24470 600563 GEN-O PROSTAGLANDIN F 2244 2007A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 22992062A>G 3 RECEPTOR OPRM1 L25119 600018 GEN- Human Mu opiate receptor 41 (-172)G>T 5 4EP (MOR1 ) mRNA, complete 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 102 (-111)C>T 5 4EP (MOR1 ) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 229 17C>T A6V 4EP (MOR1 ) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 229 17C>T A6V 4EP (MOR1 ) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 236 24G>A S 4EP (MOR1) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 330 118A>G N40D 4EP (MOR1 ) mRNA, complete eds OPRM1 L25119 600018 GEN- Human Mu opiate receptor 330 118A>G N40D 4EP (MOR1 ) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 991 779G>A R260H 4EP (MOR1) mRNA, complete eds OPRM1 L251 19 600018 GEN- Human Mu opiate receptor 1005 793C>T R265C 4EP (MOR1 ) mRNA, complete eds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 1154942G>A S 4EP (MOR1) mRNA, complete eds OPRM1 L25119 600018 GEN- Human Mu opiate receptor 1154 942G>A S 4EP (MOR1) mRNA, complete eds L26232 L26232 172425 GEN- Human phospholipid 906 819C>T S 2AK transfer protein mRNA, SD-144146.1 Page 81 complete eds L26232 L26232 172425 GEN- Human phospholipid 1547 1460C>A T487K 2AK transfer protein mRNA, complete eds PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 547 159C>T S (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 611 223G>A V75M (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 1725 1337A>G Q446R (subtype EP2), 53kD L31773 L31773 104220 GEN- Adrenergic receptor alpha 171 171 C>T S 4DD 1 b L31773 L31773 104220 GEN- Adrenergic receptor alpha 534 534C>T S 4DD 1 b L31773 L31773 104220 GEN- Adrenergic receptor alpha 549 549G>A S 4DD 1 b L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5667 5442C>G S Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5669 5444G>C G1815A Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5745 5520C>G D1840E Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5941 5716C>A 3 Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5971 5746C>A 3 Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5985 5760G>A 3 Type L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 1857 1740C>T S L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2052 1935C>T S L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2160 2043T>C S L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2280 2163T>C S L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2644 2527G>A D843N L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2749 2632C>A 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2799 2682A>G 3 SD-144146.1 Page 81 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 28042687A>G 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 28442727C>G 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 28482731G>A 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 28572740A>G 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2877 2760A>G 3 L 4-KINASE ALPHA L36151 L36151 600286 GEN-DT PHOSPHATIDYLINOSITO 2942 2825C>T 3 L 4-KINASE ALPHA L36566 L36566 601970 GEN- Human helodermin- 1397 1235A>G H412R 2N5 preferring VIP receptor (VIP2/PACAP receptor) mRNA, complete eds L36566 L36566 601970 GEN- Human helodermin- 1440 1278A>C 2N5 preferring VIP receptor (VIP2/PACAP receptor) mRNA, complete eds L37792 L37792 186590 GEN-DX syntaxin 1A 1337 1336A>G L41147 L41147 601109 GEN-2T Serotonin 5-HT receptors 287 (-181)OT 5-HT6 L42373 L42373 601643 GEN- Homo sapiens 1135564C>T 2U7 phosphatase 2A B56-alpha (PP2A) mRNA, complete eds L42373 L42373 601643 GEN- Homo sapiens 2297 1726T>A 2U7 phosphatase 2A B56-alpha (PP2A) mRNA, complete eds L42373 L42373 601643 GEN- Homo sapiens 2368 1797T>C 2U7 phosphatase 2A B56-alpha (PP2A) mRNA, complete eds L42373 L42373 601643 GEN- Homo sapiens 2782 2211 G>A 2U7 phosphatase 2A B56-alpha (PP2A) mRNA, complete eds L42373 L42373 601643 GEN- Homo sapiens 2952 2381 T>G SD-144146.1 Page 81 2U7 phosphatase 2A B56-alpha (PP2A) mRNA, complete eds L76224 L76224 138254 GEN- Glutamate Aspartate 2526 2526G>A S 30S receptor NMDA 2C L77864 L77864 602709 GEN-3QI Homo sapiens stat-like 406 306G>A S protein (Fe65) mRNA, complete eds L77864 L77864 602709 GEN-3QI Homo sapiens stat-like 1911 1811G>A C604Y protein (Fe65) mRNA, complete eds L77864 L77864 602709 GEN-3QI Homo sapiens stat-like 2639 2539A>C 3 protein (Fe65) mRNA, complete eds M10901 M10901 138040 GEN-2W Corticosteroid nuclear 1220 1088A>G N363S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- S receptor b 1893AG>AG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- F receptor b 1893delAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2054 1922A>T D641V receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2372 2240T>G I747S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>C L753F receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>T L753F receptor b M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 2166 2034C>T S M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3353 3221T>G 3 M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3398 3266T>G 3 M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 1573 1530T>A S M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 1799 1756C>T F M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 3041 2998G>A V1000I M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 4474 4431 A>C 3 M12578 M12578 152760 GEN-2Y Gonadotropin-releasing 79 47G>C W16S hormone (leutinizing- releasing hormone) M12674 12674 133430 GEN-7Z Estrogen receptor 1267 975C>G S HEXB M13519 268800 GEN-101 Human N-acetyl-beta- 63 63G>C S SD-144146.1 Page 81 glueosaminidase (HEXB) mRNA, 3 end HEXB M13519 268800 GEN-101 Human N-acetyl-beta- 490 490T>G S164A glucosaminidase (HEXB) mRNA, 3 end HEXB M13519 268800 GEN-101 Hum glucosa HEXB M13519 268800 GEN-101 Hum glucosa M14113 M14113 306700 GEN-5T DBI M14200 125950 GEN- Human diazepam binding 291 272A>T Y91 F 1QW inhibitor (DBI) mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 184 (-11)T>C proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 270 76G>C V26L proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 446 252C>T proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1254 1060C>G proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1306 1112G>A proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1336 1142T>A proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1338 1144C>T proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1451 1257G>A proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1462 1268C>T proteinase mRNA, SD-144146.1 Page 81 complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1522 1328G>C proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1557 1363G>C proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1585 1391 C>A proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1630 1436T>C proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1668 1474T>G proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1712 1518C>G proteinase mRNA, complete eds M14221 M14221 161565 GEN-QM Human cathepsin B 1898 1704A>G proteinase mRNA, complete eds M14333 M14333 137025 GEN-QO Homo sapiens c-syn 562 (-18)A>C protooncogene mRNA, complete eds M14333 M14333 137025 GEN-QO Homo sapiens c-syn 1647 1068T>C protooncogene mRNA, complete eds M14333 M14333 137025 GEN-QO Homo sapiens c-syn 2152 1573A>T T525S protooncogene mRNA, complete eds ARG1 M14502 207800 GEN- Human liver arginase 800 744C>T S IRE mRNA, complete eds M14539 M14539 134570 GEN-QP Human factor XIII subunit a 1781 1781C>T P594L mRNA, 3 end M 14539 M14539 134570 GEN-QP Human factor XIII subunit a 2041 2041 C>G Q681 E mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 2412 2412C>T 3 mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 2446 2446G>A 3 mRNA, 3 end SD-144146.1 Page 81 M14539 M14539 134570 GEN-QP Human factor XIII subunit a 3282 3282G>T 3 mRNA, 3 end NGFR M14764 162010 GEN- Human nerve growth factor 2716 2603C>T 3 1 S8 receptor mRNA, complete eds NGFR M 14764 162010 GEN- Human nerve growth factor 2729 2616C>T 1 S8 receptor mRNA, complete NGFR 14764 162010 GEN- Human nerve growth fa 1 S8 receptor mRNA, complete eds NGFR M14764 162010 GEN- Human nerve growth factor 3252 3139C>G 1 S8 receptor mRNA, complete eds M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 466 (-1122)C>G 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 565 (-1023)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1541 (-47)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1687 100G>A V34M M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1839 252G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2110 523C>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2640 1053G>C S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2826 1239G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2862 1275C>G 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2864 12770A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2865 1278C>A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 3371 1784A>T 3 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 422 293A>G D98G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 557 428G>A G143D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 564 435- F146V 436TT>AG>A G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 568 439C>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 596 467A>G Y156C SD-144146.1 Page 81 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 941 812C>T T271M M16541 M16541 177400 GEN-35 Butyrylcholinesterase 961 832A>C T278P M16541 M16541 177400 GEN-35 Butyrylcholinesterase 978 849G>C E283D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1201 1072T>A L358I M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1306 1177G>A G393R M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1382 1253G>T G418V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1549 1420T>G F474V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1564 1435G>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1703 1574A>T E525V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1756 1627C>T R543C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16765 M16765 104760 GEN- Human cerebrovascular 1283 1274A>C 3 1YM and neuritic plaque amyloid beta-protein mRNA, 3 end F5 M16967 227400 GEN- Human coagulation factor 2391 2301G>A S 1Z8 V mRNA, complete eds F5 M16967 227400 GEN- Human coagulation factor 2663 2573G>A R858K 1Z8 V mRNA, complete eds F5 M16967 227400 GEN- Human coagulation factor 2684 2594G>A R865H 1Z8 V mRNA, complete eds F5 M16967 227400 GEN- Human coagulation factor 5380 5290G>A V1764M 1Z8 V mRNA, complete eds CYP21 M17252 201910 GEN-201 Human cytochrome 224 224G>A R75H P450c21 mRNA, 3 end CYP21 M17252 201910 GEN-201 Human cytochrome 330 330C>T S P450c21 mRNA, 3 end CYP21 M17252 201910 GEN-201 Human cytochrome 745745T>C 3 P450c21 mRNA, 3 end M17262 M17262 176930 GEN-SM Human prothrombin (F2) 511 480C>T S gene, complete eds, and Alu and Kpnl repeats M20132 M20132 313700 GEN-38 Androgen receptor 995 633G>A S (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1385 1023T>C S SD-144146.1 Page 81 (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1786 1424G>A G475E (dihydrotestosterone receptor) M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 331 294G>A S iung M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 400 363C>A D121 E M21551 M21551 162340 GEN- Human neurome 24P mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 116 (-20)G>T 5 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 231 96G>C S 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143- S 25V mRNA, complete eds 144GT>GT PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143-144delGT F 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 643 508C>T 3 25V mRNA, complete eds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 700 565G>C 3 25V mRNA, complete eds M22538 M22538 600532 GEN-EO NADH dehydrogenase 219 201A>T S (ubiquinone) flavoprotein 2 (24kD) M22538 M22538 600532 GEN-EO NADH dehydrogenase 469 451 G>A A151T (ubiquinone) flavoprotein 2 (24kD) M22613 M22613 227600 GEN-3C COAGULATION FACTOR 738 7380T S X PRECURSOR M22632 M22632 138150 GEN-EP Glutamic-oxaloacetic 221 213T>C S transaminase 2, mitochondrial (aspartate aminotransferase 2) M22632 M22632 138150 GEN-EP Glutamic-oxaloacetic 236 228T>G S transaminase 2, SD-144146.1 Page 81 mitochondrial (aspartate aminotransferase 2) M22632 M22632 138150 GEN-EP Glutamic-oxaloacetic 2009 2001C>T 3 transaminase 2, mitochondrial (aspartate aminotransferase 2) M24194 M24194 None GEN-286 Human MHC protein 79 (-17)OA 5 homologous to chicken B complex protein mRNA, complete eds M24194 M24194 None GEN-286 Human MHC protein 102 7G>T F homologous to chicken B complex protein mRNA, complete eds M24194 M24194 None GEN-286 Human MHC protein 464 369A>T S homologous to chicken B complex protein mRNA, complete eds M24194 M24194 None GEN-286 Human MHC protein 846 751G>T A251S homologous to chicken B complex protein mRNA, complete eds M24194 M24194 None GEN-286 Human MHC protein 848 753C>T S homologous to chicken B complex protein mRNA, complete eds M24857 M24857 180190 GEN-80 Retinoic acid receptor, 1694 1280C>T S427L gamma 1 CRYAB M24906 123590 GEN- Homo sapiens Rosenthal 107 107T>G V36G 28V fiber protein (alpha-B- crystallin) mRNA, 3 end CRYAB M24906 123590 GEN- Homo sapiens Rosenthal 303303A>T 3 28V fiber protein (alpha-B- crystallin) mRNA, 3 end CRYAB M24906 123590 GEN- Homo sapiens Rosenthal 305305G>A 3 28V fiber protein (alpha-B- crystallin) mRNA, 3 end GAP43 M25667 162060 GEN- Human neuronal growth 1086 995T>G 3 29U protein 43 (GAP-43) mRNA, complete eds M25756 M25756 118930 GEN- Human secretogranin II 855 793G>A V265M SD-144146.1 Page 82 29W gene, complete eds M25756 M25756 118930 GEN- Human secretogranin II 899 837C>T S 29W gene, complete eds M26383 M26383 146930 GEN-3E Interleukin 8 259 185C>G A62G M26383 M26383 146930 GEN-3E Interleukin 8 1237 1163A>T 3 M26383 M26383 146930 GEN-3E Interleukin 8 1281 1207A>G 3 M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1414 13150T 3 complete eds, with a Alu repetitive sequence in the 3 untranslated region M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1508 1409A>G 3 complete eds, with a Alu repetitive sequence in the 3 untranslated region M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1588 1489T>G 3 complete eds, with a Alu repetitive sequence in the 3 untranslated region M27492 M27492 147810 GEN-3F INTERLEUKIN 1 4686 4604T>G 3 RECEPTOR, TYPE I PRECURSOR M27875 M27875 107680 GEN- Human apolipoprotein A-I 34 15G>C S 2CK mRNA, complete eds M27875 M27875 107680 GEN- Human apolipoprotein A-I 202 183C>T S 2CK mRNA, complete eds M27875 M27875 107680 GEN- Human apolipoprotein A-I 204 185T>G L62W 2CK mRNA, complete eds M27875 M27875 107680 GEN- Human apolipoprotein A-I 255 236C>T S79F 2CK mRNA, complete eds M27875 M27875 107680 GEN- Human apolipoprotein A-I 689 670C>T S 2CK mRNA, complete eds M27875 M27875 107680 GEN- Human apolipoprotein A-I 824 805G>A 3 2CK mRNA, complete eds M28211 M28211 179511 GEN- Homo sapiens GTP- 677 607A>G T203A 201 binding protein (RAB4) mRNA, complete eds M28211 M28211 179511 GEN- Homo sapiens GTP- 679 609C>A S 201 binding protein (RAB4) mRNA, complete eds M28215 M28215 179512 GEN- Homo sapiens GTP- 297 241 G>C G81 R 2D3 binding protein (RAB5) SD-144146.1 Page 82 mRNA, complete eds POMC M28636 176830 GEN- Adrenocorticotropic 92 92C>T 3 2DG hormone (ACTH) CETP M30185 118470 GEN- Human cholesteryl ester 1283 1153G>C V385L 2FK transfer protein mRNA, complete eds CETP M30185 118470 GEN- Human cholesteryl ester 1298 1168G>C A390P 2FK transfer protein mRNA, complete eds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete eds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete eds CETP M30185 118470 GEN- Human cholesteryl ester 1506 1376A>G D459G 2FK transfer protein mRNA, complete eds CETP M30185 118470 GEN- Human cholesteryl ester 1696 1566G>A 3 2FK transfer protein mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 178 79C>T P27S natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 203 104C>G A35G natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 210 111G>T S natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 327228C>T S natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 553454T>C F natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 626 527G>T 3 natriuretic factor (CDD- ANF) mRNA, complete eds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 640541T>C 3 natriuretic factor (CDD- SD-144146.1 Page 82 ANF) mRNA, complete eds M31328 M31328 139130 GEN-7G Guanine nucleotide binding 1049 1043G>A 3 protein (G protein), beta polypeptide 3 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1271 1241 C>T 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1344 1314G>A 3 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductas 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1780 1750T>C 3 1 M32315 M32315 191191 GEN-3M Tumor necrosis factor 676 587T>G M196R receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 1176 1087G>A A363T receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 1668 1579G>T 3 receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 2898 2809G>A 3 receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 3671 3582G>A 3 receptor 2 (75kD) M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 109 109G>A D37N (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 438 438A>G S (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1172 1172A>C 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1179 1179C>T 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1323 13230A 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1376 1376G>C 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1433 1433C>T 3 (lipoamide) beta M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 449 371A>G 3 protein, FK506-binding protein 1 (12kD) M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 486 408G>A 3 protein, FK506-binding SD-144146.1 Page 82 protein 1 (12kD) M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 650 572T>C 3 protein, FK506-binding protein 1 (12kD) M36035 M36035 109610 GEN-3P Benzodiazepine receptor, 500439G>A A147T peripheral-type M36035 M36035 109610 GEN-3P Benzodiazepine receptor, 500439G>A A147T peripheral-type M36035 M36035 109610 GEN-3P Benzodiazepine receptor, 546485A>G H162R peripheral-type M36035 M36035 109610 GEN-3P Benzodiazepine receptor, 546485A>G H162R peripheral-type M36035 M36035 109610 GEN-3P Benzodiazepine receptor, 711 650T>G 3 peripheral-type M37400 M37400 138180 GEN-FC Glutamic-oxaloacetic 1588 1564A>C 3 transaminase 1 , soluble (aspartate aminotransferase 1 ) M37400 M37400 138180 GEN-FC Glutamic-oxaloacetic 1810 1786G>A 3 transaminase 1 , soluble (aspartate aminotransferase 1 ) M55040 M55040 100740 GEN-3Q acetylcholinesterase 323 167C>T P56L M55040 M55040 100740 GEN-3Q acetylcholinesterase 1154998T>A V333E M55040 M55040 100740 GEN-3Q acetylcholinesterase 1213 1057C>A H353N M55040 M55040 100740 GEN-3Q acetylcholinesterase 1482 1326G>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1663 1507T>C F503L M57414 M57414 None GEN- Human neurokinin A 6868T>C I23T 4FK receptor (NK-2R) mRNA, complete eds M57414 M57414 None GEN- Human neurokinin A 951 951G>A S 4FK receptor (NK-2R) mRNA, complete eds M57414 M57414 None GEN- Human neurokinin A 1171 1171C>G P391A 4FK receptor (NK-2R) mRNA, complete eds M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase SD-144146.1 Page 82 M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 418 214G>T A72S methyltransferase M58525 M58525 1 16790 GEN-3S Catechol-O- 423 219G>A S methyltransferase M58525 M58525 1 16790 GEN-3S Catechol-O- 612 408OG S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 813 609C>T S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1031 827delC F methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1039 835C>A 3 methyltransferase M59305 M59305 108962 GEN- Human atrial natriuretic 160 (-203M- F 39P peptide clearance receptor 199)delTTTTT (ANP C-receptor) mRNA, complete eds M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 644 639C>A S M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 1892 1887C>A 3 M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 2030 2025G>A 3 TCN2 M60396 275350 GEN- Human transcobalamin II 1164 1127C>T S376L SAX (TCII) mRNA, complete eds TCN2 M60396 275350 GEN- Human transcobalamin II 1765 1728T>C 3 SAX (TCII) mRNA, complete eds M60857 M60857 123841 GEN-10 Cyclophilin B 183 171C>T S M60857 M60857 123841 GEN-10 Cyclophilin B 217 205G>T V69L M60857 M60857 123841 GEN-10 Cyclophilin B 702 690C>T 3 M60857 M60857 123841 GEN-10 Cyclophilin B 804 792A>C 3 M62762 M62762 108745 GEN-FP Vacuolar H+ ATPase 425 195C>T S proton channel subunit M62762 M62762 108745 GEN-FP Vacuolar H+ ATPase 784 554C>G 3 proton channel subunit M62762 M62762 108745 GEN-FP Vacuolar H+ ATPase 838 608C>T 3 SD-144146.1 Page 82 proton channel subunit LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 850837G>A S macroglobulin receptor- associated protein mRNA, complete eds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1093 1080C>T 3 macroglobulin receptor- associated protein mRNA, complete eds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1249 1236C>T 3 macroglobulin receptor- associated protein mRNA, complete eds FGFR3 M64347 134934 GEN- Human novel growth factor 3108 3108C>A 3 SEX receptor mRNA, 3 eds FGFR3 M64347 134934 GEN- Human novel growth factor 3715 3715G>A 3 SEX receptor mRNA, 3 eds M64590 M64590 238300 GEN-FU Glycine cleavage system: 3076 2926A>G M976V Protein P M64799 M64799 None GEN- Histamine receptor H2 398 398T>C V133A 4DN M64799 M64799 None GEN- Histamine receptor H2 525 525A>T KΪ75N 4DN M64799 M64799 None GEN- Histamine receptor H2 620 620A>G K207R 4DN M64799 M64799 None GEN- Histamine receptor H2 649 649A>G N217D 4DN M64799 M64799 None GEN- Histamine receptor H2 692692A>G K231R 4DN M64799 M64799 None GEN- Histamine receptor H2 802 802G>A V268M 4DN PRKAR1 M65066 176911 GEN- Human cAMP-dependent 1424 1424C>G 3 B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end PRKAR1 M65066 176911 GEN- Human cAMP-dependent 1514 1514G>C 3 B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end PRKAR1 M65066 176911 GEN- Human cAMP-dependent 1550 1550G>C 3 3FK protein kinase regulatory SD-144146.1 Page 82 subunit Rl-beta mRNA, 3 end >RKAR1 M65066 176911 GEN- Human cAMP-dependent 1862 1862G>A B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end 'RKAR1 M65066 176911 GEN- Human cAMP-dependent 2139 2139C>T B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end FSHR M65085 136435 GEN- FSH receptor 2105 2039G>A S680N 3FQ EDN2 M65199 131241 GEN- Endothelin 2 384 314C>T A105V CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1500 1353T>A S M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1512 1365G>A F M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1566 1419G>A S M69175 M69175 238330 GEN-FX Glycine cleavage system: 710 686C>G 3 Protein H M69175 M69175 238330 GEN-FX Glycine cleavage system: 710 686C>G 3 Protein H M69175 M69175 238330 GEN-FX Glycine cleavage system: 737 713C>T 3 Protein H M69175 M69175 238330 GEN-FX Glycine cleavage system: 1007 983C>T Protein H M69226 M69226 309850 GEN-3Z Monoamine oxidase A 435 385A>C S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 936 886C>T F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1076 1026A>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1373 1323G>A F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1609 1559A>G K520R SRD5A2 M74047 264600 GEN- Human steroid 5-alpha- 2379 2352A>G 3 SD-144146.1 Page 82 CDC reductase 2 (SRD5A2) mRNA, complete eds GALN M77140 137035 GEN- H.sapiens pro-galanin 339 339C>T 3 3PM mRNA, 3 end M80646 M80646 274180 GEN-40 Thromboxane synthase 756 585G>C S M80646 M80646 274180 GEN-40 Thromboxane synthase 1240 1069C>G L357V M81590 M81590 182131 GEN- Serotonin 5-HT receptors 190 129C>T S 3VZ 5-HT1D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 432 371 T>G F124C 3VZ 5-HT1D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 922 861 G>C "S 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 1241 1180G>A 3 3VZ 5-HT1 D TAC1 R M81797 162323 GEN- Tachylinins NK1 receptor 696 652G>A V218I 3W8 TAC1 R M81797 162323 GEN- Tachylinins NK1 receptor 1397 1353G>C 3 3W8 M81883 M81883 266100 GEN-42 Glutamate decarboxylase 424 (-127)G>A 5 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 597 47G>A G16E 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 599 49G>C A17P 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 661 111T>C S 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 1042 492C>T S 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 2005 1455A>G S 1 (brain, 67kD) M81883 M81883 266100 GEN-42 Glutamate decarboxylase 3033 2483C>T 3 1 (brain, 67kD) M82962 M82962 600388 GEN- Human N-benzoyl-L- 2316 2307T>G 3 3XC tyrosyl-p-amino-benzoic acid hydrolase alpha subunit (PPH alpha) mRNA, complete eds M82962 M82962 600388 GEN- Human N-benzoyl-L- 2428 2419A>C 3XC tyrosyl-p-amino-benzoic acid hydrolase alpha subunit (PPH alpha) SD-144146. Page 82 mRNA, complete eds M83566 M83566 114206 GEN- Human 1222 1104C>T 3Y7 neuroendocrine/beta-cell- type calcium channel alpha-1 subunit mRNA, complete eds M83566 M83566 114206 GEN- Human 1468 1350G>A 3Y7 neuroendocrine/beta-cell- type calcium channel alpha-1 subunit mRNA, complete eds CHRNA5 M83712 118505 GEN- Nicotinic, Cholinergic 1340 1192G>A D398N 3YQ receptor alpha 5 M84755 M84755 162641 GEN-46 Neuropeptide Y1 1121 1121A>C K374T TGFBR2 M85079 190182 GEN- Human TGF-beta type II 2045 1710A>C 3 3ZS receptor mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 1653 1569T>A 3 40Y mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 2599 2515C>G 3 40Y mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 2619 2535A>C 3 40Y mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 2656 2572A>C 3 40Y mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 2745 2661 C>T 3 40Y mRNA, complete eds YWHAZ M86400 601288 GEN- Human phospholipase A2 2761 2677A>C 3 40Y mRNA, complete eds GABRR2 M86868 137162 GEN- Gamma-aminobutyric acid 1369 1289C>T T430M 4FS (GABA) A receptor M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 296 16T>C S6P M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 413 133G>A G45R M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1430 1150T>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 SD-144146.1 Page 82 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1453 1173A>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1677 1397G>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1797 1517G>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1885 1605C>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1916 1636T>C 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 2158 1878A>G 3 M89473 M89473 None GEN- NEUROMEDIN K 1614 1471T>C 3 4FU RECEPTOR M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2159 2062G>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094ATATTA >ATATTA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094delATAT TA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2230 2133A>G 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2339 2242T>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2409 2312G>A 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2726 2629C>T 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2983 2886C>T 3 M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 3846 3846C>T S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphal c (alt. 5505 5505G>A S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6582 6582A>G S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6613 6613G>C G2205R splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6614 6614G>C G2205A splice) L-Type M93415 M93415 102581 GEN- Human activin type II 136 (-38)G>T 5 48S receptor mRNA, complete eds M94055 M94055 601219 GEN-493 Human voltage-gated 5226 5121 G>A S sodium channel mRNA, complete eds IL8RB M94582 146928 GEN- Interleukin 8 receptor 838 786T>C S SD-144146.1 Page 83 49G IL8RB M94582 146928 GEN- Interleukin 8 receptor 1262 1210C>T 3 49G IL8RB M94582 146928 GEN- Interleukin 8 receptor 1494 1442A>G 3 49G M98045 M98045 136510 GEN- Homo sapiens 802 732C>T S 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1747 1677G>T 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1912 1842G>A 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98045 M98045 136510 GEN- Homo sapiens 1995 1925C>G 3 4C3 folylpolyglutamate synthetase mRNA, complete eds M98539 M98539 176803 GEN-SW prostaglandin D2 synthase 157 1580A 3 gene S63912 S63912 601233 GEN- D10S102=FBRNP [human, 2193 2163G>A 3 3EJ fetal brain, mRNA, 3043 nt] GABRB2 S77553 600232 GEN- Gamma-aminobutyric acid 438 438C>G S 4FO (GABA) A receptor ADCYAP S83513 102980 GEN- pituitary adenylate cyclase 1521 1520G>A 3 1 3YA activating polypeptide [human, mRNA, 1940 nt] U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3377 3316A>C 3 U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3524 3463A>G 3 GLP1 R U01157 138032 GEN-V3 Human glucagon-like 780 780C>A F260L SD-144146.1 Page 83 peptide-1 receptor mRNA with CA dinucleotide repeat, complete eds GLP1R U01157 138032 GEN-V3 Human glucagon-like 947 947G>C G316A peptide-1 receptor mRNA with CA dinucleotide repeat, complete eds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 1200 1200C>A peptide-1 receptor mRNA with CA dinucleotide repeat, complete eds U02326 U02326 142445 GEN-PE Human clone ndf43 neu 752 644G>A G215E differentiation factor mRNA, complete eds SLO U02632 600150 GEN-XA Calcium-activated 2377 2377T>G S793A potassium channel U02882 U02882 600129 GEN-XU Human rolipram-sensitive 1798 1690T>C C564R 3,5-cyclic AMP phosphodiesterase mRNA, complete eds U02882 U02882 600129 GEN-XU Human rolipram-sensitive 1881 1773G>A 3,5-cyclic AMP phosphodiesterase mRNA, complete eds U02882 U02882 600129 GEN-XU Human rolipram-sensitive 4691 4583T>G 3,5-cyclic AMP phosphodiesterase mRNA, complete eds U04735 U04735 601100 GEN- Human microsomal stress 2120 2084A>G 15A 70 protein ATPase core (stch) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 364 209G>A S70N 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 728 573C>T 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1613 1458C>T 16V kinase TrkC (NTRK3) mRNA, complete eds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1643 1488G>C SD-144146.1 Page 83 16V kinase TrkC (NTRK3) mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 38 15C>T dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 282 259A>T S87C dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 350 327C>T dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 365 342T>C dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 464 441 G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 474 451 A>G M151V dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 532 509A>G H170R dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 538 515T>A L172Q dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 689 666T>C S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 806 783G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 872 849G>T dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 952 929T>G I310S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1020 997G>A dehydrogenase mRNA, complete eds SD-144146.1 Page 83 DDH1 U05598 600450 GEN-184 Human dihydrodiol 1035 1012G>A 3 dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1112 1089OT 3 dehydrogenase mRNA, complete eds U05875 U05875 147569 GEN-18J Human clone pSK1 2047 1399C>G 3 interferon gamma receptor accessory factor- 1 (AF-1 ) mRNA, complete eds U05875 U05875 147569 GEN-18J Human clone pSK1 2087 1439T>C 3 interferon gamma receptor accessory factor- 1 (AF-1 ) mRNA, complete eds U07225 U07225 600041 GEN- P2Y2 purinoceptor 2008 1763G>A 3 1 DM U07364 U07364 600504 GEN- Inwardly rectifying 982 885G>A S I DS potassium channel U07364 U07364 600504 GEN- Inwardly rectifying 1099 1002A>G S I DS potassium channel U07364 U07364 600504 GEN- Inwardly rectifying 1537 1440G>A 3 I DS potassium channel U07364 U07364 600504 GEN- Inwardly rectifying 1714 1617G>A 3 I DS potassium channel AMPH U07616 600418 GEN- Human amphiphysin 1856 1746G>T S 1 ED mRNA, complete eds AMPH U07616 600418 GEN- Human amphiphysin 1901 1791G>A S 1 ED mRNA, complete eds AMPH U07616 600418 GEN- Human amphiphysin 2289 2179A>G 3 1 ED mRNA, complete eds U08989 U08989 133550 GEN- Human glutamate 684 519C>T S CBZ transporter mRNA, complete eds U08989 U08989 133550 GEN- Human glutamate 1617 1452T>C S CBZ transporter mRNA, complete eds U09002 U09002 138253 GEN- Glutamate Aspartate 1430 1275A>G S 1G8 receptor NMDA 2A U09002 U09002 138253 GEN- Glutamate Aspartate 4468 4313T>C M1438T 1G8 receptor NMDA 2A U09002 U09002 138253 GEN- Glutamate Aspartate 4671 4516G>T 3 SD-144146.1 Page 83 1G8 receptor NMDA 2A U09002 U09002 138253 GEN- Glutamate Aspartate 5562 5407delC F 1G8 receptor NMDA 2A U09002 U09002 138253 GEN- Glutamate Aspartate 5765 5610OT 3 1 G8 receptor NMDA 2A SLC18A3 U09210 600336 GEN- Human vesicular 1369 927A>G S 4F3 acetylcholine transporter mRNA, complete eds SLC18A3 U09210 600336 GEN- Human vesicular 1567 1125C>G 4F3 acetylcholine transporter mRNA, complete eds SLC18A3 U09210 600336 GEN- Human vesicular 2080 1638G>T 4F3 acetylcholine transporter mRNA, complete eds SLC18A3 U09210 600336 GEN- Human vesicular 2199 1757G>A 4F3 acetylcholine transporter mRNA, complete eds SLC18A3 U09210 600336 GEN- Human vesicular 2349 1907G>T 4F3 acetylcholine transporter mRNA, complete eds U09806 U09806 None GEN- Human 120 120T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 473 473G>A R158Q 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 550 550C>T 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 668 668C>T A223V 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 1059 1059T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 1289 1289C>A E430A SD-144146.1 Page 83 4FZ methylenetetrahydrofolate reductase mRNA, partial eds U09806 U09806 None GEN- Human 1308 1308T>C 4FZ methylenetetrahydrofo reductase mRNA, pa 0PRD1 U10504 165195 GEN- Human delta opiate 921 921T>C 4F5 receptor mRNA, complete eds U12507 U12507 600681 GEN- Cardiac inward rectifier 338 13C>A 1MD potassium channel (HH- IRK1 ) U12507 U12507 600681 GEN- Cardiac inward rectifier 1597 1272G>A 1MD potassium channel (HH- IRK1) U12779 U12779 None GEN- Human MAP kinase 450 72C>G 1MV activated protein kinase 2 mRNA, complete eds U12779 U12779 None GEN- Human MAP kinase 1329 951 C>T 1MV activated protein kinase 2 mRNA, complete eds U13737 U13737 600636 GEN- Human cysteine protease 2356 2132A>C 1PC CPP32 isoform alpha mRNA, complete eds U13737 U13737 600636 GEN- Human cysteine protease 2535 2311 C>T 1PC CPP32 isoform alpha mRNA, complete eds U16125 U16125 138245 GEN- Glutamate Aspartate 2563 2563T>G C855G 1XK receptor GLU5 U16957 U16957 300034 GEN-1L Angiotensin receptor AT2 263 123T>C S U16957 U16957 300034 GEN-1L Angiotensin receptor AT2 883 743G>A R248K N0S1 U17327 163731 GEN-209 Human neuronal nitric 3391 2706C>T S oxide synthase (NOS1 ) mRNA, complete eds PDE4A U18087 600126 GEN-214 Human 3,5-cyclic AMP 642 633T>G phosphodiesterase HPDE4A6 mRNA, complete eds PDE4A U18087 600126 GEN-214 Human 3,5-cyclic AMP 804 795T>C phosphodiesterase SD-144146.1 Page 83 HPDE4A6 mRNA, complete eds PDE4A U18087 600126 GEN-214 Human 3,5-cyciic AMP 1616 1607A>C E536 S phosphodiesterase HPDE4A6 mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 2223 1932T>G F644L apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 3046 2755C>T P919S apoptosis inhibitory protein mRNA, complete eds U19251 U 19251 600355 GEN-221 Homo sapiens neuronal 5503 5212A>G 3 apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 5634 5343A>G 3 apoptosis inhibitory protein mRNA, complete eds U19251 U19251 600355 GEN-221 Homo sapiens neuronal 5644 5353A>G 3 apoptosis inhibitory protein mRNA, complete eds U19487 U19487 176804 GEN-4I PROSTAGLANDIN E2 231 75A>T S RECEPTOR, EP2 SUBTYPE U19720 U19720 600424 GEN-11 Folate Transporter 53 (-43)T>C 5 (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 341 246C>G S (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 791 696C>T S (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 1067 972G>A S (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 2100 2005 Λ 2006ins F (SLC19A1 ) G U19720 U19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 SD-144146.1 Page 83 (SLC19A1 ) U 19720 U19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1 ) U19720 U 19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 2652 2557T>C 3 (SLC19A1 ) U20157 U20157 601690 GEN-234 Human platelet-activating 1297 1136T>C V379A factor acetylhydrolase mRNA, complete eds U23143 U23143 138450 GEN- Human mitochondrial 506 506T>G F169C MIY serine hydroxymethyltransferase gene, nuclear encoded mitochondrion protein, complete eds U25029 U25029 138040 GEN-82 Glucocorticoid receptor 335 335C>T 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 386 386T>C 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 1069 1069C>T 3 alpha U26553 U26553 114131 GEN-66 Calcitonin Receptor 1412 1340C>T P447L U26553 U26553 114131 GEN-66 Calcitonin Receptor 1515 1443T>C 3 U26648 U26648 603189 GEN-IC Syntaxin 5A 501 475C>T R159W U26648 U26648 603189 GEN-IC Syntaxin 5A 1270 1244G>A 3 U26648 U26648 603189 GEN-IC Syntaxin 5A 1288 1262G>T 3 U27699 U27699 603080 GEN- Human pephBGT-1 2841 2255C>T 3 2C9 betaine-GABA transporter mRNA, complete eds U32315 U32315 600876 GEN-IL syntaxin 3 411 373C>T R125W U32315 U32315 600876 GEN-IL syntaxin 3 1601 1563G>A 3 U32500 U32500 162642 GEN-1 P Neuropeptide Y2 407 159C>T S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1706 1458- 3 1460TAT>TA SD-144146.1 Page 83 T U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1706 1458- 3 1460delTAT U32500 U32500 162642 GEN-1 P Neuropeptide Y2 2782 2534 Λ 2535ins F CA U32989 U32989 191070 GEN- Human tryptophan 991 927G>A S 2JH oxygenase (TDO) mRNA, complete eds U33052 U33052 602549 GEN-2JL Human lipid-activated, 34 25G>C E9Q protein kinase PRK2 mRNA, complete eds U33052 U33052 602549 GEN-2JL Human lipid-activated, 430421T>C protein kinase PRK2 mRNA, complete eds U33052 U33052 602549 GEN-2JL Human lipid-activated, 1112 1103T>G F368C protein kinase PRK2 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 656 572A>G D191G 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2608 2524G>A A842T 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2649 2565G>A 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2713 2629C>T 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 27852701G>A V901I 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2846 2762C>G A921 G 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2856 2772C>T 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2860 2776G>A A926T 2JK protein kinase PRK1 mRNA, complete eds SD-144146.1 Page 83 U33053 U33053 601032 GEN- Human lipid-activated 2889 2805C>T S 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2895 2811 C>T S 2JK protein kinase PRK1 mRNA, complete eds U33053 U33053 601032 GEN- Human lipid-activated 2954 2870C>T 3 2JK protein kinase PRK1 mRNA, complete eds U33632 U33632 601745 GEN-IN Two P-domain K+ channel 1386 1204G>A 3 TWIK-1 mRNA PSEN2 U34349 600759 GEN-2L2 Human seven trans160 69C>T S membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans220 129C>T S membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans220 129C>T S membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans352 261 C>T S membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans352 261C>T S membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans1437 1346C>T 3 membrane domain protein (AD3LP/AD5) mRNA, complete eds PSEN2 U34349 600759 GEN-2L2 Human seven trans1654 1563C>G 3 membrane domain protein (AD3LP/AD5) mRNA, complete eds PPP2R4 U37352 601645 GEN- Human protein 2084 1996G>A 3 205 phosphatase 2A Balphal SD-144146.1 Page 84 regulatory subunit mRNA, complete eds TAC2 U37529 162320 GEN- Substance P beta-PPT-A 644 499G>A 3 20H TAC2 U37529 162320 GEN- Substance P beta-PPT-A 694 549T>C 3 20H TAC2 U37529 162320 GEN- Substance P beta-PPT-A 799 654A>G 3 TAC2 U37529 162320 GEN- Substance P beta-PPT-A 826 681 C>T 3 20H U39412 U39412 None GEN- Homo sapiens alpha SNAP 138 71 C>T S24L 2Q5 mRNA, complete eds U39412 U39412 None GEN- Homo sapiens alpha SNAP 290 223C>T L75F 2Q5 mRNA, complete eds U39412 U39412 None GEN- Homo sapiens alpha SNAP 473 406G>A V136M 2Q5 mRNA, complete eds U39412 U39412 None GEN- Homo sapiens alpha SNAP 651 5840G T195S 2Q5 mRNA, complete eds U40347 U40347 600950 GEN- Human serotonin N- 382 148G>A E50K 2RK acetyltransferase mRNA, complete eds U40396 U40396 602691 GEN-6W Steroid receptor 285 229A>C K77Q coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 314 258A>T K86N coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 336 280C>T P94S coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 688 632C>T T211 I coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 970 914C>A A305E coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 1511 1455G>A S coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 2377 2321 C>T T774M coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 2730 2674C>T P892S coactivator (SRC-1 ) U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 661 654T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 697 690A>G S receptor alpha 7 SD-144146.1 Page 84 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 940 933G>A S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1276 1269T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1790 1783A>T 3 receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1792 1785T>A 3 receptor alpha 7 U43030 U43030 600435 GEN-LFI Human cardiotrophin-1 1404 1372C>T 3 (CTF1 ) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 446 253A>G T85A 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 519 326A>G K109R 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 1222 1029T>C S 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2161 1968G>C K656N 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2174 1981A>C T661 P 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3151 2958C>T S 2UN r) mRNA, complete eds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3250 3057G>A S 2UN r) mRNA, complete eds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1424 1228A>G 3 mRNA, complete eds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1604 1408C>G 3 mRNA, complete eds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1719 1523G>A 3 mRNA, complete eds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1827 1631G>A 3 mRNA, complete eds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 2286 2090G>A 3 mRNA, complete eds U47741 U47741 600140 GEN-6X CREB-binding protein 5369 5171A>T E 1724V (CBP) U47741 U47741 600140 GEN-6X CREB-binding protein 5372 5174A>T D 1725V (CBP) U49516 U49516 312861 GEN-1 Q Serotonin 5-HT receptors 2915 2187A>C 3 5-HT2C SD-144146.1 Page 84 U49516 U49516 312861 GEN-1Q Serotonin 5-HT receptors 2947 2219A>G 3 5-HT2C U55206 U55206 None GEN- Homo sapiens human 75 16T>C C6R 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 150 91 G>A A31T 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 511 452C>T T151 I 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U55206 U55206 None GEN- Homo sapiens human 1161 1102A>G 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete eds U56976 U56976 171891 GEN-379 Human calmodulin 1510 1476C>T dependent phosphodiesterase PDE1 B1 mRNA, complete eds U57317 U57317 None GEN-6Y p300/CBP-associated 2764 2306A>G D769G factor (P/CAF) CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2296 1742C>G 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2387 1833C>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2504 1950G>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2538 1984G>A 3 4EN receptor alpha 2 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 SD-144146.1 Page 84 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1440 1209T>G S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1458 12270T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1860 1629C>T s receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1890 1659G>A s receptor alpha 4 U62768 U62768 151300 GEN- Human oxytocinase splice 3356 3295G>C 3 3CR variant 1 mRNA, complete eds U62768 U62768 151300 GEN- Human oxytocinase splice 3547 34860T 3CR variant 1 mRNA, complete eds U71321 U71321 602623 GEN- Human FK506-binding 1248 1095C>T 2TW protein FKBP51 mRNA, complete eds U71321 U71321 602623 GEN- Human FK506-binding 1425 1272G>A 2TW protein FKBP51 mRNA, complete eds U72661 U72661 602062 GEN- Human ninjurinl mRNA, 1205 1185C>A 3 3LK complete eds U75283 U75283 None GEN- Human sigma receptor 251 204G>A S 3NV mRNA, complete eds U75283 U75283 None GEN- Human sigma receptor 1625 1578A>C 3 3NV mRNA, complete eds U81375 U81375 602193 GEN- Human placental 1989 1811 G>A 3 3VO equilibrative nucleoside transporter 1 (hENTI) mRNA, complete eds U81375 U81375 602193 GEN- Human placental 1996 1818C>T 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete eds U81375 U81375 602193 GEN- Human placental 2045 1867T>C 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete eds U81504 U81504 603401 GEN- Homo sapiens beta-3A- 1775 1683C>T 3VX adaptin subunit of the AP-3 complex mRNA, complete SD-144146.1 Page 84 eds U81504 U81504 603401 G GEENN-- Homo sapiens beta-3A- 2108 2016T>C S 3 3VVXX adaptin subunit of the AP-3 complex mRNA, complete eds U81504 U81504 603401 G GEENN-- Homo sapiens beta-3A- 2668 2576G>T S859I 3 3VVXX adaptin subunit of the AP-3 complex mRNA, comp U81554 U81554 602122 G GEENN-- Homo sapiens CaM kinase 939 727A>G 3 3 3VVWW II isoform mRNA, complete eds U84404 U84404 601623 G GEENN--8833 Ubiquitin protein ligase 1003 417A>T S E3A U84404 U84404 601623 G GEENN--8833 Ubiquitin protein ligase 1386 800T>G V267G E3A U84404 U84404 601623 G GEENN--8833 Ubiquitin protein ligase 1930 1344A>G S E3A U84404 U84404 601623 G GEENN--8833 Ubiquitin protein ligase 2299 1713A>G S E3A U95025 U95025 601116 G GEENN-- Homo sapiens 744 744T>C S 4 4FFXX metabotropic glutamate receptor 8 (GRM8) mRNA, complete eds U97669 U97669 600276 G GEENN-- Homo sapiens Notch3 7712 7634T>G 3 4 4BBUU (NOTCH3) mRNA, complete eds U97669 U97669 600276 G GEENN-- Homo sapiens Notch3 7852 7774A>G 3 4 4BBUU (NOTCH3) mRNA, complete eds U97669 U97669 600276 G GEENN-- Homo sapiens Notch3 7881 7803G>A 3 4 4BBUU (NOTCH3) mRNA, complete eds U97669 U97669 600276 G GEENN-- Homo sapiens Notch3 7934 7856T>C 3 4 4BBUU (NOTCH3) mRNA, complete eds V00518 V00518 118850 G GEENN--PP44 Human messenger RNA 565 515T>C 3 for chorionic gonadotropin V00519 V00519 139250 G GEENN--44UU Growth hormone 1 299 259C>A P87T V00519 V00519 139250 G GEENN--44UU Growth hormone 1 524 484G>T G162W IFNB1 V00546 147640 G GEENN--TTVV Messenger RNA for human 474 410T>G L137R SD-144146.1 Page 84 fibroblast interferon V00548 V00548 147562 GEN-P2 Human messenger RNA 119 119G>A R40K for leukocyte (alpha-2) interferon V00566 V00566 176760 GEN-4V Prolactin 574 570G>A S V00571 V00571 122560 GEN- corticotropin releasing 822 637delA F CBO factor V00571 V00571 122560 GEN- corticotropin releasing 837 652G>A 3 CBO factor X00734 X00734 None GEN- Human beta-tubulin gene 1059 1059G>T S MST (5-beta) with ten Alu family members X01394 X01394 191160 GEN-4Y Tumor necrosis factor 125 (-28)C>T 5 X02317 X02317 147450 GEN-KM Superoxide dismutase 1 614 550A>C 3 (Cu/Zn) X02415 X02415 134850 GEN- Human gene for fibrinogen 1000 949G>A D317N MJ0 gamma chain X02812 X02812 190180 GEN-XR Human mRNA for 870 29C>T P10L transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 979 138C>G I46M transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1632 791 C>T T264I transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1807 966C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1930 1089G>A S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1942 1101 C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 2013 1172G>A S391 N transforming growth factor- beta (TGF-beta) X03172 X03172 192340 GEN-ZM Human mRNA for 379 356T>G V119G vasopressin precursor X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S SD-144146.1 Page 84 X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 424 64G>C E22Q X03635 X03635 133430 GEN-50 estrogen receptors 617 257C>T A86V X03635 X03635 133430 GEN-50 estrogen receptors 621 261 G>C S X03635 X03635 133430 GEN-50 estrogen receptors 829 469C>T F X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1451 1091T>A V364E X03635 X03635 133430 GEN-50 estrogen receptors 1674 1314G>A M438I X03635 X03635 133430 GEN-50 estrogen receptors 2142 1782A>G S X03635 X03635 133430 GEN-50 estrogen receptors 2354 1994A>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 2550 2190A>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 2733 2373C>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 3181 2821T>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 3338 2978C>T 3 X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3 3294CCT>CC T X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3 3294delCCT X03635 X03635 133430 GEN-50 estrogen receptors 3896 3536C>A 3 X03635 X03635 133430 GEN-50 estrogen receptors 4378 4018T>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 6287 5927T>C 3 X04741 X04741 191342 GEN-KU UBIQUITIN CARBOXYL- 51 20C>A S7Y TERMINAL HYDROLASE ISOZYME L1 X04741 X04741 191342 GEN-KU UBIQUITIN CARBOXYL- 291 260C>G A87G TERMINAL HYDROLASE ISOZYME L1 X04741 X04741 191342 GEN-KU UBIQUITIN CARBOXYL- 296 265G>C A89P TERMINAL HYDROLASE ISOZYME L1 CST3 X05607 105150 GEN-189 Human mRNA for cysteine 62 (-13)C>G 5 proteinase inhibitor precursor cystatin C CST3 X05607 105150 GEN-189 Human mRNA for cysteine 455 381 C>T S proteinase inhibitor precursor cystatin C SD-144146.1 Page 84 CST3 X05607 105150 GEN-189 Human mRNA for cysteine 550476C>T 3 proteinase inhibitor precursor cystatin C CST3 X05607 105150 GEN-189 Human mRNA for cysteine 632558A>C 3 proteinase inhibitor precursor cystatin C CST3 X05607 105150 GEN-189 Human mRNA for cysteine 647573G>A 3 proteinase inhibitor precursor cystatin C CST3 X05607 105150 GEN-189 Human mRNA for cysteine 713 639C>T 3 proteinase inhibitor precursor cystatin C CST3 X05607 105150 GEN-189 Human mRNA for cysteine 746 672A>C 3 proteinase inhibitor precursor cystatin C X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 83 (-54)G>C 5 X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 940804G>A S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1327 1191T>C S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1906 1770C>T S X06562 X06562 600946 GEN-6D Growth hormone receptor 3392 3349A>T 3 X06562 X06562 600946 GEN-6D Growth hormone receptor 41454102G>A 3 X07674 X07674 138130 GEN- Human mRNA for 266 253C>T S 1 EC glutamate dehydrogenase (EC 1.4.1.3.. GDH) X07674 X07674 138130 GEN- Human mRNA for 272 259G>A E87K 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 288275G>A R92Q 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 292279G>A S 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 595582T>C S 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 598 585T>A D195E 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 646633A>G S SD-144146.1 Page 84 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 668 655A>G 1219V 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 693 680G>A S227N 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 721 708C>T 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 859 846T>C 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1134 1121 C>T A374V 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1164 1151G>C S384T 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1255 1242C>T 1 EC glutamate dehydrogenase (EC 1.4.1.3.. GDH) X07674 X07674 138130 GEN- Human mRNA for 1415 1402A>C M468L 1 EC glutamate dehydrogenase (EC 1.4.1.3. , GDH) X07674 X07674 138130 GEN- Human mRNA for 1427 1414G>T 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1501 1488G>T R496S 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1528 1515C>T 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1539 1526G>C G509A 1 EC glutamate dehydrogenase (EC 1.4.1.3. , GDH) X07674 X07674 138130 GEN- Human mRNA for 1581 1568G>A R523H 1 EC glutamate dehydrogenase (EC 1.4.1.3., GDH) SD-144146.1 Page 84 X07674 X07674 138130 GEN- Human mRNA for 1633 1620T>C 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1645 1632G>A 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1665 1652A>G N551S 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1717 1704T>A 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) X07674 X07674 138130 GEN- Human mRNA for 1830 1817G>A 1EC glutamate dehydrogenase (EC 1.4.1.3., GDH) S0D2 X07834 147460 GEN- Human mRNA for 44 40OG P14A 1ES manganese superoxide dismutase (EC 1.15.1.1 ) S0D2 X07834 147460 GEN- Human mRNA for 51 47T>C V16A 1ES manganese superoxide dismutase (EC 1.15.1.1 ) S0D2 X07834 147460 GEN- Human mRNA for 198 194C>A T65N 1ES manganese superoxide dismutase (EC 1.15.1.1 ) S0D2 X07834 147460 GEN- Human mRNA for 249 245T>C I82T 1ES manganese superoxide dismutase (EC 1.15.1.1) X12953 X12953 179509 GEN- Human rab2 mRNA, YPT1- 723 515A>C Q172P 1NA related and member of ras family X13561 X13561 147910 GEN- Human mRNA for 54 18G>T S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 441 405T>C S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 469 433G>C E145Q 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 592 556A>G K186E 10H preprokallikrein (EC 3.4.21 ) X13589 X13589 107910 GEN-56 Cytochrome P450, 364 240A>G S subfamily XIX (aromatization of SD-144146.1 Page 85 androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1655 1531C>T 3 subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1796 1672G>T 3 subfamily XIX (aromatization of androgens) X13629 X13629 107690 GEN- Human intestinal mRNA for 881 836G>A R279K 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1185 1140G>T Q380H 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1302 1257 Λ 1258ins F 100 apolipoprotein A-IV CTGT X13916 X13916 107770 GEN- Human mRNA for LDL- 28052339C>T T780I 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 8608 8142G>A S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 89238457C>T S 1Q1 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9034 8568G>T S 1Q1 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9040 8574C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9391 8925T>C S 101 receptor related protein LIF X13967 159540 GEN- Human mRNA for 3710 3666T>G 3 1PZ leukaemia inhibitory factor (LIF/HILDA) CLU X14723 185430 GEN- Human SP-40,40 mRNA 131 84C>T S 1SB for complement-associated protein SP-40,40 alpha-1 SD-144146.1 Page 85 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 429 382G>T V128F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 836 789C>T S 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1234 1187C>T S396L 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1372 1325A>T Y442F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1482 1435C>T 3 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1548 1501 C>T 3 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1645 1598A>T 3 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain X14766 X14766 137160 GEN-1X Gamma-aminobutyric acid 370 156C>T S (GABA) A receptor CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1375 1359C>T S 4EK receptor beta 1 CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1591 1575T>C 3 4EK receptor beta 1 X15263 X15263 None GEN- Muscarinic receptor, 1144 1044G>A S 4EQ CHRM1 X15357 X15357 108960 GEN- Human mRNA for 1066 1023G>C M341 I KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 1657 1614C>T S SD-144146.1 Page 85 KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 2859 2816G>A R939C KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 2983 2940G>A S KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 3259 3216delC F KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 3589 3546 Λ 3547ins F KUV natriuretic peptide receptor GAAA (ANP-A receptor) X16087 X16087 272750 GEN- Human mRNA for G(M2) 13 13A>G T5A 1XG activator protein X16087 X16087 272750 GEN- Human mRNA for G(M2) 133 133G>A V45I 1XG activator protein X16087 X16087 272750 GEN- Human mRNA for G(M2) 163 163G>A V55M 1XG activator protein PACE X17094 136950 GEN- Human fur mRNA for furin 399 183C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 1692 1476C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2067 1851C>G S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 27252509T>C 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 28552639C>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 29882772G>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 32343018C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 36253409A>G 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3883 3667C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 4053 3837A>G 3 1ZV X51362 X51362 126450 GEN- Dopamine Receptor D2 588423G>A S SD-144146.1 Page 85 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1104 939C>T S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1122 957T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1248 1083A>G S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1488 1323T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1548 1383A>G 3 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 2361 2196C>T 3 31W X51416 X51416 601998 GEN-57 STEROID HORMONE 2285 2222G>A 3 RECEPTOR ERR1 FGFR1 X51803 136350 GEN- Human mRNA for 276 159T>G S 32G fibroblast growth factor (FGF) receptor EDN3 X52001 131242 GEN- Endothelin 3 1262 1152G>A 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1649 1539C>G 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1700 1590C>T 3 33 E EDN3 X52001 131242 GEN- Endothelin 3 1742 1632C>T 3 33 E EDN3 X52001 131242 GEN- Endothelin 3 1797 1687C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1914 1804G>C 3 33E EDN3 X52001 131242 GEN- Endothelin 3 2040 1930C>T 3 33E X52008 X52008 305990 GEN-22 Glycine receptor alpha2 591 204T>G S GLRA1 X52009 138491 GEN-4FJ H.sapiens alpha-1 1477 1181C>T P394L strychnine binding subunit of inhibitory glycine receptor mRNA GLRA1 X52009 138491 GEN-4FJ H.sapiens alpha-1 1520 1224C>T strychnine binding subunit of inhibitory glycine receptor mRNA SD-144146.1 Page 85 X52479 X52479 176960 GEN-LM Protein kinase C, alpha 908 881A>C D294A NGFB X52599 162030 GEN- Human mRNA for beta 832 663G>A S 33V nerve growth factor PDHA1 X52709 312170 GEN- Human mRNA for brain 849 795A>G S 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) PDHA1 X52709 312170 GEN- Human mRNA for brain 1337 1283C>T 3 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) PDHA1 X52709 312170 GEN- Human mRNA for brain 1416 1362G>A 3 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) X52773 X52773 180245 GEN-74 Retinoid X receptor, alpha 1744 1669G>A 3 FGFR2 X52832 176943 GEN-341 Human bek mRNA for 338 159A>G S fibroblast growth factor receptor-BEK FGFR2 X52832 176943 GEN-341 Human bek mRNA for 2903 2724A>T 3 fibroblast growth factor receptor-BEK CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 212 212A>G D71 G receptor alpha 3 CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 552 552C>T S receptor alpha 3 X54199 X54199 138440 GEN-LS Phosphoribosylglycinamide 168 90G>A S formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimida zole synthetase X54315 X54315 114020 GEN-351 Human mRNA for N- 2549 2448T>C S cadherin AGXT X56092 259900 GEN- Human Ser-PyrAT mRNA 1234 1213C>A 3 36R for serine-pyruvate aminotransferase FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 83 28G>A V10I 37M fibroblast growth factor receptor (FGFR-4) FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 217 162T>G S 37M fibroblast growth factor receptor (FGFR-4) YWHAB X57346 601289 GEN- H.sapiens mRNA for HS1 432 60C>A S SD-144146.1 Page 85 37R protein YWHAB X57346 601289 X57348 X57348 601290 X57348 X57348 601290 X57830 X57830 182135 G CRHBP X58022 122559 GEN- Human mRNA for 987 941T>G I314S 38K corticotropin-releasing factor binding protein (CRF-BP) DRD1 X58987 126449 GEN- D1 dopaminergic receptor 229 (-48)A>G 5 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 366 90G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 474 198G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 1539 1263G>A S 4EH X59834 X59834 138290 GEN-M4 Glutamate-ammonia ligase 67 (-43)G>C 5 (glutamine synthase) X59834 X59834 138290 GEN-M4 Glutamate-ammonia ligase 304 195T>C S (glutamine synthase) X59834 X59834 138290 GEN-M4 Glutamate-ammonia ligase 1127 1018C>T R340C (glutamine synthase) X59834 X59834 138290 GEN-M4 Glutamate-ammonia ligase 2048 1939G>A 3 (glutamine synthase) X59834 X59834 138290 GEN-M4 Glutamate-ammonia ligase 2694 2585C>G 3 (glutamine synthase) X59847 X59847 308840 GEN- H.sapiens mRNA for neural 855 855C>T S 3A5 cell adhesion molecule L1 X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 203 96A>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1372 1265A>G H422R kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1501 1394G>A R465K kinase 1-phosphorylates beta adrenergic receptor ) SD-144146.1 Page 85 X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1766 16590T S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1823 1716T>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 2976 2869G>A 3 kinase 1-phosphorylates beta adrenergic receptor ) X63368 X63368 604139 GEN-MD DNAJ PROTEIN 2593 2568C>A 3 HOMOLOG HSJ1 X63522 X63522 180246 GEN-75 MHC class I promoter 1331 1152T>C S binding protein X64878 X64878 167055 GEN-24 Oxytocin receptor 4048 3681A>C 3 X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 51 44G>A R15H CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 116 109A>C K37Q CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 261 254G>A G85E CONVERTASE PRECURSOR NTRK1 X66397 191315 GEN- H.sapiens tpr mRNA 2632 2335G>A V779I 3GN X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2236 2225G>T 3 receptor epsilon polypeptide X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2333 2322A>G 3 receptor epsilon polypeptide X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2364 2353G>T 3 receptor epsilon polypeptide X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1182 1182T>C S RECEPTOR KINASE 2 X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1609 1609G>A E537K RECEPTOR KINASE 2 X70811 X70811 109691 GEN- beta-3-adrenergic receptor 315 190T>C W64R 3KK X71490 X71490 108746 GEN-MX ATPase, H+ transporting, 1247 991 C>A 3 SD-144146.1 Page 85 lysosomal (vacuolar proton pump) 31kD X71490 X71490 108746 GEN-MX ATPase, H+ transporting, 1555 1299C>A lysosomal (vacuolar proton pump) 31kD N0S2A X73029 163730 GEN- H-sapiens mRNA for nitric 1380 1155C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H-sapiens mRNA for nitric 1503 1278C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H-sapiens mRNA for nitric 2048 1823C>T S608L 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2287 2062G>A G688S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2339 2114A>G D705G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2583 2358T>C S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2982 2757A>G S 3LW oxide synthase N0S2A X73029 163730 GEN- H-sapiens mRNA for nitric 3022 2797C>G R933G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3051 2826C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3693 3468T>C 3 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3715 3490G>A 3 3LW oxide synthase PREP X74496 600400 GEN- Prolyl Endopeptidase 390 390T>C S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1051 1051T>G L351V 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1125 1125C>T S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1363 1363G>A V455M 3N8 X75299 X75299 192321 GEN- H-sapiens HIVR mRNA for 1915 1904T>C 3 3NU vasoactive intestinal peptide (VIP) receptor X75299 X75299 192321 GEN- H.sapiens HIVR mRNA for 2475 2464T>C 3NU vasoactive intestinal peptide (VIP) receptor SD-144146.1 Page 85 X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 30 (-68)C>G 5 30E protein-tyrosine kinase X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 2010 1913A>G 3 30E protein-tyrosine kinase X75958 X75958 600456 GEN- H.sapiens trkB mRNA for 2101 2004C>T 3 30E protein-tyrosine kinase X76228 X76228 108746 GEN-N6 ATPase, H+ transporting, 46 (-30)G>A 5 lysosomal (vacuolar proton pump) 31kD X76228 X76228 108746 GEN-N6 ATPase, H+ transporting, 1023 948A>G 3 lysosomal (vacuolar proton pump) 31 kD X76228 X76228 108746 GEN-N6 ATPase, H+ transporting, 1143 1068C>T 3 lysosomal (vacuolar proton pump) 31 kD LIPA X76488 278000 GEN- H.sapiens mRNA for 191 46A>C T16P 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 212 67G>A G23R 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 967 822G>A M274I 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 1531 1386C>T 3 3P2 lysosomal acid iipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2254 2109A>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2439 2294C>T 3 3P2 lysosomal acid lipase NMB X76534 162340 GEN- H.sapiens NMB mRNA 481 390A>G S 3P5 NMB X76534 162340 GEN- H.sapiens NMB mRNA 2478 2387T>C 3 3P5 NMB X76534 162340 GEN- H.sapiens NMB mRNA 2655 2564A>C 3 3P5 MPV17 X76538 600945 GEN- H.sapiens Mpv17 mRNA 575 548C>T 3 3P6 X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 528 351 G>A S 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 569 392A>G Y131C 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 687 510C>T S 4FN receptor SD-144146.1 Page 859 X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 1303 1126C>G 3 4FN receptor X77130 X77130 602548 GEN- H-sapiens mRNA for 0RL1 1816 1639G>T 3 4FN receptor CLCN4 X77197 302910 GEN- H.sapiens mRNA for 212 (-172)C>T 5 3P0 chloride channel X77533 X77533 602730 GEN- H.sapiens mRNA for 1462 1458C>T S 3Q3 activin type II receptor X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 253 28G>T V10F omega) receptor 2 (splice variant) X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 1128 903A>G omega) receptor 2 (splice variant) X77748 X77748 601115 GEN- Metabotropic glutamate 384 126G>A S 3QD receptor type 3 YWHAH X78138 113508 GEN- H.sapiens 14-3-3 eta 953 753A>G 3 3QU subtype mRNA YWHAH X78138 113508 GEN- H.sapiens 14-3-3 eta 960 760G>A 3 3QU subtype mRNA YWHAH X78138 113508 GEN- H.sapiens 14-3-3 eta 1387 1187C>T 3 3QU subtype mRNA X78282 X78282 601292 GEN- H.sapiens mRNA for aryl 895895T>C 3 LVF sulfotransferase (ST1A2) X78520 X78520 600580 GEN- H. sapiens RNA for CLCN3 2804 2142T>C S 3RG X78520 X78520 600580 GEN- H. sapiens RNA for CLCN3 2822 2160A>G S 3RG X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 1922 1922G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2378 2378G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2382 2382G>A 3 X80818 X80818 604100 GEN- Metabotropic glutamate 1625 1455T>C S 3VD receptor type 4 X80818 X80818 604100 GEN- Metabotropic glutamate 3060 2890A>G 3VD receptor type 4 X83378 X83378 602726 GEN-NI Putative Chloride Channel 3181 3155T>G 3 X83378 X83378 602726 GEN-NI Putative Chloride Channel 5041 5015G>A 3 X83378 X83378 602726 GEN-NI Putative Chloride Channel 5366 5340G>A 3 X83861 X83861 176806 GEN-5H Prostaglandin E receptor 3 387 180C>G S (subtype EP3) {alternative SD-144146. Page 860 products} X86681 X86681 602110 GEN- H.sapiens mRNA for 1725 1340G>A 3 41 E nucleolar protein, HNP36 X94552 X94552 604101 GEN- H.sapiens mRNA for 2027 1789C>T S 4FW metabotropic glutamate receptor type 7 X94552 X94552 604101 GEN- H.sapiens mRNA for 2434 21960T S 4FW metabotropic glutamate receptor type 7 X94552 X94552 604101 GEN- H.sapiens mRNA for 2473 2235G>A S 4FW metabotropic glutamate receptor type 7 X97058 X97058 602451 GEN- P2 purinoceptor (P2Y6) 121 (-156)T>G 5 4BB X97370 X97370 601459 GEN- H-sapiens mRNA for 167 144T>C S 4BM prepronociceptin X97370 X97370 601459 GEN- H.sapiens mRNA for 637 614C>A 3 4BM prepronociceptin X97370 X97370 601459 GEN- H.sapiens mRNA for 862 839C>G 3 4BM prepronociceptin Y00052 Y00052 123840 GEN-SX Cyclophilin A 221 207C>G S Y00052 Y00052 123840 GEN-SX Cyclophilin A 268 254A>G D85G Y00052 Y00052 123840 GEN-SX Cyclophilin A 332 318C>T S Y00052 Y00052 123840 GEN-SX Cyclophilin A 627 6130A 3 CHGB Y00064 118920 GEN-SZ Human mRNA for 2230 2118A>C 3 secretogranin I (chromogranin B) Y00285 Y00285 147280 GEN-6I IGF-2 receptor 4613 4466G>A S1489N Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6371 6224C>T T2075M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6813 6666C>T S Y00285 Y00285 147280 GEN-6I IGF-2 receptor 7150 7003G>A V2335M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 8685 8538C>A 3 Y00749 Y00749 131240 GEN-P7 Endothelin 1 846 594G>T K198N Y08110 Y08110 602005 GEN- H.sapiens mRNA for 3641 3561T>G S 1 FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H.sapiens mRNA for 3818 3738C>T S 1 FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H.sapiens mRNA for 5158 5078G>A S1693N 1 FK mosaic protein LR11 SD-144146.1 Page 861 Y08110 Y08110 602005 GEN- H.sapiens mRNA for 6571 6491 G>A R2164K 1FK mosaic protein LR11 Y08756 Y08756 602164 GEN- Serotonin 5-HT receptors 765 747T>C S 4EC 5-HT4 Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 835 809A>G H270R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 946 920G>A R307Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1068 1042OA A348T 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1096 1070C>G T357S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1405 1379A>G Q460R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1589 1563C>G H521 Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1590 1564G>A V522I 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1628 1602G>T S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1759 1733G>A R578Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1772 1746G>A S 4F4 receptor Y09567 Y09567 602534 GEN- Homo sapiens mRNA for 396 396G>A S 1H3 SNAP23A protein, complete CDS Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 358 304T>G S102A (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 1768 1714T>C 3 (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 1768 1714T>C 3 (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 1976 1922C>T 3 (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 1976 1922C>T 3 (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 24702416T>C 3 (GABA) A receptor Y09765 Y09765 300093 GEN-2C Gamma-aminobutyric acid 24992445A>G 3 (GABA) A receptor SD-144146.1 Page 86 Y11044 Y11044 603540 GENHomo sapiens mRNA for 60 61 G>T 3 US GABA-BR1 a (hGB1a) receptor Y12226 Y12226 603533 GEN- H.sapiens mRNA for 3264 3236T>C 3 1 LV gamma-adaptin Y12226 Y12226 603533 GEN- H.sapiens mRNA for 3569 3541 T>C 3 1 LV gamma-adaptin Y12226 Y12226 603533 GEN- H.sapiens mRNA for 3683 3655A>G 3 1 LV gamma-adaptin Y15286 Y15286 None GEN- Homo sapiens mRNA for 40 (-23)G>A 5 ITU vacuolar proton-ATPase subunit M9.2 Y15521 Y15521 None GEN- Homo sapiens ASMTL 1622 1622A>G K541 R MEN gene Z15108 Z15108 176982 GEN- H.sapiens mRNA for 246 240T>C S 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 1694 1688A>C D563A 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2033 2027G>A 3 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2086 2080T>G 3 1TE protein kinase C zeta Z26649 Z26649 600230 GEN- Phospholipase C beta-3 437 438C>T 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 466 467G>A 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 2664 2665C>T 3 2B5 Z31357 Z31357 603943 GEN- H-sapiens mRNA for 388 134T>C I45T 2GM cysteine dioxygenase type 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1141 1104C>T S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1627 1590T>C S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1696 1659G>A S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1946 1909G>A V637M 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 2433 2396G>A 3 2MA Enzyme 1 SD-144146.1 Page 86 PDE4C Z46632 600128 GEN- H.sapiens HSPDE4C1 280 169C>T R57C 2X2 gene for 3,5-cyclic AMP phosphodiesterase PDE4C Z46632 600128 GEN- H.sapiens HSPDE4C1 1142 1031G>A R344Q 2X2 gene for 3,5-cyclic AMP phosphodiesterase Z69028 Z69028 601644 GEN-3J4 H.sapiens mRNA for beta 2 1681 1612A>T isoform of 61 kDa regulatory subunit of PP2A PAM M37721 170270 GEN- Human peptidylglycine 3183 2995T>A 20K alpha-amidating monooxygenase mRNA, complete eds PAM M37721 170270 GEN- Human peptidylglycine 3530 3342A>G 20K alpha-amidating monooxygenase mRNA, complete eds PACE X17094 136950 GEN- Human fur mRNA for furin 399 1830T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 1692 14760T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2067 1851C>G S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2725 2509T>C 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2855 2639C>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2988 2772G>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3234 3018OT 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3625 3409A>G 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3883 3667C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 4053 3837A>G 3 1ZV Table 14. Identified Variances SD-144146.1 Page 86 In Genes and Related Pathways Identified in Pharmaco Pharmaco dynamic Paramete rs of Candidate Therapeut ic Interventi ons AAC2 D90040 243400 GEN-465 Human mRNA for 232 191G>A R64Q arylamine N- acetyltransferase (EC 2.3.1.5) AAC2 D90040 243400 GEN-465 Human mRNA for 323 282C>T S arylamine N- acetyltransferase (EC 2.3.1.5) AAC2 D90040 243400 GEN-465 Human mRNA for 844 803A>G K268R arylamine N- acetyltransferase (EC 2.3.1.5) AB00081 AB00081 602550 GEN- Human mRNA for 1084 1044C>A S 2 2 14E BMALI b, complete eds AB00379 AB00379 603797 GEN- Homo sapiens mRNA for 1617 1251 G>A 3 1 1 1 F9 keratan sulfate Gal-6- sulfotransferase, complete eds AB00379 AB00379 603797 GEN- Homo sapiens mRNA for 1643 1277G>A 3 1 1 1 F9 keratan sulfate Gal-6- sulfotransferase, complete eds SD-144146.1 Page 86 AB00485 AB00485 603608 GEN- Homo sapiens mRNA for 730 730G>A V244M 4 4 KV6 carbonyl reductase 3, complete eds AB00528 AB00528 300135 GEN- Homo sapiens mRNA for 2137 2069A>T H690L 9 9 KVU ABC transporter 7 protein, complete eds AB01467 AB01467 None GEN-L22 Homo sapiens GN6ST 1578 1189G>T V397L (GlcNAcδST), complete eds AB01467 AB01467 None GEN-L22 Homo sapiens GN6ST 2335 1946T>C 9 9 mRNA for N- acetylglucosamine-6-O- sulfotransferas e (GlcNAcδST), complete eds AB01505 AB01505 603377 GEN- Homo sapiens mRNA for 1101 978G>A S 0 0 L2D OCTN2, complete eds ABC3 X97187 601615 GEN-4BI H.sapiens mRNA for ABC- 4671 4324G>T V1442F C transporter ABC3 X97187 601615 GEN-4BI H.sapiens mRNA for ABC- 5075 4728G>A S C transporter ADH2 M24317 103720 GEN- Human class I alcohol 817 787G>A V263M 28A dehydrogenase (ADH2) beta-1 subunit mRNA, complete eds ADH3 M12272 103730 GEN- Homo sapiens alcohol 1128 1048A>G I350V 1 LU dehydrogenase class I gamma subunit (ADH3) mRNA, complete eds ADH4 M15943 103740 GEN- Human class II alchohol 826 765G>T S 1 UM dehydrogenase (ADH4) pi subunit mRNA, complete eds ADH4 M15943 103740 GEN- Human class II alchohol 1389 1328T>C 3 1 UM dehydrogenase (ADH4) pi subunit mRNA, complete eds ADH5 M29872 103710 GEN- Human alcohol 1029 1025G>A S342N SD-144146.1 Page 86 2EU dehydrogenase class III (ADH5) mRNA, complete eds ADH5 M29872 103710 GEN- Human alcohol 1375 1371T>C 3 2EU dehydrogenase class III (ADH5) mRNA, complete eds AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 75 67T>C C23R acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 116 108C>T S acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 759 751T>G S251A acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 806 798C>T S acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 866 858T>C S acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 2000 1992G>T 3 acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 2158 2150C>A 3 acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001945 AF001945 601691 GEN- Homo sapiens rim ABC 2725 2644G>A G882S 17Z transporter (ABCR) mRNA, complete eds AF001945 AF001945 601691 GEN- Homo sapiens rim ABC 5136 5055C>T S 17Z transporter (ABCR) mRNA, complete eds SD-144146.1 Page 86 AF009746 AF009746 603214 GEN- Homo sapiens peroxisomal 961 910G>A A304T 1 HZ membrane protein 69 (PMP69) mRNA, complete eds AF009746 AF009746 603214 GEN- Homo sapiens peroxisomal 1895 1844A>G 1 HZ membrane protein 69 (PMP69) mRNA, complete eds AF009746 AF009746 603214 GEN- Homo sapiens peroxisomal 2134 2083T>G 1 HZ membrane protein 69 (PMP69) mRNA, complete eds AF019386 AF019386 None GEN-231 Homo sapiens heparan 79 (-40)C>G sulfate 3-0- sulfotransferase- 1 precursor (30ST1 ) mRNA, complete eds AF026947 AF026947 603418 GEN-261 Homo sapiens aflatoxm 1013 936T>C aldehyde reductase AFAR mRNA, complete eds AF026947 AF026947 603418 GEN-261 Homo sapiens aflatoxm 1078 1001A>G aldehyde reductase AFAR mRNA, complete eds AF027302 AF027302 603429 GEN- Homo sapiens TNF-alpha 3075 2981T>C 27T stimulated ABC protein (ABC50) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 34 (-209)A>C 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 210 (-33)G>A 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 229 (-14)A>G 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) SD-144146 Page 86 mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 375 133T>G F45V 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 875 633A>C E211 D 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 881 639A>G 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 883 641G>C G214A 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 919 677A>G K226R 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 927 685T>C 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 935 693A>G 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1004 762A>G 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds SD-144146.1 Page 86 AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1017 775A>C K259Q 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1106 864A>G 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1119 877G>C G293R 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1 ) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1124 882A>C 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1) mRNA, complete eds AF028738 AF028738 602631 GEN- Homo sapiens imprinted 1166 924G>C W308C 2F6 multi-membrane spanning polyspecific transporter- related protein (IMPT1) mRNA, complete eds AF038175 AF038175 None GEN- Homo sapiens clone 23819 1100 1100G>A 3 2QM white protein homolog mRNA, partial eds AF055025 AF055025 300095 GEN- Homo sapiens clone 24776 784 785A>G 3 32U mRNA sequence AF055025 AF055025 300095 GEN- Homo sapiens clone 24776 2021 2022A>T 3 32U mRNA sequence AF058056 AF058056 None GEN- Homo sapiens 200 73G>A A25T MNJ monocarboxylate transporter 2 (hMCT2) mRNA, complete eds AF058056 AF058056 None GEN- Homo sapiens 203 76G>A A26T MNJ monocarboxylate transporter 2 (hMCT2) mRNA, complete eds AF058056 AF058056 None GEN- Homo sapiens 588 461G>A S154N SD-144146. Page 87 MNJ monocarboxylate transporter 2 (hMCT2) mRNA, complete eds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1972 1663G>A LJY phospholipase A2-gamma mRNA, complete eds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1989 1680A>T LJY phospholipase A2-gamma mRNA, complete eds AF070548 AF070548 None GEN- Homo sapiens clone 24408 1224 1113C>T LNS 2-oxoglutarate carrier protein mRNA, complete eds AF070548 AF070548 None GEN- Homo sapiens clone 24408 1483 1372A>C LNS 2-oxoglutarate carrier protein mRNA, complete eds AF093771 AF093771 None GEN-LTJ Homo sapiens 528 529G>A mitoxantrone resistance protein 1 mRNA, partial sequence AHR L19872 600253 GEN- Human AH-receptor 4722 4347G>A 3 22N mRNA, complete eds AJ000730 AJ000730 603752 GEN- Homo sapiens mRNA for 195 117G>A S KY4 cationic amino acid transporter 3 AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 65 (-39)G>C 17S maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 197 94A>G K32E 173 maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 227 124G>A G42R 173 maleylacetoacetate isomerase AJ001838 AJ001838 603758 GEN- Homo sapiens mRNA for 348 245C>T T82M 173 maleylacetoacetate isomerase AJ005162 AJ005162 600067 GEN- Homo sapiens mRNA for 1915 1882A>C KVT UDP- glucuronosyltransferase SD-144146.1 Page 87 AJ130718 AJ130718 None GEN- Homo sapiens mRNA for 1820 1527G>A LDO glycoprotein-associated amino acid transporter y+LAT1 ALDH10 L47162 270200 GE -NN--22XXII Human fatty aldehyde 1609 1446A>T dehydrogenase (FALDH) mRNA, complete eds ALDH3 M74542 100660 G GEENN-- Human aldehyde 1616 1574A>G 3 3NN99 dehydrogenase type III (ALDHIII) mRNA, complete eds ALDH6 U07919 600463 G GEENN-- Human aldehyde 2453 2401A>G 1 1 FF55 dehydrogenase 6 mRNA, complete eds ALDH6 U07919 600463 G GEENN-- Human aldehyde 3396 3344C>T 1 1 FF55 dehydrogenase 6 mRNA, complete eds ALDH6 U07919 600463 G GEENN-- Human aldehyde 3397 3345G>A 1 1 FF55 dehydrogenase 6 mRNA, complete eds ARNT M69238 126110 G GEENN-- Human aryl hydrocarbon 623 567G>C 3 3JJHH receptor nuclear translocator (ARNT) mRNA, complete eds ARSB M32373 253200 GEN N--22JJ00 Human arylsulfatase B 1631 1072G>A V358M (ASB) mRNA, complete eds ARSE X83573 300180 GEN- Homo sapiens ARSE 1759 1692C>T S 3Y8 gene, complete CDS ARSE X83573 300180 GEN- Homo sapiens ARSE 1795 1728G>A S 3Y8 gene, complete CDS CAT X04076 115500 GEN- Human kidney mRNA for 51 (-20)T>C 5 ISP catalase CAT X04076 115500 GEN- Human kidney mRNA for 218 148C>T L50F ISP catalase CAT X04076 115500 GEN- Human kidney mRNA for 1237 1167T>C S 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 1325 1255C>T S I SP catalase CAT X04076 1 15500 GEN- Human kidney mRNA for 2131 2061A>C 3 I SP catalase SD-144146.1 Page 87 CBG J02943 122500 GEN-Y2 Human corticosteroid 106 71A>T D24V binding globulin mRNA, complete eds CBG J02943 122500 GEN-Y2 Human corticosteroid 971 936T>C binding globulin mRNA, complete eds CBG J02943 122500 GEN-Y2 Human corticosteroid 1229 1194G>A S binding globulin mRNA, complete eds CBR J04056 1 14830 GEN- Human carbonyl reductase 1060 967G>A 3 130 mRNA, complete eds CBS L00972 236200 GEN-UV Human cystathionine-beta- 1022 1023T>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2001 2002C>T 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2278 2279G>A 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2358 2359G>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2524 2525T>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2545 2546C>T 3 synthase (CBS) mRNA CEL M85201 114841 GEN-404 Human cholesterol 566 558T>C S esterase mRNA, complete eds CEL M85201 1 14841 GEN-404 Human cholesterol 1306 1298G>A S433N esterase mRNA, complete eds CEL M85201 114841 GEN-404 Human cholesterol 1826 1818C>T S esterase mRNA, complete eds :FTR M28668 602421 GEN- Human cystic fibrosis 2729 2597G>A C866Y 2DF mRNA, encoding a presumed transmembrane conductance regulator (CFTR) IFTR M28668 602421 GEN- Human cystic fibrosis 5826 5694T>C 2DF mRNA, encoding a presumed transmembrane conductance regulator SD-144146.1 Page 87 (CFTR) CPA1 X67318 114850 GEN- H.sapiens mRNA for 172 165G>C S 3HJ procarboxypeptidase A1 CPA1 X67318 114850 GEN- H.sapiens mRNA for 498 491 C>G T164R 3HJ procarboxypeptidase A1 CPA1 X67318 114850 GEN- H.sapiens mRNA for 629 622G>A A208T 3HJ procarboxypeptidase A1 CRYZ L13278 123691 GEN- Homo sapiens zeta- 64 54G>A S 1 NZ crystallin/quinone reductase mRNA, complete eds CRYZ L13278 123691 GEN- Homo sapiens zeta- 902 892G>A V298M 1NZ crystallin/quinone reductase mRNA, complete eds CRYZ L13278 123691 GEN- Homo sapiens zeta- 1229 1219A>G 1NZ crystallin/quinone reductase mRNA, complete eds CTH S52028 219500 GEN- cystathionine gamma-lyase 1109 1076T>G I359S 33F {clone HCL-1} [human, liver, mRNA, 1194 nt] CYP11 B2 D13752 124080 GEN- Human CYP11 B2 gene for 1600 1593G>A CCD steroid 18-hydroxylase, complete eds CYP1 B1 U03688 601771 GEN- Human dioxin-inducible 488 142C>G R48G 11Y cytochrome P450 (CYP1 B1 ) mRNA, complete eds CYP1 B1 U03688 601771 GEN- Human dioxin-inducible 701 355G>T A119S 11Y cytochrome P450 (CYP1 B1 ) mRNA, complete eds CYP1B1 U03688 601771 GEN- Human dioxin-inducible !673 2327G>T 3 11Y cytochrome P450 (CYP1 B1 ) mRNA, complete eds CYP21 M17252 201910 GEN-201 Human cytochrome 224 224G>A R75H P450c21 mRNA, 3 end CYP21 M 17252 201910 GEN-201 Human cytochrome 330 330C>T S P450c21 mRNA, 3 end SD-144146.1 Page 87 CYP21 M17252 201910 GEN-201 Human cytochrome 745 745T>C 3 P450c21 mRNA, 3 end CYP51 U23942 601637 GEN- Human lanosterol 14- 766 644G>A C215Y 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 894 772C>T R258C 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 912 790C>T R264W 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 1476 1354C>T R452C 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 6.01637 GEN- Human lanosterol 14- 1616 1494G>A 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 1836 1714C>A 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 2283 2161G>T 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 2445 2323T>C 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 2507 2385G>A 27K demethylase cytochrome P450(CYP51)mRNA, complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 2556 2434T>A 27K demethylase cytochrome P450(CYP51)mRNA, SD-144146.1 Page 87 complete eds CYP51 U23942 601637 GEN- Human lanosterol 14- 2665 2543G>A 27K demethylase cytochrome P450 (CYP51 ) mRNA, complete eds D13138 D13138 179780 GEN- Human mRNA for 566 523T>G S175A 1 NW dipeptidase D17793 D17793 None GEN- Human mRNA for 66 15G>C Q5H 20Q KIAA0119 gene, complete eds D17793 D17793 None GEN- Human mRNA for 141 90G>A 20Q KIAA0119 gene, complete eds D 17793 D17793 None GEN- Human mRNA for 363 312A>G 20Q KIAA0119 gene, complete eds D 17793 D 17793 None GEN- Human mRNA for 980 929G>C S310T 20Q KIAA0119 gene, complete eds D87292 D87292 180370 GEN- Human mRNA for 816 768C>T S 42Y rhodanese, complete eds D87292 D87292 180370 GEN- Human mRNA for 946 898G>A 3 42Y rhodanese, complete eds D87845 D87845 602344 GEN- Human mRNA for platelet- 2299 2096G>A 3 44C activating factor acetylhydrolase 2, complete eds D87845 D87845 602344 GEN- Human mRNA for platelet- 2332 2129A>G 3 44C activating factor acetylhydrolase 2, complete eds D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 434 (-1284)A>T 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 889 (-829)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 1156 (-562)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2644 927T>C S D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2920 1203A>G 3 D90041 D90041 108345 GEN-464 Human liver arylamine N- 591 445G>A V149I acetyltransferase (EC 2.3.1.5) gene D90041 D90041 108345 GEN-464 Human liver arylamine N- 1240 1094C>A 3 SD-144146.1 Page 87 acetyltransferase (EC 2 3 1 5) gene DDH1 U05598 600450 GEN-184 Human dihydrodiol 38 15C>T dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 282 259A>T S87C dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 350 327C>T S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 365 342T>C S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 464 441 G>A S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 474 451A>G M151V dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 532 509A>G H170R dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 538 515T>A L172Q dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 689 666T>C S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 806 783G>A S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 872 849G>T S dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 952 929T>G I310S dehydrogenase mRNA complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1020 997G>A 3 dehydrogenase mRNA, complete eds SD-144146 1 Page 87 DDH1 U05598 600450 GEN-184 Human dihydrodiol 1035 1012G>A dehydrogenase mRNA, complete eds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1112 1089C>T dehydrogenase mRNA, complete eds DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 829 787C>T 3 4E9 reductase gene EHHADH L07077 261515 GEN- Human enyol-CoA: 1225 1218G>A S 1 DF hydratase 3-hydroxyacyl- CoA dehydrogenase (EHHADH) mRNA, complete eds with repeats EHHADH L07077 261515 GEN- Human enyol-CoA: 1823 1816C>A P606T 1 DF hydratase 3-hydroxyacyl- CoA dehydrogenase (EHHADH) mRNA, complete eds with repeats ELA1 M16631 130120 GEN-1YI Human elastase 2 mRNA, 510 489G>A S complete eds ELA1 M16631 130120 GEN-1YI Human elastase 2 mRNA, 693 672G>A S complete eds EPHX1 L25878 132810 GEN- Homo sapiens p33/HEH 460 337T>C Y113H 29Z epoxide hydrolase (EPHX) mRNA, complete eds EPHX1 L25878 132810 GEN- Homo sapiens p33/HEH 480 357A>G S 29Z epoxide hydrolase (EPHX) mRNA, complete eds EPHX1 L25878 132810 GEN- Homo sapiens p33/HEH 539 416A>G H139R 29Z epoxide hydrolase (EPHX) mRNA, complete eds EPHX1 L25878 132810 GEN- Homo sapiens p33/HEH 1194 1071 C>T S 29Z epoxide hydrolase (EPHX) mRNA, complete eds EPHX2 L05779 132811 GEN- Human cytosolic epoxide 1631 1590A>C S 18A hydrolase mRNA, complete eds SD-144146.1 Page 87 EPHX2 L05779 132811 GEN- Human cytosolic epoxide 1742 1701A>G 18A hydrolase mRNA, complete eds EPHX2 L05779 132811 GEN- Human cytosolic epoxide 1800 1759T>C 18A hydrolase mRNA, complete eds FABP2 M10050 134640 GEN-1 IE Human liver fatty acid 322 280G>A A94T binding protein (FABP) mRNA, complete eds FACL1 L09229 152425 GEN-1 GI Human long-chain acyl- 3026 2953G>A coenzyme A synthetase (FACL1) mRNA, complete eds FACL1 L09229 152425 GEN-1GI Human long-chain acyl- 3083 3010G>A coenzyme A synthetase (FACL1 ) mRNA, complete eds GC M12654 139200 GEN- Human serum vitamin D- 925 897T>C 1 MN binding protein (hDBP) mRNA, complete eds GC M 12654 139200 GEN- Human serum vitamin D- 1324 1296G>T E432D 1 MN binding protein (hDBP) mRNA, complete eds GC M12654 139200 GEN- Human serum vitamin D- 1335 1307C>A T436K 1 MN binding protein (hDBP) mRNA, complete eds GC M12654 139200 GEN- Human serum vitamin D- 1362 1334G>A R445H 1 MN binding protein (hDBP) mRNA, complete eds GPX1 Y00433 138320 GEN-TJ Human mRNA for 504 186G>A S glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 610 292C>G R98G glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 911 593C>T P198L glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1048 730A>C glutathione peroxidase (EC 1.11.1.9.) SD-144146.1 Page 87 GPX1 Y00433 138320 GEN-TJ Human mRNA for 1110 792A>C glutathione peroxidase (EC 1 11 1 9 ) GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 821 773C>T 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 979 931 G>A 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1187 1139T>G 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1354 1306C>T 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1443 1395C>T 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1516 1468C>A 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1581 1533C>T 38S plasma glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 718 638T>C for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 837 757C>A for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 882 802A>C for phospholipid hydroperoxide glutathione peroxidase GSTM3 J05459 138390 GEN- Human glutathione 687 670G>A V224I 170 transferase M3 (GSTM3) mRNA, complete eds GSTM5 L02321 138385 GEN- Human glutathione S- 1406 1349T>C WO transferase (GSTM5) SD-144146 1 Page 88 mRNA, complete eds GSTP1 X06547 134660 GEN- Human mRNA for class Pi 319 313A>G 1105V 19N glutathione S-transferase (GST-Pi; E.C.2.5.1.18) GSTP1 X06547 134660 GEN- Human mRNA for class Pi 347 3410T A114V 19N glutathione S-transferase (GST-Pi; E.C.2.5.1.18) GSTP1 X06547 134660 GEN- Human mRNA for class Pi 561 555C>T 19N glutathione S-transferase (GST-Pi; E.C.2.5.1.18) GSTT2 L38503 600437 GEN- Homo sapiens glutathione 203 203C>T S68L 2PC S-transferase theta 2 (GSTT2) mRNA, complete eds GSTT2 L38503 600437 GEN- Homo sapiens glutathione 543 543C>T 2PC S-transferase theta 2 (GSTT2) mRNA, complete eds HADHA U04627 600890 GEN-155 Human 78 kDa gastrin- 1507 1507G>A V503M binding protein mRNA, complete eds HADHB D16481 143450 GEN- Human mRNA for 871 825T>C 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete eds HADHB D16481 143450 GEN- Human mRNA for 1607 1561 G>C 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete eds HADHB D16481 143450 GEN- Human mRNA for 1908 1862A>C 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete eds HADHB D16481 143450 GEN- Human mRNA for 1911 1865A>C 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete eds SD-144146. Page 88 HRH1 AF026261 600167 GEN- Histamine receptor H1 1068 1068A>G S 26W HSST U17970 600853 GEN- Human heparan sulfate N- 2294 2066G>C G689A 20V deacetylase/N- sulfotransferase mRNA, complete eds IDS L40586 309900 GEN- Homo sapiens ιduronate-2- 565 438C>T 2SB sulphatase (IDS) mRNA, complete eds J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 140 72G>T S J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 1511 1443A>T E481D J03548 J03548 103260 GEN- Human adrenodoxin 1099 967G>A 3 11 M mRNA, complete eds J03548 J03548 103260 GEN- Human adrenodoxin 1123 991 T>C 3 11 M mRNA complete eds J03548 J03548 103260 GEN- Human adrenodoxin 1222 1090G>C 3 11 M mRNA complete eds J03548 J03548 103260 GEN- Human adrenodoxin 1254 1122G>A 3 11 M mRNA, complete eds J03571 J03571 152390 GEN-9 Lipoxygenases 5- 55 21C>T S poxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 304 270G>A S poxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 304 270G>A S hpoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 959 925C>A P309T lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 1762 1728A>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 2076 2042- 3 lipoxygenase (leukocytes) 2043AC>AC J03571 J03571 152390 GEN-9 Lipoxygenases 5- 2076 2042- F hpoxygenase (leukocytes) 2043delAC J03571 J03571 152390 GEN-9 Lipoxygenases 5- 2328 22940T 3 poxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases 5- 2376 2342T>G 3 poxygenase (leukocytes) J03746 J03746 138330 GEN- Human glutathione S- 560 487A>G 3 11Z transferase mRNA, complete eds J03746 J03746 138330 GEN- Human glutathione S- 598 525T>G SD-144146 1 Page 88 11Z transferase mRNA, complete eds J03817 J03817 138350 GEN-9D Glutathione S-transferase 99 84T>C S M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 543 528C>T S M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 643 628T>A S210T M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 728 713C>G 3 M1 J03817 J03817 138350 GEN-9D Glutathione S-transferase 902 887C>T 3 M1 J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 454 401 G>A R134K cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 969 916C>G Q306E cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 1614 1561T>C S cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2011 1958G>A R653Q cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2335 2282C>T T761 M cyclohydrolase J04794 J04794 None GEN-PR Human aldehyde 661 601 C>A Q201 K reductase mRNA, complete eds J05176 J05176 107280 GEN-PT Human alpha-1- 240 240A>G S antichymotrypsin mRNA, 3 end J05176 J05176 107280 GEN-PT Human alpha-1- 327 327C>T S antichymotrypsin mRNA, 3 end J05176 J05176 107280 GEN-PT Human alpha-1- 554 554T>C V185A antichymotrypsin mRNA, 3 end K03001 K03001 100650 GEN-5N Aldehyde dehydrogenase 656 656T>A V219E 2, mitochondrial K03001 K03001 100650 GEN-5N Aldehyde dehydrogenase 988 988G>C V330L 2, mitochondrial K03191 K03191 108330 GEN-9E Cytochrome P450, 1470 1384G>A V462I subfamily I (aromatic compound-inducible), SD-144146.1 Page 88 polypeptide 1 L02932 L02932 170998 GEN- Human peroxisome 648 432G>A KW4 proliferator activated receptor mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 1001 969C>T 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 1333 1301T>C F434S 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 1406 1374T>C S 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 1944 1912A>G 3 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 1970 1938G>A 3 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 2011 19790T 3 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 2047 2015T>C 3 4A (CYP4A) mRNA, complete eds L04751 L04751 601310 GEN-157 Human cytochrome p-450 2115 2083A>G 3 4A (CYP4A) mRNA, complete eds L05628 L05628 158343 GEN- Human multidrug 3369 3173G>A R1058Q 4D9 resistance-associated protein (MRP) mRNA, complete eds L05628 L05628 158343 GEN- Human multidrug 4198 4002G>A S 4D9 resistance-associated protein (MRP) mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 191 153C>T LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 200 162G>A SD-144146.1 Page 8 LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 230 192T>C LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 242 204G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 295 257C>T A86V LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 330 292G>A D98N LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 338 300G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 638 600C>G LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 676 638A>G H213R LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 940 902G>A LVD sulfotransferase mRNA, complete eds L10819 L10819 171150 GEN- Homo sapiens aryl 1011 973T>C LVD sulfotransferase mRNA, complete eds L11696 L11696 104614 GEN-D6 Solute carrier family 3 1897 1854G>A M618I (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1 L11696 L11696 104614 GEN-D6 Solute carrier family 3' 2232 2189T>C (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral SD-144146.1 Page 88 amino acid transport), member 1 L13286 L13286 600125 GEN- Human mitochondrial 1 ,25- 2031 1638G>A 103 dihydroxyvitamin D3 24- hydroxylase mRNA, complete eds L19956 L19956 600641 GEN- Human aryl 243 105A>G LVE sulfotransferase mRNA, complete eds L19956 L19956 600641 GEN- Human aryl 284 146C>T S49F LVE sulfotransferase mRNA, complete eds L31801 L31801 600682 GEN-DQ Solute carrier family 16 1482 1470A>T E490D (monocarboxylic acid transporters), member 1 L31801 L31801 600682 GEN-DQ Solute carrier family 16 1772 1760G>C (monocarboxylic acid transporters), member 1 L32179 L32179 600338 GEN- Human arylacetamide 1366 1281 G>A 2IW deacetylase mRNA, complete eds L78207 L78207 600509 GEN-5Q Cell surface receptor for 4019 3981A>G sulfonylureas on pancreatic b cells LCT X07994 603202 GEN- Human mRNA for lactase- 5845 5834C>G 1F6 phlorizin hydrolase LPH (EC 3.2.1.23-62) LIPC J03540 151670 GEN-11 J Human hepatic lipase 469 465T>G S mRNA, complete eds LIPC J03540 151670 GEN-11 J Human hepatic lipase 595 591A>G S mRNA, complete eds LIPC J03540 151670 GEN-11 J Human hepatic lipase 648 644G>A S215N mRNA, complete eds LIPC J03540 151670 GEN-11 J Human hepatic lipase 817 813C>T S mRNA, complete eds LIPC J03540 151670 GEN-11 J Human hepatic lipase 1441 1437C>A S mRNA, complete eds M10901 M10901 138040 GEN-2W Corticosteroid nuclear 1220 1088A>G N363S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- S receptor b 1893AG>AG SD-144146.1 Page 88 M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- F receptor b 1893delAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2054 1922A>T D641V receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2372 2240T>G I747S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>C L753F receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>T L753F receptor b M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 2166 2034C>T S M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3353 3221T>G 3 M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3398 3266T>G 3 M14565 M14565 118485 GEN-30 Cytochrome P450, 947 903G>C M301 I subfamily XIA (cholesterol side chain cleavage) M 14758 M14758 171050 GEN- P glycoprotein 1 978 554- V185G 1S6 555TT>GA>G A M14758 M14758 171050 GEN- P glycoprotein 1 978 554- S 1S6 555TT>TT M14758 M14758 171050 GEN- P glycoprotein 1 1623 1199G>A S400N 1S6 M14758 M14758 171050 GEN- P glycoprotein 1 3101 2677G>A A893T 1 S6 M14758 M14758 171050 GEN- P glycoprotein 1 3101 2677G>T A893S 1S6 M14758 M14758 171050 GEN- P glycoprotein 1 3859 3435C>T S 1 S6 M14758 M14758 171050 GEN- P glycoprotein 1 4460 4036A>G 3 1S6 M15856 M15856 238600 GEN-33 Lipoprotein lipase 136 (-39)T>C 5 M15856 M15856 238600 GEN-33 Lipoprotein lipase 280 106G>A D36N M15856 M15856 238600 GEN-33 Lipoprotein lipase 438 264T>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 447 273G>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 474 300C>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 480 306A>C R102S M15856 M15856 238600 GEN-33 Lipoprotein lipase 511 337T>C W113R M15856 M15856 238600 GEN-33 Lipoprotein lipase 571 397C>T F SD-144146.1 Page 88 M15856 M15856 238600 GEN-33 Lipoprotein lipase 680 506G>A G169E M15856 M15856 238600 GEN-33 Lipoprotein lipase 722 548A>G D183G M15856 M15856 238600 GEN-33 Lipoprotein lipase 770 596C>G S199C M15856 M15856 238600 GEN-33 Lipoprotein lipase 781 607G>A A203T M15856 M15856 238600 GEN-33 Lipoprotein lipase 795 621 C>G D207E M15856 M15856 238600 GEN-33 Lipoprotein lipase 818 644G>A G215E M15856 M 15856 238600 GEN-33 Lipoprotein lipase 836 662T>C I221T M 15856 M15856 238600 GEN-33 Lipoprotein lipase 839 665G>A G222E M 15856 M15856 238600 GEN-33 Lipoprotein lipase 867 693C>G D231 E M 15856 M 15856 238600 GEN-33 Lipoprotein lipase 875 701C>T P234L M15856 M15856 238600 GEN-33 Lipoprotein lipase 916 742delG F M15856 M15856 238600 GEN-33 Lipoprotein lipase 983 809G>A R270H M15856 M15856 238600 GEN-33 Lipoprotein lipase 985 811T>A S271T M15856 M15856 238600 GEN-33 Lipoprotein lipase 1003 829G>A D277N M15856 M15856 238600 GEN-33 Lipoprotein lipase 1127 953A>G N318S M15856 M15856 238600 GEN-33 Lipoprotein lipase 1255 1081 G>A A361T M 15856 M15856 238600 GEN-33 Lipoprotein lipase 1348 1174C>G L392V M15856 M15856 238600 GEN-33 Lipoprotein lipase 1401 1227G>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 1508 1334G>A C445Y M15856 M 15856 238600 GEN-33 Lipoprotein lipase 1595 1421C>G F M15856 M15856 238600 GEN-33 Lipoprotein lipase 1973 1799T>C 3 M 15856 M15856 238600 GEN-33 Lipoprotein lipase 2428 2254T>A 3 M15856 15856 238600 GEN-33 Lipoprotein lipase 2743 2569T>C 3 M15856 M 15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2958 2784G>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3017 2843T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3343 3169T>C 3 M15856 M 15856 238600 GEN-33 Lipoprotein lipase 3447 3273C>T 3 M15872 M15872 138360 GEN-QS Human glutathione S- 16 (-40)G>A 5 transferase 2 (GST) mRNA, complete eds 15872 M15872 138360 GEN-QS Human glutathione S- 54 (-2)T>C 5 transferase 2 (GST) SD-144146.1 Page 8 mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 84 29T>C F10S transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 111 56C>T T19I transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 170 115G>T transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 321 266G>A R89K transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 376 321 C>T transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 430 375G>A transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 622 567C>T transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 684 629A>C E210A transferase 2 (GST) mRNA, complete eds M15872 M15872 138360 GEN-QS Human glutathione S- 701 646G>T A216S transferase 2 (GST) mRNA, complete eds M16505 M16505 308100 GEN-7D STERYL-SULFATASE 2725 2505T>G 3 PRECURSOR M16505 M16505 308100 GEN-7D STERYL-SULFATASE 4364 4144G>A 3 PRECURSOR M16505 M16505 308100 GEN-7D STERYL-SULFATASE 4665 4445A>G 3 PRECURSOR M16505 M16505 308100 GEN-7D STERYL-SULFATASE 5894 5674A>G 3 PRECURSOR M 16541 16541 177400 GEN-35 Butyrylcholinesterase 422 293A>G D98G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 557 428G>A G143D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 564 435- F146V 436TT>AG>A G SD-144146.1 Page 8 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 568 439C>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 596 467A>G Y156C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 941 812C>T T271 M M16541 M16541 177400 GEN-35 Butyrylcholinesterase 961 832A>C T278P M16541 M16541 177400 GEN-35 Butyrylcholinesterase 978 849G>C E283D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1201 1072T>A L358I M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1306 1177G>A ■ G393R M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1382 1253G>T G418V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1549 1420T>G F474V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1564 1435G>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1703 1574A>T E525V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1756 1627C>T R543C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16827 M16827 201450 GEN-EI Acyl-Coenzyme A 1956 1938T>C 3 dehydrogenase, C-4 to C- 12 straight chain M20681 M20681 138170 GEN- Human glucose 1550 1308C>T S 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3179 2937T>C 3 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3238 2996C>T 3 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3356 3114T>C 3 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3378 3136T>C 3 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3524 32820A 3 230 transporter-like protein-Ill (GLUT3), complete eds M20681 M20681 138170 GEN- Human glucose 3572 3330G>T 3 230 transporter-like protein-Ill SD-144146, 1 Page 89 (GLUT3), complete eds M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 331 294G>A S lung M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 400 363C>A D121 E lung M24400 M24400 118890 GEN-R2 Human chymotrypsinogen 121 105G>A S mRNA, complete eds M24400 M24400 118890 GEN-R2 Human chymotrypsinogen 231 2150A T72N mRNA, complete eds M24400 M24400 118890 GEN-R2 Human chymotrypsinogen 460 444C>T S mRNA, complete eds M24400 M24400 118890 GEN-R2 Human chymotrypsinogen 649 633C>T S mRNA, complete eds M24857 M24857 180190 GEN-80 Retinoic acid receptor, 1694 1280C>T S427L gamma 1 M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 193 147C>G S amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 967 921A>G amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1009 963G>C amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1027 981T>A amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1054 1008T>C amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1093 1047T>A amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1178 1132A>G N378D amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1191 1145T>C I382T amylase mRNA, complete eds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1394 1348A>T T450S amylase mRNA, complete SD- 144146 Page 89 cds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1474 1428T>C amylase mRNA, complete cds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1492 1446C>T amylase mRNA, comp M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1504 1458C>T amylase mRNA, complete cds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1543 1497G>A amylase mRNA, complete cds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1579 1533A>G amylase mRNA, complete cds M24895 M24895 104660 GEN-R3 Homo sapiens alpha- 1601 1555T>A amylase mRNA, complete cds M26393 M26393 201470 GEN-EW Acyl-Coenzyme A 1797 1765A>G dehydrogenase, C-2 to C-3 short chain M29874 M29874 None GEN-3I Cytochrome P450, 2758 2752T>A subfamily IIB (phenobarbital-inducible), polypeptide 6 M29874 M29874 None GEN-3I Cytochrome P450, 2836 2830G>A subfamily IIB (phenobarbital-inducible), polypeptide 6 M29874 M29874 None GEN-3I Cytochrome P450, 2902 2896T>C subfamily IIB (phenobarbital-inducible), polypeptide 6 M29882 M29882 107670 GEN-6R Apolipoprotein A-I I 26 17C>A A6E M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 183 174G>A S M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 192 1830A S M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 109 109G>A D37N (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 438 438A>G (lipoamide) beta SD-144146. Page 8 M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1172 1172A>C (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1179 1179C>T (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1323 1323C>A (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1376 1376G>C (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1433 1433C>T (lipoamide) beta M55040 M55040 100740 GEN-3Q acetylcholinesterase 323 167C>T P56L M55040 M55040 100740 GEN-3Q acetylcholinesterase 1154 998T>A V333E M55040 M55040 100740 GEN-3Q acetylcholinesterase 1213 1057C>A H353N M55040 M55040 100740 GEN-3Q acetylcholinesterase 1482 1326G>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431 C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 14310T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1663 1507T>C F503L M55531 M55531 138230 GEN-FF Solute carrier family 2 1208 1133T>G V378G (facilitated glucose transporter), member 5 M55531 M55531 138230 GEN-FF Solute carrier family 2 1975 1900C>T (facilitated glucose transporter), member 5 M55531 M55531 138230 GEN-FF Solute carrier family 2 1985 1910A>G (facilitated glucose transporter), member 5 M57899 M57899 191740 GEN- Human biiirubin UDP- 1828 1813C>T 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 1956 1941C>G 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 2057 2042C>G 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C methyltransferase SD-144146.1 Page 8 M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 418 214G>T A72S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 423 219G>A S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 612 408OG S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 813 609C>T S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1031 827delC F methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1039 835C>A 3 methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 159C>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 1590T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 174 1590T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 210 195G>C W65C methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 264 249A>T S methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 265 250C>T L84F methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 265 250C>T L84F methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 442 427A>G 1143V methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 442 427A>G 1143V methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 493 478G>A G160R methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 548 533A>G K178R methyltransferase M60761 M60761 156569 GEN-FL O-6-methylguanine-DNA 582 567G>A S SD-144146.1 Page 8 methyltransferase M61855 M61855 601130 M61855 M61855 601130 M61855 M61855 601130 M63012 M63012 168820 G M63509 M63509 138380 GEN-9G Glutathione S-transferase 644 628A>T T210S M2 (muscle) M64082 M64082 136130 GEN-9H Flavin-containing 1286 1188A>G S monooxygenase 1 (DIMETHYLANILINE MONOOXYGENASE) M64082 M64082 136130 GEN-9H Flavin-containing 1808 1710C>T 3 monooxygenase 1 (DIMETHYLANILINE MONOOXYGENASE) M64082 M64082 136130 GEN-9H Flavin-containing 1904 1806OT 3 monooxygenase 1 (DIMETHYLANILINE MONOOXYGENASE) M64592 M64592 120420 GEN-3X Granulocyte colony- 271 271T>G Y91D stimulating factor M64592 M64592 120420 GEN-3X Granulocyte colony- 1533 1533C>T S stimulating factor M64799 M64799 None GEN- Histamine receptor H2 398 398T>C V133A 4DN M64799 M64799 None GEN- Histamine receptor H2 525 525A>T K175N 4DN M64799 M64799 None GEN- Histamine receptor H2 620 620A>G K207R 4DN M64799 M64799 None GEN- Histamine receptor H2 649 649A>G N217D 4DN M64799 M64799 None GEN- Histamine receptor H2 692 692A>G K231 R 4DN M64799 M64799 None GEN- Histamine receptor H2 802 802G>A V268M 4DN SD-144146.1 Page 8 M68867 M68867 180231 GEN-S1 Human cellular retinoic 604 506C>A 3 acid-binding protein II (CRABP) mRNA, complete cds M68895 M68895 103735 GEN- Human alcohol 547 454G>A V152M MH7 dehydrogenase 6 gene, complete cds M69226 M69226 309850 GEN-3Z Monoamine oxidase A 435 385A>C S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 936 886C>T F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891 T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1076 1026A>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1373 1323G>A F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1609 1559A>G K520R M80244 M80244 600182 GEN- Human E16 mRNA, 202 (-109)G>C 5 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 520 210T>C S 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 1185 875G>A 3 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 1473 1163C>G 3 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 1692 1382C>T 3 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 2591 2281A>G 3 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 3138 2828G>C 3 3UJ complete cds M80244 M80244 600182 GEN- Human E16 mRNA, 3538 3228T>C 3 3UJ complete cds M96234 M96234 138333 GEN-9J Glutathione S-transferase 797 534T>C S M4 M98045 M98045 136510 GEN- Homo sapiens 802 732C>T S 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1747 1677G>T 3 4C3 folylpolyglutamate SD-144146 1 Page 8 synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1912 1842G>A 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1995 1925C>G 4C3 folylpolyglutamate synthetase mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1467 1250C>T 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1868 16510T 106 Miller-Dieker lissencephaly protein (LIS1) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1917 1700C>T 106 Miller-Dieker lissencephaly protein (LISI ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 2962 2745G>T 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 4589 4372G>A 106 Miller-Dieker lissencephaly protein (LIS1) mRNA, complete cds MTP X75500 157147 GEN- H.sapiens mRNA for 1847 1823T>G F608C 307 microsomal triglyceride transfer protein SD-144146.1 Page 8 MTP X75500 157147 GEN- H sapiens mRNA for 3231 3207G>A 307 microsomal triglyceride transfer protein NM0R1 J03934 125860 GEN-12L Human, 609 559C>T P187S NAD(P)H menadione oxidoreductase mRNA, complete cds NM0R1 J03934 125860 GEN-12L Human, 1784 1734T>G NAD(P)H menadione oxidoreductase mRNA, complete cds NMOR1 J03934 125860 GEN-12L Human, 1994 1944C>T NAD(P)H menadione oxidoreductase mRNA, complete cds NMOR2 J02888 160998 GEN-XT Human quinone 505 330G>A oxidoreductase (NQ02) mRNA, complete cds NMOR2 J02888 160998 GEN-XT Human quinone 909 734G>C oxidoreductase (NQ02) mRNA, complete cds NRAMP1 L32185 600266 GEN-2IY Homo sapiens integral 1399 1323C>T membrane protein (NRAMPI ) mRNΛ. complete cds NRAMP2 L37347 600523 GEN- Human integral membrane 1092 1083C>T 206 protein (Nramp2) mRNA, partial ORM1 M13692 138600 GEN- Human alpha-1 acid 128 113A>G Q38R 1 P5 glycoprotein mRNA, complete cds ORM1 M13692 138600 GEN- Human alpha-1 acid 222 207C>T I PS glycoprotein mRNA, complete cds ORM1 M13692 138600 GEN- Human alpha-1 acid 273 258A>C 1 P5 glycoprotein mRNA, complete cds ORM1 M13692 138600 GEN- Human alpha-1 acid 296 281 C>A T94N 1 P5 glycoprotein mRNA, complete cds ORM1 M13692 138600 GEN- Human alpha-1 acid 514 499C>T R167C SD-144146 1 Page 89 1P5 glycoprotein mRNA, complete cds 0RM1 M13692 138600 GEN- Human alpha-1 acid 535 520G>A V174M 1 P5 glycoprotein mRNA, complete cds 0RM1 M13692 138600 GEN- Human alpha-1 acid 654 639G>T 1 P5 glycoprotein mRNA, complete cds PDHA1 X52709 312170 GEN- Human mRNA for brain 849 795A>G 33Y pyruvate dehydrogenase (EC 1 2.4.1) PDHA1 X52709 312170 GEN- Human mRNA for brain 1337 1283C>T 33Y pyruvate dehydrogenase (EC 1 2 4 1 ) PDHA1 X52709 312170 GEN- Human mRNA for brain 1416 1362G>A 33Y pyruvate dehydrogenase (EC 1 2 4 1 ) PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 116 (-20)G>T 5 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 231 96G>C S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 1 14433-- S 25V mRNA, complete cds 114444GGTT>>GGTT PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 2 977fl8 Λ4Λ4r0dλc6eA1lCG-.TT 1 F 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 643 508OT 3 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 700 565G>C 3 25V mRNA, complete cds PNLIP M93285 246600 GEN- Pancreatic lipase (PNLIP) 646 646G>T V216L 48N (Dietary supplement) PRSS1 M22612 276000 GEN- Human pancreatic trypsin 34 28G>T V10L 26A 1 (TRY1 ) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 61 55G>A D19N 26A 1 (TRY1 ) mRNA, complete cds SD-144146 Page 89 PRSS1 M22612 276000 GEN- Human pancreatic trypsin 97 91 G>A E31 K 26A 1 (TRY1 ) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 198 192C>T S 26A 1 (TRY1 ) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 412 406G>T G136C 26A 1 (TRY1 ) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 492 486T>C S 26A 1 (TRY1) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 711 705C>T S 26A 1 (TRY1 ) mRNA, complete cds PRSS1 M22612 276000 GEN- Human pancreatic trypsin 744 738T>C s 26A 1 (TRY1 ) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 29 23C>T T8I 2C7 trypsinogen (TRY2) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 34 28G>T V10F 2C7 trypsinogen (TRY2) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 61 55G>A D19N 2C7 trypsinogen (TRY2) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 97 91G>A E31 K 2C7 trypsinogen (TRY2) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 198 192C>T S 2C7 trypsinogen (TRY2) mRNA, complete cds PRSS2 M27602 601564 GEN- Human pancreatic 276 270G>A S 2C7 trypsinogen (TRY2) mRNA, complete cds PXMP1 X58528 170995 GEN-392 Human PMP70 mRNA for 2375 2351 C>T 3 a peroxisomal membrane protein SLC18A3 U09210 600336 GEN- Human vesicular 1369 927A>G S 4F3 acetylcholine transporter SD-144146. Page 90 mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 1567 1125C>G 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2080 1638G>T 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2199 1757G>A 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2349 1907G>T 4F3 acetylcholine transporter mRNA, complete cds SLC5A1 M24847 182380 GEN- Human Na+/glucose 2226 2216C>T 28S cotransporter 1 mRNA, complete cds SLC6A3 L24178 126455 GEN-283 Homo sapiens dopamine 1917 1898C>T transporter mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 676 (-721 )T>G 25C Axholesterol acyltransferase mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 814 (-583)OT 25C Axholesterol acyltransferase mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 1993 597C>T 25C Axholesterol acyltransferase mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 2365 969C>T 25C Axholesterol acyltransferase mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 2821 1425G>C 25C Axholesterol acyltransferase mRNA, complete cds SOAT L21934 102642 GEN- Human acyl coenzyme 3537 2141T>C 25C Axholesterol SD-144146. Page 90 acyltransferase mRNA, complete cds S0D2 X07834 147460 GEN- Human mRNA for 44 40C>G P14A 1 ES manganese superoxide dismutase (EC 1 ,15.1.1 ) SOD2 X07834 147460 GEN- Human mRNA for 51 47T>C V16A 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SOD2 X07834 147460 GEN- Human mRNA for 198 194C>A T65N 1 ES manganese superoxide dismutase (EC 1.15.1.1) SOD2 X07834 147460 GEN- Human mRNA for 249 245T>C I82T 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SOD3 J02947 185490 GEN-Y3 Human extracellular- 1042 973C>T superoxide dismutase (SOD3) mRNA, complete cds SPINK1 Y00705 167790 GEN-UA Homo sapiens pstl mRNA 332 272C>T for pancreatic secretory inhibitor (expressed in neoplastic tissue) TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1163 1135G>A V379I 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1186 1158G>T S 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1840 1812G>A S 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2021 1993G>A A665T 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2087 2059C>T F 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2119 2091T>G S 26P complete CDS TBG M14091 314200 GEN- Human thyroxine-binding 901 571 G>A D191 N 1QO globulin mRNA, complete cds TBG M14091 314200 GEN- Human thyroxine-binding 1239 909G>T L303F 1QO globulin mRNA, complete cds TCN2 M60396 275350 GEN- Human transcobalamin II 1164 1127C>T S376L SD-144146.1 Page 90 3AX (TCII) mRNA, complete cds TCN2 M60396 275350 GEN- Human transcobalamin II 1765 1728T>C SAX (TCII) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 536 460G>A A154T 1 LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 795 719A>G Y240C 1 LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1085 1009T>C 1 LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1336 1260C>T 1 LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1373 1297G>A 1 LY methyltransferase (TPMT) mRNA, complete cds TPP2 M55169 190470 GEN- Homo sapiens tripeptidyl 2681 2681T>G F894C 35U peptidase II mRNA, 3 end TPP2 M55169 190470 GEN- Homo sapiens tripeptidyl 3637 3637G>A 3 35U peptidase II mRNA, 3 end U03858 U03858 600007 GEN- Fms-related tyrosine 683 600C>T S MDM kinase 3 ligand U03858 U03858 600007 GEN- Fms-related tyrosine 1016 933T>C 3 MDM kinase 3 ligand U06088 U06088 253000 GEN- Human N- 1936 19360T 3 MP3 acetylgalactosamine 6- sulphatase (GALNS) gene U06088 U06088 253000 GEN- Human N- 2180 2180G>A MP3 acetylgalactosamine 6- sulphatase (GALNS) gene U06088 U06088 253000 GEN- Human N- 2221 2221G>A MP3 acetylgalactosamine 6- sulphatase (GALNS) gene U07132 U07132 600380 GEN-7M Orphan receptor 763 519G>A S U07132 U07132 600380 GEN-7M Orphan receptor 1399 1155C>T s U07132 U07132 600380 GEN-7M Orphan receptor 1726 1482G>C 3 U07132 U07132 600380 GEN-7M Orphan receptor 1952 1708C>G 3 SD-144146.1 Page 90 U08021 U08021 600008 GEN- Human nieotinamide N- 584 467C>G P156R 1 FG methyltransferase (NNMT) mRNA, complete cds U08021 U08021 600008 GEN- Human nieotinamide N- 613 496C>T S 1 FG methyltransferase (NNMT) mRNA, complete cds U08989 U08989 133550 GEN- Human glutamate 684 519C>T S CBZ transporter mRNA, complete cds U08989 U08989 133550 GEN- Human glutamate 1617 1452T>C S CBZ transporter mRNA, complete cds U09178 U09178 274270 GEN-HA Dihydropyrimidine 166 85T>C C29R Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 166 85T>C C29R Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 577 496A>G M166V Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 638 557A>G Y186C Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 1708 1627A>G I543V Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3432 3351T>C 3 Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3730 3649G>A 3 Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3925 3844A>G 3 Dehydrogenase U09178 U09178 274270 GEN-HA Dihydropyrimidine 3937 3856T>C 3 Dehydrogenase U10868 U10868 600466 GEN-1JF Human aldehyde 2681 2634T>C 3 dehydrogenase ALDH7 mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 149 122A>C E41A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U 16660 U16660 600696 GEN- Human peroxisomal enoyl- 402 375G>A S 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds SD- 144146.1 Page 9 U16660 U16660 600696 GEN- Human peroxisomal enoyl- 802 775C>G P259A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U 16660 U 16660 600696 GEN- Human peroxisomal enoyl- 1157 1130G>A 3 1YD CoA hydratase-like protein (HPXEL) mRNA, complete U17986 U17986 300036 GEN- Hu 20X GABA/noradrenaline transporter mRNA, complete cds U17986 U17986 300036 GEN- Human 1670 1641 C>T S 20X GABA/noradrenaline transporter mRNA, complete cds U17986 U17986 300036 GEN- Human 2034 2005G>A V669M 20X GABA/noradrenaline transporter mRNA, complete cds U17986 U17986 300036 GEN- Human 2088 2059C>T R687C 20X GABA/noradrenaline transporter mRNA, complete cds U17986 U17986 300036 GEN- Human 2150 21210T S 20X GABA/noradrenaline transporter mRNA, complete cds U 17986 U 17986 300036 GEN- Human 2231 2202A>G 3 20X GABA/noradrenaline transporter mRNA, complete cds U19720 U 19720 600424 GEN-11 Folate Transporter 53 (-43)T>C 5 (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1 ) U 19720 U 19720 600424 GEN-11 Folate Transporter 341 246C>G S (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 791 696C>T S SD-144146.1 Page 90 (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate U19720 U19720 600424 GEN-11 Folate U19720 U19720 600424 GEN-11 Folate U19720 U19720 600424 GEN-11 Folate U19720 U19720 600424 GEN-H Folate U19720 U19720 600424 GEN-11 Folate U19720 U19720 600424 GEN-11 Folate (SLC19A1 ) U19977 U19977 600688 GEN- Human 631 627C>T S 22Q preprocarboxypeptidase A2 (proCPA2) mRNA, complete cds U20157 U20157 601690 GEN-234 Human platelet-activating 1297 1136T>C V379A factor acetylhydrolase mRNA, complete cds U25029 U25029 138040 GEN-82 Glucocorticoid receptor 335 335C>T 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 386 386T>C 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 1069 1069C>T 3 alpha U27699 U27699 603080 GEN- Human pephBGT-1 2841 2255C>T 3 2C9 betaine-GABA transporter mRNA, complete cds U34252 U34252 602733 GEN- Human gamma- 2417 2040G>A 305 aminobutyraldehyde dehydrogenase mRNA, complete cds U34252 U34252 602733 GEN- Human gamma- 2471 2094A>C 305 aminobutyraldehyde dehydrogenase mRNA, complete cds U34252 U34252 602733 GEN- Human gamma- 2674 2297A>C 305 aminobutyraldehyde SD-144146.1 Page 90 dehydrogenase mRNA, complete cds U34252 U34252 602733 GEN- Human gamma- 2676 2299A>C 305 a inobutyraldehyde dehydrogenase mRNA, complete cds U35735 U35735 111000 GEN- Human RACH1 (RACH1) 1006 838A>G N280D 2MN mRNA, complete cds U35735 U35735 111000 GEN- Human RACH1 (RACH1) 2619 2451T>C 3 2MN mRNA, complete cds U35735 U35735 111000 GEN- Human RACH1 (RACH1) 2706 2538T>C 3 2MN mRNA, complete cds U36601 U36601 603268 GEN-IR Heparan N-deacetylase/N- 2727 2700T>G 3 sulfotransferase-2 U36601 U36601 603268 GEN-IR Heparan N-deacetylase/N- 2972 2945A>G 3 sulfotransferase-2 U37143 U37143 601258 GEN- Human cytochrome P450 338 333G>C S 2NS monooxygenase CYP2J2 mRNA, complete cds U37143 U37143 601258 GEN- Human cytochrome P450 1545 1540C>T 2NS monooxygenase CYP2J2 mRNA, complete cds U53347 U53347 109190 GEN- Human neutral amino acid 2868 2249A>T 34A transporter B mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 75 16T>C C6R 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 150 91G>A A31T 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 511 452C>T T151I 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 1161 1102A>G 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds SD-144146.1 Page 90 U70867 U70867 601460 GEN-4S prostaglandin transporter 2706 2615T>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 2839 2748T>A hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 2908 2817A>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3171 3080A>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3171 3080A>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3253 3162A>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3255 3164A>G hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3594 3503T>A hPGT U79745 U79745 None GEN- Homo sapiens 2095 1930G>A LPT monocarboxylate transporter homologue MCT6 mRNA, complete cds U81375 U81375 602193 GEN- Human placental 1989 1811G>A 3VO equilibrative nucleoside transporter 1 (hENTI) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 1996 1818C>T 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 2045 1867T>C 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81800 U81800 None GEN- Homo sapiens 1624 1562G>C 3WB monocarboxylate ansporter (MCT3) mRNA, complete cds U92314 U92314 604125 GEN- Homo sapiens 1146 771 C>T 47U hydroxysteroid sulfotransferase SULT2B1a (HSST2) SD-144146.1 Page 90 mRNA, complete cds U92314 U92314 604125 GEN- Homo sapiens 1164 789C>T 47U hydroxysteroid sulfotransferase SULT2B1a (HSST2) mRNA, complete cds U92314 U92314 604125 GEN- Homo sapiens 1278 903T>C 47U hydroxysteroid sulfotransferase SULT2B1a (HSST2) mRNA, complete cds V00494 V00494 103600 GEN-TL Human messenger RNA 34 (-6)G>T 5 for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 36 (-4)C>G 5 for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 401 362G>A G121 E for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 431 392A>G D131G for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1090 1051T>C S for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1091 1052T>G L351W for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1531 1492A>C T498P for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1533 1494C>A S for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1637 1598T>C F533S for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1707 16680T S for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1719 1680G>A S for serum albumin (HSA) V00494 V00494 103600 GEN-TL Human messenger RNA 1926 1887T>A 3 for serum albumin (HSA) V00594 V00594 156360 GEN-P6 Human mRNA for 320 263G>C 3 metallothionein from cadmium-treated cells X02317 X02317 147450 GEN-KM Superoxide dismutase 1 614 550A>C 3 (Cu/Zn) X02920 X02920 107400 GEN-PH Human mRNA for alpha 1- 107 107T>C L36P SD-144146.1 Page 90 antitrypsin carboxyterminal region (aa 268-394) X02920 X02920 107400 GEN-PH Human mRNA for alpha 1- 137 137G>A S46N antitrypsin carboxyterminal region (aa 268-394) X02920 X02920 107400 GEN-PH Human mRNA for alpha 1- 195 195C>T S antitrypsin carboxyterminal region (aa 268-394) X02920 X02920 107400 GEN-PH Human mRNA for alpha 1- 327 327A>C E109D antitrypsin carboxyterminal region (aa 268-394) X03438 X03438 138970 GEN-PM Human mRNA for 586 555G>A granulocyte colony- stimulating factor (G-CSF) X03438 X03438 138970 GEN-PM Human mRNA for 1235 1204C>T 3 granulocyte colony- stimulating factor (G-CSF) X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3732 3432T>C 3 receptor X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3951 3651 OA 3 receptor X08006 X08006 None GEN- Human mRNA for 100 100C>T P34S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 124 124G>A G42R 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 137 137 Λ 138insT F 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 271 271 C>G L91V 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 281 281A>G H94R 1FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 294 294C>G S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 336 336C>T S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 408 408G>C S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 408 408G>C S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 454 454delT F 1 FE cytochrome P450 db1 SD-144146.1 Page 91 X08006 X08006 None GEN- Human mRNA for 505 505G>T F 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 635 635G>A G212E 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 692 692T>C L231 P 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 696 696T>C S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 775 775delA F 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 801 801 C>A S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 836 836T>A M279K 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 839 839- S 1 FE cytochrome P450 db1 841AGA>AG A X08006 X08006 None GEN- Human mRNA for 839 839- K281del 1 FE cytochrome P450 db1 841 del AGA X08006 X08006 None GEN- Human mRNA for 840 840- S 1 FE cytochrome P450 db1 842GAA>GA A X08006 X08006 None GEN- Human mRNA for 840 840- K281del 1 FE cytochrome P450 db1 842delGAA X08006 X08006 None GEN- Human mRNA for 854 854A>G N285S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 886 886C>T R296C 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 971 971A>C H324P 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1108 1108G>A V370I 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1203 1203G>A S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1262 1262T>C L421 P 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1401 1401G>C S 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1457 1457G>C S486T 1 FE cytochrome P450 db1 X08006 X08006 None GEN- Human mRNA for 1457 1457G>C S486T SD-144146.1 Page 91 1 FE cytochrome P450 db1 X12387 X12387 124010 GEN- Human mRNA for 44 (-26)G>C 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 628 559A>T T187S 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 646 577A>G 1193V 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 676 607T>C F203L 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 823 754T>G S252A 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 1361 1292T>C 1431T 1 LZ cytochrome P-450 (cyp3 locus) X12387 X12387 124010 GEN- Human mRNA for 2189 2120G>A 1 LZ cytochrome P-450 (cyp3 locus) X13561 X13561 147910 GEN- Human mRNA for 54 18G>T S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 441 405T>C S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 469 433G>C E145Q 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 592 556A>G K186E 10H preprokallikrein (EC 3.4.21 ) X13589 X13589 107910 GEN-56 Cytochrome P450, 364 240A>G S subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of SD-144146.1 Page 91 androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1655 15310T 3 subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1796 1672G>T 3 subfamily XIX (aromatization of androgens) X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 60 51A>G S 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 255 246T>C S 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 272 263G>A R88K 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1072 1063G>A V355M 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1146 1137G>A S 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1485 1476G>T S 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1675 1666A>T 3 1 Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1677 1668C>G 3 1Q3 P-450 IIA4 protein X13930 X13930 122720 GEN- Human CYP2A4 mRNA for 1697 1688C>A 3 1Q3 P-450 IIA4 protein X16699 X16699 124075 GEN- Human mRNA for 1064 1064T>G F355C 1YJ cytochrome P-450HP X52773 X52773 180245 GEN-74 Retinoid X receptor, alpha 1744 1669G>A 3 X56199 X56199 None GEN- Human XIST, coding 1338 1339T>G 3 36T sequence a mRNA (locus DXS399E) X57522 X57522 170260 GEN- H.sapiens RING4 cDNA 1207 1177A>G I393V 37W X57522 X57522 170260 GEN- H.sapiens RING4 cDNA 2120 2090A>G D697G 37W X59498 X59498 176300 GEN-RU H.sapiens ttr mRNA for 92 71 G>A G24D transthyretin X59498 X59498 176300 GEN-RU H.sapiens ttr mRNA for 177 156G>T S transthyretin SD-144146.1 Page 91 X59498 X59498 176300 GEN-RU H.sapiens ttr mRNA for 380 3590T S120F transthyretin X60069 X60069 231950 GEN- Human mRNA for 102 (-257)G>A 5 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 336 (-23)C>T 5 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1173 815C>T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1173 815C>T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1399 1041C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1409 1051 G>T A351 S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1482 1124C>T T375M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1591 1233G>A S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1624 1266C>T 3AJ pancreatic gamma- g I utamyltransf erase X60069 X60069 231950 GEN- Human mRNA for 1637 1279C>A P427T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1651 1293C>T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1662 1304T>C V435A 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1783 1425A>G 3AJ pancreatic gamma- glutamyltransferase SD-144146.1 Page 91 X60069 X60069 231950 GEN- Human mRNA for 1794 1436C>T T479M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1795 1437G>A S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1981 1623C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2007 1649C>T T550M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2031 1673C>T S558L 3AJ pancreatic gamma- g lutamy Itra nsf erase X60069 X60069 231950 GEN- Human mRNA for 2047 16890T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2147 1789C>T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2176 1818C>T 3 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2224 1866C>A 3 3AJ pancreatic gamma- glutamyltransferase X63359 X63359 600070 GEN- H.sapiens UGT2BI0 1516 1506C>T S 3DC mRNA for udp glucuronosyltransferase X63359 X63359 600070 GEN- H.sapiens UGT2BI0 2714 2704G>A 3 3DC mRNA for udp glucuronosyltransferase X63522 X63522 180246 GEN-75 MHC class I promoter 1331 1152T>C S binding protein X64177 X64177 156351 GEN- H-sapiens mRNA for 63 40G>A A14T 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 90 67A>G K23E 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 125 102C>T S 3EQ metallothionein SD-144146.1 Page 91 X64177 X64177 156351 GEN- H.sapiens mRNA for 131 108T>C S 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 168 145A>G I49V 3EQ metallothionein X64177 X64177 156351 GEN- H.sapiens mRNA for 182 159G>A S 3EQ metallothionein X68836 X68836 601468 GEN-3IR H-sapiens mRNA for S- 240 175G>A V59I adenosylmethionine synthetase X71440 X71440 None GEN- H.sapiens mRNA for 949 936G>C M312I 3KS peroxisomal acyl-CoA oxidase X78282 X78282 601292 GEN- H.sapiens mRNA for aryl 895 895T>C 3 LVF sulfotransferase (ST1A2) X79389 X79389 600436 GEN- H.sapiens GSTT1 mRNA 824 824T>C 3 3T7 X86681 X86681 602110 GEN- H.sapiens mRNA for 1725 1340G>A 3 41 E nucleolar protein, HNP36 X90908 X90908 600422 GEN- H-sapiens mRNA for 1-15P 364 236C>T T79M LSA (l-BABP) protein X90999 X90999 138760 GEN-477 H-sapiens mRNA for 950 914A>G 3 Glyoxalase II X95190 X95190 601641 GEN- H-sapiens mRNA for 1394 1302OT S 49Y Branched chain Acyl-CoA Oxidase X95190 X95190 601641 GEN- H.sapiens mRNA for 1934 1842C>A S 49Y Branched chain Acyl-CoA Oxidase X96395 X96395 601107 GEN- H.sapiens mRNA for 848 811 G>T A271S 4AM canalicular multidrug resistance protein X97868 X97868 300003 GEN- H.sapiens mRNA for 1652 1582T>C Y528H LTH arylsulphatase X98332 X98332 602607 GEN- H.sapiens mRNA for 630 558C>T S MMA organic cation transporter, liver XDH U06117 278300 GEN-194 Human xanthine 3951 3888C>G S dehydrogenase (XDH) mRNA, complete cds Y00498 Y00498 601129 GEN-9N Cytochrome P450, 431 389C>A T130N subfamily IIC (mephenytoin SD-144146.1 Page 91 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 489 447T>C subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 491 449A>G H150R subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 522 480G>T K160N subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 525 483T>C subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 582 540C>T subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 583 541G>A V181 I subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 834 792C>G I264M subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601 129 GEN-9N Cytochrome P450, 999 9570G subfamily IIC (mephenytoin 4-hydroxylase) Y00498 Y00498 601129 GEN-9N Cytochrome P450, 1539 1497T>C subfamily IIC (mephenytoin 4-hydroxylase) Table 15. Identified Variances In Genes for Pathways Identified in Inflammati on and Immune Disease SD-144146.1 Page 91 AB00022 AB00022 None GEN- Homo sapiens mRNA for 427 364C>T 1 1 16K CC chemokine, complete cds AB00050 AB00050 602356 GEN-161 Homo sapiens mRNA for 2185 2131A>T 3 TRAF5, complete cds AB00088 AB00088 602227 GEN- Human mRNA for EBI1- 627 489G>A 3 14F ligand chemokine, complete cds AB00240 AB00240 602737 GEN- Homo sapiens mRNA for 794 736T>G 3 1A1 SLC, complete cds AB02068 AB02068 None GEN- Homo sapiens mRNA for 3854 3854A>G 3 0 0 LAX KIAA0873 protein, partial cds AC00577 AC00577 None GEN- Homo sapiens 1492 1482G>A 3 ML4 chromosome 19, cosmid F20237 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 365 365C>T P122L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 381 381 G>A P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 624 624A>G P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 641 641 C>T P214L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 1161 1161T>C P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 545 435C>T S 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 1748 1638G>A S 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 2360 2250G>A 3 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI) 2552 2442C>T 3 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI) 3016 2906A>G 3 SD-144146.1 Page 91 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 3073 2963A>G 3 15U AF001174 AF001174 602898 GEN- Homo sapiens p38beta2 1044 1038T>C S 18T MAP kinase mRNA, complete cds AF004709 AF004709 602899 GEN-UX Homo sapiens stress- 432 384G>A S activated protein kinase 4 mRNA, complete cds AF006689 AF006689 603014 GEN-YA Homo sapiens MAP kinase 75 (-1 )G>A 5 kinase Jnkk2 mRNA, complete cds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 808 808C>G H270D 1 HV caspase Mch5-beta mRNA, alternatively spliced, complete cds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 915 915G>A S 1 HV caspase Mch5-beta mRNA, alternatively spliced, complete cds AF012535 AF012535 None GEN- Homo sapiens death 234 95T>C L32P 1Z2 receptor 5 (DR5) mRNA, complete cds AF012535 AF012535 None GEN- Homo sapiens death 339 200C>T A67V 1Z2 receptor 5 (DR5) mRNA, complete cds AF012535 AF012535 None GEN- Homo sapiens death 1397 1258G>C 3 1Z2 receptor 5 (DR5) mRNA, complete cds AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1023 987T>C S 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1025 989T>C F330S 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1090 1054G>C E352Q 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1321 1285G>A 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 SD-144146.1 Page 91 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1424 13880G 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1512 1476G>A 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1743 1707A>G 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1858 1822A>G 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 781 781 G>A 3 2A5 binding protein (BAD) mRNA, partial cds AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 883 883C>A 3 2A5 binding protein (BAD) mRNA, partial cds AF026070 AF026070 None GEN- Homo sapiens death 455 387A>G S 26S receptor 3 beta (DR3) mRNA, complete cds AF026070 AF026070 None GEN- Homo sapiens death 1202 1134T>C S 26S receptor 3 beta (DR3) mRNA, complete cds AF026070 AF026070 None GEN- Homo sapiens death 1204 1136T>G L379R 26S receptor 3 beta (DR3) mRNA, complete cds AF026070 AF026070 None GEN- Homo sapiens death 1237 1169A>G H390R 26S receptor 3 beta (DR3) mRNA, complete cds HRH1 AF026261 600167 GEN- Histamine receptor H1 1068 1068A>G S 26W AF029761 AF029761 None GEN- Homo sapiens decoy 1011 929C>T S310L MND receptor 2 mRNA, complete cds ITGA7 AF032108 600536 GEN- Homo sapiens integrin 527 366G>A S 2NO alpha-7 mRNA, complete cds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 273 273G>A F mRNA, partial cds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 295 295G>C A99P SD-144146.1 Page 92 mRNA, partial cds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 302 302OT T101 I mRNA, partial cds TUBB AF035316 191130 GEN-2IH Homo sapiens clone 23678 1059 1059G>A 3 mRNA, partial cds AF039400 AF039400 603906 GEN- Homo sapiens calcium- 2787 2436T>C S MQY dependent chloride channel-1 (hCLCAI ) mRNA, complete cds AF043472 AF043472 603888 GEN- Homo sapiens Shab- 1840 1709T>G 3 2XX related delayed-rectifier K+ channel alpha subunit (KCNS3) mRNA, complete cds AF048837 AF048837 602973 GEN- Homo sapiens cGMP- 1551 1491T>C S LGG specific phosphodiesterase (PDE9A2) mRNA, complete cds AF053712 AF053712 None GEN- Homo sapiens 2086 1902T>G 3 MM2 osteoprotegerin ligand mRNA, complete cds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1972 1663G>A LJY phospholipase A2-gamma mRNA, complete cds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1989 1680A>T LJY phospholipase A2-gamma mRNA, complete cds AF065164 AF065164 None GEN- Homo sapiens 1980 1860T>C LKQ hyperpolarization-activated channel 1 (IH1 ) mRNA, partial cds AF094760 AF094760 None GEN- Homo sapiens RFXANK 1038 621 G>A LSB (RFXANK) mRNA, complete cds AF094760 AF094760 None GEN- Homo sapiens RFXANK 1071 654C>T LSB (RFXANK) mRNA, complete cds D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 149 100G>A D34N D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 341 292G>T V98L D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 479 430A>T N144Y SD-144146.1 Page 92 D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 1288 1239G>A 3 D12614 D12614 153440 GEN-QD Human mRNA for 319 179C>A T60N lymphotoxin (TNF-beta), complete cds D13138 D13138 179780 GEN- Human mRNA for 566 523T>G S175A 1 NW dipeptidase CYP11 B2 D13752 124080 GEN- Human CYP11 B2 gene for 1600 1593G>A 3 CCD steroid 18-hydroxylase, complete cds D13811 D13811 238310 GEN-AA Glycine cleavage system: 277 148G>T V50L Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1073 944G>A R315K Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1083 954G>A S Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1773 1644C>T 3 Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 2037 1908OT 3 Protein T D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1035 599T>G I200S I i f e. D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039C>T R347C 1 i r e D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039C>T R347C 1 c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 2048 1612C>T 3 1c D25418 D25418 600022 GEN-78 Prostaglandin 12 726 635G>A R212H (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1047 956C>G S319W (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1075 984A>C S (prostacyclin) receptor (IP) D26579 D26579 602267 GEN- Human mRNA for 709 700G>A D234N 261 transmembrane protein, complete cds D26579 D26579 602267 GEN- Human mRNA for 909 900T>C 261 transmembrane protein, complete cds D26579 D26579 602267 GEN- Human mRNA for 999 990C>T 261 transmembrane protein, SD-144146.1 Page 92 complete cds D26579 D26579 602267 GEN- Human mRNA for 1104 1095A>G S 261 transmembrane protein, complete cds D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 25 (-47)G>A 5 transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1332 1261A>G 1421V transformylase D32051 D32051 138440 GEN-4 Glycinamide ribonucleotide 1855 1784G>C 3 transformylase PTGIR D38128 600022 GEN- Human IP gene for 203 204C>G 3 4DH prostacyclin receptor, exon 3 PTGIR D38128 600022 GEN- Human IP gene for 231 232C>A 3 4DH prostacyclin receptor, exon 3 D38145 D38145 601699 GEN- Human mRNA for 1646 1619T>C 3 4E3 prostacyclin synthase, complete cds NT5 D38524 129190 GEN- Human mRNA for 5- 3075 29920T 3 2PF nucleotidase D42108 D42108 600597 GEN- Phospholipase C epsilon 1908 1705G>A V569I 2U4 D42108 D42108 600597 GEN- Phospholipase C epsilon 2864 2661 G>A S 2U4 D42108 D42108 600597 GEN- Phospholipase C epsilon 4453 4250G>A 3 2U4 D45887 D45887 114182 GEN-BA Calmodulin 1 34 (-35)G>T 5 (phosphorylase kinase, delta) D49737 D49737 602413 GEN- Homo sapiens mRNA for 908 784G>A 3 2Z7 cytochrome b large subunit of complex II, complete cds D86955 D86955 601960 GEN- Human mRNA for CC 328 270T>C S 410 chemokine LARC precursor, complete cds D87461 D87461 601931 GEN- Human mRNA for 2432 2256C>A 3 43N KIAA0271 gene, complete cds D87845 D87845 602344 GEN- Human mRNA for platelet- 2299 2096G>A 3 44C activating factor SD-144146. Page 9 acetylhydrolase 2, complete cds D87845 D87845 602344 GEN- Human mRNA for platelet- 2332 2129A>G 3 44C activating factor acetylhydrolase 2, complete cds D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 434 (-1284)A>T 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 889 (-829)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 1156 (-562)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2644 927T>C S D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2920 1203A>G 3 EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2228 1748G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2376 1896G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2840 2360G>C 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2935 2455G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 3294 2814A>G 3 4DX A J00123 J00123 131330 GEN- Human enkephalin gene 81 81 OT S MK4 DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 SD-144146.1 Page 92 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 721 679T>A 3 4E9 reductase gene DHFR J00140 126060 GEN- Human dihydrofolate 829 787C>T 3 4E9 reductase gene CBG J02943 122500 GEN-Y2 Human corticosteroid 106 71A>T D24V binding globulin mRNA, complete cds CBG J02943 122500 GEN-Y2 Human corticosteroid 971 936T>C S binding globulin mRNA, complete cds CBG J02943 122500 GEN-Y2 Human corticosteroid 1229 1194G>A S binding globulin mRNA, complete cds J03004 J03004 139360 GEN-79 Guanine nucleotide binding 758 681 C>T S protein (G protein), alpha inhibiting activity polypeptide 2 J03019 J03019 109630 GEN- Human beta-1 -adrenergic 503 417G>A S 4D6 receptor mRNA, complete cds J03143 J03143 107470 GEN-ZK Human interferon-gamma 1098 1050T>G S receptor mRNA, complete cds J03209 J03209 185250 GEN-PK Human matrix 133 133G>A E45K metalloproteinase-3 (MMP- 3) mRNA, complete cds J03209 J03209 185250 GEN-PK Human matrix 288 288C>T S metalloproteinase-3 (MMP- 3) mRNA, complete cds J03210 J03210 120360 GEN-ZY Human collagenase type 721 721 C>T P241S IV mRNA, 3 end J03210 J03210 120360 GEN-ZY Human collagenase type 1759 1759C>T P587S IV mRNA, 3 end J03250 J03250 172420 GEN-C4 DNA topoisomerase I 160 (-52)OT 5 J03250 J03250 172420 GEN-C4 DNA topoisomerase I 590 379G>A V127I J03250 J03250 172420 GEN-C4 DNA topoisomerase I 1984 1773G>A S J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 172 57C>T S dihydroxyvitamin D3) receptor SD-144146.1 Page 92 J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 559 4440T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1704 1589C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1833 1718C>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1858 1743G>T 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1959 1844A>C 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 2190 2075delT F dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3301 3186C>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3991 3876A>G 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A 3 dihydroxyvitamin D3) receptor J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 140 72G>T S J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 1511 1443A>T E481 D C7 J03507 217070 GEN- Human complement 1951 1951G>A V651 I 11 R protein component C7 mRNA, complete cds C7 J03507 217070 GEN- Human complement 3032 3032T>C 3 11 R protein component C7 mRNA, complete cds C7 J03507 217070 GEN- Human complement 3634 3634A>G 3 11 R protein component C7 mRNA, complete cds SD-144146.1 Page 92 C7 J03507 2 7070 GEN- Human complement 3831 3831A>G 3 11 R protein component C7 mRNA, complete cds J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 55 21 C>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 959 925C>A P309T lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 1762 1728A>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- lipoxygenase (leukocytes) 2043AC>AC J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- lipoxygenase (leukocytes) 2043delAC J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2328 2294C>T lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2376 2342T>G lipoxygenase (leukocytes) PTHLH J03580 168470 GEN- Human, parathyroid-like 975 37G>A V13M 11 U protein (associated with humoral hypercalcemia of malignancy) mRNA, complete cds PTHLH J03580 168470 GEN- Human, parathyroid-like 996 58G>A V20M 11 U protein (associated with humoral hypercalcemia of malignancy) mRNA, complete cds J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1202 1164C>T S 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1237 1199T>G I400S 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1372 1334C>G P445R 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1379 1341 C>T S 2c J04031 J04031 172460 GEN-C6 Methenyltetrahydrofolate 454 401 G>A R134K cyclohydrolase SD-144146.1 Page 92 J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 969 916C>G Q306E cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 1614 1561T>C S cyclohydrolase J04031 J04031 172460 GEN-C6 Methenyltetrahydrofolate 2011 1958G>A R653Q cyclohydrolase J04031 J04031 172460 GEN-CB Methenyltetrahydrofolate 2335 2282C>T T761 M cyclohydrolase J04046 J04046 114183 GEN- Human calmodulin mRNA, 791 688C>T 3 13N complete cds J04046 J04046 114183 GEN- Human calmodulin mRNA, 881 778T>C 3 13N complete cds J04046 J04046 114183 GEN- Human calmodulin mRNA, 1927 1824T>C 3 13N complete cds C1 S J04080 120580 GEN- Complement C1 S 558 356G>A R119H 13T component precursor (C1 esterase) C C11 SS JJ0044008800 112200558800 GEN- Complement C1 S 2140 1938A>T K646N 13T component precursor (C1 esterase) C C11SS JJ0044008800 112200558800 GEN- Complement C1S 2234 2032A>T T678S 13T component precursor (C1 esterase) C C11 SS JJ0044008800 112200558800 GEN- Complement C1 S 2333 2131G>T 3 13T component precursor (C1 esterase) J J0044113322 JJ0044113322 118866778800 GEN- Human T cell receptor 1403 1329G>C 3 KXY zeta-chain mRNA, complete cds J J0044113322 JJ0044113322 118866778800 GEN- Human T cell receptor 1410 1336A>T 3 KXY zeta-chain mRNA, complete cds J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 206 206G>A R69H J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 1780 1780C>T S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 2478 2478G>A S J04145 J04145 120980 GEN-6 Leukocyte integrin alpha-m 2978 2978C>A T993N J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3415 3415C>T P1139S J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3661 3661 C>T 3 J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 3804 3804A>G 3 J04145 J04145 120980 GEN-B Leukocyte integrin alpha-m 4071 4071 G>A 3 SD-144146.1 Page 92 SPN J04168 182160 GEN- Human leukosialin mRNA, 974 879C>T S 13W complete cds SPN J04168 182160 GEN- Human leukosialin mRNA, 1328 1233G>C 3 13W complete cds J04208 J04208 146691 GEN-2M IMP (inosine 349 302C>G A101G monophosphate) dehydrogenase 2 J04208 J04208 146691 GEN-2M IMP (inosine 1570 1523C>T S508L monophosphate) dehydrogenase 2 G22P1 J04611 152690 GEN-153 Human lupus p70 (Ku) 1762 1729A>T T577S autoantigen protein mRNA, complete cds G22P1 J04611 152690 GEN-153 Human lupus p70 (Ku) 1812 1779T>G S autoantigen protein mRNA, complete cds G22P1 J04611 152690 GEN-153 Human lupus p70 (Ku) 1900 1867G>T 3 autoantigen protein mRNA, complete cds BPI J04739 109195 GEN- Human bactericidal 1525 1495G>A 3 156 permeability increasing protein (BPI) mRNA, complete cds C6 J05064 217050 GEN- Human complement 3281 3126G>A 3 16S component C6 mRNA, complete cds J05480 J05480 114105 GEN-D Calcineurin A 834 834A>G 3 J05594 J05594 601688 GEN-E Prostaglandin 15-OH 173 156A>G S dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 913 896C>G 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 950 933G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1448 1431G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) K00396 K00396 107741 GEN-PO Human apolipoprotein E 112 52G>A A18T (epsilon 2 and 3 alleles) SD-144146.1 Page 9 mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 121 61G>A E21 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 151 91 G>A E31 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 197 137T>C L46P (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 204 144delG (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 238 178A>G T60A (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 365 305C>G P102R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 409 349G>A A117T (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 448 388T>C C130R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 494 434G>A G145D (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 515 455G>A R152Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 520 460C>A R154S (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 538 478C>T R160C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 547 487C>T R163C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 548 488G>A R163H SD-144146.1 Page 93 (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 550 490A>G K164E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 743 683G>A (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 785 725G>A R242Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 796 736C>T R246C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 821 761T>A V254E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 865 805C>G R269G (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 935 875G>A R292H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 1000 940A>C S314R (epsilon 2 and 3 alleles) mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 297 283T>C S chain mRNA K01171 K01171 None GEN-P6 Human HLA-DR alpha- 416 402C>A s chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 665 651C>T s chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 738 724G>T V242L chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 748 734G>A S245N SD-144146.1 Page 93 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 797 783A>G 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 842 828A>G 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 901 887G>A 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 928 914T>A 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 933 919T>A 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 942 9280T 3 chain mRNA K01171 K01171 None GEN-P6 Human HLA-DR alpha- 954 940G>A 3 chain mRNA K01171 K01171 None GEN-P6 Human HLA-DR alpha- 999 985T>G 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 1035 1021A>C 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 1077 1063C>T 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 1091 1077C>G 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 1154 1140A>C 3 chain mRNA K01171 K01171 None GEN-PB Human HLA-DR alpha- 1171 1157T>A 3 chain mRNA KNG K02566 228960 GEN-X2 Human alpha-2-thiol 1248 1199C>A T400K proteinase inhibitor mRNA, complete coding sequence K02765 K02765 120700 GEN-XM Human complement 1001 941T>C L314P component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 2575 2515G>A V839I component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 3108 3048C>T component C3 mRNA, alpha and beta subunits, SD-144146.1 Page 93 complete cds K02765 K02765 120700 GEN-XM Human complement 3561 3501 C>G component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4371 43110T component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4544 4484C>A P1495Q component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4938 4878T>C S component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4956 4896T>C S component C3 mRNA, alpha and beta subunits, complete cds K02770 K02770 147720 GEN-5M Interleukin 1 , beta 19 (-68)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 26 (-61)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 48 (-39)C>T 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 114 28G>A E10K K02770 K02770 147720 GEN-5M Interleukin 1 , beta 119 33G>A M11I L01087 L01087 600448 GEN-CM Protein kinase C-theta 1940 1846C>A S L01087 L01087 600448 GEN-CM Protein kinase C-theta 1943 1849G>A E617K L04270 L04270 600979 GEN-144 Homo sapiens (clone 1478 1310G>T 3 CD18) tumor necrosis factor receptor 2 related protein mRNA, complete cds L05148 L05148 176947 GEN- Human protein tyrosine 1886 1887G>A KYC kinase related mRNA sequence L05597 L05597 None GEN- Serotonin 5-HT receptors 824 600T>C 4EV 5-HT1 F L05597 L05597 None GEN- Serotonin 5-HT receptors 1010 786 Λ 787insA [H262Q;26 4EV 5-HT1 F ATAAAATTC 2 Λ 263insl SD-144146.1 Page 93 AT KFI] EDNRB L06623 131244 GEN- Endothelin Receptor Type 88 (-146)A>G 5 19S 6 EDNRB L06623 131244 GEN- Endothelin Receptor Type 332 99C>T S 19S 6 EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S 6 EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B TGFBR3 L07594 600742 GEN- Human transforming 3966 3618G>C 3 1 EA growth factor-beta type III receptor (TGF-beta) mRNA, complete cds L07861 L07861 176977 GEN-DO Protein kinase C, delta 445 387G>A S L07861 L07861 176977 GEN-DO Protein kinase C, delta 1835 1777G>A V593M CCKBR L08112 118445 GEN- Cholecystokinin (CCKb) 456 456G>A S 1 FL MIF L10612 153620 GEN-1J8 Human glycosylation- 170 96C>G inhibiting factor mRNA, complete cds MIF L10612 153620 GEN-1J8 Human glycosylation- 221 147C>G inhibiting factor mRNA, complete cds MIF L10612 153620 GEN-1J8 Human glycosylation- 227 153C>G inhibiting factor mRNA, complete cds MIF L10612 153620 GEN-1J8 Human glycosylation- 239 165G>A inhibiting factor mRNA, complete cds L10612 153620 GEN-1J8 Human glycosylation- 329 2550A inhibiting factor mRNA, complete cds MIF L10612 153620 GEN-1J8 Human glycosylation- 445 371 C>T inhibiting factor mRNA, complete cds L10717 L10717 186973 GEN- Homo sapiens T cell- 856 (-1168)G>A 1JB specific tyrosine kinase mRNA, complete cds L10717 L10717 186973 GEN- Homo sapiens T cell- 1472 (-552)G>A 1J6 specific tyrosine kinase mRNA, complete cds SD-144146.1 Page 93 L10717 L10717 186973 GEN- Homo sapiens T cell- 4897 2874G>A 3 1JB specific tyrosine kinase mRNA, complete cds L10717 L10717 186973 GEN- Homo sapiens T cell- 5625 3602G>C 3 1JB specific tyrosine kinase mRNA, complete cds L10717 L10717 186973 GEN- Homo sapiens T cell- 5628 3605A>C 3 1JB specific tyrosine kinase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 191 153C>T S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 200 162G>A S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 230 192T>C S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 242 204G>A S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 295 257C>T A86V LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 330 292G>A D98N LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 338 300G>A S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 638 600C>G S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 676 638A>G H213R LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 940 902G>A 3 LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 1011 973T>C 3 LVD sulfotransferase mRNA, SD-144146.1 Page 93 complete cds L11005 L11005 602841 GEN- Human aldehyde oxidase 4284 4154C>A 1JU (hAOX) mRNA, complete cds L11005 L11005 602841 GEN- Human aldehyde oxidase 4447 4317G>C 1JU (hAOX) mRNA, complete cds L11005 L11005 602841 GEN- Human aldehyde oxidase 4525 4395T>G 1JU (hAOX) mRNA, complete cds L11005 L11005 602841 GEN- Human aldehyde oxidase 4675 4545G>A 1JU (hAOX) mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 538 204G>A 1 K2 binding protein beta-chain mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 796 462C>T 1 K2 binding protein beta-chain mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 958 624C>A 1 K2 binding protein beta-chain mRNA, complete cds L11284 L11284 176872 GEN- Homosapiens ERK 1763 1764T>C 1 K8 activator kinase (MEK1 ) mRNA L11284 L11284 176872 GEN- Homosapiens ERK 1914 1915G>A 1 K8 activator kinase (MEK1) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 252 253C>A 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 276 277T>C 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 537 538C>T 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 613 614G>C 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 744 745A>C SD-144146.1 Page 93 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1156 1157G>T 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1311 1312C>T 3 1 K7 activator kinase ( L11285 L11285 601263 GEN- Homosapiens ERK 1457 1458C>A 3 1 K7 activator kinase (MEK2) mRNA L11285 L11285 601263 GEN- Homosapiens ERK 1459 1460A>C 3 1 K7 activator kinase (MEK2) mRNA L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1003 904C>A L302I L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1283 1184A>G 3 L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1479 1380T>A 3 L11667 L11667 601753 GEN-H Cyclophilin D 40kDa 1519 1420T>C 3 L11931 L11931 182144 GEN- Human cytosolic serine 1444 1420OT L474F 4DT hydroxymethyltransferase (SHMT) mRNA, complete cds L11931 L11931 182144 GEN- Human cytosolic serine 1541 1517C>T 3 4DT hydroxymethyltransferase (SHMT) mRNA, complete cds L12052 L12052 171885 GEN- Human cAMP 1707 1707G>A 3 1 LK phosphodiesterase mRNA, 3 end L12691 L12691 125220 GEN-ST Human neutrophil peptide- 244 194A>C D65A 3 gene, complete cds L12691 L12691 125220 GEN-ST Human neutrophil peptide- 433 383T>C 3 3 gene, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1467 1250C>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1868 1651 C>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds SD-144146.1 Page 93 MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1917 1700C>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 2962 2745G>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 4589 4372G>A 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds L14754 L14754 600502 GEN-D9 DNA-binding protein 2129 2080C>T R694W (SM6P2) L14754 L14754 600502 GEN-D9 DNA-binding protein 2365 2316C>T S (SMBP2) L14754 L14754 600502 GEN-D9 DNA-binding protein 3696 36470T 3 (SMBP2) L14754 L14754 600502 GEN-D9 DNA-binding protein 3712 3663T>C 3 (SMBP2) L14754 L14754 600502 GEN-D9 DNA-binding protein 3771 37220G 3 (SM6P2) BF L15702 138470 GEN- Human complement factor 135 95A>G Q32R 1 UA 6 mRNA, complete cds L19067 L19067 164014 GEN-DE TRANSCRIPTION 1129 1091C>T S364L FACTOR P65 L19956 L19956 600641 GEN- Human aryl 243 105A>G S LVE sulfotransferase mRNA, complete cds L19956 L19956 600641 GEN- Human aryl 284 146C>T S49F LVE sulfotransferase mRNA, complete cds L20298 L20298 121360 GEN-DH Transcription Factor 2696 2696A>G 3 (C6F6) L20463 L20463 600445 GEN-M G-protein coupled 1671 1380A>G 3 adenosine A3 receptor L22214 L22214 102775 GEN-2S Adenosine A1 receptor 557 147G>C S (ADORA1 ) L22214 L22214 102775 GEN-2S Adenosine A1 receptor 2622 2212G>A 3 (ADORA1 ) L22473 L22473 600040 GEN- Human 6ax alpha mRNA, 552 552G>A S SD-144146.1 Page 9 L9D complete cds SLC6A3 L24178 126455 GEN-283 Homo sapiens dopamine 1917 1898C>T transporter mRNA, complete cds L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1422 1185T>C 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1490 12530T 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1517 1280A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2244 2007A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2299 2062A>G 3 RECEPTOR 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 41 (-172)G>T 5 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 102 (-111)C>T 5 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 229 17C>T A6V 4EP (MOR1) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 229 17C>T A6V 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 236 24G>A S 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 330 118A>G N40D 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 330 118A>G N40D 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 991 779G>A R260H 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 1005 793C>T R265C 4EP (MOR1 ) mRNA, complete cds SD-144146.1 Page 93 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 1154 942G>A 4EP (MOR1 ) mRNA, complete cds 0PRM1 L25119 600018 GEN- Human Mu opiate receptor 1154 942G>A 4EP (MOR1 ) mRNA, complete cds L25259 L25259 601020 GEN-298 Human CTLA4 counter- 1034 928G>A A310T receptor (B7-2) mRNA, complete cds PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 547 159C>T S (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 611 223G>A V75M (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 1725 1337A>G Q446R (subtype EP2), 53kD L31584 L31584 600242 GEN- Human G protein-coupled 608 545T>G I182S MDW receptor (E61 1 ) gene L31773 L31773 104220 GEN- Adrenergic receptor alpha 171 171C>T S 4DD 1 b L31773 L31773 104220 GEN- Adrenergic receptor alpha 534 534C>T S 4DD 1b L31773 L31773 104220 GEN- Adrenergic receptor alpha 549 549G>A S 4DD 1 b NRAMP1 L32185 600266 GEN-2IY Homo sapiens integral 1399 1323C>T S membrane protein (NRAMPI ) mRNA, complete cds L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5667 5442C>G S Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5669 5444G>C G1815A Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5745 5520C>G D1840E Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5941 5716C>A 3 Type L33798 L33798 114208 GEN-Q Ca Channel alphals L- 5971 5746C>A 3 Type L33798 L33798 1 14208 GEN-Q Ca Channel alphal s L- 5985 5760G>A 3 Type L36719 L36719 602315 GEN- Homo sapiens MAP kinase 1227 890C>A T297N 2NE kinase 3 (MKK3) mRNA, SD-144146.1 Page 94 complete cds L36719 L36719 602315 GEN- Homo sapiens MAP kinase 1271 934A>G K312E 2NE kinase 3 (MKK3) mRNA, complete cds NRAMP2 L37347 600523 GEN- Human integral membrane 1092 1083OT 206 protein (Nramp2) mRNA, partial ALCAM L38608 601662 GEN- Homo sapiens CD6 ligand 1401 1338G>A 2PJ (ALCAM) mRNA, complete cds L38928 L38928 None GEN- Homo sapiens 5,10- 617 604A>G T202A 2PT methenyltetrahydrofolate synthetase mRNA, complete cds L40992 L40992 600211 GEN- Homo sapiens (clone 265 265G>A V89I 2SO PE6P2aA1) core-binding factor, runt domain, alpha subunit 1 (C6FA1) mRNA, 3 end of cds L76191 L76191 601108 GEN- Homo sapiens interleukin-1 902 823G>T A275S 30Q receptor-associated kinase (IRAK) mRNA, complete cds L76191 L76191 601108 GEN- Homo sapiens interleukin-1 1051 972G>A 30Q receptor-associated kinase (IRAK) mRNA, complete cds L76191 L76191 601108 GEN- Homo sapiens interleukin-1 2191 2112C>T S 30Q receptor-associated kinase (IRAK) mRNA, complete cds M10901 M10901 138040 GEN-2W Corticosteroid nuclear 1220 1088A>G N363S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- S receptor b 1893AG>AG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- F receptor b 1893delAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2054 1922A>T D641V receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2372 2240T>G I747S receptor b SD-144146.1 Page 94 M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>C L753F receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>T L753F receptor b M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 2166 2034C>T S M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3353 3221 T>G 3 M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3398 3266T>G 3 M1 1313 M1 1313 103950 GEN-E7 alpha-2-macroglobulin 1573 1530T>A S M11313 M1 1313 103950 GEN-E7 alpha-2-macroglobulin 1799 1756C>T F M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 3041 2998G>A V1000I M11313 M11313 103950 GEN-E7 alpha-2-macroglobulin 4474 4431A>C 3 M12807 M12807 186940 GEN-QG Human T-cell surface 868 793C>T R265W glycoprotein T4 mRNA, complete cds M12824 M12824 186910 GEN-QH Human T-cell 1545 1458C>T 3 differentiation antigen Leu- 2 T8 mRNA, partial cds M12824 12824 186910 GEN-QH Human T-cell 1765 1678C>T 3 differentiation antigen Leu- 2/T8 mRNA, partial cds M12959 M12959 186880 GEN-S CD3 glycoprotein on T 431 295T>G S99A lymphocytes M12959 M12959 186880 GEN-S CD3 glycoprotein on T 1060 924T>C 3 lymphocytes M12959 M12959 186880 GEN-S CD3 glycoprotein on T 1129 993C>A 3 lymphocytes M12959 M12959 186880 GEN-S CD3 glycoprotein on T 1343 1207T>C 3 lymphocytes M12959 M 12959 186880 GEN-S CD3 glycoprotein on T 1345 1209G>C 3 lymphocytes M12959 M12959 186880 GEN-S CD3 glycoprotein on T 1394 1258T>G 3 lymphocytes M12959 M12959 186880 GEN-S CD3 glycoprotein on T 1463 1327G>A 3 lymphocytes C1 NH M13690 106100 GEN- Human plasma protease 1475 1438G>A V480M 1 P6 (C1 ) inhibitor mRNA, complete cds C1 NH M13690 106100 GEN- Human plasma protease 1595 1558C>T 3 1 P6 (C1 ) inhibitor mRNA, complete cds SD-144146.1 Page 9 C1 NH M13690 106100 GEN- Human plasma protease 1714 1677A>C 1 P6 (C1 ) inhibitor mRNA, complete cds BCL2 M13994 151430 GEN- Human B-cell 1744 286G>A A96T 1Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds BCL2 M13994 151430 GEN- Human B-cell 1786 328G>C G110R 1Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds BCL2 M 13994 151430 GEN- Human B-cell 2959 1501A>G 3 1Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds C1 R M14058 216950 GEN- Human complement C1r 1519 14560T R486C 1QJ mRNA, complete cds ARG1 M14502 207800 GEN- Human liver arginase 800 744C>T S I RE mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 2716 2603OT 3 1 S8 receptor mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 2729 2616C>T 3 1S8 receptor mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 2912 2799G>A 3 1S8 receptor mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 3252 3139C>G 3 1S8 receptor mRNA, complete cds M14766 M14766 151445 GEN-QQ Human Fc-epsilon receptor 1338 1153G>A 3 CD23 antigen (IgE receptor) mRNA complete cds M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 466 (-1122)C>G 5 M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 565 (-1023)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1182 (-406)C>T 5 SD-144146.1 Page 94 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1221 (-367)OT 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1326 (-262)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1541 (-47)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1687 100G>A V34M M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1839 252G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2110 523C>A S M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 2640 1053G>C s M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 2826 1239G>A s M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2862 1275C>G 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2864 1277C>A 3 M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 2865 1278C>A 3 M15169 M15169 109690 GEN-T 6eta2 Adrenergic Receptor 3371 1784A>T 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 890 818G>A G273E M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 978 906A>G S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1173 1101 C>A S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1395 1323T>C S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1614 1542C>T S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 1965 1893C>T S M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2505 2433G>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2505 2433G>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2528 24560A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2528 2456C>A 3 M15395 M15395 600065 GEN-U Leukocyte integrin beta-2 2553 2481 G>C 3 DAF M 15799 125240 GEN- Human complement 1160 1160A>C 3 1 UD decay-accelerating factor (DAF) mRNA; 3 end M16405 M16405 None GEN- Muscarinic receptor, 2138 1338C>T S 4ES CHRM4 M16405 M16405 None GEN- Muscarinic receptor, 2409 1609G>A 3 4ES CHRM4 M16541 M16541 177400 GEN-35 6utyrylcholinesterase 422 293A>G D98G SD-144146.1 Page 9 M16541 M16541 177400 GEN-35 eutyryicholinesterase 557 428G>A G143D M16541 M16541 177400 GEN-35 eutyryicholinesterase 564 435- F146V 436TT>AG>A G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 568 439C>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 596 467A>G Y156C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 941 812C>T T271M M16541 M16541 177400 GEN-35 Butyrylcholinesterase 961 832A>C T278P M16541 M16541 177400 GEN-35 Butyrylcholinesterase 978 849G>C E283D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1201 1072T>A L358I M16541 M16541 177400 GEN-35 eutyryicholinesterase 1306 1177G>A G393R M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1382 1253G>T G418V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1549 1420T>G F474V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1564 1435G>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1703 1574A>T E525V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1756 1627C>T R543C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 C86 M16973 120960 GEN- Human complement 1860 1833C>T 3 1ZA protein C8 beta subunit mRNA, complete cds CYP21 17252 201910 GEN-201 Human cytochrome 224 224G>A R75H P450c21 mRNA, 3 end CYP21 M17252 201910 GEN-201 Human cytochrome 330 330C>T S P450c21 mRNA, 3 end CYP21 M 17252 201910 GEN-201 Human cytochrome 745 745T>C 3 P450c21 mRNA, 3 end C8G M17999 120930 GEN- Human complement 193 132T>G S 20Y component C8-gamma mRNA, complete cds M 19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 156 143G>T C48F complete cds M 9045 M19045 153450 GEN-QZ Human lysozyme mRNA, 638 625T>C 3 complete cds M19045 M 19045 153450 GEN-QZ Human lysozyme mRNA, 825 812A>G 3 complete cds SD-144146.1 Page 94 M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 876 863T>C 3 complete cds M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 939 926C>T 3 complete cds M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 973 960T>C 3 complete cds M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 981 968A>G 3 complete cds M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 1018 1005G>A 3 complete cds M19045 M19045 153450 GEN-QZ Human lysozyme mRNA, 1304 1291C>T 3 complete cds M20137 M20137 147740 GEN- Human interleukin 3 (IL-3) 132 79C>T P27S CCJ mRNA, complete cds, clone pcD-SR-alpha M20566 M20566 147880 GEN-3A Interleukin 6A 3058 2621A>T 3 M21054 M21054 172410 GEN-36 Phospholipase A-2 (PLA-2) 331 294G>A S lung M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 400 363C>A D121E lung SCYA5 M21121 187011 GEN- Human T cell-specific 234 208C>T R70C 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 524 498T>C 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 634 608OT 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 666 640OT 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 667 641 G>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 690 664G>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 695 669C>T 24E protein (RANTES) mRNA, complete cds SD-144146.1 Page 94 SCYA5 M21121 187011 GEN- Human T cell-specific 696 670G>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 698 672G>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 702 676C>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 719 693C>T 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 728 702G>A 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 735 709C>T 24E protein (RANTES) mRNA, complete cds SCYA5 M21121 187011 GEN- Human T cell-specific 736 710G>A 24E protein (RANTES) mRNA, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 1052 932C>T A311V 25R N/CD13 mRNA encoding aminopeptidase N, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 2168 2048C>G T683S 25R N/CD13 mRNA encoding aminopeptidase N, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 2375 2255G>A S752N 25R N/CD13 mRNA encoding aminopeptidase N, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 2505 2385C>T 25R N/CD13 mRNA encoding aminopeptidase N, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 3053 2933G>C 25R N/CD13 mRNA encoding aminopeptidase N, complete cds SD-144146.1 Page 94 M22324 M22324 151530 GEN- Human aminopeptidase 3299 3179A>G 25R N/CD13 mRNA encoding aminopeptidase N, complete cds M22324 M22324 151530 GEN- Human aminopeptidase 3405 3285C>T 25R N/CD13 mRNA encoding aminopeptidase N, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 116 (-20)G>T 5 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 231 96G>C S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143- S 25V mRNA, complete cds 144GT>GT PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143-144delGT F 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 643 508C>T 3 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 700 565G>C 3 25V mRNA, complete cds M24283 M24283 147840 GEN-V Intercellular adhesion 238 167A>T K56M molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 238 167A>T K56M molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 792 721 G>A G241 R molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 792 721 G>A G241 R molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1126 1055C>T P352L molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1166 1095C>T S molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1295 1224G>A S molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E SD-144146.1 Page 94 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2043 1972C>T 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2043 1972C>T 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2551 2480C>T 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2681 2610G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2842 2771 G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2842 2771 G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2935 2864T>C 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2938 2867G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2950 2879C>T 3 molecule 1 CD36 M24795 173510 GEN- Human CD36 antigen 79 (-132)C>A 5 28R mRNA, complete cds CD36 M24795 173510 GEN- Human CD36 antigen 341 131T>G L44R 28R mRNA, complete cds CD36 M24795 173510 GEN- Human CD36 antigen 1851 1641A>G 3 28R mRNA, complete cds M24857 M24857 180190 GEN-80 Retinoic acid receptor, 1694 1280C>T S427L gamma 1 SELL M25280 153240 GEN-29J Human lymph node 436 321T>C S homing receptor mRNA, complete cds SELL M25280 153240 GEN-29J Human lymph node 692 577C>T L193F homing receptor mRNA, complete cds SELL M25280 153240 GEN-29J Human lymph node 1378 1263C>T 3 homing receptor mRNA, complete cds SELL M25280 153240 GEN-29J Human lymph node 2157 2042A>C 3 homing receptor mRNA, complete cds SD-144146.1 Page 94 SELL M25280 153240 GEN-29J Human lymph node 2215 2100C>G 3 homing receptor mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 32 (-52)T>C 5 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 67 (-17)G>A 5 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 110 27T>C S 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 153 70T>C S24P 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 203 120G>A S 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 263 180C>T S 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 264 181G>A G61 S 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 285 202C>A S 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 288 205A>G S69G 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 291 208C>G R70G 29M 464) potential SD-144146. Page 95 lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 335 252T>C 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 341 258C>T 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 395 312G>A 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 452 369C>T 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 479 396G>A 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 549 466G>A 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 561 478C>T 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 617 5340G 29M 464) potential lymphokine/cytokine mRNA, complete cds SCYA3 M25315 601395 GEN- Homo sapiens (clone pAT 660 577A>G 29M 464) potential lymphokine/cytokine mRNA, complete cds M25813 M25813 None GEN- Human unidentified gene 1357 1357G>A V453I 2A0 complementary to P450c21 gene, partial cds SD-144146.1 Page 95 M25813 M25813 None GEN- Human unidentified gene 2082 2082C>G I694M 2A0 complementary to P450c21 gene, partial cds M25813 M25813 None GEN- Human unidentified gene 2502 2502G>A 3 2A0 complementary to P450c21 gene, partial cds M25813 M25813 None GEN- Human unidentified gene 2626 2626A>G 3 2A0 complementary to P450c21 gene, partial cds M26383 M26383 146930 GEN-3E Interleukin 8 259 185C>G A62G M26383 M26383 146930 GEN-3E Interleukin 8 1237 1163A>T 3 M26383 M26383 146930 GEN-3E Interleukin 8 1281 1207A>G 3 M27492 M27492 147810 GEN-3F INTERLEUKIN 1 4686 4604T>G 3 RECEPTOR, TYPE I PRECURSOR M28226 M28226 158105 GEN-R8 Human JE gene encoding 90 44C>G A15G a monocyte secretory protein mRNA, complete cds M28226 M28226 158105 GEN-R8 Human JE gene encoding 151 105C>T S a monocyte secretory protein mRNA, complete cds M28226 M28226 158105 GEN-R8 Human JE gene encoding 411 365T>C 3 a monocyte secretory protein mRNA, complete cds POMC M28636 176830 GEN- Adrenocorticotropic 92 92C>T 3 2DG hormone (ACTH) CFTR M28668 602421 GEN- Human cystic fibrosis 2729 2597G>A C866Y 2DF mRNA, encoding a presumed transmembrane conductance regulator (CFTR) CFTR M28668 602421 GEN- Human cystic fibrosis 5826 5694T>C 3 2DF mRNA, encoding a presumed transmembrane conductance regulator (CFTR) CD1 B M28826 188360 GEN- Human thymocyte antigen 886 841 G>A V281 M 2DO CD1 b mRNA, complete SD-144146.1 Page 9 cds M29551 M29551 114106 GEN-F3 SERINE/THREONINE 936 820G>A V274M PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM M29551 M29551 114106 GEN-F3 SERINE/THREONINE 2640 2524G>A PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM M29696 M29696 146661 GEN-3H Interleukin 7 receptor 1088 1066G>A V356I M30640 M30640 131210 GEN-R6 Human endothelial 3506 3366A>G 3 leukocyte adhesion molecule I (ELAM1) mRNA, complete cds M30773 M30773 114106 GEN-X Calcineurin B type I 331 (-428)T>C 5 M30773 M30773 114106 GEN-X Calcineurin 6 type I 1658 900C>A 3 M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 1599 1572A>G S HELICASE II, 86 KD SUBUNIT M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 2549 2522T>C HELICASE II, 86 KD SUBUNIT M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 2953 2926C>A HELICASE II, 86 KD SU6UNIT M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 2953 2926C>A HELICASE II, 86 KD SU6UNIT M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 3037 3010G>A HELICASE II, 86 KD SUBUNIT M30938 M30938 194364 GEN-F5 ATP-DEPENDENT DNA 3067 3040G>A HELICASE II, 86 KD SUBUNIT M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 1321 1291 G>A G431S immunoglobulin enhancer binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 1323 1293C>T immunoglobulin enhancer SD-144146.1 Page 95 binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 1332 1302OA immunoglobulin enhancer binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 1338 1308T>C immunoglobulin enhancer binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 1608 1578C>G S immunoglobulin enhancer binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 4022 3992G>A 3 immunoglobulin enhancer binding factors E12/E47) M31523 M31523 147141 GEN-F7 Transcription factor 3 (E2A 4254 4224T>A 3 immunoglobulin enhancer binding factors E12/E47) M32315 M32315 191191 GEN-3M Tumor necrosis factor 676 587T>G M196R receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 1176 1087G>A A363T receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 1668 1579G>T 3 receptor 2 (75kD) M32315 M32315 191 191 GEN-3M Tumor necrosis factor 2898 2809G>A 3 receptor 2 (75kD) M32315 M32315 191191 GEN-3M Tumor necrosis factor 3671 3582G>A 3 receptor 2 (75kD) VEGF M32977 192240 GEN-2JF Human heparin-binding 50 (-7)OT 5 vascular endothelial growth factor (VEGF) mRNA, complete cds VEGF M32977 192240 GEN-2JF Human heparin-binding 92 36C>T vascular endothelial growth factor (VEGF) mRNA, complete cds M33195 M33195 147139 GEN- Human Fc-epsilon-receptor 446 421T>G 2JR gamma-chain mRNA, complete cds M33195 M33195 147139 GEN- Human Fc-epsilon-receptor 489 464T>C 2JR gamma-chain mRNA, complete cds M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 92 92C>T S31 L SD-144146.1 Page 95 end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 392 392C>G T131 R end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 609 609G>A S end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 707 707G>A C236Y end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 730 730G>A A244T end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 837 837T>G 3 end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 840 840G>T 3 end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 1008 1008T>C 3 end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 1050 1050C>T 3 end M33491 M33491 191080 GEN-RD Human tryptase-l mRNA, 3 1060 1060A>G 3 end M33680 M33680 186845 GEN- Human 26-kDa cell surface 1065 827G>A 3 2K3 protein TAPA-1 mRNA, complete cds M33680 M33680 186845 GEN- Human 26-kDa cell surface 1284 1046T>C 3 2K3 protein TAPA-1 mRNA, complete cds M33680 M33680 186845 GEN- Human 26-kDa cell surface 1412 1174C>T 3 2K3 protein TAPA-1 mRNA, complete cds M33680 M33680 186845 GEN- Human 26-kDa cell surface 1416 1178G>A 3 2K3 protein TAPA-1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 561 516T>C S DQ81 2KB DQB1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 641 596G>A R199H DQB1 2KB DQB1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 648 603C>T S DQ61 2KB DQB1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 695 650T>C I217T SD-144146.1 Page 9 DQB1 2KB DQB1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 771 726G>C DQB1 2KB DQB1 mRNA, complete cds HLA- M33907 142857 GEN- Human MHC class II HLA- 780 735C>T DQ61 2K6 DQ61 mRNA, complete cds M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 449 371A>G protein, FK506-binding protein 1 (12kD) M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 486 408G>A protein, FK506-binding protein 1 (12kD) M34539 M34539 186945 GEN-3N FKBP, tacrolimus binding 650 572T>C protein, FK506-binding protein 1 (12kD) M35011 M3501 1 147561 GEN- Human integrin beta-5 1448 1419C>T 2LV subunit mRNA, complete cds M35011 M3501 1 147561 GEN- Human integrin beta-5 2778 2749A>C 2LV subunit mRNA, complete cds M35011 M35011 147561 GEN- Human integrin beta-5 2904 2875T>C 2LV subunit mRNA, complete cds M35011 M35011 147561 GEN- Human integrin beta-5 3077 3048G>A 3 2LV subunit mRNA, complete cds M35011 M35011 147561 GEN- Human integrin beta-5 3095 3066T>A 3 2LV subunit mRNA, complete cds M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 53 35T>C V12A M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 149 131C>A A44D M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 194 176T>C L59P M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 364 346C>T L116F M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 900 882T>C S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 987 969G>T E323D M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S SD-144146.1 Page 95 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1562 1544G>A R515Q M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2226 2208C>T S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2426 2408G>C 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3056 3038C>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3098 3080A>G 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3403 3385A>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3927 3909C>T 3 LIG1 M36067 126391 GEN- Human DNA ligase I 2526 2406T>C S 2MS mRNA, complete cds M36712 M36712 186730 GEN- Human T lymphocyte 1046 1001 OA 3 2NC surface glycoprotein (CD8- beta) mRNA, complete cds M36712 M36712 186730 GEN- Human T lymphocyte 1281 1236T>C 3 2NC surface glycoprotein (CD8- beta) mRNA, complete cds M36712 M36712 186730 GEN- Human T lymphocyte 1326 12810A 3 2NC surface glycoprotein (CD8- beta) mRNA, complete cds PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 449 297A>G S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 883 731 A>G H244R 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 922 770A>T H257L 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 954 802C>T R268W 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 1301 1149T>C S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 1649 1497T>C S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 2666 2514G>A S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 3245 3093C>T S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 3245 3093C>T S SD-144146 Page 95 201 PLCG2 M37238 600220 GEN- Phosphohpase C gamma-2 3436 3284G>A G1095D 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 4207 4055C>G 3 201 PECAM1 M37780 173445 GEN- Human leukocyte surface 152 27C>G S 20L protein (CD31 ) mRNA, complete cds PECAM1 M37780 173445 GEN- Human leukocyte surface 1577 1452C>T S 20L protein (CD31 ) mRNA, complete cds PECAM1 M37780 173445 GEN- Human leukocyte surface 1813 1688A>G N563S 20L protein (CD31 ) mRNA, complete cds PECAM1 M37780 173445 GEN- Human leukocyte surface 2133 2008G>A G670R 20L protein (CD31 ) mRNA, complete cds PECAM1 M37780 173445 GEN- Human leukocyte surface 2400 2275G>A 3 20L protein (CD31 ) mRNA, complete cds CD9 M38690 143030 GEN- Human CD9 antigen 819 768T>G 3 2PK mRNA, complete cds CD9 M38690 143030 GEN- Human CD9 antigen 826 775T>G 3 2PK mRNA, complete cds CD9 M38690 143030 GEN- Human CD9 antigen 947 896G>A 3 2PK mRNA, complete cds M55040 M55040 100740 GEN-3Q acetylcholinesterase 323 167C>T P56L M55040 M55040 100740 GEN-3Q acetylcholinesterase 1154 998T>A V333E M55040 M55040 100740 GEN-3Q acetylcholinesterase 1213 1057C>A H353N M55040 M55040 100740 GEN-3Q acetylcholinesterase 1482 1326G>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1663 1507T>C F503L CSNK2A1 M55265 115440 GEN- Human casein kinase II 193 45T>C S 35Y alpha subunit mRNA, complete cds CSNK2A1 M55265 115440 GEN- Human casein kinase II 1007 859A>C S287R 35Y alpha subunit mRNA, complete cds CSNK2A1 M55265 115440 GEN- Human casein kinase II 1180 1032G>A S SD-144146. Page 95 35Y alpha subunit mRNA, complete cds CSNK2A1 M55265 115440 GEN- Human casein kinase II 1199 1051A>G M351V 35Y alpha subunit mRNA, complete cds CSNK2A2 M55268 115442 GEN- Human casein kinase II 1532 1369C>A 3 35X alpha subunit mRNA, complete cds M55643 M55643 164011 GEN-RP Human factor KBF1 1936 1755G>A S mRNA, complete cds M57414 M57414 None GEN- Human neurokinin A 68 68T>C I23T 4FK receptor (NK-2R) mRNA, complete cds M57414 M57414 None GEN- Human neurokinin A 951 951 G>A S 4FK receptor (NK-2R) mRNA, complete cds M57414 M57414 None GEN- Human neurokinin A 1171 11710G P391A 4FK receptor (NK-2R) mRNA, complete cds M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 418 214G>T A72S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 423 219G>A S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 612 408OG S ethyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 1 16790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 813 609C>T S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1031 827delC F methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1039 835C>A 3 methyltransferase M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 226 170C>T A57V transducer mRNA, SD-144146- 1 Page 95 complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 570 514A>T transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1109 1053A>G transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1334 1278C>G transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1345 1289T>C transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1374 1318C>T transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1403 1347C>T transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1408 1352T>G transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1415 13590A transducer mRNA, complete cds M58664 M58664 103000 GEN-395 Homo sapiens CD24 signal 1677 1621A>G transducer mRNA, complete cds CD48 M59904 109530 GEN- Human pan-leukocyte 903 886T>G 3AE antigen (CD48) mRNA, complete cds M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 644 639C>A S M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 1892 1887C>A 3 M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 2030 2025G>A 3 M60335 M60335 192225 GEN-3U Vascular cell adhesion 1562 1463A>G H488R molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2178 2079C>T S molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2178 2079OT S molecule 1 SD-144146.1 Page 96 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2196 2097T>C S molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2307 2208A>G S molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2321 2222T>C 3 molecule 1 TCN2 M60396 275350 GEN- Human transcobalamin II 1164 1127C>T S376L SAX (TCII) mRNA, complete cds TCN2 M60396 275350 GEN- Human transcobalamin II 1765 1728T>C 3 SAX (TCII) mRNA, complete cds FPR1 M60626 136537 GEN- Human N-formylpeptide 1082 1037C>A A346E 3B5 receptor (fMLP-R98) mRNA, complete cds FPR1 M60626 136537 GEN- Human N-formylpeptide 1164 1119G>C 3 365 receptor (fMLP-R98) mRNA, complete cds M60857 M60857 123841 GEN-10 Cyclophilin B 183 171C>T S M60857 M60857 123841 GEN-10 Cyclophilin B 217 205G>T V69L M60857 M60857 123841 GEN-10 Cyclophilin B 702 690C>T 3 M60857 M60857 123841 GEN-10 Cyclophilin B 804 792A>C 3 CD53 M60871 151525 GEN- Human cell surface antigen 645 572G>A C191Y 36A (CD53) mRNA, complete cds M61764 M61764 191135 GEN-FO Tubulin, gamma 693 669A>G S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 723 699T>C S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 849 825T>G S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 858 834G>A S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1033 1009T>C S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1053 1029C>G S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1131 1107G>A S polypeptide M61764 M61764 191135 GEN-FO Tubulin, gamma 1188 1164C>T S polypeptide SD-144146.1 Page 96 M64592 M64592 120420 GEN-3X Granulocyte colony- 271 271T>G Y91 D stimulating factor M64592 M64592 120420 GEN-3X Granulocyte colony- 1533 1533C>T S stimulating factor M64799 M64799 None GEN- Histamine receptor H2 398 398T>C V133A 4DN M64799 M64799 None M64799 M64799 None GEN- Histamine receptor H2 620 620A>G K207R 4DN M64799 M64799 None GEN- Histamine receptor H2 649 649A>G N217D 4DN M64799 M64799 None GEN- Histamine receptor H2 692 692A>G K231 R 4DN M64799 M64799 None GEN- Histamine receptor H2 802 802G>A V268M 4DN C5 M65134 120900 GEN- Human complement 1171 1171A>G 1391V 3FT component C5 mRNA, 3end EDN2 M65199 131241 GEN- Endothelin 2 384 314C>T A105V CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1500 1353T>A S M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1512 1365G>A F M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1566 1419G>A S M68892 M68892 147559 GEN-15 Leukocyte integrin beta-7 1327 11760T S M69043 M69043 164008 GEN-3IZ Homo sapiens MAD-3 400 306T>C S mRNA encoding IkB-like activity, complete cds M69043 M69043 164008 GEN-3IZ Homo sapiens MAD-3 1050 956T>C mRNA encoding IkB-like activity, complete cds M69043 M69043 164008 GEN-3IZ Homo sapiens MAD-3 1119 1025G>A mRNA encoding IkB-like activity, complete cds M69043 M69043 164008 GEN-3IZ Homo sapiens MAD-3 1174 1080A>G mRNA encoding IkB-like activity, complete cds SD-144146.1 Page 96 M69226 M69226 309850 GEN-3Z Monoamine oxidase A 435 385A>C S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 936 886C>T F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G s M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1076 1026A>T s M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1373 1323G>A F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T s M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1609 1559A>G K520R M71246 M71246 None GEN- Interferon alpha 17 131 131A>C H44P 3KO M71246 M71246 None GEN- Interferon alpha 17 483 483C>T S 3KO M71246 M71246 None GEN- Interferon alpha 17 512 512G>T R171I 3KO M73700 M73700 150210 GEN-S6 Human neutrophil 2673 85G>A A29T lactoferrin mRNA, complete cds and 5 promoter region M73700 M73700 150210 GEN-S6 Human neutrophil 3090 502G>A V168M lactoferrin mRNA, complete cds and 5 promoter region M73700 M73700 150210 GEN-S6 Human neutrophil 4101 1513G>A D505N lactoferrin mRNA, complete cds and 5 promoter region M73700 M73700 150210 GEN-S6 Human neutrophil 4211 1623T>C S lactoferrin mRNA, complete cds and 5 promoter region M73700 M73700 150210 GEN-S6 Human neutrophil 4325 1737G>C E579D lactoferrin mRNA, complete cds and 5 promoter region M73700 M73700 150210 GEN-S6 Human neutrophil 4482 1894C>T S lactoferrin mRNA, complete cds and 5 promoter region M74782 M74782 308385 GEN-64 Interleukin 3 receptor.alpha 1396 1250C>T 3 SD-144146.1 Page 96 (low affininty) CD79B M80461 147245 GEN- Human B29 rnRNA, 795 781 C>T 3 3UT complete cds CD79B M80461 147245 GEN- Human B29 mRNA, 804 790C>A 3 3UT complete cds CD79B M80461 147245 GEN- Human B29 mRNA, 1033 1019C>T 3 3UT complete cds M80462 M80462 112205 GEN- Human MB-1 mRNA, 241 205G>A V69I 3US complete cds M80646 M80646 274180 GEN-40 Thromboxane synthase 756 585G>C S M80646 M80646 274180 GEN-40 Thromboxane synthase 1240 1069C>G L357V CD34 M81104 142230 GEN- Human CD34 mRNA, 1338 1045A>G K349E 3VN complete cds CD34 M81104 142230 GEN- Human CD34 mRNA, 2490 2197G>A 3 3VN complete cds M81590 M81590 182131 GEN- Serotonin 5-HT receptors 190 129C>T S 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 432 371T>G F124C 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 922 861 G>C S 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 1241 1180G>A 3 3VZ 5-HT1 D M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 1834 1770G>C S M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 3282 3218C>T T1073M M81695 M81695 151510 GEN-17 Leukocyte integrin alpha-x 4213 4149C>G 3 TAC1 R M81797 162323 GEN- Tachylinins NK1 receptor 696 652G>A V218I 3W8 TAC1R M81797 162323 GEN- Tachylinins NK1 receptor 1397 1353G>C 3 3W8 M83566 M83566 114206 GEN- Human 1222 1104C>T S 3Y7 neuroendocrine/beta-cell- type calcium channel alpha-1 subunit mRNA, complete cds M83566 M83566 114206 GEN- Human 1468 1350G>A S 3Y7 neuroendocrine/beta-cell- type calcium channel alpha-1 subunit mRNA, complete cds SD-144146.1 Page 96 CHRNA5 M83712 118505 GEN- Nicotinic, Cholinergic 1340 1192G>A D398N 3YQ receptor alpha 5 M84379 M84379 142800 GEN-SA Human MHC class I 28 28G>C V10L lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 98 98T>A F33Y lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 102 102A>C lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 144 144A>C lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 240 240T>G lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 257 257G>A G86E lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 292 292C>G H98D lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 362 362G>T R121 M lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 391 391T>G W131G lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 418 418T>G Y140D lymphocyte antigen (HLA- A 0201 ) mRNA, complete SD-144146.1 Page 96 cds M84379 M84379 142800 GEN-SA Human MHC class I 453 453A>C K151 N lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 527 527T>A V176E lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 539 539T>G L180W lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 622 622G>C A208P lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 630 630A>G lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 666 666A>G lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 762 762C>T lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 789 789A>G lymphocyte antigen (HLA- A 0201) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 806 806C>T A269V lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 807 807G>A lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds SD-144146 1 Page 96 M84379 M84379 142800 GEN-SA Human MHC class I 808 808G>T A270S lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 819 819G>A lymphocyte antigen (HLA- A 0201 ) mRNA, comp M84379 M84379 142800 GEN-SA Human MHC class I 829 829C>G Q277E lymphocyte antigen (HLA- A 0201) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 868 868T>C lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 870 870G>C L290F lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 900 900G>A lymphocyte antigen (HLA- A 0201) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 901 901T>G S301A lymphocyte antigen (HLA- A 0201) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 916 916A>G I306V lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 945 945G>A lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 952 952T>C F318L lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 967 967A>G T323A SD-144146.1 Page 96 lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 987 987T>C lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 992 992T>G M331 R lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 1005 1005G>C K335N lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 1013 1013A>G D338G lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 1029 1029C>T lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 1033 1033T>A S345T lymphocyte antigen (HLA- A 0201 ) mRNA, complete cds M84379 M84379 142800 GEN-SA Human MHC class I 1072 1072G>A V358M lymphocyte antigen (HLA- A 0201) mRNA, complete cds M84526 M84526 134350 GEN- Human 46 (-9)C>T 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 399 345C>A 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 408 354A>G 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 859 805C>T SD-144146.1 Page 96 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 891 837G>C 3 3ZL adipsin/complement factor D mRNA, complete cds M84747 M84747 300007 GEN-45 Interleukin 9 receptor 1273 1094G>A R365H TGFBR2 M85079 190182 GEN- Human TGF-beta type II 2045 1710A>C 3 3ZS receptor mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 1653 1569T>A 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2599 2515C>G 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2619 2535A>C 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2656 2572A>C 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2745 2661C>T 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2761 2677A>C 40Y mRNA, complete cds M86511 M86511 158120 GEN-419 Human monocyte antigen 1142 1067C>A T356N CD14 (CD14) mRNA, complete cds M86511 M86511 158120 GEN-419 Human monocyte antigen 1176 1101G>C CD14 (CD14) mRNA, complete cds M87503 M87503 None GEN-443 Human IFN-responsive 1424 1390T>A transcription factor subunit mRNA, complete cds M87503 M87503 None GEN-443 Human IFN-responsive 1524 1490A>C transcription factor subunit mRNA, complete cds M89473 M89473 None GEN- NEUROMEDIN K 1614 1471T>C 4FU RECEPTOR M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2159 2062G>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094ATATTA >ATATTA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094delATAT SD-144146.1 Page 96 TA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2230 2133A>G 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2339 2242T>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2409 2312G>A 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2726 2629C>T 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2983 2886C>T 3 M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 3846 3846C>T S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 5505 5505G>A S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6582 6582A>G S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6613 6613G>C G2205R splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6614 6614G>C G2205A splice) L-Type M92303 M92303 114207 GEN-1 C L-Type voltage sensitive 860 711G>A S channel beta-1 IL8RB M94582 146928 GEN- Interleukin 8 receptor 838 786T>C S 49G IL8RB M94582 146928 GEN- Interleukin 8 receptor 1262 1210C>T 3 49G 1L8R6 M94582 146928 GEN- Interleukin 8 receptor 1494 1442A>G 3 49G M95678 M95678 604114 GEN- Homo sapiens 1346 1182T>C S 4A6 phospholipase C-beta-2 mRNA, complete cds M95678 M95678 604114 GEN- Homo sapiens 3436 3272A>G E1091G 4A6 phospholipase C-beta-2 mRNA, complete cds M95678 M95678 604114 GEN- Homo sapiens 4137 3973C>T 3 4A6 phospholipase C-beta-2 mRNA, complete cds M95708 M95708 107271 GEN-SF Homo sapiens Ly-6-like 497 435C>T 3 protein (CD59) mRNA, complete cds M96652 M96652 147851 GEN-65 Interleukin 5 receptor alpha 883 634T>G S212A M96954 M96954 603413 GEN- Homo sapiens nucleolysin 957 912A>C Q304H 465 TIAR mRNA, complete cds ID2 M97796 600386 GEN- Human helix-loop-helix 402 294C>G S SD-144146.1 Page 9 4C0 protein (ld-2) mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 802 732C>T S 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1747 1677G>T 3 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1900 1830T>C 3 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1912 1842G>A 3 4C3 folylpolyglutamate synthetase mRNA, complete cds M98045 M98045 136510 GEN- Homo sapiens 1995 1925C>G 3 4C3 folylpolyglutamate synthetase mRNA, complete cds S46622 S46622 114107 GEN-1 F Calcineurin A-gamma 1893 1607C>G 3 S46622 S46622 114107 GEN-1 F Calcineurin A-gamma 1941 1655A>G 3 S57235 S57235 153634 GEN- CD68=110kda 775 760A>C K254Q 37N transmembrane glycoprotein [human, promonocyte cell line U937, mRNA, 1722 nt] U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3377 3316A>C 3 U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3524 3463A>G 3 U02882 U02882 600129 GEN-XU Human rolipram-sensitive 1798 1690T>C C564R 3,5-cyclic AMP phosphodiesterase mRNA, complete cds U02882 U02882 600129 GEN-XU Human rolipram-sensitive 1881 1773G>A S 3,5-cyclic AMP SD-144146.1 Page 9 phosphodiesterase mRNA, complete cds U02882 U02882 600129 GEN-XU Human rolipram-sensitive 4691 4583T>G 3 3,5-cyclic AMP phosphodiesterase mRNA, complete cds U03858 U03858 600007 GEN- Fms-related tyrosine 683 600C>T S MDM kinase 3 ligand U03858 U03858 600007 GEN- Fms-related tyrosine 1016 933T>C 3 MDM kinase 3 ligand U03882 U03882 601267 GEN- Human monocyte 1436 1397G>A 3 12B chemoattractant protein 1 receptor (MCP-1RA) alternatively spliced mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 38 15C>T S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 282 259A>T S87C dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 350 327C>T S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 365 342T>C S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 464 441 G>A S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 474 451A>G M151V dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 532 509A>G H170R dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 538 515T>A L172Q dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 689 666T>C S dehydrogenase mRNA, SD-144146.1 Page 97 complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 806 783G>A S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 872 849G>T S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 952 929T>G 131 OS dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1020 997G>A 3 dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1035 1012G>A 3 dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1112 1089C>T 3 dehydrogenase mRNA, complete cds U05875 U05875 147569 GEN-18J Human clone pSK1 2047 1399C>G 3 interferon gamma receptor accessory factor- 1 (AF-1) mRNA, complete cds U05875 U05875 147569 GEN-18J Human clone pSK1 2087 1439T>C 3 interferon gamma receptor accessory factor- 1 (AF-1) mRNA, complete cds XDH U06117 278300 GEN-194 Human xanthine 3951 3888C>G S dehydrogenase (XDH) mRNA, complete cds U07225 U07225 600041 GEN- P2Y2 purinoceptor 2008 1763G>A 3 1 DM U07989 U07989 None GEN-Q2 Human Burkitts lymphoma 39 39T>A S immunoglobulin kappa light chain mRNA, partial cds U07989 U07989 None GEN-Q2 Human Burkitts lymphoma 307 307G>C V103L immunoglobulin kappa light chain mRNA, partial cds U07989 U07989 None GEN-Q2 Human Burkitts lymphoma 312 312A>G S immunoglobulin kappa light chain mRNA, partial cds SD-144146, 1 Page 9 U07989 U07989 None GEN-Q2 Human Burkitts lymphoma 568 568G>C V190L immunoglobulin kappa light chain mRNA, partial cds U07989 U07989 None GEN-Q2 Human Burkitts lymphoma 610 610G>A V204I immunoglobulin kappa light chain mRNA, partial cds U08015 U08015 600489 GEN- Human NF-ATc mRNA, 530 291C>T S 1 FD complete cds U08015 U08015 600489 GEN- Human NF-ATc mRNA, 1094 855G>A S 1 FD complete cds U08015 U08015 600489 GEN- Human NF-ATc mRNA, 2222 1983G>A S 1 FD complete cds U08015 U08015 600489 GEN- Human NF-ATc mRNA, 2225 1986A>G S 1 FD complete cds U08015 U08015 600489 GEN- Human NF-ATc mRNA, 2295 2056A>C S686R 1 FD complete cds U09117 U09117 602142 GEN- Phospholipase C delta- 1 333 239G>A R80H 1 GC U09117 U09117 602142 GEN- Phospholipase C delta-1 460 366G>A S 1 GC U09117 U09117 602142 GEN- Phospholipase C delta- 1 1858 1764G>A S 1 GC SLC18A3 U09210 600336 GEN- Human vesicular 838 396T>C S 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 1369 927A>G S 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 1567 1125C>G S 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2080 1638G>T 3 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2199 1757G>A 3 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2349 1907G>T 3 4F3 acetylcholine transporter mRNA, complete cds U09607 U09607 600173 GEN- Janus kinase 3 (a protein 1925 1830G>A M610I SD-144146.1 Page 97 MKU tyrosine kinase, leukocyte) U09759 U09759 602896 GEN- Human protein kinase 303 152A>G N51S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1079 928A>G 1310V 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1280 1129C>T P377S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1559 1408C>T 1 HA (JNK2) mRNA, complete cds U09806 U09806 None GEN- Human 120 120T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 473 473G>A R158Q 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 550 550C>T 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 668 668C>T A223V 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1059 1059T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1289 1289C>A E430A 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1308 1308T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial cds SD-144146.1 Page 97 0PRD1 U10504 165195 GEN- Human delta opiate 921 921T>C S 4F5 receptor mRNA, complete cds U11276 U11276 602890 GEN- Human hNKR-P1 a protein 563 503T>C I168T IKS (NKR-P1A) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 536 460G>A A154T 1LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 795 719A>G Y240C 1LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1085 1009T>C 3 1LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1336 1260C>T 3 1LY methyltransferase (TPMT) mRNA, complete cds TPMT U12387 187680 GEN- Human thiopurine 1373 1297G>A 3 1LY methyltransferase (TPMT) mRNA, complete cds U 12507 U12507 600681 GEN- Cardiac inward rectifier 338 13C>A S 1MD potassium channel (HH- IRK1) U12507 U12507 600681 GEN- Cardiac inward rectifier 1597 1272G>A S 1MD potassium channel (HH- IRK1) U12597 U12597 601895 GEN-4E tumor necrosis factor type 2182 2128G>T 3 2 receptor associated protein (TRAP3) U13737 U13737 600636 GEN- Human cysteine protease 2356 2132A>C 3 1PC CPP32 isoform alpha mRNA, complete cds U13737 U13737 600636 GEN- Human cysteine protease 2535 2311 C>T 3 1PC CPP32 isoform alpha mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2128 2104A>C M702L 1RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2516 2492T>G L831W 1RD NFATx mRNA, complete SD-144146.1 Page 97 cds U14510 U14510 602698 GEN- Human transcription factor 2720 2696C>G A899G 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2792 2768C>T A923V 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2828 2804C>G A935G 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2903 2879C>G A960G 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 2967 2943G>A S 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 3333 3309G>A 3 1 RD NFATx mRNA, complete cds U14510 U14510 602698 GEN- Human transcription factor 3577 3553G>A 3 1 RD NFATx mRNA, complete cds U14650 U14650 602243 GEN- Human platelet-endothelial 638 579A>G S 1 RL tetraspan antigen 3 mRNA, complete cds U14650 U14650 602243 GEN- Human platelet-endothelial 1048 989G>A 3 1 RL tetraspan antigen 3 mRNA, complete cds U14650 U14650 602243 GEN- Human platelet-endothelial 1171 1112T>C 3 1 RL tetraspan antigen 3 mRNA, complete cds U 14650 U 14650 602243 GEN- Human platelet-endothelial 1263 1204G>C 3 1 RL tetraspan antigen 3 mRNA, complete cds U 14650 U 14650 602243 GEN- Human platelet-endothelial 1301 1242C>T 3 1 RL tetraspan antigen 3 mRNA, complete cds U14650 U14650 602243 GEN- Human platelet-endothelial 1351 1292T>C 3 1 RL tetraspan antigen 3 mRNA, complete cds U14650 U14650 602243 GEN- Human platelet-endothelial 1389 1330A>T 3 SD-144146.1 Page 97 1 RL tetraspan antigen 3 mRNA, complete cds U 14650 U 14650 602243 GEN- Human platelet-endothelial 1404 1345G>A 1 RL tetraspan antigen 3 mRNA, complete cds U15637 U15637 601896 GEN- Human CD40 binding 596 386T>C M129T 1 U8 protein (CD40bp) mRNA, complete cds U15637 U15637 601896 GEN- Human CD40 binding 1317 1107C>T S 1 U8 protein (CD40bp) mRNA, complete cds U16031 U16031 None GEN-HX Transcription Factor IL-4 2964 2799G>A 3 Stat SDF1 U16752 600835 GEN- Human cytokine SDF-1- 47 (-34)C>T 5 1YK beta mRNA, complete cds SDF1 U16752 600835 GEN- Human cytokine SDF-1- 2927 2847G>C 3 1YK beta mRNA, complete cds SDF1 U 16752 600835 GEN- Human cytokine SDF-1 - 3159 3079T>C 3 1YK beta mRNA, complete cds SDF1 U16752 600835 GEN- Human cytokine SDF-1- 3294 3214T>G 3 1YK beta mRNA, complete cds NOS1 U17327 163731 GEN-209 Human neuronal nitric 3391 2706C>T S oxide synthase (NOS1 ) mRNA, complete cds PDE4A U18087 600126 GEN-214 Human 3,5-cyclic AMP 642 633T>G S phosphodiesterase HPDE4A6 mRNA, complete cds PDE4A U18087 600126 GEN-214 Human 3,5-cyclic AMP 804 795T>C S phosphodiesterase HPDE4A6 mRNA, complete cds PDE4A U18087 600126 GEN-214 Human 3,5-cyclic AMP 1616 1607A>C E536A phosphodiesterase HPDE4A6 mRNA, complete cds U18242 U 18242 601118 GEN-1 N Cyclophilin Ligand (calcium 1117 1081T>G 3 modulating) U 19487 U 19487 176804 GEN-4I PROSTAGLANDIN E2 85 (-72)A>G 5 RECEPTOR, EP2 SU6TYPE SD-144146.1 Page 97 U19487 U19487 176804 GEN-4I PROSTAGLANDIN E2 231 75A>T S RECEPTOR, EP2 SUBTYPE U 19720 U 19720 600424 GEN-11 Folate Transporter 53 (-43)T>C 5 (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1) U19720 U 19720 600424 GEN-11 Folate Transporter 175 80G>A R27H (SLC19A1 ) U 19720 U19720 600424 GEN-11 Folate Transporter 341 246C>G S (SLC19A1) U19720 U19720 600424 GEN-11 Folate Transporter 791 696C>T S (SLC19A1 ) U 19720 U19720 600424 GEN-11 Folate Transporter 1067 972G>A S (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 2100 2005 Λ 2006ins F (SLC19A1 ) G U 19720 U 19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 (SLC19A1) U 19720 U 19720 600424 GEN-11 Folate Transporter 2582 2487T>G 3 (SLC19A1 ) U 19720 U 19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1 ) U19720 U19720 600424 GEN-11 Folate Transporter 2617 2522C>T 3 (SLC19A1 ) U 19720 U 19720 600424 GEN-11 Folate Transporter 2652 2557T>C 3 (SLC19A1 ) U 19775 U19775 600289 GEN- Human MAP kinase Mxi2 731 688G>A D230N 22C (MXI2) mRNA, complete cds U20157 U20157 601690 GEN-234 Human platelet-activating 1297 1136T>C V379A factor acetylhydrolase mRNA, complete cds U20350 U20350 602237 GEN-239 Human G protein-coupled 1304 1217T>C 3 receptor V28 mRNA, complete cds U20536 U20536 601532 GEN- Human cysteine protease 982 904C>T 3 23K Mch2 isoform alpha (Mch2) mRNA, complete cds U20536 U20536 601532 GEN- Human cysteine protease 1117 1039G>A 3 23K Mch2 isoform alpha (Mch2) SD-144146.1 Page 97 mRNA, complete cds U20536 U20536 601532 GEN- Human cysteine protease 1322 1244T>C 3 23K Mch2 isoform alpha (Mch2) mRNA, complete cds U20536 U20536 601532 GEN- Human cysteine protease 1363 1285T>C 3 23K Mch2 isoform alpha (Mch2) mRNA, complete cds U21847 U21847 601878 GEN-252 Human TGF-beta inducible 986 900C>T S early protein (TIEG) mRNA, complete cds U21847 U21847 601878 GEN-252 Human TGF-beta inducible 1670 1584C>T 3 early protein (TIEG) mRNA, complete cds U21847 U21847 601878 GEN-252 Human TGF-beta inducible 2542 2456A>C 3 early protein (TIEG) mRNA, complete cds U23143 U23143 138450 GEN- Human mitochondrial 506 506T>G F169C MIY serine hydroxymethyltransferase gene, nuclear encoded mitochondrion protein, complete cds U25029 U25029 138040 GEN-82 Glucocorticoid receptor 335 335C>T 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 386 386T>C 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 1069 1069C>T 3 alpha U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1) 476 442T>C F148L 26X mRNA, complete cds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 481 447A>G S 26X mRNA, complete cds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 542 508C>G L170V 2BX mRNA, complete cds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 578 544C>T 3 2BX mRNA, complete cds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 614 580T>C 3 26X mRNA, complete cds U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1 ) 616 582G>A 3 2BX mRNA, complete cds CSNK1 D U29171 600864 GEN- Human casein kinase I 1612 1435C>A 3 SD-144146.1 Page 98 2E2 delta mRNA, complete cds U31628 U31628 601070 GEN-4J Interleukin 15 receptor 1250 1168G>T 3 alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1266 1205C>A P402Q alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1513 1452C>T 3 alpha chain U32989 U32989 191070 GEN- Human tryptophan 991 927G>A S 2JH oxygenase (TDO) mRNA, complete cds U33017 U33017 603492 GEN- Human signaling 1489 1356A>T 3 2JO lymphocytic activation molecule (SLAM) mRNA, complete cds U33017 U33017 603492 GEN- Human signaling 1661 15280T 3 2JO lymphocytic activation molecule (SLAM) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 736 693G>A S 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1285 1242T>C 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1294 1251T>C 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1580 1537A>T 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1621 1578G>T 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1715 1672G>A 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1764 1721 G>A 3 20C alpha (Mch3) mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 912 825C>T S 20G apoptosis inducing ligand SD-144146.1 Page 98 TRAIL mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 1140 1053A>G 3 2QG apoptosis inducing ligand TRAIL mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 1289 1202OA 3 20G apoptosis inducing ligand TRAIL mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 1525 1438G>A 3 20G apoptosis inducing ligand TRAIL mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 1588 1501 G>A 3 20G apoptosis inducing ligand TRAIL mRNA, complete cds U37518 U37518 None GEN- Human TNF-related 1595 1508C>T 3 20G apoptosis inducing ligand TRAIL mRNA, complete cds TAC2 U37529 162320 GEN- Substance P beta-PPT-A 644 499G>A 3 20H TAC2 U37529 162320 GEN- Substance P beta-PPT-A 694 549T>C 3 20H TAC2 U37529 162320 GEN- Substance P beta-PPT-A 799 654A>G 3 20H TAC2 U37529 162320 GEN- Substance P beta-PPT-A 826 681 C>T 3 20H U39656 U39656 601254 GEN- Human MAP kinase kinase 431 91A>C S 2Q8 6 (MKK6) mRNA, complete cds U39656 U39656 601254 GEN- Human MAP kinase kinase 713 373G>A V125M 2Q8 6 (MKK6) mRNA, complete cds U40038 U40038 600998 GEN-70 Guanine nucleotide binding 825 783C>T S protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 878 836T>C L279P protein (G protein), q SD-144146.1 Page 98 polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1029 987G>A S protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1051 1009A>G I337V protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1068 1026T>A S protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1093 1051T>C S protein (G protein), q polypeptide U40282 U40282 602366 GEN- Homo sapiens integrin- 453 297C>T S 2RJ linked kinase (ILK) mRNA, complete cds U40282 U40282 602366 GEN- Homo sapiens integrin- 975 819G>A S 2RJ linked kinase (ILK) mRNA, complete cds U40282 U40282 602366 GEN- Homo sapiens integrin- 1580 1424G>A 3 2RJ linked kinase (ILK) mRNA, complete cds U40282 U40282 602366 GEN- Homo sapiens integrin- 1670 1514G>C 3 2RJ linked kinase (ILK) mRNA, complete cds U40282 U40282 602366 GEN- Homo sapiens integrin- 1769 1613A>C 3 2RJ linked kinase (ILK) mRNA, complete cds U40347 U40347 600950 GEN- Human serotonin N- 382 148G>A E50K 2RK acetyltransferase mRNA, complete cds U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 661 654T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 697 690A>G S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 940 933G>A S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1276 1269T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1790 1783A>T 3 receptor alpha 7 SD-144146 1 Page 98 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1792 1785T>A 3 receptor alpha 7 U43030 U43030 600435 GEN-LFI Human cardiotrophin-1 1404 1372C>T 3 (CTF1 ) mRNA, complete cds U43142 U43142 601528 GEN- Human vascular 1499 1128C>T S 2UM endothelial growth factor related protein VRP mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 446 253A>G T85A 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 519 326A>G K109R 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 861 668A>G Q223R 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 1222 1029T>C S 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2161 1968G>C K656N 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2174 1981A>C T661P 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2764 2571T>G S 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3151 2958C>T S 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3250 3057G>A S 2UN r) mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1424 1228A>G 3 mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1604 1408C>G 3 mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1719 1523G>A 3 mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1827 1631G>A 3 mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 2286 2090G>A 3 mRNA, complete cds SCYA11 U46573 601156 GEN- Human eotaxin precursor 120 67G>A A23T 2WZ mRNA, complete cds SCYA11 U46573 601156 GEN- Human eotaxin precursor 554 501T>C 3 2WZ mRNA, complete cds SD-144146.1 Page 98 U47634 U47634 None GEN- Human beta-tubulin class 1005 1005C>T S 2XR III isotype (beta-3) mRNA, complete cds U47634 U47634 None GEN- Human beta-tubulin class 1035 1035C>T S 2XR III isotype (beta-3) mRNA, complete cds U47634 U47634 None GEN- Human beta-tubulin class 1431 1431T>C 3 2XR III isotype (beta-3) mRNA, complete cds U47634 U47634 None GEN- Human beta-tubulin class 1502 1502G>A 3 2XR III isotype (beta-3) mRNA, complete cds U49516 U49516 312861 GEN-1Q Serotonin 5-HT receptors 2915 2187A>C 3 5-HT2C U49516 U49516 312861 GEN-1Q Serotonin 5-HT receptors 2947 2219A>G 3 5-HT2C U50040 U50040 601582 GEN- Human signaling inositol 196 180A>G S 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 418 402OG 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 2613 2597C>A P866H 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 2638 2622G>A 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 2882 2866C>T H956Y 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 3193 3177C>T 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 3222 3206C>T SD- 144146.1 Page 98 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds U50040 U50040 601582 GEN- Human signaling inositol 3863 3847G>A 2ZR polyphosphate 5 phosphatase SIP-110 mRNA, complete cds IRF4 U52682 601900 GEN- Human lymphocyte specific 4296 4297G>A 33X interferon regulatory factor/interferon regulatory factor 4 (LSI RF/IRF4) mRNA, complete cds IRF4 U52682 601900 GEN- Human lymphocyte specific 4680 4681T>G 33X interferon regulatory factor/interferon regulatory factor 4 (LSIRF/IRF4) mRNA, complete cds IRF4 U52682 601900 GEN- Human lymphocyte specific 4732 4733T>G 33X interferon regulatory factor/interferon regulatory factor 4 (LSIRF/IRF4) mRNA, complete cds IRF4 U52682 601900 GEN- Human lymphocyte specific 4942 4943A>G 33X interferon regulatory factor/interferon regulatory factor 4 (LSI RF/IRF4) mRNA, complete cds IRF4 U52682 601900 GEN- Human lymphocyte specific 5079 5080T>C 33X interferon regulatory factor/interferon regulatory factor 4 (LSIRF/IRF4) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 75 16T>C C6R 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 150 91 G>A A31T 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 511 452C>T T151 I SD-144146.1 Page 98 35Z gamma-glutamyl hydrolase (hGH) mRNA, complete cds U55206 U55206 None GEN- Homo sapiens human 1161 1102A>G 3 35Z gamma-glutamyl hydrolase (hGH) mRNA complete cds U56390 U56390 602234 G complete cds U58196 U58196 147685 GEN-67 INTERLEUKIN 2711 2514A>G 3 ENHANCER-BINDING FACTOR U59863 U59863 None GEN- Human TRAF-interacting 367 209A>G D70G 3A7 protein l-TRAF mRNA, complete cds U59863 U59863 None GEN- Human TRAF-interacting 1863 1705A>T 3 3A7 protein l-TRAF mRNA, complete cds U59863 U59863 None GEN- Human TRAF-interacting 2046 1888G>A 3 3A7 protein l-TRAF mRNA, complete cds U60519 U60519 601762 GEN- Human apoptotic cysteine 304 157G>A E53K 3AZ protease Mch4 (Mch4) mRNA, complete cds U60519 U60519 601762 GEN- Human apoptotic cysteine 324 177A>G S 3AZ protease Mch4 (Mch4) mRNA, complete cds U60800 U60800 None GEN- Human semaphoπn 779 692T>G V231G SBC (CD100) mRNA, complete cds U61849 U61849 602367 GEN- Human neuronal pentraxin 4963 4825T>C 3 SCO 1 (NPTXI ) mRNA, complete cds CHRNA2 U62431 118502 GEN- Nicotinic Cholinergic 2296 17420G 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2387 1833C>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2504 1950G>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2538 1984G>A 3 SD-144146 1 Page 98 4EN receptor alpha 2 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 1 18504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1440 1209T>G S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1440 1209T>G S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1458 1227C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1584 1353G>A S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1781 1550OT S517L receptor alpha 4 U62433 U62433 1 18504 GEN-4P Nicotinic, Cholinergic 1860 1629C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1860 1629C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1890 1659G>A S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1890 1659G>A S receptor alpha 4 U70321 U70321 None GEN- Human herpesvirus entry 343 50G>A R17K 3K9 mediator mRNA, complete cds U70321 U70321 None GEN- Human herpesvirus entry 1014 721 G>A V241 I 3K9 mediator mRNA, complete cds U70321 U70321 None GEN- Human herpesvirus entry 1218 925A>G 3 3K9 mediator mRNA, complete cds U70321 U70321 None GEN- Human herpesvirus entry 1249 9560T 3 3K9 mediator mRNA, complete cds U70321 U70321 None GEN- Human herpesvirus entry 1453 1160G>A 3K9 mediator mRNA, complete SD- 144146.1 Page 98 cds U70451 U70451 602170 GEN- Human myleoid 2167 2135A>G 3 3KB differentiation primary response protein MyD88 mRNA, complete cds U70451 U70451 602170 GEN- Human myleoid 2516 2484A>G 3 3KB differentiation primary response protein MyD88 mRNA, complete cds U71321 U71321 602623 GEN- Human FK506-binding 1248 1095C>T S 2TW protein FKBP51 mRNA, complete cds U71321 U71321 602623 GEN- Human FK506-binding 1425 1272G>A S 2TW protein FKBP51 mRNA, complete cds U73338 U73338 156570 GEN-69 Methionine Synthase 1158 764G>A C255Y U73338 U73338 156570 GEN-69 Methionine Synthase 5095 4701 G>A 3 U73338 U73338 156570 GEN-69 Methionine Synthase 6750 6356G>A 3 U75283 U75283 None GEN- Human sigma receptor 251 204G>A S 3NV mRNA, complete cds U75283 U75283 None GEN- Human sigma receptor 1625 1578A>C 3 3NV mRNA, complete cds U78294 U78294 603697 GEN- Homo sapiens 15S- 2449 2378A>G 3 3QZ lipoxygenase mRNA, complete cds U81375 U81375 602193 GEN- Human placental 1989 1811G>A 3 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 1996 1818C>T 3 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 2045 1867T>C 3 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U84487 U84487 601880 GEN-3ZJ Human CX3C chemokine 3015 2936T>C 3 precursor, mRNA, alternatively spliced, complete cds SD-144146.1 Page 98 U84487 U84487 601880 GEN-3ZJ Human CX3C chemokine 3058 2979T>C precursor, mRNA, alternatively spliced, complete cds U86358 U86358 602565 GEN- Human chemokine (TECK) 378 378A>G S LR6 mRNA, complete cds CD39 U87967 601752 GEN-44L Human ATP 1233 1203C>T S diphosphohydrolase mRNA, complete cds V00537 V00537 147578 GEN-U1 Interferon alpha 13 40 (-17)T>C 5 V00537 V00537 147578 GEN-U1 Interferon alpha 13 55 (-2)C>T 5 V00537 V00537 147578 GEN-U1 Interferon alpha 13 466 410C>T A137V V00537 V00537 147578 GEN-U1 Interferon alpha 13 808 752G>A 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 47 (-10)G>A 5 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 50 (-7)A>G 5 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 579 523T>C F175L IFNA14 V00542 147579 GEN-TT Interferon alpha 14 630 574C>G 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 740 684C>T 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 760 704T>A 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 771 715G>A 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 775 719T>A 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 812 756T>G 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 898 842A>T 3 IFNA14 V00542 147579 GEN-TT Interferon alpha 14 921 865G>A 3 IFNB1 V00546 147640 GEN-TV Messenger RNA for human 474 410T>G L137R fibroblast interferon V00548 V00548 147562 GEN-P2 Human messenger RNA 119 119G>A R40K for leukocyte (alpha-2) interferon IFNA10 V00551 147577 GEN-TS Interferon alpha 7 462 4160T S139F IFNA10 V00551 147577 GEN-TS Interferon alpha 7 510 464T>C I155T IFNA10 V00551 147577 GEN-TS Interferon alpha 7 516 470G>A R157K IFNA10 V00551 147577 GEN-TS Interferon alpha 7 712 666G>C 3 IFNA10 V00551 147577 GEN-TS Interferon alpha 7 716 670C>T 3 V00567 V00567 109700 GEN-P3 Human messenger RNA 303 303C>A S fragment for the beta-2 microglobulin HLA- X00033 146880 GEN-TO Human RNA sequence of 41 22A>C M8L SD-144146.1 Page 99 DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 79 60T>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 145 126C>T DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 157 138C>G DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 162 143T>A F48Y DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 165 146C>G T49S DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 227 208A>C K70Q DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) SD-144146.1 Page 99 HLA- X00033 146880 GEN-TO Human RNA sequence of 243 224A>G H75R DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 248 229C>T L77F DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 298 279T>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 311 292C>G L98V DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 334 315C>T DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 388 369A>G DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibi ty complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 559 540T>G DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibihty SD-144146 1 Page 99 complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 564 545C>A A182D DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 607 588T>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibi ty complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 644 625G>A A209T DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibihty complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 646 627A>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 679 660T>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibi ty complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 688 669G>A DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibihty complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 704 685G>A V229M DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major SD-144146 1 Page 99 histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 721 702G>C DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 724 705C>T DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 730 711 G>C L237F DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) HLA- X00033 146880 GEN-TO Human RNA sequence of 800 781A>G DQA1 the human DS glycoprotein alpha subunit from the HLA-D region of the major histocompatibility complex(MHC) X00497 X00497 142790 GEN-TN Human mRNA for HLA-DR 805 750A>G 3 antigens associated invariant chain (p33) X00497 X00497 142790 GEN-TN Human mRNA for HLA-DR 881 826A>G 3 antigens associated invariant chain (p33) X00497 X00497 142790 GEN-TN Human mRNA for HLA-DR 1144 1089C>G 3 antigens associated invariant chain (p33) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 13 13T>A S5T DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 91 91T>A S31T DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 94 94C>T R32C DPB1 chain (clone pll-beta-7) SD-144146.1 Page 99 HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 151 151 C>A L51 M DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 154 154C>A S DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 158 158G>C S53T DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 213 213G>A S DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 281 281C>T T94M DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 306 306OT S DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 341 341 A>G Q114R DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 353 353G>A R118Q DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 488 488C>T T163M DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 496 496T>C S166P DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 524 5240T T175I DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 568 568A>G R190G DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 600 600G>A S DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 708 708C>G F DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 761 761G>A 3 DPB1 chain (clone pll-beta-7) HLA- X00532 142858 GEN-U2 Human mRNA for SB beta- 840 840G>A 3 DPB1 chain (clone pll-beta-7) EGFR X00663 131550 GEN-U4 Human mRNA fragment for 1136 1136G>A R379K epidermal growth factor (EGF) receptor EGFR X00663 131550 GEN-U4 Human mRNA fragment for 1935 1935A>G S epidermal growth factor (EGF) receptor EGFR X00663 131550 GEN-U4 Human mRNA fragment for 2283 2283C>T S epidermal growth factor (EGF) receptor SD-144146.1 Page 99 X00734 X00734 None GEN- Human beta-tubulin gene 1059 1059G>T MST (5-beta) with ten Alu family members X00737 X00737 164050 GEN-P8 Human mRNA for purine 59 -51 )T>G nucleoside phosphorylase (PNP; EC 2.4.2.1) X00737 X00737 164050 GEN-P8 Human mRNA for purine 169 60T>C nucleoside phosphorylase (PNP; EC 2.4.2.1 ) X00737 X00737 164050 GEN-P8 Human mRNA for purine 260 151A>G S51 G nucleoside phosphorylase (PNP; EC 2.4.2,1 ) X00737 X00737 164050 GEN-P8 Human mRNA for purine 280 171T>C nucleoside phosphorylase (PNP; EC 2.4.2.1) X00737 X00737 164050 GEN-P8 Human mRNA for purine 1254 1145G>A nucleoside phosphorylase (PNP; EC 2.4.2.1) X01394 X01394 191160 GEN-4Y Tumor necrosis factor 125 (-28)C>T 5 X01586 X01586 147680 GEN-PC Interleukin 2 332 225T>G H75Q X01586 X01586 147680 GEN-PC Interleukin 2 563 456G>A S X02317 X02317 147450 GEN-KM Superoxide dismutase 1 614 550A>C 3 (Cu/Zn) X02469 X02469 191170 GEN-PF Human mRNA for p53 350 2150G P72R cellular tumor antigen X02469 X02469 191170 GEN-PF Human mRNA for p53 953 818G>A R273H cellular tumor antigen X02492 X02492 147572 GEN-1T Interferon alpha inducible 415 346C>G R116G protein X02492 X02492 147572 GEN-1T Interferon alpha inducible 417 348G>C S protein X02598 X02598 305370 GEN-X6 Human mRNA for EPA 64 23C>T A8V glycoprotein (erythroid- potentiating activity) X02598 X02598 305370 GEN-X6 Human mRNA for EPA 108 67C>G P23A glycoprotein (erythroid- potentiating activity) X02598 X02598 305370 GEN-X6 Human mRNA for EPA 298 257C>A T86N glycoprotein (erythroid- potentiating activity) X02598 X02598 305370 GEN-X6 Human mRNA for EPA 413 372T>C SD-144146.1 Page 99 glycoprotein (erythroid- potentiating activity) X02812 X02812 190180 GEN-XR Human mRNA for 870 29C>T P10L transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 979 138C>G I46M transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1632 791C>T T264I transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1807 966C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1930 1089G>A transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1942 1101OT transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 2013 1172G>A S391N transforming growth factor- beta (TGF-beta) H LA-DOB X03066 600629 GEN-ZG Human mRNA for HLA-D 32 (-25)G>A 5 class II antigen DO beta chain HLA-DOB X03066 600629 GEN-ZG Human mRNA for HLA-D 1147 1091 C>T class II antigen DO beta chain HLA-DOB X03066 600629 GEN-ZG Human mRNA for HLA-D 1299 1243A>G 3 class II antigen DO beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 79 (-3)A>G 5 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 97 16T>G S6A class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 203 122A>T Y41 F class II antigen DQw1.1 beta chain SD-144146.1 Page 99 X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 318 237C>T S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 408 327G>A S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 523 442A>G 1148V class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 550 469A>G S157G class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 566 485G>A R162Q class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 597 516C>T S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 618 5370T S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 627 546C>T S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 639 558C>T S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 677 596G>A R199H class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 684 603T>C S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 767 686G>A S229N class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 784 703G>A V235I class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 816 735T>C S class II antigen DQw1.1 SD-144146- 1 Page 99 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 822 741 T>G S class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 848 767G>A R256Q class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 879 798G>A 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 889 808A>G 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 892 811C>T 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 924 843C>G 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 998 917A>G 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1073 992A>T 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1082 1001A>G 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1095 1014OT 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1107 1026C>T 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1117 1036A>T 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1128 1047G>A 3 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1133 1052C>T 3 SD-144146. Page 99 class II antigen DQw1.1 beta chain X03068 X03068 142857 GEN-ZH Human mRNA for HLA-D 1180 1099C>T class II antigen DQw1.1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 99 37A>G T13A class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 104 42G>T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 348 2860A L96I class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 361 299G>A R100K class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 452 390G>A class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 459 397T>G S133A class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 463 401A>G K134R class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 471 409C>A P137T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 500 438C>T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 508 446G>A S149N class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 523 461 G>C G154A class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 547 485G>T R162L class II antigen DR1 beta chain SD-144146.1 Page 100 X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 551 489C>T S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 552 490G>A G164S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 567 505G>A A169T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 573 511 G>A V171 M class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 584 522A>G S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 593 531 C>T S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 596 534G>C Q178H class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 605 543T>C S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 632 570G>A S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 647 585G>A S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 686 624T>C S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 691 629C>T T210M class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 692 630G>A S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 716 654A>T R218S class II antigen DR1 beta SD-144146.1 Page 100 chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 721 659G>A R220Q class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 756 694G>A V232I class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 767 705C>T S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 800 738G>A S class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 814 752G>A R251 K class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 847 785C>G T262R class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 865 803A>G 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 868 806C>A 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 893 831 C>T 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 899 837T>C 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 903 841 A>G 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 913 851A>G 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 988 926G>A 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1004 942G>A 3 SD-144146. Page 100 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1027 9650T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1105 1043G>C class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1128 1066C>T class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1139 1077C>T 3 class II antigen DR1 beta chain X03069 X03069 142857 GEN-PI Human mRNA for HLA-D 1140 1078G>C 3 class II antigen DR1 beta chain X03438 X03438 138970 GEN-PM Human mRNA for 586 555G>A S granulocyte colony- stimulating factor (G-CSF) X03438 X03438 138970 GEN-PM Human mRNA for 1235 1204C>T 3 granulocyte colony- stimulating factor (G-CSF) X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3732 3432T>C 3 receptor X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3951 3651 C>A 3 receptor X03674 X03674 305900 GEN-9K Glucose-6-phosphate 503 33C>G H11Q dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 589 119C>T S40L dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 672 202G>A V68M dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 846 376A>G N126D dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 2215 1745T>C 3 dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 2242 1772T>C 3 dehydrogenase X03674 X03674 305900 GEN-9K Glucose-6-phosphate 2341 1871G>A 3 dehydrogenase SD-144146.1 Page 100 X03884 X03884 186830 GEN-52 CD3E antigen, epsilon 108 54C>T S polypeptide (TiT3 complex) X03884 X03884 186830 GEN-52 CD3E antigen, epsilon 1258 1204T>A 3 polypeptide (TiT3 complex) X04391 X04391 None GEN- Human mRNA for 2084 2012G>A 3 14D lymphocyte glycoprotein T1/Leu-1 CD1A X04450 188370 GEN-14J Human CD1 mRNA 402 402T>C S fragment for HTA1 thymocyte antigen (3terminal fragment) X04476 X04476 153390 GEN- Human mRNA fragment for 601 601 G>A 3 14K p56(LSTRA) protein- tyrosine kinase X04571 X04571 131530 GEN- Human mRNA for kidney 4507 4071 G>A 3 KYO epidermal growth factor (EGF) precursor X04608 X04608 104770 GEN-PQ Human mRNA for serum 698 602T>C I201T amyloid P component (SAP) X06180 X06180 186820 GEN- Human mRNA for CD7 1121 1122C>T 3 19A antigen (gp40) ITGA5 X06256 135620 GEN- Human mRNA for 2562 2539C>A L847I 19B fibronectin receptor alpha subunit X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 83 (-54)G>C 5 X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 940 804G>A S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1327 1191T>C S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1906 1770C>T S TCRD X06557 186810 GEN- Human mRNA for TCR- 1032 1014C>A 3 19M delta chain X07523 X07523 134371 GEN- Human mRNA for 1170 1097G>A G366E 1 E5 truncated form of complement factor H X07523 X07523 134371 GEN- Human mRNA for 1277 1204T>C Y402H 1 E5 truncated form of complement factor H SOD2 X07834 147460 GEN- Human mRNA for 44 40C>G P14A 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SD-144146.1 Page 100 S0D2 X07834 147460 GEN- Human mRNA for 51 47T>C V16A 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SOD2 X07834 147460 GEN- Human mRNA for 198 194C>A T65N 1ES manganese superoxide dismutase (EC 1.15.1.1 ) SOD2 X07834 147460 GEN- Human mRNA for 249 245T>C I82T 1ES manganese superoxide dismutase (EC 1.15.1.1 ) ITGB1 X07979 135630 GEN- Human mRNA for 1189 1086A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 1279 1176A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2713 2610T>C 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2878 2775T>A 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3339 3236A>G 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3531 3428G>A 3 4E5 fibronectin receptor beta subunit ANX5 X12454 131230 GEN- Human mRNA for vascular 128 (-1 )OT 5 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1413 1285T>G 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1431 1303C>T 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1518 1390G>A 3 1 M2 anticoagulant X12530 X12530 112210 GEN- Human mRNA for B 131 38C>T P13L 1 MH lymphocyte antigen CD20 (B1 , Bp35) X12530 X12530 112210 GEN- Human mRNA for B 1318 1225G>A 3 1 MH lymphocyte an SD-144146.1 Page 100 X13403 X13403 164175 GEN-L8 POU domain, class 2, 1298 1239T>C S transcription factor 1 X13403 X13403 164175 GEN-L8 POU domain, class 2, 1476 1417G>A A473T transcription factor 1 X13561 X13561 147910 GEN- Human mRNA for 54 18G>T S 10H preprokallikrein (EC 3.4.21) X13561 X13561 147910 GEN- Human mRNA for 441 405T>C S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 469 433G>C E145Q 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 592 556A>G K186E 10H preprokallikrein (EC 3.4.21 ) LIF X13967 159540 GEN- Human mRNA for 3710 3666T>G 3 1 PZ leukaemia inhibitory factor (LIF/HILDA) X14356 X14356 146760 GEN- Human mRNA for high 195 159T>C S 1R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1006 970G>A D324N 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1161 1125G>A S 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1164 1128G>A 3 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1174 1138G>T 3 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1203 1167C>T 3 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1217 1181G>A 3 1 R0 affinity Fc receptor (FcRI) X14356 X14356 146760 GEN- Human mRNA for high 1279 1243G>A 3 1R0 affinity Fc receptor (FcRI) X14583 X14583 None GEN- Human mRNA for Ig 131 107A>G K36R 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 132 108G>A S 1RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 164 140A>C N47T 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 255 231 G>T S 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 381 357A>G S 1 RJ lambda-chain SD-144146.1 Page 100 X14583 X14583 None GEN- Human mRNA for Ig 400 376C>G L126V 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 412 388G>A G130S 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 450 426G>A S 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 522 498C>T S 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 540 516G>C K172N 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 553 529C>A P177T 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 594 570A>G S 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 624 600T>C s 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 639 615T>C s 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 659 635G>A R212K 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 738 714A>C 3 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 740 716A>T 3 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 752 728C>A 3 1 RJ lambda-chain X14583 X14583 None GEN- Human mRNA for Ig 858 834C>G 3 1 RJ lambda-chain CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1375 1359C>T S 4EK receptor beta 1 CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1591 1575T>C 3 4EK receptor beta 1 X15263 X15263 None GEN- Muscarinic receptor, 1144 1044G>A S 4EQ CHRM1 X15606 X15606 146630 GEN-20 Intercellular adhesion 884 822G>A S molecule 2 IRF2 X15949 147576 GEN- Human mRNA for 842 744G>A S 1 UO interferon regulatory factor- 2 (IRF-2) X16166 X16166 182284 GEN-QT Human mRNA for putative 41 (-12)T>G 5 cytokine 21 (HC21 ) SD-144146.1 Page 100 X16166 X16166 182284 GEN-QT Human mRNA for putative 86 34A>G M12V cytokine 21 (HC21) X16166 X16166 182284 GEN-QT Human mRNA for putative 111 59C>T P20L cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 115 63G>A S cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 162 110C>T S37F cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 260 208A>G S70G cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 274 222T>C S cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 280 228T>C S cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 289 237A>G S cytokine 21 (HC21) X16166 X16166 182284 GEN-QT Human mRNA for putative 375 323C>T 3 cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 393 341A>C 3 cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 395 343A>G 3 cytokine 21 (HC21) X16166 X16166 182284 GEN-QT Human mRNA for putative 437 385C>T 3 cytokine 21 (HC21 ) X16166 X16166 182284 GEN-QT Human mRNA for putative 549 497G>C 3 cytokine 21 (HC21 ) CSNK2B X16312 115441 GEN- Human mRNA for 271 138T>C S 1XW phosvitin/casein kinase II beta subunit CSNK2B X16312 115441 GEN- Human mRNA for 812 679A>T 1XW phosvitin/casein kinase II beta subunit CSNK2B X16312 115441 GEN- Human mRNA for 885 752T>C 1XW phosvitin/casein kinase II beta subunit X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 141 108C>G S36R 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 147 114T>C 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) SD-144146.1 Page 100 X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 277 244A>G N82D 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 473 440A>G D147G 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 505 472C>T H158Y 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 531 498T>C S 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 559 526G>T V176F 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 733 700T>C F 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 766 733C>T 3 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) X16863 X16863 146740 GEN- Human Fc-gamma RIII-1 829 796G>A 3 1YV cDNA for Fc-gamma receptor 111-1 (CD 16) MIC2 X16996 313470 GEN- Human mRNA for T-cell 210 87T>C S 1ZE surface glycoprotein E2 MIC2 X16996 313470 GEN- Human mRNA for T-cell 283 160G>A D54N 1ZE surface glycoprotein E2 MIC2 X16996 313470 GEN- Human mRNA for T-cell 486 363C>T S 1ZE surface glycoprotein E2 MIC2 X16996 313470 GEN- Human mRNA for T-cell 1068 945C>T 3 1ZE surface glycoprotein E2 X17033 X17033 192974 GEN-LG Integrin, alpha 2 (CD49B, 4193 4145T>G 3 alpha 2 subunit of VLA-2 receptor) X17033 X17033 192974 GEN-LG Integrin, alpha 2 (CD49B, 4849 4801A>G 3 alpha 2 subunit of VLA-2 receptor) X17033 X17033 192974 GEN-LG I ntegrin, alpha 2 (CD49B, 4897 4849A>G 3 alpha 2 subunit of VLA-2 receptor) SD-144146.1 Page 10 X17042 X17042 177040 GEN- Human mRNA for 324 300C>T S 1ZN hematopoetic proteoglycan core protein X17042 X17042 177040 GEN- Human mRNA for 1021 997G>T 3 1ZN hematopoetic proteoglycan core protein IGHM X17115 147020 GEN- Human mRNA for IgM 849 777T>C S 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1102 1030A>G S344G 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1107 1035G>A S 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1175 1103T>G V368G 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1212 1140OT S 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1561 1489C>G R497G 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1692 1620G>T Q540H 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 1816 1744G>C V582L 1ZX heavy chain complete sequence IGHM X17115 147020 GEN- Human mRNA for IgM 2006 1934T>A 3 1ZX heavy chain complete sequence HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 20 15G>A S mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 41 36G>A S mRNA for non classical class I transplantation antigen SD-144146.1 Page 101 HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6 0) 248 243G>A mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 356 351C>T mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6 0) 812 807A>C mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 839 834G>A mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 947 942C>T mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 1004 999A>G mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 1123 1118G>C mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 1140 11350A mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6 0) 1148 1143C>T mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6 0) 1254 1249T>G mRNA for non classical class I transplantation antigen HLA-G X17273 142871 GEN-205 Human HLA G (HLA 6.0) 1255 1250C>G SD-144146.1 Page 101 mRNA for non classical class I transplantation antigen X51362 X51362 126450 GEN- Dopamine Receptor D2 588 423G>A S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1104 9390T S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1122 957T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1248 1083A>G S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1488 1323T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1548 1383A>G 3 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 2361 2196C>T 3 31W EDN3 X52001 131242 GEN- Endothelin 3 1262 1152G>A 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1649 1539C>G 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1700 1590OT 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1742 16320T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1797 1687C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1914 1804G>C 3 33E EDN3 X52001 131242 GEN- Endothelin 3 2040 1930C>T 3 33E X52079 X52079 602272 GEN- H-sapiens transcription 979 979T>G S327A 33B factor (ITF-2) mRNA, 3 end X52079 X52079 602272 GEN- H.sapiens transcription 1794 1794G>A S 33B factor (ITF-2) mRNA, 3 end X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3044 2869G>A 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3289 3114A>G 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3391 3216C>T 3 X52479 X52479 176960 GEN-LM Protein kinase C, alpha 908 881A>C D294A CD22 X52785 107266 GEN- H.sapiens CD22 mRNA 1357 1323C>T S 33Z SD-144146.1 Page 101 CD22 X52785 107266 GEN- H.sapiens CD22 mRNA 1531 14970T S 33Z CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 212 212A>G D71G receptor alpha 3 CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 552 5520T S receptor alpha 3 KAI1 X53795 600623 GEN- Human R2 mRNA for an 510 354C>T S 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1196 1040OT 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1309 1153G>A 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1325 1169G>A 3 34 P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1335 1179G>A 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1362 1206C>T 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1367 1211 C>T 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1368 1212G>A 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1370 1214G>A 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1371 1215T>C 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1378 1222C>T 3 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1382 1226G>A 3 34P inducible membrane SD-144146.1 Page 101 protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1392 1236C>T 34P inducible membrane protein KAI1 X53795 600623 GEN- Human R2 mRNA for an 1423 1267C>T 34P inducible membrane protein X54101 X54101 None GEN- Human NKG5 mRNA, 484 356C>T T119I 34W expressed in natural killer cells and T-cells X54101 X54101 None GEN- Human NKG5 mRNA, 625 4970G 34W expressed in natural killer cells and T-cells X54101 X54101 None GEN- Human NKG5 mRNA, 717 589C>G 3 34W expressed in natural killer cells and T-cells FCAR X54150 147045 GEN- Human mRNA for Fc 363 324A>G S 34T receptor X54199 X54199 138440 GEN-LS Phosphoribosylglycinamide 168 90G>A S formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimida zole synthetase X54315 X54315 114020 GEN-351 Human mRNA for N- 2549 2448T>C S cadherin X54867 X54867 161555 GEN- Human mRNA for NKG2-A 1188 1024G>C 3 MIV gene X54867 X54867 161555 GEN- Human mRNA for NKG2-A 1214 1050T>A 3 MIV gene X54867 X54867 161555 GEN- Human mRNA for NKG2-A 1232 1068A>T 3 MIV gene X54867 X54867 161555 GEN- Human mRNA for NKG2-A 1269 1105G>A 3 MIV gene X54867 X54867 161555 GEN- Human mRNA for NKG2-A 1353 1189C>T 3 MIV gene X55415 X55415 137060 GEN-364 Human mRNA for 28 (-12)G>C 5 UDP_galactose:N- acetylglucosaminide-(beta 1-&gt;4) galactosyltransferase SD-144146. Page 101 X55415 X55415 137060 GEN-364 Human mRNA for 30 (-10)C>G UDP_galactose N- acetylglucosamιnιde-(beta 1-&gt 4) galactosyltransferase X55415 X55415 137060 GEN-364 Human mRNA for 531 492G>A UDP_galactose N- acetylglucosamιnιde-(beta 1-&gt,4) galactosyltransferase X55415 X55415 137060 GEN-364 Human mRNA for 770 731A>G H244R UDP_galactose N- acetylglucosamιnιde-(beta 1-&gt,4) galactosyltransferase X55415 X55415 137060 GEN-364 Human mRNA for 1041 1002G>A UDP_galactose N- acetylglucosamιnιde-(beta 1-&gt,4) galactosyltransferase X55740 X55740 129190 GEN- Human placental cDNA 3373 3324T>G 36H coding for δnucleotidase (EC 3 1 3 5) CRP X56692 123260 GEN-373 H sapiens mRNA for C- 330 241A>G 181V reactive protein CRP X56692 123260 GEN-373 H sapiens mRNA for C- 636 547G>A V183M reactive protein CRP X56692 123260 GEN-373 H sapiens mRNA for C- 1020 931 G>A 3 reactive protein YWHAB X57346 601289 GEN- H sapiens mRNA for HS1 432 60C>A S 37R protein YWHAB X57346 601289 GEN- H sapiens mRNA for HS1 1135 763T>C 3 37R protein X57348 X57348 601290 GEN- H sapiens mRNA (clone 1317 1152C>T 3 373 9112) X57348 X57348 601290 GEN- H sapiens mRNA (clone 1342 1177C>T 3 373 9112) X57522 X57522 170260 GEN- H sapiens RING4 cDNA 1207 1177A>G I393V 37W X57522 X57522 170260 GEN- H sapiens RING4 cDNA 2120 2090A>G D697G 37W SD-144146 1 Page 101 X57819 X57819 None GEN-389 Human rearranged 499 499T>C C167R immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 524 524G>A F immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 545 545G>A S182N immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 558 558A>C Q186H immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 571 571G>A E191 K immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 616 616C>T F immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 639 639G>A S immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 695 695A>G Y232C immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 714 714C>T 3 immunoglobulin lambda light chain mRNA X57819 X57819 None GEN-389 Human rearranged 724 724C>T 3 immunoglobulin lambda light chain mRNA X57830 X57830 182135 GEN-7V Serotonin 5-HT2 receptor 247 102T>C S X58377 X58377 147681 GEN- Interleukin 11 807 744A>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 927 864T>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 1964 1901T>C 3 38V BTK X58957 300300 GEN- H sapiens atk mRNA for 2228 2096A>C 3 39A agammaglobulinaemia tyrosine kinase BTK X58957 300300 GEN- H sapiens atk mRNA for 2304 2172A>G SD-144146 1 Page 101 39A agammaglobulinaemia tyrosine kinase DRD1 X58987 126449 GEN- D1 dopaminergic receptor 229 (-48)A>G 5 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 366 90G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 474 198G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 1539 1263G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2040 1764A>C 3 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2045 1769C>A 3 4EH ITGA6 X59512 147556 GEN- H sapiens mRNA for 186 186C>G S 39W integrin alphaδ subunit ITGA6 X59512 147556 GEN- H.sapiens mRNA for 188 188G>C G63A 39W integrin alphaδ subunit X60069 X60069 231950 GEN- Human mRNA for 102 (-257)G>A 5 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 336 (-23)C>T 5 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1173 8150T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1173 815C>T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1399 1041 C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1409 1051 G>T A351S 3AJ pancreatic gamma- g I utamyltransf erase X60069 X60069 231950 GEN- Human mRNA for 1482 1124C>T T375M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1591 1233G>A S 3AJ pancreatic gamma- SD-144146.1 Page 101 glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1624 1266C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1637 12790A P427T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1651 1293C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1662 1304T>C V435A 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1783 1425A>G S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1794 1436C>T T479M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1795 1437G>A S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1981 1623C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2007 1649C>T T550M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2031 1673C>T S558L 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2047 1689C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2147 1789C>T 3 3AJ pancreatic gamma- g I utamyltra nsf erase X60069 X60069 231950 GEN- Human mRNA for 2176 1818C>T 3 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2224 1866C>A 3 SD-144146.1 Page 101 3AJ pancreatic gamma- glutamyltransferase X60992 X60992 186720 GEN-3BI H.sapiens CD6 mRNA for 2556 2436T>C 3 T cell glycoprotein CD6 X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 203 96A>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1372 1265A>G H42: kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1501 1394G>A R46! kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1766 1659C>T S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1823 1716T>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 2976 2869G>A kinase 1-phosphorylates beta adrenergic receptor ) NFKB2 X61498 164012 GEN- H.sapiens mRNA for NF- 2457 2294C>T P765L 3BW kB subunit KDR X61656 191306 GEN- H.sapiens mRNA for 2308 2308A>G T770A 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2353 2353G>C G785R 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2499 2499C>G N833K 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2537 2537A>T E846V 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 4123 4123G>C 3 3BZ growth factor receptor tyrosine kinase X62572 X62572 146790 GEN- H.sapiens RNA for Fc 967 968T>C 3CL receptor, PC23 SD-144146.1 Page 101 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1240 1241A>G 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1300 1301 C>T 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1542 1543G>C 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1560 1561 C>A 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1709 1710T>G 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 1931 1932A>T 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 2032 2033G>A 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 2136 2137G>A 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 2176 2177C>T 3 3CL receptor, PC23 X62572 X62572 146790 GEN- H.sapiens RNA for Fc 2201 2202G>A 3 3CL receptor, PC23 X62744 X62744 142855 GEN- Human RING6 mRNA for 541 496G>A V166I 3CQ HLA class II alpha chainlike product X62744 X62744 142855 GEN- Human RING6 mRNA for 674 629G>A R210H 3CQ HLA class II alpha chainlike product X62744 X62744 142855 GEN- Human RING6 mRNA for 750 705G>C S 3CQ HLA class II alpha chainlike product X62744 X62744 142855 GEN- Human RING6 mRNA for 1081 1036A>T 3 3CQ HLA class II alpha chainlike product X63053 X63053 602492 GEN- H.sapiens PTX3 mRNA 1689 1684G>A 3 3D4 TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 421 411G>C K137N 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 496 486G>A S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 516 506T>A F169Y SD-144146.1 Page 10 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 520 510C>T S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 580 570A>G S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 754 7440T S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 805 795T>C S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 811 801 G>C S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 813 803T>A V268E 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 817 807C>T S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H-sapiens mRNA for T-cell 860 850C>T S 3DG antigen receptor beta- chain TCRB X63456 186930 GEN- H.sapiens mRNA for T-cell 878 868C>A L290M 3DG antigen receptor beta- chain X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 51 44G>A R15H CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 116 109A>C K37Q CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 261 254G>A G85E CONVERTASE PRECURSOR X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2236 2225G>T 3 receptor epsilon polypeptide SD-144146.1 Page 10 X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2333 2322A>G 3 receptor epsilon polypeptide X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2364 2353G>T 3 receptor epsilon polypeptide CD44 X66733 107269 GEN- H.sapiens mRNA for 384 255C>T S 3H2 epican CD44 X66733 107269 GEN- H.sapiens mRNA for 455 3260A S109Y 3H2 epican X67325 X67325 600009 GEN-25 Interferon alpha inducible 311 257G>A S86N protein 27 X67325 X67325 600009 GEN-25 Interferon alpha inducible 320 266G>C G89A protein 27 X67325 X67325 600009 GEN-25 Interferon alpha inducible 485 431 C>G 3 protein 27 X67699 X67699 114280 GEN- H.sapiens HE5 mRNA for 143 119G>A S40N 3HP CDw52 antigen X67699 X67699 114280 GEN- H.sapiens HE5 mRNA for 147 123G>A M41 I 3HP CDw52 antigen X68596 X68596 168468 GEN-3IJ H.sapiens mRNA for 1563 1389T>C S parathyroid hormone receptor X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1182 1182T>C S RECEPTOR KINASE 2 X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1609 1609G>A E537K RECEPTOR KINASE 2 X69819 X69819 146631 GEN-28 Intercellular adhesion 195 187A>G I63V molecule 3 X69819 X69819 146631 GEN-28 Intercellular adhesion 317 309C>T S molecule 3 X69819 X69819 146631 GEN-28 Intercellular adhesion 436 428G>A G143D molecule 3 X69819 X69819 146631 GEN-28 Intercellular adhesion 1172 1164G>A S molecule 3 X69819 X69819 146631 GEN-28 Intercellular adhesion 1219 1211G>A R404Q molecule 3 X70340 X70340 190170 GEN-S3 H.sapiens mRNA for 3756 3725C>G 3 transforming growth factor alpha X70811 X70811 109691 GEN- beta-3-adrenergic receptor 315 190T>C W64R SD- 144146.1 Page 102 3KK X70811 X70811 109691 GEN- beta-3-adrenergic receptor 315 190T>C W64R 3KK ENG X72012 131195 GEN-3L3 H.sapiens end mRNA for 1165 884C>G T295R endoglin N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 1380 1155C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H-sapiens mRNA for nitric 1503 12780T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2048 1823C>T S608L 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2287 2062G>A G688S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2339 2114A>G D705G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2583 2358T>C S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2982 2757A>G S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3022 2797C>G R933G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3051 2826C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3693 3468T>C 3 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3715 3490G>A 3 3LW oxide synthase RGS1 X73427 600323 GEN- H.sapiens 1r20 mRNA for 247 233C>T A78V 3M6 alpha helical basic phosphoprotein MHC2TA X74301 600005 GEN- H.sapiens mRNA for MHC 1614 1499C>G A500G 3N5 class II transactivator MHC2TA X74301 600005 GEN- H.sapiens mRNA for MHC 3759 3644G>A 3 3N5 class II transactivator MHC2TA X74301 600005 GEN- H.sapiens mRNA for MHC 4422 4307T>C 3 3N5 class II transactivator X75913 X75913 601269 GEN- H-sapiens mRNA for gClq- 1052 974A>G 3 30G R X75913 X75913 601269 GEN- H.sapiens mRNA for gClq- 1074 996T>C 3 30G R X75962 X75962 600315 GEN- H.sapiens mRNA for OX40 836 831 OT S SD-144146.1 Page 102 MNA homologue LIPA X76488 278000 GEN- H.sapiens mRNA for 191 46A>C T16P 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 212 67G>A G23R 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 967 822G>A M274I 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 1531 1386C>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2254 2109A>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2439 2294C>T 3 3P2 lysosomal acid lipase X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 528 351G>A S 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 569 392A>G Y131C 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 687 510C>T S 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 1303 1126C>G 3 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 1601 1424T>G 3 4FN receptor X77130 X77130 602548 GEN- H.sapiens mRNA for ORL1 1816 1639G>T 3 4FN receptor X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 253 28G>T V10F omega) receptor 2 (splice variant) X77722 X77722 602376 GEN-29 Interferon (alpha, beta, 1128 903A>G S omega) receptor 2 (splice variant) ID1 X77956 600349 GEN- H.sapiens Id1 mRNA 380 345G>A S SQL ID1 X77956 600349 GEN- H.sapiens Id1 mRNA 382 347C>A T116N SQL ID1 X77956 600349 GEN- H-sapiens Id1 mRNA 842 807A>C 3 SQL ID1 X77956 600349 GEN- H.sapiens Id1 mRNA 851 816G>A 3 SQL YWHAH X78138 113508 GEN- H.sapiens 14-3-3 eta 953 753A>G 3 3QU subtype mRNA SD-144146.1 Page 102 YWHAH X78138 113508 GEN- H sapiens 14-3-3 eta 960 760G>A 3 3QU subtype mRNA YWHAH X78138 113508 GEN- H sapiens 14-3-3 eta 1387 1187C>T 3 3QU subtype mRNA X78282 X78282 601292 GEN- H sapiens mRNA for aryl 895 895T>C 3 LVF sulfotransferase (ST1A2) X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 1922 1922G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2378 2378G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2382 2382G>A 3 X79483 X79483 602399 GEN- H sapiens ERK6 mRNA for 1287 1254T>G 3 LPR extracellular signal regulated kinase X80200 X80200 None GEN- H sapiens MLN62 mRNA 1581 1496C>A 3 3UL X80200 X80200 None GEN- H sapiens MLN62 mRNA 1684 1599G>A 3 3UL IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 528 529C>T 3 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 534 535C>T 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 594 595T>C 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 601 602A>C 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 668 669A>T 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 726 727T>C 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 796 797G>A 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 804 805G>A 3W4 VH-D-JH-Hιnge-CH2-CH3 region IGHG3 X81695 147120 GEN- H sapiens rearranged IgG 827 828A>T SD-1441461 Page 102 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 828 829C>T 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 842 843C>T 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 849 850G>T 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 853 854A>C 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 900 901 T>C 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 905 906G>A 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 916 917G>A 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 957 958G>C 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 963 964G>A 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 970 971 G>A 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 973 974C>G 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 999 1000C>T 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1002 1003T>C 3W4 VH-D-JH-Hinge-CH2-CH3 region SD-144146. Page 10 IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1012 1013A>C 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1045 1046G>A 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1050 1051C>T 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1073 1074C>G 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1075 1076C>T 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1088 1089A>T 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H-sapiens rearranged IgG 1092 1093G>A 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H-sapiens rearranged IgG 1113 1114C>T 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1130 1131G>C 3 3W4 VH-D-JH-Hinge-CH2-CH3 region IGHG3 X81695 147120 GEN- H.sapiens rearranged IgG 1137 1138G>A 3 3W4 VH-D-JH-Hinge-CH2-CH3 region X82321 X82321 None GEN- H.sapiens mRNA for thiol- 304 304G>A G102R 3WT specific antioxidant X82321 X82321 None GEN- H.sapiens mRNA for thiol- 422 422G>T W141 L 3WT specific antioxidant X82321 X82321 None GEN- H-sapiens mRNA for thiol- 640 640C>G 3 3WT specific antioxidant X82321 X82321 None GEN- H.sapiens mRNA for thiol- 655 655C>T 3 3WT specific antioxidant HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 43 22G>A A8T 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 49 28C>A L10I SD-144146.1 Page 102 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 68 47G>C G16A 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 80 59C>T T20I 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 94 73T>G C25G 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 118 97G>T D33Y 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 126 105C>T S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 155 134G>A R45H 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 163 142T>G S48A 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 222 201 G>A S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 234 213C>G S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 239 218C>A A73E 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 291 270G>C K90N 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 310 289G>A A97T 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 323 302G>A S101 N 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 333 312C>A N104K 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 362 341A>C D114A 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 374 353C>T T118I 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 382 361A>T R121W 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 408 387C>G S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 430 409T>C Y137H 3XX Cw * 0704 HLA-C X83394 142840 GEN- H sapiens mRNA for HLA- 433 412G>A D138N 3XX Cw * 0704 SD-144146 Page 102 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 441 420C>A F140L 3XX Cw * 0704 HLA-C X83394 142840 GEN- H-sapiens mRNA for HLA- 474 453C>T S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 480 459C>T S HLA-C X83394 142840 HLA-C X83394 142840 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 520 499A>T T167S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 533 512T>G L171W 3XX Cw * 0704 HLA-C X83394 142840 GEN- H-sapiens mRNA for HLA- 548 527C>A A176E 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 622 601A>G K201 E 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 626 605C>A T202K 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 639 618G>A S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 644 623C>A P208H 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 669 6480T S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 673 652C>G L218V 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 724 703G>A A235T 3XX Cw * 0704 HLA-C X83394 142840 GEN- H-sapiens mRNA for HLA- 748 727C>T R243W 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 756 735G>C S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 765 744G>A S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 768 747C>T S 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 777 756C>T S 3XX Cw*0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 835 814G>A V272M SD-144146.1 Page 102 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 850 829C>G Q277E 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 874 853A>G M285V 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 893 872A>C Q291P 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 912 891C>A S297R 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 933 912C>T S 3XX Cw*0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 946 925A>G M309V 3XX Cw * 0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 977 956T>C V319A 3XX Cw*0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 1012 991A>G M331V 3XX Cw*0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 1070 1049G>C C350S 3XX Cw*0704 HLA-C X83394 142840 GEN- H.sapiens mRNA for HLA- 1108 1087A>G T363A 3XX Cw * 0704 X83861 X83861 176806 GEN-5H Prostaglandin E receptor 3 387 180C>G S (subtype EP3) {alternative products} X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 32 (-161 )OT 5 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 317 125G>A R42H 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 435 243C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 616 424G>A V142I 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 663 471 C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 900 708T>C 3 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 974 782C>T 3 3ZC BCI-2 homologue CD97 X84700 601211 GEN- H.sapiens mRNA for 828 758C>G P253R 3ZO leucocyte antigen CD97 X86474 X86474 600250 GEN- H.sapiens mRNA for ATAC 249 225A>G S SD-144146.1 Page 103 CD σ> 0- CO O co co CO m CO O o CO σ. co co Q > CC - O CD lO r- r- T- O CVI S co Ν l-O CM l- CM CM CD CO CM CO o o σ- O CO -r ^1- f- oo M M CO O -r in oo • * m CO -r o o o o r- cD cn c-- o o o o o o o o o 0 0 0 in in in i- in m in m -r -r -r -r co co o o o -i- t>-. - < - CM CM CM -- ^J- -t- ^-- ^l- -O 0O 0O 00 -t- -ζ)- CD CD CD CM C-O O- CM CM CM r- CD CD O O O O O O O O CM CM CM CM in in o o o co oo co ~ h~ . oo ιn h- t-~ r-~ ιn m m ιn co co 00 cc co 'S σj c- ^l- τ-- -r cD θ co co co o o o o o o -j- -j- -f s s s CO CO CO CD t^- r- I^ I^ O O O O O o o o o 0 0 0 co co co co cn c-- σ) cj) θ o o o o o o o o 0 0 0 x x x x x x x x >- >- >- >- >- >- >- >- >- >- v ^ • -f -r t- CO O O O CM CM CM CM ϋ ϋ O CD D O ) (5 (5 -- h- r « - h. oo -O . - r-- m in m i fv » ?? °o oo co ^" n-> n? — ■ f f -c D o c co co o o o o y- Jf- -q- -j- ■ * i^- r^ r; ^t- CO CO CD CD I-~ r^- l^ l~ O O O θ P- P- o o o o O C ^t- oo co oo co σ> σ> cj) σ o o o o l— I— o o o o H H — X X X X X X X X >- >- Q- 0. -j- >. i oo receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 528 492C>T S receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 555 519A>T S receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 559 523A>G 1175V receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 636 600C>T S receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 676 640G>A E214K receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 733 697A>G I233V receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 849 813G>T W271 C receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 908 872C>T T291 M receptor gamma-chain TCRG Y00790 186970 GEN-UC Human mRNA for T-cell 970 934A>G R312G receptor gamma-chain Y00796 Y00796 153370 GEN-2B Leukocyte integrin alpha-l 1006 918C>T S Y00796 Y00796 153370 GEN-2B Leukocyte integrin alpha-l 4519 4431A>G 3 CR1 Y00816 120620 GEN-UG Human mRNA for 207 180G>C E60D complement receptor type 1 (CR1 , C3b/C4b receptor, CD35) Y07683 Y07683 600843 GEN- H.sapiens mRNA for P2X3 717 552C>T S 4F1 purinoceptor Y07683 Y07683 600843 GEN- H.sapiens mRNA for P2X3 753 588A>G S 4F1 purinoceptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 835 809A>G H270R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 946 920G>A R307Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1068 1042G>A A348T 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1096 1070C>G T357S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1405 1379A>G Q460R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1589 1563C>G H521Q 4F4 receptor SD-144146. Page 10 Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1590 1564G>A V522I 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1628 1602G>T S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1759 1733G>A R578Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1772 1746G>A S 4F4 receptor Y10659 Y10659 300119 GEN-1J6 H.sapiens IL-13Ra mRNA 1116 1073G>A G358D Y12509 Y12509 None GEN- Homo sapiens mRNA for 257 257G>A G86D 1 ME UDP-Gal:GlcNAc galactosyltransferase Y12510 Y12510 None GEN- Homo sapiens mRNA for 909 909OT 1 MC UDPGal:GlcNAc b1 ,4 galactosyltransferase Z1 1695 Z11695 176948 GEN-1 L1 H.sapiens 40 kDa protein 1287 1153G>A 3 kinase related to rat ERK2 Z11696 Z11696 601795 GEN-1 L0 H.sapiens 44kDa protein 449 449T>G I150S kinase related to rat ERK1 Z15108 Z15108 176982 GEN- H.sapiens mRNA for 246 240T>C S 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 1694 1688A>C D563A 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2033 2027G>A 3 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2086 2080T>G 3 1TE protein kinase C zeta Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 25 25G>C V9L Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 103 103G>T A35S Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 106 106A>G M36V Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 165 165C>G S Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 209 209A>C E70A Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 213 213C>G S Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 222 222A>G S Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 259 259A>G N87D Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 261 261 C>G N87K Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 353 353T>C I118T Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 355 355A>C I119L Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 362 362G>C R121T SD-144146.1 Page 10 Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 379 379C>G L127V Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 387 387C>G S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 409 409C>T H137Y Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 412 412G>A D138N Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 435 435G>A S Z22651 Z2265 None GEN-268 H-sapiens HLA-B35 mRNA 463 463A>C S155R Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 477 477G>C S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 486 486C>G S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 527 527T>A V176E Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 538 538C>T R180W Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 539 539G>T R180L Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 544 544G>A A182T Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 572 572G>C W191 S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 583 583T>C Y195H Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 603 603G>C E201 D Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 610 610C>G Q204E Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 621 621 C>A D207E Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 623 623C>A P208H Z22651 Z2265 None GEN-268 H-sapiens HLA-B35 mRNA 636 636C>T S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 648 6480T S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 652 652G>A V218I Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 668 668C>T A223V Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 693 693C>T S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 756 756T>C S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 774 774A>G S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 786 786T>C S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 846 846A>G S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 900 900A>G S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 909 909G>A S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 916 916A>G I306V Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 985 985A>G T329A Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 1008 1008C>T S Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 1046 1046C>G S349C Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 1120 1120T>C 3 Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 1164 1164G>A 3 Z22651 Z2265 None GEN-268 H.sapiens HLA-B35 mRNA 1192 1192C>T 3 SD- 144146.1 Page 103 Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 1209 1209OT 3 Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA 1219 1219C>A 3 Z22651 Z22651 None GEN-268 H.sapiens HLA-B35 mRNA TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1163 1135G>A V379I 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1186 1158G>T S 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 1840 1812G>A S 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2021 1993G>A A665T 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2087 2059C>T F 26P complete CDS TAP2 Z22935 170261 GEN- H.sapiens TAP2B mRNA, 2119 2091 T>G S 26P complete CDS HLA-DMB Z23139 142856 GEN-277 H.sapiens RING7 mRNA 380 212G>A S71N for HLA class II alpha chain-like product HLA-DMB Z23139 142856 GEN-277 H.sapiens RING7 mRNA 1125 957C>T for HLA class II alpha chain-like product Z26649 Z26649 600230 GEN- Phospholipase C beta-3 437 438C>T 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 466 467G>A 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 2664 2665C>T 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 3168 3169G>T 3 2B5 ECE1 Z35307 600423 GEN- Endothelin Converting 1141 1104C>T S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1627 1590T>C S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1696 1659G>A S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1946 1909G>A V637M 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 2433 2396G>A 3 2MA Enzyme 1 Z35491 Z35491 601497 GEN- H.sapiens mRNA for novel 315 37G>A E13K 2ME glucocorticoid receptor- SD-144146.1 Page 103 associated protein Z35491 Z35491 601497 GEN- H.sapiens mRNA for novel 333 55G>A E19K 2ME glucocorticoid receptor- associated protein Z35491 Z35491 601497 GEN- H sapiens mRNA for novel 1297 1019A>C 3 2ME glucocorticoid receptor- associated protein PDE4C Z46632 600128 GEN- H sapiens HSPDE4C1 280 169C>T R57C 2X2 gene for 3,5-cyclic AMP phosphodiesterase PDE4C Z46632 600128 GEN- H.sapiens HSPDE4C1 1142 1031 G>A R344Q 2X2 gene for 3,5-cyclic AMP phosphodiesterase Z48810 Z48810 602664 GEN- H.sapiens mRNA for TX 1280 1239A>C 3 2YJ protease precursor Z56281 Z56281 603734 GEN- H.sapiens mRNA for 883 837G>A S 36V interferon regulatory factor 3 Z56281 Z56281 603734 GEN- H sapiens mRNA for 1114 1068G>A S 36V interferon regulatory factor 3 Z56281 Z56281 603734 GEN- H.sapiens mRNA for 1175 1129G>A E377K 36V interferon regulatory factor 3 Z56281 Z56281 603734 GEN- H.sapiens mRNA for 1326 1280G>C S427T 36V interferon regulatory factor 3 Z56281 Z56281 603734 GEN- H.sapiens mRNA for 1373 1327A>C 3 36V interferon regulatory factor 3 Table 16. Identified Variances In Genes for Pathways Identified in Endocrine and SD-144146.1 Page 103 Metabolic Disease AB00026 AB00026 602784 GEN- Human mRNA for prepro 215 210T>C 3 3 16N cortistatin like peptide, complete cds AB00238 AB00238 601698 GEN- Human mRNA for 612 612A>G S 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 628 628A>G T210A 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 871 871T>C +291Q 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 948 948G>A S 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 973 973T>C +325R 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 1600 1600C>T R534C 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 2308 2308T>C C770R 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 2770 2770G>A V924M 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 3727 3727G>A 3 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 4036 4036G>A 3 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 4602 4602C>A 3 5 5 1D6 KIAA0387 gene, partial cds AB00238 AB00238 601698 GEN- Human mRNA for 4621 4621C>A 3 5 5 1D6 KIAA0387 gene, partial cds AB00528 AB00528 300135 GEN- Homo sapiens mRNA for 2137 2069A>T H690L 9 9 KVU ABC transporter 7 protein, complete cds AB00529 AB00529 170290 GEN-W4 Homo sapiens mRNA for 2197 2073A>T 3 3 3 perilipin, complete cds AB00942 AB00942 600130 GEN- Homo sapiens gene for 1016 5340T S 6 6 MDN apobec-1 AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1071 1010T>A 3 0 0 1SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 3 SD-144146.1 Page 103 1SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1801 1740A>G 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 2199 2138G>A 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB01336 AB01336 None GEN- Homo sapiens mRNA for 249 213T>C S 1 1 L6C DPM2, complete cds AB01336 AB01336 None GEN- Homo sapiens mRNA for 263 227C>G T76S 1 1 L6C DPM2, complete cds AB01678 AB01678 None GEN-L39 Homo sapiens mRNA for 2468 2369G>A 3 9 9 Glutamine:fructose-6- phosphate amidotransferase, complete cds AB01678 AB01678 None GEN-L39 Homo sapiens mRNA for 2549 2450G>A 9 9 Glutamine:fructose-6- phosphate amidotransferase, complete cds AB01678 AB01678 None GEN-L39 Homo sapiens mRNA for 2755 2656G>A 9 9 Glutamine:fructose-6- phosphate amidotransferase, complete cds ACLY X64330 108728 GEN- H.sapiens mRNA for ATP- 3998 3914G>T 3 3F0 citrate lyase ACLY X64330 108728 GEN- H.sapiens mRNA for ATP- 4229 4145A>C 3 3F0 citrate lyase AF001174 AF001174 602898 GEN- Homo sapiens p38beta2 1044 1038T>C S 18T MAP kinase mRNA, complete cds AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 75 67T>C C23R acetyltransferase (E2 component of pyruvate dehydrogenase complex) SD-144146, Page 103 AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 116 108OT acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 759 751T>G S251A acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 806 798C>T acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 866 858T>C acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 2000 1992G>T acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF001437 AF001437 245349 GEN-9T Dihydrolipoamide S- 2158 2150C>A acetyltransferase (E2 component of pyruvate dehydrogenase complex) AF004709 AF004709 602899 GEN-UX Homo sapiens stress- 432 384G>A activated protein kinase 4 mRNA, complete cds AF009923 AF009923 603169 GEN- Homo sapiens 702 702C>T KZM preprocathepsin P mRNA, partial cds AF009923 AF009923 603169 GEN- Homo sapiens 1018 1018T>C KZM preprocathepsin P mRNA, partial cds AF009923 AF009923 603169 GEN- Homo sapiens 1129 1129G>A KZM preprocathepsin P mRNA, partial cds AF013611 AF01361 1 602364 GEN- Homo sapiens lymphopain 537 537T>G H179Q 20Z mRNA, complete cds AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 314 291 C>T S AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 431 408T>C S AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 506 483A>G S SD-144146.1 Page 103 AF053712 AF053712 None GEN- Homo sapiens 2086 1902T>G 3 MM2 osteoprotegerin ligand mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 1695 1647C>T S KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4037 3989C>T A1330V KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4683 4635C>A S KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4802 4754C>T S1585L KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF066859 AF066859 232600 GEN- Homo sapiens muscle 53 53G>A G18D LKT glycogen phosphorylase (PYGM) mRNA, complete cds AF066859 AF066859 232600 GEN- Homo sapiens muscle 856 856T>C F286L LKT glycogen phosphorylase (PYGM) mRNA, complete cds AF066859 AF066859 232600 GEN- Homo sapiens muscle 1716 1716C>T S LKT glycogen phosphorylase (PYGM) mRNA, complete cds AF071748 AF071748 None GEN- Homo sapiens cathepsin F 1055 963C>T S LOZ (CATSF) mRNA, complete cds AF071748 AF071748 None GEN- Homo sapiens cathepsin F 1344 1252G>A 3 LOZ (CATSF) mRNA, complete cds AF071748 AF071748 None GEN- Homo sapiens cathepsin F 1513 1421T>C 3 LOZ (CATSF) mRNA, complete cds AF071748 AF071748 None GEN- Homo sapiens cathepsin F 1574 1482C>A 3 SD-144146. Page 104 LOZ (CATSF) mRNA, complete cds AF071748 AF071748 None GEN- Homo sapiens cathepsin F 1576 1484G>A 3 LOZ (CATSF) mRNA complete cds AGL U84007 232400 GEN- Human glycogen 7309 6909A>G 3 3Z7 debranching enzyme isoform 1 (AGL) mRNA, alternatively spliced isoform, complete cds AGT K02215 106150 GEN-WK Human angiotensinogen 659 620C>T T207M mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 842 803T>C M268T mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1155 1116G>A S mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1476 1437C>A S mRNA complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1821 1782G>A 3 mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 2053 2014A>C 3 mRNA, complete CDS AJ005162 AJ005162 600067 GEN- Homo sapiens mRNA for 1915 1882A>C 3 KVT UDP- glucuronosyltransferase APOH M62839 138700 GEN- Human apolipoprotein H 500 461 G>A R154H 3CY mRNA, complete cds APOH M62839 138700 GEN- Human apolipoprotein H 835 796G>T V266L 3CY mRNA, complete cds APOH M62839 138700 GEN- Human apolipoprotein H 1098 1059T>C 3 3CY mRNA, complete cds ARG1 M14502 207800 GEN- Human liver arginase 800 744C>T S I RE mRNA, complete cds AVPR1B AF030512 600264 GEN- Homo sapiens small cell 273 150G>A S 4FF vasopressin subtype 1 b receptor mRNA, complete cds BMP1 M22488 112264 GEN- Human bone 2224 2195G>A 3 25X morphogenetic protein 1 (BMP-l ) mRNA BMP4 M22490 112262 GEN- Human bone 849 455T>C V152A SD-144146 1 Page 104 25Y morphogenetic protein-2B (BMP-2B) mRNA BMP7 X51801 1 12267 GEN- Human OP-1 mRNA for 1752 1630T>C 3 32H osteogenic protein BMP7 X51801 1 12267 GEN- Human OP-1 mRNA for 1789 1667G>A 3 32H osteogenic protein CAT X04076 115500 GEN- Human kidney mRNA for 51 (-20)T>C 5 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 218 148C>T L50F I SP catalase CAT X04076 115500 GEN- Human kidney mRNA for 1237 1167T>C S ISP catalase CAT X04076 115500 GEN- Human kidney mRNA for 1325 1255C>T S 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 2131 2061A>C 3 I SP catalase CBG J02943 122500 GEN-Y2 Human corticosteroid 106 71A>T D24V binding globulin mRNA, complete cds CBG J02943 122500 GEN-Y2 Human corticosteroid 971 936T>C binding globulin mRNA, complete cds CBG J02943 122500 GEN-Y2 Human corticosteroid 1229 1194G>A binding globulin mRNA, complete cds CCKBR L08112 118445 GEN- Cholecystokinin (CCKb) 456 456G>A S 1 FL CETP M30185 118470 GEN- Human cholesteryl ester 1283 1153G>C V385L 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1298 1168G>C A390P 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1506 1376A>G D459G 2FK transfer protein mRNA, SD-144146.1 Page 104 complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1696 1566G>A 2FK transfer protein mRNA, complete cds CLU X14723 185430 GEN- Human SP-40,40 mRNA 131 84C>T 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 429 382G>T V128F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 836 7890T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1234 1187C>T S396L 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1372 1325A>T Y442F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1482 14350T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1548 1501 OT 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1645 1598A>T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain COL18A1 L22548 120328 GEN-262 Human collagen type XVIII 22 22A>G I8V alpha 1 (COL18A1) mRNA, partial cds COL18A1 L22548 120328 GEN-262 Human collagen type XVIII 2071 2071A>G alpha 1 (COL18A1 ) mRNA, SD-144146.1 Page 104 partial cds C0L18A1 L22548 120328 GEN-262 Human collagen type XVIII 2126 2126A>G 3 alpha 1 (C0L18A1 ) mRNA, partial cds C0L18A1 L22548 120328 GEN-262 Human collagen type XVIII 2395 2395A>G 3 alpha 1 (COL18A1 ) mRNA, partial cds C0L18A1 L22548 120328 GEN-262 Human collagen type XVIII 3372 3372A>T 3 alpha 1 (COL18A1 ) mRNA, partial cds C0L18A1 L22548 120328 GEN-262 Human collagen type XVI 11 3374 3374A>C 3 alpha 1 (COL18A1) mRNA, partial cds CRHBP X58022 122559 GEN- Human mRNA for 987 941T>G I314S 38K corticotropin-releasing factor binding protein (CRF-BP) CTGF U 14750 121009 GEN- Human connective tissue 1878 1878A>C 3 1S3 growth factor mRNA, partial cds CTSG M16117 116830 GEN-1XI Human cathepsin G 382 374A>G N125S mRNA, complete cds CTSL X12451 116880 GEN- Human mrRNA for pro- 1300 1012C>T 3 1M1 cathepsin L (major excreted protein MEP) CYP11 B2 D13752 124080 GEN- Human CYP11 B2 gene for 1600 1593G>A 3 CCD steroid 18-hydroxylase, complete cds CYP21 M17252 201910 GEN-201 Human cytochrome 224 224G>A R75H P450c21 mRNA, 3 end CYP21 M17252 201910 GEN-201 Human cytochrome 330 330C>T S P450c21 mRNA, 3 end CYP21 M17252 201910 GEN-201 Human cytochrome 745 745T>C 3 P450c21 mRNA, 3 end D13811 D13811 238310 GEN-AA Glycine cleavage system: 277 148G>T V50L Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1073 944G>A R315K Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1083 954G>A S Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 1773 16440T 3 SD-144146,1 Page 104 Protein T D13811 D13811 238310 GEN-AA Glycine cleavage system: 2037 1908C>T 3 Protein T D50678 D50678 602600 GEN- Human mRNA for 3378 3276G>A 3 30Y apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 3755 3653G>A 3 30Y apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 3949 3847G>C 3 30Y apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 4368 4266T>A 3 30Y apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 4455 4353G>A 3 30Y apolipoprotein E receptor 2, complete cds D63480 D63480 1 16898 GEN- Human mRNA for 1728 1728G>A S 3DN KIAA0146 gene, partial cds D82347 D82347 601724 GEN- Neurogenic differentiation 804 695G>A G232D MIP 1 D85730 D85730 140559 GEN- Homo sapiens HSPA1 L 2156 2021 C>G 3 LR0 mRNA for Heat shock protein 70 testis variant, complete cds D87258 D87258 602194 GEN- Homo sapiens mRNA for 150 102C>T S 42R serin protease with IGF- binding motif, complete cds D87812 D87812 600528 GEN-6 Camitine 2363 2344T>C Palmitoyltransferase I (muscle) D90228 D90228 203750 GEN- ACAT1 547 471 C>A 46A DCN M14219 125255 GEN- Human 1490 1409A>G 1 QX chondroitin/dermatan sulfate proteoglycan (PG40) core protein mRNA, complete cds DCN M14219 125255 GEN- Human 1534 1453C>T 1 QX chondroitin/dermatan SD-144146.1 Page 10 sulfate proteoglycan (PG40) core protein mRNA, complete cds DRD1 X58987 126449 GEN- D1 dopaminergic receptor 229 (-48)A>G 5 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 366 90G>A S 4EH DRD1 X58987 126449 DRD1 X58987 126449 GEN- D1 dopaminergic receptor 1539 1263G>A s 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2040 1764A>C 3 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2045 1769C>A 3 4EH ECE1 Z35307 600423 GEN- Endothelin Converting 1141 1104OT S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1627 1590T>C S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1696 1659G>A S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1946 1909G>A V637M 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 2433 2396G>A 3 2MA Enzyme 1 EDN2 M65199 131241 GEN- Endothelin 2 384 314C>T A105V CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS EDN3 X52001 131242 GEN- Endothelin 3 1262 1152G>A 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1649 15390G 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1700 1590C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1742 1632C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1797 16870T 3 33E SD- 144146- 1 Page 10 EDN3 X52001 131242 GEN- Endothelin 3 1914 1804G>C 3 33E EDN3 X52001 131242 GEN- Endothelin 3 2040 1930OT 3 33E EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2228 1748G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2376 1896G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2840 2360G>C 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2935 2455G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 3294 2814A>G 3 4DX A EDNRB L06623 131244 GEN- Endothelin Receptor Type 88 (-146)A>G 5 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 332 99C>T S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B EHHADH L07077 261515 GEN- Human enyol-CoA: 1225 1218G>A S 1 DF hydratase 3-hydroxyacyl- CoA dehydrogenase SD-144146- 1 Page 10 (EHHADH) mRNA, complete cds with repeats EHHADH L07077 261515 GEN- Human enyol-CoA: 1823 1816C>A P606T 1 DF hydratase 3-hyd roxyacyl- CoA dehydrogenase (EHHADH) mRNA, complete cds with repeats FACL1 L09229 152425 GEN-1GI Human long-chain acyl- 3026 2953G>A coenzyme A synthetase (FACL1 ) mRNA, complete cds FACL1 L09229 152425 GEN-1GI Human long-chain acyl- 3083 3010G>A coenzyme A synthetase (FACL1 ) mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 323 (-123)G>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1180 735T>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1201 756A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1216 771A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1218 773G>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1266 821A>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1306 861 C>T 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1654 1209A>T 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1657 1212T>C 3BE growth factor mRNA, SD-144146.1 Page 10 complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1799 1354A>T 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1801 1356C>T 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1867 1422A>G 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1945 1500C>A 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1973 1528G>A 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2167 1722G>A 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2186 1741A>G 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2302 1857T>A 3 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2328 1883G>A 3 3BE growth factor mRNA, complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 300 291T>C S 2MX factor 8 (FGF-8) mRNA, complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 645 636G>C S 2MX factor 8 (FGF-8) mRNA, complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 648 639A>G 2MX factor 8 (FGF-8) mRNA, complete cds FGFR1 X51803 136350 GEN- Human mRNA for 276 159T>G 32G fibroblast growth factor (FGF) receptor FGFR2 X52832 176943 GEN-341 Human bek mRNA for 338 159A>G SD-144146.1 Page 10 fibroblast growth factor receptor-BEK FGFR2 X52832 176943 GEN-341 Human bek mRNA for 2903 2724A>T 3 fibroblast growth factor receptor-BEK FGFR3 M64347 134934 GEN- Human novel growth factor 3108 3108C>A 3 SEX receptor mRNA, 3 cds FGFR3 M64347 134934 GEN- Human novel growth factor 3715 3715G>A 3 SEX receptor mRNA, 3 cds FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 83 28G>A V10I 37M fibroblast growth factor receptor (FGFR-4) FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 217 162T>G S 37M fibroblast growth factor receptor (FGFR-4) FSHR M65085 136435 GEN- FSH receptor 2105 2039G>A S680N 3FQ GAA Y00839 232300 GEN-UJ a-glucosidase 815 (-14)G>A 5 GAA Y00839 232300 GEN-UJ a-glucosidase 861 33C>T S GAA Y00839 232300 GEN-UJ a-glucosidase 3301 2473C>T 3 GAA Y00839 232300 GEN-UJ a-glucosidase 3477 2649C>T 3 GAA Y00839 232300 GEN-UJ a-glucosidase 3496 2668T>G 3 GAA Y00839 232300 GEN-UJ a-glucosidase 3509 2681 G>A 3 GALN M77140 137035 GEN- H.sapiens pro-galanin 339 339C>T 3 3PM mRNA, 3 end GC M12654 139200 GEN- Human serum vitamin D- 925 897T>C 1 MN binding protein (hDBP) mRNA, complete cds GC M12654 139200 GEN- Human serum vitamin D- 1324 1296G>T E432D 1 MN binding protein (hDBP) mRNA, complete cds GC M12654 139200 GEN- Human serum vitamin D- 1335 1307C>A T436K 1 MN binding protein (hDBP) mRNA, complete cds GC M 12654 139200 GEN- Human serum vitamin D- 1362 1334G>A R445H 1 MN binding protein (hDBP) mRNA, complete cds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 780 780C>A F260L peptide-1 receptor mRNA with CA dinucleotide SD-144146.1 Page 10 repeat, complete cds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 780 780C>A F260L peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds GLP1R U01157 138032 GEN-V3 Human glucagon-like 947 947G>C G316A peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 947 947G>C G316A peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 1200 1200C>A S peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds GLP1 R U01157 138032 GEN-V3 Human glucagon-like 1200 1200OA peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds GNRHR L07949 138850 GEN- Gonadotropin releasing 1371 1347C>A 3 1 F1 hormone agonist GPX1 Y00433 138320 GEN-TJ Human mRNA for 504 186G>A S glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 610 292C>G R98G glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 911 593C>T P198L glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1048 730A>C glutathione peroxidase (EC 1.11.1.9.) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1110 792A>C glutathione peroxidase (EC 1.11.1.9.) GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 821 7 3C>T 38S plasma glutathione peroxidase SD-144146.1 Page 10 GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 979 931 G>A 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1187 1139T>G 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1354 1306C>T 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1443 1395C>T 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1516 1468C>A 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1581 1533C>T 3 38S plasma glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 718 638T>C 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 837 757C>A 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H.sapiens GPx-4 mRNA 882 802A>C 3 for phospholipid hydroperoxide glutathione peroxidase GSS U34683 601002 GEN- Human glutathione 364 324G>A S 2LF synthetase mRNA, complete cds GYS1 J04501 138570 GEN- Human muscle glycogen 567 407T>C I136T 14W synthase mRNA, complete cds GYS1 J04501 138570 GEN- Human muscle glycogen 2276 2116C>A R706S 14W synthase mRNA, complete cds GYS1 J04501 138570 GEN- Human muscle glycogen 2457 2297A>C 3 14W synthase mRNA, complete SD-144146.1 Page 10 cds GYS1 J04501 138570 GEN- Human muscle glycogen 2470 2310C>T 3 14W synthase mRNA, complete cds GYS1 J04501 138570 GEN- Human muscle glycogen 3099 2939T>C 3 14W synthase mRNA, complete cds HADHA U04627 600890 GEN-155 Human 78 kDa gastrin- 1507 1507G>A V503M binding protein mRNA, complete cds HADHB D16481 143450 GEN- Human mRNA for 871 825T>C S 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1607 1561G>C 3 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1908 1862A>C 3 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1911 1865A>C 3 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HGF X16323 142409 GEN- Human mRNA for 5740 5606T>A 3 1Y1 hepatocyte growth factor (HGF) HSD17B3 U05659 264300 GEN-186 Human 17beta- 894 846G>C S hydroxysteroid dehydrogenase type 3 mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 859 776G>A S 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds SD-144146.1 Page 10 IGFBP4 M62403 146733 GEN- Human insulin-like growth 1403 1320G>T 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1443 1360G>A 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1446 1363G>A 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1485 1402A>T 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 751 751 A>C factor binding protein 6 (IGFBP6) mRNA, complete mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 835 835A>C factor binding protein 6 (IGFBP6) mRNA, complete mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 850 850G>A factor binding protein 6 (IGFBP6) mRNA, complete mature peptide ITGA5 X06256 135620 GEN- Human mRNA for 2562 2539C>A L847I 19B fibronectin receptor alpha subunit J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 17 (-9)G>A N BETA CHAIN PRECURSOR J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 155 130C>A P44T N BETA CHAIN PRECURSOR J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 331 306C>A N BETA CHAIN PRECURSOR J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 435 410A>C D137A SD-144146.1 Page 10 N BETA CHAIN PRECURSOR J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 475 450C>T S N BETA CHAIN PRECURSOR J00117 J00117 118860 GEN-2H CHORIOGONADOTROPI 517 492A>C S N BETA CHAIN PRECURSOR J00123 J00123 131330 GEN- Human enkephalin gene 81 81 C>T s MK4 J00277 J00277 190020 GEN- Human (genomic clones 81 81T>C s MH8 lambda-[SK2-T2, HS578T]; cDNA clones RS-[3,4, 6]) c-Ha-ras1 proto-oncogene, complete coding sequence J02610 J02610 107730 GEN-6N Apolipoprotein B (including 1931 1853T>C V618A Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 6616 6538C>T F Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 7014 6936T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 7623 7545T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 8294 8216C>T P2739L Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 8625 8547T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10033 9955G>C D3319H Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10358 10280C>A T3427K Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10372 10294C>G Q3432E Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11273 11195T>C I3732T Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11705 11627C>T A3876V Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11862 11784T>A S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11923 11845T>C F3949L Ag(x) antigen) SD-144146.1 Page 10 J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12461 12383A>T E4128V Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12476 12398G>C G4133A Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12486 12408G>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12619 12541G>A E4181 K Ag(x) antigen) J02611 J02611 107740 GEN-60 Human apolipoprotein D 676 615T>G 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 683 622T>G 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 701 640OG 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 745 684A>G 3 mRNA, complete cds J03209 J03209 185250 GEN-PK Human matrix 133 133G>A E45K metalloproteinase-3 (MMP- 3) mRNA, complete cds J03209 J03209 185250 GEN-PK Human matrix 288 288C>T S metalloproteinase-3 (MMP- 3) mRNA, complete cds J03210 J03210 120360 GEN-ZY Human collagenase type 721 721 C>T P241 S IV mRNA, 3 end J03210 J03210 120360 GEN-ZY Human collagenase type 1759 1759C>T P587S IV mRNA, 3 end J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 932 380G>A R127H J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1063 511G>A A171T J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1190 638C>G 3 J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1201 6490T 3 J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 172 57C>T S dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 559 444C>T dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1704 1589C>A dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1833 17180G dihydroxyvitamin D3) SD-144146.1 Page 10 receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1858 1743G>T dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 1959 1844A>C dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 2190 2075delT dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3301 3186C>A dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 3991 3876A>G dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A dihydroxyvitamin D3) receptor J03258 J03258 601769 GEN-2J Vitamin D (1 ,25- 4187 4072G>A dihydroxyvitamin D3) receptor J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1569 1493A>C N498T dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1624 1548T>A dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 1813 1737A>G dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, SD-144146.1 Page 105 branched chain keto acid dehydrogenase complex) J03490 J03490 246900 GEN-C5 Dihydrolipoamide 2096 2020T>C 3 dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex) J03548 J03548 103260 GEN- Human adrenodoxin 1099 967G>A 3 11M mRNA, complete cds J03548 J03548 103260 GEN- Human adrenodoxin 1123 991T>C 3 11 M mRNA, complete cds J03548 J03548 103260 GEN- Human adrenodoxin 1222 1090G>C 3 11 M mRNA, complete cds J03548 J03548 103260 GEN- Human adrenodoxin 1254 1122G>A 3 11 M mRNA, complete cds J04144 J04144 106180 GEN-2L Angiotensin-converting 501 479A>G N160S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 604 582C>T S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 803 781 G>T A261 S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1042 1020OT S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- S enzyme (ACE) 1515CCT>CC T J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- [P505V;50 enzyme (ACE) 1515delCCT 6-505del] J04144 J04144 106180 GEN-2L Angiotensin-converting 1797 1775A>G D592G enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2215 2193G>A S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2350 2328A>G S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2505 2483T>C M828T enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S SD-144146.1 Page 10 enzyme (ACE) J05070 J05070 120361 GEN- Human type IV 1840 1821A>C 16U collagenase mRNA, complete cds J05070 J05070 120361 GEN- Human type IV 2101 2082G>A 16U collagenase mRNA, complete cds J05070 J05070 120361 GEN- Human type IV 2146 2127C>T 16U collagenase mRNA, complete cds J05070 J05070 120361 GEN- Human type IV 2288 2269T>C 16U collagenase mRNA, complete cds J05158 J05158 603104 GEN-173 Human carboxypeptidase 2314 2314C>T N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2316 2316G>T N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2332 2332G>T N mRNA 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2541 2541G>A N mRNA 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2651 2651 C>T N mRNA, 3 end K00396 K00396 107741 GEN-PO Human apolipoprotein E 112 52G>A A18T (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 121 61G>A E21 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 151 91 G>A E31 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 197 137T>C L46P (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 204 144delG F (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 238 178A>G T60A (epsilon 2 and 3 alleles) mRNA SD- 144146 Page 10 K00396 K00396 107741 GEN-PO Human apolipoprotein E 365 305C>G P102R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 409 349G>A A117T (epsilon 2 and 3 alleles) K00396 K00396 107741 GEN-PO Human apolipop (epsilon 2 and 3 K00396 K00396 107741 GEN-PO Human apolipopr otein E 494 434G>A G145D (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 515 455G>A R152Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 520 460OA R154S (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 538 478C>T R160C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 547 487C>T R163C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 548 488G>A R163H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 550 490A>G K164E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 743 683G>A (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 785 725G>A R242Q (epsilon 2 and 3 alleles) SD-144146.1 Page 106 mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 796 736C>T R246C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 821 761T>A V254E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 865 805C>G R269G (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 935 875G>A R292H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 1000 940A>C S314R (epsilon 2 and 3 alleles) mRNA K01911 K01911 162640 GEN-20 Neuropeptide Y 236 150G>A S K01911 K01911 162640 GEN-20 Neuropeptide Y 290 204C>T S K02770 K02770 147720 GEN-5M Interleukin 1 , beta 19 (-68)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 26 (-61 )A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 48 (-39)C>T 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 114 28G>A E10K K02770 K02770 147720 GEN-5M Interleukin 1 , beta 119 33G>A M11 I K03195 K03195 138140 GEN-ZT Human (HepG2) glucose 1484 1305C>T S transporter gene mRNA, complete cds K03195 K03195 138140 GEN-ZT Human (HepG2) glucose 2120 1941 G>C 3 transporter gene mRNA, complete cds KDR X61656 191306 GEN- H.sapiens mRNA for 2308 2308A>G T770A 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2353 2353G>C G785R 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2499 2499C>G N833K 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2537 2537A>T E846V 3BZ growth factor receptor SD-144146.1 Page 10 tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 4123 4123G>C 3BZ growth factor receptor tyrosine kinase L00352 L00352 143890 GEN- Human low density 71 72C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 103 104G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 716 717C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 881 882G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1180 1181A>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1186 1187C>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1187 1188T>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1191 1192G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1222 1223G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1223 1224C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1224 1225G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1227 1228T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1234 1235T>C SD-144146.1 Page 106 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1252 1253A>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1268 1269A>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1268 1269A>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1279 1280C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1280 1281G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1308 1309OT 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1309 1310G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1316 1317G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1320 1321T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1345 1346G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1368 1369T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1376 1377C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1383 1384C>T 2S8 lipoprotein receptor gene, exon 18 SD-144146- Page 106 L00352 L00352 143890 GEN- Human low density 1406 1407T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1418 1419G>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1428 1429T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1453 1454C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1796 1797T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 2108 2109G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 2490 2491A>C 2S8 lipoprotein receptor gene, exon 18 L02932 L02932 170998 GEN- Human peroxisome 648 432G>A KW4 proliferator activated receptor mRNA, complete cds L07592 L07592 600409 GEN- Human peroxisome 3119 2782C>G 1 E7 proliferator activated receptor mRNA, complete cds L13286 L13286 600125 GEN- Human mitochondrial 1 ,25- 2031 1638G>A 3 103 dihydroxyvitamin D3 24- hydroxylase mRNA, complete cds L13436 L13436 108961 GEN-2Q guanylate cyclase 1410 1411T>A 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1646 1647C>G 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1650 1651 G>C 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1677 1678C>G 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 2222 2223C>T 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 2444 2445C>T 3 L13858 L13858 182530 GEN- Human guanine nucleotide 423 423T>C S SD-144146.1 Page 106 1 PL exchange factor mRNA, complete cds L13858 L13858 182530 GEN- Human guanine nucleotide 3957 3957G>A S 1PL exchange factor mRNA, complete cds L17075 L17075 601284 GEN- Human TGF-b superfamily 838 747G>A S 1ZQ receptor type I mRNA, complete cds L19182 L19182 602867 GEN- Human MAC25 mRNA, 297 284G>A R95K 21Z complete cds L20859 L20859 137570 GEN- Human leukemia virus 3141 2771A>G 3 23V receptor 1 (GLVR1) mRNA, complete cds L26232 L26232 172425 GEN- Human phospholipid 906 819C>T S 2AK transfer protein mRNA, complete cds L26232 L26232 172425 GEN- Human phospholipid 1547 1460C>A T487K 2AK transfer protein mRNA, complete cds L27080 L27080 None GEN- Human melanocortin 5 146 (-38)A>C 5 4G2 receptor (MC5R) gene, complete cds L27080 L27080 None GEN- Human melanocortin 5 927 744C>T S 4G2 receptor (MC5R) gene, complete cds L40992 L40992 600211 GEN- Homo sapiens (clone 265 265G>A V89I 2SO PEBP2aA1 ) core-binding factor, runt domain, alpha subunit 1 (CBFAI ) mRNA, 3 end of cds L78207 L78207 600509 GEN-5Q Cell surface receptor for 4019 3981A>G S sulfonylureas on pancreatic b cells LEPR U43168 601007 GEN- Human leptin receptor (Ob- 446 253A>G T85A 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 519 326A>G K109R 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 861 668A>G Q223R 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 1222 1029T>C S 2UN r) mRNA, complete cds SD-144146.1 Page 106 LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2161 1968G>C K656N 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2174 1981A>C T661 P 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 2764 2571T>G S 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3151 29580T S 2UN r) mRNA, complete cds LEPR U43168 601007 GEN- Human leptin receptor (Ob- 3250 3057G>A S 2UN r) mRNA, complete cds LIPA X76488 278000 GEN- H.sapiens mRNA for 191 46A>C T16P 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 212 67G>A G23R 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 967 822G>A M274I 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 1531 1386C>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2254 2109A>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2439 2294C>T 3 3P2 lysosomal acid lipase LIPC J03540 151670 GEN-11 J Human hepatic lipase 469 465T>G S mRNA, complete cds LIPC J03540 151670 GEN-11 J Human hepatic lipase 595 591A>G S mRNA, complete cds LIPC J03540 151670 GEN-11 J Human hepatic lipase 648 644G>A S215N mRNA, complete cds LIPC J03540 151670 GEN-11 J Human hepatic lipase 817 813C>T S mRNA, complete cds LIPC J03540 151670 GEN-11J Human hepatic lipase 1441 1437C>A S mRNA, complete cds LRP1 D90070 107770 GEN-466 Human ATL-derived PMA- 686 513T>G 3 responsive (APR) peptide mRNA :PAPI M63959 104225 GEN-3EI Human alpha-2- 850 837G>A macroglobulin receptor- associated protein mRNA, complete cds :PAPI M63959 104225 GEN-3EI Human alpha-2- 1093 1080C>T macroglobulin receptor- SD-144146.1 Page 10 associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1175 1162G>A macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1249 1236C>T macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1249 1236C>T macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1392 1379T>G macroglobulin receptor- associated protein mRNA, complete cds M10051 M10051 147670 GEN-2V Insulin receptor 2757 2619G>A S M10051 M10051 147670 GEN-2V Insulin receptor 4391 4253G>A 3 M10901 M10901 138040 GEN-2W Corticosteroid nuclear 1220 1088A>G N363S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- S receptor b 1893AOAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2024 1892- F receptor b 1893delAG M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2054 1922A>T D641V receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2372 2240T>G I747S receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>C L753F receptor b M10901 M10901 138040 GEN-2W Corticosteroid nuclear 2391 2259A>T L753F receptor b M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 2166 2034C>T S M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3353 3221T>G 3 M11050 M11050 138040 GEN-7Y Glucocorticoid receptor 3398 3266T>G 3 M11717 M11717 140550 GEN- Human heat shock protein 54 (-162)G>A 5 MF3 (hsp 70) gene, complete cds SD-144146.1 Page 10 M11717 M11717 140550 GEN- Human heat shock protein 190 (-26)C>G 5 MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 320 105C>T S MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 390 175G>A V59M MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 431 216C>G S MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 545 330G>C E110D MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 1907 1692C>G S MF3 (hsp 70) gene, complete cds M11717 M11717 140550 GEN- Human heat shock protein 2319 2104A>G 3 MF3 (hsp 70) gene, complete cds M12578 M12578 152760 GEN-2Y Gonadotropin-releasing 79 47G>C W16S hormone (leutinizing- releasing hormone) M12674 M12674 133430 GEN-7Z Estrogen receptor 1267 975C>G S M13509 M13509 120353 GEN-QJ Human skin collagenase 383 315A>G S mRNA, complete cds M13509 M13509 120353 GEN-QJ Human skin collagenase 899 831 G>A S mRNA, complete cds M13509 M13509 120353 GEN-QJ Human skin collagenase 1522 1454A>G 3 mRNA, complete cds M13509 M13509 120353 GEN-QJ Human skin collagenase 1747 16790T 3 mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 184 (-11 )T>C 5 proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 270 76G>C V26L proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 446 252C>T proteinase mRNA, SD-144146.1 Page 10 complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1254 1060C>G proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1306 1112G>A proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1336 1142T>A proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1338 1144C>T proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1451 1257G>A proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1462 1268C>T proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1522 1328G>C proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1557 1363G>C proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1585 1391 C>A proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1630 1436T>C proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1668 1474T>G proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1712 1518C>G proteinase mRNA, complete cds M14221 M14221 161565 GEN-QM Human cathepsin B 1898 1704A>G proteinase mRNA, complete cds M14565 M14565 118485 GEN-30 Cytochrome P450, 947 903G>C M301 I SD-144146.1 Page 10 subfamily XIA (cholesterol side chain cleavage) M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 466 (-1122)C>G 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 565 (-1023)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1182 (-406)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1221 (-367)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1326 (-262)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1541 (-47)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1687 100G>A V34M M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1839 252G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2110 523C>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2640 1053G>C S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2826 1239G>A s M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2862 1275C>G 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2864 1277C>A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2865 1278C>A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 3371 1784A>T 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 136 (-39)T>C 5 M15856 M15856 238600 GEN-33 Lipoprotein lipase 280 106G>A D36N M15856 M15856 238600 GEN-33 Lipoprotein lipase 438 264T>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 447 273G>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 474 300C>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 480 306A>C R102S M15856 M 15856 238600 GEN-33 Lipoprotein lipase 511 337T>C W113R M15856 M15856 238600 GEN-33 Lipoprotein lipase 571 397C>T F M15856 M15856 238600 GEN-33 Lipoprotein lipase 680 506G>A G169E M15856 M15856 238600 GEN-33 Lipoprotein lipase 722 548A>G D183G M15856 M15856 238600 GEN-33 Lipoprotein lipase 770 596C>G S199C M15856 M15856 238600 GEN-33 Lipoprotein lipase 781 607G>A A203T M15856 M15856 238600 GEN-33 Lipoprotein lipase 795 621C>G D207E M15856 M15856 238600 GEN-33 Lipoprotein lipase 818 644G>A G215E SD-144146.1 Page 10 M15856 M15856 238600 GEN-33 Lipoprotein lipase 836 662T>C I221T M15856 M15856 238600 GEN-33 Lipoprotein lipase 839 665G>A G222E M15856 M15856 238600 GEN-33 Lipoprotein lipase 843 669C>T S M15856 M15856 238600 GEN-33 Lipoprotein lipase 867 693C>G D231 E M15856 M15856 238600 GEN-33 Lipoprotein lipase 875 701 C>T P234L M15856 M15856 238600 GEN-33 Lipoprotein lipase 916 742delG F M 15856 M15856 238600 GEN-33 Lipoprotein lipase 983 809G>A R270H M15856 M 15856 238600 GEN-33 Lipoprotein lipase 985 811T>A S271T M15856 M15856 238600 GEN-33 Lipoprotein lipase 1003 829G>A D277N M15856 M15856 238600 GEN-33 Lipoprotein lipase 1 127 953A>G N318S M15856 M 15856 238600 GEN-33 Lipoprotein lipase 1255 1081 G>A A361T M15856 M15856 238600 GEN-33 Lipoprotein lipase 1348 1174C>G L392V M15856 M15856 238600 GEN-33 Lipoprotein lipase 1401 1227G>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 1508 1334G>A C445Y M15856 M15856 238600 GEN-33 Lipoprotein lipase 1553 1379C>T A460V M15856 M 15856 238600 GEN-33 Lipoprotein lipase 1595 1421 C>G F M15856 M15856 238600 GEN-33 Lipoprotein lipase 1611 1437G>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 1973 1799T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2428 2254T>A 3 M 15856 M15856 238600 GEN-33 Lipoprotein lipase 2743 2569T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2958 2784G>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3017 2843T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3343 3169T>C 3 M 15856 M15856 238600 GEN-33 Lipoprotein lipase 3447 3273C>T 3 M16660 M16660 140571 GEN- Human 90-kDa heat-shock 825 741 G>A S 1YC protein gene, cDNA, complete cds M16660 M16660 140571 GEN- Human 90-kDa heat-shock 825 741 G>A S 1YC protein gene, cDNA, complete cds M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 175 (-42)C>G 5 (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 754 538A>G 1180V SD-144146 1 Page 10 (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 938 722C>T A241V (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 1221 1005delC F (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 1591 1375delT F (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 1713 1497C>T S (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 1825 1609C>T F (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 2438 2222T>G V741 G (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 2730 2514G>A S (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 5243 5027T>A 3 (aldosterone receptor) M16801 M16801 600983 GEN-36 Mineralocorticoid receptor 5645 5429G>A 3 (aldosterone receptor) M16827 M16827 201450 GEN-EI Acyl-Coenzyme A 1956 1938T>C 3 dehydrogenase, C-4 to C- 12 straight chain M20132 M20132 313700 GEN-38 Androgen receptor 995 633G>A S (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1385 1023T>C S (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1786 1424G>A G475E (dihydrotestosterone receptor) M20566 M20566 147880 GEN-3A Interleukin 6A 3058 2621A>T 3 M20681 M20681 138170 GEN- Human glucose 1550 1308C>T S 230 transporter-like protein-Ill (GLUT3), complete cds M20681 M20681 138170 GEN- Human glucose 3179 2937T>C 230 transporter-like protein-Ill (GLUT3), complete cds M20681 M20681 138170 GEN- Human glucose 3238 2996C>T 230 transporter-like protein-Ill (GLUT3), complete cds SD-144146.1 Page 10 M20681 M20681 138170 GEN- Human glucose 3356 3114T>C 3 230 transporter-like protein-Ill (GLUT3), complete cds M20681 M20681 138170 GEN- Human glucose 3378 3136T>C 3 230 transporter-like protein-Ill (GLUT3), complete cds M20681 M20681 138170 GEN- Human glucose 3524 3282C>A 3 230 transporter-like protein-Ill (GLUT3), complete cds M20681 M20681 138170 GEN- Human glucose 3572 3330G>T 3 230 transporter-like protein-Ill (GLUT3), complete cds M23725 M23725 179050 GEN-ES Pyruvate kinase, muscle 547 438C>T S M23725 M23725 179050 GEN-ES Pyruvate kinase, muscle 850 741 G> A S M23725 M23725 179050 GEN-ES Pyruvate kinase, muscle 1259 1150G>A E384K M24857 M24857 180190 GEN-80 Retinoic acid receptor, 1694 1280C>T S427L gamma 1 M26393 M26393 201470 GEN-EW Acyl-Coenzyme A 1797 1765A>G 3 dehydrogenase, C-2 to C-3 short chain M27137 M27137 109715 GEN-5W 3beta hydroxysteroid 1103 1100C>A T367N dehydrogenase M27492 M27492 147810 GEN-3F INTERLEUKIN 1 4686 4604T>G 3 RECEPTOR, TYPE I PRECURSOR M27875 M27875 107680 GEN- Human apolipoprotein A-I 34 I 5G>C S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 202 183C>T S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 204 185T>G L62W 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 255 236C>T S79F 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 689 670C>T S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 824 805G>A 3 2CK mRNA, complete cds M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 370 340C>G 3 M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 401 371T>G 3 M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 479 449T>A 3 SD-144146.1 Page 10 M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 26 17C>A A6E M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 183 174G>A S M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 192 183C>A S M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 178 79C>T P27S natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 178 79C>T P27S natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 203 104C>G A35G natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 203 104OG A35G natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 210 111G>T S natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 210 111 G>T S natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atnal 327 228C>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 327 228C>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 553 454T>C natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atnal 553 454T>C natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atnal 626 527G>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atnal 626 527G>T natriuretic factor (CDD- ANF) mRNA complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 640 541T>C natriuretic factor (CDD- SD-144146 1 Page 10 ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atnal 640 541T>C natriuretic factor (CDD- ANF) mRNA, complete cds M31145 M31145 146730 GEN-3J Insulin-like growth factor 923 759A>G I253M binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1048 884T>C 3 binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1260 1096C>G 3 binding protein 1 precursor M31159 M31159 146732 GEN- Human growth hormone- 204 95G>C G32A 2GD dependent insulin-like growth factor-binding protein mRNA, complete cds M31159 M31159 146732 GEN- Human growth hormone- 2178 2069A>T 2GD dependent insulin-like growth factor-binding protein mRNA, complete cds M31328 M31328 139130 GEN-7G Guanine nucleotide binding 1049 1043G>A 3 protein (G protein) beta polypeptide 3 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1271 1241 C>T 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1344 1314G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1489 1459G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1780 1750T>C 3 1 M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 109 109G>A D37N (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 438 438A>G S (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1172 1172A>C 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1179 1179C>T 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1323 1323C>A 3 (lipoamide) beta SD-144146 1 Page 10 M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1376 1376G>C 3 (lipoamide) beta M34479 M34479 179060 GEN-F9 Pyruvate dehydrogenase 1433 1433C>T 3 (lipoamide) beta M34720 M34720 103880 GEN-RH aldose reductase 676 663C>A S M34720 M34720 103880 GEN-RH aldose reductase 1176 1163C>A 3 M37825 M37825 165190 GEN- Human fibroblast growth 787 648T>G S 20M factor-5 (FGF-5) mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 711 519T>C S 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 936 744G>T 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 1270 1078T>C 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 3268 3076T>G 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4529 4337A>C 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4555 4363A>G 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4672 4480A>C 3 35G protein mRNA, complete cds M55531 M55531 138230 GEN-FF Solute carrier family 2 1208 1133T>G V378G (facilitated glucose transporter), member 5 M55531 M55531 138230 GEN-FF Solute carrier family 2 1975 1900C>T 3 (facilitated glucose transporter), member 5 M55531 M55531 138230 GEN-FF Solute carrier family 2 1985 1910A>G 3 (facilitated glucose transporter), member 5 M57899 M57899 191740 GEN- Human biiirubin UDP- 1828 1813C>T 3 38A glucuronosyltransferase SD-144146.1 Page 107 isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 1956 1941C>G 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 2057 2042C>G 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M59305 M59305 108962 GEN- Human atrial natriuretic 160 (-203M- 39P peptide clearance receptor 199)delTTTπ (ANP C-receptor) mRNA, complete cds M59830 M59830 603012 GEN- Human MHC class III 1860 1860C>G MSB HSP70-2 gene (HLA), complete cds M61906 M61906 171833 GEN-RV Human P13-kinase 3112 3113A>G associated p85 mRNA sequence M62782 M62782 146734 GEN- Homo sapiens insulin-like 908 852C>T 3CU growth factor binding protein 5 (IGFBP-5) mRNA, complete cds M63960 M63960 176875 GEN-FT Protein phosphatase 1 , 1087 1058G>T 3 catalytic subunit, alpha isoform M63960 M63960 176875 GEN-FT Protein phosphatase 1 , 1292 1263G>A 3 catalytic subunit, alpha isoform M64590 M64590 238300 GEN-FU Glycine cleavage system: 3076 2926A>G M976V Protein P M64710 M64710 None GEN- Human C-type natriuretic 199 200C>G 3 KUW peptide gene, complete cds M64710 M64710 None GEN- Human C-type natriuretic 777 778G>A 3 KUW peptide gene, complete cds M64710 M64710 None GEN- Human C-type natriuretic 1215 1216A>G 3 KUW peptide gene, complete cds SD-144146.1 Page 10 M65028 M65028 602372 GEN- Human hnRNP type A/B 273 131C>G P44R 3FM protein mRNA, complete cds M65028 M65028 602372 GEN- Human hnRNP type A B 595 4530G S 3FM protein mRNA, complete cds M65028 M65028 602372 GEN- Human hnRNP type A/B 1255 1113A>G 3 3FM protein mRNA, complete cds M68867 M68867 180231 GEN-S1 Human cellular retinoic 604 506C>A 3 acid-binding protein II (CRABP) mRNA, complete cds M82962 M82962 600388 GEN- Human N-benzoyl-L- 2316 2307T>G 3 3XC tyrosyl-p-amino-benzoic acid hydrolase alpha subunit (PPH alpha) mRNA, complete cds M82962 M82962 600388 GEN- Human N-benzoyl-L- 2428 2419A>C 3 3XC tyrosyl-p-amino-benzoic acid hydrolase alpha subunit (PPH alpha) mRNA, complete cds M83667 M83667 116898 GEN- Human NF-IL6-beta 574 486G>T E162D 3YG protein mRNA, complete cds M83667 M83667 116898 GEN- Human NF-IL6-beta 578 490C>T P164S 3YG protein mRNA, complete cds M83667 M83667 116898 GEN- Human NF-IL6-beta 581 493C>T R165C 3YG protein mRNA, complete cds M83667 M83667 116898 GEN- Human NF-IL6-beta 974 886C>G 3 3YG protein mRNA, complete cds M84755 M84755 162641 GEN-46 Neuropeptide Y1 1121 1121A>C K374T M86553 M86553 116845 GEN-416 Human cathepsin S 26 20T>C V7A mRNA, complete cds M86553 M86553 116845 GEN-416 Human cathepsin S 487 481 A>T T161 S mRNA, complete cds M86553 M86553 116845 GEN-416 Human cathepsin S 705 699G>C S SD-144146.1 Page 107 mRNA, complete cds M86553 M86553 116845 GEN-416 Human cathepsin S 1149 1143T>G mRNA, complete cds M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 296 16T>C S6P M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 413 133G>A G45R M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1430 1150T>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1453 1173A>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1677 1397G>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1797 1517G>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1885 1605C>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1916 1636T>C 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 2158 1878A>G 3 M90516 M90516 138292 GEN-GI Glutamine-fructose-6- 2968 2846T>G 3 phosphate transaminase M93415 M93415 102581 GEN- Human activin type II 136 (-38)G>T 48S receptor mRNA, complete cds MC1 R X67594 155555 GEN- H.sapiens mRNA for MSH 346 178G>T V60L 4G4 receptor MC1 R X67594 155555 GEN- H.sapiens mRNA for MSH 656 488A>G Q163R 4G4 receptor MC1 R X67594 155555 GEN- H.sapiens mRNA for MSH 1068 900OT S 464 receptor MC1 R X67594 155555 GEN- H.sapiens mRNA for MSH 1110 942A>G S 404 receptor MC1 R X67594 155555 GEN- H.sapiens mRNA for MSH 1134 966G>A 3 404 receptor MET M35074 164860 GEN- Human met oncogene 60 60OT S 2LU mRNA, 3 end MET M35074 164860 GEN- Human met oncogene 294 294G>A S 2LU mRNA, 3 end SD-144146.1 Page 10 MGP M58549 154870 GEN- Human matrix Gla protein 330 304A>G T102A 38Y (MGP) mRNA, complete cds MMP12 L23808 601046 GEN-27J Human metalloproteinase 1082 1070A>G N357S (HME) mRNA, complete cds MMP2 D85510 602261 GEN- Homo sapiens mRNA for 2389 2389G>C 3 40A SMCP-2, partial cds MPV17 X76538 600945 GEN- H-sapiens Mpv17 mRNA 575 548C>T 3 3P6 MTP X75500 157147 GEN- H.sapiens mRNA for 1847 1823T>G F608C 307 microsomal triglyceride transfer protein MTP X75500 157147 GEN- H.sapiens mRNA for 3231 3207G>A 3 307 microsomal triglyceride transfer protein NGFB X52599 162030 GEN- Human mRNA for beta 832 663G>A S 33V nerve growth factor NGFR M14764 162010 GEN- Human nerve growth factor 2716 2603C>T 3 1 S8 receptor mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 2729 2616C>T 1 S8 receptor mRNA, complete cds NGFR M 14764 162010 GEN- Human nerve growth factor 2912 2799G>A 1 S8 receptor mRNA, complete cds NGFR M14764 162010 GEN- Human nerve growth factor 3252 31390G 1S8 receptor mRNA, complete cds N0S1 U 17327 163731 GEN-209 Human neuronal nitric 3391 2706OT oxide synthase (NOS1) mRNA, complete cds N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 1380 11550T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 1380 1155C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 1503 12780T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 1503 1278C>T S 3LW oxide synthase SD-144146.1 Page 10 N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2048 1823C>T S608L 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2048 1823C>T S608L 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2287 2062G>A G688S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2287 2062G>A G688S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2339 2114A>G D705G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2339 2114A>G D705G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2583 2358T>C S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2583 2358T>C S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2982 2757A>G S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 2982 2757A>G S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3022 2797C>G R933G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3022 2797C>G R933G 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3051 28260T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3051 2826C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3693 3468T>C 3 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3693 3468T>C 3 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3715 3490G>A 3 3LW oxide synthase N0S2A X73029 163730 GEN- H.sapiens mRNA for nitric 3715 3490G>A 3 3LW oxide synthase NRAS X02751 164790 GEN-XG Human N-ras mRNA and 221 (-506)A>G 5 flanking regions NRAS X02751 164790 GEN-XG Human N-ras mRNA and 390 (-337)C>A 5 flanking regions NTRK1 X66397 191315 GEN- H-sapiens tpr mRNA 2632 2335G>A V779I SD-144146.1 Page 10 3GN NTRK3 U05012 191316 GEN- Human receptor tyrosine 364 209G>A S70N 16V kinase TrkC (NTRK3) mRNA, complete cds NTRK3 U05012 191316 GEN- Human receptor tyrosine 728 573C>T 16V kinase TrkC (NTRK3) mRNA, complete cds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1613 1458C>T 16V kinase TrkC (NTRK3) mRNA, complete cds NTRK3 U05012 191316 GEN- Human receptor tyrosine 1643 1488G>C 16V kinase TrkC (NTRK3) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 216 (-265)T>G protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 802 322C>T protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 888 408C>T protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 934 454T>G S152A protein (OSBP) mRNA, complete cds PACE X17094 136950 GEN- Human fur mRNA for furin 399 183C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 1692 1476C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2067 1851C>G S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2725 2509T>C 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2855 2639C>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2988 2772G>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3234 3018C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3625 3409A>G 3 SD-144146.1 Page 10 PACE X17094 136950 GEN- Human fur mRNA for furin 3883 3667C>T 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 4053 3837A>G 1ZV PAM M37721 170270 GEN- Human peptidylglycine 3183 2995T>A 20K alpha-amidating monooxygenase mRNA, complete cds PAM M37721 170270 GEN- Human peptidylglycine 3530 3342A>G 20K alpha-amidating monooxygenase mRNA, complete cds PAX6 M77844 106210 GEN- H.sapiens oculorhombin 669 307C>T 3QG (aniridia) mRNA, complete cds PC U04641 266150 GEN-150 Human pyruvate 1391 13530T carboxylase (PC) mRNA, complete cds PC U04641 266150 GEN-150 Human pyruvate 2219 2181 C>T carboxylase (PC) mRNA, complete cds PC U04641 266150 GEN-150 Human pyruvate 2912 2874G>T carboxylase (PC) mRNA, complete cds PC U04641 266150 GEN-150 Human pyruvate 3897 3859C>T carboxylase (PC) mRNA, complete cds PCK1 L05144 261680 GEN-172 Homo sapiens (clone 1223 1102G>A V368I lamda-hPEC-3) phosphoenolpyruvate carboxykinase (PCK1) mRNA, complete cds PDHA1 X52709 312170 GEN- Human mRNA for brain 849 795A>G 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) PDHA1 X52709 312170 GEN- Human mRNA for brain 1337 1283C>T 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) PDHA1 X52709 312170 GEN- Human mRNA for brain 1416 1362G>A 33Y pyruvate dehydrogenase (EC 1.2.4.1 ) SD-144146.1 Page 10 PEDF M90439 172860 GEN- Human molecular marker 40 2T>C F 46E (EPC-1 ) gene, complete cds PEDF M90439 172860 GEN- Human molecular marker 215 177T>C S 46E (EPC-1 ) gene, complete cds PEDF M90439 172860 GEN- Human molecular marker 788 750C>T S 46E (EPC-1 ) gene, complete cds PEDF M90439 172860 GEN- Human molecular marker 900 862C>G R288G 46E (EPC-1 ) gene, complete cds PEDF M90439 172860 GEN- Human molecular marker 952 914G>T G305V 46E (EPC-1 ) gene, complete cds PHKG2 M31606 172471 GEN- Human phosphorylase 1155 1062C>G S 2H7 kinase (PSK-C3) mRNA, complete cds PNLIP M93285 246600 GEN- Pancreatic lipase (PNLIP) 646 646G>T V216L 48N (Dietary supplement) POMC M28636 176830 GEN- Adrenocorticotropic 92 92C>T 3 2DG hormone (ACTH) PREP X74496 600400 GEN- Prolyl Endopeptidase 390 390T>C S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1051 1051T>G L351V 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1 ι25 1125C>T S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1363 1363G>A V455M 3N8 PTHLH J03580 168470 GEN- Human, parathyroid-like 975 37G>A V13M 11 U protein (associated with humoral hypercalcemia of malignancy) mRNA, complete cds PTHLH J03580 168470 GEN- Human, parathyroid-like 996 58G>A V20M 11 U protein (associated with humoral hypercalcemia of malignancy) mRNA, complete cds PTPRF Y00815 179590 GEN-UH Human mRNA for LCA- 6939 6569A>G 3 SD-144146.1 Page 10 homolog. LAR protein (leukocyte antigen related) PYGB J03544 138550 GEN-11 L Human brain glycogen 718 639C>T S phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 2449 2370G>A S phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 2712 2633C>G 3 phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 3346 3267C>T 3 phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 3644 3565G>A 3 phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 3687 3608G>A 3 phosphorylase mRNA, complete cds PYGB J03544 138550 GEN-11 L Human brain glycogen 3770 3691 G>A 3 phosphorylase mRNA, complete cds PYGL M36807 232700 GEN- Human liver glycogen 702 702G>C R234S 2NJ phosphorylase type IV mRNA, 3 end PYGL M36807 232700 GEN- Human liver glycogen 1108 1108C>G 3 2NJ phosphorylase type IV mRNA, 3 end RAF1 X06409 164760 GEN- Human mRNA fragment for 486 487T>C 3 19K activated c-raf-1 (exons 8- 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1947 1948C>T 3 19K activated c-raf-1 (exons 8- 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1992 1993C>A 3 19K activated c-raf-1 (exons 8- 17) S63912 S63912 601233 GEN- D10S102=FBRNP [human, 2193 2163G>A 3 3EJ fetal brain, mRNA, 3043 nt] S70154 S70154 100678 GEN-GY ACAT2 669 632A>G K211 R SD-144146.1 Page 10 S70154 S70154 100678 GEN-GY ACAT2 820 783T>C S S70154 S70154 100678 GEN-GY ACAT2 820 783T>C S S70154 S70154 100678 GEN-GY ACAT2 856 819G>A S S70154 S70154 100678 GEN-GY ACAT2 856 819G>A S S70154 S70154 100678 GEN-GY ACAT2 1388 1351T>G 3 S70154 S70154 100678 GEN-GY ACAT2 1395 1358- 3 1362CTTTA> CTTTA S70154 S70154 100678 GEN-GY ACAT2 1395 1358- 1362delCTTT A S70154 S70154 100678 GEN-GY ACAT2 1419 1382C>A 3 S70154 S70154 100678 GEN-GY ACAT2 1419 1382C>A 3 S74445 S74445 180230 GEN- cellular retinoic acid- 134 60G>C S 3N7 binding protein [human, skin, mRNA, 735 nt] SLC5A1 M24847 182380 GEN- Human Na+/glucose 2226 2216C>T 283 cotransporter 1 mRNA, complete cds SLO U02632 600150 GEN-XA Calcium-activated 2377 2377T>G S793A potassium channel SOD2 X07834 147460 GEN- Human mRNA for 44 40C>G P14A 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SOD2 X07834 147460 GEN- Human mRNA for 51 47T>C V16A 1 ES manganese superoxide dismutase (EC 1.15.1.1) SOD2 X07834 147460 GEN- Human mRNA for 198 194C>A T65N 1 ES manganese superoxide dismutase (EC 1.15.1.1) SOD2 X07834 147460 GEN- Human mRNA for 249 245T>C I82T 1 ES manganese superoxide dismutase (EC 1.15.1.1 ) SORD U07361 182500 GEN- Homo sapiens sorbitol 606 465C>T 1 DR dehydrogenase gene, complete cds SORD U07361 182500 GEN- Homo sapiens sorbitol 857 716A>T Q239L 1 DR dehydrogenase gene, complete cds SORD U07361 182500 GEN- Homo sapiens sorbitol 1247 1106T>C SD-144146-1 Page 10 1 DR dehydrogenase gene, complete cds SORD U07361 182500 GEN- Homo sapiens sorbitol 1275 1134T>G 1 DR dehydrogenase gene, complete cds SPARC J03040 182120 GEN-ZC Human 70 13A>T I5F SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 123 66A>G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 184 127G>T V43L SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 559 502C>G R168G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 998 941 C>G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 1183 1126C>G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 1413 1356G>A SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 1551 1494C>G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 1922 1865G>T SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 2072 2015T>C SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 2092 2035A>G SPARC/osteonectin mRNA, complete cds SPARC J03040 182120 GEN-ZC Human 2104 2047A>C SPARC/osteonectin mRNA, complete cds SD-144146.1 Page 10 SPP1 X13694 166490 GEN- Human mRNA for 349 282T>C S 1 P2 osteopontin SPP1 X13694 166490 GEN- Human mRNA for 817 750C>T S 1 P2 osteopontin SPP1 X13694 166490 GEN- Human mRNA for 969 902G>A R301 H 1 P2 osteopontin SPP1 X13694 166490 GEN- Human mRNA for 1150 1083A>G 3 1 P2 osteopontin SPP1 X13694 166490 GEN- Human mRNA for 1306 1239A>C 3 1 P2 osteopontin SRD5A2 M74047 264600 GEN- Human steroid 5-alpha- 2379 2352A>G 3 CDC reductase 2 (SRD5A2) mRNA, complete cds STAR U 17280 600617 GEN-208 Human steroidogenic 1439 1313C>T 3 acute regulatory protein (StAR) mRNA, complete cds TBG M14091 314200 GEN- Human thyroxine-binding 901 571G>A D191 N 1QO globulin mRNA, complete cds TBG M14091 314200 GEN- Human thyroxine-binding 1239 909G>T L303F 1 QO globulin mRNA, complete cds TCF14 X76930 600281 GEN- H.sapiens HNF4 mRNA for 1325 1306C>T P436S 3PH hepatocyte nuclear factor 4 TF M 12530 190000 GEN- Human transferrin mRNA, 654 624G>A S 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 768 738C>G C246W 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1447 1417G>T V473F 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1602 1572G>C S 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1632 1602C>T S 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1795 1765C>T P589S 1 MK complete cds TGFBR2 M85079 190182 GEN- Human TGF-beta type II 2045 1710A>C 3 3ZS receptor mRNA, complete cds TGFBR3 L07594 600742 GEN- Human transforming 3966 3618G>C 3 SD-144146- 1 Page 10 1 EA growth factor-beta type III receptor (TGF-beta) mRNA, complete cds U00968 U00968 184756 GEN-UU Human SREBP-1 mRNA, 3983 3817G>A 3 complete cds U02031 U02031 600481 GEN-WD Human sterol regulatory 1089 972G>A S element binding protein-2 mRNA, complete cds U09648 U09648 600650 GEN-11 Camitine 2556 2040G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2675 2159G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2792 2276G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2825 2309G>A 3 Palmitoyltransferase II U09759 U09759 602896 GEN- Human protein kinase 303 152A>G N51S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1079 928A>G 1310V 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1280 1129C>T P377S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1559 1408C>T 3 1 HA (JNK2) mRNA, complete cds U16031 U16031 None GEN-HX Transcription Factor IL-4 2964 2799G>A 3 Stat U16660 U16660 600696 GEN- Human peroxisomal enoyl- 149 122A>C E41A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 402 375G>A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 802 7750G P259A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete SD-144146.1 Page 10 cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 1157 1130G>A 3 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U 19775 U 19775 600289 GEN- Human MAP kinase Mxi2 731 688G>A D230N 22C (MXI2) mRNA, complete cds U24183 U24183 232800 GEN-I9 Phosphofructokinase, 70 (-1204)G>A 5 muscle U24183 U24183 232800 GEN-I9 Phosphofructokinase, 237 (-1037)G>A 5 muscle U24183 U24183 232800 GEN-I9 Phosphofructokinase, 592 (-682)T>C 5 muscle U24183 U24183 232800 GEN-I9 Phosphofructokinase, 2662 1389T>G S muscle U24183 U24183 232800 GEN-I9 Phosphofructokinase, 2953 1680C>T 3 muscle U25029 U25029 138040 GEN-82 Glucocorticoid receptor 335 335C>T 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 386 386T>C 3 alpha U25029 U25029 138040 GEN-82 Glucocorticoid receptor 1069 1069C>T 3 alpha U26553 U26553 114131 GEN-66 Calcitonin Receptor 1412 1340C>T P447L U26553 U26553 114131 GEN-66 Calcitonin Receptor 1515 1443T>C 3 U32500 U32500 162642 GEN-1 P Neuropeptide Y2 407 159C>T S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1706 1458- 3 1460TAT>TA T U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1706 1458- 3 1460delTAT U32500 U32500 162642 GEN-1P Neuropeptide Y2 2782 2534 Λ 2535ins F CA U32989 U32989 191070 GEN- Human tryptophan 991 927G>A S 2JH oxygenase (TDO) mRNA, SD-144146.1 Page 10 complete cds U40002 U40002 151750 GEN- Human hormone-sensitive 2076 17990A P600H 2RH lipase testicular isoform mRNA, complete cds U40347 U40347 600950 GEN- Human serotonin N- 382 148G>A E50K 2RK acetyltransferase mRNA, complete cds U40396 U40396 602691 GEN-6W Steroid receptor 285 229A>C K77Q coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 314 258A>T K86N coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 336 280C>T P94S coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 688 632C>T T211 I coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 970 914C>A A30δE coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 1511 14δδG>A S coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 2377 2321 C>T T774M coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 2730 2674C>T P892S coactivator (SRC-1 ) U41078 U41078 600754 GEN- Human membrane-type 22 22C>T P8S 2SU matrix metalloproteinase-1 mRNA, complete cds U43142 U43142 601528 GEN- Human vascular 1499 1128C>T S 2UM endothelial growth factor related protein VRP mRNA, complete cds U48730 U48730 601511 GEN-JA Transcription Factor Statδb 494 484T>C S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 496 486A>G S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 499 489A>G S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 502 492G>A S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 570 560G>C G187A U48730 U48730 601511 GEN-JA Transcription Factor Statδb 573 563C>A P188Q U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1003 993G>A S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1063 1053T>C S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1066 10δ6G>A S SD-144146.1 Page 10 U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1105 109δOT S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1159 1149C>T S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1969 19δ9C>T S U49516 U49516 312861 GEN-1Q Serotonin 5-HT receptors 2915 2187A>C 3 5-HT2C U49516 U49516 312861 GEN-1Q Serotonin δ-HT receptors 2947 2219A>G δ-HT2C U62768 U62768 151300 GEN- Human oxytocinase splice 3356 329δG>C 3CR variant 1 mRNA, complete cds U62768 U62768 151300 GEN- Human oxytocinase splice 3547 3486C>T 3 3CR variant 1 mRNA, complete cds U71321 U71321 602623 GEN- Human FK506-binding 1248 109δC>T S 2TW protein FKBP51 mRNA, complete cds U71321 U71321 602623 GEN- Human FKδ06-binding 1425 1272G>A S 2TW protein FKBPδl mRNA, complete cds U94357 U94357 None GEN-498 Homo sapiens glycogenin- 1 δ95 1 δ9δC>T 3 2 delta (glycogenin-2) mRNA, partial cds U94357 U943δ7 None GEN-498 Homo sapiens glycogenin- 1844 1844A>C 3 2 delta (glycogenin-2) mRNA, partial cds UCP2 U76367 601693 GEN- Human uncoupling protein- 164 164C>T A55V 30V 2 (UCP2) mRNA, nuclear gene encoding mitochondrial protein, complete cds V00518 V00518 118850 GEN-P4 Human messenger RNA 56δ 51δT>C for chorionic gonadotropin V00δ19 V00619 139260 GEN-4U Growth hormone 1 299 259C>A P87T V00519 V00619 139250 GEN-4U Growth hormone 1 524 484G>T G162W V00566 V00δ66 176760 GEN-4V Prolactin 574 δ70G>A S V00571 V00671 122560 GEN- corticotropin releasing 822 637delA F CBO factor V00δ71 V00δ71 122560 GEN- corticotropin releasing 837 6δ2G>A 3 CBO factor VEGF M32977 192240 GEN-2JF Human heparin-binding 50 (-7)OT 5 SD-144146.1 Page 10 vascular endothelial growth factor (VEGF) mRNA, complete cds VEGF M32977 192240 GEN-2JF Human heparin-binding 92 36C>T vascular endothelial growth factor (VEGF) mRNA, complete cds VLDLR L20470 192977 GEN- Human very low density 336 (-56)C>T δ 23D lipoprotein receptor mRNA, complete cds VLDLR L20470 192977 GEN- Human very low density 3566 3175T>C 3 23D lipoprotein receptor mRNA, complete cds X00264 X00264 1 δ2780 GEN- Human beta-LH gene 1015 1016G>C 3 CC2 (luteinizing hormone gene beta subunit) X00264 X00264 162780 GEN- Human beta-LH gene 1033 1034C>A 3 CC2 (luteinizing hormone gene beta subunit) X00δ68 X00668 207750 GEN-6Z Apolipoprotein C-ll 70 70C>A Q24K X02317 X02317 147450 GEN-KM Superoxide dismutase 1 614 5δOA>C 3 (Cu/Zn) X02812 X02812 190180 GEN-XR Human mRNA for 870 29C>T P10L transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 979 138C>G I46M transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1632 791C>T T264I transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1807 966C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1930 1089G>A S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1942 1101C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 2013 1172G>A S391 N SD-144146 1 Page 10 transforming growth factor- beta (TGF-beta) X03172 X03172 192340 GEN-ZM Human mRNA for 379 356T>G V119G vasopressin precursor X03635 X03636 133430 GEN-60 estrogen receptors 390 30T>C S X03635 X0363δ 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 424 64G>C E22Q X03635 X03635 133430 GEN-50 estrogen receptors 617 257C>T A86V X03635 X0363δ 133430 GEN-50 estrogen receptors 621 261 G>C S X03635 X0363δ 133430 GEN-50 estrogen receptors 829 4690T F X0363δ X0363δ 133430 GEN-50 estrogen receptors 133δ 975C>G S X03636 X03636 133430 GEN-50 estrogen receptors 1335 97δC>G S X03635 X03636 133430 GEN-50 estrogen receptors 1451 1091T>A V364E X03635 X03635 133430 GEN-50 estrogen receptors 1674 1314G>A M438I X03635 X03635 133430 GEN-50 estrogen receptors 2142 1782A>G S X0363δ X0363δ 133430 GEN-δO estrogen receptors 2354 1994A>G 3 X0363δ X0363δ 133430 GEN-δO estrogen receptors 25δ0 2190A>C 3 X03635 X03635 133430 GEN-δO estrogen receptors 2733 2373C>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 3181 2821T>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 3338 2978C>T 3 X03635 X03635 133430 GEN-50 estrogen receptors 36δ2 3292- 3 3294CCT>CC T X03636 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3 3294delCCT X03636 X03635 133430 GEN-50 estrogen receptors 3896 3δ36C>A 3 X03635 X03636 133430 GEN-50 estrogen receptors 4378 4018T>C 3 X03635 X0363δ 133430 GEN-50 estrogen receptors 6287 δ927T>C 3 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 363 3δ1C>T S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding δ25 513C>T protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 967 9550A R319S protein (G protein), alpha SD-144146.1 Page 10 stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1023 1011OA s protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1083 1071C>T s protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1213 1201T>G 3 protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1460 1438A>C 3 protein (G protein), alpha stimulating activity polypeptide 1 X04707 X04707 190160 GEN- Human c-erb-A mRNA for 129δ 99δT>C I332T CCA thyroid hormone receptor X0δ199 X06199 173350 GEN-PU Human mRNA for 384 330C>T S plasminogen X0δ199 X06199 173350 GEN-PU Human mRNA for 82δ 771 C>T S plasminogen X06199 X06199 173350 GEN-PU Human mRNA for 996 9420T S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 1137 1083A>G S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 1485 14310T S plasminogen X06199 X06199 173350 GEN-PU Human mRNA for 2340 2286T>G S plasminogen X06199 X06199 173350 GEN-PU Human mRNA for 2532 2478G>A 3 plasminogen X06199 X06199 173350 GEN-PU Human mRNA for 2606 2δδ2T>G 3 plasminogen X06344 X06344 116840 GEN-PW Human mRNA for 1683 1δ81 C>G 3 cathepsin D from oestiogen responsive breast cancer cells X06344 X06344 1 16840 GEN-PW Human mRNA for 1703 1701 C>T 3 SD-144146 1 Page 10 cathepsin D from oestrogen responsive breast cancer cells X05344 X05344 116840 GEN-PW Human mRNA for 17δ4 1752G>A cathepsin D from oestrogen responsive breast cancer cells X05344 X05344 116840 GEN-PW Human mRNA for 1798 1796A>C cathepsin D from oestrogen responsive breast cancer cells X05344 X05344 1 16840 GEN-PW Human mRNA for 1837 1835A>C cathepsin D from oestrogen responsive breast cancer cells X05344 X06344 116840 GEN-PW Human mRNA for 1901 1899C>T cathepsin D from oestrogen responsive breast cancer cells X06344 X06344 116840 GEN-PW Human mRNA for 197δ 1973T>G cathepsin D from oestrogen responsive breast cancer cells X0δ61δ X05615 188450 GEN-188 Human mRNA for δ94δ δ904G>A S thyroglobulin X05615 X05615 188450 GEN-188 Human mRNA for 7627 7δ86G>A 2529Q thyroglobulin X05615 X05615 188450 GEN-1. Human mRNA for 7704 7663G>T V2655F thyroglobulin X0561δ X05616 1884δ0 GEN-188 Human mRNA for 79δ8 7917C>T S thyroglobulin X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 83 (-54)G>C 5 X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 940 804G>A S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1327 1191T>C S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1906 1770C>T S X06662 X06662 600946 GEN-6D Growth hormone receptor 3392 3349A>T 3 X06662 X06562 600946 GEN-6D Growth hormone receptor 4145 4102G>A 3 X07549 X07549 116820 GEN- Human mRNA for 276 244T>C 3 1 DZ cathepsin H (E.C.3.4.22.16.) SD-144146.1 Page 10 X07549 X07δ49 116820 GEN- Human mRNA for 664 632G>A 3 1 DZ cathepsin H (E.C.3.4.22.16.) X07649 X07649 116820 GEN- Human mRNA for 1006 974G>A 3 1 DZ cathepsin H (E.C.3.4.22.16.) X07649 X07549 116820 GEN- Human mRNA for 1029 997G>A 3 1 DZ cathepsin H (E.C.3.4.22.16.) X13589 X13589 107910 GEN-56 Cytochrome P450, 364 240A>G S subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-δ6 Cytochrome P4δ0, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13689 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13689 X13689 107910 GEN-56 Cytochrome P450, 165δ 1531C>T 3 subfamily XIX (aromatization of androgens) X13689 X13689 107910 GEN-56 Cytochrome P450, 1796 1672G>T 3 subfamily XIX (aromatization of androgens) X13629 X13629 107690 GEN- Human intestinal mRNA for 881 836G>A R279K 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1185 1140G>T Q380H 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1302 12δ7 Λ 12δ8ins F 100 apolipoprotein A-IV CTGT X13916 X13916 107770 GEN- Human mRNA for LDL- 1636 1170T>C S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 1675 1209C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 2805 2339C>T T780I 101 receptor related protein SD-144146.1 Page 109 X13916 X13916 107770 GEN- Human mRNA for LDL- 38δ3 3387T>C S 1Q1 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 6443 δ977C>T R1993W 1Q1 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 7036 6δ70C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 8608 8142G>A S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 8923 84δ7C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9034 8δ68G>T S 1Q1 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9040 8574C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9391 8925T>C S 101 receptor related protein X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 1066 1023G>C M341I KUV natriuretic peptide receptor (ANP-A receptor) X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 1667 1614C>T KUV natriuretic peptide receptor (ANP-A receptor) X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 28δ9 2816G>A R939Q KUV natriuretic peptide receptor (ANP-A receptor) X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 2983 2940G>A KUV natriuretic peptide receptor (ANP-A receptor) X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 3269 3216delC KUV natriuretic peptide receptor (ANP-A receptor) X1δ3δ7 X1δ3δ7 108960 GEN- Human mRNA for 3589 3δ46 Λ 3δ47ins F KUV natriuretic peptide receptor GAAA (ANP-A receptor) Xδ1362 X61362 126460 GEN- Dopamine Receptor D2 588 423G>A S 31W X61362 Xδ1362 126460 GEN- Dopamine Receptor D2 1104 939C>T S 31W X61362 X61362 126460 GEN- Dopamine Receptor D2 1122 9δ7T>C S 31W X61362 X61362 126450 GEN- Dopamine Receptor D2 1248 1083A>G S SD-144146.1 Page 10 31W X61362 X51362 126450 GEN- Dopamine Receptor D2 1488 1323T>C S 31W X61362 X61362 126450 GEN- Dopamine Receptor D2 1648 1383A>G 3 31W X61362 X61362 126450 GEN- Dopamine Receptor D2 2361 2196C>T 3 31W X51416 X51416 601998 GEN-57 STEROID HORMONE 228δ 2222G>A 3 RECEPTOR ERR1 X52773 X52773 180245 GEN-74 Retinoid X receptor, alpha 1744 1669G>A 3 XδδOOδ X55006 190120 GEN- Human c-erbA-1 mRNA for 493 27A>G S 3δS thyroid hormone receptor alpha X55005 X55005 190120 GEN- Human c-erbA-1 mRNA for 1523 10δ7G>A V353I 3δS thyroid hormone receptor alpha X59498 X59498 176300 GEN-RU H sapiens ttr mRNA for 92 71G>A G24D transthyretin X59498 X59498 176300 GEN-RU H sapiens ttr mRNA for 177 156G>T S transthyretin X59498 X59498 176300 GEN-RU H sapiens ttr mRNA for 380 3δ9C>T S120F transthyretin X69842 X69842 600214 GEN- Human PBX2 mRNA 2339 2043T>G 3 3A3 X63369 X63369 600070 GEN- H sapiens UGT2BIO 1516 1506OT S 3DC mRNA for udp glucuronosyltransferase X63369 X63359 600070 GEN- H sapiens UGT2BIO 2714 2704G>A 3 3DC mRNA for udp glucuronosyltransferase X63622 X63522 180246 GEN-76 MHC class I promoter 1331 1152T>C S binding protein X68596 X68596 168468 GEN-3IJ H sapiens mRNA for 1δ63 1389T>C S parathyroid hormone receptor X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 112 21T>C S squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 292 201 C>T S squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1436 134δT>C 3 squalene synthase SD-144146 1 Page 10 X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1679 1488T>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1621 1530C>T 3 squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1719 1628A>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H.sapiens mRNA for 1904 1813G>C 3 squalene synthase X69699 X69699 167415 GEN- H-sapiens Pax8 mRNA 1412 1413G>C 3 3JS X69699 X69699 167415 GEN- H-sapiens Pax8 mRNA 2164 2165T>G 3 3JS X69699 X69699 167415 GEN- H-sapiens Pax8 mRNA 2δ08 2509T>C 3 3JS X69699 X69699 167415 GEN- H.sapiens Pax8 mRNA 2514 2δ1δA>C 3 3JS X69699 X69699 167415 GEN- H.sapiens Pax8 mRNA 2552 2δδ3A>C 3 3JS X70811 X70811 109691 GEN- beta-3-adrenergic receptor 315 190T>C W64R 3KK X70811 X70811 109691 GEN- beta-3-adrenergic receptor 315 190T>C W64R 3KK X71440 X71440 None GEN- H.sapiens mRNA for 949 936G>C M312I 3KS peroxisomal acyl-CoA oxidase X76958 X75958 600456 GEN- H.sapiens trkB mRNA for 30 (-68)C>G δ 30E protein-tyrosine kinase X75968 X75968 600456 GEN- H.sapiens trkB mRNA for 2010 1913A>G 3 30E protein-tyrosine kinase X76958 X75958 600456 GEN- H.sapiens trkB mRNA for 2101 2004C>T 3 30E protein-tyrosine kinase X76180 X76180 600228 GEN-N5 Solute carrier family 9 1901 1802G>A G601D (sodium/hydrogen exchanger), isoform 1 (antiporter, Na+/H+, amiloride sensitive) X77383 X77383 600δδ0 GEN- H.sapiens mRNA for 1595 1δ46C>T 3 3PT cathepsin-0 X77533 X77533 602730 GEN- H.sapiens mRNA for 1462 14δ8C>T S 3Q3 activin type II receptor X78873 X78873 601792 GEN- H.sapiens mRNA for 538 δ3δG>A D179N SD-144146.1 Page 11 3RQ inhibitor 2 gene X78873 X78873 601792 GEN- H.sapiens mRNA for 812 809G>A 3 3RQ inhibitor 2 gene X79483 X79483 602399 GEN- H.sapiens ERK6 mRNA for 1287 12δ4T>G 3 LPR extracellular signal regulated kinase X79537 X79537 603942 GEN- H.sapiens mRNA for 635 δδ2G>A S 3TA glycogenin X79537 X79537 603942 GEN- H.sapiens mRNA for 1381 1298A>G 3 3TA glycogenin X83368 X83368 601232 GEN- H.sapiens mRNA for 3884 3661 C>T 3 3XT phosphatidylinositol 3 kinase gamma X87212 X87212 602366 GEN- H.sapiens mRNA for 318 28δG>T S 42U cathepsin C X87212 X87212 602366 GEN- H.sapiens mRNA for 870 837G>C Q279H 42U cathepsin C X87212 X87212 602366 GEN- H.sapiens mRNA for 1390 13δ7A>G I463V 42U cathepsin C X87212 X87212 602366 GEN- H.sapiens mRNA for 1758 1725A>C 3 42U cathepsin C X92521 X92621 601807 GEN-480 H.sapiens mRNA for MMP- 1722 1621T>G 3 19 protein X92720 X92720 261660 GEN-484 H.sapiens mRNA for 1494 1428A>C R476S phosphoenolpyruvate carboxykinase X95190 X96190 601641 GEN- H.sapiens mRNA for 1394 1302C>T S 49Y Branched chain Acyl-CoA Oxidase X95190 X96190 601641 GEN- H.sapiens mRNA for 1934 1842C>A S 49Y Branched chain Acyl-CoA Oxidase Y00285 Y00285 147280 GEN-6I IGF-2 receptor 4613 4466G>A S1489N Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6371 62240T T2076M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6813 6666C>T S Y00285 Y00285 147280 GEN-6I IGF-2 receptor 7160 7003G>A V2335M Y0028δ Y0028δ 147280 GEN-6I IGF-2 receptor 868δ 85380A 3 Y00406 Y00406 274600 GEN-6J Peroxidase (thyoid) 218δ 214δT>C S Y00406 Y00406 274600 GEN-6J Peroxidase (thyoid) 2213 2173C>A P725T Y00406 Y00406 274600 GEN-6J Peroxidase (thyoid) 2680 2δ40C>T A847V SD-144146.1 Page 1 10 Y00406 Y00406 274500 GEN-6J Peroxidase (thyoid) 2923 2883C>G 3 Y00749 Y00749 131240 GEN-P7 Endothelin 1 846 594G>T K198N Y08110 Y08110 602005 GEN- H.sapiens mRNA for 3641 3δ61T>G S 1FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H-sapiens mRNA for 3818 3738C>T S 1FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H.sapiens mRNA for 5158 δ078G>A S1693N 1FK mosaic protein LR11 Y08110 Y08110 602006 GEN- H.sapiens mRNA for 6571 6491 G>A R2164K 1FK mosaic protein LR11 Y100δδ YlOOδδ 602839 GEN-1IC H.sapiens mRNA for 954 7δ8G>A S253N phosphoinositide 3-kinase Y10065 Y10055 602839 GEN-1IC H.sapiens mRNA for 2491 2295C>T S phosphoinositide 3-kinase Y10056 Y10056 602839 GEN-1IC H.sapiens mRNA for 3004 2808C>T S phosphoinositide 3-kinase Y11625 Y11626 116897 GEN- H.sapiens mRNA for 922 773C>T A258V 1KR CCAAT/enhancer binding protein alpha Y11526 Y11626 116897 GEN- H-sapiens mRNA for 1007 858G>A 1KR CCAAT/enhancer binding protein alpha Y11δ2δ Y11δ2δ 116897 GEN- H.sapiens mRNA for 1441 1292G>A 3 1KR CCAAT/enhancer binding protein alpha Y11626 Y11δ2δ 116897 GEN- H.sapiens mRNA for 2327 2178T>C 3 1KR CCAAT/enhancer binding protein alpha Y16409 Y16409 602671 GEN- Homo sapiens mRNA for 1393 1224G>A S 1U1 putative glucose 6- phosphate translocase Y16409 Y16409 602671 GEN- Homo sapiens mRNA for 1δ84 141δC>G 3 1U1 putative glucose 6- phosphate translocase Y15409 Y16409 602671 GEN- Homo sapiens mRNA for 1877 1708C>T 3 1U1 putative glucose 6- phosphate translocase Y15621 Y15521 None GEN- Homo sapiens ASMTL 1622 1622A>G K641R MEN gene Z1169δ Z11695 176948 GEN-1L1 H.sapiens 40 kDa protein 1287 11δ3G>A 3 kinase related to rat ERK2 SD-144146.1 Page 11 Z11696 Z11696 601795 GEN-1 L0 H.sapiens 44kDa protein 449 449T>G I150S kinase related to rat ERK1 Z82022 Z82022 191350 GEN- H.sapiens mRNA for 1266 1153A>G I385V 3WH GlcNac-1-P transferase Z82022 Z82022 191350 GEN- H-sapiens mRNA for 1491 1388G>A 3 3WH GlcNac-1-P transferase Z82022 Z82022 191350 GEN- H.sapiens mRNA for 1723 1620T>C 3 3WH GlcNac-1-P transferase Table 17. Identified Variances In Genes for Pathways Identified in Endocrine and Metabolic Disease and Related Disorders AB00026 AB00026 602784 GEN- Human mRNA for prepro 215 210T>C S 3 3 16N cortistatin like peptide, complete cds AB00102 AB00102 180903 GEN- Homo sapiens mRNA for 14689 14603T>G 3 5 δ 18S brain ryanodine receptor, complete cds AB00102 AB00102 180903 GEN- Homo sapiens mRNA for 15621 15435G>A 3 5 δ 18S brain ryanodine receptor, complete cds AB00132 AB00132 600170 GEN- Human AQP3 gene for 1203 1143G>A 3 5 5 KYP aquaporine 3 (water channel), partail cds AB00628 AB00528 300136 GEN- Homo sapiens mRNA for 2137 2069A>T H690L 9 9 KVU ABC transporter 7 protein, complete cds AB00629 AB00629 170290 GEN-W4 Homo sapiens mRNA for 2197 2073A>T 3 SD-144146.1 Page 1 1 3 3 peπϊipin, complete cds AB00942 AB00942 600130 GEN- Homo sapiens gene for 1016 534C>T S 6 6 MDN apobec-1 AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1071 1010T>A 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1073 1012T>C 3 0 0 1SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 1801 1740A>G 3 0 0 1SQ lectin-like oxidized LDL receptor, complete cds AB01071 AB01071 602601 GEN- Homo sapiens mRNA for 2199 2138G>A 3 0 0 1 SQ lectin-like oxidized LDL receptor, complete cds AB02068 AB02068 None GEN- Homo sapiens mRNA for 3864 3854A>G 3 0 0 LAX KIAA0873 protein, partial cds AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 365 365C>T P122L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 381 381 G>A S P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 624 624A>G S P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 641 641 C>T P214L P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000234 AF000234 600846 GEN-16J PURINERGIC RECEPTOR 1 161 1161T>C 3 P2X, LIGAND-GATED ION CHANNEL, 4; P2RX4 AF000671 AF000671 192600 GEN- K+ channel (KvLQTI) 545 435C>T S 15U AF000671 AF000671 192600 GEN- K+ channel (KvLQTI ) 1748 1638G>A S 15U AF000671 AF000671 192600 GEN- K+ channel (KvLQTI ) 2360 2250G>A 3 SD- 144146.1 Page 1 1 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 2552 2442C>T 3 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 3016 2906A>G 3 15U AF000571 AF000571 192500 GEN- K+ channel (KvLQTI ) 3073 2963A>G 3 15U AF001174 AF001174 602898 GEN- Homo sapiens p38beta2 1044 1038T>C S 18T MAP kinase mRNA, complete cds AF004709 AF004709 602899 GEN-UX Homo sapiens stress- 432 384G>A S activated protein kinase 4 mRNA, complete cds AF005043 AF005043 603501 GEN-VX Homo sapiens poly(ADP- 1916 1750G>A A584T ribose) glycohydrolase (hPARG) mRNA, complete cds AF005043 AF005043 603501 GEN-VX Homo sapiens poly(ADP- 3780 3614C>G 3 ribose) glycohydrolase (hPARG) mRNA, complete cds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 808 808C>G H270D 1 HV caspase Mch5-beta mRNA, alternatively spliced, complete cds AF009620 AF009620 601763 GEN- Homo sapiens apoptotic 915 915G>A S 1 HV caspase Mch5-beta mRNA, alternatively spliced, complete cds AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1023 987T>C S 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1025 989T>C F330S 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1090 1054G>C E352Q 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF0 6709 602836 GEN- PURINERGIC RECEPTOR 1321 1285G>A 3 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 SD-144146.1 Page 1 1 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1424 1388C>G 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1512 1476G>A 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1743 1707A>G 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF016709 AF016709 602836 GEN- PURINERGIC RECEPTOR 1858 1822A>G 1 NE P2X, LIGAND-GATED ION CHANNEL, 5; P2RX5 AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 781 781G>A 2A5 binding protein (BAD) mRNA, partial cds AF021792 AF021792 603167 GEN- Homo sapiens Bcl-X/Bcl-2 883 883C>A 2A5 binding protein (BAD) mRNA, partial cds HRH1 AF026261 600167 GEN- Histamine receptor H1 1068 1068A>G S 26W AVPR1B AF030512 600264 GEN- Homo sapiens small cell 273 150G>A S 4FF vasopressin subtype 1 b receptor mRNA, complete cds AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 314 291 OT S AF030625 AF030625 600821 GEN-2 Vasopressin V1 A receptor 431 408T>C S AF030625 AF030625 600821 GEN-2 Vasopressin V1A receptor 506 483A>G S ITGA7 AF032108 600536 GEN- Homo sapiens integrin 527 366G>A S 2NO alpha-7 mRNA, complete cds AF033850 AF033850 602384 GEN- Homo sapiens 795 634C>T R212C 20B phospholipase D2 (PLD2) mRNA, complete cds AF033850 AF033850 602384 GEN- Homo sapiens 2531 2370G>A S 20B phospholipase D2 (PLD2) mRNA, complete cds AF033850 AF033850 602384 GEN- Homo sapiens 3290 3129C>T 3 20B phospholipase D2 (PLD2) mRNA, complete cds AF037335 AF037335 603263 GEN- Homo sapiens carbonic 1551 1436G>T 3 2KJ anhydrase precursor (CA SD-144146.1 Page 11 12) mRNA, complete cds AF037335 AF037335 603263 GEN- Homo sapiens carbonic 2442 2327C>T 3 2KJ anhydrase precursor (CA 12) mRNA, complete cds AF038955 AF038955 600874 GEN-LEI Homo sapiens G protein 490 453A>T 3 gamma 5 subunit mRNA, complete cds AF041381 AF041381 602944 GEN- Homo sapiens putative 1214 1214C>T 3 LG 1 transcriptional repressor E2F-6 mRNA, partial cds AF052692 AF052692 603324 GEN- Homo sapiens connexin 31 2302 1169A>G 3 MKO (GJB3) mRNA, complete cds AF052692 AF052692 603324 GEN- Homo sapiens connexin 31 2438 1305T>C 3 MKO (GJB3) mRNA, complete cds AF052692 AF052692 603324 GEN- Homo sapiens connexin 31 2504 1371G>C 3 MKO (GJB3) mRNA, complete cds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1972 1663G>A 3 LJY phospholipase A2-gamma mRNA, complete cds AF058921 AF058921 None GEN- Homo sapiens cytosolic 1989 1680A>T 3 LJY phospholipase A2-gamma mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 1695 1647C>T S KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4037 3989C>T A1330V KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4683 4635C>A S KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds AF064548 AF064548 603506 GEN- Homo sapiens low-density 4802 4754C>T S1585L KV4 lipoprotein receptor-related protein 5 (LRP5) mRNA, complete cds SD-144146.1 Page 1 1 AF084040 AF084040 107940 GEN- Homo sapiens beta- 986 986A>T E329V LQ9 arrestin 1 A mRNA, complete cds AF084040 AF084040 107940 GEN- Homo sapiens beta- 1279 1279G>A LQ9 arrestin 1 A mRNA, complete cds AJ005162 AJ005162 600067 GEN- Homo sapiens mRNA for 1915 1882A>C KVT UDP- glucuronosyltransferase AJ224538 AJ224538 602741 GEN-243 Homo sapiens mRNA for 631 631 C>T H211Y AMP-activated protein kinase beta 2 subunit D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 149 100G>A D34N D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 341 292G>T V98L D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 479 430A>T N144Y D00017 D00017 151740 GEN-2D Lipocortin II (Annexin II) 1288 1239G>A 3 ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 1059 741A>C S 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 1059 741A>C 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 1428 1110G>A S 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 2538 2220T>C S 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3324 3006C>T S 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3375 3057G>A S 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3397 3079G>A 3 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3408 3090OA 3 4E8 Na,K-ATPase alpha- subunit, complete cds SD-144146.1 Page 11 ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3505 3187C>A 3 4E8 Na,K-ATPase alpha- subunit, complete cds ATP1A1 D00099 182310 GEN- Homo sapiens mRNA for 3538 3220G>T 3 4E8 Na,K-ATPase alpha- subunit, complete cds FECH D00726 177000 GEN-UB Human mRNA for 827 798G>C S ferrochelatase (EC 4.99.1.1 ) FECH D00726 177000 GEN-UB Human mRNA for 1253 1224T>A N408K ferrochelatase (EC 4.99.1.1 ) FECH D00726 177000 GEN-UB Human mRNA for 1549 1520C>T 3 ferrochelatase (EC 4.99.1.1 ) FECH D00726 177000 GEN-UB Human mRNA for 1645 1616G>A 3 ferrochelatase (EC 4.99.1.1) D13138 D13138 179780 GEN- Human mRNA for 566 523T>G S175A 1 NW dipeptidase CYP11 B2 D13752 124080 GEN- Human CYP11 B2 gene for 1600 1593G>A 3 CCD steroid 18-hydroxylase, complete cds D14874 D14874 103275 GEN- Human mRNA for 1293 1137A>G 3 1 SG adrenomedullin, complete cds D14874 D14874 103275 GEN- Human mRNA for 1394 1238A>C 3 1 SG adrenomedullin, complete cds HADHB D16481 143450 GEN- Human mRNA for 871 825T>C S 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1607 1561G>C 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1908 1862A>C 1Y5 mitochondrial 3-ketoacyl- SD-144146.1 Page 1 1 CoA thiolase beta-subunit of trifunctional protein, complete cds HADHB D16481 143450 GEN- Human mRNA for 1911 1865A>C 3 1Y5 mitochondrial 3-ketoacyl- CoA thiolase beta-subunit of trifunctional protein, complete cds D21243 D21243 141251 GEN-9C Heme oxygenase 828 828C>G S (decycling) 2 D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1035 599T>G I200S 1c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039OT R347C 1c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 1475 1039C>T R347C 1c D25235 D25235 104221 GEN-3 Adrenergic receptor alpha 2048 1612C>T 3 1c D25418 D25418 600022 GEN-78 Prostaglandin I2 726 635G>A R212H (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1047 956C>G S319W (prostacyclin) receptor (IP) D25418 D25418 600022 GEN-78 Prostaglandin 12 1075 984A>C S (prostacyclin) receptor (IP) PTGIR D38128 600022 GEN- Human IP gene for 203 204C>G 3 4DH prostacyclin receptor, exon 3 PTGIR D38128 600022 GEN- Human IP gene for 231 232C>A 3 4DH prostacyclin receptor, exon 3 D38145 D38145 601699 GEN- Human mRNA for 1646 1619T>C 3 4E3 prostacyclin synthase, complete cds D42108 D42108 600597 GEN- Phospholipase C epsilon 1908 1705G>A V569I 2U4 D42108 D42108 600597 GEN- Phospholipase C epsilon 2864 2661 G>A S 2U4 D42108 D42108 600597 GEN- Phospholipase C epsilon 4453 4250G>A 3 2U4 D45906 D45906 601988 GEN- Human mRNA for LIMK-2, 1323 1209G>C S 2WP complete cds SD-144146.1 Page 1 1 D45906 D45906 601988 GEN- Human mRNA for LIMK-2, 1475 13610T S454L 2WP complete cds D49394 D49394 182139 GEN-5 Serotonin 5-HT receptors 1914 1695C>G 3 5-HT3 D50678 D50678 602600 GEN- Human mRNA for 3378 3276G>A 3 SOY apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 3755 3653G>A 3 SOY apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 3949 3847G>C 3 SOY apolipoprotein E receptor 2, complete cds D50678 D50678 602600 GEN- Human mRNA for 4368 4266T>A SOY apolipoprotein E receptor 2, complete cds D50678 D50678602600 GEN- Human mRNA for 4455 4353G>A SOY apolipoprotein E receptor 2, complete cds D67031 D67031 601568 GEN- Homo sapiens ADDL 1441 1258G>A V420M 3HA mRNA for adducin-like protein, complete cds D67031 D67031 601568 GEN- Homo sapiens ADDL 2782 2599T>C 3HA mRNA for adducin-like protein, complete cds D87258 D87258 602194 GEN- Homo sapiens mRNA for 150 102C>T 42R serin protease with IGF- binding motif, complete cds D87461 D87461 601931 GEN- Human mRNA for 2432 2256C>A 43N KIAA0271 gene, complete cds D87812 D87812 600528 GEN-6 Camitine 2363 2344T>C Palmitoyltransferase I (muscle) D87845 D87845 602344 GEN- Human mRNA for platelet- 2299 2096G>A 44C activating factor acetylhydrolase 2, complete cds D87845 D87845 602344 GEN- Human mRNA for platelet- 2332 2129A>G 44C activating factor acetylhydrolase 2, SD-144146.1 Page 1 1 complete cds D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 434 (-1284)A>T 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 889 (-829)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 1156 (-562)G>C 5 D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2644 927T>C S D89078 D89078 601531 GEN-7 P2Y7 purinoceptor 2920 1203A>G 3 LRP1 D90070 107770 GEN-466 Human ATL-derived PMA- 686 513T>G 3 responsive (APR) peptide mRNA D90187 D90187 153622 GEN-6M Macrophage scavenger 1414 1368T>G 3 receptor 1 D90187 D90187 153622 GEN-6M Macrophage scavenger 1532 1486A>G 3 receptor 1 D90187 D90187 153622 GEN-6M Macrophage scavenger 1558 1512G>A 3 receptor 1 D90187 D90187 153622 GEN-6M Macrophage scavenger 1599 1553A>G 3 receptor 1 D90187 D90187 153622 GEN-6M Macrophage scavenger 1642 1596T>C 3 receptor 1 D90187 D90187 153622 GEN-6M Macrophage scavenger 1689 1643G>C 3 receptor 1 D90228 D90228 203750 GEN- ACAT1 547 471 C>A S 46A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1449 969C>T S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1485 1005A>G S 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 1834 1354C>G 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2228 1748G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2376 1896G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 SD-144146.1 Page 11 4DX EDNRA D90348 131243 GEN- Endothelin Receptor Type 2764 2284G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2840 2360G>C 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 2935 2455G>A 3 4DX A EDNRA D90348 131243 GEN- Endothelin Receptor Type 3294 2814A>G 3 4DX A FGA J00127 134820 GEN-T3 Human fibrinogen alpha- 560 530T>A I177N chain mRNA, complete cds FGA J00127 134820 GEN-T3 Human fibrinogen alpha- 1138 1108G>T A370S chain mRNA, complete cds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 543 543C>T S chain mRNA, partial cds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 1101 1101 OT S chain mRNA partial cds J00129 J00129 134830 GEN-T4 Human fibrinogen beta- 1409 1409G>A R470K chain mRNA, partial cds J00137 J00137 306900 GEN-OX COAGULATION FACTOR 581 580A>G T194A IX J00277 J00277 190020 GEN- Human (genomic clones 81 81T>C S MH8 lambda-[SK2-T2, HS578T], cDNA clones RS-[3,4, 6]) c-Ha-ras1 proto-oncogene, complete coding sequence J02610 J02610 107730 GEN-6N Apolipoprotein B (including 1931 1853T>C V618A Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 6616 6538C>T F Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 7014 6936T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 7623 7545T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 8294 8216C>T P2739L Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 8625 8547T>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10033 9955G>C D3319H Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10358 10280C>A T3427K SD- 144146 Page 11 Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 10372 10294C>G Q3432E Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11273 11195T>C I3732T Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11705 11627C>T A3876V Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11862 11784T>A S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 11923 11845T>C F3949L Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12461 12383A>T E4128V Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12476 12398G>C G4133A Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12486 12408G>C S Ag(x) antigen) J02610 J02610 107730 GEN-6N Apolipoprotein B (including 12619 12541 G>A E4181 K Ag(x) antigen) J02611 J02611 107740 GEN-60 Human apolipoprotein D 676 615T>G 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 683 622T>G 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 701 640C>G 3 mRNA, complete cds J02611 J02611 107740 GEN-60 Human apolipoprotein D 745 684A>G 3 mRNA, complete cds J03004 J03004 139360 GEN-79 Guanine nucleotide binding 758 681 C>T S protein (G protein), alpha inhibiting activity polypeptide 2 GNAI1 J03005 139370 GEN-ZI Human alternative guanine 1437 1429G>A 3 nucleotide-binding regulatory protein (G) alpha-inhibitory-subunit mRNA, complete cds J03019 J03019 109630 GEN- Human beta-1 -adrenergic 503 417G>A S 4D6 receptor mRNA, complete cds J03037 J03037 259730 GEN-2I Carbonic anhydrase II 627 562C>T S J03037 J03037 259730 GEN-2I Carbonic anhydrase II 1334 1269A>C 3 SD-144146. Page 1 1 J03037 J03037 259730 GEN-2I Carbonic anhydrase II 1487 1422A>C 3 J03048 J03048 142290 GEN-ZD Huma hemopexin mRNA, 3 244 244C>T R82W end J03048 J03048 142290 GEN-ZD Huma hemopexin mRNA, 3 635 635G>A R212K end J03225 J03225 152310 GEN-ZZ Human lipoprotein- 1189 1057G>A 3 associated coagulation inhibitor mRNA, complete cds J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 932 380G>A R127H J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1063 511G>A A171T J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1190 638C>G 3 J03242 J03242 147470 GEN-PJ Insulin-like growth factor 2 1201 649C>T 3 J03250 J03250 172420 GEN-C4 DNA topoisomerase I 160 (-52)C>T 5 J03250 J03250 172420 GEN-C4 DNA topoisomerase I 590 379G>A V127I J03250 J03250 172420 GEN-C4 DNA topoisomerase I 1984 1773G>A S J03260 J03260 139160 GEN-7A Guanine nucleotide binding 1491 1479A>G 3 protein (G protein), alpha z polypeptide J03260 J03260 139160 GEN-7A Guanine nucleotide binding 2541 2529T>C protein (G protein), alpha z polypeptide J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 140 72G>T S J03459 J03459 151570 GEN-8 Leukotriene A4 hydrolase 1511 1443A>T E481 D C7 J03507 217070 GEN- Human complement 1951 1951G>A V651 I 11 R protein component C7 mRNA, complete cds C7 J03507 217070 GEN- Human complement 3032 3032T>C 3 11 R protein component C7 mRNA, complete cds C7 J03507 217070 GEN- Human complement 3634 3634A>G 3 11 R protein component C7 mRNA, complete cds 07 J03507 217070 GEN- Human complement 3831 3831A>G 3 11 R protein component C7 mRNA, complete cds LIPC J03540 151670 GEN-11 J Human hepatic lipase 469 465T>G S mRNA, complete cds LIPC J03540 151670 GEN-11J Human hepatic lipase 595 591A>G S mRNA, complete cds SD-144146. Page 11 LIPC J03540 151670 GEN-11J Human hepatic lipase 648 644G>A S215N mRNA, complete cds LIPC J03540 151670 GEN-11J Human hepatic lipase 817 813C>T S mRNA, complete cds LIPC J03540 151670 GEN-11 J Human hepatic lipase 1441 1437C>A S mRNA, complete cds J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 55 21 C>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 304 270G>A S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 959 925C>A P309T lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 1762 1728A>T S lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- 3 lipoxygenase (leukocytes) 2043AC>AC J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2076 2042- F lipoxygenase (leukocytes) 2043delAC J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2328 2294C>T 3 lipoxygenase (leukocytes) J03571 J03571 152390 GEN-9 Lipoxygenases: 5- 2376 2342T>G 3 lipoxygenase (leukocytes) J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1202 1164C>T S 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1237 1199T>G I400S 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1372 1334C>G P445R 2c J03853 J03853 104250 GEN-A Adrenergic receptor alpha 1379 1341 C>T S 2c C1 S J04080 120580 GEN- Complement C1 S 558 356G>A R119H 13T component precursor (C1 esterase) C1 S J04080 120580 GEN- Complement C1S 2140 1938A>T K646N 13T component precursor (C1 esterase) C1 S J04080 120580 GEN- Complement C1S 2234 2032A>T T678S 13T component precursor (C1 esterase) SD-144146. Page 1 1 1 C1 S J04080 120580 GEN- Complement C1 S 2333 2131 G>T 3 13T component precursor (C1 esterase) J04144 J04144 106180 GEN-2L Angiotensin-converting 501 479A>G N160S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 604 582C>T S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 803 781 G>T A261 S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1042 1020C>T S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- S enzyme (ACE) 1515CCT>CC T J04144 J04144 106180 GEN-2L Angiotensin-converting 1535 1513- [P505V;50 enzyme (ACE) 1515delCCT 6-505del] J04144 J04144 106180 GEN-2L Angiotensin-converting 1797 1775A>G D592G enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2215 2193G>A S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2350 2328A>G S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 2505 2483T>C M828T enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S enzyme (ACE) J04144 J04144 106180 GEN-2L Angiotensin-converting 3409 3387T>C S enzyme (ACE) C6 J05064 217050 GEN- Human complement 3281 3126G>A 3 16S component C6 mRNA, complete cds J05096 J05096 182340 GEN-SL alpha-subunit of Na+/K+ 2364 2260T>G S754A ATPase isoform2 J05096 J05096 182340 GEN-SL alpha-subunit of Na+/K+ 5295 5191 G>A 3 ATPase isoform2 J05158 J05158 603104 GEN-173 Human carboxypeptidase 2314 2314C>T 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2316 2316G>T 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2332 2332G>T 3 SD-144146.1 Page 1 1 1 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2541 2541 G> A 3 N mRNA, 3 end J05158 J05158 603104 GEN-173 Human carboxypeptidase 2651 2651 C>T 3 N mRNA, 3 end J05480 J05480 114105 GEN-D Calcineurin A 834 834A>G 3 M6PR J05550 153618 GEN-180 Human mannose receptor 4890 4787T>A 3 mRNA, complete cds J05594 J05594 601688 GEN-E Prostaglandin 15-OH 173 156A>G S dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 913 896C>G 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 950 933G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1448 1431G>A 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) J05594 J05594 601688 GEN-E Prostaglandin 15-OH 1972 1955T>C 3 dehydrogenase (PGDH) K00396 K00396 107741 GEN-PO Human apolipoprotein E 112 52G>A A18T (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 121 61G>A E21 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 151 91 G>A E31 K (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 197 137T>C L46P (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 204 144delG F (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 238 178A>G T60A (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 365 305C>G P102R (epsilon 2 and 3 alleles) mRNA SD-144146 1 Page 111 K00396 K00396 107741 GEN-PO Human apolipoprotein E 409 349G>A A117T (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 448 388T>C C130R (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 494 434G>A G145D (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 515 455G>A R152Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 520 460C>A R154S (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 538 478C>T R160C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 547 487C>T R163C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 548 488G>A R163H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 550 490A>G K164E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 586 526C>T R176C (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 743 683G>A F (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 785 725G>A R242Q (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 796 736C>T R246C (epsilon 2 and 3 alleles) SD-144146.1 Page 1 1 mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 821 761T>A V254E (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 865 805OG R269G (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 935 875G>A R292H (epsilon 2 and 3 alleles) mRNA K00396 K00396 107741 GEN-PO Human apolipoprotein E 1000 940A>C S314R (epsilon 2 and 3 alleles) mRNA K01911 K01911 162640 GEN-20 Neuropeptide Y 236 150G>A S K01911 K01911 162640 GEN-20 Neuropeptide Y 290 204C>T S AGT K02215 106150 GEN-WK Human angiotensinogen 659 620C>T T207M mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 842 803T>C M268T mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1155 1116G>A S mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1476 1437C>A S mRNA, complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 1821 1782G>A 3 mRNA complete CDS AGT K02215 106150 GEN-WK Human angiotensinogen 2053 2014A>C 3 mRNA complete CDS K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 260 260C>G A87G end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 449 449G>C +150S end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 887 887A>G Y296C end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 902 902C>A P301 H end K02286 K02286 191840 GEN-SQ Human urokinase gene, 3 905 905A>G N302S end KNG K02566 228960 GEN-X2 Human alpha-2-thιol 1248 1199C>A T400K proteinase inhibitor mRNA complete coding sequence K02765 K02765 120700 GEN-XM Human complement 1001 941T>C L314P SD-144146 1 Page 11 component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 2575 2515G>A V839I component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 3108 3048C>T component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 3561 3501 C>G component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4371 4311C>T component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4544 4484C>A P1495Q component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4938 4878T>C S component C3 mRNA, alpha and beta subunits, complete cds K02765 K02765 120700 GEN-XM Human complement 4956 4896T>C S component C3 mRNA, alpha and beta subunits, complete cds K02770 K02770 147720 GEN-5M Interleukin 1 , beta 19 (-68)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 26 (-61)A>C 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 48 (-39)C>T 5 K02770 K02770 147720 GEN-5M Interleukin 1 , beta 114 28G>A E10K K02770 K02770 147720 GEN-5M Interleukin 1 , beta 119 33G>A M11I L00352 L00352 143890 GEN- Human low density 71 72C>T 3 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 103 104G>A SD-144146.1 Page 11 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 716 717C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 881 882G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1180 1181A>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1186 1187C>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1187 1188T>G 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1191 1192G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1222 1223G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1223 1224C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1224 1225G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1227 1228T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1234 1235T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1252 1253A>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1268 1269A>C 2S8 lipoprotein recep SD-144146.1 Page 11 L00352 L00352 143890 GEN- Human low density 1268 1269A>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1279 1280C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1280 1281G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1308 1309C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1309 1310G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1316 1317G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1320 1321T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1345 1346G>A 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1368 1369T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1376 13770T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1383 1384C>T 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1406 1407T>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1418 1419G>C 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1428 1429T>C 2S8 lipoprotein receptor gene, SD-144146.1 Page 11 exon 18 L00352 L00352 143890 GEN- Human low density 1453 1454C>T 3 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 1796 1797T>C 3 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 2108 2109G>A 3 2S8 lipoprotein receptor gene, exon 18 L00352 L00352 143890 GEN- Human low density 2490 2491A>C 3 2S8 lipoprotein receptor gene, exon 18 CBS L00972 236200 GEN-UV Human cystathionine-beta- 1022 1023T>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2001 2002C>T 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2278 2279G>A 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2358 2359G>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2524 2525T>C 3 synthase (CBS) mRNA CBS L00972 236200 GEN-UV Human cystathionine-beta- 2545 2546C>T 3 synthase (CBS) mRNA L01087 L01087 600448 GEN-CM Protein kinase C-theta 1940 1846C>A S L01087 L01087 600448 GEN-CM Protein kinase C-theta 1943 1849G>A E617K L05186 L05186 600758 GEN-174 Homo sapiens focal 2564 2550C>T S adhesion kinase mRNA, complete cds L05485 L05485 178635 GEN- Surfactant, pulmonary- 921 918T>C S MJL associated protein D L05597 L05597 None GEN- Serotonin 5-HT receptors 824 600T>C S 4EV 5-HT1 F L05597 L05597 None GEN- Serotonin 5-HT receptors 1010 786 Λ 787insA [H262Q;26 4EV 5-HT1 F ATAAAATTC 2 Λ 263insl AT KFI] EDNRB L06623 131244 GEN- Endothelin Receptor Type 88 (-146)A>G 5 19S B SD-144146.1 Page 11 EDNRB L06623 131244 GEN- Endothelin Receptor Type 332 99C>T S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A S 19S B EDNRB L06623 131244 GEN- Endothelin Receptor Type 1064 831 G>A s 19S B EHHADH L07077 261515 GEN- Human enyol-CoA: 1225 1218G>A s 1DF hydratase 3-hydroxyacyl- CoA dehydrogenase (EHHADH) mRNA, complete cds with repeats EHHADH L07077 261515 GEN- Human enyol-CoA: 1823 1816C>A P606T 1 DF hydratase 3-hydroxyacyl- CoA dehydrogenase (EHHADH) mRNA, complete cds with repeats ADD1 L07261 102680 GEN- Human alpha adducin 1852 1853C>G 3 1 DJ mRNA, partial cds including alternate exons A and B TGFBR3 L07594 600742 GEN- Human transforming 3966 3618G>C 3 1 EA growth factor-beta type III receptor (TGF-beta) mRNA, complete cds L07861 L07861 176977 GEN-DO Protein kinase C, delta 445 387G>A S L07861 L07861 176977 GEN-DO Protein kinase C, delta 1835 1777G>A V593M CCKBR L08112 118445 GEN- Cholecystokinin (CCKb) 456 456G>A S 1 FL FACL1 L09229 152425 GEN-1GI Human long-chain acyl- 3026 2953G>A 3 coenzyme A synthetase (FACL1 ) mRNA, complete cds FACL1 L09229 152425 GEN-1GI Human long-chain acyl- 3083 3010G>A 3 coenzyme A synthetase (FACL1 ) mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 191 153C>T S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 200 162G>A S LVD sulfotransferase mRNA, SD-144146.1 Page 11 L10819 L10819 171150 GEN- Homo sapiens aryl 230 192T>C S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 242 204G>A S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 295 257C>T A86V LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 330 292G>A D98N LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 338 300G>A S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 638 600C>G S LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 676 638A>G H213R LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 940 902G>A 3 LVD sulfotransferase mRNA, complete cds L10819 L10819 171150 GEN- Homo sapiens aryl 1011 973T>C 3 LVD sulfotransferase mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 538 204G>A S 1K2 binding protein beta-chain mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 796 462C>T S 1 K2 binding protein beta-chain mRNA, complete cds C4BPB L11244 120831 GEN- Human (clone A12) C4b- 958 624C>A S 1 K2 binding protein beta-chain mRNA, complete cds L11669 L11669 102680 GEN- Human tetracycline 544 424G>A A142T 1 KW transporter-like protein mRNA, complete cds L11669 L11669 102680 GEN- Human tetracycline 980 860C>T S287L SD-144146.1 Page 1 1 1 KW transporter-like protein mRNA, complete cds L11669 L1 1669 102680 GEN- Human tetracycline 1293 1 173G>A S 1 KW transporter-like protein mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1467 1250C>T 3 106 Miller-Dieker lissencephaly protein (LIS1) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1868 1651C>T 3 106 Miller-Dieker lissencephaly protein (LIS1) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 1917 1700C>T 3 106 Miller-Dieker lissencephaly protein (LISI ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 2962 2745G>T 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds MDCR L13385 601545 GEN- Homo sapiens(clone 71 ) 4589 4372G>A 3 106 Miller-Dieker lissencephaly protein (LIS1 ) mRNA, complete cds L13436 L13436 108961 GEN-2Q guanylate cyclase 1410 1411T>A 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1646 1647C>G 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1650 1651G>C 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 1677 1678C>G 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 2222 2223C>T 3 L13436 L13436 108961 GEN-2Q guanylate cyclase 2444 2445C>T 3 L13977 L13977 176785 GEN- Human 2009 1980T>C 3 I PX prolylcarboxypeptidase mRNA, complete cds BF L15702 138470 GEN- Human complement factor 135 95A>G Q32R 1 UA B mRNA, complete cds PRKCI L18964 300094 GEN- Human protein kinase C 573 309T>G S 21 N iota isoform (PRKCI) mRNA, complete cds L19182 L19182 602867 GEN- Human MAC25 mRNA, 297 284G>A R95K SD- 144146- Page 1 1 21Z complete cds L19956 L19956 600641 GEN- Human aryl 243 105A>G LVE sulfotransferase mRNA, complete cds L19956 L19956 600641 GEN- Human aryl 284 146C>T S49F LVE sulfotransferase mRNA, complete cds L20463 L20463 600445 GEN-M G-protein coupled 1671 1380A>G adenosine A3 receptor VLDLR L20470 192977 GEN- Human very low density 336 (-56)C>T 23D lipoprotein receptor mRNA, complete cds VLDLR L20470 192977 GEN- Human very low density 3566 3175T>C 23D lipoprotein receptor mRNA, complete cds L22214 L22214 102775 GEN-2S Adenosine A1 receptor 557 147G>C S (ADORA1 ) L22214 L22214 102775 GEN-2S Adenosine A1 receptor 2622 2212G>A 3 (ADORA1 ) L22473 L22473 600040 GEN- Human Bax alpha mRNA, 552 552G>A S L9D complete cds SLC6A3 L24178 126455 GEN-283 Homo sapiens dopamine 1917 1898C>T 3 transporter mRNA, complete cds L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1422 1185T>C 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1490 1253C>T 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 1517 1280A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2244 2007A>G 3 RECEPTOR L24470 L24470 600563 GEN-0 PROSTAGLANDIN F 2299 2062A>G 3 RECEPTOR L26232 L26232 172425 GEN- Human phospholipid 906 819C>T S 2AK transfer protein mRNA, complete cds L26232 L26232 172425 GEN- Human phospholipid 1547 1460OA T487K 2AK transfer protein mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 213 175C>G Q59E SD-144146.1 Page 1 1 208 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 257 219C>A 2C8 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 295 257G>T C86F 2C8 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 434 396G>A 2C8 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 436 398A>T N133I 2C8 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 801 763G>A 2C8 pathway inhibitor-2 mRNA, complete cds L27624 L27624 600033 GEN- Homo sapiens tissue factor 885 847C>A 2C8 pathway inhibitor-2 mRNA, complete cds PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 547 159C>T S (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 611 223G>A V75M (subtype EP2), 53kD PTGER2 L28175 601586 GEN-7C Prostaglandin E receptor 2 1725 1337A>G Q446R (subtype EP2), 53kD L31773 L31773 104220 GEN- Adrenergic receptor alpha 171 171C>T S 4DD 1 b L31773 L31773 104220 GEN- Adrenergic receptor alpha 534 534C>T S 4DD 1 b L31773 L31773 104220 GEN- Adrenergic receptor alpha 549 549G>A S 4DD 1b L34357 L34357 600576 GEN- Homo sapiens GATA-4 1996 1756T>C 3 KV3 mRNA, complete cds L34357 L34357 600576 GEN- Homo sapiens GATA-4 2133 1893C>G 3 KV3 mRNA, complete cds L36566 L36566 601970 GEN- Human helodermin- 1397 1235A>G H412R 2N5 preferring VIP receptor (VIP2/PACAP receptor) mRNA, complete cds L36566 L36566 601970 GEN- Human helodermin- 1440 1278A>C SD-144146.1 Page 1 1 2N5 preferring VIP receptor (VIP2/PACAP receptor) mRNA, complete cds NRAMP2 L37347 600523 GEN- Human integral membrane 1092 1083C>T S 206 protein (Nramp2) mRNA, partial L38969 L38969 None GEN- Homo sapiens 2968 2947C>T 3 MPS thrombospondin 3 (THBS3) gene, complete cds L41147 L41147 601109 GEN-2T Serotonin 5-HT receptors 287 (-181 )C>T 5 5-HT6 L41147 L41147 601109 GEN-2T Serotonin 5-HT receptors 1718 1251C>T S 5-HT6 L48513 L48513 602447 GEN- Homo sapiens 460 443C>G A148G 2YD paraoxonase 2 (PON2) mRNA, complete cds L48513 L48513 602447 GEN- Homo sapiens 598 581 G>A G194E 2YD paraoxonase 2 (PON2) mRNA, complete cds L48513 L48513 602447 GEN- Homo sapiens 949 932G>C C311S 2YD paraoxonase 2 (PON2) mRNA, complete cds L78207 L78207 600509 GEN-5Q Cell surface receptor for 4019 3981 A>G S sulfonylureas on pancreatic b cells M10051 M10051 147670 GEN-2V Insulin receptor 2757 2619G>A S M10051 M10051 147670 GEN-2V Insulin receptor 4391 4253G>A 3 M11146 M11146 134770 GEN-Q7 Human ferntin H chain 193 116C>T S39F mRNA, complete cds M1 1 146 M11 146 134770 GEN-Q7 Human ferntin H chain 326 249T>G S mRNA, complete cds M11146 M11146 134770 GEN-Q7 Human ferntin H chain 628 551 A>T F mRNA, complete cds M11146 M11146 134770 GEN-Q7 Human ferntin H chain 630 553G>A 3 mRNA, complete cds M11146 M11146 134770 GEN-Q7 Human ferntin H chain 652 575G>A 3 mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferntin L chain 180 29C>A S10Y mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferntin L chain 240 89C>A T30N SD-144146 1 Page 1 1 mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferritin L chain 314 163C>T S mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferritin L chain 340 189C>A F mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferritin L chain 375 224G>A G75D mRNA, complete cds FTL M11147 134790 GEN-1JZ Human ferritin L chain 751 600T>G 3 mRNA, complete cds TF M12530 190000 GEN- Human transferrin mRNA, 654 624G>A S 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 768 738C>G C246W 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1447 1417G>T V473F 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1602 1572G>C S 1 MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1632 1602OT S 1MK complete cds TF M12530 190000 GEN- Human transferrin mRNA, 1795 1765C>T P589S 1 MK complete cds M 12674 M 12674 133430 GEN-7Z Estrogen receptor 1267 975C>G S M12783 M12783 190040 GEN-QF Human c-sis/platelet- 1896 804T>C 3 derived growth factor 2 (SIS/PDGF2) mRNA, complete cds M12783 M12783 190040 GEN-QF Human c-sis/platelet- 2148 1056T>C derived growth factor 2 (SIS/PDGF2) mRNA, complete cds M12783 M12783 190040 GEN-QF Human c-sis/platelet- 2250 1158G>A derived growth factor 2 (SIS/PDGF2) mRNA, complete cds M13686 M13686 178630 GEN- Human pulmonary 144 56C>T A19V 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 341 253T>C C85R 1 P1 surfactant-associated protein mRNA, complete SD-144146.1 Page 1 13 cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 370 282G>A S 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 430 342T>C S 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 694 606C>T S 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 736 648C>T S 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A M13686 M13686 178630 GEN- Human pulmonary 883 795C>G 3 1 P1 surfactant-associated protein mRNA, complete cds, clone MPSAP-6A C1 NH M13690 106100 GEN- Human plasma protease 1475 1438G>A V480M 1 P6 (C1 ) inhibitor mRNA, complete cds C1NH M13690 106100 GEN- Human plasma protease 1595 15580T 3 1 P6 (C1 ) inhibitor mRNA, complete cds C1 NH M13690 106100 GEN- Human plasma protease 1714 1677A>C 3 1 P6 (C1) inhibitor mRNA, complete cds ALAD M13928 125270 GEN- Human delta- 234 168T>C S 1 Q2 aminolevulinate dehydratase mRNA, complete cds ALAD M 13928 125270 GEN- Human delta- 480 414C>T S 1Q2 aminolevulinate dehydratase mRNA, complete cds ALAD M 13928 125270 GEN- Human delta- 784 718C>T R240W 1Q2 aminolevulinate dehydratase mRNA, SD-144146. Page 1 13 complete cds BCL2 M 13994 151430 GEN- Human B-cell 1744 286G>A A96T 1Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds BCL2 M 13994 151430 GEN- Human B-cell 1786 328G>C G110R 1Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds BCL2 M13994 151430 GEN- Human B-cell 2959 1501A>G 1 Q9 leukemia/lymphoma 2 (bcl- 2) proto-oncogene mRNA encoding bcl-2-alpha protein, complete cds UROD M14016 176100 GEN- Human uroporphyrinogen 248 230C>T P77L 1QM decarboxylase mRNA, complete cds UROD M14016 176100 GEN- Human uroporphyrinogen 850 832G>T 1QM decarboxylase mRNA, complete cds C1 R M14058 216950 GEN- Human complement C1 r 1519 1456C>T R486C 1 QJ mRNA, complete cds M14113 M14113 306700 GEN-5T Factor VIII 8899 8728G>A 3 ARG1 M14502 207800 GEN- Human liver arginase 800 744C>T S I RE mRNA, complete cds M14539 M14539 134570 GEN-QP Human factor XIII subunit a 1781 1781 C>T P594L mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 2041 2041 C>G Q681 E mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 2412 2412C>T 3 mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 2446 2446G>A 3 mRNA, 3 end M14539 M14539 134570 GEN-QP Human factor XIII subunit a 3282 3282G>T 3 mRNA, 3 end M14565 M14565 118485 GEN-30 Cytochrome P450, 947 903G>C M301 I subfamily XIA (cholesterol side chain cleavage) M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 466 (-1122)C>G 5 SD-144146 1 Page 113 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 565 (-1023)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1182 (-406)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1221 (-367)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1326 (-262)G>A 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1541 (-47)C>T 5 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1633 46A>G R16G M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1666 79C>G Q27E M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1687 100G>A V34M M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 1839 252G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2110 523C>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2640 1053G>C S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2826 1239G>A S M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2862 1275C>G 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2864 1277C>A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 2865 1278C>A 3 M15169 M15169 109690 GEN-T Beta2 Adrenergic Receptor 3371 1784A>T 3 PCNA M15796 176740 GEN- Human cyclin protein gene, 1063 945C>G 3 1 UE complete cds DAF M15799 125240 GEN- Human complement 1160 1160A>C 3 1 UD decay-accelerating factor (DAF) mRNA, 3 end M15856 M15856 238600 GEN-33 Lipoprotein lipase 136 (-39)T>C 5 M15856 M15856 238600 GEN-33 Lipoprotein lipase 280 106G>A D36N M15856 M 15856 238600 GEN-33 Lipoprotein lipase 438 264T>A F M15856 M15856 238600 GEN-33 Lipoprotein lipase 447 273G>A F M15856 M 15856 238600 GEN-33 Lipoprotein lipase 474 300C>A F M15856 M 15856 238600 GEN-33 Lipoprotein lipase 480 306A>C R102S M15856 M15856 238600 GEN-33 Lipoprotein lipase 511 337T>C W113R M15856 M15856 238600 GEN-33 Lipoprotein lipase 571 397C>T F M15856 M15856 238600 GEN-33 Lipoprotein lipase 680 506G>A G169E M15856 M15856 238600 GEN-33 Lipoprotein lipase 722 548A>G D183G M15856 M15856 238600 GEN-33 Lipoprotein lipase 770 596C>G S199C M15856 M15856 238600 GEN-33 Lipoprotein lipase 781 607G>A A203T SD-144146.1 Page 1 1 M15856 M15856 238600 GEN-33 Lipoprotein lipase 795 621 C>G D207E M 15856 M 15856 238600 GEN-33 Lipoprotein lipase 818 644G>A G215E M 15856 M15856 238600 GEN-33 Lipoprotein lipase 836 662T>C I221T M15856 M15856 238600 GEN-33 Lipoprotein lipase 839 665G>A G222E M15856 M 15856 238600 GEN-33 Lipoprotein lipase 843 669C>T S M 15856 M15856 238600 GEN-33 Lipoprotein lipase 867 693C>G D231 E M15856 M15856 238600 GEN-33 Lipoprotein lipase 875 701 C>T P234L M15856 M15856 238600 GEN-33 Lipoprotein lipase 916 742delG F M15856 M15856 238600 GEN-33 Lipoprotein lipase 983 809G>A R270H M15856 M15856 238600 GEN-33 Lipoprotein lipase 985 811T>A S271T M15856 M15856 238600 GEN-33 Lipoprotein lipase 1003 829G>A D277N M15856 M15856 238600 GEN-33 Lipoprotein lipase 1127 953A>G N318S M15856 M15856 238600 GEN-33 Lipoprotein lipase 1255 1081G>A A361T M15856 M15856 238600 GEN-33 Lipoprotein lipase 1348 1174C>G L392V M15856 M15856 238600 GEN-33 Lipoprotein lipase 1401 1227G>A F M15856 M 15856 238600 GEN-33 Lipoprotein lipase 1508 1334G>A C445Y M15856 M15856 238600 GEN-33 Lipoprotein lipase 1553 1379C>T A460V M15856 M15856 238600 GEN-33 Lipoprotein lipase 1595 1421C>G F M15856 M15856 238600 GEN-33 Lipoprotein lipase 1611 1437G>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 1973 1799T>C 3 M15856 M 15856 238600 GEN-33 Lipoprotein lipase 2428 2254T>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2743 2569T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2851 2677A>G 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 2958 2784G>A 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3017 2843T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3272 3098T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3343 3169T>C 3 M15856 M15856 238600 GEN-33 Lipoprotein lipase 3447 3273C>T 3 M16006 M16006 173360 GEN-34 Tissue Plasminogen 124 49G>A V17I activator inhibitor, type I M16006 M16006 173360 GEN-34 Tissue Plasminogen 411 336T>C S activator inhibitor, type I M16006 M16006 173360 GEN-34 Tissue Plasminogen 1645 1570T>C 3 activator inhibitor, type I SD-144146.1 Page 11 M16006 M16006 173360 GEN-34 Tissue Plasminogen 1974 1899T>C 3 activator inhibitor, type I M16006 M16006 173360 GEN-34 Tissue Plasminogen 2006 1931T>G 3 activator inhibitor, type I M 16405 M16405 None GEN- Muscarinic receptor, 2138 1338C>T S 4ES CHRM4 M16405 M 16405 None GEN- Muscarinic receptor, 2409 1609G>A 3 4ES CHRM4 M16538 M16538 139390 GEN- Human signal-transducing 867 720C>T S 1Y8 guanine nucleotide-binding regulatory (G) protein beta subunit mRNA, complete cds M16538 M16538 139390 GEN- Human signal-transducing 1270 1123G>T 1Y8 guanine nucleotide-binding regulatory (G) protein beta subunit mRNA, complete cds M16538 M16538 139390 GEN- Human signal-transducing 1388 1241 C>T 1Y8 guanine nucleotide-binding regulatory (G) protein beta subunit mRNA, complete cds M16541 M16541 177400 GEN-35 Butyrylcholinesterase 422 293A>G D98G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 557 428G>A G143D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 564 435- F146V 436TT>AG>A G M16541 M16541 177400 GEN-35 Butyrylcholinesterase 568 4390T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 596 467A>G Y156C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 941 8120T T271 M M16541 M16541 177400 GEN-35 Butyrylcholinesterase 961 832A>C T278P M16541 M16541 177400 GEN-35 Butyrylcholinesterase 978 849G>C E283D M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1201 1072T>A L358I M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1306 1177G>A G393R M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1382 1253G>T G418V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1549 1420T>G F474V M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1564 1435G>T F M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1703 1574A>T E525V SD-144146.1 Page 1 1 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1756 1627C>T R543C M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 1828 1699G>A A567T M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16541 M16541 177400 GEN-35 Butyrylcholinesterase 2127 1998A>G 3 M16660 M16660 140571 GEN- Human 90-kDa heat-shock 825 741 G>A S 1 YC protein gene, cDNA, complete cds M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 175 (-42)C>G 5 (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 754 538A>G 1180V (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 938 722C>T A241V (aldosterone receptor] M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 1221 1005delC F (aldosterone receptor] M16801 M16801 600983 GEN-36 Mineralocorticoid receptoi 1591 1375delT F (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 1713 14970T S (aldosterone receptor] M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 1825 1609C>T F (aldosterone receptor] M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 2438 2222T>G V741 G (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 2730 2514G>A S (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 5243 5027T>A 3 (aldosterone receptor M16801 M16801 600983 GEN-36 Mineralocorticoid recepto 5645 5429G>A 3 (aldosterone receptor] M16827 M16827 201450 GEN-EI Acyl-Coenzyme A 1956 1938T>C 3 dehydrogenase, C-4 to C- 12 straight chain F5 M16967 227400 GEN- Human coagulation factor 2391 2301G>A S 1Z8 V mRNA, complete cds F5 M16967 227400 GEN- Human coagulation factor 2663 2573G>A R858K 1Z8 V mRNA, complete cds F5 M16967 227400 GEN- Human coagulation factor 2684 2594G>A R865H 1Z8 V mRNA, complete cds F5 M16967 227400 GEN- Human coagulation factor 5380 5290G>A V1764M SD-144146. Page 1 1 1Z8 V mRNA, complete cds C8B M16973 120960 GEN- Human complement 1860 1833C>T 3 1ZA protein C8 beta subunit mRNA, complete cds M17262 M 17262 176930 GEN-SM Human prothrombin (F2) 511 480C>T S gene, complete cds and Alu and Kpnl repeats C8G M17999 120930 GEN- Human complement 193 132T>G S 20Y component C8-gamma mRNA, complete cds M18112 M18112 173870 GEN-EK ADP-nbosyltransferase 2424 2285T>C V762A (NAD+, poly (ADP-ribose) polymerase) M18112 M18112 173870 GEN-EK ADP-nbosyltransferase 2679 2540G>T R847L (NAD+, poly (ADP-ribose) polymerase) M18182 M18182 173370 GEN-37 Tissue Plasminogen 391 378G>A S activator tissue type (t-PA) M18182 M18182 173370 GEN-37 Tissue Plasminogen 499 486C>T S activator tissue type (t-PA) M18182 M18182 173370 GEN-37 Tissue Plasminogen 514 501 C>T S activator, tissue type (t-PA) M18182 M18182 173370 GEN-37 Tissue Plasminogen 1822 1809G>A 3 activator, tissue type (t-PA) M18182 M18182 173370 GEN-37 Tissue Plasminogen 1977 1964A>G 3 activator, tissue type (t-PA) M18182 M18182 173370 GEN-37 Tissue Plasminogen 2161 2148G>C 3 activator, tissue type (t-PA) M20132 M20132 313700 GEN-38 Androgen receptor 995 633G>A S (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1385 1023T>C S (dihydrotestosterone receptor) M20132 M20132 313700 GEN-38 Androgen receptor 1786 1424G>A G475E (dihydrotestosterone receptor) M20137 M20137 147740 GEN- Human interleukin 3 (IL-3) 132 79C>T P27S CCJ mRNA, complete cds, clone pcD-SR-alpha M20560 M20560 106490 GEN-39 Lipocortin III (Annexin III) 1057 1011C>T SD- 144146 1 Page 1 1 M20560 M20560 106490 GEN-39 Lipocortin III (Annexin III) 1302 1256C>A 3 M20566 M20566 147880 GEN-3A Interleukin 6A 3058 2621A>T 3 M21054 M21054 172410 GEN-3B Phosphoiipase A-2 (PLA-2) 331 294G>A S lung M21054 M21054 172410 GEN-3B Phospholipase A-2 (PLA-2) 400 363C>A D121 E lung CYBA M21186 233690 GEN-24I Human neutrophil 242 214C>T H72Y cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds CYBA M21186 233690 GEN-24I Human neutrophil 549 521C>T A174V cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds CYBA M21186 233690 GEN-24I Human neutrophil 640 612A>G 3 cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds CYBA M21186 233690 GEN-24I Human neutrophil 665 637C>T 3 cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds M21616 M21616 173410 GEN-R1 Human platelet-derived 4312 4126C>T 3 growth factor (PDGF) receptor mRNA, complete cds M21616 M21616 173410 GEN-R1 Human platelet-derived 5171 4985C>A 3 growth factor (PDGF) receptor mRNA, complete cds M21616 M21616 173410 GEN-R1 Human platelet-derived 5295 5109A>G 3 growth factor (PDGF) receptor mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 116 (-20)G>T 5 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 231 96G>C S SD-144146.1 Page 1 1 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 267 132C>T S 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143- S 25V mRNA, complete cds 144GT>GT PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 278 143-144delGT F 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 643 508C>T 3 25V mRNA, complete cds PLA2G2A M22430 172411 GEN- Human RASF-A PLA2 700 565G>C 3 25V mRNA, complete cds M22613 M22613 227600 GEN-3C COAGULATION FACTOR 738 738C>T S X PRECURSOR ATP2A2 M23114 108740 GEN-276 Homo sapiens calcium- 2382 2219C>T S740F ATPase (HK1 ) mRNA, complete cds M24283 M24283 147840 GEN-V Intercellular adhesion 238 167A>T K56M molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 238 167A>T K56M molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 792 721 G>A G241 R molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 792 721 G>A G241 R molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1126 1055C>T P352L molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1166 1095C>T S molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1295 1224G>A S molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 1476 1405A>G K469E molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2043 1972C>T 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2043 1972C>T 3 SD-144146 Page 1 1 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2551 2480C>T 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2681 2610G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2842 2771 G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2842 2771 G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2935 2864T>C 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2938 2867G>A 3 molecule 1 M24283 M24283 147840 GEN-V Intercellular adhesion 2950 2879C>T 3 molecule 1 CD36 M24795 173510 GEN- Human CD36 antigen 79 (-132)C>A 5 28R mRNA, complete cds CD36 M24795 173510 GEN- Human CD36 antigen 341 131T>G L44R 28R mRNA, complete cds CD36 M24795 173510 GEN- Human CD36 antigen 1851 1641A>G 3 28R mRNA, complete cds M25813 M25813 None GEN- Human unidentified gene 1357 1357G>A V453I 2A0 complementary to P450c21 gene, partial cds M25813 M25813 None GEN- Human unidentified gene 2082 2082C>G I694M 2A0 complementary to P450c21 gene, partial cds M25813 M25813 None GEN- Human unidentified gene 2502 2502G>A 3 2A0 complementary to P450c21 gene, partial cds M25813 M25813 None GEN- Human unidentified gene 2626 2626A>G 3 2A0 complementary to P450c21 gene, partial cds M26383 M26383 146930 GEN-3E Interleukin 8 259 185C>G A62G M26383 M26383 146930 GEN-3E Interleukin 8 1237 1163A>T 3 M26383 M26383 146930 GEN-3E Interleukin 8 1281 1207A>G 3 M26393 M26393 201470 GEN-EW Acyl-Coenzyme A 1797 1765A>G 3 dehydrogenase, C-2 to C-3 short chain M27137 M27137 109715 GEN-5W 3beta hydroxysteroid 1103 1100C>A T367N dehydrogenase SD-144146.1 Page 1 1 M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1414 13150T 3 complete cds, with a Alu repetitive sequence in the 3 untranslated region M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1508 1409A>G 3 complete cds, with a Alu repetitive sequence in the 3 untranslated region M27436 M27436 134390 GEN-R7 Human tissue factor gene, 1588 1489T>G 3 complete cds, with a Alu repetitive sequence in the 3 untranslated region M27492 M27492 147810 GEN-3F INTERLEUKIN 1 4686 4604T>G 3 RECEPTOR, TYPE I PRECURSOR M27875 M27875 107680 GEN- Human apolipoprotein A-I 34 15G>C S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 202 183C>T S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 204 185T>G L62W 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 255 236C>T S79F 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 689 670C>T S 2CK mRNA, complete cds M27875 M27875 107680 GEN- Human apolipoprotein A-I 824 805G>A 3 2CK mRNA, complete cds M28226 M28226 158105 GEN-R8 Human JE gene encoding 90 44C>G A15G a monocyte secretory protein mRNA, complete cds M28226 M28226 158105 GEN-R8 Human JE gene encoding 151 105C>T S a monocyte secretory protein mRNA, complete cds M28226 M28226 158105 GEN-R8 Human JE gene encoding 411 365T>C 3 a monocyte secretory protein mRNA, complete cds M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 370 340C>G M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 401 371T>G SD-144146.1 Page 1 1 M28614 M28614 107720 GEN-6Q Apolipoprotein C-lll 479 449T>A 3 CFTR M28668 602421 GEN- Human cystic fibrosis 2729 2597G>A C866Y 2DF mRNA, encoding a presumed transmembrane conductance regulator (CFTR) CFTR M28668 602421 GEN- Human cystic fibrosis 5826 5694T>C 2DF mRNA, encoding a presumed transmembrane conductance regulator (CFTR) M29551 M29551 114106 GEN-F3 SERINE/THREONINE 936 820G>A V274M PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM M29551 M29551 114106 GEN-F3 SERINE/THREONINE 2640 2524G>A PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM M29696 M29696 146661 GEN-3H Interleukin 7 receptor 1088 1066G>A V356I M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 26 17C>A A6E M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 183 174G>A S M29882 M29882 107670 GEN-6R Apolipoprotein A-ll 192 183C>A S CETP M30185 118470 GEN- Human cholesteryl ester 1283 1153G>C V385L 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1298 1168G>C A390P 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1394 1264A>G I422V 2FK transfer protein mRNA, complete cds CETP M30185 118470 GEN- Human cholesteryl ester 1506 1376A>G D459G 2FK transfer protein mRNA, complete cds SD-144146. Page 1 1 CETP M30185 118470 GEN- Human cholesteryl ester 1696 1566G>A 2FK transfer protein mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 178 79C>T P27S natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 203 104C>G A35G natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 210 111 G>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 327 228C>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 553 454T>C natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 626 527G>T natriuretic factor (CDD- ANF) mRNA, complete cds M30262 M30262 600295 GEN-WA Human cardiodilatin-atrial 640 541T>C natriuretic factor (CDD- ANF) mRNA, complete cds M30773 M30773 1 14106 GEN-X Calcineurin B type I 331 (-428)T>C M30773 M30773 114106 GEN-X Calcineurin B type I 1658 900C>A M31145 M31145 146730 GEN-3J Insulin-like growth factor 923 759A>G I253M binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1048 884T>C 3 binding protein 1 precursor M31145 M31145 146730 GEN-3J Insulin-like growth factor 1260 1096OG 3 binding protein 1 precursor PRKAR2 M31158 176912 GEN- Human cAMP-dependent 2790 26240G 3 B 2GE protein kinase subunit Rll- beta mRNA, complete cds M31159 M31159 146732 GEN- Human growth hormone- 204 95G>C G32A 2GD dependent insulin-like growth factor-binding protein mRNA, complete cds M31159 M31 159 146732 GEN- Human growth hormone- 2178 2069A>T 3 SD-144146.1 Page 11 2GD dependent insulin-like growth factor-binding protein mRNA, complete cds M31328 M31328 139130 GEN-7G Guanine nucleotide binding 1049 1043G>A 3 protein (G protein), beta polypeptide 3 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1271 1241 C>T 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1344 1314G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1489 1459G>A 3 1 M32313 M32313 184753 GEN-5Y Steroid 5 alpha reductase 1780 1750T>C 3 1 VEGF M32977 192240 GEN-2JF Human heparin-binding 50 (-7)OT 5 vascular endothelial growth factor (VEGF) mRNA, complete cds VEGF M32977 192240 GEN-2JF Human heparin-binding 92 36C>T vascular endothelial growth factor (VEGF) mRNA, complete cds M33336 M33336 188830 GEN-RC Human cAMP-dependent 2440 2353T>G protein kinase type l-alpha subunit (PRKAR1 A) mRNA, complete cds M33336 M33336 188830 GEN-RC Human cAMP-dependent 2472 2385C>T protein kinase type l-alpha subunit (PRKAR1 A) mRNA, complete cds M33336 M33336 188830 GEN-RC Human cAMP-dependent 3005 2918T>C 3 protein kinase type l-alpha subunit (PRKAR1 A) mRNA, complete cds M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 53 35T>C V12A M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 149 I 31C>A A44D M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 194 176T>C L59P M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 364 3460T L116F M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 900 882T>C S SD-144146.1 Page 11 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 987 969G>T E323D M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1161 1143C>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1551 1533G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1562 1544G>A R515Q M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 1563 1545G>A S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2226 2208C>T S M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 2426 2408G>C 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3056 3038C>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3098 3080A>G 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3403 3385A>T 3 M35999 M35999 173470 GEN-Y Leukocyte integrin beta-3 3927 3909C>T 3 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 449 297A>G S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 883 731 A>G H244R 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 922 770A>T H257L 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 954 802C>T R268W 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 1301 1149T>C S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 1649 1497T>C S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 2666 2514G>A S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 3245 3093C>T S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 3245 3093C>T S 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 3436 3284G>A G1095D 201 PLCG2 M37238 600220 GEN- Phospholipase C gamma-2 4207 4055C>G 3 201 PAM M37721 170270 GEN- Human peptidylglycine 3183 2995T>A 3 20K alpha-amidating monooxygenase mRNA, SD-144146.1 Page 11 complete cds PAM M37721 170270 GEN- Human peptidylglycine 3530 3342A>G 3 20K alpha-amidating monooxygenase mRNA, complete cds M37825 M37825 165190 GEN- Human fibroblast growth 787 648T>G S 20M factor-5 (FGF-5) mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 711 519T>C S 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 936 744G>T 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 1270 1078T>C 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 3268 3076T>G 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4529 4337A>C 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4555 4363A>G 3 35G protein mRNA, complete cds M54968 M54968 190070 GEN- Human K-ras oncogene 4672 4480A>C 3 35G protein mRNA, complete cds M55040 M55040 100740 GEN-3Q acetylcholinesterase 323 167C>T P56L M55040 M55040 100740 GEN-3Q acetylcholinesterase 1154 998T>A V333E M55040 M55040 100740 GEN-3Q acetylcholinesterase 1213 1057C>A H353N M55040 M55040 100740 GEN-3Q acetylcholinesterase 1482 1326G>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431 C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1587 1431 C>T S M55040 M55040 100740 GEN-3Q acetylcholinesterase 1663 1507T>C F503L NCF1 M55067 233700 GEN- Human 47-kD autosomal 291 269G>A R90H 35R chronic granulomatous disease protein mRNA, complete cds SD-144146.1 Page 1 1 NCF1 M55067233700 GEN- Human 47-kD autosomal 367 345C>T 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 409 387G>A 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 518 496G>A D166N 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 580 558G>A 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 847 825T>C 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 871 849G>A 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 930 908OT S303L 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 945 923C>T A308V 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 958 936T>C 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 966 944C>T S315L 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 1024 1002G>A SD-144146.1 Page 1 1 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 1089 1067C>A T356K 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 1098 1076C>T S359F 35R chronic granulomatous disease protein mRNA, complete cds NCF1 M55067 233700 GEN- Human 47-kD autosomal 1250 12280T 3 35R chronic granulomatous disease protein mRNA, complete cds M55643 M55643 164011 GEN-RP Human factor KBF1 1936 1755G>A S mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 1828 1813C>T 3 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 1956 1941 C>G 3 38A glucuronosyltransferase isozyme 1 mRNA, complete cds M57899 M57899 191740 GEN- Human biiirubin UDP- 2057 2042C>G 3 38A glucuronosyltransferase isozyme 1 mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 407 321T>G D107E heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 732C>T S heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 2132 2046C>G S heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 2837 2751T>C S heavy chain (MYH7) mRNA, complete cds SD-144146. Page 11 MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 2913 2827T>C S heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 3300 3214G>T D1072Y heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 3456 3370T>G S1124A heavy chain (MYH7) mRNA, complete cds MYH7 M58018 160760 GEN-38J Homo sapiens beta-myosin 5507 5421C>G S heavy chain (MYH7) mRNA, complete cds M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 390 186T>C S methyltransferase M58525 M58525 1 16790 GEN-3S Catechol-O- 418 214G>T A72S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 423 219G>A S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 612 408C>G S methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 676 472A>G M158V methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 813 609C>T S methyltransferase M58525 M58525 1 16790 GEN-3S Catechol-O- 1031 827delC F methyltransferase M58525 M58525 116790 GEN-3S Catechol-O- 1039 835C>A 3 methyltransferase M59305 M59305 108962 GEN- Human atrial natriuretic 160 (-203M- F 39P peptide clearance receptor 199)delTTTTT (ANP C-receptor) mRNA, complete cds M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 644 639C>A S M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 1892 1887C>A 3 M59979 M59979 176805 GEN-Z Cyclooxygenase 1 COX1 2030 2025G>A 3 M60335 M60335 192225 GEN-3U Vascular cell adhesion 1562 1463A>G H488R molecule 1 SD-144146.1 Page 1 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2178 2079C>T S molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2178 2079OT S molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2196 2097T>C s molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2307 2208A>G s molecule 1 M60335 M60335 192225 GEN-3U Vascular cell adhesion 2321 2222T>C 3 molecule 1 FGF7 M60828 148180 GEN- Human keratinocyte 323 (-123)G>C 5 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1180 735T>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1201 756A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1216 771A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1218 773G>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1266 821 A>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1306 861 C>T 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1654 1209A>T 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1657 1212T>C 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1799 1354A>T 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1801 1356C>T SD-144146.1 Page 1 1 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1867 1422A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1945 1500C>A 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 1973 1528G>A 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2167 1722G>A 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2186 1741A>G 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2302 1857T>A 3BE growth factor mRNA, complete cds FGF7 M60828 148180 GEN- Human keratinocyte 2328 1883G>A 3BE growth factor mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 859 776G>A 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1403 1320G>T 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1443 1360G>A 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1446 1363G>A 3CJ factor binding protein 4 (IGFBP4) mRNA, complete cds IGFBP4 M62403 146733 GEN- Human insulin-like growth 1485 1402A>T 3CJ factor binding protein 4 SD-144146.1 Page 1 1 (IGFBP4) mRNA, complete cds M62424 M62424 187930 GEN-3W Coagulation factor II 3210 2986C>T 3 (thrombin) receptor M62424 M62424 187930 GEN-3W Coagulation factor II 3211 2987G>A 3 (thrombin) receptor M62424 M62424 187930 GEN-3W Coagulation factor II 3247 3023T>C 3 (thrombin) receptor M62782 M62782 146734 GEN- Homo sapiens insulin-like 908 852C>T 3 3CU growth factor binding protein 5 (IGFBP-5) mRNA, complete cds APOH M62839 138700 GEN- Human apolipoprotein H 500 461 G>A R154H 3CY mRNA, complete cds APOH M62839 138700 GEN- Human apolipoprotein H 835 796G>T V266L 3CY mRNA, complete cds APOH M62839 138700 GEN- Human apolipoprotein H 1098 1059T>C 3 3CY mRNA, complete cds M63012 M63012 168820 GEN-9F Paraoxonase 1 172 163A>T M55L LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 850 837G>A S macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1093 1080C>T 3 macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1175 1162G>A 3 macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1249 1236C>T macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1249 1236C>T macroglobulin receptor- associated protein mRNA, complete cds LRPAP1 M63959 104225 GEN-3EI Human alpha-2- 1392 1379T>G macroglobulin receptor- SD-144146.1 Page 1 1 associated protein mRNA, complete cds FGFR3 M64347 134934 GEN- Human novel growth factor 3108 3108C>A 3 SEX receptor mRNA, 3 cds FGFR3 M64347 134934 GEN- Human novel growth factor 3715 3715G>A 3 SEX receptor mRNA, 3 cds M64592 M64592 120420 GEN-3X Granulocyte colony- 271 271T>G Y91 D stimulating factor M64592 M64592 120420 GEN-3X Granulocyte colony- 1533 1533C>T S stimulating factor M64710 M64710 None GEN- Human C-type natriuretic 199 200C>G 3 KUW peptide gene, complete cds M64710 M64710 None GEN- Human C-type natriuretic 777 778G>A KUW peptide gene, complete cds M64710 M64710 None GEN- Human C-type natriuretic 1215 1216A>G 3 KUW peptide gene, complete cds M64799 M64799 None GEN- Histamine receptor H2 398 398T>C V133A 4DN M64799 M64799 None GEN- Histamine receptor H2 525 525A>T K175N 4DN M64799 M64799 None GEN- Histamine receptor H2 620 620A>G K207R 4DN M64799 M64799 None GEN- Histamine receptor H2 649 649A>G N217D 4DN M64799 M64799 None GEN- Histamine receptor H2 692 692A>G K231 R 4DN M64799 M64799 None GEN- Histamine receptor H2 802 802G>A V268M 4DN M65028 M65028 602372 GEN- Human hnRNP type A/B 273 131C>G P44R 3FM protein mRNA, complete cds M65028 M65028 602372 GEN- Human hnRNP type A/B 595 453C>G S 3FM protein mRNA, complete cds M65028 M65028 602372 GEN- Human hnRNP type A/B 1255 1113A>G 3 3FM protein mRNA, complete cds KAR1 M65066 176911 GEN- Human cAMP-dependent 1424 1424C>G 3 SD-144146.1 Page 11 3FK protein kinase regulatory subunit Ri-beta mRNA, 3 end PRKAR1 M65066 176911 GEN- Human cAMP-dependent 1514 1514G>C B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end PRKAR1 M65066 176911 GEN- Human cAMP-depen B 3FK protein kinase regulatory subunit Rl-beta mRNA 3 end PRKAR1 M65066 176911 GEN- Human cAMP-dependent 1862 1862G>A B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end PRKAR1 M65066 176911 GEN- Human cAMP-dependent 2139 21390T B 3FK protein kinase regulatory subunit Rl-beta mRNA, 3 end C5 M65134 120900 GEN- Human complement 1171 1171A>G 1391V 3FT component C5 mRNA, 3end EDN2 M65199 131241 GEN- Endothelin 2 384 314C>T A105V CBS EDN2 M65199 131241 GEN- Endothelin ? 997 927A>G 3 CBS EDN2 M65199 131241 GEN- Endothelin 2 997 927A>G 3 CBS M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1500 1353T>A S M67439 M67439 126453 GEN-4E1 Dopamine Receptor D5 1512 1365G>A F M67439 M67439 126453 GEN-4EI Dopamine Receptor D5 1566 1419G>A S M69013 M69013 139313 GEN-7L Guanine nucleotide binding 957 771 C>T S protein (G protein), alpha 11 IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 751 751 A>C factor binding protein 6 (IGFBP6) mRNA complete mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 835 835A>C factor binding protein 6 (IGFBP6) mRNA, complete SD-144146 1 Page 11 mature peptide IGFBP6 M69054 146735 GEN-3J0 Human insulin-like growth 850 850G>A factor binding protein 6 (IGFBP6) mRNA, complete mature peptide M69226 M69226 309850 GEN-3Z Monoamine oxidase A 435 385A>C S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 936 886C>T F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 941 891T>G S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1076 1026A>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1373 1323G>A F M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410C>T S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1460 1410OT S M69226 M69226 309850 GEN-3Z Monoamine oxidase A 1609 1559A>G K520R SRD5A2 M74047 264600 GEN- Human steroid 5-alpha- 2379 2352A>G 3 CDC reductase 2 (SRD5A2) mRNA, complete cds M74782 M74782 308385 GEN-64 Interleukin 3 receptor.alpha 1396 1250OT 3 (low affininty) M77829 M77829 107776 GEN- Human channel-like 172 134C>T A45V 3QJ integral membrane protein (CHIP28) mRNA, complete cds M77829 M77829 107776 GEN- Human channel-like 1249 1211 C>G 3 3QJ integral membrane protein (CHIP28) mRNA, complete cds PAX6 M77844 106210 GEN- H.sapiens oculorhombin 669 307C>T F 3QG (aniridia) mRNA, complete cds M80646 M80646 274180 GEN-40 Thromboxane synthase 756 585G>C S M80646 M80646 274180 GEN-40 Thromboxane synthase 1240 1069C>G L357V M81181 M81181 182331 GEN-G4 ATPase, Na+/K+ 107 (-301)C>G 5 transporting, beta 2 polypeptide M81181 M81181 182331 GEN-G4 ATPase, Na+/K+ 1070 663C>A S transporting, beta 2 polypeptide M81181 M81181 182331 GEN-G4 ATPase, Na+/K+ 1974 1567C>A 3 SD-144146.1 Page 1 15 transporting, beta 2 polypeptide M81181 M81181 182331 GEN-G4 ATPase, Na+/K+ 2364 1957T>C 3 transporting, beta 2 polypeptide THBS2 M81339 188061 GEN- Human thrombospondin 1684 16850T 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 1920 1921 C>T 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 2034 2035T>G 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 2331 2332C>T 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 2561 2562C>T 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 2655 2656C>T 3 3VQ mRNA THBS2 M81339 188061 GEN- Human thrombospondin 2729 2730C>T 3 3VQ mRNA M81590 M81590 182131 GEN- Serotonin 5-HT receptors 190 129C>T S 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 432 371T>G F124C 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 922 861 G>C S 3VZ 5-HT1 D M81590 M81590 182131 GEN- Serotonin 5-HT receptors 1241 1180G>A 3 3VZ 5-HT1 D M81757 M81757 603474 GEN- H.sapiens S19 ribosomal 276 254A>T N85I 3W6 protein mRNA, complete cds M81757 M81757 603474 GEN- H.sapiens S19 ribosomal 338 316G>A A106T 3W6 protein mRNA, complete cds M81757 M81757 603474 GEN- H.sapiens S19 ribosomal 496 474G>A 3 3W6 protein mRNA, complete cds M81768 M81768 107310 GEN-G6 Solute carrier family 9 3042 2989G>A 3 (sodium/hydrogen exchanger) M82962 M82962 600388 GEN- Human N-benzoyl-L- 2316 2307T>G 3 3XC tyrosyl-p-amino-benzoic SD-144146.1 Page 11 acid hydrolase alpha subunit (PPH alpha) mRNA, complete cds M82962 M82962 600388 GEN- Human N-benzoyl-L- 2428 2419A>C 3 3XC tyrosyl-p-amino-benzoic acid hydrolase alpha subunit (PPH alpha) mRNA, complete cds CHRNA5 M83712 1 18505 GEN- Nicotinic, Cholinergic 1340 1192G>A D398N 3YQ receptor alpha 5 M84526 M84526 134350 GEN- Human 46 (-9)C>T 5 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 399 345C>A S 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 408 354A>G S 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 859 805C>T 3 3ZL adipsin/complement factor D mRNA, complete cds M84526 M84526 134350 GEN- Human 891 837G>C 3 3ZL adipsin/complement factor D mRNA, complete cds M84747 M84747 300007 GEN-45 Interleukin 9 receptor 1273 1094G>A R365H M84755 M84755 162641 GEN-46 Neuropeptide Y1 1121 1121A>C K374T TGFBR2 M85079 190182 GEN- Human TGF-beta type II 2045 1710A>C 3 3ZS receptor mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 1653 1569T>A 3 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2599 2515C>G 3 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2619 2535A>C 3 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2656 2572A>C 3 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2745 2661C>T 3 40Y mRNA, complete cds YWHAZ M86400 601288 GEN- Human phospholipase A2 2761 2677A>C 3 SD-144146.1 Page 115 mRNA, complete cds GJB2 M86849 121011 GEN-41 L Human connexin 26 1947 1948T>G 3 (GJB2) mRNA GJB2 M86849 121011 GEN-41 L Human connexin 26 2035 2036A>G 3 (GJB2) mRNA OSBP M86917 167040 GEN-425 Human oxysterol-binding 216 (-265)T>G 5 protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 802 322C>T F protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 888 408C>T S protein (OSBP) mRNA, complete cds OSBP M86917 167040 GEN-425 Human oxysterol-binding 934 454T>G S152A protein (OSBP) mRNA, complete cds M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 296 16T>C S6P M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 413 133G>A G45R M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 853 573T>C S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1342 1062A>G S M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1430 1150T>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 11660A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1446 1166C>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1453 1173A>G 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1677 1397G>A 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1797 1517G>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1885 1605C>T 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 1916 1636T>C 3 M87290 M87290 106165 GEN-19 Angiotensin receptor AT1 2158 1878A>G 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2159 2062G>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2186 2089- 3 2094ATATTA >ATATTA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2 2118866 2089- 3 SD-144146.1 Page 1 15 2094delATAT TA M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2230 2133A>G 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2339 2242T>C 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2409 2312G>A 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2726 2629C>T 3 M90100 M90100 600262 GEN-1A Cyclooxygenase 2 COX2 2983 2886C>T 3 M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 3846 3846C>T S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 5505 5505G>A S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6582 6582A>G S splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6613 6613G>C G2205R splice) L-Type M92269 M92269 114205 GEN-SV Ca Channel alphalc (alt. 6614 6614G>C G2205A splice) L-Type PNLIP M93285 246600 GEN- Pancreatic lipase (PNLIP) 646 646G>T V216L 48N (Dietary supplement) M95678 M95678 604114 GEN- Homo sapiens 1346 1182T>C S 4A6 phospholipase C-beta-2 mRNA, complete cds M95678 M95678 604114 GEN- Homo sapiens 3436 3272A>G E1091 G 4A6 phospholipase C-beta-2 mRNA, complete cds M95678 M95678 604114 GEN- Homo sapiens 4137 3973C>T 3 4A6 phospholipase C-beta-2 mRNA, complete cds M95708 M95708 107271 GEN-SF Homo sapiens Ly-6-like 497 435C>T 3 protein (CD59) mRNA, complete cds M96652 M96652 147851 GEN-65 Interleukin 5 receptor alpha 883 634T>G S212A GJA4 M96789 121012 GEN- Homo sapiens connexin 37 211 147G>A S 4B1 (GJA4) mRNA, complete cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 620 556G>A V186M 4B1 (GJA4) mRNA, complete cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 1019 955C>T P319S 4B1 (GJA4) mRNA, complete SD-144146.1 Page 11 cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 1179 1115A>G 4B1 (GJA4) mRNA, complete cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 1223 1159C>A 4B1 (GJA4) mRNA, complete cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 1411 1347G>A 4B1 (GJA4) mRNA, complete cds GJA4 M96789 121012 GEN- Homo sapiens connexin 37 1477 1413C>G 4B1 (GJA4) mRNA, complete cds M98539 M98539 176803 GEN-SW prostaglandin D2 synthase 157 158C>A gene S70154 S70154 100678 GEN-GY ACAT2 669 632A>G K211 R S70154 S70154 100678 GEN-GY ACAT2 820 783T>C S S70154 S70154 100678 GEN-GY ACAT2 820 783T>C S S70154 S70154 100678 GEN-GY ACAT2 856 819G>A S S70154 S70154 100678 GEN-GY ACAT2 856 819G>A S S70154 S70154 100678 GEN-GY ACAT2 1388 1351T>G 3 S70154 S70154 100678 GEN-GY ACAT2 1395 1358- 3 1362CTTFA> CTTTA S70154 S70154 100678 GEN-GY ACAT2 1395 1358- 1362delCTTT A S70154 S70154 100678 GEN-GY ACAT2 1419 1382C>A S70154 S70154 100678 GEN-GY ACAT2 1419 1382C>A ADCYAP S83513 102980 GEN- pituitary adenylate cyclase 1521 1520G>A 1 3YA activating polypeptide [human, mRNA, 1940 nt] U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3377 3316A>C U00672 U00672 146933 GEN-4A Interleukin 10 receptor 3524 3463A>G U00968 U00968 184756 GEN-UU Human SREBP-1 mRNA, 3983 3817G>A complete cds U02031 U02031 600481 GEN-WD Human sterol regulatory 1089 972G>A element binding protein-2 mRNA, complete cds SD-144146. Page 1 1 U03642 U03642 None GEN- Human G protein-coupled 333 135A>C S KUU receptor APJ gene, complete cds U03642 U03642 None GEN- Human G protein-coupled 1096 898G>A V300I KUU receptor APJ gene, complete cds U03858 U03858 600007 GEN- Fms-related tyrosine 683 600C>T S MDM kinase 3 ligand U03858 U03858 600007 GEN- Fms-related tyrosine 1016 933T>C 3 MDM kinase 3 ligand U04270 U04270 152427 GEN-H6 Potassium channel subunit 1650 1467C>T S (h-erg) U04270 U04270 152427 GEN-H6 Potassium channel subunit 3888 3705A>C 3 (h-erg) HADHA U04627 600890 GEN-155 Human 78 kDa gastrin- 1507 1507G>A V503M binding protein mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 632 239C>T S80L 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 837 444G>C S 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 882 4890T S 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 945 552T>C S 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1119 726C>G S I SP PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1131 7380T S 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1134 741C>T S 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1193 800T>A L267Q 15P PITSLRE alpha 1 mRNA. complete cds SD-144146. Page 1 1 CDC2L1 U04815 139380 GEN- Human protein kinase 1266 873T>C 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1314 921 G>T K307N 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1692 1299C>A D433E 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1700 1307T>A L436Q 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1706 1313A>G E438G 15P PITSLRE alpha 1 mRNA, complete cds CDC2L1 U04815 139380 GEN- Human protein kinase 1776 1383C>T 15P PITSLRE alpha 1 mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 38 15C>T dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 282 259A>T S87C dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 350 327C>T dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 365 342T>C dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 464 441 G>A dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 474 451A>G M151V dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 532 509A>G H170R dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 538 515T>A L172Q dehydrogenase mRNA, SD- 144146.1 Page 1 1 complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 689 666T>C S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 806 783G>A S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 872 849G>T S dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 952 929T>G 131 OS dehydrogenase mRNA, complete cds DDH 1 U05598 600450 GEN-184 Human dihydrodiol 1020 997G>A 3 dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1035 1012G>A 3 dehydrogenase mRNA, complete cds DDH1 U05598 600450 GEN-184 Human dihydrodiol 1 1 12 1089C>T 3 dehydrogenase mRNA, complete cds HSD17B3 U05659 264300 GEN-186 Human 17beta- 894 846G>C S hydroxysteroid dehydrogenase type 3 mRNA, complete cds U07225 U07225 600041 GEN- P2Y2 purinoceptor 2008 1763G>A 3 1 DM U091 17 U091 17 602142 GEN- Phospholipase C delta-1 333 239G>A R80H 1 GC U091 17 U091 17 602142 GEN- Phospholipase C delta-1 460 366G>A S 1 GC U091 17 U091 17 602142 GEN- Phospholipase C delta-1 1858 1764G>A S 1GC SLC18A3 U09210 600336 GEN- Human vesicular 838 396T>C S 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 1369 927A>G S 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 1567 11250G S SD-144146. Page 1 1 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2080 1638G>T 3 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2199 1757G>A 3 4F3 acetylcholine transporter mRNA, complete cds SLC18A3 U09210 600336 GEN- Human vesicular 2349 1907G>T 3 4F3 acetylcholine transporter mRNA, complete cds U09648 U09648 600650 GEN-11 Camitine 2556 2040G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2675 2159G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2792 2276G>A 3 Palmitoyltransferase II U09648 U09648 600650 GEN-11 Camitine 2825 2309G>A 3 Palmitoyltransferase II U09759 U09759 602896 GEN- Human protein kinase 303 152A>G N51 S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1079 928A>G 1310V 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1280 1129C>T P377S 1 HA (JNK2) mRNA, complete cds U09759 U09759 602896 GEN- Human protein kinase 1559 1408OT 3 1 HA (JNK2) mRNA, complete cds U09806 U09806 None GEN- Human 120 120T>C S 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 473 473G>A R158Q 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 550 550C>T F 4FZ methylenetetrahydrofolate SD-144146.1 Page 11 reductase mRNA, partial cds U09806 U09806 None GEN- Human 668 668C>T A223V 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1059 1059T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1289 1289C>A E430A 4FZ methylenetetrahydrofolate reductase mRNA, partial cds U09806 U09806 None GEN- Human 1308 1308T>C 4FZ methylenetetrahydrofolate reductase mRNA, partial cds THPO U11025 600044 GEN- Human megakaryocyte 76 41T>C L14P 1JW growth and development factor (MGDF) mRNA, complete cds THPO U11025 600044 GEN- Human megakaryocyte 172 137G>A R46K 1JW growth and development factor (MGDF) mRNA, complete cds THPO U11025 600044 GEN- Human megakaryocyte 382 347G>A G116E 1JW growth and development factor (MGDF) mRNA, complete cds THPO U11025 600044 GEN- Human megakaryocyte 674 639T>A 1JW growth and development factor (MGDF) mRNA, complete cds THPO U11025 600044 GEN- Human megakaryocyte 1132 1097G>A 1JW growth and development factor (MGDF) mRNA, complete cds U12507 U12507 600681 GEN- Cardiac inward rectifier 338 13C>A 1MD potassium channel (HH- IRK1 ) SD-144146.1 Page 1 1 U12507 U12507 600681 GEN- Cardiac inward rectifier 1597 1272G>A S 1 MD potassium channel (HH- IRK1 ) U 12789 U 12789 600234 GEN-4F HMG CoA synthase 720 720T>A H240Q (HSH1) mitochondrial U 13737 U13737 600636 GEN- Human cysteine protease 2356 2132A>C 3 1 PC CPP32 isoform alpha mRNA, complete cds U13737 U13737 600636 GEN- Human cysteine protease 2535 2311 C>T 3 1 PC CPP32 isoform alpha mRNA, complete cds CTGF U14750 121009 GEN- Human connective tissue 1878 1878A>C 3 1 S3 growth factor mRNA, partial cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 149 122A>C E41A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 402 375G>A S 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 802 775C>G P259A 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U16660 U16660 600696 GEN- Human peroxisomal enoyl- 1157 1130G>A 3 1YD CoA hydratase-like protein (HPXEL) mRNA, complete cds U 16957 U16957 300034 GEN-1 L Angiotensin receptor AT2 263 123T>C S U 16957 U 16957 300034 GEN-1 L Angiotensin receptor AT2 883 743G>A R248K STAR U17280 600617 GEN-208 Human steroidogenic 1439 1313C>T 3 acute regulatory protein (StAR) mRNA, complete cds N0S1 U17327 163731 GEN-209 Human neuronal nitric 3391 2706C>T S oxide synthase (NOS1 ) mRNA, complete cds U 19487 U19487 176804 GEN-4I PROSTAGLANDIN E2 85 (-72)A>G 5 RECEPTOR, EP2 SD-144146.1 Page 11 oo vo CO --j ' o 3; <g -*- -5.--: -5. _.: 2 2 -4. X A x A X A X A X 7 --- C co ^- c *— co -- co -- co - ^ rn ^ rn _- rn _- rQ <^- rn 2 CN CM UJ c LU CM LU M UJ ■ ' UJ CD ± ± CD CD CD CD 2 Z CD P O C CD u j u j n CD CD U U vd - m . o cD CD CD cD m Lo r--- - r- - r^ -j- CO h- in oo cO CO CO C CN CN CD CD CO CD CD ^i -j- 1^ -- -- in m m in co co ---- -r -j- ^-r -r ^r -n o- O O o o o o -^- - r^ r^- i^- i^ - -j- τ- 1- CM CM CN CM CM CM CN CM CM CM CM CM CM •— ■ 3 3 3 3 3 3 3 3 3 3 3 3 3 Q oo U27467 U27467 601056 GEN- Human Bcl-2 related (Bfl-1) 616 582G>A 3 2BX mRNA, complete cds U31628 U31628 601070 GEN-4J Interleukin 15 receptor 1250 1168G>T 3 alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1266 1205OA P402Q alpha chain U32324 U32324 600939 GEN-4K interleukin 11 receptor 1513 1452C>T 3 alpha chain U32500 U32500 162642 GEN-1 P Neuropeptide Y2 407 159C>T S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1P Neuropeptide Y2 833 585T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1184 936T>C S U32500 U32500 162642 GEN-1P Neuropeptide Y2 1706 1458- 3 1460TAT>TA T U32500 U32500 162642 GEN-1 P Neuropeptide Y2 1706 1458- 3 1460delTAT U32500 U32500 162642 GEN-1 P Neuropeptide Y2 2782 2534 Λ 2535ins F CA U32989 U32989 191070 GEN- Human tryptophan 991 927G>A S 2JH oxygenase (TDO) mRNA, complete cds U33052 U33052 602549 GEN-2JL Human lipid-activated, 34 25G>C E9Q protein kinase PRK2 mRNA, complete cds U33052 U33052 602549 GEN-2JL Human lipid-activated, 430 421T>C S protein kinase PRK2 mRNA, complete cds U33052 U33052 602549 GEN-2J Human lipid-activated, 1112 1103T>G F368C protein kinase PRK2 mRNA, complete cds GSS U34683 601002 GEN- Human glutathione 364 324G>A S 2LF synthetase mRNA, complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 300 291T>C S 2MX factor 8 (FGF-8) mRNA, complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 645 636G>C S 2MX factor 8 (FGF-8) mRNA, SD-144146.1 Page 116 complete cds FGF8 U36223 600483 GEN- Human fibroblast growth 648 639A>G S 2MX factor 8 (FGF-8) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 736 693G>A S 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1285 1242T>C 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1294 1251T>C 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1580 1537A>T 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1621 1578G>T 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1715 1672G>A 3 20C alpha (Mch3) mRNA, complete cds U37448 U37448 601761 GEN- Human Mch3 isoform 1764 1721 G>A 3 20C alpha (Mch3) mRNA, complete cds U38545 U38545 602382 GEN- Human ARF-activated 3100 3005T>G F1002C 2PB phosphatidylcholine- specific phospholipase D1a (hPLD1) mRNA, complete cds U40002 U40002 151750 GEN- Human hormone-sensitive 2076 1799C>A P600H 2RH lipase testicular isoform mRNA, complete cds U40038 U40038 600998 GEN-70 Guanine nucleotide binding 825 783C>T S protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 878 836T>C L279P protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1029 987G>A S protein (G protein), q SD-144146.1 Page 1 17 polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1051 1009A>G I337V protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1068 1026T>A S protein (G protein), q polypeptide U40038 U40038 600998 GEN-70 Guanine nucleotide binding 1093 1051T>C S protein (G protein), q polypeptide U40347 U40347 600950 GEN- Human serotonin N- 382 148G>A E50K 2RK acetyltransferase mRNA, complete cds U40396 U40396 602691 GEN-6W Steroid receptor 285 229A>C K77Q coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 314 258A>T K86N coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 336 280C>T P94S coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 688 632C>T T211 I coactivator (SRC-1) U40396 U40396 602691 GEN-6W Steroid receptor 970 914C>A A305E coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 1511 1455G>A S coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 2377 23210T T774M coactivator (SRC-1 ) U40396 U40396 602691 GEN-6W Steroid receptor 2730 2674C>T P892S coactivator (SRC-1 ) U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 661 654T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 697 690A>G S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 940 933G>A S receptor alpha 7 U40583 U40583 1 18511 GEN-40 Nicotinic, Cholinergic 1276 1269T>C S receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1790 1783A>T 3 receptor alpha 7 U40583 U40583 118511 GEN-40 Nicotinic, Cholinergic 1792 1785T>A 3 receptor alpha 7 SD-144146 1 Page 1 1 U43142 U43142 601528 GEN- Human vascular 1499 1128C>T 2UM endothelial growth factor related protein VRP mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1424 1228A>G mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1604 1408C>G mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1719 1523G>A mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 1827 1631G>A mRNA, complete cds U45448 U45448 600845 GEN-4FI Human P2x1 receptor 2286 2090G>A mRNA, complete cds U48730 U48730 601511 GEN-JA Transcription Factor Stat5b 494 484T>C S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 496 486A>G S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 499 489A>G S U48730 U48730 601511 GEN-JA Transcription Factor Stat5b 502 492G>A S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 570 560G>C G187A U48730 U48730 601511 GEN-JA Transcription Factor Stat5b 573 563C>A P188Q U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1003 993G>A S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1063 1053T>C S U48730 U48730 601511 GEN-JA Transcription Factor Stat5b 1066 1056G>A S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1105 1095C>T S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1159 1149C>T S U48730 U48730 601511 GEN-JA Transcription Factor Statδb 1969 1959C>T S U49516 U49516 312861 GEN-1 Q Serotonin 5-HT receptors 2915 2187A>C 3 5-HT2C U49516 U49516 312861 GEN-1 Q Serotonin 5-HT receptors 2947 2219A>G 5-HT2C U50929 U50929 602888 GEN-JF Methionine synthetase 2017 1991A>G (aka homocysteine methyltransferase) U50929 U50929 602888 GEN-JF Methionine synthetase 2418 2392A>T (aka homocysteine methyltransferase) U51478 U51478 601867 GEN- Human sodium/potassium- 1099 1071 G>C 31Z transporting ATPase beta- 3 subunit mRNA, complete SD-144146.1 Page 1172 cds U51478 U51478 601867 GEN- Human sodium/potassium- 1121 1093T>C 3 31Z transporting ATPase beta- 3 subunit mRNA, complete cds U51478 U51478 601867 GEN- Human sodium/potassium- 1133 1105G>T 31Z transporting ATPase beta- 3 subunit mRNA, complete cds U56390 U56390 602234 GEN- Human cysteine protease 411 408C>T 36X ICE-LAP6 mRNA, complete cds U56976 U56976 171891 GEN-379 Human calmodulin 1510 14760T dependent phosphodiesterase PDE1 B1 mRNA, complete cds DES U59167 125660 GEN- Human desmin mRNA, 140 60C>G S 39F complete cds DES U59167 125660 GEN- Human desmin mRNA, 905 825T>C S 39F complete cds DES U59167 125660 GEN- Human desmin mRNA, 1091 1011 C>G S 39F complete cds DES U59167 125660 GEN- Human desmin mRNA, 1181 1101G>A S 39F complete cds DES U59167 125660 GEN- Human desmin mRNA, 2176 2096C>A 3 39F complete cds U60519 U60519 601762 GEN- Human apoptotic cysteine 304 157G>A E53K 3AZ protease Mch4 (Mch4) mRNA, complete cds U60519 U60519 601762 GEN- Human apoptotic cysteine 324 177A>G 3AZ protease Mch4 (Mch4) mRNA, complete cds CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2296 1742C>G 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2387 1833C>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2504 1950G>T 3 4EN receptor alpha 2 CHRNA2 U62431 118502 GEN- Nicotinic, Cholinergic 2538 1984G>A 3 4EN receptor alpha 2 SD-144146.1 Page 1 1 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 870 639C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 909 678C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1440 1209T>G S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1440 1209T>G S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1458 1227C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1584 1353G>A S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1781 1550C>T S517L receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1860 1629C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1860 1629C>T S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1890 1659G>A S receptor alpha 4 U62433 U62433 118504 GEN-4P Nicotinic, Cholinergic 1890 1659G>A S receptor alpha 4 U62768 U62768 151300 GEN- Human oxytocinase splice 3356 3295G>C 3 3CR variant 1 mRNA, complete cds U62768 U62768 151300 GEN- Human oxytocinase splice 3547 3486C>T 3 3CR variant 1 mRNA, complete cds U70136 U70136 600044 GEN-4R Thrombopoietin 4138 4105G>T A1369S U70136 U70136 600044 GEN-4R Thrombopoietin 4141 4108T>A F1370I U70867 U70867 601460 GEN-4S prostaglandin transporter 2706 2615T>G 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 2839 2748T>A 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 2908 2817A>G 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3171 3080A>G 3 SD- 144146.1 Page 1 17 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3171 3080A>G 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3253 3162A>G 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3255 3164A>G 3 hPGT U70867 U70867 601460 GEN-4S prostaglandin transporter 3594 3503T>A 3 hPGT U71321 U71321 602623 GEN- Human FK506-binding 1248 1095C>T S 2TW protein FKBP51 mRNA, complete cds U71321 U71321 602623 GEN- Human FK506-binding 1425 1272G>A S 2TW protein FKBP51 mRNA, complete cds U73338 U73338 156570 GEN-69 Methionine Synthase 1158 764G>A C255Y U73338 U73338 156570 GEN-69 Methionine Synthase 5095 4701G>A 3 U73338 U73338 156570 GEN-69 Methionine Synthase 6750 6356G>A 3 U78294 U78294 603697 GEN- Homo sapiens 15S- 2449 2378A>G 3 3QZ lipoxygenase mRNA, complete cds U79269 U79269 123829 GEN-K7 Cyclin-Dependent Protein 1281 972A>T Kinase U81375 U81375 602193 GEN- Human placental 1989 1811G>A 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 1996 1818C>T 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U81375 U81375 602193 GEN- Human placental 2045 1867T>C 3VO equilibrative nucleoside transporter 1 (hENTI ) mRNA, complete cds U82812 U82812 602592 GEN- Human scavenger receptor 1280 1220T>A 3X7 cysteine rich Sp alpha mRNA, complete cds U96781 U96781 108730 GEN- ATPase, Ca++ 3007 3007G>A MQL transporting, cardiac muscle, fast twitch 1 SD-144146.1 Page 1 17 HBA1 V00493 141800 GEN-TK Human messenger RNA 198 161 C>T A54V for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 244 207C>A N69K for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 307 270C>A H90Q for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 314 277C>T R93W for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 326 289G>T V97F for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 393 356C>A T119N for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 399 362C>G A121G for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 418 381 C>A D127E for alpha globin HBA1 V00493 141800 GEN-TK Human messenger RNA 481 444A>G 3 for alpha globin V00497 V00497 141900 GEN-P1 Human messenger RNA 59 9C>T S for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 257 207OA S for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 284 234C>A H78Q for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 304 254C>A T85N for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 370 320T>C L107P for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 385 335T>G V112G for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 529 479T>G 3 for beta-globin V00497 V00497 141900 GEN-P1 Human messenger RNA 537 487T>G 3 for beta-globin V00519 V00519 139250 GEN-4U Growth hormone 1 299 259C>A P87T V00519 V00519 139250 GEN-4U Growth hormone 1 524 484G>T G162W X00568 X00568 207750 GEN-6Z Apolipoprotein C-ll 70 70C>A Q24K X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 687 424A>G S142G CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 2823 2560delT F CD71) SD-144146.1 Page 1 1 X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 3766 3503T>G 3 CD71) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4122 3859A>C 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4147 3884G>A 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4247 3984T>C 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4309 4046T>A 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4381 4118A>G 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4547 4284G>A 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4619 4356T>G 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4726 4463A>T 3 CD71 ) X01060 X01060 190010 GEN-6C Transferrin receptor (p90, 4766 4503OT 3 CD71) X01586 X01586 147680 GEN-PC Interleukin 2 332 225T>G H75Q X01586 X01586 147680 GEN-PC Interleukin 2 563 456G>A S X02317 X02317 147450 GEN-KM Superoxide dismutase 1 614 550A>C 3 (Cu/Zn) X02415 X02415 134850 GEN- Human gene for fibrinogen 1000 949G>A D317N MJO gamma chain X02469 X02469 191170 GEN-PF Human mRNA for p53 350 215C>G P72R cellular tumor antigen X02469 X02469 191170 GEN-PF Human mRNA for p53 953 818G>A R273H cellular tumor antigen X02750 X02750 176860 GEN-4Z Anticoagulant Protein C 1600 1503G>C 3 (inactivator of coagulation factors Va and Villa) NRAS X02751 164790 GEN-XG Human N-ras mRNA and 221 (-506)A>G 5 flanking regions NRAS X02751 164790 GEN-XG Human N-ras mRNA and 390 (-337)C>A 5 flanking regions X02812 X02812 190180 GEN-XR Human mRNA for 870 29C>T P10L transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 979 138C>G I46M SD-144146.1 Page 1 1 transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1632 791 C>T T2641 transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1807 966C>T S transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1930 1089G>A s transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 1942 1101 C>T s transforming growth factor- beta (TGF-beta) X02812 X02812 190180 GEN-XR Human mRNA for 2013 1172G>A S391 N transforming growth factor- beta (TGF-beta) X03172 X03172 192340 GEN-ZM Human mRNA for 379 356T>G V119G vasopressin precursor X03438 X03438 138970 GEN-PM Human mRNA for 586 555G>A S granulocyte colony- stimulating factor (G-CSF) X03438 X03438 138970 GEN-PM Human mRNA for 1235 1204C>T 3 granulocyte colony- stimulating factor (G-CSF) X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 390 30T>C S X03635 X03635 133430 GEN-50 estrogen receptors 424 64G>C E22Q X03635 X03635 133430 GEN-50 estrogen receptors 617 257C>T A86V X03635 X03635 133430 GEN-50 estrogen receptors 621 261 G>C S X03635 X03635 133430 GEN-50 estrogen receptors 829 469C>T F X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1335 975C>G S X03635 X03635 133430 GEN-50 estrogen receptors 1451 1091T>A V364E X03635 X03635 133430 GEN-50 estrogen receptors 1674 1314G>A M438I X03635 X03635 133430 GEN-50 estrogen receptors 2142 1782A>G S X03635 X03635 133430 GEN-50 estrogen receptors 2354 1994A>G 3 X03635 X03635 133430 GEN-50 estrogen receptors 2550 2190A>C 3 X03635 X03635 133430 GEN-50 estrogen receptors 2733 2373C>G SD-144146.1 Page 1 1 X03635 X03635 133430 GEN-50 estrogen receptors 3181 2821T>C X03635 X03635 133430 GEN-50 estrogen receptors 3338 2978C>T X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3294CCT>CC T X03635 X03635 133430 GEN-50 estrogen receptors 3652 3292- 3294delCCT X03635 X03635 133430 GEN-50 estrogen receptors 3896 3536C>A X03635 X03635 133430 GEN-50 estrogen receptors 4378 4018T>C X03635 X03635 133430 GEN-50 estrogen receptors 6287 5927T>C X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3732 3432T>C receptor X03663 X03663 164770 GEN-51 Colony stimulating factor 1 3951 3651 C>A receptor X03747 X03747 182330 GEN-KR ATPase, Na+/K+ 447 321 G>A transporting, beta 1 polypeptide X03747 X03747 182330 GEN-KR ATPase, Na+/K+ 1516 1390G>T transporting, beta 1 polypeptide X03747 X03747 182330 GEN-KR ATPase, Na+/K+ 2182 2056C>T transporting, beta 1 polypeptide CYBB X0401 1 306400 GEN- Human mRNA of X-CGD 2517 2310A>G 13S gene involved in chronic granulomatous disease located on chromosome X CYBB X04011 306400 GEN- Human mRNA of X-CGD 2544 2337A>T 13S gene involved in chronic granulomatous disease located on chromosome X CYBB X04011 306400 GEN- Human mRNA of X-CGD 2831 2624T>C 13S gene involved in chronic granulomatous disease located on chromosome X CAT X04076 115500 GEN- Human kidney mRNA for 51 (-20)T>C 5 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 218 148C>T L50F ISP catalase CAT X04076 1 15500 GEN- Human kidney mRNA for 1237 1167T>C S SD-144146 1 Page 11 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 1325 1255C>T S 13P catalase CAT X04076 115500 GEN- Human kidney mRNA for 2131 2061A>C 3 13P catalase HMBS X04217 176000 GEN-145 Human mRNA for 121 40G>T A14S porphobilinogen deaminase (PBG-D, EC 4 3 1 8) X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 363 351 C>T S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 525 513C>T S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 967 955C>A R319S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1023 1011OA S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1083 1071 C>T S protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1213 1201T>G 3 protein (G protein), alpha stimulating activity polypeptide 1 X04409 X04409 139320 GEN-7Q Guanine nucleotide binding 1450 1438A>C 3 protein (G protein), alpha stimulating activity polypeptide 1 X04526 X04526 139380 GEN-7R Guanine nucleotide binding 426 146G>C R49T protein (G protein) beta polypeptide 1 THBS1 X04665 188060 GEN-151 Human mRNA for 145 70T>G S24A SD-144146 1 Page 11 thrombospondin THBS1 X04665 188060 GEN-151 Human mRNA for 903 828G>A S thrombospondin THBS1 X04665 188060 GEN-151 Human mRNA for 1485 1410C>T S thrombospondin THBS1 X04665 188060 GEN-151 Human mRNA for 3667 3592C>T 3 thrombospondin THBS1 X04665 188060 GEN-151 Human mRNA for 3866 3791 G>A 3 thrombospondin X05199 X05199 173350 GEN-PU Human mRNA for 384 330C>T S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 825 771 C>T S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 996 942C>T S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 1137 1083A>G S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 1485 1431C>T S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 2340 2286T>G S plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 2532 2478G>A 3 plasminogen X05199 X05199 173350 GEN-PU Human mRNA for 2606 2552T>G 3 plasminogen X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 83 (-54)G>C 5 X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 940 804G>A S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1327 1191T>C S X06318 X06318 176970 GEN-KY Protein kinase C, beta 1 1906 1770C>T S PDGFA X06374 173430 GEN- Human mRNA for platelet- 2223 1820C>T 3 19E derived growth factor PDGF-A PDGFA X06374 173430 GEN- Human mRNA for platelet- 2267 1864C>T 3 19E derived growth factor PDGF-A RAF1 X06409 164760 GEN- Human mRNA fragment for 486 487T>C 3 19K activated c-raf-1 (exons 8- 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1947 1948C>T 3 19K activated c-raf-1 (exons 8- SD-144146.1 Page 11 17) RAF1 X06409 164760 GEN- Human mRNA fragment for 1992 1993C>A 19K activated c-raf-1 (exons 8- 17) X06562 X06562 600946 GEN-6D Growth hormone receptor 3392 3349A>T 3 X06562 X06562 600946 GEN-6D Growth hormone receptor 4145 4102G>A 3 X07523 X07523 134371 GEN- Human mRNA for 1170 1097G>A G366E 1 E5 truncated form of complement factor H X07523 X07523 134371 GEN- Human mRNA for 1277 1204T>C Y402H 1 E5 truncated form of complement factor H S0D2 X07834 147460 GEN- Human mRNA for 44 40C>G P14A 1ES manganese superoxide dismutase (EC 1 15 1 1 ) S0D2 X07834 147460 GEN- Human mRNA for 51 47T>C V16A 1 ES manganese superoxide dismutase (EC 1 15 1 1) S0D2 X07834 147460 GEN- Human mRNA for 198 194C>A T65N 1 ES manganese superoxide dismutase (EC 1 15 1 1 ) S0D2 X07834 147460 GEN- Human mRNA for 249 245T>C I82T 1 ES manganese superoxide dismutase (EC 1 15 1 1 ) TNNC1 X07897 191040 GEN- Human mRNA for slow 234 208G>C G70R 1 EW skeletal troponin C (TnC) TNNC1 X07897 191040 GEN- Human mRNA for slow 249 223G>T D75Y 1EW skeletal troponin C (TnC) ITGB1 X07979 135630 GEN- Human mRNA for 1189 1086A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 1279 1176A>C S 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2713 2610T>C 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 2878 2775T>A 3 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3339 3236A>G 3 SD-144146 1 Page 11 4E5 fibronectin receptor beta subunit ITGB1 X07979 135630 GEN- Human mRNA for 3531 3428G>A 3 4E5 fibronectin receptor beta subunit ANX5 X12454 131230 GEN- Human mRNA for vascular 128 (-DOT 5 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1413 1285T>G 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1431 1303C>T 3 1 M2 anticoagulant ANX5 X12454 131230 GEN- Human mRNA for vascular 1518 1390OA 3 1M2 anticoagulant X13561 X13561 147910 GEN- Human mRNA for 54 18G>T S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 441 405T>C S 10H preprokallikrein (EC 3.4.21 ) X13561 X13561 147910 GEN- Human mRNA for 469 433G>C E145Q 10H preprokallikrein (EC 3.4.21) X13561 X13561 147910 GEN- Human mRNA for 592 556A>G K186E 10H preprokallikrein (EC 3.4.21 ) X13589 X13589 107910 GEN-56 Cytochrome P450, 364 240A>G S subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 914 790C>T R264C subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1655 1531C>T subfamily XIX (aromatization of androgens) X13589 X13589 107910 GEN-56 Cytochrome P450, 1796 1672G>T subfamily XIX (aromatization of androgens) SD-144146.1 Page 1 1 X13629 X13629 107690 GEN- Human intestinal mRNA for 881 836G>A R279K 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1185 1140G>T Q380H 100 apolipoprotein A-IV X13629 X13629 107690 GEN- Human intestinal mRNA for 1302 1257 Λ 1258ins F 100 apolipoprotein A-IV CTGT X13916 X13916 107770 GEN- Human mRNA for LDL- 1636 1170T>C S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 1675 1209C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 2805 2339C>T T780I 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 3853 3387T>C S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 6443 5977C>T R1993W 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 7036 6570C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 8608 8142G>A S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 8923 8457C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9034 8568G>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9040 8574C>T S 101 receptor related protein X13916 X13916 107770 GEN- Human mRNA for LDL- 9391 8925T>C S 101 receptor related protein CLU X14723 185430 GEN- Human SP-40,40 mRNA 131 84C>T S 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 429 382G>T V128F 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 836 789C>T 1SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1234 1187C>T S396L SD-144146. Page 11 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1372 1325A>T Y442F 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1482 1435C>T 3 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1548 1501C>T 3 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CLU X14723 185430 GEN- Human SP-40,40 mRNA 1645 1598A>T 3 1 SB for complement-associated protein SP-40,40 alpha-1 and beta-1 chain CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1375 1359C>T S 4EK receptor beta 1 CHRNB1 X14830 100710 GEN- Nicotinic, Cholinergic 1591 1575T>C 3 4EK receptor beta 1 X15263 X15263 None GEN- Muscarinic receptor, 1144 1044G>A S 4EQ CHRM1 X15357 X15357 108960 GEN- Human mRNA for 1066 1023G>C M341 I KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 1657 1614C>T S KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 2859 2816G>A R939Q KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 2983 2940G>A S KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 3259 3216delC F KUV natriuretic peptide receptor (ANP-A receptor) X15357 X15357 108960 GEN- Human mRNA for 3589 3546 Λ 3547ins F SD-144146. Page 1 18 KUV natriuretic peptide receptor GAAA (ANP-A receptor) PACE X17094 136950 GEN- Human fur mRNA for furin 399 183C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 1692 1476C>T S 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2067 1851C>G S PACE X17094 136950 G 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2855 2639C>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 2988 2772G>A 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3234 3018C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3625 3409A>G 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 3883 3667C>T 3 1ZV PACE X17094 136950 GEN- Human fur mRNA for furin 4053 3837A>G 3 1ZV X51362 X51362 126450 GEN- Dopamine Receptor D2 588 423G>A S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1104 939C>T S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1122 957T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1248 1083A>G S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1488 1323T>C S 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 1548 1383A>G 3 31W X51362 X51362 126450 GEN- Dopamine Receptor D2 2361 21960T 3 31W X51416 X51416 601998 GEN-57 STEROID HORMONE 2285 2222G>A 3 RECEPTOR ERR1 FLT1 X51602 165070 GEN-329 Human fit mRNA for 192 (-58)OT 5 receptor-related tyrosine kinase SD-144146.1 Page 1 1 FLT1 X51602 165070 GEN-329 Human fit mRNA for 1723 1474C>T receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 1953 1704G>A receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 3061 2812A>G M938V receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 3150 2901 G>A receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 4497 4248T>G receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 5295 5046 Λ 5047ins receptor-related tyrosine GAG kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 6976 6727G>A receptor-related tyrosine kinase FLT1 X51602 165070 GEN-329 Human fit mRNA for 7013 6764T>G receptor-related tyrosine kinase FGFR1 X51803 136350 GEN- Human mRNA for 276 159T>G 32G fibroblast growth factor (FGF) receptor EDN3 X52001 131242 GEN- Endothelin 3 1262 1152G>A 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1649 1539C>G 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1700 1590C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1742 1632C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1797 1687C>T 3 33E EDN3 X52001 131242 GEN- Endothelin 3 1914 1804G>C 3 33E EDN3 X52001 131242 GEN- Endothelin 3 2040 1930C>T 3 33E SD-144146.1 Page 1 1 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3044 2869G>A 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3289 3114A>G 3 X52425 X52425 147781 GEN-59 Interleukin 4 receptor 3391 3216C>T 3 X52479 X52479 176960 GEN-LM Protein kinase C, alpha 908 881A>C D294A FGFR2 X52832 176943 GEN-341 Human bek mRNA for 338 159A>G S fibroblast growth factor receptor-BEK FGFR2 X52832 176943 GEN-341 Human bek mRNA for 2903 2724A>T 3 fibroblast growth factor receptor-BEK CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 212 212A>G D71G receptor alpha 3 CHRNA3 X53559 118503 GEN-34I Nicotinic, Cholinergic 552 552C>T S receptor alpha 3 TNNI3 X54163 191044 GEN- Human mRNA for cardiac 626 537G>A S 34U troponin I FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 83 28G>A V10I 37M fibroblast growth factor receptor (FGFR-4) FGFR4 X57205 134935 GEN- Human FGFR-4 mRNA for 217 162T>G 37M fibroblast growth factor receptor (FGFR-4) YWHAB X57346 601289 GEN- H sapiens mRNA for HS1 432 60C>A S 37R protein YWHAB X57346 601289 GEN- H sapiens mRNA for HS1 1135 763T>C 3 37R protein X57830 X57830 182135 GEN-7V Serotonin 5-HT2 receptor 247 102T>C S GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 821 773C>T 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 979 931G>A 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1187 1139T>G 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1354 1306C>T 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1443 1395C>T SD-144146 1 Page l lϋ 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1516 1468C>A 3 38S plasma glutathione peroxidase GPX3 X58295 138321 GEN- Human GPx-3 mRNA for 1581 1533C>T 3 38S plasma glutathione peroxidase X58377 X58377 147681 GEN- Interleukin 11 807 744A>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 927 864T>G 3 38V X58377 X58377 147681 GEN- Interleukin 11 1964 1901T>C 3 38V DRD1 X58987 126449 GEN- D1 dopaminergic receptor 229 (-48)A>G 5 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 366 90G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 474 198G>A S 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 1539 1263G>A s 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2040 1764A>C 3 4EH DRD1 X58987 126449 GEN- D1 dopaminergic receptor 2045 1769C>A 3 4EH X59842 X59842 600214 GEN- Human PBX2 mRNA 2339 2043T>G 3 3A3 X60069 X60069 231950 GEN- Human mRNA for 102 (-257)G>A 5 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 336 (-23)C>T 3AJ pancreatic gamma- g I utamy Itransf erase X60069 X60069 231950 GEN- Human mRNA for 1173 815C>T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1173 815C>T A272V 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1399 1041 C>T SD-144146.1 Page 118 3AJ pancreatic gamma- glutamyltransferase X60069 X60069231950 GEN- Human mRNA for 1409 1051G>T A351S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1482 1124C>T T375M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1591 1233G>A 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1624 1266C>T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1637 1279C>A P427T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1651 1293C>T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1662 1304T>C V435A 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1783 1425A>G 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1794 1436C>T T479M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1795 1437G>A 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 1981 1623C>T 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2007 1649C>T T550M 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2031 1673C>T S558L 3AJ pancreatic gamma- glutamyltransferase SD-144146.1 Page 1 19 X60069 X60069 231950 GEN- Human mRNA for 2047 1689C>T S 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2147 1789C>T 3 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2176 1818C>T 3 3AJ pancreatic gamma- glutamyltransferase X60069 X60069 231950 GEN- Human mRNA for 2224 1866C>A 3 3AJ pancreatic gamma- glutamyltransferase X60957 X60957 600222 GEN- Human tie mRNA for 2194 2158G>A A720T 3BF putative receptor tyrosine kinase X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 203 96A>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1372 1265A>G H422R kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1501 1394G>A R465K kinase 1-phosphorylates beta adrenergic receptor ) X61 157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1766 1659C>T S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 1823 1716T>C S kinase 1-phosphorylates beta adrenergic receptor ) X61157 X61157 109635 GEN-23 Adrenergic receptor (Beta 2976 2869G>A 3 kinase 1-phosphorylates beta adrenergic receptor ) NFKB2 X61498 164012 GEN- H.sapiens mRNA for NF- 2457 2294C>T P765L 3BW kB subunit KDR X61656 191306 GEN- H.sapiens mRNA for 2308 2308A>G T770A 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2353 2353G>C G785R 3BZ growth factor receptor tyrosine kinase SD-144146.1 Page 119 KDR X61656 191306 GEN- H.sapiens mRNA for 2499 2499C>G N833K 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 2537 2537A>T E846V 3BZ growth factor receptor tyrosine kinase KDR X61656 191306 GEN- H.sapiens mRNA for 4123 4123G>C 3 3BZ growth factor receptor tyrosine kinase X63359 X63359 600070 GEN- H.sapiens UGT2BIO 1516 1506C>T S 3DC mRNA for udp glucuronosyltransferase X63359 X63359 600070 GEN- H.sapiens UGT2BIO 2714 2704G>A 3 3DC mRNA for udp glucuronosyltransferase ACLY X64330 108728 GEN- H.sapiens mRNA for ATP- 3998 3914G>T 3 3F0 citrate lyase ACLY X64330 108728 GEN- H.sapiens mRNA for ATP- 4229 4145A>C 3 3F0 citrate lyase X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 51 44G>A R15H CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 116 109A>C K37Q CONVERTASE PRECURSOR X65019 X65019 147678 GEN-6G INTERLEUKIN 1 BETA 261 254G>A G85E CONVERTASE PRECURSOR X66364 X66364 123831 GEN- H.sapiens mRNA 495 471T>G C157W 3GM PSSALRE for serine/threonine protein kinase X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2236 2225G>T 3 receptor epsilon polypeptide X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2333 2322A>G 3 receptor epsilon polypeptide X66403 X66403 100725 GEN-5D Nicotinic, Cholinergic 2364 2353G>T 3 receptor epsilon polypeptide SD-144146.1 Page 119 X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1182 1182T>C S RECEPTOR KINASE 2 X69117 X69117 109636 GEN-5G BETA-ADRENERGIC 1609 1609G>A E537K RECEPTOR KINASE 2 X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 112 21T>C S squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 292 201 C>T S squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1436 1345T>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1579 1488T>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1621 1530C>T 3 squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1719 1628A>C 3 squalene synthase X69141 X69141 184420 GEN-3J9 H sapiens mRNA for 1904 1813G>C 3 squalene synthase X70811 X70811 109691 GEN- beta-3-adrenergιc receptor 315 190T>C W64R 3KK X70811 X70811 109691 GEN- beta-3-adrenergιc receptor 315 190T>C W64R 3KK X71440 X71440 None GEN- H sapiens mRNA for 949 936G>C M312I 3KS peroxisomal acyl-CoA oxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 718 638T>C 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 837 757C>A 3 for phospholipid hydroperoxide glutathione peroxidase GPX4 X71973 138322 GEN-3L1 H sapiens GPx-4 mRNA 882 802A>C 3 for phospholipid hydroperoxide glutathione peroxidase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 1380 1155C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 1503 1278C>T S 3LW oxide synthase SD-144146 1 Page 1 19 N0S2A X73029 163730 GEN- H sapiens mRNA for nitnc 2048 1823C>T S608L 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 2287 2062G>A G688S 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 2339 2114A>G D705G 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 2583 2358T>C S 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 2982 2757A>G S 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 3022 2797C>G R933G 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 3051 2826C>T S 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 3693 3468T>C 3 3LW oxide synthase N0S2A X73029 163730 GEN- H sapiens mRNA for nitric 3715 3490G>A 3 3LW oxide synthase PREP X74496 600400 GEN- Prolyl Endopeptidase 390 390T>C S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1051 1051T>G L351V 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1125 1125C>T S 3N8 PREP X74496 600400 GEN- Prolyl Endopeptidase 1363 1363G>A V455M 3N8 X75299 X75299 192321 GEN- H sapiens HIVR mRNA for 1915 1904T>C 3 3NU vasoactive intestinal peptide (VIP) receptor X75299 X75299 192321 GEN- H sapiens HIVR mRNA for 2475 2464T>C 3 3NU vasoactive intestinal peptide (VIP) receptor MTP X75500 157147 GEN- H sapiens mRNA for 1847 1823T>G F608C 307 microsomal triglyceride transfer protein MTP X75500 157147 GEN- H sapiens mRNA for 3231 3207G>A 3 307 microsomal triglyceride transfer protein X75913 X75913 601269 GEN- H sapiens mRNA for gClq- 1052 974A>G 3 30G R X75913 X75913 601269 GEN- H sapiens mRNA for gClq- 1074 996T>C 3 SD-144146 1 Page 1 1 30G R X76180 X76180600228 GEN-N5 Solute carrier family 9 1901 1802G>A G601D (sodium/hydrogen exchanger), isoform 1 (antiporter, Na+/H+, amiloπde sensitive) LIPA X76488 278000 GEN- H sapiens mRNA for 191 46A>C T16P 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H sapiens mRNA for 212 67G>A G23R 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H sapiens mRNA for 967 822G>A M274I 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H sapiens mRNA for 1531 1386C>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H.sapiens mRNA for 2254 2109A>T 3 3P2 lysosomal acid lipase LIPA X76488 278000 GEN- H sapiens mRNA for 2439 2294C>T 3 3P2 lysosomal acid lipase X77094 X77094 601488 GEN- H sapiens mRNA for 865 735C>T S 3PK p40phox YWHAH X78138 113508 GEN- H sapiens 14-3-3 eta 953 753A>G 3 3QU subtype mRNA YWHAH X78138 113508 GEN- H sapiens 14-3-3 eta 960 760G>A 3 3QU subtype mRNA YWHAH X78138 113508 GEN- H sapiens 14-3-3 eta 1387 1187C>T 3 3QU subtype mRNA X78282 X78282 601292 GEN- H.sapiens mRNA for aryl 895 895T>C 3 LVF sulfotransferase (ST1A2) X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 1922 1922G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2378 2378G>A 3 X78706 X78706 600184 GEN-2A Camitine Acetyltransferase 2382 2382G>A 3 X79483 X79483 602399 GEN- H sapiens ERK6 mRNA for 1287 1254T>G 3 LPR extracellular signal regulated kinase TNNT2 X79857 191045 GEN-3TJ H sapiens HTNT4 mRNA 191 80G>T W27L for cardiac troponin T TNNT2 X79857 191045 GEN-3TJ H sapiens HTNT4 mRNA 225 114G>C S for cardiac troponin T TNNT2 X79857 191045 GEN-3TJ H.sapiens HTNT4 mRNA 304 193G>T F for cardiac troponin T SD-144146 1 Page 11 TNNT2 X79857 191045 GEN-3TJ H.sapiens HTNT4 mRNA 920 809C>A for cardiac troponin T X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 25 (-74)C>T SUM 2k) mRNA for serine/threonine protein kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 77 (-22)C>T SUM 2k) mRNA for serine/threonine protein kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 1516 1418G>A 3 SUM 2k) mRNA for serine/threonine protein kinase X80230 X80230 603251 GEN- H.sapiens mRNA (clone C- 1574 1476A>G 3 SUM 2k) mRNA for serine/threonine protein kinase X81411 X81411 None GEN- Serotonin 5-HT receptors 75 76A>T 3 4EY 5-HT5a X83582 X83582 600734 GEN- Potassium channel Kir3 4 171 171C>T S 3YD X83582 X83582 600734 GEN- Potassium channel Kir3.4 834 834C>T S 3YD X83861 X83861 176806 GEN-5H Prostaglandin E receptor 3 387 180C>G S (subtype EP3) {alternative products} X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 32 (-161)OT 5 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H sapiens BAK mRNA for 317 125G>A R42H 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 435 243C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H sapiens BAK mRNA for 616 424G>A V142I 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 663 471C>T S 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 900 708T>C 3 3ZC BCI-2 homologue X84213 X84213 600516 GEN- H.sapiens BAK mRNA for 974 782C>T 3 3ZC BCI-2 homologue SD-144146 Page 11 X86097 X86097 600967 GEN- H sapiens mRNA for E2F-5 162 132G>C S 40O protein X86097 X86097 600967 GEN- H sapiens mRNA for E2F-5 1281 1251T>C 3 40O protein X86097 X86097 600967 GEN- H sapiens mRNA for E2F-5 1725 1695A>C 3 40O protein X86681 X86681 602110 GEN- H sapiens mRNA for 1725 1340G>A 3 41E nucleolar protein, HNP36 X93086 X93086 109750 GEN- H sapiens mRNA for 669 609G>A S 48G biliverdin IX alpha reductase X93086 X93086 109750 GEN- H sapiens mRNA for 720 660A>G S 48G biliverdin IX alpha reductase X95190 X95190 601641 GEN- H sapiens mRNA for 1394 1302C>T S 49Y Branched chain Acyl-CoA Oxidase X95190 X95190 601641 GEN- H sapiens mRNA for 1934 1842C>A S 49Y Branched chain Acyl-CoA Oxidase X97058 X97058 602451 GEN- P2 purinoceptor (P2Y6) 121 (-156)T>G 5 4BB RYR2 X98330 180902 GEN- H sapiens mRNA for 13745 13624G>A A4542T 4CB ryanodine receptor 2 RYR2 X98330 180902 GEN- H sapiens mRNA for 15541 15420T>G 3 4CB ryanodine receptor 2 Y00285 Y00285 147280 GEN-6I IGF-2 receptor 4613 4466G>A S1489N Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6371 6224C>T T2075M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 6813 6666C>T S Y00285 Y00285 147280 GEN-6I IGF-2 receptor 7150 7003G>A V2335M Y00285 Y00285 147280 GEN-6I IGF-2 receptor 8685 8538C>A 3 GPX1 Y00433 138320 GEN-TJ Human mRNA for 504 186G>A S glutathione peroxidase (EC 1 11 1 9 ) GPX1 Y00433 138320 GEN-TJ Human mRNA for 610 292C>G R98G glutathione peroxidase (EC 1 11 1 9 ) GPX1 Y00433 138320 GEN-TJ Human mRNA for 911 593C>T P198L glutathione peroxidase (EC 1 11 1 9 ) SD-144146 Page 11 GPX1 Y00433 138320 GEN-TJ Human mRNA for 1048 730A>C 3 glutathione peroxidase (EC 1 11 1 9 ) GPX1 Y00433 138320 GEN-TJ Human mRNA for 1110 792A>C 3 glutathione peroxidase (EC 1 11 1 9 ) ALAS1 Y00451 125290 GEN-TE Human mRNA for 5- 509 426T>G S aminolevu nate synthase ALAS1 Y00451 125290 GEN-TE Human mRNA for 5- 608 525C>T S aminolevulinate synthase PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 430 358A>G N120D Serpin (plasminogen activator-inhibitor 2, PAI-2) PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 1251 1179T>G S Serpin (plasminogen activator-inhibitor 2, PAI-2) PAI2 Y00630 173390 GEN-U6 Human mRNA for Arg- 1762 1690G>A 3 Serpin (plasminogen activator-inhibitor 2, PAI-2) Y00692 Y00692 176880 GEN-6K Anticoagulant protein S 785 586C>T 3 Y00692 Y00692 176880 GEN-6K Anticoagulant protein S 910 711T>C 3 Y00692 Y00692 176880 GEN-6K Anticoagulant protein S 1156 957G>T 3 Y00749 Y00749 131240 GEN-P7 Endothelin 1 846 594G>T K198N CR1 Y00816 120620 GEN-UG Human mRNA for 207 180G>C E60D complement receptor type 1 (CR1 , C3b/C4b receptor, CD35) Y07683 Y07683 600843 GEN- H sapiens mRNA for P2X3 717 552C>T S 4F1 purinoceptor Y07683 Y07683 600843 GEN- H sapiens mRNA for P2X3 753 588A>G S 4F1 purinoceptor Y08110 Y08110 602005 GEN- H sapiens mRNA for 3641 3561T>G S 1 FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H sapiens mRNA for 3818 3738C>T S 1FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H sapiens mRNA for 5158 5078G>A S1693N 1 FK mosaic protein LR11 Y08110 Y08110 602005 GEN- H sapiens mRNA for 6571 6491 G>A R2164K 1 FK mosaic protein LR11 Y08756 Y08756 602164 GEN- Serotonin 5-HT receptors 765 747T>C S 4EC 5-HT4 SD-144146 Page 1 1 Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 835 809A>G H270R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 946 920G>A R307Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1068 1042G>A A348T 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1096 1070C>G T357S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1405 1379A>G Q460R 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1589 1563C>G H521 Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1590 1564G>A V522I 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1628 1602G>T S 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1759 1733G>A R578Q 4F4 receptor Y09561 Y09561 None GEN- H.sapiens mRNA for P2X7 1772 1746G>A S 4F4 receptor Y10659 Y10659 300119 GEN-1J6 H.sapiens IL-13Ra mRNA 1116 1073G>A G358D 1REB1 Z11559 147581 GEN- H.sapiens mRNA for iron 2855 2748T>C 3 1 KO regulatory factor IREB1 Z11559 147581 GEN- H.sapiens mRNA for iron 3162 3055C>A 3 1 KO regulatory factor IREB1 Z11559 147581 GEN- H.sapiens mRNA for iron 3460 3353A>T 3 1 KO regulatory factor Z11695 Z11695 176948 GEN-1 L1 H.sapiens 40 kDa protein 1287 1153G>A 3 kinase related to rat ERK2 Z11696 Z11696 601795 GEN-1 L0 H.sapiens 44kDa protein 449 449T>G I150S kinase related to rat ERK1 Z15108 215108 176982 GEN- H.sapiens mRNA for 246 240T>C S 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 1694 1688A>C D563A 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2033 2027G>A 3 1TE protein kinase C zeta Z15108 Z15108 176982 GEN- H.sapiens mRNA for 2086 2080T>G 3 1TE protein kinase C zeta Z19585 Z19585 600715 GEN- H.sapiens mRNA for 2135 2108G>A C703Y 22A thrombospondin-4 SD-144146.1 Page 1 1 Z22555 Z22555 601040 GEN-264 H.sapiens encoding CLA-1 1119 1050C>T S mRNA Z22555 Z22555 601040 GEN-264 H.sapiens encoding CLA-1 2553 2484A>G 3 mRNA TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 585 259G>T F 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 606 280G>T F 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 668 342C>A S 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 780 454C>A Q152K 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 1333 1007T>C 3 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 1356 1030A>G 3 280 isoform mRNA, complete CDS TPM1 Z24727 191010 GEN- H.sapiens tropomyosin 1553 1227T>G 3 280 isoform mRNA, complete CDS Z26649 Z26649 600230 GEN- Phospholipase C beta-3 437 438C>T 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 466 467G>A 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 2664 2665C>T 3 2B5 Z26649 Z26649 600230 GEN- Phospholipase C beta-3 3168 3169G>T 3 2B5 CPO Z28409 121300 GEN- H.sapiens coprox gene for 1994 1994G>A 3 2D8 coproporphyrinogen oxidase ECE1 Z35307 600423 GEN- Endothelin Converting 1141 1104C>T S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1627 1590T>C S 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1696 1659G>A S SD-144146.1 Page 12 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 1946 1909G>A V637M 2MA Enzyme 1 ECE1 Z35307 600423 GEN- Endothelin Converting 2433 2396G>A 3 2MA Enzyme 1 Z35491 Z35491 601497 GEN- H.sapiens mRNA for novel 315 37G>A E13K 2ME glucocorticoid receptor- associated protein Z35491 Z35491 601497 GEN- H.sapiens mRNA for novel 333 55G>A E19K 2ME glucocorticoid receptor- associated protein Z35491 Z35491 601497 GEN- H.sapiens mRNA for novel 1297 1019A>C 3 2ME glucocorticoid receptor- associated protein Z48810 Z48810 602664 GEN- H.sapiens mRNA for TX 1280 1239A>C 3 2YJ protease precursor Z69881 Z69881 601929 GEN- H.sapiens mRNA for 2023 2017G>A A673T 3JV adenosine triphosphatase, calcium Z69881 Z69881 601929 GEN- H.sapiens mRNA for 3636 3630C>G 3 3JV adenosine triphosphatase, calcium SD-144146. Page 1201 Table 18. Identified Variances in Genes or Related Pathways involved in Cancer and Related Disorders human DNA mismatch U07418 120436 SER252TER repair protein hMLHl/MutL human DNA mismatch U07418 120436 SER44PHE repair protein hMLHl/MutL human DNA mismatch U07418 120436 3-BP DEL LYS618DEL repair protein hMLHl/MutL human DNA mismatch U07418 120436 3.5-KB DEL repair protein hMLHl/MutL human DNA mismatch U07418 120436 G-to-A intron 5 frameshift repair protein splice junction hMLHl/MutL human DNA mismatch U07418 120436 370-BP DEL frameshift repair protein hMLHl/MutL human DNA mismatch U07418 120436 IVS14DS, 7-BP repair protein DEL AND 4-BP INS hMLHl/MutL human DNA mismatch U07418 120436 HIS329PRO repair protein hMLHl/MutL human DNA mismatch U07418 120436 1784delT truncated SD-144141.1 Page 1202 repair protein hMLHl/MutL human DNA mismatch U07418 120436 676C-T ARG226TER repair protein hMLHl/MutL human DNA mismatch U07418 120436 GGG to TGG GLY67TRP repair protein hMLHl/MutL human DNA mismatch U07418 120436 A->T codon 26 repair protein hMLHl/MutL human DNA mismatch U07418 120436 GG->AT 177 and 178 repair protein hMLHl/MutL human DNA mismatch U07418 120436 -93 nt repair protein hMLHl/MutL human DNA mismatch U07418 120436 Val384Asp repair protein hMLHl/MutL human DNA mismatch U07418 120436 T insertion 3 splice repair protein site post exon 9 hMLHl/MutL human DNA mismatch U07418 120436 deletion of repair protein codon 618K hMLHl/MutL human DNA mismatch U07418 120436 A-to-G transition repair protein exon 6 hMLHl/MutL human DNA mismatch U07418 120436 exon 5 missense repair protein SD-144141.1 Page 1203 hMLHl/MutL human DNA mismatch U07418 120436 exon 9 missense repair protein hMLHl/MutL topoisomerase lib U54831 126431 reported 06 alkylguanine-DNA M60761 156569 GGA to AGA GLY160ARG alkyltransferase class I aldehyde M26761 100640 none found dehydrogenase glutathione-S- AF020918 ****** none found transferase GSTA4 glutathione-S- J05459 138390 3bp deletion intron 6 transfcrase GSTM3 glutathione-S- X79389 600436 null genotype transfcrase GSTT1 glutathione-S- L38503 600437 none found transfcrase GSTT2 glutathione peroxidase Y00433 138320 P197L GPxl glutathione peroxidase Y00433 138320 1167T/C Silent GPxl glutathione peroxidase X68314 138319 A/T intron GPx2 glutathione peroxidase X68314 138319 TC repeats intron GPx2 glutathione peroxidase X58295 138321 none found GPx3 glutathione peroxidase X71973 138322 none found GPx4 glutathione peroxidase AJ005277 603435 none found GPx5 SD-144141.1 Page 120 glutathione reductase X15722 138300 two polymorphisms reported N-methylpurine-DNA M74905 156565 none found glycosylase proliferating cell J04718 176740 none found nuclear antigen multidrug resistance L05628 158343 none found associated protein MRP1 multidrug resistance U83659 601107 none found associated protein MRP2 dihydrofolate reductase J00140 126060 intronic polymoφhism dihydrofolate reductase J00140 126060 2 RFLP's thymidylate synthetase X02308 188350 5' trinucleotide repeat thymidylate synthetase X02308 188350 tyr33his thymidylate synthetase X02308 188350 A->G 3'UTR human cell adhesion M33374 603842 none found protein SQM1 reduced folate carrier U19720 600424 none found RFC1 thymidylate synthetase X02308 188350 Triple tandem 5'end thymidylate synthetase X02308 188350 tyr33his cytidine deaminase L27943 123920 none found folylpolyglutamate M98045 136510 none found synthetase FPGS gamma-glutamyl U55206 601509 none found hydrolase GGH dihydropyrimidine U09178 274270 165-BP DEL SD-144141 Page 120 dehydrogenase DPD dihydropyrimidine U09178 274270 ASP974VAL dehydrogenase DPD dihydropyrimidine U09178 274270 4-BP DEL 296 to dehydrogenase DPD 299 (TCAT) dihydropyrimidine U09178 274270 CYS29ARG dehydrogenase DPD dihydropyrimidine U09178 274270 1-BP DEL, 1897C Frameshift dehydrogenase DPD dihydropyrimidine U09178 274270 ARG886HIS dehydrogenase DPD dihydropyrimidine U09178 274270 Arg21Gln dehydrogenase DPD dihydropyrimidine U09178 274270 Val335Leu dehydrogenase DPD dihydropyrimidine U09178 274270 Glu386Ter dehydrogenase DPD dihydropyrimidine U09178 274270 deltaC1897 dehydrogenase DPD dihydropyrimidine U09178 274270 Ser534Asn dehydrogenase DPD dihydropyrimidine U09178 274270 Ile543Val dehydrogenase DPD dihydropyrimidine U09178 274270 Val732Ile dehydrogenase DPD deoxycytidine kinase M60527 125450 115-base pan- deletion M60527 125450 G to A glutamic acid for glycine glucosylceramide DD5500884400 602874 none found synthase SD-144141.1 Page 120 hypoxanthine-guanine M31642 308000 ILE132MET phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ASP80VAL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ASP201GLY phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 1-BP INS frameshift phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 EX8DEL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 LEU41PRO phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 24AA+ phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 PHE74LEU phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ASP194ASN phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ASP 193 ASN phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 SER110LEU SD-144141 Page 120 phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 VAL179DEL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 VAL130ASP phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ALA161SER phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 SER 104 ARG phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 PHE199VAL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 GLY70GLU phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 GLY71ARG phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 GLN108TER phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 HIS203ASP phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ARG44LYS phosphoribosyltransfer SD-144141 Page 120 ase hypoxanthine-guanine M31642 308000 ASP176TYR phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 2-BP DEL frameshift phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 1-BP DEL,TTA-TA frameshift phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 1-BP DEL, TTG-TG frameshift phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 40-BP DEL frameshift phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 G-to-A +5 intron 8 splice phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ATAG-TTTG -4 intron 8+129 phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 GTAAGT-to- phosphonbosyltransfer GTAAAT intron 7 ase hypoxanthine-guanine M31642 308000 AG-to-TG intron 1 phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 PRO176LEU phosphonbosyltransfer ase SD- 144141 Page 120 hypoxanthine-guanine M31642 308000 ARG51GLY phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ARG51TER phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 MET56THR phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 MET143LYS phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 ARG170TER phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 13-BP DEL, 5- phosphonbosyltransfer PRIME UTR ase hypoxanthine-guanine M31642 308000 EX2DEL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 EX4-9DEL phosphonbosyltransfer ase hypox anth i ne-guanine M31642 308000 EX6-9DEL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 EX9DEL phosphonbosyltransfer ase hypoxanthine-guanine M31642 308000 1-BP INS G 207 frameshift SD-144141.1 Page 121 phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 EX2-3DUP phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 THR168ILE phosphoribosyltransfer ase hypox anth ine-guanine M31642 308000 GLY16SER phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 GLY58ARG phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 LEU78VAL phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 EX6DEL phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 1-BP INS, T INS phosphoribosyltransfer 14823 ase hypoxanthine-guanine M31642 308000 ASP52GLY phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 GLY140ASP phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 ASP194GLU phosphoribosyltransfer SD-144141. Page 121 ase hypoxanthine-guanine M31642 308000 TYR153TER phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 Mnl l phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 Bam Hl phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 54 (from ATG phosphoribosyltransfer to CTG) ase resulting in the replacement of methionine with leucine hypoxanthine-guanine M31642 308000 vall79gly phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 glyl80arg phosphoribosyltransfer ase hypoxanthine-guanine M31642 308000 51 del 747 and 797 trucated protein phosphoribosyltransfer ase Bcl-2 M13994 151430 ACC->GCC Ala43Thr Bcl-2 M13994 151430 EcoRI polymoφhism Bcl-2 M13994 151430 G to A exon 2 protein kinase C alpha X52479 176960 ASP294GLY protein kinase C beta 1 X06318 176970 none found SD-144141 Page 121 -> 60 . O *" ϋ *O ' " C3 '"O 3 3 3 3 C H u-ι 3 3 3 3 3 c. s+-* -t— , -t—t --—, -t— , t~- -U <-D CD -D (D - _< 3 3 S 3 3 o o o o o -J 3 3 3 3 3 W Q PQ r-- * oo CN o o O o O O O O O O O O O r- * "3- 00 VO vo VO o O VO VO v σs * ■ ^r C-Λ . r—-, l — t — , — f —- , r r—- , — r —- , r — —- , r- r -—- , ^ r-_-, t^ - r—^ , l - vo # o VO σ. r- * o r~- CN t- r- - • ->- r- r- r- t-~ r~- r~~ r^ c^ t SO 78 alkaline phosphatase NM 0004 171760 ARG119HIS 78 alkaline phosphatase NM 0004 171760 GLY 145 VAL 78 alkaline phosphatase NM 0004 171760 ScrFI 78 alkaline phosphatase NM 0004 171760 Bell 78 ribonucleotide X59543 180410 Sad polymoφhism reductase Ml subunit within intron IX ribonucleotide X59543 180410 Taql reductase Ml subunit ribonucleotide X59618 180390 none found reductase M2 subunit aminopeptidase A L14721 138297 none found signal transducer and M97935 600555 none found activator of transcription STAT1 topoisomerase Ila J04088 126430 AGA to AAA ARG486LYS topoisomerase Ila J04088 126430 deletion of 1320- Deletion of 1322 Ala429 topoisomerase Ila J04088 126430 Lys-797->Asn topoisomerase Ila J04088 126430 Arg449Gln topoisomerase I J03250 126420 ASP533GLY topoisomerase I J03250 126420 ASP583GLY topoisomerase I J03250 126420 Asn722Ser topoisomerase I J03250 126420 Taql myeloperoxidase X04876 254600 C8089T ARG569TRP myclopcroxidase X04876 254600 TYR173CYS myeloperoxidase X04876 254600 MET251THR SD-144141 Page 121 myeloperoxidase X04876 254600 G to A (promoter) myeloperoxidase X04876 254600 Kpnl myeloperoxidase X04876 254600 Dinucleotide Repeat myeloperoxidase X04876 254600 EcoRV myeloperoxidase X04876 254600 Pstl b3-tubulin U47634 60266 none found interleukin 6 (IL6) M14584 147620 174G-C interleukin 6 (IL6) M14584 147620 CA repeat interleukin 6 (IL6) M14584 147620 Nlalll promoter interleukin 6 (IL6) M14584 147620 AT repeat interleukin 6 (IL6) M14584 147620 Mspl interleukin 6 (IL6) M14584 147620 Bgll interleukin 6 (IL6) M14584 147620 Bglll interferon alphal X02956 147660 none found (IFNal) tyrosine kinase-type X03363 164870 VAL655ILE cell surface receptor HER2/ERBB2 tyrosine kinase-type X03363 164870 VAL654ILE cell surface receptor HER2/ERBB2 tumor protein p53 X02469 191170 CGC-CCC Arg72 Pro tumor protein p53 X02469 191170 CCG-CTG Pro82Leu tumor protein p53 X02469 191170 ATG- ACG Metl33Thr tumor protein p53 X02469 191170 cCAA-TAA Glnl36Term tumor protein p53 X02469 191170 cAGA-TGA Arg209Term tumor protein p53 X02469 191170 aCCC-TCC Prol51Ser tumor protein p53 X02469 191170 CCG-CTG Prol52Leu tumor protein p53 X02469 191170 gCCC-TCC Pro219Ser tumor protein p53 X02469 191170 cAAC-GAC Asn235Asp tumor protein p53 X02469 191170 GGC-GTC Glyl54Val SD-144141 Page 121 tumor protein p53 X02469 191170 ACA-ATA Thr256Ile tumor protein p53 X02469 191170 CGC-CAC Argl75His tumor protein p53 X02469 191170 CAT-CGT Hisl93Arg tumor protein p53 X02469 191170 tCGA-TGA Arg213Term tumor protein p53 X02469 191170 gCGT-TGT Arg273Cys tumor protein p53 X02469 191170 TGT-TAT Cys275Tyr tumor protein p53 X02469 191170 tGAG-AAG Glul80Lys tumor protein p53 X02469 191 170 CGC-CAC Argl81His tumor protein p53 X02469 191170 gCGC-TGC ArglδlCys tumor protein p53 X02469 191170 cCGA-TGA Argl96Term tumor protein p53 X02469 191170 TAT-TGT Tyr220Cys tumor protein p53 X02469 191170 cTCT-ACT Ser227Thr tumor protein p53 X02469 191170 AAC-AGC Asn235Ser tumor protein p53 X02469 191170 CGA-CCA Arg306Pro tumor protein p53 X02469 191170 cCAC-AAC His233Asn tumor protein p53 X02469 191170 ATCc-ATG Ile251Met tumor protein p53 X02469 191170 TCC-TTC Ser241Phe tumor protein p53 X02469 191170 CGG-CAG Arg248Gln tumor protein p53 X02469 191170 GGC-GAC Gly245Asp tumor protein p53 X02469 191170 cGGC-AGC Gly245Ser tumor protein p53 X02469 191170 cCGG-TGG Arg282Trp tumor protein p53 X02469 191170 cGGC-TGC Gly245Cys tumor protein p53 X02469 191170 cCGG-TGG Arg248Tφ tumor protein p53 X02469 191 170 CTC-CCC Leu252Pro tumor protein p53 X02469 191 170 gGAA-AAA Glu258Lys tumor protein p53 X02469 191170 CTG-CAG Leu257Gln tumor protein p53 X02469 191170 CTG-CCG Leu265Pro tumor protein p53 X02469 191170 gCGA-TGA Arg306Term tumor protein p53 X02469 191170 gGTG-TTG Val272Leu tumor protein p53 X02469 191170 CGT-CAT Arg273His tumor protein p53 X02469 191170 GGA-GTA Gly325Val SD-144141 Page 121 tumor protein p53 X02469 191170 CCT-CTT Pro278Leu tumor protein p53 X02469 191170 GAA-GCA Glu286Ala tumor protein p53 X02469 191170 gCGC-TGC Arg337Cys tumor protein p53 X02469 191170 CTG-CCG Leu344Pro tumor protein p53 X02469 191170 ARG249SER tumor protein p53 X02469 191170 VAL157PHE tumor protein p53 X02469 191 170 CYS242TYR tumor protein p53 X02469 191170 1-BP INS, 151 C frameshift tumor protein p53 X02469 191 170 2-BP DEL, frameshift CODONS 209-210 tumor protein p53 X02469 191170 1-BP INS, CODONS frameshift 71-72 tumor protein p53 X02469 191170 LYS120TER tumor protein p53 X02469 191170 ARG280THR tumor protein p53 X02469 191170 PRO151THR tumor protein p53 X02469 191170 LEU35PHE tumor protein p53 X02469 191170 1-BP DEL, CODON 257 tumor protein p53 X02469 191170 ALA138PRO tumor protein p53 X02469 191 170 1-BP DEL Codon frameshift 178 tumor necrosis factor X01394 191160 LEU29SER alpha (TNFa) tumor necrosis factor X01394 191160 -1,031 T->C alpha (TNFa) tumor necrosis factor X01394 191160 -863 C->A alpha (TNFa) tumor necrosis factor X01394 191160 C-850T alpha (TNFa) tumor necrosis factor X01394 191160 G -238 A alpha (TNFa) SD-144141.1 Page 121 tumor necrosis factor X01394 191160 G -376 A alpha (TNFa) tumor necrosis factor X01394 191160 C to T, -857T alpha (TNFa) tumor necrosis factor X01394 191160 -308 G/A alpha (TNFa) tumor necrosis factor X01394 191160 Ncol alpha (TNFa) tumor necrosis factor X01394 191160 C-ins 5'UTR of exon alpha (TNFa) 1 tumor necrosis factor X01394 191160 ARG32TRP alpha (TNFa) tumor necrosis factor X01394 191160 G-376A alpha (TNFa) 2',5'-oligoadenylate NM 0061 164350 none found synthetase 1 (OAS1) 87 2',5'-oligoadenylate M87284 603350 none found synthetase 2 (OAS2) 2',5'-oligoadenylate ****** 603351 none found synthetase 3 (OAS3) excision repair protein M13194 126380 codon 118 C~>T ERCC1 xeroderma D14533 278700 ILE132MET pigmentosum complementation group A xeroderma D14533 278700 ASP80VAL pigmentosum complementation group A xeroderma D14533 278700 ASP201GLY SD-144141 Page 121 pigmentosum complementation group A xeroderma D14533 278700 56 CCTTGA to FS20TER pigmentosum CCTTTGA complementation group A xeroderma D14533 278700 EX8DEL pigmentosum complementation group A xeroderma D14533 278700 LEU41PRO pigmentosum complementation group A xeroderma D14533 278700 24AA+ pigmentosum complementation group A xeroderma D14533 278700 PHE74LEU pigmentosum complementation group A xeroderma D14533 278700 ASP 194 ASN pigmentosum complementation group A xeroderma D14533 278700 ASP 193 ASN pigmentosum complementation group A SD-144141 - Page 121 xeroderma D14533 278700 SERl lOLEU pigmentosum complementation group A xeroderma D14533 278700 3-BP DEL VAL179DEL pigmentosum complementation group A xeroderma D14533 278700 VAL130ASP pigmentosum complementation group A xerodemia D14533 278700 ALA161SER pigmentosum complementation group A xeroderma D14533 278700 SER104ARG pigmentosum complementation group A xeroderma D14533 278700 PHE 199 VAL pigmentosum complementation group A xeroderma D14533 278700 GLY70GLU pigmentosum complementation group A xeroderma D14533 278700 GLY71ARG pigmentosum complementation SD-144141. Page 122 group A xeroderma D14533 278700 GLN108TER pigmentosum complementation group A xeroderma D14533 278700 HIS203ASP pigmentosum complementation group A xeroderma D 14533 278700 ARG44LYS pigmentosum complementation group A xeroderma D 14533 278700 ASP176TYR pigmentosum complementation group A xeroderma D14533 278700 2-BP DEL, GT DEL frameshift pigmentosum complementation group A xeroderma D14533 278700 1-BP DEL, TTA- frameshift pigmentosum TA complementation group A xeroderma D14533 278700 40-BP DEL, FS frameshift pigmentosum complementation group A xeroderma D 14533 278700 G+5A intron 8 pigmentosum SD-144141.1 Page 122 complementation group A xeroderma D14533 278700 ATAG-TTTG pigmentosum intron 8 complementation group A xeroderma D 14533 278700 GTAAGT-to- pigmentosum GTAAAT intron 7 complementation group A xeroderma D 14533 278700 AG-to-TG last 2 pigmentosum nucleotides of intron complementation 1 group A xeroderma D 14533 278700 PRO176LEU pigmentosum complementation group A xeroderma D14533 278700 ARG51GLY pigmentosum complementation group A xeroderma D14533 278700 ARG51TER pigmentosum complementation group A xeroderma D 14533 278700 MET56THR pigmentosum complementation group A xeroderma D 14533 278700 MET143LYS SD-144141.1 Page 122 pigmentosum complementation group A xeroderma D14533 278700 ARG170TER pigmentosum complementation group A xeroderma D14533 278700 13-BP DEL, 5- pigmentosum PRIME UTR complementation group A xeroderma D14533 278700 EX2DEL pigmentosum complementation group A xeroderma D14533 278700 EX4-9DEL pigmentosum complementation group A xeroderma D14533 278700 EX6-9DEL pigmentosum complementation group A xeroderma D14533 278700 EX9DEL pigmentosum complementation group A xeroderma D14533 278700 null allele pigmentosum complementation group A SD-144141. Page 122 xeroderma D14533 278700 G insertion at about pigmentosum nucleotide 207 complementation group A xeroderma D14533 278700 INV/DEL, EX6-9 pigmentosum complementation group A xeroderma D 14533 278700 duplication of exons pigmentosum 2 and 3 and deletion complementation of intron 1 group A xeroderma D14533 278700 THR168ILE pigmentosum complementation group A xeroderma D 14533 278700 GLY16SER pigmentosum complementation group A xeroderma D 14533 278700 GLY58ARG pigmentosum complementation group A xeroderma D14533 278700 LEU78VAL pigmentosum complementation group A xeroderma D 14533 278700 EX6DEL pigmentosum complementation SD-144141.1 Page 122 group A xeroderma D14533 278700 T insertion pigmentosum nucleotide at either complementation nucleotide 14823 or group A 14824 xeroderma D14533 278700 ASP52GLY pigmentosum complementation group A xeroderma D14533 278700 GLY 140 ASP pigmentosum complementation group A xeroderma D14533 278700 ASP194GLU pigmentosum complementation group A xeroderma D14533 278700 TYR153TER pigmentosum complementation group A metallothionein lb AH00151 156349 none found 0 metallothionein le Ml 0942 156351 none found metallothionein If Ml 0943 156352 none found metallothionein lg J03910 156353 none found metallothionein 2a NM_0059 156360 BamHl 53 metallothionein 3 NM_0059 139255 none found 54 asparagine synthetase M27396 108370 none found SD-144141.1 Page 122 vo DO O C-Λ σN σ C-Λ u-ι -) -ι o -. -) -rι ---ι -. u^ • -f vo vo vo vo r - ^ ro r ro r r c c r'-i vo -o -i -i -i ^r ^ "^- T -^f 'f ' 'r ^r sr> V O Ό VO VO O O O O O O O O O O v -- -O U-ι -n (N CN CN CN CN CN cN CN C CN mismatch repair U03911 120435 A-943+3-T DEL Exon 5 protein 1.MSH2 mismatch repair U03911 120435 OT at codon 389 protein 1.MSH2 mismatch repair U03911 120435 711bp CGA>TGA arg>ter protein hMSH2 mismatch repair U03911 120435 C/T promoter protein hMSH2 mismatch repair U03911 120435 CTT to TTT at phe>leu protein hMSH2 codon 390 mismatch repair U03911 120435 1-bp insertion in protein 1.MSH2 exon 12 mismatch repair U03911 120435 codon 888 del C protein hMSH2 mismatch repair U03911 120435 T-to-C exon 13 protein l MSH2 cytochrome P450 X13589 107910 ARG435CYS aromatase (CYP 19) cytochrome P450 X13589 107910 CYS437TYR aromatase (CYP 19) cytochrome P450 X13589 107910 splice donor 29 extra amine aromatase (CYP 19) (GT>GC) of intron 6 acids cytochrome P450 X13589 107910 ARG375CYS aromatase (CYP 19) cytochrome P450 X13589 107910 1-BP DEL, 408C frameshift aromatase (CYP 19) cytochrome P450 X13589 107910 GT to AT exon and aromatase (CYP 19) intron 3 cytochrome P450 X13589 107910 G-1094 -A ARG365GLN aromatase (CYP 19) cytochrome P450 X13589 107910 G->A at Val80 silent SD-144141. Page 122 aromatase (CYP 19) cytochrome P450 X13589 107910 G-to-A Val370-to-Met aromatase (CYP 19) cytochrome P450 X13589 107910 (TTTA)n in intron 5 aromatase (CYP 19) cytochrome P450 X13589 107910 Arg264cys aromatase (CYP 19) glucocorticoid receptor Ml 1050 138040 ASP641VAL glucocorticoid receptor Ml 1050 138040 4-BP DEL 2 bases of the exon and the first 2 nucleotides of intron 6 glucocorticoid receptor Ml 1050 138040 LEU753PHE glucocorticoid receptor M11050 138040 ILE747THR glucocorticoid receptor Ml 1050 138040 CYS736SER glucocorticoid receptor Ml 1050 138040 CYS736THR glucocorticoid receptor Ml 1050 138040 ASN363SER glucocorticoid receptor Ml 1050 138040 Base-pair deletion in 32 amino acid exon 9 deletion glucocorticoid receptor Ml 1050 138040 Q710X glucocorticoid receptor Ml 1050 138040 L753F glucocorticoid receptor Ml 1050 138040 trinucleotide Arg453 insertion glucocorticoid receptor Ml 1050 138040 T insertion 1188 and frameshift 1189 glucocorticoid receptor Ml 1050 138040 A to G 3'-splice frameshift junction of intron G glucocorticoid receptor Ml 1050 138040 Bell glucocorticoid receptor Ml 1050 138040 Tthllll glucocorticoid receptor U25029 138040 none found SD- 144141 Page 122 alpha glucocorticoid receptor X03348 138040 none found beta multidrug resistance X96395 171050 GLY185VAL protein MDRl multidrug resistance X96395 171050 Ser893Ala protein MDRl multidrug resistance X96395 171050 Hindlll protein MDRl progesterone receptor M15716 264080 insulin-like growth X16302 146731 EcoRI factor binding protein 2 insulin-like growth M62403 146733 none found factor binding protein 4 multidrug resistance NM 0003 601107 none found protein MDR2 92 lipocortin 1 /annexin 1 V00546 151690 none found androgen receptor M20132 313700 PARTIAL DEL androgen receptor M20132 313700 ARG773CYS androgen receptor M20132 313700 TRP717TER androgen receptor M20132 313700 VAL866MET androgen receptor M20132 313700 TRP794TER androgen receptor M20132 313700 LYS588TER androgen receptor M20132 313700 TYR761CYS androgen receptor M20132 313700 LYS882TER androgen receptor M20132 313700 ARG772CYS androgen receptor M20132 313700 ALA771THR androgen receptor M20132 313700 MET786VAL androgen receptor M20132 313700 VAL730MET androgen receptor M20132 313700 (CAG)n androgen receptor M20132 313700 ARG773HIS SD-144141. Page 122 androgen receptor M20132 313700 ARG607GLN androgen receptor M20132 313700 VAL865MET androgen receptor M20132 313700 VAL865LEU androgen receptor M20132 313700 ARG855HIS androgen receptor M20132 313700 ILE869MET androgen receptor M20132 313700 GLN60TER androgen receptor M20132 313700 5-KB DEL,EX E androgen receptor M20132 313700 5-KB DEL, EX F,G androgen receptor M20132 313700 ARG608LYS androgen receptor M20132 313700 ARG839HIS androgen receptor M20132 313700 ARG839CYS androgen receptor M20132 313700 THR877ALA androgen receptor M20132 313700 LEU676PRO androgen receptor M20132 313700 THR877SER androgen receptor M20132 313700 HIS874TYR androgen receptor M20132 313700 GLN902ARG androgen receptor M20132 313700 ALA721THR androgen receptor M20132 313700 SER647ASN androgen receptor M20132 313700 LEU707ARG androgen receptor M20132 313700 CYS579PHE androgen receptor M20132 313700 PHE582TYR androgen receptor M20132 313700 PRO546SER androgen receptor M20132 313700 GLU2LYS androgen receptor M20132 313700 MET780ILE androgen receptor M20132 313700 ARG846HIS androgen receptor M20132 313700 Insert of 69 nucleotides androgen receptor M20132 313700 LEU172TER androgen receptor M20132 313700 (CAA)n androgen receptor M20132 313700 (GGN)n androgen receptor M20132 313700 pro892ser SD-144141. Page 123 androgen receptor M20132 313700 598 or 599 ter androgen receptor M20132 313700 Del T at 3286 frameshift androgen receptor M20132 313700 Gln798Glu androgen receptor M20132 313700 G214R androgen receptor M20132 313700 G Codon 210 A androgen receptor M20132 313700 G Codon 211 A androgen receptor M20132 313700 Arg615His androgen receptor M20132 313700 Arg752Gln androgen receptor M20132 313700 C>T within exon B silent androgen receptor M20132 313700 G2677A glu629arg androgen receptor M20132 313700 Stu l androgen receptor M20132 313700 arg7261eu androgen receptor M20132 313700 dell 893 frameshift androgen receptor M20132 313700 arg840his androgen receptor M20132 313700 Hind III androgen receptor M20132 313700 val 581 phe androgen receptor M20132 313700 Maelll androgen receptor M20132 313700 CAG340TAG Gln>Ter androgen receptor M20132 313700 gly743val androgen receptor M20132 313700 Hpall androgen receptor M20132 313700 Hhal androgen receptor M20132 313700 G2314A ala>thr clustrin/TRPM-2 M64722 185430 asp317 his clustrin/TRPM-2 M64722 185430 codon 328 (G->A) asp328asp fos proto-oncogene K00650 164810 T— >C transition in intron 2 myc proto-oncogene V00568 190080 PRO59ALA myc proto-oncogene V00568 190080 PRO57SER myc proto-oncogene V00568 190080 ASN86THR myc proto-oncogene V00568 190080 GLU39ASP bleomycin hydrolase X92106 602403 1450A-G ILE443VAL SD-144141. 1 Page 123 estrogen receptor 1 Ml2674 133430 done (ESR1) estrogen receptor 2 X99101 601663 done (ESR2) trefoil factor l/sP2 X00474 113710 Bcl-2 associated L22473 600040 1-BP INS Codons 38 to 41 protein/bax Bcl-2 associated L22473 600040 1-BP DEL Codons 38 to 41 protein/bax Bcl-2 associated L22473 600040 GLY67ARG protein/bax Bcl-2 associated L22473 600040 7-BP DEL codons 38 to 41 protein/bax protein kinase C alpha X52479 176960 ASP294GLY protein kinase C beta 1 X06318 176970 none found protein kinase C delta L07861 176977 none found protein kinase C mu X75756 ****** none found protein kinase C theta L01087 600448 none found protein kinase C zeta L14283 176982 none found insulin-like growth NM 0005 146730 none found factor binding protein 1 96 insulin-like growth U62015 602369 none found factor binding protein 10 insulin-like growth NM 0005 146732 none found factor binding protein 3 98 insulin-like growth L27560 146734 none found factor binding protein 5 insulin-like growth M69054 146735 none found factor binding protein 6 insulin-like growth L19182 602867 none found SD-144141 Page 123 factor binding protein 7 interfereon gamma NM 0008 602376 none found receptor 2 (IFNGR2) 74 interferon alpha X77722 107450 none found receptor 1 (IFNAR1) interferon alpha U68755 147569 Gln64Arg receptor 2 (IFNAR2) interferon betal V00546 147640 none found (IFNbl) interferon gamma L07633 147570 CA repeat itron 1 (IFNg) interferon gamma L07633 147570 CGA to CAA Argl40Gln (IFNg) inlci fcron gamma L07633 147570 G5644A (IFNg) interferon gamma J03143 107470 395C-A SER-TER receptor 1 (IFNGR1) interferon gamma J03143 107470 1-BP DEL frameshift receptor 1 (IFNGR1) interferon gamma J03143 107470 ILE87THR receptor 1 (IFNGR1) interferon gamma J03143 107470 4-BP INS 104 to 107 frameshift receptor 1 (IFNGR1) interferon gamma J03143 107470 IVS3 receptor 1 (IFNGR1) interferon gamma J03143 107470 4-BP DEL truncated receptor 1 (IFNGR1) protein interferon gamma J03143 107470 Vall4Met receptor 1 (IFNGR1) interferon gamma J03143 107470 Taql receptor 1 (IFNGR1) SD-144141 Page 123 interferon omegal X02669 147553 none found (IFNwl) interleukin 1 alpha M15329 147760 C to T -889 (ILl a) interleukin 1 alpha M15329 147760 Dinucleotide repeat (ILla) interleukin 1 alpha M15329 147760 46 bp tandem repeat (ILla) intron 6 interleukin 1 beta K02770 147720 Taql (ILlb) interleukin 1 beta K02770 147720 +5887 C -> T (ILlb) interleukin 1 beta K02770 147720 position -511 (ILlb) interleukin 1 beta K02770 147720 exon 5 (position (ILlb) +3953) interleukin 1 beta K02770 147720 Asp 106 Asn (ILlb) interleukin 1 receptor M27492 147810 Pstl (IL-1R) interleukin 10 (IL10) M57627 124092 G -1082 A interleukin 10 (IL10) M57627 124092 C-to-A 571 interleukin 10 (IL10) M57627 124092 A-597 C interleukin 10 (IL10) M57627 124092 T -824 C interleukin 10 (IL10) M57627 124092 second dinucleotide repeat interleukin 10 (IL10) M57627 124092 A -592 C interleukin 10 (IL10) M57627 124092 2 CA repeat interleukin 10 receptor U00672 146933 none found alpha (IL-1 ORa) interleukin 11 (ILl l) X58377 147681 5' dinucleotide SD-144141.1 Page 123 ( -> ift PL, Ct, ω Pi 00 <S w H m H w Is H <U C (N 00 CN VO £ 00 ϋ 00 cd W J < 00 ϋ » CN σs oo N o * v vo vo vo t-- O v O VO VO r- » t-- r- r- C CN * 0O 00 00 00 u-i U-) VO oo 00 OO 00 O oo CN CN O ■ r V O ιτ i as ro * U"l U") u-- u-i o VO o O O o s -X- o V O vo vo --. ro * o o o o o o CN SSX^^ * X X X X X X Q Q Q interleukin 2 receptor D11086 308380 G-to-A first position gamma (IL-2Rg) of intron 3 interleukin 2 receptor D11086 308380 ILE 153 ASN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 LEU271GLN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 9-BP DUP GLN-HIS-TRP gamma (IL-2Rg) INS interleukin 2 receptor D11086 308380 CYS115ARG gamma (IL-2Rg) interleukin 2 receptor D11086 308380 ARG285GLN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 ARG222CYS gamma (IL-2Rg) interleukin 2 receptor D11086 308380 690-691 hotspot gamma (IL-2Rg) interleukin 3 (IL3) M20137 147740 none found interleukin 3 alpha M74782 308385 none found receptor (IL-3aR) interleukin 4 (IL4) M13982 147780 C-589T interleukin 4 (IL4) M13982 147780 Dinucleotide Repeat intron 2 interleukin 4 (IL4) M13982 147780 -285 C-T interleukin 4 (IL4) M13982 147780 -81 A-G interleukin 4 receptor X52425 147781 GLN576ARG (IL-4R) interleukin 4 receptor X52425 147781 ILE50VAL (IL-4R) interleukin 4 receptor X52425 147781 S503P (IL-4R) interleukin 5 (IL5) X04688 147850 none found SD-144141.1 Page 123 interleukin 5 receptor M96652 147851 Dinucleotide repeat alpha (IL-5Ra) interleukin 6 receptor M20566 147880 dinucleotide (CA) (IL-6R) (20) interleukin 7 (IL7) J04156 146660 none found interleukin 7 receptor M29696 146661 THR66ILE (IL-7R) interleukin 7 receptor M29696 146661 ILE138VAL (IL-7R) interleukin 7 receptor M29696 146661 AG-to-AA splice (IL-7R) junction intron 4 interleukin 7 receptor M29696 146661 trp217 to ter (IL-7R) interleukin 8 (IL8) M26383 146930 Hindlll interleukin 8 receptor M68932 146929 none found alpha (IL-8Ra) interleukin 8 receptor M94582 146928 none found beta (IL-8Rb) interleukin 9 (IL9) X17543 146931 Dinucleotide repeat interleukin 9 receptor M84747 300007 none found (IL-9R) interleukin receptor 11 U32324 600939 none found alpha (IL-1 la) interleukin receptor 12 U03187 601604 GLN32TER beta (I L-l 2b) interleukin receptor 12 U03187 601604 GLN376TER beta (IL-12b) interleukin receptor 12 U03187 601604 409-549DEL frameshift bcta (IL-12b) interleukin receptor 12 U03187 601642 none found beta2 (IL-12b2) SD-144141.1 Page 123 interleukin receptor 13 S80963 300119 none found alpha (IL-13a) interleukin receptor 13 X95302 300130 none found alpha2 (IL-13a2) lipocortin 2/annexin 2 D00017 151740 none found lipocortin 3/annexin 3 M20560 106490 tandem repeat TAAA lipocortin 3/annexin 3 M20560 106490 Sail lipocortin 3/annexin 3 M20560 106490 Bglll lipocortin 5/annexin 5 NM 0011 131230 EcoRI 54 lipocortin 5/annexin 5 NM 0011 131230 PvuII 54 lipocortin 7/annexin 7 NM 0040 186360 none found (splice variant 1 ) 34 lipocortin 7/annexin 7 NM 0011 186360 none found (splice variant 2) 56 trefoil factor 2/TFF2 X51698 182590 25 bp tandem repeat trefoil factor 3/sP2 L08044 600633 none found Table 19- Identified Variances in Genes or Related Pathways involved in Neurological or Psychiatric Disease Nicotinic, Cholinergic X14830 100710 LEU263MET receptor beta 1 Nicotinic, Cholinergic X14830 100710 VAL266MET receptor beta 1 SD-144141.1 Page 123 Nicotinic, Cholinergic X55019 100720 none found receptor, muscle d Nicotinic, Cholinergic X66403 100725 ARG147LEU receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 ARG64TER receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 LEU269PHE receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 PRO121LEU receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 THR264PRO receptor epsilon nπyjilvyr U-Cp--πUt11.UHPC Nicotinic, Cholinergic NM 0051 100730 none found receptor, muscle g 99 Acetylcholinesterase/A M55040 100740 1431 C/T 446 silent CHE Acetylcholincsterase/A M55040 100740 408 G/C arg561pro CHE Acetylcholinesterase/A M55040 100740 HIS322ASN CHE adenosine deaminase NM 0000 102700 LYS80ARG 22 adenosine deaminase NM_0000 102700 ARGIOITRP 22 adenosine deaminase NM_0000 102700 ARG101GLN 22 SD-144141 Page 123 adenosine deaminase NM 0000 102700 ARG211HIS 22 adenosine deaminase NM 0000 102700 LEU304ARG 22 adenosine deaminase NM 0000 102700 ALA329VAL 22 adenosine deaminase NM 0000 102700 ALA39VAL 22 adenosine deaminase NM 0000 102700 3.25-KB DEL 22 adenosine deaminase NM 0000 102700 PRO297GLN 22 adenosine deaminase NM 0000 102700 ARG76TRP 22 adenosine deaminase NM 0000 102700 ARG149GLN 22 adenosine deaminase NM 0000 102700 PRO274LEU 22 adenosine deaminase NM 0000 102700 LEU107PRO 22 adenosine deaminase NM 0000 102700 ARG211CYS 22 adenosine deaminase NM 0000 102700 ALA215THR 22 adenosine deaminase NM 0000 102700 GLY216ARG 22 adenosine deaminase NM 0000 102700 IVS3AS, A-G, -2 EX4DEL 22 adenosine deaminase NM 0000 102700 ARG156CYS 22 adenosine deaminase NM 0000 102700 SER291LEU SD- 144 141.1 Page 124 adenosine deaminase NM 0000 102700 IVS10AS, G-A, -34 22 adenosine deaminase NM 0000 102700 ASP8ASN 22 adenosine deaminase NM 0000 102700 IVS2DS, , G-A, +1 22 adenosine deaminase NM 0000 102700 7-BP INS, IVS8AS 22 adenosine deaminase NM 0000 102700 IVSIDS , G-C, +1 22 adenosine deaminase NM 0000 102700 GLY74VAL 22 adenosine deaminase NM 0000 102700 IVS5DS, G-A. +1, EX5 DEL 22 116-BP DEL adenosine deaminase NM 0000 102700 LEU152MET 22 adenosine deaminase NM 0000 102700 THR233ILE 22 adenosine deaminase NM 0000 102700 TYR97CYS 22 adenosine deaminase NM 0000 102700 LEU106VAL 22 adenosine deaminase NM 0000 102700 G74C 22 adenosine deaminase NM 0000 102700 V129M 22 adenosine deaminase NM 0000 102700 G140E 22 adenosine deaminase NM 0000 102700 R149W 22 SD-144141.1 Page 124 cu -3 u 3 < o H- H o o CU ω u U <u < o r-- 3 Ul — 3 O +- cd *- 3 ϋ.g > 3 o O o o o o o o o o o Ul u-i o O o o o o o o o o o r- r- r- r- t-~ r- r^ r- r- r-- CN <N CN CN CN N CN N CN O o o o o o o o o o o Adenosine Al L22214 102775 1904C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2126G/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2294insT Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 267 + 275C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2776C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2777del36 Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2819T/G Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 805T/G Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 48T/A Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 716T/G Receptor; Adoral/G protein-coupled Adenosine A2 X68486 102776 1083C/T SD-144141.1 Page 124 Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 405C/T Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 432C/T Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 Gly-340-Ser Receptor; Adora2a/G protein-coupled Adenosine A2 102777 none found Receptor- like/ADORA2Ll adenylate-cyclase D17516 102981 none found activating polypeptide 1 receptor/ADCYAPlRl alpha-2a-adrenergic M18415 104210 -1291 receptor; ADRA2A alpha-2a-adrenergic M18415 104210 Dral receptor; ADRA2A alpha-2a-adrenergic M18415 104210 Hhal receptor; ADRA2A alpha-2a-adrenergic M18415 104210 Mspl promoter receptor; ADRA2A alpha- 1 a-adrenergic M76446 104219 none found receptor; ADRA1A alpha- 1 b-adrenergic L31773 104220 none found receptor; ADRA1B alpha- 1 c-adrenergic D25235 104221 Pstl SD-144 I 41.1 Page 124 receptor; ADRAIC alpha- 1 d-adrenergic M76446 104222 none found receptor; ADRA1D alpha-2c-adrenergic J03853 104250 (CA)n receptor; ADRA2C alpha-2b-adrenergic AF005900 104260 none found receptor; ADRA2B presenilin 1 NM 0000 104311 IVS8AS, G-T, -1, 21 EX9DEL presenilin 1 NM 0000 104311 1-BP DEL, G 21 presenilin 1 NM 0000 104311 intron 3' to exon 8 21 presenilin 1 NM 0000 104311 T/G intron 9 21 presenilin 1 NM 0000 10431 1 HIS 163 ARG 21 presenilin 1 NM 0000 104311 ALA246GLU 21 presenilin 1 NM 0000 104311 ALA426PRO 21 presenilin 1 NM 0000 104311 ARG278THR 21 presenilin 1 NM 0000 104311 CYS410TYR 21 presenilin 1 NM 0000 104311 GLU120ASP 21 presenilin 1 NM 0000 104311 GLU280ALA 21 presenilin 1 NM 0000 10431 1 GLU280GLY 21 SD-144141.1 Page 124 preseni in 1 NM 0000 104311 Glu318Gly 21 preseni 111 NM 0000 104311 gly378glu 21 preseni in NM 0000 104311 HIS163TYR 21 preseni in 1 NM 0000 104311 LEU250SER 21 preseni in NM 0000 104311 Leu262Phe 21 preseni in NM 0000 104311 Leu282Arg 21 preseni in NM 0000 104311 LEU286VAL 21 preseni in NM 0000 104311 lysl23glu 21 preseni in NM 0000 104311 MET139VAL 21 preseni i n NM 0000 104311 MET146ILE 21 preseni in NM 0000 104311 MET146LEU 21 preseni in NM 0000 104311 MET 146 VAL 21 preseni in NM 0000 104311 PRO267SER 21 preseni in NM 0000 104311 Pro436Gln 21 preseni in 1 NM 0000 104311 Serl69Leu 21 Human cerebrovascular M16765 104760 SD- 144141 - 1 Page 124 and neuritic plaque amyloid beta-protein mRNA, 3' end angiotensin receptor M87290 106165 1166A-C 1/AGTR1A angiotensin converting NM 0007 106180 250-bρ in/del enzym c/d i p eptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 3 in the 3' UTR enzyme/dipeptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 5 in the 5' region enzym c/d i peptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 Pst I RFLP enzy e/d i p ep ti dyl 89 carboxypeptidase Interferon (alpha,beta, J03171 107450 none found omega) receptor 1 apolipoprotein NM 0000 107741 7 AA insertion; E/APOE 41 tandem repeat of residues 121-127 apolipoprotein NM 0000 107741 A178G Threonine42Ala E/APOE 41 nine apolipoprotein NM 0000 107741 A490C Lysine 146Gluta E/APOE 41 mine apolipoprotein NM 0000 107741 A490G Lysine 146Gluta E/APOE 41 ic Acid apolipoprotein NM 0000 107741 A940C Serine296Argini E/APOE 41 ne apolipoprotein NM 0000 107741 Aintron3G substitution SD-144141 Page 124 E/APOE 41 creates 2 abnormally spliced mRNA forms apolipoprotein NM 0000 107741 C305G Proline84Argini E/APOE 41 ne apolipoprotein NM 0000 107741 C460A Argininel36Seri E/APOE 41 ne apolipoprotein NM 0000 107741 C478T Argl42142Cysl E/APOE 41 42 apolipoprotein NM 0000 107741 C487T Argininel45Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C526T Arginine 158Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C736T Arginine228Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C805G Arg251251Gly2 E/APOE 41 51 apolipoprotein NM 0000 107741 G144deletion LeucineόOTermi E/APOE 41 nation Codon (frameshift) apolipoprotein NM 0000 107741 G349A Ala9999Thr99 E/APOE 41 apolipoprotein NM 0000 107741 G434A Glyl27127Aspl E/APOE 41 27 apolipoprotein NM 0000 107741 G455A Argininel34Glu E/APOE 41 tamine apolipoprotein NM 0000 107741 G488A Argininel45His E/APOE 41 tidine apolipoprotein NM 0000 107741 G568C Alal52Proline E/APOE 41 SD-144141.1 Page 124 apolipoprotein NM 0000 107741 G61A Glutamic E/APOE 41 Acid3 Lysine apolipoprotein NM 0000 107741 G683A Tryptophan210 E/APOE 41 Termination Codon apolipoprotein NM 0000 107741 G725A Arg224224Gln2 E/APOE 41 24 apolipoprotein NM 0000 107741 G875A Arginine274His E/APOE 41 tidine apolipoprotein NM 0000 107741 G91A Glutamic E/APOE 41 Acid 13 Lysine apolipoprotein NM 0000 107741 GAG-GAG844- Glu244/Glu245 E/APOE 41 849AAG-AAG 244- 245Lys244/Lys 245 apolipoprotein NM 0000 107741 T137C Leucine28Prolin E/APOE 41 e apolipoprotein NM 0000 107741 T388C Cysteinel l2Arg E/APOE 41 inine apolipoprotein NM 0000 107741 T761A Valine236Gluta E/APOE 41 mic Acid Aromatic L-Amino M76180 107930 Sspl Acid Decarboxylase/ AADC/ dopa decarboxylase Benzodiazepine NM 0007 109610 none found receptor, peripheral 14 type beta- 1 -adrenergic J03019 109630 Bgl l. receptor; Adrbl beta- 1 -adrenergic J03019 109630 C1165G ARG389GLY SD-144141. Page 124 receptor; Adrbl beta-adrinergic NM_0016 109635 none found receptor kinase 19 1/BAR 1 Beta-Adrenergic X691 17 109636 none found Receptor Kinase 2; Adrbk2 Beta-2- Adrenergic M15169 109690 Fnu4HI Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 A->G -1343 Receptor; Adrb2 Beta-2- Adrenergic Ml 5169 109690 C->G -468 Receptor; Adrb2 Beta-2-Adrcnergic M15169 109690 G->A -1023 Receptor; Adrb2 Beta-2-Adrcnergic M15169 109690 G~>A -654 Receptor; Adrb2 Beta-2- Adrenergic Ml 5169 109690 T->A -1429 Receptor; Adrb2 Beta-2- Adrenergic M15169 109690 T->C -20 Receptor; Adrb2 Beta-2-Adrcnergic M15169 109690 T->C -367 Receptor; Adrb2 Beta-2-Adrcnergic M15169 109690 T->C -47 Receptor; Adrb2 Beta-2- Adrenergic M15169 109690 ARG16GLY Receptor; Adrb2 Beta-2-Adrcnergic M15169 109690 GLN27GLU Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 Thrl64Ile Receptor; Adrb2 SD-144141.1 Page 125 Beta-2-Adrcnergic M15169 109690 val 34 met Receptor; Adrb2 Beta-3-Adrenergic X70811 109691 intron 1 gl856t Receptor; Adrb3 Beta-3-Adrcnergic X70811 109691 TRP64ARG Receptor; Adrb3 serotonin 5-HT X57829 109760 Rsal receptors 5-HT1 A, G protein-coupled bradykinin receptor NM 0006 113503 -143C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -412C/G B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -536C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -640T/C B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 1 13503 -649insG B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -704C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -78C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -845C/T SD- 1 I 1 14 1 . 1 Page 125 B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 9bpde(-)21-29 B2/BDKRJB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 C>T promoter 54 B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 repeat 3 'UTR B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 tandem repeat near B2/BDKRB2 G 23 promoter protein-coupled brad\ kin in receptor NM 0006 113503 R14C B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 T21M B2/BDKRB2 G 23 protein-coupled L-typc voltage NM 0007 114205 none found dependent calcium 19 channel alpha I C subunit/CACNAlC L-type voltage NM 0000 114208 ARG1086HIS dependent calcium 69 channel alpha IS subunit/CACNAlS L-type voltage NM 0000 114208 ARG1239GLY dependent calcium 69 channel alpha I S SD- 1 14141 .1 Page 125 subunit/CACNAlS L-type voltage NM_0000 114208 ARG1239HIS dependent calcium 69 channel alpha I S subunit/CACNAlS L-type voltage NM_0000 114208 ARG528HIS dependent calcium 69 channel alpha IS subunit/CACNAlS calpain, large NM_0000 114240 ARG572GLN pol) peptide 70 L3/CAPN3 calpain, large NM_0000 114240 ARG110TER polypeptide 70 L3/CAPN3 calpain, large NM_0000 114240 ARG769GLN polypeptide 70 L3/CΛPN3 calpain, large NM_0000 114240 PRO319LEU polypeptide 70 L3/CAPN3 calpain, large NM_0000 114240 SER86PHE polj'peptide 70 L3/CAPN3 cannabinoid receptor NM_0018 114610 1359G->A silent 1/G protein- 40 coupled/CNRl Catcchol-O- M58525 116790 186C > T at exon 3 Methyltransferase Catcchol-O- M58525 116790 408C > G at exon 4 Methyltransferase SD-1 4141.1 Page 125 Catcchol-O- M58525 116790 472G > A at exon 4 Methyltrans (erase Catcc ol-O- M58525 116790 597G > A at exon 5 Methyltransferase Catcchol-O- M58525 1 16790 821-827insC at the 3' Methyltransferase Catcchol-O- M58525 116790 Bgll Methyltransferase Catcchol-O- M58525 116790 C256G silent Methyltransferase Catcchol-O- M58525 116790 G/A 1947 M et I lyl trans (erase Catcchol-O- M58525 116790 Mspl Melln ltransferase Catcc-hol-O- M58525 116790 Nlalll Methyltransferase Catcchol-O- M58525 116790 val-108-met Metln ltransferase Catcchol-O- M58525 116790 Vall58->Met Methyltransferase cathepsin B/b- M14221 116810 10-bp insertion in aCTSBmyloid the 3'-UT precursor protein secretase CTSB cathepsin B/b- M14221 116810 CYS26ARG aCI SBmyloid precursor protein secretase/CTSB cathepsin β/b- M14221 116810 EcoRI aCTSBmyloid precursor protein SD- 1 1 114 1. Page 125 secretase/CTSB cathepsin B/b- M14221 116810 Taql aCTSBmyloid precursor protein secretase/CTSB Cholecystokinin A LI 3605 118444 GLY21ARG receptor/CCKAR Cholecystokinin A LI 3605 118444 VAL365ILE receptor/CCKAR Cholecystokinin B L08112 118445 1550 G->A Vall25->Ile receptor/CCKBR Cholecystokinin B L08112 118445 CAT 207 CAC His207His receptor/CCKBR Cholecystokinin B L08112 118445 Arg215His receptor/CCKBR Cholecystokinin B L08112 118445 Vall38Met receptor/CCKBR plasma cholesterol NM_0000 118470 A1503G ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 G-A splice junction alternative ester transfer 78 splice protein/CETP plasma cholesterol NM_0000 118470 G 1696 A ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 C-T transition in ester transfer 78 intron 12 protein/CETP plasma cholesterol NM_0000 118470 EcoNI ester transfer 78 SD-144141 .1 Page 1255 protein/CETP plasma cholesterol NM 0000 118470 G-->A intron 14 ester transfer 78 protein CETP plasma cholesterol NM 0000 118470 G-A transition in ester transfer 78 intron 15 protein/CETP plasma cholesterol NM 0000 118470 G1533A ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 INS T alternative ester transfer 78 (intron exonl4) splice protein/CETP plasma cholesterol NM 0000 118470 Stul ester transfer 78 protei n/CETP plasma cholesterol NM 0000 118470 T->G tyr57stop ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 TaqlA ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 TaqlB in intron 1 ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 268 Arg- ester transfer 78 >STOP protein/CETP plasma cholesterol NM 0000 118470 Asp 442 tc ester transfer 78 protein/CETP SD-14414 1.1 Page 1256 plasma cholesterol NM 0000 118470 ASP442GLY ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 G181X ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 I405V ester transfer 78 protein CETP plasma cholesterol NM 0000 118470 Lys309-Stop ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 R451Q ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 Val421-Ile ester transfer 78 protein/CETP Choline NM 0030 118490 none found acetyltraπsferase/CHA 55 T Cholinergic Receptor, U19800 118493 none found Muscarinic, 2; CHRM2 Cholinergic Receptor, U29589 118494 none found Muscarinic, 3; CHRM3 Cholinergic Receptor, Ml 6405 118495 Sstl Muscarinic, 4; CHRM4 Cholinergic Receptor, AF026263 118496 none found Muscarinic, 5; CHRM5 Nicotinic, Cholinergic U62431 118502 none found receptor alpha 2 SD- 14 U41 Page 1257 Nicotinic, Cholinergic X53559 118503 none found receptor alpha 3 Nicotinic, Cholinergic U62433 118504 3-BP INS, 776GCT receptor alpha 4 Nicotinic, Cholinergic U62433 118504 Cfol exon 5 receptor alpha 4 Nicotinic, Cholinergic U62433 118504 Dinucleotide intron receptor alpha 4 1 Nicotinic, Cholinergic U62433 118504 fokl receptor alpha 4 Nicotinic, Cholinergic U62433 118504 PvuII receptor alpha 4 Nicotinic, Cholinergic U62433 118504 SER-TER receptor alpha 4 Nicotinic, Cholinergic U62433 118504 SER248PHE receptor alpha 4 Nicotinic, Cholinergic M83712 118505 none found receptor alpha 5 Nicotinic, Cholinergic Y08415 118507 none found receptor beta 2 Nicotinic, Cholinergic X67513 118508 none found receptor beta 3 Nicotinic, Cholinergic X68275 118509 none found receptor beta 4 Cholinergic Receptor, X15263 118510 none found Muscarinic, 1 ; CHRMl Nicotinic, Cholinergic U40583 118511 none found receptor alpha 7 ciliary neurotrophic ooi8 118946 none found factor rcceptor/CNTFR 42 Corticotropin releasing U16273 122561 none found SD-144141.1 Page 1258 hoπnone receptor 1 diazepam binding M15887 125950 none found inhibitor/DBI Human dihydrofolate J00140 126060 reductase gene Dopamine Receptor DI X58987 126449 C/T Isoleucine49 Dopamine Receptor D2 X51362 126450 141 C ins/del Dopamine Receptor D2 X51362 126450 A241G Dopamine Receptor D2 X51362 126450 Ncol RFLP Dopamine Receptor D2 X51362 126450 Taql A, Taql B, Taql D, and (CA)n ST-RP Dopamine Receptor D2 X51362 126450 Serine 311Cysteine Dopamine Receptor D3 U32499 126451 exonic Ball polymoφhism Dopamine Receptor D3 U32499 126451 intronic Mspl polymorphism Dopamine Receptor D3 U32499 126451 Serine9Glycine Dopamine Receptor D4 L12398 126452 12 bp duplication/deletion in exon 1 Dopamine Receptor D4 L12398 126452 12 bp tandem repeat in extracellular N- terminal part of receptor Dopamine Receptor D4 L12398 126452 12 bp VNTR in exon 1 Dopamine Receptor D4 L12398 126452 48 bp VNTR in exon 3 Dopamine Receptor D4 L12398 126452 48 bp VNTR in exon SD- 1 1414 1 1 Page 1259 Dopamine Receptor D4 L12398 126452 48 bp VNTR in exon 3 Dopamine Receptor D4 L12398 126452 48 bp VNTR in third cytoplasmic loop Dopamine Receptor D4 L12398 126452 exon 1 ~ nondeleted sequence in 13bp deletion site Dopamine Receptor D4 L12398 126452 exon 3 (48 bp repeat) Dopamine Receptor D4 L12398 126452 exon 3 (position 194) — common valine producing T at glycine subst site Dopamine Receptor D4 L12398 126452 poly G in intron 1 Dopamine Receptor D4 L12398 126452 Smal cutting site (bands of413bp and 302bp) in 5' noncoding region Dopamine Receptor D4 L12398 126452 Smal RFLP in 5' noncoding region Dopamine Receptor D5 M67439 126453 (TC)n Dopamine Receptor D5 M67439 126453 dinucleotide repeat poly (CT/GT/GA)n Dopamine Receptor D5 M67439 126453 T978C P326P Dopamine Receptor D5 M67439 126453 transmembrane L88F domain II Dopamine Transporter/ L24178 126455 40-bp VNTR in the DA 1 3'-untranslated Dopamine Transporter/ L24178 126455 5' Taql RFLP DA ' I 1 SD-144141. Page 1260 Dopamine Transporter/ L24178 126455 9-repeat allele DAT1 estrogen receptor 1 M12674 133430 RFLP (Pssl enzyme) (ESR1) estrogen receptor 1 M12674 133430 RFLP (PvuII (ESR1) enzyme) Solute Carrier Family U08989 133550 none found 1, Member l ; Slclal Gamma-Aminobutyric S62907 137140 none found Acid Receptor, Alpha- 2; Gabra2 Gamma-Aminobutyric U30461 137141 none found Acid Receptor, Alpha- 4; Gabra4 Gam l na- Aminobutyric L08485 137142 Dinucleotide repeat Acid Receptor, Alpha- 5; Gabra5 Gamma-Aminobutyric S81944 137143 none found Acid Receptor, Alpha- 6; Gabra6 GABA-glulamate NM_0006 137150 3' DELETION transaminase 63 GAB A- glutamate NM_0006 137150 ARG220LYS transaminase 63 Gamma-Aminobutyric X14766 137160 Dinucleotide repeat Acid Receptor, Alpha- 1; Gabral Gamma-Aminobutyric M62400 137161 Pstl Acid Receptor Subunit Rho l Gamma-Aminobutyric M86868 137162 none found SD- 14414 1.1 Page 1261 Acid Receptor Subunit Rho2 Gamma-Aminobutyric AF016917 137163 none found Acid Receptor, Delta; Ga ma-Λminobutyric X15376 137164 Neil Acid Recepto , Gamma-2; Gabrg2 Soluie carrier family 6 X54673 137165 none found ( GABA), member 1/SLC6A1 Gamma-Aminobutyric 137166 none found Acid Receptor,Gamma-l ; Gab gl Gam ma-Aminobutyric X14767 137190 C~>G his396glu Acid Receptor, Beta-1 ; Gabrbl Gam i na- A minobutyric M82919 137192 Dinucleotide repeat Acid Receptor, Beta-3; Gabrb3 glucagon-like peptide 1 U01156 138032 silent substitution in recepto r/GLPIR exon 6 glucagon ■ ike peptide 1 UOI 156 138032 simple tandem receplor/GLPlR repeat DNA polymoφhism glucagon NM_0001 138033 Alu-repeat receptor/GCGR 60 glucagon NM_0001 138033 GLY40SER receptor/GCGR 60 SD- 1 1414 1 1 Page 1262 Glutamate X07674 138130 G/A at ntd 955 dehydrogenase 1 Glutamate X07674 138130 Taql dehydrogenase 1 Glutamate X07674 138130 GLY446ASP dehydrogenase 1 Glutamate X07674 138130 GLY446SER dehydrogenase 1 Glutamate X07674 138130 HIS454TYR dehydrogenase 1 Glutamate X07674 138130 SER445LEU dehydrogenase 1 Glutamate X07674 138130 SER448PRO dehydrogenase 1 mitochondrial NM 0020 138150 none found glutamate oxaloacetate 80 transaminase 2/GOT2 soluble glutamate NM 0020 138180 none found oxaloacetate 79 transaminase 1/GOTl Glutamate Receptor, U16127 138243 none found Ionotropic, Kainate 3; Grik Glutamate Receptor, S75105 138244 trinucleotide repeat Ionotropic, Kainate 2; 3' Glutamate Receptor, U16125 138245 none found Ionotropic, Kainate 1; Glutamate Receptor, NM 0008 138246 none found Ionotropic, Ampa 4; 29 SD-N 'I M ! 1 Gria4 Glutamate Receptor, L20814 138247 none found Ionotropic, -Ampa 2; Gria2 Glutamate Receptor, M64752 138248 none found Ionotropic, Ampa 1; Gria ! Glutamate Receptor, L13266 138249 none found Ionotropic, N-Methyl- D-Asp 1 ; Grinl Glutamate Receptor, 138251 none found Ionotropic, N-Methyl- D-Asp A; Grina Glutamate Receptor, U28758 138252 none found Ionotropic, N-Methyl- Glutamate Receptor, U09002 138253 none found Ionotropic, N-Methyl- D-Asp 2a; Grin2a Glutamate Receptor, L76224 138254 none found Ionotropic, N-Methyl- D-Asp 2c; Grin2c Glutamate X69936 138275 (CA) repeat decarboxylase 2 (brain, polymoφhism 65kD) Glutamate 138276 none found decarboxylase 3 Glycine Receptor, X52009 138491 null allele Alpha- 1 Subunit; Glral Glycine Receptor, X52009 138491 ARG271GLN Alpha- l Subunit; Glral SD- Page 1264 Glycine Receptor, X52009 138491 ARG271LEU Alpha-1 Subunit; Glral Glycine Receptor, X52009 138491 GLN266HIS Alpha-1 Subunit; Glral Glycine Receptor, X52009 138491 ILE244ASN Alpha-1 Subunit; Glral Glycine Receptor, X52009 138491 LYS276GLU Alpha-1 Subunit; Glral Glycine Receptor, X52009 138491 P250T Alpha-1 Subunit; Glral Glycine Receptor, X52009 138491 TYR279CYS Alpha-1 Subunit; Glral Glycine Receptor, Beta U33267 138492 none found Subunit; Glrb gonadotropin releasing NM 0004 138850 ARG262GLN hormone receptor/G 06 protein- coup led LHRHR/GNR HR gonndoli opin releasing NM_0004 138850 GLN106ARG hormone receptor/G 06 protei n- coupled/LHRHR/GNR HR gonadotropin releasing NM_0004 138850 Mae III hormone rcceptor/G 06 protein- coLipled/LI IRHR/GNR HR gonadoti opin releasing NM_0004 138850 TYR284CYS hormone receptor/G 06 SD-1 41 U 1 Page 1265 prolein- coupled/LHRHR/GNR HR growth hormone U34195 139191 IVS8DS, G-C, -1 alternative releasing hormone splice receptor/G protein- coup led/ GHRHR growth hoπnone U34195 139191 1-BP DEL -frameshift releasing hormone recepto /G protein- coupled/GHRHR grow th hormone U34195 139191 2-BP DEL frameshift releasing hormone receptor/G protein- coupled/GHRHR gro th hormone U34195 139191 C to T codon 236. silent releasing hormone receptor/G protein- coupled/GHRHR grow th hormone U34195 139191 EX4,6DEL releasin-' hormone receptor/G protein- coup led/GHRHR growth hormone U34195 139191 GAA180GAG silent releasing hormone receptor/G protein- coup led/GHRHR growth hormone U34195 139191 IVS4DS, G-A, +1 alternative releasing hormone splice receptor/G protein- couple /GHRHR SD- 1 1414 1 .1 Page 1266 grow th hormone U34195 139191 IVS6AS, G-T, -1 releasing hormone receptor G protein- coup led/GHRHR grow th hormone U34195 139191 IVS8AS, G-C, -1 releasing hormone receptoi/G protein- coupled/GHRHR grow th hormone U34195 139191 IVS9DS, G-A, +1 frameshift releasing hormone receptoi/G protein- couplecl/GHRHR grow th hormone U34195 139191 P561T releasing hormone receptor/G protein- coup led/GHRHR grow th hormone U34195 139191 ARG161CYS releasing hormone reccploi/G protein- coupled. GHRHR grow th hormone U34195 139191 ARG217TER releasing hormone receptoi/G protein- coup le 'GHRHR grow th hormone U34195 139191 ARG43TER releasi , hormone reccntor'G protein- coupled GHRHR grow th hormone U34195 139191 ASP152HIS releasing, hormone receptoi G protein- Page 1267 SD-1 141 I I coup led/GHRHR growth hormone U34195 139191 CYS38TER releasing hormone receptor/G protein- coup lech GHRHR grow th hormone U34195 139191 GLN154PRO releasing hormone rece to! G protein- coupled, GHRHR grow th hormone U34195 139191 GLU224ASP releasing hormone reccptor/G protein- coup led/GHRHR grow th hormone U34195 139191 GLU224TER releasing, hormone recepto! G protein- coup led/GHRHR grow th hormone U34195 139191 GLU44LYS releasing hormone receπtoi G protein- coupled GHRHR grow th hormone U34195 139191 ILE153THR releasing hormone rece toi G protein- coup led/GHRHR grow th hormone U34195 139191 PHE96SER releasing hormone receptoi G protein- coupled. GHRHR grow th hormone U34195 139191 PRO131GLN rclcasiii " hormone SD- 1 14 1 Page 1268 receptor/G protein- coupled/GHRHR growth hormone U34195 139191 VAL144ILE releasing hormone receptor/G protein- coiφled/GHRHR grow th hormone U34195 139191 VAL155GLY releasing, hormone receptor/G protein- coupled GHRHR Histamine receptor H2 M64799 142703 A649G Histidine M60445 142704 none found Decarboxylase HMGCoA NM 0008 142910 HgiAI reductasc/HMGCR 59 HMGCoA NM 0008 142910 ScrFI polymorphism reductase/HMGCR 59 in the 2nd intron Superoxide Dismutase NM 0004 147450 T-G, -10, 9-BP INS 1/SOD l (soluble) 54 Superox ide Dismutase NM 0004 147450 VS4AS. A-G. -11 1/SOD l (soluble) 54 Supero \ ide Dismutase NM 0004 147450 ALA145THR 1/SOD l (soluble) 54 Supero ide Dismutase NM 0004 147450 ALA4THR 1/SOD ! (soluble) 54 Superox ide Dismutase NM 0004 147450 ALA4VAL 1/SOD l (soluble) 54 Superoxide Dismutase NM 0004 147450 ASP90ALA 1/SOD l (soluble) 54 Supero ide Dismutase NM 0004 147450 CYS6PHE 1/SOD l (soluble) 54 Superoxide Dismutase NM 0004 147450 GLUIOOGLY 1/SODl (soluble) 54 Supcro . idc Dismutase NM 0004 147450 GLU21LYS 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY16SER 1/SODi (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY37ARG 1/SOD i (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY41ASP 1/SODi (soluble) 54 Superox ide Dismutase NM 0004 147450 GLY41SER 1/SODI (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY72SER 1/SODl (soluble) 54 Supero ide Dismutase NM 0004 147450 GLY85ARG 1/SODl (soluble) 54 Supcro -• ide Dismutase NM 0004 147450 GLY93ALA 1/SODl (soluble) 54 Supero .ide Dismutase NM 0004 147450 GLY93CYS 1/SOD 1 (soluble) 54 Supero ide Dismutase NM 0004 147450 HIS43ARG 1/SODI (soluble) 54 Sup. ro .ide Dismutase NM 0004 147450 HIS46ARG 1/SOD' (soluble) 54 Supero vide Dismutase NM 0004 147450 ILE104THE 1/SOD! (soluble) 54 Superoxide Dismutase NM 0004 147450 ILE113THR 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU106VAL 1/SODi (soluble) 54 Supi ro xicle Dismutase NM 0004 147450 LEU126TER SD- 114! !! Page 1270 1/SOD l (soluble) 54 Superoxide Dismutase NM_0004 147450 LEU144SER 1/SOD l (soluble) 54 Supero ide Dismutase NM_0004 147450 LEU38VAL 1/SOD i (soluble) 54 Superoxide Dismutase NM_0004 147450 LEU84VAL 1/SOD i (soluble) 54 Superoxide Dismutase NM_0004 147450 SER134ASN 1/SOD l (soluble) 54 Supero .ide Dismutase NM_0004 147450 THR151ILE 1/SOD 1 (soluble) 54 Sup< ro ide Dismutase NM_0004 147450 Val7->Glu 1/SOD i (soluble) 54 Su ei oxide dismutase X02317 147450 1 (Cu/Zn) Sup* roxide Dismutase X65965 147460 ALA16VAL 2/SOD2 (mitochondrial) I luman clone pSKl U05875 147569 Gln64Arg interferon gamma receptor accessory factor- 1 (AF-1) RN , complete cds M ICROTUBULE- J03778 157140 +39deltaG itron 4 ASSOCIATED i'ROTEIN TAU MICROTUBULE- J03778 157140 IVS10, A-G, +13 ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 rvsιo, c-u, +i4 ASSOCIATED SD- Page 1271 PROTEIN TAU M ICROTUBULE- J03778 157140 IVS10, C-U, +16 ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 IVS 10 , G-A, +1 ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 ARG406TRP ASSOCIATED PROTEIN TAU MICROTUBULE- J03778 157140 ASN279LYS ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 GLY272VAL ASSOCIATED PROTEIN TAU M ICROTUBULE- J03778 157140 PRO301LEU ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 SER305ASN ASSOCIATED PROTEIN TAU ICROTUBULE- J03778 157140 VAL337MET ASSOCIATED PROTEIN TAU nerve growth factor NM_0025 162010 Hindi rcceptor/NGFR 07 ncr . c growth factor NM_0025 162010 Hindlll i-eceptor/NGFR 07 nerve growth factor NM_0025 162010 Two Taql sites receptor/NGFR 07 SD- 1 !41 Page 1272 neiΛ e growth factor NM_0025 162010 Xmnl receptor/NGFR 07 1 [.sapiens encoding X64810 162150 IVS5DS, A-C, +4 PC1/PC3 1 [.sapiens encoding X64810 162150 GLY483ARG PC1/PC3 Tachykinin NK2 M57414 162321 none found rece tor/TACR2 Tachykinin NKl M81797 162323 none found receptor/TACRl Tachykinin NK3 M89473 162332 none found rece to ,'TACR3 neuromedin B ****** 162341 none found reccptor'g protein- coυpleci. NMBR Neuropeptide Y K01911 162640 LEU7PRO Neuropeptide Y M84755 162641 none found receptor Y1/NPY1R Neuropeptide Y U32500 162642 none found recepto-- Y2/NPY2R Neuropeptide Y X71635 162643 none found receptoi- Y3/chemokine recenior 4/CXCR4 Neurotensin receptor X70070 162651 Tetranucleotide * repeat 1 l uma n AD amyloid L08850 163890 Dinucleotide repeat 11V.IN A, complete cds Human AD amyloid L08850 163890 ALA30PRO m NA. complete cds 1 luman AD amyloid L08850 163890 ALA53THR in RNA. complete cds SD- 1 14 1 Human AD amyloid L08850 163890 G209A mRNA, complete cds Solute carrier family 6 , NM 0010 163970 none found member 43 5/S1.C6A2/NAT1/NET 1 (glycine) Human obese (ob) U18915 164160 -1387 G/A RNA, complete cds Human obese (ob) U18915 164160 1-BP DEL frameshift RNA, complete cds Human obese (ob) U18915 164160 A --> G + 19 exonl NA. complete cds Human obese (ob) U18915 164160 C(-188)A RNA, complete cds Human obese (ob) U18915 164160 ARG105TRP RNA. complete cds Human obese (ob) U18915 164160 Glu-126-Gln RNA, complete cds Human obese (ob) U18915 164160 Ser-91-Ser RNA, complete cds Opioid Receptor, U10504 165195 T to C in codon 307 silent Deli i- l ; Oprdl Opioid Receptor, U17298 165196 none found Kappa- 1 ; Oprkl Oxj tocin receptor X64878 167055 C to T exon 3 Oxy.ocin receptor X64878 167055 CA repeat Human peptidylglycine M37721 170270 none found al ha-amidating monooxygenase NA, complete cds Phenol-preferring NM 0010 171150 Arg213His SD- ' 1 141 Page 1274 sulfotransferase, family 55 1A, member 1/SULTl Al phenylethanolamine N- NM_0026 171190 BANI meti 1 yltransferase/PN 86 MT phospholipid transfer NM_0062 172425 TaqlB prot in/PLTP 27 Mctlienyltetrahydrofola J04031 172460 ARG293HIS te cyclohydrolase pro 1 act in NM_0009 176761 none found reccptor/PRLR 49 Adrenocorticotropic M28636 176830 3804C-A hormone (ACTH) . \drenocorticotropic M28636 176830 7013G-T hormone (ACTH) .Adrenocorticotropic M28636 176830 7133C DEL hormone (ACTH) i ylcholinesterase NM_0000 177400 209 A/G Asp-70 to Gly 1 /sci urn cholinesterase 55 1/BCHEl but) rylcholinesterase NM_0000 177400 342-bp Alu in exon Alu insertion 1/seι urn cholinesterase 55 two 1/BC HE 1 ylcholinesterase NM_0000 177400 A-to-G Y128C 1/seι nm cholinesterase 55 1/BCHE l but} rylcholinesterase NM_0000 177400 GCA to ACA ALA539THR 1/seι urn cholinesterase 55 1/BCHEl but} ■ ylch linesterase NM 0000 177400 GGT to GTT Gly 390 to Val SD- l 1414 1 1 Page 1275 1/se, uni cholinesterase 55 1/Bι HEl but) ' ylcholinesterase NM 0000 177400 GGT-to-GGAG Gly 117 1/scι um cholinesterase 55 Frameshift 1/BCHEl but) i ylcholinesterase NM 0000 177400 E451X 1/scrum cholinesterase 55 1/Bc HEl but} rylcholinesterase NM 0000 177400 F446V 1/scoιm cholinesterase 55 1/Bι HE l but) > ylcholinesterase NM 0000 177400 G365R 1/se mn cholinesterase 55 1/Bι. HEl but) i ylcholi esterase NM 0000 177400 GLU497VAL 1/scι um cholinesterase 55 1/BCHEl but) ylcholinesterase NM 0000 177400 Glyl l5 by Asp 1/se. um cholinesterase 55 1/B( HE l but) • ylcholinesterase NM 0000 177400 LEU330ILE 1/se um cholinesterase 55 1/B ( HEl but) ylcholinesterase NM 0000 177400 Q119X 1/scoim cholinesterase 55 1/BCHE l but) i ylcholinesterase NM 0000 177400 R515C 1/scι tin cholinesterase 55 1/Bt HE! but) i ylcholinesterase NM 0000 177400 THR243MET l/se> um cholinesterase 55 ' SD 14 1 1 Page 1276 1/B' HE l but) ■ ylcholinesterase NM 0000 177400 THR250PRO 1/scι iim cholinesterase 55 1/B' HE l but) rylcholinesterase NM 0000 177400 1/seι um cholinesterase 55 1/BCHEl butyi ylcholinestarase ****** 177500 none found 2/seι um cholinesterase 2/B( HE2 retinoic acid receptor M57707 180190 none found gaπ I ' RA RG ret in ύc acid receptor NM 0009 180220 none found bet., RARB 65 retin acid receptor NM 0009 180240 7 -base deletion frameshift alp ./RARA 64 retinoic acid receptor NM 0009 180240 codon 411 C to T retinoic acid receptor NM 0009 180240 Arg272Gln alpha/RΛRA 64 retir ic acid receptor NM 0009 180240 Met297Leu alpl . t/RΛR Λ- 64 retii oid X receptor NM 0029 180245 none found alpl .' RXRA 57 ret moid \ receptor X66424 180246 none found beta RXRB reti i -id X receptor U38480 180247 none found gamma/RXRG serotonin 5-HT M81590 182131 C129T receptors 5-HT1B, G protein-coupled SD- ■ 141 Page 1277 oo -o ' Ξ & o CN V. g <o -I-. r--. o υ Ό s T3 e U 3 -3 a & 3 C, .2 -2 o H CN ϋ oo ω to m co e fi c o o o S3 c c — — ( CN rn → in W-ϊ r- oo oo oo co rn ro ro ro ro ro ro rn m — — ( * —- -- * CN CN CN CN CN CN CN CN CN CN oo oo oo 00 oo oo oo 00 00 Q o to 1 the promoter sen -onin transporter X70697 182138 two polyadenylation sites ser 'onin transporter X70697 182138 VNTR intron 2 sen -onin transporter X70697 182138 silent polymoφhism serotonin 5-HT D49394 182139 none found rec c ; ι tors vlIT3, gated ion hannel type 1 voltage S71446 182389 none found dep. ndent sodium channel alpha subunit/SCNlA type 11 voltage M94055 182390 none found depi ndeni sodium channel alpha 1 sub ιit/SCN2Al type HI voltage S69887 182391 none found dep I idem sodium channel alpha sub. ,nit/SCN3A typt- VI \ ullage M55662 182392 none found dep ' ndent sodium cha. -ncl alpha subui .it/SCN6A Son -atostatin receptor M81829 182451 (CA)n 5* 1/G prolein-coupled Somatostatin receptor 2 M81830 182452 TRP188TER Son iatostatin receptor M96738 182453 none found 3/ti' I 'iiyl \ clase cou. i led SD- 1 114 1 Page 1279 Son ito tatin receptor 4 L07833 182454 none found Son itostalin receptor 5 D16827 182455 2 RFLP's promoter i lum in rapamycin- M65128 186946 none found bim ! > ng pι otein (FKBp- 1 ' j m NA, complete cds thyi )tιopιn releasing X75071 188545 9-BP DEL deletion of 3 hoi i -one i cceptor/G amino acids pro. in coupled/TRHR thyi iiro releasing X75071 188545 ALA118THR hoi, on icceptor/G proi in coupled/TRHR thyi ui opm releasing X75071 188545 ARG171TER hori one i cceptor/G proi in coupled TRHR oncogene NM 0019 190151 none found LRBB3/HER3 82 tryp opl n X52836 191060 -5806OT tryp' ophan X52836 191060 -6526A>G Hyc ixNise, TPH tryp iphan X52836 191060 -7065OT try), iphan X52836 191060 7180T>G try j v pl n X52836 191060 A218C in intron 7 try t φhan X52836 191060 A779C tryp ι)pha.. X52836 191060 A779C in intron 7 tryptoph. - X52836 191060 T1095C Hydroxy ,se, i PH Human l' \ ptophan U32989 191070 6G~>T intron ox λ ena c (TDO) mRNA complete cds Human ti vptophan U32989 191070 CCCCT repeat m-RN-Λ complete cds Hui in ptophan U32989 191070 GTT repeat ox ' ona-e (TDO) mRNA complete cds tyrosine 1 ' ydi xylase X05290 191290 (TCAT)n intron 1 tyrosine 1 ydi ovylase X05290 191290 Bglll tyrosine ' i vdi vylase X05290 191290 Dral tyrosine I - yd xylase X05290 191290 Pstl tyrosine ! 1 ydmxylase X05290 191290 Seal tyrosine i ivdioxylase X05290 191290 T-229A tyrosine 1 l yd' xylase X05290 191290 [AATG]n tyrosine ' . vdi oxylase X05290 191290 ARG233HIS tyrosine i vdioxylase X05290 191290 GLN381LYS tyrosine i vdi ovylase X05290 191290 LEU205PRO tyrosine dmxylase X05290 191290 Val468Met tyrosine ydi xylase X05290 191290 ValδlMet neurol >phκ tyrosine Y09033 191315 1-BP DEL, 1726C frameshift kinas ια . ,Uor type ! NTRK1 neurol i φ ic tyrosine Y09033 191315 1810OT kinas ιeu ptor type 1 'NTRK1 neurol i >phιc tyrosine Y09033 191315 1838G>T kinas, ι c< ι olor type SD-14414 Page 1281 1/NTRKl neurotrophic tyrosine Y09033 191315 G1795C GLY571ARG kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 IVS4, G-C, -1 kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 IVSDS, A-C, +3 kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 ARG774PRO kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 ARG85SER] kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 GLN9TER kinase receptor type 1/NTRKl neurolrophic tyrosine Y09033 191315 GLY607VAL kinase receptor type 1/NTRKl neurotrophic tyrosine Y09033 191315 HIS598TYR kinase receptor type 1/NTRKl neurotrophic tyrosine NM_0025 191316 none found kinase receptor type 30 3/NTRK3 vasoactive intestinal 192321 none found peptide receptor 1/VIPR1 SD-144141 Page 1282 Vesicular Amine L09118 193001 Taql Transporter 2; VAT2 Vesicular Amine ****** 193002 none found Transporter 1; VAT1 melanocortin 2 NM 0005 202200 1-BP INS frameshift receptor/ACTH 29 receptor/MC2R melanocortin 2 NM 0005 202200 ARG128CYS receptor/ACTH 29 receptor/MC2R melanocortin 2 NM 0005 202200 ARG201TER receptor/ACTH 29 reccptor/MC2R melanocortin 2 NM 0005 202200 ASP 107 ASN receptor/ACTH 29 reccptor/MC2R melanocortin 2 NM 0005 202200 CYS251PHE receptor/ACTH 29 receptor/MC2R melanocortin 2 NM 0005 202200 SER120ARG receptor/ACTH 29 receptor/MC2R melanocortin 2 NM 0005 202200 SER74ILE receptor/ACTH 29 receptor/MC2R dopamine beta Y00096 223360 hydroxylase glutamate ****** 229100 none found form i mi notransferase/d ihyd ofolate synthetase 5,10- U09806 236250 1027T-G SD- U41 Page 1283 @METHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 1084C-T @METHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 1298A-C @METHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 1711C-T @M ET1 IYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 677C-T ala --> val @M 1 < T11YLENETET RAHYDROFOLATE R EDUCTASE 5,10- U09806 236250 983A-G @ ETHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 exon 7 Aia~>Glu @METHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 A225V @MbTHYLENETET RAHYDROFOLATE REDUCTASE SD- 1 1414 1 Page 1284 5,10- U09806 236250 ARG158GLN @METHYLENETET RAHYDROFOLATE REDUCTASE 5,10- U09806 236250 ARG184TER @METHYLENETET RAHYDROFOLATE REDUCTASE Glycine cleavage D13811 238310 1-BP DEL, 183C system: Protein T Glycine cleavage D13811 238310 ASP276HIS system: Protein T Glycine cleavage D13811 238310 GLY269ASP system: Protein T Glycine cleavage D13811 238310 GLY47ARG system: Protein T Glycine cleavage D13811 238310 HIS42ARG system: Protein T 6-pyruvoyl Q03393 261640 14-BP DEL K120->Stop letrahydrobiopterin nthase/PTPS 6-pyruvoyl Q03393 261640 ARG16CYS synthase/PTPS 6-pyruvoyl Q03393 261640 ARG25GLN letrahydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 ASN47ASP t etral . ydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 ASN52SER SD-14 J 141 Page 1285 letrahydrobiopterin synthase PTPS 6-pyruvoyl Q03393 261640 ASP116GLY t ctrah ydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 ASP96ASN tetrah ydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 D136V tetrah ydrobiopterin svnthase/PTPS 6-pyruvoyl Q03393 261640 K129E tetrah ydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 PRO87SER tetrah ydrobiopterin synthase/PTPS 6-pyruvoyl Q03393 261640 T67M tetrah ydrobiopterin s> nthase/PTPS 6-pyruvoyl Q03393 261640 VAL56MET tetrah, ydrobiopterin s> nthase/PTPS Glutamate M81883 266100 none found decarboxx lase 1 (brain, 67kD) Human hydroxyindole- U11090 300015 none found 0-methyltransferase promoter A-derived (I llOMT) mRNA, complete cds SD- 14414 1 Page 1286 oo a o VO O so VO VO CO CN i - CN CN CN CN CN CN CN CN r- o O o σs O vθ O VO VO VO VO CN o IΛ r- c-~ Os O O O o O O o — — < 1 VO Os CN oo ro ro ro ro ro ro ro ro O o O O O O O O O o § < 1 ID 53 Ϊ3 5. % 53 53 receptor 2 Arginine \ isopressin AF030626 304800 ALA132ASP receptor 2 Arginine \ asopressin AF030626 304800 ARG181CYS receptor 2 Arginine \ isopressin AF030626 304800 ARG113TRP receptor 2 Arginine isopressin AF030626 304800 ARG203CYS receptor 2 Arginine \ isopressin AF030626 304800 ARG337TER receptor 2 Arginine \ isopressin AF030626 304800 ASP85ASN receptor 2 Arginine \ isopressin AF030626 304800 G107E receptoi 2 Arginine \ isopressin AF030626 304800 GLY185CYS receptor 2 Arginine \ isopressin AF030626 304800 GLY201ASP receptoi- 2 Arginine \ isopressin AF030626 304800 L43P receptor 2 Arginine \ isopressin AF030626 304800 P322H receptor 2 Arginine \ isopressin AF030626 304800 P322S receptor 2 Arg'iiinc \ isopressin AF030626 304800 R137H receptor 2 Arginine \ isopressin AF030626 304800 TRP71TER receptor 2 Arginine \ isopressin AF030626 304800 TYR205CYS receptor 2 SD- i ,-i Page 1288 Arginine vasopressin AF030626 304800 TYR280CYS receptor 2 Arginine vasopressin AF030626 304800 W193X receptor 2 Gamma-Aminobutyric S62908 305660 16-repeat allele Acid Receptor, Alpha- 3; Gabra3 Gamma-Aminobutyric S62908 305660 Dinucleotide repeat Acid Receptor, Alpha- 3; Gabra3 gastrin-releasing D87058 305670 two single polypeptide receptor/G nucleotide protei, , - coupled/GRPR substitutions in exon 2 Glutamate Receptor, X82068 305915 none found Ionotropic, Ampa 3; Gria Glycine Receptor, X52008 305990 none found Alpha--- Subunit; Glra2 Monoamine Oxidase M69226 309850 23-bp VNTR A; MAO A Monoamine Oxidase M69226 309850 3rd base of codon 941 A; M O A 941 G>T Monoamine Oxidase M69226 309850 A1026T ProlineProline A; MAOΛ Monoamine Oxidase M69226 309850 A1559G Lysine Arginine A; rvlAOΛ Monoamine Oxidase M69226 309850 A385C Arginine Arginin A; MAOΛ e Monoamine Oxidase M69226 309850 C1410T Aspartic A; MAO A AcidAspartic SD- 1 '-I I Page 1289 Acid Monoamine Oxidase M69226 309850 C886T Gluta ine296T A; MAO ' ermination codon Monoamine Oxidase M69226 309850 C886T GlutamineTermi A; MAO A nation codon Monoamine Oxidase M69226 309850 exon 14 ~ RFLP A; MAOΛ (EcoRV enzyme) Monoamine Oxidase M69226 309850 length of (CA)n A; MAOΛ repeat Monoamine Oxidase M69226 309850 RFLP (EcoRV A;M OΛ enzyme) Mono., mine Oxidase M69226 309850 RFLP (Pst I) A; MΛO . Monoamine Oxidase M69226 309850 T891G ArginineArginin Monoamine Oxidase M69226 309850 T891G A; MΛOΛ Moiioanime Oxidase M69177 309860 (GT)n repeat B;MA 13 Mono -mine Oxidase M69177 309860 36 bases upstream B; M \OF! from intron 13-exon 14 boundary Monoamine Oxidase M69177 309860 A at position 644 of B; MΛOi- intron 13 Mono -mine Oxidase M69177 309860 G at position 644 of B; Λ l > , intron 13 Monoamine Oxidase M69177 309860 RFLP (Maelll B;MΛOB enzyme) seioton.n -HT U49516 312861 2831T>Ginthe3' receptor S-HT1C.G SD-i '-mi Page 1290 prole in- coupled seroionin 5-HT U49516 312861 CYS23SER receptors -HT1C. G prolein-co ipled and) >gen receptor M20132 313700 Hind III andi >gen receptor M20132 313700 (CAA)n andr .gen receptor M20132 313700 (CAG)n and gen receptor M20132 313700 (GGN)n andr ■ >gen receptor M20132 313700 5-KB DEL, EX F,G andi igen receptor M20132 313700 5-KB DEL,EX E andi )gen receptor M20132 313700 C>T within exon B silent andi i en receptor M20132 313700 CAG340TAG Gln>Ter andi 'gen receptor M20132 313700 Del T at 3286 frameshift andi 'gen receptor M20132 313700 dell 893 frameshift andi i en receptor M20132 313700 G Codon 210 A andi )gen receptor M20132 313700 G Codon 211 A andi )gen receptor M20132 313700 G2314A ala thr andr l en receptor M20132 313700 G2677A glu629arg ane!10gen receptor M20132 313700 Hhal andi )gen receptor M20132 313700 Hpall ancii )gen receptor M20132 313700 Insert of 69 nucleotides nc-ti )gen receptor M20132 313700 Maelll andr igen receptor M20132 313700 PARTIAL DEL >gen receptor M20132 313700 Stu l igen receptor M20132 313700 598 or 599 ter 1: 1 I I gen receptor M20132 313700 ALA721THR mdi )gen receptor M20132 313700 ALA771THR inch )gen receptor M20132 313700 ARG607GLN n ull ■ gen receptor M20132 313700 ARG608LYS null igen receptor M20132 313700 Arg615His SD- t -μ i i i < Page 1291 and 10 en receptor M20132 313700 arg7261eu andi ogen receptor M20132 313700 Arg752Gln andi ogen receptor M20132 313700 ARG772CYS andi ogen receptor M20132 313700 ARG773CYS andi ogen receptor M20132 313700 ARG773HIS andi ogen receptor M20132 313700 ARG839CYS andi ogen receptor M20132 313700 ARG839HIS andi ogen receptor M20132 313700 arg840his andi ogen receptor M20132 313700 ARG846HIS andi ogen receptor M20132 313700 ARG855HIS andi ogen receptor M20132 313700 CYS579PHE andi ogen receptor M20132 313700 G214R 1 i 1 ogen receptor M20132 313700 GLN60TER an n ogen receptor M20132 313700 Gln798Glu ικ ! Ogen receptor M20132 313700 GLN902ARG andi gen receptor M20132 313700 GLU2LYS andi ogen receptor M20132 313700 gly743val andi ogen receptor M20132 313700 HIS874TYR an i gen receptor M20132 313700 ILE869MET andi ogen receptor M20132 313700 LEU172TER andi ogen receptor M20132 313700 LEU676PRO andi ogen receptor M20132 313700 LEU707ARG iin li ogen receptor M20132 313700 LYS588TER an i gen receptor M20132 313700 LYS882TER an i ogen receptor M20132 313700 MET780ILE aa ii ' Ogen receptor M20132 313700 MET786VAL and! igen receptor M20132 313700 PHE582TYR andi ogen receptor M20132 313700 PRO546SER andi ogen receptor M20132 313700 pro892ser andi ogen receptor M20132 313700 SER647ASN an di ogen receptor M20132 313700 THR877ALA SD- 1 1 I Page 1292 androgen receptor M20132 313700 THR877SER androgen receptor M20132 313700 TRP717TER andi ogen receptor M20132 313700 TRP794TER andi ogen receptor M20132 313700 TYR761CYS andi ogen receptor M20132 313700 val 581 phe androgen receptor M20132 313700 VAL730MET androgen receptor M20132 313700 VAL865LEU androgen receptor M20132 313700 VAL865MET androgen receptor M20132 313700 VAL866MET AC1-.1 Y I SEROTONI 402500 none found N ME I ' 1 I ' RANSFER ASE, Y- Cl l l OMOSOMAL voltage dependent U07139 600003 none found calcium channel beta 2 subunit," WCNB2 vasculai angiotensin II NM 0048 600015 none found reccpior ι \ pe 35 1B/AG I 1 B Opi id i ' eeeptor, Mu- NM 0009 600018 (CA)n 1 ; Opπu 1 14 Opioid I'eeeptor, Mu- NM 0009 600018 Asn40Asp 1; Oprn, 1 14 P2Y2 purinoceptor/G U07225 600041 none found protein-c oupled Solute Carrier Family U03504 600111 none found 1, Member 3; Slcla3 type V \ υkage NM 0003 600163 1-BP DEL frameshift depen ent sodium 35 channel dplia SD- Page 1293 subunit' SCN5A type V \ oltage NM_0003 600163 2-BP INS dependent sodium 35 channel alpha subiini .- --.NN5A type V voltage NM_0003 600163 dependent sodium 35 LYS1505/PRO1 channel alpha 506/GLN1507D subui.it/SCN5A EL type V \ ollage NM_0003 600163 ARG1232TRP dependent sodium 35 channel ,lpha subunit/ SCN5A type V \ ol lage NM_0003 600163 ARG1623GLN depe nd -nt sodium 35 channel alpha subunit S N5A type V \ oltage NM_0003 600163 ARG1644HIS] dependent sodium 35 channel ilpha subunit/ ,(- ' N5A type V \ diage NM_0003 600163 GLU1784LYS de])' n k i sodium 35 channel npha subunit \CN5A type V \' iliage NM_0003 600163 THR1620MET dependent sodium 35 channel alpha subunit/ »CN5A Histamine receptor HI AF026261 600167 none found Gamma- \minobutyric S77553 600232 none found SD- Page 1294 Acid Receptor, Beta-2; Gabrb2 Gamma 08 600233 none found Acid Recepto r.Gamma-3; Gabrg3 type 1 voltage NM_0010 600235 CYS121TRP dependent sodium 37 channel beta subunit'SCNlB Arginine Vasopressin AF030512 600264 none found Receptor I B/AVPR1B Glu.amaie Receptor, S67803 600282 none found Ionotropic. Kainate 4; Gri Gluuim-.ie Receptor, S40369 600283 none found Ionotro ic, Kainate 5; Gril Solute ( " airier Family U03505 600300 none found 1, Member 2; Slcla2 Vesicula acetylcholine NM 0030 600336 none found transpo' ϊer 55 bradykinin receptor NM 0007 600337 9-base pair deletion Bl/! i i<13l G 10 prolein-. oupled brad ykir, ui receptor NM 0007 600337 A1098->G Bl'HDKUl G 10 protei - oupled bradykinin receptor NM 0007 600337 C181->T Bl/BDKRBl G 10 protein-coupled SD- Page 1295 bradykinin receptor NM 0007 600337 G-699->C Bl/BDK RB l G 10 protein-, oupled Glycine Receptor, AF018157 600421 none found Alpha-3 Subunit; Glra3 Adenosine A3 L20463 600445 none found Receptor: Adora3/G protein-coupled Adenosine Λ2b X68487 600446 none found Receptoi - Λdora2b/G protein- upled lcairoi i ophic tyrosine NM 0061 600456 none found kinace receptor type 80 2/NTRK2 inw rclb, rectifying NM 0049 600504 none found potassium channel, 81 .1 , member recliirR i- ' l N NM 0050 600514 none found 45 Human iininunophilin M88279 600611 none found XV BI > 52) mRNA, complete cds opioid b ".ding cell ****** 600632 none found adh ■ - ιθι molecϋi. OBCAM Solute c -men' family 1, NM 0050 600637 none found member (. 71 (GΛL-A GI U)/SLC1A 6 Human aryl L19956 600641 none found SD- Page 1296 sulfotransferase NA. complete cds MELATONIN 600665 A157V RECEPTOR 1 A MELATONIN 600665 R54W RECEPTOR 1A inv- rdh rectifying NM 0008 600681 C~>T silent potassium channel, 91 sublainilv .1, member 2/KCN.π-HHIRKl type VI 11 voltage sf: :f: - - % 600702 none found dep> ndeu! sodium channel alpha subunit -t- 8A G pi lα '.-coupled U22491 600730 none found G ]) otei i coupled U22492 600731 none found pre cnilin 2 NM 0004 600759 exon 3 47 pre enihn 2 NM 0004 600759 ASN141ILE 47 pre ι en i I,, i 2 NM 0004 600759 MET239VAL 47 V1 LATONIN 600804 none found 1 l-.CEPTORlB Ars'inin. \'asopressin AF030625 600821 none found Recepto 1Λ/AVPR1A R R red iied o han NM 0029 600825 none found receptoi v'RORA 43 Pui crgic Receptor Y07683 600843 none found SD-. I 11 Page 1297 oo > ao 03 lep 1 n u eptor/LEPR NM 0023 601007 K109R 03 lepn n re .eptor/LEPR NM 0023 601007 K656N 03 lep i n ie • eptor/LEPR NM 0023 601007 Lys 109 Arg 03 leptin K eptor/LEPR NM 0023 601007 Lys656Asn 03 lep t i n n eptor/LEPR NM 0023 601007 Prol019Pro 03 lep i in n - ptor/LEPR NM 0023 601007 Ser343Ser 03 lep, n ' i .ptor/LEPR NM 0023 601007 Ser492Thr 03 Sol ute c ii ner family 6, S70612 601019 none found Mcuibc l > SLC6A9 (gh enu sen (on i n 5-HT L41147 601109 C267T prυ' eiπ- aipled Ghi am e Receptor, X77748 601115 none found proiein- ' oιιpled/Grm3 Glu am ■ e Receptor, U95025 601116 none found proi ein . oupled/Gππδ Thi met ( • l igopeptidase Z50115 601117 none found sen loin i HT X77307 601122 none found proi ein-v. oupled SD Page 1299 © © ro 00 1/1< N l 1 vit. iiin » NM 0003 601769 A(T/C)G putative rec >u, \ DR 76 translation start site vit, mn ! ) NM 0003 601769 Apal rec no, \ DR 76 vita nm D NM 0003 601769 Xbal vita nil i NM 0003 601769 ARG-GLY vita mn D NM 0003 601769 ARG391CYS re DI I \ DR 76 vit; nin ) NM 0003 601769 HIS305GLN rec phe \ DR 76 vit. ιin D NM 0003 601769 ILE314SER rec ,)k V DR 76 vita iii , - NM 0003 601769 ARG271LEU rec cto \ DR 76 vita nin ■ NM 0003 601769 ARG30TER rec to V DR 76 vita nil D NM 0003 601769 ARG47GLN rec plot V DR 76 vit; n in ) NM 0003 601769 ARG77GLN SD Page 1301 vita nil 1 1 ) NM 0003 601769 codon 352 vit, nin J NM 0003 601769 GLN149TER rec old \ DR 76 vita uiir D NM 0003 601769 GLY30ASP rec. pto: \ DR 76 vit, lip D NM 0003 601769 TYR292TER rec pto ^DR 76 Nc, mp ntideY D86519 601770 none found vol ice .dependent NM 0010 601784 none found cha ne! ΛCCNl vob 1^1 lependent ****** 601949 none found cab [111, . Iiannel beta 4 sub nil ΛCNB4 vob ly dependent 601958 none found cal can hannel beta 3 NM 0007 sub mil ■ ACNB3 25 va ,aι i e intestinal L40764 601970 none found pei a • i eptor 2Λ ,'! RN .ted o han ****** 601972 none found rec illc, !.,RORB Op .iii ■ ec eptor, U75283 601978 Gln2Pro SI) Page 1302 ro © ro 00 c- CU i—i ■ ---" C--T. O © f ro 00 CN uo O O ro v-o r- --H vo ON o ro ro ro O O O O — i CN CN CN CN CN CN CN CN CN CN CN CN CN CN CN o o o o o O o O o O O O o eo vo VO o VO VO VO δ r ° j o δ fc CD y o ι_ V--J j-3 c -- KC 1 -III - subfamily, NM 0002 602235 ALA306THR pol -Si' n channel, 18 KC l -l I e subfamily, mc ibe VKCNQ2 An ne \ idase D88213 602268 none found (co P < - containing) 2// )( Gli Ul' 1 e Receptor, AF009014 602368 none found Ion tlυ c, Delta 2; Gn 1? P2 6,, i imidinergic NM 0041 602451 none found rec ,t< ' G protein- 54 opi 'd 1 i eptor-like X77130 602548 none found 1/C X i Pll! ne, Receptor Y09561 602566 none found P2 1 i nd-Gated Ion Ch UK 7; P2rx7 Hi l-.l N<-506-binding U71321 602623 none found i ιoteinFKBP51 1 V, complete cds P2 11 nirinoceptor/G ****** 602697 none found pre mi oupled Gli 1 am le Receptor, U77783 602717 none found Ion llu i ic, N-Methyl- Page 1304 SD It' 11 -o © ro 0) c-o Os O O VO en VO CN 00 00 ro ro r» vo r~ o O oo 00 Os Os Os CN N CN CN CN CN CN CN CN © o o © o O O V VO o VO VO vo VO VO VO Q 00 o ro < .a J E Sβ tΛ E ^ 00 CΛ — X c .. o ..-- o e e " is B O "5 r O 0 " 5 \ 0 Q > O " _j ~ O S " 3 CO CN > CO CO > Cu co ^ Λ C Λ 0 th\ , oid i imulating NM 0003 603372 2 bases deleted of hoi uoi , receptor 69 codon 655 th> ■ oici t imulating NM 0003 603372 C253A hoi non • receptor 69 th) oici limulatmg NM 0003 603372 duplication of hoi non receptor 69 nucleotides -346 to - th) oid simulating NM 0003 603372 G to C +3 i hoi uoi receptor 69 th\ ic' ! imulating NM 0003 603372 G-A -4 intron hoi ' iron - receptor 69 th) oid '.imulating NM 0003 603372 Taql hoi non receptor 69 th) oic, l imulating NM 0003 603372 CYS41SER hoi uoi • receptor 69 th) oid Simulating NM 0003 603372 LEU629PHE hoi .101 receptor 69 th) ' oic! (imulating NM 0003 603372 SER505ASN hoi ,10 receptor 69 th) oid t imulating NM 0003 603372 ALA553THR hoi non ■ receptor 69 th) i oid i imulating NM 0003 603372 ALA623ILE hoi no receptor 69 th) oic! (imulating NM 0003 603372 alanine 623 to hoi no, receptor 69 valine oid imulating NM 0003 603372 ARG109GLN ho 1 no receptor 69 th) oid simulating NM 0003 603372 Asn715Asp hoi no , e receptor 69 th) oic t imulating NM 0003 603372 Asρ219Glu hoi 10 receptor 69 SD 14 Page 1307 th) oid - .i imulating NM 0003 603372 ASP36HIS ho" mon receptor 69 th: oid I imulating NM 0003 603372 ASP410ASN ho, o , receptor 69 th) oid t imulating NM 0003 603372 ASP619GLY hoi mon, - receptor 69 th) , oid i imulating NM 0003 603372 ASP633HIS hoi l lO l i i receptor 69 th) oid I imulating NM 0003 603372 asp727glu ho i ne receptor 69 «N oui 1 imulating NM 0003 603372 Asp727Glu ho, non. . receptor 69 th oid t imulating NM 0003 603372 CAG he no; , receptor 69 [Glu]227CAT [His] th: -.id 1 imulating NM 0003 603372 CYS390TRP hoi UO ' receptor 69 th\ Old simulating NM 0003 603372 CYS672TYR ho, no. receptor 69 th\ oid l imulating NM 0003 603372 GCG ho no i receptor 69 [Ala]460GCA [Ala] tlr oid (imulating NM 0003 603372 GGT[Arg]201C he non receptor 69 AT [His] th: ici i imulating NM 0003 603372 GLN324TER hoi , 10 receptor 69 th) ok' limulatmg NM 0003 603372 ILE167ASN hoi no I , -- receptor 69 th) oid l imulating NM 0003 603372 leu677val hoi receptor 69 th) on! l imulating NM 0003 603372 LYS 183 ARG SU H i I I Page 1308 hoi noi , receptor 69 th: OK 1 Simulating NM 0003 603372 Lys723 Met hoi no. i . receptor 69 th) oid Simulating NM 0003 603372 MET453THR hoi moi i receptor 69 th) oic' timulating NM 0003 603372 P52T hoi oi . receptor 69 thy oid timulating NM 0003 603372 Phel97Ile hoi non v receptor 69 thy oici timulating NM 0003 603372 PHE525LEU hoi not receptor 69 oid timulating NM 0003 603372 PHE631LEU hoi noi receptor 69 oid timulating NM 0003 603372 PRO162ALA hoi noi receptor 69 th; on! -timulating NM 0003 603372 SER281ASN hoi noi i receptor 69 th\ OK 1 1 imulating NM 0003 603372 SER281ILE hoi n ' receptor 69 >ιd (imulating NM 0003 603372 TRP546TER hoi ' i receptor 69 th) oid .timulating NM 0003 603372 VAL509ALA hoi IO i - receptor 69 tyr ^ oltage NM 0029 603415 none found d i in 1 nt sodium 77 ch. m 1 , alpha hoi IOIO -- of Drosophila AF071062 603448 none found dis hX i D-A-B l Ga urv ! Aminobutyric Y1 1044 603540 none found Ac 1 1 . i .eceptor 1 ; SD Page 1309 60 ca Pu σs n f » oo m t^ r- ~ t-> r~ r» t-~ m cn oo oo cn o θ VO VO VO vθ v V f- r~ oo σs Λ σ\ σs σs σs σs OS ro m rn m ro m C m cn rn m m © © © © © © O o © © © © VO o VO VO VO θ VO VO VO U CΛ subunit/SCN4A sodium channel alpha- U24693 603967 ILE 1 160V AL subunit/SCN4A sodium channel alpha- U24693 603967 LEU1433ARG subunit/SCN4A sodium channel alpha- U24693 603967 MET1592VAL subunit/SCN4A sodium channel alpha- U24693 603967 SER804PHE subunit/SCN4A sodium channel alpha- U24693 603967 THR1313MET subunit/SCN4A sodium channel alpha- U24693 603967 THR704MET subunit/SCN4A sodium channel alpha- U24693 603967 VAL1293ILE subunit/SCN4A sodium channel alpha- U24693 603967 VAL1589MET subunit/SCN4A sodium channel alpha- U24693 603967 VAL445MET subunit/SCN4A Glutamate Receptor, U82083 604096 none found Metabotropic 6/G protein-coupled/Grmό Glutamate Receptor, L35318 604099 none found Metabotropic 2/G protein-coupled/ Grm2 Glutamate Receptor, X80818 604100 none found Metabotropic 4/G protein-coupled/Grm4 Glutamate Receptor, X94552 604101 none found Metabotropic 7/G protein-coup led/Grm 7 SD-144141.1 Page 131 Glutamate Receptor, D28538 604102 none found Metabotropic 5/G protein-coup leαVGrm5 dihydrofolate reductase J00140 126060 2 RFLP's dihydrofolate reductase J00140 126060 intronic polymoφhism FKBP, tacrolimus M34539 186945 none found binding protein, FK506-binding protein 1 (12kD) Cyclooxygenase 1 M59979 176805 none found COX1 Cyclooxygenase 2 M90100 600262 none found COX2 beta-synuclein [human, S69965 602569 none found brain, mRNA, 730 nt] histamine N- A939G methyltransferase histamine N- Thrl05Ile methyltransferase Table 20. Identified Variances in Genes or Related Pathways involved in the Pharmcokinetics and Pharmacodynamics of Candidate Therapeutic Interventions 3'(2'), 5'-bisphosphate 604053 NM_00608 none found SD-144141.1 Page 131 nucleotidase 1/BPNT 5 Acetylcho 1 inesterase/ A 100740 M55040 1431 C/T 446 silent CHE Acetylcholinesterase/A 100740 M55040 408 G/C arg561pro CHE Acetylcholinesterase/A 100740 M55040 HIS322ASN CHE acyl-Coenzyme A none found dehydrogenase, C-4 to C-12 straight chain/ACADM (mitochondrial) ALCOHOL 103700 none found DEHYDROGENASE 1 aldehyde 100650 K03001 GLU487LYS dehydrogenase 2/ALDH2 (liver mitochondria) aldehyde 100650 K03001 A-361G dehydrogenase 2/ALDH2 (liver mitochondria) aldehyde 100650 K03001 -357 G/A dehydrogenase 2/ALDH2 (liver mitochondria) ALDEHYDE 100670 C183T silent DEHYDROGENASE 5 ALDEHYDE 100670 C257T VaK~>Ala SD-144141.1 Page 131 5 ALDEHYDE 100670 T320G Arg<->Leu DEHYDROGENASE 5 ALDO-KETO 600449 none found REDUCTASE FAMILY 1, MEMBER 1 ; AKR1C1 ALDO-KETO 103830 none found REDUCTASE FAMILY 1 , MEMBER Al ; AKR1A1 ALDO-KETO 603966 none found REDUCTASE FAMILY 1, MEMBER C3 Aldo-keto reductase 600451 ****** none found family 1 , member C4/chlorodecone reductase/AKRlC4 Aldo-keto reductase 603418 NM 00368 none found family 7, member 9 A2/aflatoxin aldehyde reductase/AKR7A2 anthracylcline 603234 NM 00117 none found resistance-related 1 protein/ ARA antigen peptide 170260 NM 00059 ILE333VAL transporter 1/MHC 3 1/TAPl SD-144141.1 Page 131 antigen peptide 170260 NM 00059 ASP637GLY transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 ARG659GLN transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 val- leucine transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 silent glycine transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 silent glutamic acid transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 silent alanine transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 GTC-->ATC Val518Ile transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 G~>T promoter transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 10-bp insert intron 9 transporter 1/MHC 3 1/TAPl antigen peptide 170260 NM 00059 G->T 80-bp 3' transporter 1/MHC 3 termination codon 1/TAPl antigen peptide 170260 NM_00059 dinucleotide repeat SD-144141. Page 131 transporter 1/MHC intron 3 1/TAPl antigen peptide 170261 NM 00054 ILE379VAL transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM_ 00054 ALA665THR transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM_ 00054 GLN687TER transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 Thr374Ala transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 ACG to ACA 458Thr transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 GGG to GGA 466Gly transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 GTT to ATT 467Val-Ile transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 ATG->GTG Met577Val transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM 00054 565 (Ala-Thr) transporter 2/MHC 4 2/TAP2 antigen peptide 170261 NM . 00054 silent codon 386 transporter 2/MHC 4 SD-144141 , 1 Page 131 2/TAP2 Aromatic L-Amino 107930 M76180 Sspl Acid Decarboxylase/ AADC/ dopa decarboxylase Aryl hydrocarbon 602550 NM 00117 none found receptor nuclear translocator- like/ARNTL Aryl hydrocarbon 126110 NM_ 00166 Mspl receptor nuclear 8 translocator/ARNT Aryl hydrocarbon 600253 NM . 00162 none found receptor/AHR 1 Arylsulfatase A/steroid 250100 NM . 00048 A-to-G transition sulfatase/ARSA 7 changed the first polyadenylation Arylsulfatase A/steroid 250100 NM . 00048 ARG350SER sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM_ 00048 IVS2DS, G-A, +1 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM . 00048 PRO426LEU sulfatase/ARSA ' l Arylsulfatase A/steroid 250100 NM . 00048 GLY99ASP sulfatase/ARSA ~ 7 Arylsulfatase A/steroid 250100 NM . 00048 SER96PH sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM_ 00048 11-BP DEL, EX8 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 1LE-TO-SER, sulfatase/ARSA EX3 SD-144141.1 Page 131 Arylsulfatase A/steroid 250100 NM 00048 IVS7DS, G-A, +1 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG84GLN sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLY309SER sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 -BP DEL FS105TER sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLY86ASP sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 SER96LEU sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLY122SER sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PRO136LEU sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 1-BP DEL, 297C sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLY154ASP sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PRO155ARG sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PRO 167 ARG sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ASP169ASN sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ALA212VAL sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ALA224VAL sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PRO231THR SD-144141.1 Page 131 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG244CYS sulfatase/ARSA 7 Arylsulfatase -A/steroid 250100 NM 00048 GLY245ARG sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 THR274MET sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 IVS4DS, G-A, +1 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG288CYS sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 SER295TYR sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLY325CYS sulfatase/ARSA 7 Arylsulfatase -A/steroid 250100 NM 00048 ASP335VAL sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG370TRP sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG370GLN sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PRO377LEU sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 GLU382LYS sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 ARG390TRP sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 PHE398DEL sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 THR409ILE sulfatase/ARSA 7 SD-144141.1 Page 1 1 Arylsulfatase A/steroid 250100 NM 00048 GLN486TER sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 THR799GLY sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 P148L sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM_00048 R496H sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 N350S sulfatase/ARSA 7 Arylsulfatase -A/steroid 250100 NM_00048 9-bp deletion sulfatase/ARSA 7 (2320del9) Arylsulfatase A/steroid 250100 NM 00048 Nlallll sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 NlaIII2 sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 Bsrl sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 BamHl sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 L428P sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 I179S sulfatase/ARSA 7 Arylsulfatase -A/steroid 250100 NM 00048 R84Q sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 S96F sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 S95N SD-144141.1 Page 132 sulfatase/ARSA Arylsulfatase A/steroid 250100 NM 00048 G119R sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 D152Y sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 R244H sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 S250Y sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 A314T sulfatase/ARSA 7 Arylsulfatase -A/steroid 250100 NM 00048 R384C sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 R496H sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 K367N sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 leu76pro sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 A2725G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 A1788G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 D255H sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 287 C~>T sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 1524+95 A->G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 Q190->H sulfatase/ARSA 7 SD-144141.1 Page 132 Arylsulfatase A/steroid 250100 NM 00048 A1788G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 A2723G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 C2330T sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 11 -bp deletion in sulfatase/ARSA 7 exon 8 Arylsulfatase A/steroid 250100 NM 00048 A1049G sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 Taql sulfatase/ARSA 7 Arylsulfatase A/steroid 250100 NM 00048 BamHl sulfatase/ARSA 7 Arylsulfatase B/steroid 253200 NM 00004 GLY137VAL sulfatase/ ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 CYS117ARG sulfatase/ ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 LEU236PRO sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 CYS405TYR sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 1-BP DEL frameshift sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 743C DEL frameshift sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 11-BP DEL sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 G302R sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 Q456X SD-144141.1 Page 132 sulfatase/ARSB Arylsulfatase B/steroid 253200 NM 00004 A1191G sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 *534Q sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 R160* sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 R160Q sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 7-bp del frameshift sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 deletion (delta sulfatase/ARSB 6 G237-C243) Arylsulfatase B/steroid 253200 NM 00004 R152W sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 argl44gly sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 argl92cys sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 pro3211eu sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 insertion between sulfatase/ARSB 6 T1284 and G1285 Arylsulfatase B/steroid 253200 NM 00004 deletion C 1577 sulfatase/ARSB 6 Arylsulfatase B/steroid 253200 NM 00004 T1600C sulfatase/ARSB 6 Arylsulfatase C, 308100 NM 00035 TRP372A] isozyme s/steroid 1 sulfatase/ARCSl Arylsulfatase C, 308100 NM 00035 CYS446TYR SD-144141.1 Page 132 isozyme s/steroid 1 sulfatase/ ARCS 1 Arylsulfatase C, 308100 NM_00035 SER341LEU isozyme s/steroid 1 sulfatase/ARCSl Arylsulfatase C, 308100 NM_00035 TRP372PRO isozyme s/steroid 1 sulfatase/ARCSl Arylsulfatase C, 308100 NM 00035 HIS444ARG isozyme s/steroid sulfatase/ARCSl Arylsulfatase C, 308100 NM_00035 19-bp insertion 1477 frameshift isozyme s/steroid 1 intron/exon 18 sulfatase/ARCSl Arylsulfatase D/steroid 300002 ****** none found sulfatase/ARSD Arylsulfatase E/steroid 300180 NM 00004 ARG12SER sulfatase/ARSE 7 Arylsulfatase E/steroid 300180 NM 00004 GLY117ARG sulfatase/ARSE 7 Arylsulfatase E/steroid 300180 NM 00004 ARG1 1 1PRO sulfatase/ARSE 7 Arylsulfatase E/steroid 300180 NM 00004 GLY137VAL sulfatase/ARSE 7 Arylsulfatase E/steroid 300180 NM 00004 GLY245ARG sulfatase/ARSE 7 Arylsulfatase E/steroid 300180 NM 00004 CYS492TYR sulfatase/ARSE 7 Arylsulfatase F/steroid 300003 NM 00404 none found sulfatase/ARSF 2 bile salt export 603201 NM 00374 ARG575TER SD-144141.1 Page 132 pump/BSEP 2 bile salt export 603201 NM 00374 GLU297GLY pump/BSEP 2 bile salt export 603201 NM 00374 1-BP DEL, 908G frameshift bi butyrylcholinestarase 177500 none found 2/serum cholinesterase 2/BCHE2 butyrylcholinesterase 177400 NM 00005 GCA to ACA ALA539THR 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 GGT to GTT Gly 390 to Val 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 E451X 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 F446V 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 THR250PRO 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 A-to-G Y128C 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 LEU330ILE 1 /serum cholinesterase 5 1/BCHEl SD-144141.1 Page 132 butyrylcholinesterase 177400 NM_00005 G365R 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM_00005 Q119X 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM_00005 R515C 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM_00005 GLU497VAL 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 MM_00005 THR243MET 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM 00005 GGT-to-GGAG Gly 117 1 /serum cholinesterase 5 Frameshift 1/BCHEl butyrylcholinesterase 177400 NM_00005 Glyl l5 by Asp 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM_00005 342-bp Alu in exon Alu insertion 1 /serum cholinesterase 5 two 1/BCHEl butyrylcholinesterase 177400 NM_00005 209 A/G Asp-70 to Gly 1 /serum cholinesterase 5 1/BCHEl butyrylcholinesterase 177400 NM_00005 1 /serum cholinesterase 5 1/BCHEl CARBOXYLESTERA 114835 none found SD-144141.1 Page 132 SE 1 ; CES1 Catechol-O- 1 16790 M58525 Bgll Methyltransferase Catechol-O- 116790 M58525 186C > T at exon 3 Methyltransferase Catechol-O- 1 16790 M58525 408C > G at exon 4 Methyltransferase Catechol-O- 1 16790 M58525 472G > A at exon 4 M ethyl trans ferase Catechol-O- 116790 M58525 597G > A at exon 5 Methyltransferase Catechol-O- 1 16790 M58525 821-827insC at the 3' Methyltransferase Catechol-O- 116790 M58525 Vall58->Met Methyltransferase Catechol-O- 116790 M58525 Nlalll Methyltransferase Catechol-O- 116790 M58525 Mspl Methyltransferase Catechol-O- 1 16790 M58525 val-108-met Methyltransferase Catechol-O- 1 16790 M58525 G/A 1947 Methyltransferase Catechol-O- 116790 M58525 C256G silent Methyltransferase class I aldehyde 100640 M26761 none found dehydrogenase cytochrome P450 107910 XI 3589 (TTT A)n in intron 5 aromatase (CYP 19) cytochrome P450 107910 X13589 1-BP DEL, 408C frameshift aromatase (CYP 19) SD-144141.1 Page 132 cytochrome P450 107910 X13589 G-->A at Val80 silent aromatase (CYP 19) cytochrome P450 107910 X13589 G- 1094 -A ARG365GLN aromatase (CYP 19) cytochrome P450 107910 X13589 G-to-A Val370-to-Met aromatase (CYP 19) cytochrome P450 107910 X13589 GT to AT exon and aromatase (CYP 19) intron 3 cytochrome P450 107910 X13589 splice donor 29 extra amino aromatase (CYP 19) (GT>GC) of intron 6 acids cytochrome P450 107910 XI 3589 Arg264cys aromatase (CYP 19) cytochrome P450 107910 X13589 ARG375CYS aromatase (CYP 19) cytochrome P450 107910 X13589 ARG435CYS aromatase (CYP 19) cytochrome P450 107910 X13589 CYS437TYR aromatase (CYP 19) cytochrome P450, 108330 NM_00049 cATT-GTT Ile462Val subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 Mspl subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 T6235C subfamily I- 9 polypeptide 1 (aryl SD-144141. Page 132 hydrocarbon oxidaseYCYPlAl cytochrome P450, 108330 NM_00049 A4889G subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 T5639C subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 C4887A subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 C(-459)T subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 G(-469)A subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 108330 NM_00049 C(4151)T) subfamily I, 9 polypeptide 1 (aryl hydrocarbon SD-144141.1 Page 132 oxidase)/CYPlAl cytochrome P450, 108330 NM 00049 HinCII subfamily I, 9 polypeptide 1 (aryl hydrocarbon oxidase)/CYPlAl cytochrome P450, 124060 AH002667 C->A subfamily I, polymoφhism in polypeptide 2 intron 1 (phenacetin metabolism)/CYPlA2 cytochrome P450, 124060 AH002667 G->A -2964 subfamily I, polypeptide 2 (phenacetin metabolism)/CYPlA2 cytochrome P450, 124060 AH002667 F21L subfamily I, polypeptide 2 (phenacetin metabolism)/CYPlA2 cytochrome P450, 601771 NM_00010 deletion 1410 to frameshift subfamily IB, 4 1422 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM_00010 insertion between frameshift subfamily IB, 4 1209 and 1214 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM_00010 GLY61GLU subfamily IB, 4 SD-144141 - 1 Page 133 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 1546DUP10 frameshift subfamily IB, 4 polypeptide 1 (dioxin inducibleVCYPlBl cytochrome P450, 601771 NM . 00010 GLY365TRP subfamily IB, 4 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 ARG469TRP subfamily IB, 4 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 ASP374ASN subfamily IB, 4 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 LYS387GLU subfamily IB, ~ 4 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 432 (Val->Leu) subfamily IB, 4 polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 601771 NM . 00010 453 (Asn->Ser) subfamily IB, Ά polypeptide 1 (dioxin inducible)/CYPlBl cytochrome P450, 123960 X13897 Xmnl SD-144141.1 Page 133 subfamily II, polypeptide 1 (phenobarbital inducible)/CYP2A cytochrome P450, 122720 NM_00076 LEU160HIS subfamily IIA, 2 polypeptide 6 (coumarin-7- hydroxylase)/CYP2A6 cytochrome P450, 122720 NM_00076 CYP2A6 null subfamily IIA, 2 polypeptide 6 (coumarin-7- hydroxylase)/CYP2A6 cytochrome P450, 122720 NM_00076 Ddel subfamily IIA, 2 polypeptide 6 (coumarin-7- hydroxylase)/CYP2A6 cytochrome P450, 123930 M29874 none found subfamily IIB (phenobarbital inducible)/CYP2B cytochrome P450, 601131 T204 -> A subfamily IIC, polypeptide 18/CYP2C18 cytochrome P450, 601131 A-460 -> T subfamily IIC, polypeptide 18/CYP2C18 SD-144141.1 Page 133 cytochrome P450, 601 131 ****** Ddel subfamily IIC, polypeptide 18/CYP2C18 cytochrome P450, 601131 ****** Thr385Met subfamily IIC, polypeptide 18/CYP2C18 cytochrome P450, 124020 NM 00076 40-BP DEL subfamily IIC, 9 polypeptide 19 (mephenytoin 4- hydroxylase)/CYP2Cl 9 cytochrome P450, 124020 NM 00076 ARG433TRP subfamily IIC, 9 polypeptide 19 (mephenytoin 4- hydroxylase)/CYP2Cl q cytochrome P450, 601129 ****** subfamily IIC, polypeptide 8/CYP2C8 cytochrome P450, 601 130 ****** ILE359LEU subfamily IIC, polypeptide 9 (hydroxylation of tolbutamide)/CYP2C9 cytochrome P450, 601130 ****** ARG144CYS subfamily IIC, polypeptide 9 SD- 144141.1 Page 133 (hydroxylation of tolbutamide)/CYP2C9 cytochrome P450, 601 130 ****** Tyr358/Cys subfamily IIC, polypeptide 9 (hydroxylation of tolbutamide)/CYP2C9 cytochrome P450, 601130 ****** Gly417/Asp subfamily IIC, polypeptide 9 (hydroxylation of tolbutamide)/CYP2C9 cytochrome P450, 124030 NM 00010 G>C Glutamine subfamily IID, 6 intron splice site polypeptide 6 Histidine (debrisoquine (splicing defect; hydroxylation)/CYP2D does not splice 6 intron at 3' site) cytochrome P450, 124030 NM 00010 G>A Glycine intron subfamily IID, 6 splice site polypeptide 6 Arginine (debrisoquine (splicing defect; hydroxylation)/CYP2D does not splice 6 intron at 3' site) cytochrome P450, 124030 NM 00010 G>C Valine 136 subfamily IID, 6 Valine polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM_00010 G>C Serine 486 SD- 144141 1 Page 133 subfamily IID, 6 Threonine polypeptide 6 (debrisoquine hydroxylation)/CYP2D u cytochrome P450, 124030 NM 00010 insertion Arginine subfamily IID, 6 (A)>deletion (A) Glycine polypeptide 6 (frameshift - (debrisoquine premature stop hydroxylation)/CYP2D next codon) f u. cytochrome P450, 124030 NM 00010 A>C Histidine 324 subfamily IID, 6 Proline polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM 00010 G>T Glycine 169 subfamily IID, 6 Stop Codon polypeptide 6 (debrisoquine hydroxyl ation)/CYP2D f u. cytochrome P450, 124030 NM 00010 G>A Glycine 42 subfamily IID, 6 Arginine polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM 00010 insertion Tryptophan subfamily IID, 6 (T)>deletion (T) Glycine SD- 144141.1 Page 133 polypeptide 6 (frameshift - (debrisoquine premature stop hydroxylation)/CYP2D at next codon) u cytochrome P450, 124030 NM 00010 OT Arginine 296 subfamily IID, 6 Cysteine polypeptide 6 (debrisoquine hydroxylation)/CYP2D u cytochrome P450, 124030 NM 00010 C>T Proline 34 subfamily IID, 6 Serine polypeptide 6 (debrisoquine hydroxylation)/CYP2D f. cytochrome P450, 124030 NM 00010 Deletion Leucine subfamily IID, 6 (T)>Insertion (T) Leucine polypeptide 6 (frameshift - (debrisoquine premature stop) hydroxylation)/CYP2D s) cytochrome P450, 124030 NM 00010 G>A Serine 401 subfamily IID, 6 Serine polypeptide 6 (debrisoquine hydroxylation)/CYP2D cytochrome P450, 124030 NM 00010 G AA>deletion Lysine 281 subfamily IID, 6 Lysine deletion polypeptide 6 SD-144141.1 Page 133 (debrisoquine hydroxylation)/CYP2D cytochrome P450, 124030 NM 00010 A G Histidine 94 subfamily IID, 6 Arginine polypeptide 6 (debrisoquine hydroxylation)/CYP2D cytochrome P450, 124030 NM 00010 T>C Leucine 421 subfamily IID, 6 Proline polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM 00010 AG A>deletion Lysine 281 subfamily IID, 6 Lysine deletion polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM 00010 C>G Threonine 98 subfamily IID, 6 Threonine polypeptide 6 (debrisoquine hydroxylation)/CYP2D 6 cytochrome P450, 124030 NM 00010 C>G Leucine 91 subfamily IID, 6 Valine polypeptide 6 (debrisoquine SD-144141.1 Page 133 hydroxylation)/CYP2D fi, cytochrome P450, 124030 NM 00010 G>A Glycine 212 subfamily IID, 6 Glutamic acid polypeptide 6 (debrisoquine hydroxylation)/CYP2D cytochrome P450, 124030 NM 00010 C>T Phenylalanine subfamily IID, 6 112 polypeptide 6 Phenylalanine (debrisoquine hydroxylation)/CYP2D fi. cytochrome P450, 124040 J02843 (GGAT)n.(CCTA)n subfamily HE (ethanol repeat element intron inducible)/CYP2E cytochrome P450, 124040 J02843 Mspl subfamily HE (ethanol inducible)/CYP2E cytochrome P450, 124040 J02843 Pstl subfamily HE (ethanol inducible)/CYP2E cytochrome P450, 124040 J02843 Rsal subfamily HE (ethanol inducible)/CYP2E cytochrome P450, 124040 J02843 Xmnl subfamily HE (ethanol inducible)/CYP2E cytochrome P450, 124040 J02843 Taq l subfamily HE (ethanol SD- 144141.1 Page 133 inducible)/CYP2E cytochrome P450, 124070 NM 00077 none found subfamily IIF 4 (ethoxycoumarin monooxygenase), polypeptide 1/CYP2F1 cytochrome P450, 124010 NM 00077 a-g PROMOTER subfamily IIIA 6 (niphedipine oxidase), polypeptide 3/CYP3A3 cytochrome P450, 124010 NM 00077 -292 a-g subfamily IIIA 6 (niphedipine oxidase), polypeptide 3/CYP3A3 cytochrome P450, 124010 NM 00077 Thr431Ile subfamily IIIA 6 (niphedipine oxidase), polypeptide 3/CYP3A3 cytochrome P450, 124010 NM 00077 Trp392Val subfamily IIIA 6 (niphedipine oxidase), polypeptide 3/CYP3A3 cytochrome P450, 124010 NM 00077 Ile224 replacing subfamily IIIA 6 Thr224-Val225 (niphedipine oxidase), polypeptide 3/CYP3A3 Dehydroepiandrosteron 125263 NM 00316 Met 57 --> Thr e (DHEA)-preferring 7 sulfotransferase, family 2A, member 1/SULT2A1 SD-144141.1 Page 133 Dehydroepiandrosteron 125263 NMJ30316 Glu 186 --> Val e (DHEA)-preferring 7 sulfotransferase, family 2A, member 1/SULT2A1 Dihydrolipoamide 246900 J03490 LYS37GLU dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase complex) Dihydrolipoamide 246900 J03490 PRO453LEU dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase complex) Dihydrolipoamide 246900 J03490 1 -BP INS frameshift dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase SD-144141.1 Page 134 complex) Dihydrolipoamide 246900 J03490 GLY229CYS dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase complex) Dihydrolipoamide 246900 J03490 Y35X dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase complex) Dihydrolipoamide 246900 J03490 R460G dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxoglutarate complex, branched chain keto acid dehydrogenase complex) Dihydrolipoamide S- 245349 AF001437 85-BP DEL acetyltransferase (E2 component of pyruvate SD-144141 Page 134 dehydrogenase complex) Dihydrolipoamide S- 245349 AF001437 69-BP DEL acetyltransferase (E2 component of pyruvate dehydrogenase complex) Dihydrolipoamide S- 245349 AF001437 4-BP DEL acetyltransferase (E2 component of pyruvate dehydrogenase complex) dihydropyrimidine 274270 U09178 deltaC1897 dehydrogenase DPD dihydropyrimidine 274270 U09178 Arg21Gln dehydrogenase DPD dihydropyrimidine 274270 U09178 Val335Leu dehydrogenase DPD dihydropyrimidine 274270 U09178 Glu386Ter dehydrogenase DPD dihydropyrimidine 274270 U09178 165-BP DEL dehydrogenase DPD dihydropyrimidine 274270 U09178 Ser534Asn dehydrogenase DPD dihydropyrimidine 274270 U09178 Ile543Val dehydrogenase DPD dihydropyrimidine 274270 U09178 Val732Ile dehydrogenase DPD dihydropyrimidine 274270 U09178 4-BP DEL 296 to dehydrogenase DPD 299 (TCAT) dihydropyrimidine 274270 U09178 1-BP DEL, 1897C Frameshift SD-144141. Page 134 dehydrogenase DPD dihydropyrimidine 274270 U09178 ARG886HIS dehydrogenase DPD dihydropyrimidine 274270 U09178 CYS29ARG dehydrogenase DPD dihydropyrimidine 274270 U09178 ASP974VAL dehydrogenase DPD Dopamine Transporter/ 126455 L24178 5' Taql RFLP DAT1 Dopamine Transporter/ 126455 L24178 9-repeat allele DAT1 Dopamine Transporter/ 126455 L24178 40-bp VNTR in the DAT1 3 '-untranslated eosinophil 131399 ARG286HIS peroxidase/EPX eosinophil 131399 INS G, NT1537 epoxide hydrolase 132810 NM 00012 TYR113HIS 1/EPHX1 0 (microsomal) epoxide hydrolase 132810 NM 00012 Exon 3 T to C 1/EPHX1 0 (microsomal) epoxide hydrolase 132810 NM 00012 His/ Arg 139 1/EPHX1 0 (microsomal) epoxide hydrolase 132811 ****** none found 2/EPHX2 (cytosolic) ESTERASE A-4 133220 none found ESTERASE A-5; 133230 none found ESA5 SD- 144141.1 Page 134 -r r 73 73 73 73 CN c G C C _, 73 73 73 3 3 fi 3 w C C C 3 3 3 ,o , -,o--. ,o , efio u Q ,o r O CD 03 CD CD fi c c C H (D 03 O o o o r-- CO c C c c σs c c Os O o O © c c c CN dehydrogenase Glucose-6-phosphate 305900 X03674 ALA335THR dehydrogenase Glucose-6-phosphate 305900 X03674 GLU156LYS dehydrogenase Glucose-6-phosphate 305900 X03674 GLY163SER dehydrogenase Glucose-6-phosphate 305900 X03674 SER188PHE dehydrogenase Glucose-6-phosphate 305900 X03674 ASP58ASN dehydrogenase Glucose-6-phosphate 305900 X03674 ARG393HIS dehydrogenase Glucose-6-phosphate 305900 X03674 GLY447ARG dehydrogenase Glucose-6-phosphate 305900 X03674 ASP282HIS dehydrogenase Glucose-6-phosphate 305900 X03674 PHE216LEU dehydrogenase Glucose-6-phosphate 305900 X03674 LYS386GLU dehydrogenase Glucose-6-phosphate 305900 X03674 ARG387HIS dehydrogenase Glucose-6-phosphate 305900 X03674 CYS385ARG dehydrogenase Glucose-6-phosphate 305900 X03674 GLY410CYS dehydrogenase Glucose-6-phosphate 305900 X03674 ARG285HIS dehydrogenase Glucose-6-phosphate 305900 X03674 NTH 16, G-A dehydrogenase SD- 144141 .1 Page 134 Glucose-6-phosphate 305900 X03674 NT131 L , C-T dehydrogenase Glucose-6-phosphate 305900 X03674 EX6, -60, C-G dehydrogenase G 1 ucose-6-phosphate 305900 X03674 ARG454HIS dehydrogenase Glucose-6-phosphate 305900 X03674 ARG459LEU dehydrogenase Glucose-6-phosphate 305900 X03674 GLU398LYS dehydrogenase Glucose-6-phosphate 305900 X03674 ASP181VAL dehydrogenase Glucose-6-phosphate 305900 X03674 ASN 126ASP dehydrogenase Glucose-6-phosphate 305900 X03674 VAL213LEU dehydrogenase Glucose-6-phosphate 305900 X03674 ARG393HIS dehydrogenase Glucose-6-phosphate 305900 X03674 VAL291MET dehydrogenase Glucose-6-phosphate 305900 X03674 ARG227LEU dehydrogenase Glucose-6-phosphate 305900 X03674 LEU323PRO dehydrogenase Glucose-6-phosphate 305900 X03674 ARG463HIS dehydrogenase Glucose-6-phosphate 305900 X03674 ASN363LYS dehydrogenase Glucose-6-phosphate 305900 X03674 ARG198CYS dehydrogenase Glucose-6-phosphate 305900 X03674 SER106CYS SD-144141.1 Page 134 dehydrogenase Glucose-6-phosphate 305900 X03674 ARG182TRP dehydrogenase Glucose-6-phosphate 305900 X03674 ARG198CYS dehydrogenase Glucose-6-phosphate 305900 X03674 ASN165ASP dehydrogenase Glucose-6-phosphate 305900 X03674 ARG198PRO dehydrogenase Glucose-6-phosphate 305900 X03674 ARG227GLN dehydrogenase Glucose-6-phosphate 305900 X03674 PR0353SER dehydrogenase Glucose-6-phosphate 305900 X03674 ARG387CYS dehydrogenase Glucose-6-phosphate 305900 X03674 VAL394LEU dehydrogenase Glucose-6-phosphate 305900 X03674 GLY410ASP dehydrogenase Glucose-6-phosphate 305900 X03674 ARG439PRO dehydrogenase Glucose-6-phosphate 305900 X03674 ILE35DEL dehydrogenase Glucose-6-phosphate 305900 X03674 GLU317LYS dehydrogenase Glucose-6-phosphate 305900 X03674 ILE48THR dehydrogenase Glucose-6-phosphate 305900 X03674 HIS32ARG dehydrogenase Glucose-6-phosphate 305900 X03674 GLY131VAL dehydrogenase SD- 144141.1 Page 1347 Glucose-6-phosphate 305900 X03674 LEU342PHE dehydrogenase Glucose-6-phosphate 305900 X03674 ALA44GLY dehydrogenase Glucose-6-phosphate 305900 X03674 PHE173LEU dehydrogenase Gl ucose-6-phosphate 305900 X03674 ASP181VAL dehydrogenase Glucose-6-phosphate 305900 X03674 PRO467ARG dehydrogenase Glucose-6-phosphate 305900 X03674 ALA361VAL dehydrogenase Glucose-6-phosphate 305900 X03674 24-BP DEL, NT953 dehydrogenase Glucose-6-phosphate 305900 X03674 Prol72->Ser dehydrogenase Glucose-6-phosphate 305900 X03674 R459L dehydrogenase Glucose-6-phosphate 305900 X03674 R463H dehydrogenase Glucose-6-phosphate 305900 X03674 C->T 563 dehydrogenase Glucose-6-phosphate 305900 X03674 376A->G dehydrogenase Glucose-6-phosphate 305900 X03674 202G->A dehydrogenase Glucose-6-phosphate 305900 X03674 680G->T dehydrogenase Glucose-6-phosphate 305900 X03674 968T->C dehydrogenase Glucose-6-phosphate 305900 X03674 563C->T SD- 144141.1 Page 1348 dehydrogenase Glucose-6-phosphate 305900 X03674 202G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1311C->T dehydrogenase Glucose-6-phosphate 305900 X03674 406 C->T dehydrogenase Glucose-6-phosphate 305900 X03674 1155 C-->G dehydrogenase Glucose-6-phosphate 305900 X03674 185 C->T, 62 Pro->Phe dehydrogenase Glucose-6-phosphate 305900 X03674 695 G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1387 C->T 463 Arg-->Cys dehydrogenase Glucose-6-phosphate 305900 X03674 1246 G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1 160 G-->A dehydrogenase Glucose-6-phosphate 305900 X03674 Bel l dehydrogenase Glucose-6-phosphate 305900 X03674 202 G->A dehydrogenase Glucose-6-phosphate 305900 X03674 335 Ala->Thr dehydrogenase Glucose-6-phosphate 305900 X03674 G->T at nt l376 dehydrogenase Glucose-6-phosphate 305900 X03674 G->A at l388 dehydrogenase Gl ucose-6-phosphate 305900 X03674 A~>G at nt 95 dehydrogenase SD- 144141.1 Page 134 Glucose-6-phosphate 305900 X03674 A209G dehydrogenase Glucose-6-phosphate 305900 X03674 493 A->G dehydrogenase Glucose-6-phosphate 305900 X03674 592 C->T dehydrogenase Glucose-6-phosphate 305900 X03674 844 G > C dehydrogenase Glucose-6-phosphate 305900 X03674 224 T->C dehydrogenase Glucose-6-phosphate 305900 X03674 488 G-->A dehydrogenase Glucose-6-phosphate 305900 X03674 833 C->T dehydrogenase Glucose-6-phosphate 305900 X03674 1360C->T 454Arg->Cys dehydrogenase Glucose-6-phosphate 305900 X03674 383T->C 128Leu->Pro dehydrogenase Glucose-6-phosphate 305900 X03674 208T->C 70Tyr->His dehydrogenase Glucose-6-phosphate 305900 X03674 497G->A 166Arg->His dehydrogenase Glucose-6-phosphate 305900 X03674 A->G 1138 val380iso dehydrogenase Glucose-6-phosphate 305900 X03674 T->C 1139 iso380thr dehydrogenase Glucose-6-phosphate 305900 X03674 C-->G 1177 gly393arg dehydrogenase Glucose-6-phosphate 305900 X03674 C->T 1187 dehydrogenase Glucose-6-phosphate 305900 X03674 527A->G SD-144141.1 Page 135 dehydrogenase Glucose-6-phosphate 305900 X03674 1003G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1159C->T dehydrogenase Glucose-6-phosphate 305900 X03674 1160G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1229G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1246G->A dehydrogenase Glucose-6-phosphate 305900 X03674 1361G->A dehydrogenase Glucose-6-phosphate 305900 X03674 C->T 563 dehydrogenase Glucose-6-phosphate 305900 X03674 C->T 1311 dehydrogenase Glucose-6-phosphate 305900 X03674 241 C to T dehydrogenase Glucose-6-phosphate 305900 X03674 487 G->A dehydrogenase glutathione peroxidase 138320 Y00433 P197L GPxl glutathione peroxidase 138320 Y00433 1167T/C Silent GPxl glutathione peroxidase 138319 X68314 A/T intron GPx2 glutathione peroxidase 138319 X68314 TC repeats intron GPx2 glutathione peroxidase 138321 X58295 none found GPx3 SD- 144141.1 Page 1351 00 a Or ft fi CO CN m O ro © © Oo rr-- O CΛs © __, © © CN CO ro ro σσss O CΛS r roo rroo - -nn O CN t-~ in ro '-t ro r- rroo rroo ■ --f- • " "ccTr rroo ro ro CN ro 00 • = ro 00 oooo oooo © © © © oooo oo CN OO OO ro O ro o rroo © © © © rroo *— ' — -. © r ro ro © ro ro VO — . — -, V VO --. -— VO 00 transporter MOAT-B (MOAT-B) mRNA, complete cds Homo sapiens alcohol 103730 M12272 ile349-to-val dehydrogenase class I gamma subunit (ADH3) mRNA, complete cds Homo sapiens alcohol 103730 M12272 ARG271 GLU dehydrogenase class I gamma subunit (ADH3) mRNA, complete cds Homo sapiens gamma- 601176 L35546 none found glutamylcysteine synthetase light subunit mRNA, complete cds Homo sapiens mRNA 264700 AB005038 ARG107HIS for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 264700 AB005038 GLY125GLU for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 264700 AB005038 ARG335PRO for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete SD-144141.1 Page 135 cds Homo sapiens mRNA 264700 AB005038 PRO382SER for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 264700 AB005038 1-BP DEL frameshift for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 264700 AB005038 1-BP DEL, 958G for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 264700 AB005038 7-BP DUP for 25-hydroxyvitamin D3 1-alpha- hydroxylase, complete cds Homo sapiens mRNA 603608 AB004854 none found for carbonyl reductase 3, complete cds Homo sapiens 602447 L48513 CYS31 1SER paraoxonase 2 (PON2) mRNA, complete cds Homo sapiens 602447 L48513 ALA148GLY paraoxonase 2 (PON2) mRNA, complete cds Homo sapiens 602720 L48516 none found SD- 144141.1 Page 1 5 paraoxonase 3 (PON3) mRNA, 3' end of cds Homo sapiens retinoic 602239 AF005418 none found acid hydroxylase mRNA, complete cds Homo sapiens SMRP SMRP AB005659 none found mRNA, complete cds Human alcohol 600086 U07821 none found dehydrogenase (ADH7) mRNA, complete cds Human alcohol 103735 M68895 none found dehydrogenase 6 gene, complete cds Human alcohol 103710 M29872 Mspl dehydrogenase class III (ADH5) mRNA, complete cds Human aldehyde 601917 U37519 none found dehydrogenase (ALDH8) mRNA, complete cds Human aldehyde 600463 U07919 none found dehydrogenase 6 mRNA, complete cds Human aldehyde 600466 U10868 none found dehydrogenase ALDH7 mRNA, complete cds Human aldehyde 100660 M74542 none found dehydrogenase type III (ALDHIII) mRNA, SD-144141 - 1 Page 135 complete cds Human alpha-1 acid 138600 M13692 VAL156MET glycoprotein mRNA, complete cds Human alpha-1 acid 138600 M13692 GLN20ARG glycoprotein mRNA, complete cds Human aminopeptidase 151530 M22324 none found N/CD13 mRNA encoding aminopeptidase N, complete cds Human arylacetamide 600338 L32179 none found deacetylase mRNA, complete cds Human carbonyl 114830 J04056 none found reductase mRNA, complete cds Human class I alcohol 103720 M24317 ARG47HIS dehydrogenase (ADH2) beta-1 subunit mRNA, complete cds Human class I alcohol 103720 M24317 ARG369CYS dehydrogenase (ADH2) beta-1 subunit mRNA, complete cds Human class II 103740 M15943 -75A-->C alchohol dehydrogenase (ADH4) pi subunit mRNA, complete cds SD-144141.1 Page 135 Human factor KBF 1 16401 1 M55643 (CA)n mRNA, complete cds Human fatty aldehyde 270200 L47162 1-BP DEL, 525T dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 1-BP DEL, 808G dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 3-BP DEL/21-BP dehydrogenase INS (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 ALA314GLY dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 PRO315ALA dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 CYS214TYR dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 PRO315SER dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 2-BP DEL, 1297GA frameshift SD-144141.1 Page 135 dehydrogenase (FALDH) mRNA, complete cds Human fatty aldehyde 270200 L47162 5-BP INS, NT1311 dehydrogenase (FALDH) mRNA, complete cds Human gamma- 602733 U34252 CYS1 15SER aminobutyraldehyde dehydrogenase mRNA, complete cds Human gamma- 230450 M90656 A->T 1 109 His370Leu glutamylcysteine synthetase (GCS) mRNA, complete cds Human gamma- 230450 M90656 (CAGC)n 1972-1975 glutamylcysteine synthetase (GCS) mRNA, complete cds Human gamma- 137168 M64099 none found glutmyl transpeptidase- related protein (GGT- Rel) mRNA, complete cds Human glutathione 601002 U34683 ARG164GLN synthetase mRNA, complete cds Human glutathione 601002 U34683 1-BP DEL frameshift synthetase mRNA, complete cds Human glutathione 601002 U34683 ARG267TRP SD- 144141.1 Page 135 synthetase mRNA, complete cds Human glutathione 601002 U34683 ARG283CYS synthetase mRNA, complete cds Human glutathione 601002 U34683 ARG125CYS synthetase mRNA, complete cds Human glutathione 601002 U34683 PRO314LEU synthetase mRNA, complete cds Human glutathione 601002 U34683 6-BP DEL VAL-GLN del synthetase mRNA, complete cds Human glutathione 601002 U34683 ASP219GLY synthetase mRNA, complete cds Human kidney mRNA 115500 X04076 IVS4, G-A, +5 for catalase Human kidney mRNA 115500 X04076 A to T -21 for catalase Human kidney mRNA 115500 X04076 C to A -20 for catalase Human kidney mRNA 115500 X04076 C to T -18 for catalase Human kidney mRNA 115500 X04076 T to C 4 for catalase Human kidney mRNA 115500 X04076 T to C 44 for catalase Human kidney mRNA 115500 X04076 T to C 49 for catalase SD-144141.1 Page 136 Human kidney mRNA 1 15500 X04076 C to T 12 for catalase Human kidney mRNA 1 15500 X04076 C to A 27 for catalase Human kidney mRNA 1 15500 X04076 358 T->del for catalase Human kidney mRNA 115500 X04076 Mspl for catalase Human messenger 103600 V00494 ARG-2HIS RNA for serum albumin (HSA) Human messenger 103600 V00494 ARG-1 GLN RNA for serum albumin (HSA) Human messenger 103600 V00494 ARG- 1 PRO RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP 1 VAL RNA for serum albumin (HSA) Human messenger 103600 V00494 HIS3GLN RNA for serum albumin (HSA) Human messenger 103600 V00494 ARG1 14GLY RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU1 19LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP269GLY RNA for serum SD-144141.1 Page 1361 albumin (HSA) Human messenger 103600 V00494 LYS313ASN RNA for serum albumin (HSA) Human messenger 103600 V00494 ALA320THR RNA for serum albumin (HSA) Human messenger 103600 V00494 ARG-2CYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU321LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU354LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU358LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP365HIS RNA for serum albumin (HSA) Human messenger 103600 V00494 LYS372GLU RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP375ASN RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU376LYS RNA for serum albumin (HSA) SD- 144141.1 Page 136 Human messenger 103600 V00494 GLU382LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU501LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 LYS541GLU RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP550GLY RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP563ASN RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU565LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU570LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 LYS573GLU RNA for serum albumin (HSA) Human messenger 103600 V00494 LYS574ASN RNA for serum albumin (HSA) Human messenger 103600 V00494 IVS6, A-G, -2 RNA for serum albumin (HSA) Human messenger 103600 V00494 EX14DEL SD-144141.1 Page 136 RNA for semm albumin (HSA) Human messenger 103600 V00494 LYS536GLU RNA for semm albumin (HSA) Human messenger 103600 V00494 ARG- 1 LEU RNA for semm albumin (HSA) Human messenger 103600 V00494 GLN580LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU60LYS RNA for serum albumin (HSA) Human messenger 103600 V00494 GLU82LYS RNA for semm albumin (HSA) Human messenger 103600 V00494 ASP494ASN RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP365VAL RNA for semm albumin (HSA) Human messenger 103600 V00494 HIS 128 ARG RNA for semm albumin (HSA) Human messenger 103600 V00494 IVS13DS, G-C, +1 RNA for semm SD-144141.1 Page 136 albumin (HSA) Human messenger 103600 V00494 LYS240GLU RNA for serum albumin (HSA) Human messenger 103600 V00494 AAT267AAAT frameshift RNA for semm albumin (HSA) Human messenger 103600 V00494 ARG218HIS RNA for serum albumin (HSA) Human messenger 103600 V00494 HIS3TYR RNA for serum albumin (HSA) Human messenger 103600 V00494 LYS225GLN RNA for semm albumin (HSA) Human messenger 103600 V00494 LYS276ASN RNA for semm albumin (HSA) Human messenger 103600 V00494 TGC567GC frameshift RNA for semm albumin (HSA) Human messenger 103600 V00494 TYR140CYS RNA for serum albumin (HSA) Human messenger 103600 V00494 ASP63ASN RNA for semm albumin (HSA) Human messenger 103600 V00494 CYS177PHE RNA for semm albumin (HSA) SD-144141- 1 Page 136 Human messenger 103600 V00494 GLN268ARG RNA for serum albumin (HSA) Human messenger 103600 V00494 ASN318LYS RNA for semm albumin (HSA) Human messenger 103600 V00494 GLU333LYS RNA for semm albumin (HSA) Human messenger 103600 V00494 GLU376ASN RNA for semm albumin (HSA) Human messenger 103600 V00494 GLU479LYS RNA for semm albumin (HSA) Human messenger 103600 V00494 GLU505LYS RNA for semm albumin (HSA) Human messenger 103600 V00494 ARG218PRO RNA for semm albumin (HSA) Human messenger 103600 V00494 LEU66PRO RNA for serum albumin (HSA) Human messenger 103600 V00494 Arg218His RNA for semm albumin (HSA) Human messenger 103600 V00494 Haelll intron 7 RNA for semm albumin (HSA) Human mitochondrial 600125 L13286 none found SD-144141.1 Page 136 1 ,25 -dihydroxyvitamin D3 24-hydroxylase mRNA, complete cds Human mRNA for 312170 X52709 4-BP DEL brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 7-BP DEL brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 ARG378HIS brain pyruvate dehydrogenase (EC 1.2.4.1 ) Human mRNA for 312170 X52709 LYS313DEL brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 2-BP DEL frameshift brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 20-BP DEL, brain pyruvate EX1 1DEL dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 21-BP INS brain pyruvate dehydrogenase (EC 1.2.4.1) SD-144141.1 Page 136 Human mRNA for 312170 X52709 ARG234GLY brain pyruvate dehydrogenase (EC 1.2.4.1) Human m-RNA for 312170 X52709 ARG302CYS brain dehydroge Human mRNA for 312170 X52709 4-BP INS frameshift brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 ASP258ALA brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 PHE205LEU brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 TYR243ASN brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 ASP315ASN brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 MET282LEU brain pyruvate dehydrogenase (EC SD-144141.1 Page 136 1.2.4.1) Human mRNA for 312170 X52709 -BP INS FS 141TER brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 ARG10PRO brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 13-BP INS, EX10 brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 312170 X52709 36-BP INS brain pyruvate dehydrogenase (EC 1.2.4.1) Human mRNA for 179780 D13138 none found dipeptidase Human mRNA for 138300 X15722 none found glutathione reductase (EC 1.6.4.2) Human mRNA for 231950 X60069 none found pancreatic gamma- glutamyltransferase Human multidrug CMOAT2 U83659 none found resistance-associated protein homolog (MRP3) Human 182396 L21893 none found Na/taurocholate SD-144141.1 Page 136 cotransportmg polypeptide mRNA, complete cds Monoamine Oxidase 309850 M69226 23-bp VNTR A; MAOA Monoamine Oxidase 309850 M69226 3rd base of codon 941 A; MAOA 941 G>T Monoamine Oxidase 309850 M69226 A1026T ProlineProline A; MAOA Monoamine Oxidase 309850 M69226 A1559G LysineArginine A; MAOA Monoamine Oxidase 309850 M69226 A385C Arginine Arginin A; MAOA e Monoamine Oxidase 309850 M69226 C1410T Aspartic A; MAOA AcidAspartic Acid Monoamine Oxidase 309850 M69226 C886T GlutamineTermi A; MAOA nation codon Monoamine Oxidase 309850 M69226 C886T Glutamine296T A; MAOA ermination codon Monoamine Oxidase 309850 M69226 exon 14 - RFLP A; MAOA (EcoRV enzyme) Monoamine Oxidase 309850 M69226 length of (CA)n A; MAOA repeat Monoamine Oxidase 309850 M69226 RFLP (EcoRV A; MAOA enzyme) Monoamine Oxidase 309850 M69226 RFLP (Pst I) A; MAOA Monoamine Oxidase 309850 M69226 T891G A; MAOA SD-144141.1 Page 137 Monoamine Oxidase 309850 M69226 T891 G ArginineArginin A; MAOA e Monoamine Oxidase 309860 M69177 (GT)n repeat B; MAOB Monoamine Oxidase 309860 M69177 36 bases upstream B; MAOB from intron 13 -exon 14 boundary Monoamine Oxidase 309860 M69177 A at position 644 of B; MAOB intron 13 Monoamine Oxidase 309860 M69177 G at position 644 of B; MAOB intron 13 Monoamine Oxidase 309860 M69177 RFLP (Maelll B; MAOB enzyme) multidrug resistance 158343 L05628 none found associated protein MRP1 multidrug resistance 601 107 U83659 none found associated protein MRP2 multidrug resistance 171050 X96395 Hindlll protein MDRl multidmg resistance 171050 X96395 Ser893Ala protein MDRl multidrug resistance 171050 X96395 GLY185VAL protein MDRl multidrug resistance 602347 X06181 none found protein MDR3/P- glycoprotein 3/PGY3 myeloperoxidase/MPO 254600 ARG569TRP myeloperoxidase/MPO 254600 TYR173CYS myeloperoxidase/MPO 254600 MET251THR SD-144141.1 Page 1371 myeloperoxidase/MPO 254600 G to A in the promoter myeloperoxidase/MPO 254600 -463 G/A myeloperoxidase/MPO 254600 Dinucleotide repeat myeloperoxidase/MPO 254600 EcoRV RFLP myeloperoxidase/MPO 254600 Pstl. N-acetyltransferase 108345 NM 00066 POLYADENYLATI 1/arylamide acetylase 2 ON SIGNAL 1/NAT1 VARIANT N-acetyltransferase 108345 NM 00066 VAL149ILE 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 C1095A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 T1088A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 C1095A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM 00066 9 bp deletion 1/arylamide acetylase 2 1/ AT1 N-acetyltransferase 108345 NM_00066 G560A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM 00066 C559T 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM 00066 C190T SD-144141.1 Page 137 1/arylamide acetylase 1/NAT1 N-acetyltransferase 108345 NM_00066 350-351 (GG to CC) 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 497-499 (GGG to 1/arylamide acetylase 2 CCC) 1/NAT1 N-acetyltransferase 108345 NM_00066 C97T 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 C190T 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 T402C 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 G445A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM 00066 G459A 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 T640G 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 C559T 1/arylamide acetylase 2 1/NAT1 N-acetyltransferase 108345 NM_00066 G560A 1/arylamide acetylase 2 SD-144141.1 Page 137 1/NATl N-acetyltransferase 108345 NM 00066 A613G 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 A752T 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 T777C 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 G781A 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 A787G 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 Argl87 to a 1/arylamide acetylase 2 stop codon 1/NATl N-acetyltransferase 108345 NM_00066 Argl 87 to Gln 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 -344 (C->T) 1/arylamide acetylase 2 1/NATl N-acetyltransferase 108345 NM 00066 640 T->G Ser->Ala 1/arylamide acetylase 2 1/NATl N-acetyltransferase 243400 NM 00001 ARG197GLN 2/arylamide acetylase 5 2/NAT2 SD-144141.1 Page 137 N-acetyltransferase 243400 NM_ 00001 ILEl 14THR 2/arylamide acetylase 5 2/NAT2 N-acetyl 2/arylamid N-acetyl 2/arylamide acetylase 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 191 G-A Arg64->Gln 2/arylamide acetylase " 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 C282T (silent) 2/arylamide acetylase 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 T341C Ilel l4->Thr 2/arylamide acetylase _ 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 481C->T silent 2/arylamide acetylase 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 590 G->A Argl97-->Gln 2/arylamide acetylase " 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 803 A~>G Lys268->Arg 2/arylamide acetylase " 5 2/NAT2 N-acetyltransferase 243400 NM_ 00001 857 G->A Gly286->Glu 2/arylamide acetylase ~ 5 2/NAT2 N-acetyltransferase 243400 NM 00001 C759T SD-144141.1 Page 137 2/arylamide acetylase 2/NAT2 NAD(P)H menadione 125860 NM_00090 609C-T prol 87ser oxidoreductase 1, 3 dioxin- inducible/NMOR 1 /diap horase 4/DIA4 NAD(P)H menadione 160998 NM_00090 none found oxidoreductase 2, 4 dioxin- inducible/NMOR2 NEUROPATHY 603197 none found TARGET ESTERASE nieotinamide N- 600008 NM_00616 eight SNPs within methyltransferase/NN 9 intron 1 MT 06 alkylguanine-DNA 156569 M60761 GGA to AGA glyl60arg alkyltransferase 06 alkylguanine-DNA 156569 M60761 1034A>G alkyltransferase 06 alkylguanine-DNA 156569 M60761 1099OT alkyltransferase 06 alkylguanine-DNA 156569 M60761 79G>T alkyltransferase paraoxonase 1/PONl 168820 AH004193 GLN192ARG (arylesterase) paraoxonase 1/PONl 168820 AH004193 MET54LEU (arylesterase) paraoxonase 1/PONl 168820 AH004193 Leu55Met (arylesterase) paraoxonase 1/PONl 168820 AH004193 CA repeat intron 4. SD-144141.1 Page 137 (arylesterase) PEPTIDE 601250 none found METHIONINE SULFOXIDE REDUCTASE Peroxisome 170998 NM 00503 none found proliferative activated 6 receptor, alpha/PPARA Peroxisome 600409 NM 00623 none found proliferative activated 8 receptor, delta/PPARD Peroxisome 601487 NM 00503 PRO1 15GLN proliferative activated 7 receptor, gamma/PPARG Peroxisome 601487 NM 00503 PRO 12 ALA proliferative activated 7 receptor, gamma/PPARG Peroxisome 601487 NM 00503 1-BP DEL, 472A Frameshift proliferative activated 7 receptor, gamma/PPARG Peroxisome 601487 NM 00503 GLN286PRO proliferative activated 7 receptor, gamma/PPARG Peroxisome 601487 NM 00503 LYS319TER proliferative activated 7 receptor, gamma/PPARG SD-144141. Page 137 Peroxisome 601487 NM 00503 ARG288HIS proliferative activated 7 receptor, gamma PPARG Phenol-preferring 171150 NM 00105 Arg213His sulfotransferase, family 5 1A, member 1/SULTlAl Phenol-preferring 601292 NM 00105 none found sulfotransferase, family 4 1A, member 2/SULT1A2 Phenol-preferring 600641 L19956 none found sulfotransferase, family 1A, member 3/SULT1A3 phenylethanolamine N- 171190 NM 00268 BANI methyltransferase/PN 6 MT PHOSPHOADENOSI 603262 none found NE- PHOSPHOSULFATE SYNTHETASE 1 Pyruvate 179060 M34479 none found dehydrogenase (lipoamide) beta RAR related orphan 600825 NM 00294 none found receptor A/RORA 3 RAR related orphan 602943 NM 00506 none found receptor C/RORC 0 reduced folate carrier 600424 U19720 none found SD-144141.1 Page 137 RFCl renal microsomal 179780 NM 00441 none found dipeptidase/DPEPl (b- 3 lactam ring hydrolysis) renal transport of beta- 109660 none found amino acids/ AABT retinoic acid receptor 180240 NM 00096 7-base deletion frameshift alpha/RARA 4 retinoic acid receptor 180240 NM 00096 codon 411 C to T alpha/RARA 4 retinoic acid receptor 180240 NM 00096 Arg272Gln alpha/RARA Ά retinoic acid receptor 180240 NM 00096 Met297Leu alpha/RARA 4 retinoic acid receptor 180220 NM 00096 none found beta/RARB 5 retinoic acid receptor 180190 M57707 none found gama/RARG retinoid X receptor 180245 NM 00295 none found alpha/RXRA 7 retinoid X receptor 180246 X66424 none found beta/RXRB retinoid X receptor 180247 U38480 none found gamma/RXRG serotonin transporter 182138 X70697 Pstl serotonin transporter 182138 X70697 promoter 44-bp ins/del serotonin transporter 182138 X70697 tandem repeat close to the promoter serotonin transporter 182138 X70697 two polyadenylation sites SD-144141.1 Page 137 serotonin transporter 182138 X70697 VNTR intron 2 serotonin transporter 182138 X70697 silent polymoφhism Solute Carrier Family 133550 U08989 none found 1, Member 1 ; Slclal Solute Carrier Family 600300 U03505 none found 1 , Member 2; Sic la2 Solute Carrier Family 600111 U03504 none found 1, Member 3; Slcla3 Solute carrier family 1, 600229 NM_00303 none found member 4/SLC1A4 8 (glutamate) Solute carrier family 1 , 109190 AF105230 none found member 5/SLC1A5 (neutral AA) Solute carrier family 1 , 600637 NM_00507 none found member 6 1 (GABA/GLUySLClA 6 Solute carrier family 182396 NM_00304 none found 10, member 9 1/SLClOAl (taurocholate) Solute carrier family 601295 NM_00045 LEU243PRO 10, member 2 2/SLC10A2 (taurocholate) Solute carrier family 601295 NM_00045 THR262MET 10, member 2 2/SLC10A2 (taurocholate) SD-144141 - 1 Page 138 Solute carrier family 601295 NM 00045 A171 S 10, member 2 2/SLC10A2 (taurocholate) Solute carrier family 604148 NM 00398 none found 12, member 4 2/SLC12A2 (dicarboxylic acids) Solute carrier family 600544 U13173 none found 15, member 1/SLC15A1 (peptides) Solute carrier family 602339 S78203 none found 15, member 2/SLC 15 A2 (peptides) Solute carrier family 600682 NM 00305 none found 16, member 1 1/SLC16A1 (monocarboxylic acids) Solute carrier family 300095 NM 00651 none found 16, member 7 2/SLC16A2 (monocarboxylic acids) Solute carrier family 603877 NM 00420 none found 16, member 7 3/SLC16A3 (monocarboxylic acids) Solute carrier family 603878 ****** none found 16, member 4/SLC16A4 (monocarboxylic acids) Solute carrier family 603879 NM_00469 none found SD-144141 - 1 Page 1381 16, member 5 5/SLC16A5 (monocarboxylic acids) Solute carrier family 603880 NM 00469 none found 16, member 4 (monocarboxylic acids) Solute carrier family 603654 AF049608 none found 16, member 7/SLC16A7 (monocarboxylic acids) Solute carrier family 601460 NM 00563 none found 21 , member 0 2/SLC21A2 (prostaglandin) Solute carrier family 602883 NM 00507 none found 21, member 5 3/SLC21A3 (organic anion) Solute carrier family 602631 AF037064 111-BP INS 22, member 1- like/SLC22Al (organic cation) Solute carrier family 602631 AF037064 688G-A 22, member 1- like/SLC22Al (organic cation) Solute carrier family 602607 NM 00305 none found 22, member 8 1/SLC22A2 (organic cation) SD- 144141 .1 Page 1382 Solute carrier family 602608 NM_00305 22, member 8 2/SLC22A2 (organic cation) Solute carrier family 603377 113-BP DEL 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 1-BP INS, 226C 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 TRP132TER 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 G-to-A transition in 22, member the last nucleotide of 5/SLC22A5 (camitine) intron 8 Solute carrier family 603377 1394-BP DEL 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 19-BP INS 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 171-BP DEL 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 ARG282TER 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 TYR401TER 22, member 5/SLC22A5 (camitine) SD-144141.1 Page 138 Solute carrier family 603377 1-BP DEL, 1345G 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 PRO478LEU 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 TYR21 1 CYS 22, member 5/SLC22A5 (camitine) Solute carrier family 603377 Argl69Gln 22, member 5/SLC22A5 (camitine) Solute carrier family 190315 X96924 none found 25, member 1/SLC25A1 (tricarboxylic acids) Solute carrier family 29 602193 NM_00495 none found (nucleosides), member 5 1/SLC29A1/ENT1 Solute carrier family 29 6021 10 X86681 none found (nucleosides), member 2/SLC29A2/ENT2 Solute carrier family 3 104614 ****** none found member 1/SLC3A1 (aa transporter) Solute carrier family 5 604024 none found member 6/SLC5A6 (folate, biotin, lipoate) Solute carrier family 6 137165 X54673 none found ( GABA), member 1/SLC6A1 SD-144141.1 Page 138 Solute carrier family 6 603080 U27699 none found (betaine/GABA), member 12 Solute carrier family 6 , 163970 NM 00104 none found member 3 5/SLC6A2/NAT1/NET 1 (glycine) Solute carrier family 6, 604159 NM 00421 none found member 5/SLC6A5 1 (glycine) Solute carrier family 6, 186854 U16120 Dinucleotide repeat member 6/SLC6A6 (taurine) Solute carrier family 6, 601019 S70612 none found Member 9; SLC6A9 (glycine) Solute carrier family 7, 104615 ****** Taql member 1/SLC7A1 (cationic AA) Solute carrier family 7, 601872 D29990 none found member 2/SLC7A2 (cationic AA) Solute carrier family 7, 603752 ****** none found member 4/SLC7A4 (cationic AA) Solute carrier family 7, 600182 M80244 none found member 5/SLC7A5 (neutral AA) Solute carrier family 7, 603593 Y 18474 1 181 , A-T, -2 A->T member 7/SLC7A7 (dibasic AA) SD-144141.1 Page 138 Solute carrier family 7, 603593 Y18474 543-BP DEL member 7/SLC7A7 (dibasic AA) Solute carrier family 7, 603593 Y18474 4-BP INS member 7/SLC7A7 (dibasic AA) Solute carrier family 7, 604144 ****** member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** GLY 105 ARG member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** ALA182THR member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** GLY 195 ARG member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** GLY259ARG member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** 2-BP DEL, 596TG member 9/SLC7A9 (neutral AA) Solute carrier family 7, 604144 ****** 1-BP INS, 520T member 9/SLC7A9 (neutral AA) sterol-O-acyl 102642 L21934 none found transferase 1/SOATl sterol-O-acyl 60131 1 ****** none found transferase 2/SOAT2 SD-144141.1 Page 138 Succinic semialdehyde 271980 L34820 IVS9, , G-T, +1 dehydrogenase Succinic semialdehyde 271980 L34820 IVS5, G-A, +1 dehydrogenase SULFONYLUREA 601439 none found RECEPTOR 2 Sulfotransferase, 602385 U66036 none found family I C, member 3/SULT1C1 Sulfotransferase, 604125 NM 00460 none found family 2B, member 5 1/SULT2B1 Superoxide Dismutase 147450 NM 00045 GLY37ARG 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 LEU38VAL 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY41SER 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY41 ASP 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 HIS43ARG 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY85ARG 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY93CYS 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY93ALA 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLUI OOGLY 1/SODl (soluble) ~ 4 Superoxide Dismutase 147450 NM 00045 LEU 106 VAL SD-144141.1 Page 138 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ILE1 13THR 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ALA4VAL 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 HIS46ARG 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ALA4THR 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ASP90ALA 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ILE104THE 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 LEU144SER 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 ALA145THR 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 T-G, -10, 9-BP INS 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 CYS6PHE 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 THR151ILE 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLU21LYS 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 SER134ASN 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 LEU84VAL 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY16SER 1/SODl (soluble) 4 SD-144141.1 Page 138 Superoxide Dismutase 147450 NM 00045 LEU126TER 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 VS4AS, A-G, -11 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 GLY72SER 1/SODl (soluble) 4 Superoxide Dismutase 147450 NM 00045 Val7->Glu 1/SODl (soluble) 4 Superoxide Dismutase 147460 X65965 ALA16VAL 2/SOD2 (mitochondrial) Superoxide Dismutase 185490 NM 00310 ARG213GLY 3/SOD3 (extracellular) 2 Superoxide Dismutase 185490 NM 00310 A241G 3/SOD3 (extracellular) 2 Superoxide Dismutase 185490 NM 00310 C280T 3/SOD3 (extracellular) 2 Thiopurine 187680 U12387 ALA80PRO methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 ALA154THR methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 TYR240CYS methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 IVS9AS, G-A, -1 methyltransferase (6- SD-144141. Page 138 mercaptopurine detoxification) Thiopurine 187680 U12387 ALA154THR methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 TYR240CYS methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 ARG215HIS methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 G460 to A methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 A719 to G methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 VNTR promoter methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 G644A methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 G238C SD-144141.1 Page 139 methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U12387 T681G methyltransferase (6- mercaptopurine detoxification) Thiopurine 187680 U 12387 C->T at nucleotide methyltransferase (6- 178 mercaptopurine detoxification) Thiopurine 187680 U12387 T->G681 methyltransferase (6- mercaptopurine detoxification) TRANSCRIPTION 164014 LI 9067 494, Glu-Asp FACTOR P65 UDP 191740 NM_00107 13-BP DEL glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 SER-PHE glycosyltransferase 2 1/UGTl UDP 191740 NM 00107 GLN331TER glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 ARG341TER glycosyltransferase 2 1/UGTl UDP 191740 NMJXH07 GLN331 ARG glycosyltransferase 2 SD-144141.1 Page 1391 1/UGTl UDP 191740 NM_00107 PHE170DEL glycosyltransferase 2 1/UGTl UDP 191740 NM 00107 SER376PHE glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 GLY309GLU glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 CYS-TER glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 PR0229GLN glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 2-BP INS, TA, glycosyltransferase 2 TATAA ELEMENT 1/UGTl UDP 191740 NM_00107 1-BP INS, 470T glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 IVS1, G-C, +l glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 145C-T glycosyltransferase 2 1/UGTl UDP 191740 NM_00107 IVS3, A-G, -2 glycosyltransferase 2 1/UGTl SD-144141.1 Page 139 UDP 601291 U30930 none found glycosyltransferase 8/UGT8 UDP 600070 NM 00107 none found glycosyltransferase 5 family 2, member B10/UGT2B10 UDP 600069 U06641 asp85tyr glycosyltransferase family 2, member B15/UGT2B15 UDP 601903 NM 00107 none found glyco syltrans ferase 7 family 2, member B17/UGT2B17 UDP 600067 NM 00107 asp458glu glycosyltransferase 3 family 2, member B4/UGT2B4 UDP 600067 NM 00107 leul09phe glycosyltransferase 3 family 2, member B4/UGT2B4 UDP 600067 NM 00107 leu396phe glycosyltransferase 3 family 2, member B4/UGT2B4 UDP 600068 NM 00107 none found glycosyltransferase 4 family 2, member B7/UGT2B7 SD-144141.1 Page 1393 UDP- 218800 AJ005162 none found glucuronosyltransferas Vesicular acetylcholine 600336 NM_00305 none found transporter 5 Vesicular Amine 193002 ****** none found Transporter 1 ; VAT1 Vesicular Amine 193001 L091 18 Taql XX Transporter 2; VAT2 Table 21. Identified Variances in Genes or Related Pathways involved in Inflammatioinand Immune Disease 3,5 cyclic nucleotide 171890 U40370 none found phosphodiesterase (HSPDE1A3A) activated leucocyte cell 601662 L38608 none found adhesion molecule/CD6 ligand/ALCAM alpha-2-macroglobulin 103950 M11313 VAL1000ILE alpha-2-macroglobulin 103950 M11313 CYS972TYR alpha-2-macroglobulin 103950 M1 1313 deletion of the intron alpha-2-macroglobulin 103950 M1 1313 ARG681HIS alpha-2-macroglobulin 103950 Ml 1313 EX18DEL alpha-2-macroglobulin 103950 M1 1313 5-BP DEL alpha-2-macroglobulin 103950 M11313 intronic SD-144141.1 Page 139 polymoφhism alpha-2-macroglobulin 103950 M11313 EcoRI antigen peptide 170260 X57522 ILE333VAL transporter 1/MHC 1/TAPl antigen peptide 170260 X57522 ASP637GLY transporter 1/MHC 1/TAPl antigen peptide 170260 X57522 ARG659GLN transporter 1/MHC 1/TAPl antigen peptide 170260 X57522 518 (GTC~>ATC) Val~>Ile transporter 1/MHC 1/TAPl antigen peptide 170260 X57522 G~>T substitution in transporter 1/MHC the promoter region 1/TAPl antigen peptide 170260 X57522 10-bp insert in intron transporter 1/MHC 9 1/TAPl antigen peptide 170260 X57522 G~>T 80bp 3' of transporter 1/MHC termination codon 1/TAPl antigen peptide 170261 Z22935 Ala665Thr transporter 2/MHC 2/TAP2 antigen peptide 170261 Z22935 Gln687Stop transporter 2/MHC 2/TAP2 antigen peptide 170261 Z22935 ILE379VAL transporter 2/MHC SD-144141.1 Page 139 2/TAP2 apoptosis-related 147678 X65019 none found cystein protease 1 /interleukin 1-beta converting enzyme/ICE/caspase 1/CASPl beta-1 -adrenergic 109630 J03019 C1 165G ARG389GLY receptor; Adrbl beta-1 -adrenergic 109630 J03019 Bgl l. receptor; Adrbl Beta-2-Adrenergic 109690 Ml5169 val 34 met Receptor; Adrb2 Beta-2-Adrenergic 109690 Ml5169 A->G -1343 Receptor; Adrb2 Beta-2- Adrenergi c 109690 M15169 C->G -468 Receptor; Adrb2 Beta-2-Adrenergic 109690 M15169 G->A -1023 Receptor; Adrb2 Beta-2-Adrenergic 109690 Ml 5169 G->A -654 Receptor; Adrb2 Beta-2-Adrenergic 109690 M15169 T->A -1429 Receptor; Adrb2 Beta-2-Adrenergic 109690 M15169 T->C -367 Receptor; Adrb2 Beta-2-Adrenergic 109690 Ml 5169 Fnu4HI Receptor; Adrb2 Beta-2-Adrenergic 109690 M l 5169 T->C -20 Receptor; Adrb2 Beta-2-Adrenergic 109690 M15169 T->C -47 Receptor; Adrb2 SD-144141.1 Page 139 Beta-3-Adrenergic 109691 X70811 TRP64ARG Receptor; Adrb3 Beta-3-Adrenergic 109691 X7081 1 intron 1 gl 856t Receptor; Adrb3 Beta-Adrenergic 109636 X691 17 none found bradykinin receptor 600337 U12512 9-base pair deletion Bl/BDKRBl G protein-coupled bradykinin receptor 600337 U12512 A1098~>G B1/BDK-RB1 G protein-coupled bradykinin receptor 600337 U12512 C181->T Bl/BDKRBl G protein-coupled bradykinin receptor 600337 U12512 G-699->C Bl/BDKRBl G protein-coupled bradykinin receptor 1 13503 X86164 -845C/T B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86165 -704C/T B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86166 -649insG B2/BDKRB2 G protein-coupled bradykinin receptor 1 13503 X86167 -640T/C B2/BDKRB2 G protein-coupled SD-144141.1 Page 139 bradykinin receptor 113503 X86168 -536C/T B2/BDK-RB2 G protein-coupled bradykinin receptor 113503 X86169 -412C/G B2/BDKRB2 G protein-coupled bradykinin receptor 1 13503 X86170 •143 C/T B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86171 -78C/T B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86172 T21M B2/BDKRB2 G protein-coupled bradykinin receptor 1 13503 X86173 9 bp de (-)21 -29 B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86174 C>T promoter 54 B2/BDKRB2 G protein-coupled bradykinin receptor 113503 X86175 tandem repeat near B2/BDKRB2 G promoter protein-coupled bradykinin receptor 113503 X86176 R14C B2/BDKRB2 G protein-coupled bradykinin receptor 1 13503 X86177 repeat 3 'UTR B2/BDKRB2 G protein-coupled Ca Channel alphala 601011 AF004884 ARG192GLN SD-144141.1 Page 139 (alt. splice) L-Type Ca Channel alpha la 601011 AF004884 THR666MET (alt. splice) L-Type Ca Channel alphal a 601011 AF004884 VAL714ALA (alt. splice) L-Type Ca Channel alphal a 60101 1 AF004884 ILEl 81 1 LEU (alt. splice) L-Type Ca Channel alphal a 60101 1 AF004884 1-BP DEL, 4073C frameshift (alt. splice) L-Type Ca Channel alpha la 601011 AF004884 G-to-A first (alt. splice) L-Type nucleotide of intron 24 Ca Channel alpha la 60101 1 AF004884 (CAG)n (alt. splice) L-Type Ca Channel alphal a 601011 AF004884 GLY293ARG (alt. splice) L-Type Ca Channel alphal a 601011 AF004884 ASP715GLU (alt. splice) L-Type Ca Channel alpha la 60101 1 AF004884 C4914T premature stop (alt. splice) L-Type Ca Channel gamma L- 114209 L07738 none found Type Ca2+-dependent 601192 U03090 none found phospholipase A2 CD3E antigen, epsilon 186830 X03884 T-to-C splice change polypeptide (TiT3 complex) CD3E antigen, epsilon 186830 X03884 TRP59TER polypeptide (TiT3 complex) CD3E antigen, epsilon 186830 X03884 Taql SD-144141.1 Page 139 polypeptide (TiT3 complex) CD3G antigen, gamma 186740 X04145 MET1VAL polypeptide (TiT3 complex) CD3G antigen, gamma 186740 X04145 17-BP DEL polypeptide (TiT3 complex) CD3G antigen, gamma 186740 X04145 Mspl polypeptide (TiT3 complex) Complement CIS 120580 J04080 4-BP DEL component precursor (Cl esterase) Cyclooxygenase 1 176805 M59979 none found COX1 Cyclooxygenase 2 600262 M90100 none found COX2 H.sapiens ACTH-R None X65633 none found gene for adrenocorticotropic hormone receptor Histamine receptor HI 600167 AF026261 none found Histamine receptor H2 142703 M64799 A649G Histamine receptor H3 none found Human DP prostanoid None U31332 none found receptor (PTGDR) gene, 5 region and partial cds Human IP gene for 600022 D38128 none found prostacyclin receptor, SD-144141.1 Page 140 exon 3 Human leukotriene-C4 246530 U11552 promoter synthase mRNA, polymoφhism complete cds Human mRNA for 601699 D38145 none found prostacyclin synthase, complete cds Human prostaglandin 176802 L22647 none found receptor epl subtype mRNA, complete cds Intercellular adhesion 147840 M24283 K E 469 molecule 1 Intercellular adhesion 147840 M24283 Dinucleotide repeat molecule 1 3' Intercellular adhesion 146630 X15606 none found molecule 2 Intercellular adhesion 146631 X69819 LYS29ME ^ molecule 3 interferon-gamma 147569 U05875 Gln64Arg receptor 2/IFNGR2 interferon-gamma 147569 2-BP DEL, AG, receptor 2/IFNGR2 NT278-279 interferon-gamma 107470 J03143 395C-A SER-TER receptor 1/IFNGR1 interferon-gamma 107470 1-BP DEL frameshift receptor 1/IFNGR1 interferon-gamma 107470 ILE87THR receptor 1/IFNGR1 interferon-gamma 107470 4-BP INS, 107TTAC receptor 1/IFNGR1 interferon-gamma 107470 G-A, +1 SD-144141.1 Page 14 receptor 1/IFNGRl interferon-gamma 107470 4-BP DEL, NT818 receptor 1/IFNGRl interferon-gamma 107470 ValHMet receptor 1/IFNGRl interferon-gamma 107470 Taql receptor 1/IFNGRl interleukin 1 beta 147720 K02770 Taql (ILlb) interleukin 1 beta 147720 K02770 +5887 C --> T (ILlb) interleukin 1 beta 147720 K02770 exon 5 (position (ILlb) +3953) interleukin 1 beta 147720 K02770 position -511 (ILlb) interleukin 1 beta 147720 K02770 Asp 106 Asn (ILlb) Interleukin 1 receptor 147679 X52015 86-bp tandem repeat antagonist Kallikrein Inhibitor 147935 L19684 none found Kallikrein KLK1 147910 X13561 A1 166->C Kallikrein KLK1 147910 X13561 Taql Kallikrein KLK2 147960 S39329 C to T at base 792 L-Type Ca Channel 114204 Z28613 none found alpha 2/delta L-Type Ca Channel 114206 Z26289 none found alpha Id L-type voltage 1 14205 M92269 none found dependent calcium channel alpha IC subunit/CACNAlC SD-144141.1 Page 140 L-type voltage 114208 L33798 ARG1086HIS dependent calcium channel alpha 1 S subunit/CACNAlS L-type voltage 114208 L33798 ARG1239GLY dependent calcium channel alpha 1 S subunit/CACNAl S L-type voltage 114208 L33798 ARG1239HIS dependent calcium channel alpha IS subunit/CACNAlS L-type voltage 114208 L33798 ARG528HIS dependent calcium channel alpha 1 S subunit/CACNAlS Leukocyte integrin 192975 L12002 none found alpha-4 Leukocyte integrin 602453 U40274 none found alpha-d Leukocyte integrin 153370 Y00796 none found alpha-1 Leukocyte integrin 120980 J04145 none found alpha-m Leukocyte integrin 151510 M81695 none found alpha-x Leukocyte integrin 135630 U28252 none found beta-1 Leukocyte integrin 600065 M15395 ARG593CYS beta-2 Leukocyte integrin 600065 M15395 LYS196THR SD-144141.1 Page 1403 beta-2 Leukocyte integrin 600065 M15395 LEU149PRO beta-2 Leukocyte integrin 600065 M15395 GLY169ARG beta-2 Leukocyte integrin 600065 Ml 5395 ATG-to-AAG initiation codon beta-2 Leukocyte integrin 600065 M15395 ARG586TRP beta-2 Leukocyte integrin 600065 M15395 12-bp insertion pro-ser-ser-gln beta-2 Leukocyte integrin 600065 M15395 ASN351 SER beta-2 Leukocyte integrin 600065 M15395 . PRO178LEU beta-2 Leukocyte integrin 600065 M 15395 ASP128ASN beta-2 Leukocyte integrin 600065 Ml 5395 G-A, splice/donor beta-2 site Leukocyte integrin 600065 M15395 GLY284SER beta-2 Leukocyte integrin 600065 M15395 SER138PRO beta-2 Leukocyte integrin 600065 M15395 GLY273ARG beta-2 Leukocyte integrin 600065 M15395 S138P beta-2 Leukocyte integrin 173470 M35999 ARG214GLN beta-3 Leukocyte integrin 173470 M35999 ASP1 19TYR beta-3 SD-144141.1 Page 1404 Leukocyte integrin 173470 M35999 ARG214TRP beta-3 Leukocyte integrin 173470 M35999 SER752PRO beta-3 Leukocyte integrin 173470 M35999 ARG143GLN beta-3 Leukocyte integrin 173470 M35999 LEU33PRO beta-3 Leukocyte integrin 173470 M35999 PRO407ALA beta-3 Leukocyte integrin 173470 M35999 G-T, EXiDEL beta-3 Leukocyte integrin 173470 M35999 ARG489GLN beta-3 Leukocyte integrin 173470 M35999 CYS374TYR beta-3 Leukocyte integrin 173470 M35999 1 1.2-KB DEL beta-3 Leukocyte integrin 173470 M35999 ARG724TER beta-3 Leukocyte integrin 173470 M35999 GLU616TER beta-3 Leukocyte integrin 147557 X51841 1-BP INS, 3801T beta-4 Leukocyte integrin 147557 X51841 1-BP DEL, 1150G beta-4 Leukocyte integrin 147557 X51841 LEU156PRO beta-4 Leukocyte integrin 147557 X51841 ARG554TER beta-4 Leukocyte integrin 147557 X51841 CYS61TYR SD-144141.1 Page 14 beta-4 Leukocyte integrin 147557 X51841 CYS562ARG beta-4 Leukocyte integrin 147557 X51841 IVS30DS, G-A, +1 beta-4 Leukocyte integrin 147557 X51841 TRP1478TER Leukocyte integrin 147557 X51841 CYS38ARG beta-4 Leukocyte integrin 147557 X51841 1-BP DEL, 4776G beta-4 Leukocyte integrin 147557 X51841 3434delT beta-4 Leukocyte integrin 147557 X51841 8-bp deletion beta-4 Leukocyte integrin 147559 M68892 none found beta-7 Leukotriene A4 151570 J03459 none found hydrolase Leukotriene C4 none found receptor Leukotriene D4/E4 none found receptor lipocortin 1 /annexin 1 151690 X05908 none found lipocortin 2/annexin 2 151740 D00017 none found lipocortin 3/annexin 3 106490 M20560 Bglll lipocortin 3/annexin 3 106490 M20560 Sail lipocortin 3/annexin 3 106490 M20560 tandem repeat TAAA Lipoxygenases: 12- 152391 M62982 none found lipoxygenase (platelet) SD-144141.1 Page 140 Lipoxygenases: 5- 152390 J03571 none found lipoxygenase (leukocytes) lymphotoxin beta 600979 L04270 none found receptor (TNFR superfamily, member 3/LTBR N-acylamino acid 104620 L07548 none found aminohydrolase P2Y7 601531 D89078 none found purinoceptor/leukotrien e B4 receptor/G protein-coupled Phospholipase A-2 172410 M21054 none found (PLA-2) lung Phospholipase C beta-3 600230 Z26649 none found Phospholipase C delta- 602142 U09117 none found Phospholipase C 600597 D42108 none found epsilon Phospholipase C 172420 M34667 none found gamma- 1 Phospholipase C 600220 M37238 none found gamma-2 Phospholipase C, beta 600810 L41349 none found 4 Platelet-activating 173393 M76674 none found factor receptor Prostaglandin 15-OH 601688 J05594 none found dehydrogenase (PGDH) SD-144141.1 Page 140 Prostaglandin E 601586 L28175 none found receptor 2 (subtype EP2), 53kD Prostaglandin E 176806 X83861 none found receptor 3 (subtype EP3) {alternative products} PROSTAGLANDIN 176804 U19487 none found E2 RECEPTOR, EP2 SUBTYPE PROSTAGLANDIN F 600563 L24470 none found RECEPTOR PROSTAGLANDIN U26664 none found F2 ALPHA RECEPTOR prostaglandin 601460 U70867 none found transporter hPGT recombination 179615 M29474 GLU722LYS activating gene 1/RAG1 recombination 179615 M29474 GLU774TER activating gene 1/RAG1 recombination 179615 M29474 TYR938TER activating gene 1/RAG1 recombination 179615 M29474 ALA156VAL activating gene 1/RAG1 recombination 179615 M29474 ARG561HIS activating gene SD- 144141 - Page 140 1/RAGl recombination 179615 M29474 ARG396CYS activating gene 1/RAGl recombination 179615 M29474 TYR912CYS activating gene 1/RAGl recombination 179615 M29474 ARG396HIS activating gene 1/RAGl recombination 179615 M29474 ASP429GLY activating gene 1/RAGl recombination 179615 M29474 ARG561CYS activating gene 1/RAGl recombination 179615 M29474 A G737HIS activating gene 1/RAGl recombination 179615 M29474 13-BP DEL, activating gene NT1723 1/RAGl recombination 179615 M29474 2-BP DEL, NT368 activating gene 1/RAG l recombination 179616 CYS476TYR activating gene 2/RAG2 recombination 179616 ARG220GLN activating gene 2/RAG2 SD- 144141.1 Page 1409 recombination 179616 CYS41TRP activating gene 2/RAG2 recombination 179616 MET285ARG activating gene 2/RAG2 regulator of G-protein 600323 X73427 none found signalling 1/RGS1 Retinoic acid receptor, 180240 X06538 7-base deletion frameshift alpha/RARA Retinoic acid receptor, 180240 X06538 Arg272Gln alpha/RARA Retinoic acid receptor, 180240 X06538 Met297Leu alpha/RARA Retinoic acid receptor, 180240 X06538 codon 411 C to T alpha/RARA Retinoic acid receptor, 180220 X07282 none found beta/RARB Retinoic acid receptor, 180190 M24857 none found gamma/RARG serotonin 5-HT 182139 D49394 none found receptors 5-HT3, gated ion channel signaling lymphocytic 603492 U33017 none found activation molecule/SLAM small inducible 158105 M28226 -2518 (G or A) cytokine subfamily A (Cys-Cys), member 2/monocyte chemotactic protein SD-144141.1 Page 141 1/MCP1/SCYA2 small inducible 158105 M28226 -2076 (A or T) cytokine subfamily A (Cys-Cys), member 2/monocyte chemotactic protein 1/MCP1/SCYA2 small inducible 182283 M25315 none found cytokine subfamily A (Cys-Cys), member 3/macrophage inflammatory protein 1A/MIP1A/SCYA3 Solute carrier family 4, 109270 M27819 LYS56GLU anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 24-BP DEL CODONS 400- anion exchanger, 408 member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 PRO327ARG anion exchanger, SD-144141.1 Page 141 member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLU40LYS anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 10-BP DUP anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLU658LYS anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLY771ASP SD-144141.1 Page 141 anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLN330TER anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 ARG150TER anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute earner family 4, 109270 M27819 89G-A anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) SD-144141. Page 141 Solute carrier family 4, 109270 M27819 VAL557MET anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 ARG589HIS anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 ARG589CYS anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 SER613PHE anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS SD-144141.1 Page 1414 THE MEMBRANE) Solute carrier family 4, 109270 M27819 ARG589SER anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLY701ASP anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 PR0854LEU anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 GLY130ARG anion exchanger, member 1 (MEDIATES EXCHANGE OF INORGANIC SD-144141.1 Page 1415 ANIONS ACROSS THE MEMBRANE) Solute carrier family 4, 109270 M27819 THR837ALA anion exchanger, member 1 (MEDIATES EXCHANGE OF -INORGANIC ANIONS ACROSS THE MEMBRANE) T cell receptor- 176947 L05148 GG-AG, -11 associated protein tyrosine kinase ZAP- 70/ZAP70 T cell receptor- 176947 L05148 G-A, -9 associated protein tyrosine kinase ZAP- 70/ZAP70 T cell receptor- 176947 L05148 SER518ARG associated protein tyrosine kinase ZAP- 70/ZAP70 T cell receptor- 176947 L05148 13-BP DEL frameshift associated protein tyrosine kinase ZAP- 70/ZAP70 Thromboxane A2 TP 188070 U27325 ARG60LEU receptor, platelet and non-platelet Thromboxane synthase 274180 M80646 (CA)n intron 9 transforming growth 190181 LI 1695 S387Y SD-144141.1 Page 141 factor, beta receptor I (activin A receptor type Il-like kinase, 53kD)/TGFBRl transforming growth 190182 M85079 2-BP INS frameshift factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 THR315MET factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 GG to TT Stop codon factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 a7g intron 2 factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 a-4t intron 3 factor, beta receptor II (70-80kD)/TGFBR2 transfoπning growth 190182 M85079 codon 128 factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 ACA to GCA Thr to Ala factor, beta receptor II (70-80kD)/TGFBR2 transforming growth 190182 M85079 base in the factor, beta receptor II polyadenine tract of (70-80kD)/TGFBR2 exon 3 trans fonning growth 600742 L07594 none found factor, beta receptor III (betaglycan, SD-144141.1 Page 14 300kD)/TGFBR3 tumor necrosis factor 191160 X01394 C-850T alpha (TNFa) tumor necrosis factor 191 160 X01394 C-ins 5'UTR of exon alpha (TNFa) 1 tumor necrosis factor 191 160 X01394 G -238 A alpha (TNFa) tumor necrosis factor 191 160 X01394 G -376 A alpha (TNFa) tumor necrosis factor 191 160 X01394 -1,031 T-->C alpha (TNFa) tumor necrosis factor 191160 X01394 -863 C->A alpha (TNFa) tumor necrosis factor 191160 X01394 -308 G/A alpha (TNFa) tumor necrosis factor 191 160 X01 94 ARG32TRP alpha (TNFa) tumor necrosis factor 191 160 X01394 LEU29SER alpha (TNFa) tumor necrosis factor 191 160 X01394 G-376A alpha (TNFa) tumor necrosis factor 191160 X01394 Ncol alpha (TNFa) tumor necrosis factor 191160 X01394 C to T, -857T alpha (TNFa) TUMOR NECROSIS 191 190 M58286 CYS33TYR FACTOR RECEPTOR 1 PRECURSOR TUMOR NECROSIS 191 190 M58286 THR50MET FACTOR RECEPTOR 1 PRECURSOR SD-144141.1 Page 14 TUMOR NECROSIS 191190 M58286 CYS30ARG FACTOR RECEPTOR 1 PRECURSOR TUMOR NECROSIS 191 190 M58286 CYS52PHE FACTOR RECEPTOR 1 PRECURSOR TUMOR NECROSIS 191 190 M58286 CYS88ARG FACTOR RECEPTOR 1 PRECURSOR TUMOR NECROSIS 191190 M58286 CYS88TYR FACTOR RECEPTOR 1 PRECURSOR Tumor necrosis factor 191 191 M32315 M196R receptor 2 (75kD) tumor necrosis factor None U12595 none found type 1 receptor associated protein (TRAP1) tumor necrosis factor 601895 U12597 none found type 2 receptor associated protein (TRAP3) Vascular cell adhesion 192225 M60335 none found molecule 1 vitamin D (1,25- 601769 J03258 GLY30ASP dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ARG-GLY dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 TYR292TER SD-144141.1 Page 14 dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ARG77GLN dihydroxyvitamin D3) receptor/VDR vitamin D (1 ,25- 601769 J03258 ARG47GLN dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 GLN149TER dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ARG271LEU dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 GLY46ASP dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 HIS305GLN dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ILE314SER dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ARG391CYS dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 ARG30TER dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 Bsml dihydroxyvitamin D3) SD-144141.1 Page 14 receptor/VDR vitamin D (1,25- 601769 J03258 ATG to ACG initiation codon dihydroxyvitamin D3) receptor/VDR vitamin D (1 ,25- 601769 J03258 Apa I dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 Taq l dihydroxyvitamin D3) receptor/VDR vitamin D (1 ,25- 601769 J03258 codon 79 silent dihydroxyvitamin D3) receptor/VDR vitamin D (1,25- 601769 J03258 base change in intron dihydroxyvitamin D3) 3 receptor/VDR vitamin D (1 ,25- 601769 J03258 EcoRV xx dihydroxyvitamin D3) receptor/VDR Table 22. Identified Variances in Genes or Related Pathways involved in Endocrine and Metabolic Disease 2,3-cyclic nucleotide 3 M19650 123830 none found phosphodiesterase 3beta hydroxysteroid M27137 109715 none found dehydrogenase a-glucosidase Y00839 232300 EX18DEL SD-144141.1 Page 14 a-glucosidase Y00839 232300 1-BP DEL frameshift a-glucosidase Y00839 232300 T-G, -13 intron 1 a-glucosidase Y00839 232300 ARG725TRP a-glucosidase Y00839 232300 PRO545LEU a-glucosidase Y00839 232300 SER529VAL a-glucosidase Y00839 232300 GLY643ARG a-glucosidase Y00839 232300 GLU521 LYS a-glucosidase Y00839 232300 GLU689LYS a-glucosidase Y00839 232300 ARG854TER a-glucosidase Y00839 232300 LEU299ARG a-glucosidase Y00839 232300 LYS903DEL a-glucosidase Y00839 232300 MET318THR a-glucosidase Y00839 232300 ASP91ASN a-glucosidase Y00839 232300 ASP645GLU a-glucosidase AB D42041 None none found AC ATI D90228 203750 1 -BP INS, 1083A AC ATI D90228 203750 1 163 + 2 ACAT1 D90228 203750 4-BP INS ACAT1 D90228 203750 828 + 1 AC ATI D90228 203750 IVS10. A-C. -2 AC ATI D90228 203750 IVS 10, G-C, -1 AC ATI D90228 203750 IVS8, G-T, +1 ACAT1 D90228 203750 ALA347THR AC ATI D90228 203750 GLY150ARG AC ATI D90228 203750 MET 1 LYS AC ATI D90228 203750 GLY379VAL AC ATI D90228 203750 GLN272TER ACAT1 D90228 203750 GLU345DEL AC ATI D90228 203750 ASN93SER ACAT1 D90228 203750 ILE312THR AC ATI D90228 203750 ALA333PRO SD-144141.1 Page 14 ACATl D90228 203750 N158D ACAT2 S70154 100678 1 163 + 2 ACAT2 S70154 100678 828 + 1 ACAT2 S70154 100678 Taql ACAT2 S70154 100678 N158D ACAT2 S70154 100678 Q272X Adrenocorticotropic M28636 176830 3804C-A hormone (ACTH) Adrenocorticotropic M28636 176830 7013G-T hormone (ACTH) Adrenocorticotropic M28636 176830 7133C DEL hormone (ACTH) aldose reductase M34720 103880 (AC)n Alpha Amylase 2A; M28443 104650 none found pancreatic androgen receptor M20132 313700 Hind III androgen receptor M20132 313700 (CAA)n androgen receptor M20132 313700 (CAG)n androgen receptor M20132 313700 (GGN)n androgen receptor M20132 313700 5-KB DEL, EX F,G androgen receptor M20132 313700 5-KB DEL,EX E androgen receptor M20132 313700 C>T within exon B silent androgen receptor M20132 313700 CAG340TAG Gln>Ter androgen receptor M20132 313700 Del T at 3286 frameshift androgen receptor M20132 313700 del 1893 frameshift androgen receptor M20132 313700 G Codon 210 A androgen receptor M20132 313700 G Codon 21 1 A androgen receptor M20132 313700 G2314A ala>thr androgen receptor M20132 313700 G2677A glu629arg androgen receptor M20132 313700 Hhal androgen receptor M20132 313700 Hpall SD-144141.1 Page 14 androgen receptor M20132 313700 Insert of 69 nucleotides androgen receptor M20132 313700 Maelll androgen receptor M20132 313700 PARTIAL DEL androgen receptor M20132 313700 Stu l androgen receptor M20132 313700 VAL730MET androgen receptor M20132 313700 ALA721THR androgen receptor M20132 313700 GLN902ARG androgen receptor M20132 313700 HIS874TYR androgen receptor M20132 313700 SER647ASN androgen receptor M20132 313700 THR877SER androgen receptor M20132 313700 ARG607GLN androgen receptor M20132 313700 VAL865LEU androgen receptor M20132 313700 VAL865MET androgen receptor M20132 313700 LYS588TER androgen receptor M20132 313700 CYS579PHE androgen receptor M20132 313700 PHE582TYR androgen receptor M20132 313700 pro892ser androgen receptor M20132 313700 PRO546SER androgen receptor M20132 313700 ILE869MET androgen receptor M20132 313700 GLU2LYS androgen receptor M20132 313700 ARG839CYS androgen receptor M20132 313700 ARG839HIS androgen receptor M20132 313700 GLN60TER androgen receptor M20132 313700 TRP794TER androgen receptor M20132 313700 LEU172TER androgen receptor M20132 313700 LEU707ARG androgen receptor M20132 313700 MET786VAL androgen receptor M20132 313700 TYR761CYS androgen receptor M20132 313700 ARG772CYS androgen receptor M20132 313700 598 or 599 ter SD-144141 - 1 Page 14 androgen receptor M20132 313700 gly743val androgen receptor M20132 313700 Gln798Glu androgen receptor M20132 313700 arg7261eu androgen receptor M20132 313700 LEU676PRO androgen receptor M20132 313700 ARG608LYS androgen receptor M20132 313700 val 581 phe androgen receptor M20132 313700 G214R androgen receptor M20132 313700 THR877ALA androgen receptor M20132 313700 Arg615His androgen receptor M20132 313700 Arg752Gln androgen receptor M20132 313700 arg840his androgen receptor M20132 313700 ALA771THR androgen receptor M20132 313700 LYS882TER androgen receptor M20132 313700 ARG846HIS androgen receptor M20132 313700 ARG773HIS androgen receptor M20132 313700 TRP717TER androgen receptor M20132 313700 ARG773CYS androgen receptor M20132 313700 VAL866MET androgen receptor M20132 313700 ARG855HIS androgen receptor M20132 313700 MET780ILE Arginine Vasopressin AF030625 600821 none found Receptor 1A/AVPR1A Arginine Vasopressin AF030512 600264 none found Receptor 1B/AVPR1B Arginine vasopressin AF030626 304800 1-BP DEL receptor 2 Arginine vasopressin AF030626 304800 1 -BP DEL, 102G receptor 2 Arginine vasopressin AF030626 304800 1 -BP INS frameshift receptor 2 Arginine vasopressin AF030626 304800 1-BP INS 804 frameshift SD-144141.1 Page 14 vo 00 ft ft 00 00 00 f > Dd 00 t X X 00 ft H ftl < X o O o r CN o 7, U CD ft N m c mn u ι uoo o < oo oooo o <f ffi — uo o JΓ <- 1 s (') o 5 c 3 ∞ CN ft X X ft cn cn Pi ft X oo ft -13 H ft ft , < ϋ H y Ό " ω -r> ft ---_---. oo r- fi C ϋ ft u o o o o o o o o O o o o o O O o o o o o o O o o oo oo oo oo oo oo oo oo "* • ■ r o o → *-.- "<-- • o o o o o o o o o o o o o cn ro ro ro ro ro ro ro ro ro ro ro vo o o O o cn cn ro ro ro ro ro ro ro ro ro ro ro o o o o o o ft ft ft ft ft ft ft ft ft ft ft ft ft ft ft < < < < < < < < < < < < < < o 8 A Um ^ r^ -r D 00 ft ft X ro H u o ft ^ ■ Pi vO ro oo < ^r O ro ft X O ro SO i O o ro Os 5 ft Pi Pi ro < 5 < - ft < 2 o o o o o r-~- ,— . 00 O o o o o o o r- σs σs ro ro ro uo oo oo 00 oo oo 00 oo O VO CN • <-.- " - ■ - ^r ^r o σ Os ro 5 ^ o o o o o o o o ? o ro ro ro ro ro ro VO O VO potassium channel calpain, large NM 0000 1 14240 ARG572GLN polypeptide 70 L3/CAPN3 calpain, large NM 0000 114240 ARG1 10TER polypeptide 70 L3/CAPN3 calpain, large NM 0000 114240 ARG769GLN polypeptide 70 L3/CAPN3 calpain, large NM 0000 114240 PRO319LEU polypeptide 70 L3/CAPN3 calpain, large NM 0000 114240 SER86PHE polypeptide 70 L3/CAPN3 Camitine X78706 600184 none found Acetyltransferase Camitine D87812 600528 ASP454GLY Palmitoyltransferase I (muscle) Camitine U09648 600650 413 del AG Palmitoyltransferase II Camitine U09648 600650 ARG631 CYS Palmitoyltransferase II Camitine U09648 600650 E174K Palmitoyltransferase II Camitine U09648 600650 F352C Palmitoyltransferase II Camitine U09648 600650 M647V Palmitoyltransferase II SD- 144141 - 1 Page 142 Camitine U09648 600650 V368I Palmitoyltransferase II Camitine U09648 600650 SER1 13LEU Palmitoyltransferase II Camitine U09648 600650 R124Stop Palmitoyltransferase II Camitine U09648 600650 ASP553ASN Palmitoyltransferase II Camitine U09648 600650 PRO50HIS Palmitoyltransferase II Camitine U09648 600650 GLU174LYS Palmitoyltransferase II Camitine U09648 600650 PHE383TYR Palmitoyltransferase II Camitine U09648 600650 F448L Palmitoyltransferase II Camitine U09648 600650 G549D Palmitoyltransferase II Camitine U09648 600650 ARG503CYS Palmitoyltransferase II Camitine U09648 600650 TYR628SER Palmitoyltransferase II CCAAT/ENHANCER- 138972 none found BINDING PROTEIN, GAMMA; CEBPG Cell surface receptor L78207 600509 EX35, G-A for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 G-A, -9 EXON ALPHA for sulfonylureas on DEL pancreatic b cells SD-144141 - 1 Page 14 Cell surface receptor L78207 600509 3-BP DEL PHE1388DEL for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 ACC~>ACT Thr759Thr for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 BRANCH POINT, for sulfonylureas on A-G, -20 pancreatic b cells Cell surface receptor L78207 600509 Exon 16 -3c— >t for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 G-A, -1 splice change for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 G-A, -1 exon 5 for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 ARG1353PRO for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 ARG 1421 CYS for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 ARG1494TRP for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 R275Q for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 V560M SD- 144141.1 Page 14 for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 F591 L for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 G1382S for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 H125Q for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 N188S for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 R1215Q for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 R1394H for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 T1139M for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 S1370A for sulfonylureas on pancreatic b cells Cell surface receptor L78207 600509 GLY716VAL for sulfonylureas on pancreatic b cells cytochrome P450 X13589 107910 (TTTA)n in intron 5 aromatase (CYP 19) SD-144141.1 Page 143 cytochrome P450 X13589 107910 1-BP DEL, 408C frameshift aromatase (CYP 19) cytochrome P450 X13589 107910 G->A at Val80 silent aromatase (CYP 19) cytochrome P450 X13589 107910 G-1094 -A ARG365GLN aromatase (CYP 19) cytochrome P450 X13589 107910 G-to-A Val370-to-Met aromatase (CYP 19) cytochrome P450 X13589 107910 GT to AT exon and aromatase (CYP 19) intron 3 cytochrome P450 X13589 107910 splice donor 29 extra amino aromatase (CYP 19) (GT>GC) of intron 6 acids cytochrome P450 X13589 107910 ARG435CYS aromatase (CYP 19) cytochrome P450 X13589 107910 CYS437TYR aromatase (CYP 19) cytochrome P450 X13589 107910 Arg264cys aromatase (CYP 19) cytochrome P450 X13589 107910 ARG375CYS aromatase (CYP 19) Cytochrome P450 S90469 124015 none found reductase Cytochrome P450, M29874 None none found subfamily IIB (phenobarbital- inducible), polypeptide 6 Cytochrome P450, M14565 118485 5' UTR subfamily XIA pentanucleotide (cholesterol side chain repeat cleavage) SD- 144141.1 Page 143 Cytochrome P450, M14564 202110 1-BP DEL frameshift subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hyperplasia Cytochrome P450, M14564 202110 1 -bp C del codon subfamily XVII 131 (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 -BP DEL frameshift subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 4-BP DUP, EX8 subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, Ml 4564 2021 10 469-BP INS subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 518-BP DEL subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 7-BP DUP, EX2 SD-144141.1 Page 143 subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 IVS2, G-T, +5 subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 IVS7+5G to A subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 T— >C promoter subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 ARG347HIS subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 ARG358GLN subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 TRP17TER subfamily XVII SD-144141.1 Page 1434 (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 PHE417CYS subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 PHE53/54 DEL subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 ARG239TER subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 PRO342THR subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 2021 10 SER106PRO subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 PHE53DEL subfamily XVII (steroid 17-alpha- SD-144141.1 Page 1435 hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 his3731eu subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, Ml 4564 2021 10 Arg496Cys subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 Gln461Stop subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia Cytochrome P450, M14564 202110 ARG96TRP subfamily XVII (steroid 17-alpha- hydroxylase), adrenal hypeφlasia DOLICHOL- 603503 none found PHOSPHATE MANNOSYLTRANSF ERASE 1 DOLICHYL- 603564 none found PHOSPHATE MANNOSYLTRANSF ERASE 2 REGULATORY SD-144141.1 Page 143 SUBUNIT Endothelin Receptor D90348 131243 none found Type A Endothelin Receptor L06623 131244 1-BP INS, 878T Type B Endothelin Receptor L06623 131244 TRP275TER Type B Endothelin Receptor L06623 131244 ALA183GLY Type B Endothelin Receptor L06623 131244 TRP276CYS Type B Endothelin Receptor L06623 131244 SER305ASN Type B Endothelin Receptor L06623 131244 GLY57SER Type B estrogen receptor 1 X03635 133430 RFLP (Pssl enzyme) (ESR1) estrogen receptor 1 X03635 133430 RFLP (PvuII (ESR1) enzyme) Estrogen-preferring NM 0054 600043 none found sulfotransferase/STE 20 FATTY ACID 152426 none found COENZYME A LIGASE, LONG- CHAIN 2 Folic Acid (Folate M28099 136430 none found Receptor) follicle stimulating Ml 6646 136530 CYS51GLY hormone-beta (FSH) follicle stimulating Ml 6646 136530 FS87TER hormone-beta (FSH) SD-144141.1 Page 143 FSH receptor M65085 136435 566C-->T FSH receptor M65085 136435 Bsml FSH receptor M65085 136435 Hindlll FSH receptor M65085 136435 Pstl FSH receptor M65085 136435 ARG573CYS FSH receptor M65085 136435 ILE160THR FSH receptor M65085 136435 PHE591SER FSH receptor M65085 136435 Thr307Ala FSH receptor M65085 136435 Asp567Gly FSH receptor M65085 136435 Ser680Asn FSH receptor M65085 136435 Asp334Gly FSH receptor M65085 136435 ALA189VAL G PROTEIN- 601751 none found COUPLED RECEPTOR 24; GPR24 Glucagon J04040 138030 Dinucleotide repeat glucagon NM_0001 138033 Alu-repeat receptor/GCGR 60 glucagon NM_0001 138033 GLY40SER receptor/GCGR 60 glucagon-like peptide 1 UOI 156 138032 silent substitution in receptor/GLPIR exon 6 glucagon-like peptide 1 UOI 156 138032 simple tandem receptor/GLPIR repeat DNA polymoφhism glucagon-like peptide 2 603659 none found receptor/GLP2R glucocorticoid receptor M 1050 138040 4-BP DEL 2 bases of the exon and the first 2 SD-144141.1 Page 143 nucleotides of intron 6 glucocorticoid receptor Ml 1050 138040 A to G 3'-splice frameshift junction of intron G glucocorticoid receptor Ml 1050 138040 Base-pair deletion in 32 amino acid exon 9 deletion glucocorticoid receptor Ml 1050 138040 Bell glucocorticoid receptor Ml 1050 138040 T insertion 1188 and frameshift 1189 glucocorticoid receptor Ml 1050 138040 trinucleotide Arg453 insertion glucocorticoid receptor Ml 1050 138040 Tthllll glucocorticoid receptor Ml 1050 138040 LEU753PHE glucocorticoid receptor M 1 1050 138040 CYS736SER glucocorticoid receptor Ml 1050 138040 CYS736THR glucocorticoid receptor Ml 1050 138040 ILE747THR glucocorticoid receptor M 1 1050 138040 ASP641 VAL glucocorticoid receptor M 1 1050 138040 L753F glucocorticoid receptor Ml 1050 138040 Q710X glucocorticoid receptor Ml 1050 138040 ASN363SER glucocorticoid receptor U25029 138040 none found alpha glucocorticoid receptor X03348 138040 none found beta GLUCOCORTICOID 601993 none found RECEPTOR- INTERACTING PROTEIN 1 glycogen synthase S70004 138571 1VS6, G-C, +1 [human, liver, mRNA, 2912 nt] SD-144141.1 Page 143 glycogen synthase S70004 138571 ALA339PRO [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 ARG246TER [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 ASN39SER [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 HIS446ASP [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 MET491ARG [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 SER483PRO [human, liver, mRNA, 2912 nt] glycogen synthase S70004 138571 PRO479GLN [human, liver, mRNA, 2912 nt] gonadotropin releasing NM_0004 138850 ARG262GLN hormone receptor/G 06 protein- coupled/LHRHR/GNR HR gonadotropin releasing NM_0004 138850 GLN106ARG hormone receptor/G 06 protein- coupled/LHRHR/GNR HR SD-144141.1 Page 1440 gonadotropin releasing NM 0004 138850 TYR284CYS hormone receptor/G 06 protein- coupled/LHRHR/GNR HR gonadotropin releasing NM 0004 138850 Mae III hormone receptor/G 06 protein- coupled/LHRHR/GNR HR Gonadotropin-releasing M12578 152760 none found hormone (leutinizing- rel easing hormone) GROWTH FACTOR 108355 none found RECEPTOR-BOUND PROTEIN 2; GRB2 Growth hormone 1 V00519 139250 G-T, +1 intron 4 Growth hoπnone 1 V00519 139250 1-BP DEL, 371 C Growth hormone 1 V00519 139250 18-BP DEL, +28-45 intron 3 Growth hormone 1 V00519 139250 2-BP DEL FS132TER Growth hormone 1 V00519 139250 6.7-KB DEL Growth hormone 1 V00519 139250 BgHI Growth hormone 1 V00519 139250 G-A, +1 intron 3 Growth hormone 1 V00519 139250 G-A, +28 Growth hormone 1 V00519 139250 G-C, +1 intron 3 Growth hormone 1 V00519 139250 G-C, +1 intron 4 Growth hormone 1 V00519 139250 Hindi Growth hormone 1 V00519 139250 Mspl Growth hormone 1 V00519 139250 T-C, +6 intron 3 Growth hormone 1 V00519 139250 ARG77CYS SD-144141.1 Page 144 Growth hormone 1 V00519 139250 ASP112GLY Growth hormone 1 V00519 139250 TRP20TER Growth hormone X06562 600946 none found receptor growth hormone U34195 139191 IVS8DS, G-C, -1 alternative releasing hormone splice receptor/G protein- coup led/GHRHR growth hormone U34195 139191 1-BP DEL frameshift releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 2-BP DEL frameshift releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 C to T codon 236. silent releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 EX4,6DEL releasing hormone receptor/G protein- coup led/GHRHR growth hormone U34195 139191 GAA180GAG silent releasing hormone receptor/G protei ii- coupled/GHRHR growth hoπnone U34195 139191 IVS4DS, G-A, +1 alternative releasing hormone splice receptor/G protein- SD-144141.1 Page 144 coupled/GHRHR growth hormone U34195 139191 IVS6AS, G-T, -1 releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 IVS8AS, G-C, -1 releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 IVS9DS, G-A, +1 frameshift releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 ARG 161 CYS releasing hormone receptor/G protein- coup 1 ed/GHRHR growth hoπnone U34195 139191 GLU224ASP releasing hormone receptor/G protein- coupled/GHRHR growth hoπnone U34195 139191 GLU44LYS releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 PHE96SER releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 ASP152HIS releasing hormone SD- 144141 1 Page 1443 receptor/G protein- coupled/GHRHR growth hormone U34195 139191 GLN154PRO releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 ILE153THR releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 VAL155GLY releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 VAL144ILE releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 PRO131GLN releasing hormone receptor/G protein- couplcd/GHRHR growth hormone U34195 139191 GLU224TER releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 P561T releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 ARG217TER SD-144141.1 Page 1444 releasing homione receptor/G protein- coupled/GHRHR growth hormone U34195 139191 ARG43TER releasing hormone receptor/G protein- coupled/GHRHR growth hormone U34195 139191 CYS38TER releasing hoπnone receptor/G protein- coupled/GHRHR growth honnone- L29177 none found releasing factor (GRF) Guanylate cyclase 1, X63282 601244 none found soluble, alpha 2 Guanylate cyclase X66534 139396 none found soluble, alpha-3 chain Guanylate cyclase X66533 139397 none found soluble, beta-1 chain H.sapiens ACTH-R X65633 202200 C818A gene for adrenocorticotropic hormone receptor H.sapiens ACTH-R X65633 202200 Ser74Ile gene for adrenocorticotropic hormone receptor H.sapiens ALK-3 Z22535 601299 none found mRNA H . sapi ens encoding X64810 162150 IVS5DS, A-C, +4 PC1/PC3 SD-144141.1 Page 144 H.sapiens encoding X64810 162150 GLY483ARG PC1/PC3 H.sapiens HNF4 X76930 600281 1-BP DEL PHE75T mRNA for hepatocyte nuclear factor 4 H.sapiens HNF4 X76930 600281 GLN268TER mRNA for hepatocyte nuclear factor 4 H.sapiens HNF4 X76930 600281 ARG154TER mRNA for hepatocyte nuclear factor 4 H.sapiens HNF4 X76930 600281 ARG127TRP mRNA for hepatocyte nuclear factor 4 H.sapiens HNF4 X76930 600281 VAL393ILE mRNA for hepatocyte nuclear factor 4 H.sapiens HNF4 X76930 600281 Val/Met255 mRNA for hepatocyte nuclear factor 4 H.sapiens IL-1 R2 X59770 14781 1 none found mRNA for type II interleukin-1 receptor, (cell line CB23) H.sapiens mRNA for X87159 600760 1-BP INS, 592C beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 32-BP DEL beta subunit of SD-144141.1 Page 1446 epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 ARG564TER beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 PRO616LEU beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 GLY37SER beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 TYR618HIS beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for X87159 600760 PRO615SER beta subunit of epithelial amiloride- sensitive sodium channel H.sapiens mRNA for Y10319 212138 -BP INS frameshift camitine carrier H.sapiens mRNA for Y10319 212138 110-BP DEL SD-144141.1 Page 144 camitine carrier H.sapiens mRNA for Y10319 212138 128-BP DEL camitine carrier H.sapiens mRNA for Y10319 212138 ARG166TER camitine carrier H.sapiens mRNA for X82153 601 105 TER330TRP cathepsin O H.sapiens mRNA for X82153 601 105 GLY146ARG cathepsin O H.sapiens mRNA for X82153 601105 ARG241TER cathepsin O H.sapiens mRNA for X82153 601105 ALA277VAL cathepsin O H.sapiens mRNA for X77383 600550 none found cathepsin-O H.sapiens mRNA for Yl 1525 1 16897 none found CCAAT/enhancer binding protein alpha H.sapiens mRNA for X95520 602047 1389 (A/G) cyclic nucleotide phosphodiesterase H.sapiens mRNA for X95520 602047 dinucleotide repeat cyclic nucleotide introns 12 phosphodiesterase H.sapiens mRNA for X95520 602047 dinucleotide repeat cyclic nucleotide introns 5 phosphodiesterase H.sapiens mRNA for X87160 600761 none found gamma subunit of epithelial amiloride- sensitive sodium SD-144141.1 Page 144 O 73 73 o C u H U U ro 3 Λ Λ uo o ft CN Os -2 H ro < CN n c VO o ft" o uo < O o ω c G • t Q ft CN CN CN o o o CN ro ro o o oo o o o oo VO o o uo uo CN uo uo o uo OO oo oo r~- r- N X X X X X X protein H.sapiens mRNA for X75500 157147 IVS, G-A, +5 microsomal triglyceride transfer protein H.sapiens mRNA for X75500 157147 IVS9AS, G-A, -1 microsomal triglyceride transfer protein H.sapiens mRNA for X75500 157147 ARG215TER microsomal triglyceride transfer protein H.sapiens mRNA for X68596 168468 33-BP DEL parathyroid hormone receptor H.sapiens mRNA for X68596 168468 HIS223ARG parathyroid hormone receptor H.sapiens mRNA for X68596 168468 THR410PRO parathyroid hormone receptor H.sapiens mRNA for X68596 168468 ARG383GLN parathyroid hormone receptor H.sapiens mRNA for X68596 168468 PRO132LEU parathyroid hormone receptor H.sapiens mRNA for X92720 261650 none found phosphoenolpyruvate carboxykinase SD- 144141. Page 145 H.sapiens M77844 106210 IVS 12DS, G-C, -1 oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 2-BP INS oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 dinucleotide repeat oculorhombin promoter (aniridia) mRNA, complete cds H.sapiens 77844 106210 EXON G DEL oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 IVS10AS, A-T, -2 oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 IVSl lDS, A-G, -2 oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 ARG103TER oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 SER353TER oculorhombin (aniridia) mRNA, SD-144141.1 Page 1451 complete cds H.sapiens M77844 106210 ARG26GLY oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 I29V oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 N17S oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 Q178H oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 R44Q oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 Q422R oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 ARG203TER oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 ARG240TER oculorhombin SD- 144141 1 Page 1452 (aniridia) mRNA, complete cds H.sapiens M77844 106210 GLY64VAL oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 VAL 126 ASP oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 GLN1 16TER oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 I87R oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 ARG125CYS oculorhombin (aniridia) mRNA, complete cds H.sapiens M77844 106210 VAL54ASP oculorhombin (aniridia) mRNA, complete cds H.sapiens PPP1R3 X78578 600917 5-BP INS/DEL 3'UTR mRNA for protein phosphatase 1, glycogen-binding regulatory subunit SD- 144141.1 Page 1453 H.sapiens PPP1 R3 X78578 600917 ASP905TYR mRNA for protein phosphatase 1, glycogen-binding regulatory subunit HEPATOCYTE 600288 none found NUCLEAR FACTOR 3-BETA; HNF3B HEPATOCYTE 602295 none found NUCLEAR FACTOR 3-GAMMA; HNF3G HEPATOCYTE 604164 none found NUCLEAR FACTOR 6 HMG CoA synthase U12789 600234 none found (HSH1) mitochondrial HMG CoA synthase X66435 142940 none found soluble HMGCoA NM 0008 142910 HgiAI reductase/HMGCR 59 HMGCoA NM 0008 142910 ScrFI polymorphism reductase/HMGCR 59 ini the 2nd intron Homo sapiens (clone L05144 261680 none found lamda-hPEC-3) phosphoenolpyruvate carboxykinase (PCK1) mRNA, complete cds Homo sapiens (clone L40992 600211 16-BP INS PEBP2aAl) core- binding factor, runt domain, alpha subunit SD- 144141 1 Page 145 1 (CBFAl) mRNA, 3' end of cds Homo sapiens (clone L40992 600211 ALA REPEAT PEBP2aAl) core- binding factor, runt domain, alpha subunit 1 (CBFAl ) mRNA, 3' end of cds Homo sapiens (clone L40992 60021 1 MET 175 ARG PEBP2aAl) core- binding factor, runt domain, alpha subunit 1 (CBFAl) mRNA, 3' end of cds Homo sapiens (clone L40992 600211 SER191ASN PEBP2aAl) core- binding factor, runt domain, alpha subunit 1 (CBFAl ) mRNA, 3' end of cds Homo sapiens (clone L40992 600211 TRP283TER PEBP2aAl) core- binding factor, runt domain, alpha subunit 1 (CBFAl) mRNA, 3' end of cds Homo sapiens acyl- AF030555 300157 none found CoA synthetase 4 (ACS4) mRNA, complete cds Homo sapiens low M28219 143890 ATn SD-144141.1 Page 1455 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX2-6DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 -19(CGG)n density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 1 -BP DEL, 197G density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 1061-8T->C density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ! 650delG frameshift density lipoprotein SD-144141.1 Page 145 receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 165delG density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 18-BP DUP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 1846-1 G->A density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 2-BP DEL, 694AC density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 2199delCA density lipoprotein receptor (FH 10 mutant SD-144141.1 Page 145 causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 2201delCA density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 313 + 1G->A density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 335dell 0 frameshift density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 347delGCC density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 4-BP INS, EX8 frameshift density lipoprotein receptor (FH 10 mutant causing familial SD-144141.1 Page 1458 hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 7-BP DEL frameshift density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 785insG density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 9-BP DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 AGG450AGA silent density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C766T density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) SD-144141.1 Page 1459 mRNA, 3 end Homo sapiens low M28219 143890 EX13-14DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX13-15DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX13-15DUP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX15DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX16-17DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end SD- 144141.1 Page 1460 Homo sapiens low M28219 143890 EX16-18DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX16DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX17-18DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX17DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX2-12DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX2-3DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX2-5DUP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX2-8DUP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX3-8DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX4-6DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX5DEL density lipoprotein SD-144141 Page 1462 receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX7-14DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX7-8DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX7DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX9-10DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 EX9DUP density lipoprotein receptor (FH 10 mutant SD-144141.1 Page 1463 causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Hhal intron 9 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Hindi density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 IVS3, G-A, +1 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 IVS4, T-C, +2 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 null allele density lipoprotein receptor (FH 10 mutant causing familial SD- 144141.1 Page 1464 hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 PvuII density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Stul density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 T -> A28 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ALA410THR density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 VAL502MET density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) SD-144141-1 Page 146 mRNA, 3 end Homo sapiens low M28219 143890 ASP283ASN density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY27DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLU207LYS density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 D154N density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 D206E density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end SD-144141.1 Page 1466 Homo sapiens low M28219 143890 V408M density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY197DEL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C127W density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C139G density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 E397X density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLN12TER SD-144141.1 Page 1467 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY525ASP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY528ASP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 CYS163TYR density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ASP206GLU density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 CYS646TYR density lipoprotein SD-144141.1 Page 1468 receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 TRP66GLY density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 SER156LEU density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY544VAL density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 R329X density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ASN543HIS density lipoprotein receptor (FH 10 mutant SD-144141 - 1 Page 1469 causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ASP154ASN density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 N543H density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Glul l 9-Lys density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C152R density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 T705I density lipoprotein receptor (FH 10 mutant causing familial SD-144141.1 Page 1470 hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Cys297->Phe density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 aspl47his density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Trp469Stop density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 ASP412HIS density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 PR0664LEU density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) SD-144141.1 Page 1471 mRNA, 3 end Homo sapiens low M28219 143890 Ala370->Thr density lipoprotein receptor (FH 10 mutant causing familial hyperch Homo sapiens low M28219 143890 C356->Y density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 CYS240PHE density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Asp200->Gly density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C122X density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end SD-144141.1 Page 1472 Homo sapiens low M28219 143890 Pro84->Ser density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 pro6641eu density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Cys646->Tyr density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Glu207->Lys density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 Trp66-->Gly density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 CYS660TER SD- 144141.1 Page 1473 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 TYR807CYS density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 TRP792TER density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 CYS210TER density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 GLY823ASP density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 LEU380HIS density lipoprotein SD- 144141.1 Page 1474 receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 TYR167TER density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 VAL408MET density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 C331C density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 E1 19-K density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 N494 N density lipoprotein receptor (FH 10 mutant SD-144141.1 Page 1475 causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 T383P density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 T7051 density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 W23X density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 W556S density lipoprotein receptor (FH 10 mutant causing familial hypercholesterolemia) mRNA, 3 end Homo sapiens low M28219 143890 W66G density lipoprotein receptor (FH 10 mutant causing familial SD-144141.1 Page 147 hypercholesterolemia) mRNA, 3 end Homo sapiens mRNA D89053 602371 none found for Acyl-CoA synthetase 3, complete cds Homo sapiens mRNA AB006590 601663 none found for estrogen receptor beta, complete cds Homo sapiens mRNA AB005293 170290 none found for perilipin, complete cds Homo sapiens mRNA AJ006276 603652 none found for transient receptor potential protein TRP6 Homo sapiens mRNA D88308 603247 none found for very-long-chain acyl-CoA synthetase, complete cds Homo sapiens muscle AF066859 232600 IVS 14, G-A, +1 , 67- glycogen BP DEL phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 ARG49TER glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 GLY204SER glycogen SD-144141.1 Page 147 phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 LYS542THR glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 METiGLY glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 GLU654LYS glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 LEU396PRO glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 GLY685ARG glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 ARG575TER glycogen phosphorylase SD-144141.1 Page 147 (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 GLN665GLU glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 LYS753, DEL glycogen A phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 METiVAL glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens muscle AF066859 232600 GLU540TER glycogen phosphorylase (PYGM) mRNA, complete cds Homo sapiens L07833 182454 none found somatostatin receptor (SSTR4) gene, complete cds Homo sapiens sorbitol U07361 182500 none found dehydrogenase gene, complete cds HOMOLOG OF 600725 GLY31ARG SONIC HEDGEHOG SD-144141.1 Page 147 HOMOLOG OF 600725 GLNIOOTER SONIC HEDGEHOG HOMOLOG OF 600725 LYS105TER SONIC HEDGEHOG HOMOLOG OF 600725 TRP117GLY SONIC HEDGEHOG HOMOLOG OF 600725 TRP1 17ARG SONIC HEDGEHOG Human (HepG2) K03195 138140 GCT15GCC silent glucose transporter gene mRNA, complete cds Human (HepG2) K03195 138140 Xbal glucose transporter gene mRNA, complete cds Human (HepG2) K03195 138140 DEL glucose transporter gene mRNA, complete cds Human (HepG2) K03195 138140 LYS456TER glucose transporter gene mRNA, complete cds Human (HepG2) K03195 138140 TYR449TER glucose transporter gene mRNA, complete cds Human activin LI 1695 190181 S387Y receptor-like kinase (ALK-5) mRNA, SD-144141.1 Page 14 complete cds Human bek mRNA for X52832 176943 ALU INS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 CYS342TYR fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 CYS342ARG fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 CYS342SER fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TYR340HIS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 SER354CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 ALA344ALA fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 ALA344GLY fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TYR328CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 SER347CYS fibroblast growth factor receptor-BEK SD-144141.1 Page 14 Human bek mRNA for X52832 176943 SER252TRP fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 PRO253ARG fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 THR341PRO fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 CYS342TRP fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 GLN289PRO fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TYR375CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 SER372CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 SER252PHE fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 PRO253SER fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TRP290CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 LYS292GLU SD-144141.1 Page 148 fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TRP290ARG fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TRP290GLY fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 LYS292GLU fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TRP290ARG fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 TRP290GLY fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 VAL-VAL fibroblast growth factor DEL receptor-BEK Human bek mRNA for X52832 176943 SER351CYS fibroblast growth factor receptor-BEK Human bek mRNA for X52832 176943 SER252PHE fibroblast growth factor receptor-BEK Human beta-LH gene X00264 152780 ILE15THR (luteinizing hormone gene beta subunit) Human beta-LH gene X00264 152780 TRP8ARG (luteinizing hormone SD-144141.1 Page 1483 gene beta subunit) Human beta-LH gene X00264 152780 GLN54ARG (luteinizing hormone gene beta subunit) Human brain glycogen J03544 138550 none found phosphorylase mRNA, complete cds Human c-erb- A mRNA X04707 190160 1-BP INS, CODON frameshift for thyroid hormone 443 receptor Human c-erb- A mRNA X04707 190160 1305G-C for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 C1644i frameshift for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 EX4-10DEL for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 Hindlll for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 VAL458ALA for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 R338L for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLY340ARG for thyroid hormone receptor SD-144141.1 Page 148 Human c-erb-A mRNA X04707 190160 ALA229THR for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 THR332DEL for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG383HIS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 LYS438GLU for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLY340SER for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG320LEU for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG311HIS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG438HIS for thyroid homione receptor Human c-erb-A mRNA X04707 190160 ARG320CYS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG338TRP for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ALA312THR SD-144141.1 Page 1485 for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLY327ARG for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLY340VAL for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLY342GLU for thyroid hoπnone receptor Human c-erb-A mRNA X04707 190160 MET437VAL for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 PRO448THR for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 PRO448HIS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 THR337ALA for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 CYS434TER for thyroid hoπnone receptor Human c-erb-A mRNA X04707 190160 CYS446ARG for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 LEU445HIS for thyroid hormone SD- 144141 Page 1486 receptor Human c-erb-A mRNA X04707 190160 GLY340ASP for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 GLN335HIS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 pro453ser for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 R316H for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 met313thre for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 L346V for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 MET310THR for thyroid homione receptor Human c-erb-A mRNA X04707 19 160 LEU325PHE for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG243GLN for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG243TRP for thyroid hormone receptor SD- 144141. Page 1487 Human c-erb-A mRNA X04707 190160 ASP317HIS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 PHE454CYS for thyroid hormone receptor Human c-erb-A mRNA X04707 190160 ARG315HIS for thyroid hormone receptor Human c-erbA-1 X55005 190120 LYS370ASN mRNA for thyroid hormone receptor alpha Human c-erb A- 1 X55005 190120 SER377LEU mRNA for thyroid hormone receptor alpha Human c-erb A- 1 X55005 190120 SER45ILE mRNA for thyroid homione receptor alpha Human cGMP- M91667 123805 none found inhibited cAMP phosphodiesterase mRNA, complete cds Human colipase J02883 120105 none found mRNA, complete cds Human collagen type L22548 120328 none found XVIII alpha 1 (COLI 8A1) mRNA, partial cds Human CYP1 1B2 gene D13752 124080 -344C/T for steroid 18- hydroxylase, complete SD-144141.1 Page 148 cds Human CYPl 1B2 gene D13752 124080 5-BP DEL frameshift for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 T4986C for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D 13752 124080 GLU198ASP for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 GLU255TER for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 LYS 173 ARG for steroid 18- hydroxylase, complete cds Human CYPl 1 B2 gene D13752 124080 THR185ILE for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 LEU461PRO for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D 13752 124080 ARG181TRP for steroid 18- SD-144141.1 Page 1489 hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 VAL386ALA for steroid 18- hydroxylase, complete cds Human CYPl 1B2 gene D13752 124080 T318M for steroid 18- hydroxylase, complete cds Human cytochrome M17252 201910 1761Tins P450c21 mRNA, 3' end Human cytochrome M17252 201910 C-G intron 2 P450c21 mRNA, 3' end Human cytochrome M17252 201910 DEL P450c21 mRNA, 3' end Human cytochrome M17252 201910 PvuII P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 TGC to AC P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 3-BP INS LEU10INS P450c21 mRNA, 3' end Human cytochrome M17252 201910 656 A->G P450c21 mRNA, 3' end Human cytochrome M17252 201910 8-BP DEL P450c21 mRNA, 3' end Human cytochrome Ml7252 201910 ClusterEό P450c21 mRNA, 3' end Human cytochrome M17252 201910 F306+t P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 G-T exon 7 SD-144141.1 Page 1490 P450c21 mRNA, 3' end Human cytochrome M17252 201910 GG dinucleotide to a P450c21 mRNA, 3' end C in exon 10 Human cytochrome M17252 201910 Haelll P450c21 mRNA, 3' end Human cytochrome M17252 201910 IVS2AS A/C-G, -13 P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 IVS7DS, G-C, +1 P450c21 mRNA, 3' end Human cytochrome M17252 201910 Ncol P450c21 mRNA, 3' end Human cytochrome M17252 201910 Rsa l P450c21 mRNA, 3' end Human cytochrome M17252 201910 T-A exon 4 P450c21 mRNA, 3' end Human cytochrome M17252 201910 ILE 172 ASN P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 VAL281 LEU P450c21 mRNA, 3' end Human cytochrome M l 7252 201910 PRO30LEU P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 SER268THR P450c21 mRNA, 3' end Human cytochrome M17252 201910 GLY292SER P450c21 mRNA, 3' end Human cytochrome M17252 201910 PRO453SER P450c21 mRNA, 3' end Human cytochrome M17252 201910 TYR 102 ARG P450c21 mRNA, 3' end Human cytochrome M17252 201910 ILE235ASN P450c21 mRNA, 3' end SD-144141.1 Page 149 Human cytochrome M17252 201910 VAL236GLU P450c21 mRNA, 3' end Human cytochrome Ml7252 201910 MET238LYS P450c21 mRNA, 3' end Human cytochrome Ml7252 201910 GLN318TER P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 ARG339HIS P450c21 mRNA, 3' end Human cytochrome M17252 201910 TRP406TER P450c21 mRNA, 3' end Human cytochrome M17252 201910 GLU380ASP P450c21 mRNA, 3' end Human cytochrome M17252 201910 Q318X P450c21 mRNA, 3' end Human cytochrome M17252 201910 R356W P450c21 mRNA, 3' end Human cytochrome M17252 201910 I236N P450c21 mRNA, 3' end Human cytochrome Ml 7252 201910 V237E P450c21 mRNA, 3' end Human cytochrome M17252 201910 M239K P450c21 mRNA, 3' end Human cytochrome M17252 201910 GLY524SER P450c21 mRNA, 3' end Human cytochrome M17252 201910 R356Q P450c21 mRNA, 3' end Human cytochrome Ml7252 201910 Y97X P450c21 mRNA, 3' end Human cytochrome Ml7252 201910 Arg357Trp P450c21 mRNA, 3' end Human cytochrome l7252 201910 D183E SD-144141.1 Page 1492 P450c21 mRNA, 3' end Human cytochrome M17252 201910 W23X P450c21 mRNA, 3' end Human fatty acid U26644 600212 none found synthase (fas) mRNA, complete cds Human gene for X52560 189965 none found nuclear factor NF-IL6 Human glucagon-like UOI 157 138032 none found peptide-1 receptor mRNA with CA dinucleotide repeat, complete cds Human heparin- M32977 192240 none found binding vascular endothelial growth factor (VEGF) mRNA, complete cds Human hepatic lipase J03540 151670 SER267PHE mRNA, complete cds Human hepatic lipase J03540 151670 THR383MET mRNA, complete cds Human hepatic nuclear M57732 142410 A-C, -58 factor 1 (TCF1) mRNA, complete cds, clones HCL10, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 -BP DEL frameshift factor 1 (TCF1) mRNA, complete cds, SD-144141.1 Page 149 clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 -BP INS frameshift factor 1 (TCF1 ) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 Rsal promoter factor 1 (TCF1) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 PR0447LEU factor 1 (TCF1 ) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 E619K factor 1 (TCF1) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 R537T factor 1 (TCF1) mRNA, complete cds, clones HCL10, SD-144141.1 Page 149 HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 Ala/Val98 factor 1 (TCF1) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 TYR122CYS factor 1 (TCF1) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 THR620ILE factor 1 (TCF1) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 Gly574Ser factor 1 (TCF1) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 Cys241Gly factor 1 (TCF1 ) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and SD-144141 - Page 1495 HCL20 Human hepatic nuclear M57732 142410 Glu48Lys factor 1 (TCFl) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 Pro291fsdelA factor 1 (TCFl) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 ARG272HIS factor 1 (TCFl ) mRNA, complete cds, clones HCLI O, HCL12, HCL1 7, and HCL20 Human hepatic nuclear M57732 142410 ARG583GLY factor 1 (TCFl) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human -hepatic nuclear M57732 142410 K205Q factor 1 (TCFl ) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 SD-144141.1 Page 1496 Human hepatic nuclear M57732 142410 R131Q factor 1 (TCFl) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 T392fsdelA factor 1 (TCFl) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 L12H factor 1 (TCFl) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 L584S585fsinsT factor 1 (TCFl) C mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 P379fsdelCT factor 1 (TCFl ) mRNA, complete cds, clones HCL10, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 R263C SD- 144141 Page 1497 factor 1 (TCFl) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 G191D factor 1 (TCFl) mRNA, complete cds, clones HCLIO, HCL12, HCL17, and HCL20 Human hepatic nuclear M57732 142410 GLY319SER factor 1 (TCFl) mRNA, complete cds, clones HCLI O, HCL12, HCL17, and HCL20 Human hepatocyte U39840 602294 none found nuclear factor-3 alpha (HNF-3 alpha) mRNA, complete cds Human hormone- U40002 151750 dinucleotide repeat sensitive lipase testicular isoform mRNA, complete cds Human hormone- U40002 151750 Arg309Cys sensitive lipase testicular isoform mRNA, complete cds Human HXC-26 D83260 601125 none found mRNA, complete cds SD-144141 Page 149 Human insulin U30329 600733 1 -BP DEL frameshift promoter factor 1 (IPFl) mRNA, complete cds Human insulin- M21188 146680 none found degrading enzyme (IDE) mRNA, complete cds Human insulin- M20747 138190 VAL383ILE responsive glucose transporter (GLUT4) mRNA, complete cds Human liver glycogen M36807 232700 IVS13DS, G-A, +1 phosphorylase type IV mRNA, 3' end Human liver glycogen M36807 232700 IVS14DS, G-A, +1 phosphorylase type IV mRNA, 3' end Human liver glycogen M36807 232700 IVS4AS, G-C, -1 phosphorylase type IV mRNA, 3' end Human liver glycogen M36807 232700 ASN338SER phosphorylase type IV mRNA, 3' end Human liver glycogen M36807 232700 ASN376LYS phosphorylase type IV mRNA, 3' end Human liver glycogen M36807 232700 VAL221ILE phosphorylase type IV mRNA, 3' end Human long-chain L09229 152425 A— >T new initiation SD-144141.1 Page 149 acyl-coenzyme A codon +18 synthetase (FACL1) amino acids mRNA, complete cds Human luteinizing M63108 152790 6-BP DEL, NT1822 hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 LEU-GLN INS, hoπnone- CODON 19-20 choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 SER616TYR hoπnone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ARG554TER hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ALA593PRO hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ASP578GLY hormone- choriogonadrotropin SD-144141.1 Page 150 receptor mRNA, complete cds Human luteinizing M63108 152790 ILE625LYS hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ILE542LEU hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ALA373VAL hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 GLU354LYS hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ARG133CYS hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ASP578GLY hormone- choriogonadrotropin receptor mRNA, SD-144141.1 Page 1501 complete cds Human luteinizing M63108 152790 ALA572VAL hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 THR577ILE hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 ASP582GLY hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 MET575ILE hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 MET398THR hormone- choriogonadrotropin receptor mRNA, complete cds Human luteinizing M63108 152790 CYS545TER hormone- choriogonadrotropin receptor mRNA, complete cds SD-144141.1 Page 1502 Human U60475 307800 2-BP DEL frameshift metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 A-G, NT-429 metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 IVS IAS, G-A, metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 IVS 1 AS, G-C, -1 metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 LEU555PRO metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 CYS82TYR metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 LEU274TER metalloendopeptidase homolog (PEX) mRNA, partial cds Human U60475 307800 MET250ILE metalloendopeptidase homolog (PEX) SD-144141.1 Page 150 mRNA, partial cds Human U60475 307800 PHE249SER metalloendopeptidase homolog (PEX) mRNA, partial cds Human molecular M90439 172860 G to A 5 marker (EPC-1) gene, complete cds Human molecular M90439 172860 Met72Thr marker (EPC-1) gene, complete cds Human molecular M90439 172860 Thrl30Thr marker (EPC-1) gene, complete cds Human molecular M90439 172860 Tyr321Tyr marker (EPC-1) gene, complete cds Human mRNA for D49488 600415 1-BP DEL 744 alpha-tocopherol transfer protein, complete cds Human mRNA for D49488 600415 1-BP DEL, 485T frameshift alpha-tocopherol transfer protein, complete cds Human mRNA for D49488 600415 2-BP INS, 513TT alpha-tocopherol transfer protein, complete cds Human mRNA for D49488 600415 552G-A alpha-tocopherol SD-144141.1 Page 150 transfer protein, complete cds Human mRNA for D49488 600415 HIS101GLN alpha-tocopherol transfer protein, complete cds Human mRNA for D49488 600415 ARG192HIS alpha-tocopherol transfer protein, complete cds Human mRNA for D49488 600415 ARG134TER alpha-tocopherol transfer protein, complete cds Human mRNA for X51405 114855 none found carboxypeptidase E (EC 3.4.17.10) Human mRNA for X55764 202010 2-BP INS, CODON frameshift cytochrome P-450 ( 1 1 394 Beta) Human mRNA for X55764 202010 28bp deletion cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 5 bp duplication cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 CHIMERA cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 Mspl cytochrome P-450 (1 1 SD-144141.1 Page 150 Beta) Human mRNA for X55764 202010 PvuII cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 ARG448HIS cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 TRP1 16TER cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 N133H cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 P42S cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 Y423X cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 arg384gly cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 ARG374GLN cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 THR318MET cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 C494F cytochrome P-450 (11 Beta) SD-144141.1 Page 150 Human mRNA for X55764 202010 G267D cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 G267R cytochrome P-450 (1 1 Beta) Human mRNA for X55764 202010 Q356X cytochrome P-450 (11 Beta) Human mRNA for X55764 202010 R427H cytochrome P-450 (11 Beta) Human mRNA for Y00083 190220 none found glioblastoma-derived T-cell suppressor factor G-TsF (transforming growth factor-beta2, TGF-beta2) Human mRNA for X05199 173350 IVS 17, 1 -BP DEL, plasminogen G, +l Human mRNA for X05199 173350 Taql plasminogen Human mRNA for X05199 173350 GLU460TER plasminogen Human mRNA for X05199 173350 ALA600THR plasminogen Human mRNA for X05199 173350 ARG216HIS plasminogen Human mRNA for X05199 173350 GLY732ARG plasminogen Human mRNA for X05199 173350 LYS19GLU SD-144141.1 Page 150 plasminogen Human mRNA for X05199 173350 LYS212DEL plasminogen Human mRNA for X05199 173350 SER572PRO plasminogen Human mRNA for X0 199 173350 TRP597TER plasminogen Human mRNA for X05199 173350 VAL355PHE plasminogen Human mRNA for X05199 173350 D676N plasminogen Human mRNA for X05199 173350 Ala675Thr plasminogen Human mRNA for X02812 190180 713-8delC transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 713-8delC Leul0->Pro transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 713-8delC Arg25->Pro transforming growth factor-beta (TGF-beta) Human mRNA for X14149 190230 none found transforming growth factor-beta 3 (TGF- beta 3) Human mRNA for X58840 189907 75-BP DEL, NT409 variant hepatic nuclear factor 1 (vHNFl ) Human mRNA for X58840 189907 ARG177TER variant hepatic nuclear SD-144141.1 Page 150 factor 1 (vHNFl) Human mRNA X02404 1 14160 none found fragment for second calcitonin gene related peptide (CGRP) from medullary thyroid carcinoma (MTC) Human mrRNA for X12451 116880 none found pro-cathepsin L (major excreted protein MEP) Human muscle J04501 138570 TTC342TTT glycogen synthase mRNA, complete cds Human muscle J04501 138570 Gln71His glycogen synthase mRNA, complete cds Human muscle J04501 138570 Gly464Ser glycogen synthase mRNA, complete cds Human muscle J04501 138570 Met416Val glycogen synthase mRNA, complete cds Human myeloid- U80982 600749 none found specific C/EBP-epsilon transcription factor (CEBPE) gene, complete cds Human neurokinin A M57414 162321 none found receptor (NK-2R) mRNA, complete cds Human NF-IL6-beta M83667 116898 none found SD- 144141 .1 Pas_,e 1509 protein mRNA, complete cds Human obese (ob) U18915 164160 -1387 G/A mRNA, complete cds Human obese (ob) U18915 164160 1-BP DEL frameshift mRNA, complete cds Human obese (ob) U18915 164160 A --> G + 19 exonl mRNA, complete cds Human obese (ob) U18915 164160 C(-188)A mRNA, complete cds Human obese (ob) U18915 164160 ARG105TRP mRNA, complete cds Human obese (ob) U18915 164160 Glu-126-Gln mRNA, complete cds Human obese (ob) U18915 164160 Ser-91 -Ser mRNA, complete cds Human pancreatic M88011 138079 CCC[Pro]~ beta-cell glucokinase >CCG[Pro] at codon mRNA, complete cds 145 Human pancreatic M88011 138079 intron 1 a variant beta-cell glucokinase (C->T) mRNA, complete cds Human pancreatic M8801 1 138079 (-258) G-to-A beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 (TAC->TAT) in beta-cell glucokinase codon 215 mRNA, complete cds Human pancreatic M88011 138079 -120 (G->T) beta-cell glucokinase mRNA, complete cds SD- 144141. 1 Page 15 1 Human pancreatic M8801 1 138079 •194 (A-->G) beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 -282 (C->T) beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 -30 G/A beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 10-bp (base pair) beta-cell glucokinase deletion in exon 3; mRNA, complete cds Human pancreatic M8801 1 138079 33-bp deletion at the beta-cell glucokinase exon 5/intron 5 mRNA, complete cds junction Human pancreatic M88011 138079 403 (C->G) beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 603 (G->T beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 A~> G 244 beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 C-> T 8 bp 3' to the beta-cell glucokinase exon 9 mRNA, complete cds Human pancreatic M88011 138079 compound imperfect beta-cell glucokinase dinucleotide repeat mRNA, complete cds Human pancreatic M88011 138079 G--> A 13 SD- 144141.1 Page 151 beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 IVS4DS, 15-BP beta-cell glucokinase DEL mRNA, complete cds Human pancreatic M88011 138079 TGG257->CGG257 beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 ARG186TER beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 GLU265TER beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 GLU279TER beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 GLY261ARG beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 GLY299ARG beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 SER131 PRO beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 THR228MET beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 VAL455MET beta-cell glucokinase SD- 144141.1 Page 151 mRNA, complete cds Human pancreatic M8801 1 138079 Val62Ala beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Thr209- beta-cell glucokinase >Met209 mRNA, complete cds Human pancreatic M88011 138079 Gly261- beta-cell glucokinase >Glu261 mRNA, complete cds Human pancreatic M8801 1 138079 Arg36~>Trp36 beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Glu70->Lys beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Serl31->Pro beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Alal 88->Thr beta-cell glucokinase mRNA, complete cds Human pancreatic M8801 1 138079 Trp257-->Arg beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Lys414->Glu beta-cell glucokinase mRNA, complete cds Human pancreatic M88011 138079 Asp4->Asn beta-cell glucokinase mRNA, complete cds SD-144141.1 Page 1513 Human pancreatic M88011 138079 Ala 11 Thr beta-cell glucokinase mRNA, complete cds Human parathyroid cell U20759 601199 (CA)n calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 2-BP DEL/1 -BP INS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 ALU INS, CODON calcium-sensing 877 receptor mRNA, complete cds Human parathyroid cell U20759 601199 T/C fifth intron calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 ARG796TRP calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 GLU298LYS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 ARG185GLN calcium-sensing receptor mRNA, complete cds SD- 144141.1 Page 151 Human parathyroid cell U20759 601199 GLU 128 ALA calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 ARG227LEU calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 CYS582TYR calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 GLU681HIS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 ALA1 16THR calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 PHE806SER calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 THR151MET calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 ASN1 18LYS calcium-sensing receptor mRNA, SD-144141.1 Page 1515 complete cds Human parathyroid cell U20759 601199 PHE128LEU calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 THR151MET calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 GLU191LYS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 PHE612SER calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 LEU773ARG calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 ARG185TER calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 GLY670GLU calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 PRO40ALA calcium-sensing SD-144141.1 Page 1516 receptor mRNA, complete cds Human parathyroid cell U20759 601199 ARG228GLN calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 THR139MET calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 GLY144GLU calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 ARG63MET calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 ARG67CYS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 PHE788CYS calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601 199 LYS47ASN calcium-sensing receptor mRNA, complete cds Human parathyroid cell U20759 601199 A986S SD-144141.1 Page 1517 calcium-sensing receptor mRNA, complete cds Human patched U43148 601309 1 148G-A homolog (PTC) mRNA, complete cds Human patched U43148 601309 1 -BP DEL homolog (PTC) mRNA, complete cds Human patched U43148 601309 1-BP INS homolog (PTC) mRNA, complete cds Human patched U43148 601309 11-BP DEL frameshift homolog (PTC) mRNA, complete cds Human patched U43148 601309 2-BP PNS homolog (PTC) mRNA, complete cds Human patched U43148 601309 3340A-T homolog (PTC) mRNA, complete cds Human patched U43148 601309 37-BP DEL homolog (PTC) mRNA, complete cds Human patched U43148 601309 451C-T Pro-Ser homolog (PTC) mRNA, complete cds Human patched U43148 601309 9-BP INS CODON 815, homolog (PTC) PRO-ASN-ILE mRNA, complete cds INS Human patched U43148 601309 CAG to TAG at nonsense SD-144141.1 Page 1518 homolog (PTC) codon 361 mRNA, complete cds Human patched U43148 601309 GLN210TER homolog (PTC) mRNA, complete cds Human patched U43148 601309 Gln816Leu homolog (PTC) mRNA, complete cds Human PTH2 U25128 601469 none found parathyroid hormone receptor mRNA, complete cds Human putative U47050 602345 none found calcium influx channel (htrp3) mRNA, complete cds Human receptor for M91211 600214 none found advanced glycosylation end products (RAGE) mRNA, partial cds Human serum vitamin M12654 139200 Haelll D-binding protein (hDBP) mRNA, complete cds Human serum vitamin M12654 139200 (TAAA)n D-binding protein (hDBP) mRNA, complete cds Human serum vitamin M12654 139200 Mspl D-binding protein (hDBP) mRNA, SD-144141.1 Page 1519 complete cds Human semm vitamin Ml 2654 139200 Styl D-binding protein (hDBP) mRNA, complete cds H complete cds Human serum vitamin M12654 139200 THR420LYS D-binding protein (hDBP) mRNA, complete cds Human somatostatin I J00306 182450 BamHl intron gene and flanks Human somatostatin I J00306 182450 EcoRI 3' gene and flanks Human SREBP-1 U00968 184756 none found mRNA, complete cds Human stanniocalcin U46768 601185 none found mRNA, complete cds Human steroid 5-alpha- M74047 264600 1-BP DEL PRO251DEL reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 null allele reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 ARG246TRP reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY1 15ASP SD-144141.1 Page 1520 reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY183SER reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY196SER reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 HIS231ARG reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 LEU55GLN reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 MET157DEL reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 THR228ALA reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 ARG227TER reductase 2 (SRD5A2) mRNA, complete cds Human steroidogenic U17280 600617 840delA acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 ΓVS4AS, T-A, -I I acute regulatory protein (StAR) mRNA, complete cds SD-144141.1 Page 152 Human steroidogenic U17280 600617 GLN258TER acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 ARG182LEU acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 1-BP DEL, acute regulatory 261T protein (StAR) mRNA, complete cds Human steroidogenic U 17280 600617 IVS2, 1 -BP acute regulatory INS, T, +3 protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 D203A acute regulatory protein (StAR) mRNA, complete cds Human sterol U02031 600481 none found regulatory element binding protein-2 mRNA, complete cds Human transforming L07594 600742 none found growth factor-beta type III receptor (TGF-beta) mRNA, complete cds Human type II U53506 601413 none found iodothyronine deiodinase mRNA, SD-144141.1 Page 152 complete cds Human type II U20165 600799 none found serine/threonine kinase receptor mRNA, complete cds Human vascular U43142 601528 none found endothelial growth factor related protein VRP mRNA, complete cds Human VEGF related U43368 601398 none found factor isoform VRF186 precursor (VRF) mRNA, complete cds Hydroxy-delta-5- M67466 201810 1-BP PNS steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 Dinucleotide repeat steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 ARG249TER steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 VAL248ASN steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 TRP171TER SD-144141.1 Page 152 steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 hyrotropin beta (TSH- M21023 none found beta) IGF-2 receptor Y00285 147280 17 bp deletion IGF-2 receptor Y00285 147280 CA repeat polymoφhisms IGF-2 receptor Y00285 147280 Sad IGF-2 receptor Y00285 147280 Asn2020Ser IGF-2 receptor Y00285 147280 GLY 1449 VAL IGF-2 receptor Y00285 147280 GLY1464GLU Insulin receptor M10051 147670 10 base pair deletion Insulin receptor M10051 147670 1058 CAC->CAT silent Insulin receptor M10051 147670 12 additional base insertion Leu- pairs in exon 3 His-Leu-Val Insulin receptor M10051 147670 3' flanking intron (T- ->G at position 74) Insulin receptor M10051 147670 400-bp insertion intron Insulin receptor M l 0051 147670 8-BP DEL Insulin receptor M 10051 147670 A-G, -2 intron 4 Insulin receptor M 10051 147670 Alu lysl030 Insulin receptor M10051 147670 codon 1058 (CAC- silent >CAT) Insulin receptor M10051 147670 deletion of the gene Insulin receptor M10051 147670 EcoRI Insulin receptor M10051 147670 EX14DEL Insulin receptor M10051 147670 Four RSAI Insulin receptor M10051 147670 G— >T at position 13, 5' intron SD-144141.1 Page 152 Insulin receptor M10051 147670 Gln276 (CAA- silent >CAG) Insulin receptor Ml 0051 147670 Gly8 (GGA- ->GGG) silent Insulin receptor M10051 147670 Hisl068 ; (CAC- silent >CAT) Insulin receptor M10051 147670 Insertion intron 9, Insulin receptor Ml 0051 147670 Nsil Insulin receptor Ml 0051 147670 Nsil Insulin receptor M10051 147670 Short repeats in intron 2 Insulin receptor M10051 147670 Thr789 (ACG- silent >ACA) Insulin receptor M10051 147670 GLY996VAL Insulin receptor M10051 147670 GLU672TER Insulin receptor M10051 147670 LYS460GLU Insulin receptor M10051 147670 Asn461Thr Insulin receptor M10051 147670 MET1153ILE Insulin receptor M10051 147670 ARG86PRO Insulin receptor M10051 147670 TRP1200SER Insulin receptor M 10051 147670 TRP7SER Insulin receptor M10051 147670 ALA1 134THR Insulin receptor M10051 147670 LYS 121 TER Insulin receptor M10051 147670 ILE119MET Insulin receptor Ml 0051 147670 ARG735SER Insulin receptor M10051 147670 ARG981GLN Insulin receptor M10051 147670 ARG988TER Insulin receptor M10051 147670 TRP412SER Insulin receptor M10051 147670 ALA1135GLU Insulin receptor M10051 147670 ARG1000TER Insulin receptor M10051 147670 ASN462SER Insulin receptor M10051 147670 CODON 897 SD- 144141.1 Page 152 nonsense Insu n receptor M10051 147670 HIS209ARG Insu n receptor M10051 147670 TRP133TER Insu n receptor M10051 147670 Asn281del Insu n receptor M10051 147670 hi s252 arg Insu n receptor M10051 147670 Leu999del Insu n receptor M10051 147670 glycl 008val Insu n receptor M10051 147670 glul 131 arg Insu n receptor M10051 147670 Leu 193 Pro Insu n receptor M10051 147670 ser462asp Insu n receptor M10051 147670 GLY31ARG Insu n receptor M10051 147670 PHE382VAL Insu n receptor M10051 147670 LEU233PRO Insu n receptor M10051 147670 Arg86ter Insu n receptor M10051 147670 Trpl l93Leu Insu n receptor M10051 147670 Leul l 78Pro Insu n receptor M10051 147670 ARG1 174GLN Insu n receptor M10051 147670 VAL985MET Insu n receptor M10051 147670 GLY366ARG Insu n receptor M10051 147670 VAL28ALA Insu n receptor M10051 147670 Asp59Gly Insu n receptor M10051 147670 Leu62Pro Insu n receptor M10051 147670 ARG372TER Insu n receptor M10051 147670 ASN15LYS Insu n receptor M10051 147670 ARG1152GLN Insulin- ke growth X04434 147370 none found factor 1 receptor Insulin-like growth J03242 147470 (CA)n factor 2 Insulin-like growth J03242 147470 Apal 3'UTR factor 2 SD-144141.1 Page 1526 Insulin-like growth J03242 147470 Avail factor 2 Insulin-like growth J03242 147470 BamHl factor 2 Insulin-like growth J03242 147470 Eco RI factor 2 Insulin-like growth J03242 147470 Sst l factor 2 Insulin-like growth J03242 147470 VNTR upstream factor 2 insulin-like growth NM_0005 146730 none found factor binding protein 1 96 Insulin-like growth M29644 147440 (CA)n factor 1 Insulin-like growth M29644 147440 EcoRV factor 1 Insulin-like growth M29644 147440 EX4,5 DEL factor 1 Insulin-like growth M29644 147440 Hindlll factorl Insulin-like growth M29644 147440 PvuII factorl interleukin 1 receptor M27492 147810 Pstl (IL-1R) interleukin 6 receptor M20566 147880 dinucleotide (CA) (IL-6R) (20) inward rectifier K D50582 none found channel leptin receptor/LEPR NM 0023 601007 (CTTTA)n 03 leptin receptor/LEPR NM 0023 601007 3'-UTR SD-144141.1 Page 152 03 insertion deletion leptin receptor/LEPR NM 0023 601007 CA microsatelhte 03 repeat in intron 3, leptin receptor/LEPR NM 0023 601007 IVS 16, G-A, +1 03 leptin receptor/LEPR NM 0023 601007 K109R 03 leptin receptor/LEPR NM 0023 601007 K656N 03 leptin receptor/LEPR NM 0023 601007 Ala976Asp 03 leptin receptor/LEPR NM 0023 601007 Gln223Arg 03 leptin receptor/LEPR NM_0023 601007 Lys 109 Arg J?2) leptin receptor/LEPR NM 0023 601007 Lys656Asn 03 leptin receptor/LEPR NM 0023 601007 Prol019Pro 03 leptin receptor/LEPR NM 0023 601007 Ser343Ser 03 leptin receptor/LEPR NM 0023 601007 Ser492Thr 03 leptin receptor/LEPR NM 0023 601007 GLN23ARG 03 Leukocyte integrin Y00796 153370 none found alpha-1 Leukocyte integrin M81695 151510 none found alpha-x Lipoprotein lipase M15856 238600 INS Lipoprotein lipase M15856 238600 (TTTA)n SD-144141.1 Page 1528 Lipoprotein lipase M15856 238600 -39T-C Lipoprotein lipase M15856 238600 -93T-G Lipoprotein lipase M15856 238600 1 -BP DEL frameshift Lipoprotein lipase M15856 238600 1 -BP DEL, 221 G frameshift Lipoprotein lipase M15856 238600 2-KB DUP Lipoprotein lipase M 15856 238600 6-KB DEL Lipoprotein lipase M15856 238600 C->A -3 intron 6 Lipoprotein lipase M15856 238600 C-to-T -480 Lipoprotein lipase M15856 238600 C1338->A Thr361 Thr Lipoprotein lipase M15856 238600 C1595->G S447X Lipoprotein lipase M15856 238600 G579->A V108V Lipoprotein lipase M15856 238600 Hindlll Lipoprotein lipase M15856 238600 IVS 1, G-C, +1 Lipoprotein lipase M15856 238600 IVS2DS, G-A Lipoprotein lipase M15856 238600 IVS2DS, G-A, +l Lipoprotein lipase M 15856 238600 ALA176THR Lipoprotein lipase M 15856 238600 GLY188GLU Lipoprotein lipase M15856 238600 TRP64TER Lipoprotein lipase M 15856 238600 ARG75SER Lipoprotein lipase M15856 238600 TYR73TER Lipoprotein lipase M15856 238600 SER172CYS Lipoprotein lipase M15856 238600 TRP382TER Lipoprotein lipase M15856 238600 TYR61 TER Lipoprotein lipase M15856 238600 ASP204GLU Lipoprotein lipase M15856 238600 GLY142GLU Lipoprotein lipase M15856 238600 GLY195GLU Lipoprotein lipase M15856 238600 ILE194THR Lipoprotein lipase M15856 238600 ARG243HIS Lipoprotein lipase M15856 238600 ASP156GLY Lipoprotein lipase M15856 238600 SER447TER Lipoprotein lipase M15856 238600 Cys239->stop SD-144141.1 Page 152 Lipoprotein lipase M15856 238600 Hisl 83->Gln Lipoprotein lipase M15856 238600 ARG243CYS Lipoprotein lipase M15856 238600 ASN291SER Lipoprotein lipase M 15856 238600 E163G Lipoprotein lipase M15856 238600 E410K Lipoprotein lipase M15856 238600 ASP180GLU Lipoprotein lipase M15856 238600 ASP250ASN Lipoprotein lipase M15856 238600 Pro 157 Arg Lipoprotein lipase M15856 238600 Glul lδ Glu Lipoprotein lipase M15856 238600 Glu421Lys Lipoprotein lipase M15856 238600 CYS418TYR Lipoprotein lipase M15856 238600 LEU365VAL Lipoprotein lipase M15856 238600 ALA334THR Lipoprotein lipase M15856 238600 ASP9ASN Lipoprotein lipase M15856 238600 ILE225THR Lipoprotein lipase M15856 238600 TRP86ARG Lipoprotein lipase M15856 238600 SER244THR Lipoprotein lipase M15856 238600 GLN106TER Lipoprotein lipase M15856 238600 PRO207LEU Lipoprotein lipase M15856 238600 Tyr262->His MELANOCORTIN 4 155541 4-BP DEL NT631 RECEPTOR MELANOCORTIN 4 155541 4-BP INS, NT732 RECEPTOR MELANOCORTIN 4 155541 TYR35TER RECEPTOR MELANOCORTIN 4 155541 ASP37VAL RECEPTOR MELANOCORTIN 4 155541 Thrl l2Met RECEPTOR MELANOCORTIN 4 155541 Ilel37Thr SD-144141.1 Page 153 RECEPTOR Mineralocorticoid M 16801 600983 1 -BP DEL frameshift at receptor (aldosterone codon 337 receptor) Mineralocorticoid M16801 600983 1-BP DEL frameshift at receptor (aldosterone codon 459 receptor) Mineralocorticoid M16801 600983 760->G760 lieu 180- receptor (aldosterone >Vall80 receptor) Mineralocorticoid M16801 600983 A DEL, +3 intron 5 receptor (aldosterone receptor) Mineralocorticoid M16801 600983 C944->T944 Ala241- receptor (aldosterone >Val241 receptor) Mineralocorticoid M16801 600983 ARG537TER receptor (aldosterone receptor) natriuretic peptide L13436 108961 none found receptor B/guanylate cyclase B NEUROMEDIN K M89473 162332 none found RECEPTOR Neuropeptide Y U94320 602001 none found receptor Y5 Nicotinic, Cholinergic 118502 U62431 none found receptor alpha 2 Norepinephrine M65105 163970 none found transporter Opioid Receptor, U17298 165196 none found SD- 144141 1 Page 153 Kappa- 1 ; Oprkl Oxytocin receptor X64878 167055 C to T exon 3 Oxytocin receptor X64878 167055 CA repeat PAIRED BOX GENE 167413 none found 4 Pancreatic lipase M93285 246600 C-to-T promoter (PNLIP) (Dietary supplement) Pancreatic lipase M93285 246600 Ser267Phe (PNLIP) (Dietary supplement) Pancreatic lipase M93285 246600 Thr383Met (PNLIP) (Dietary supplement) Parathyroid hormone V00597 168450 Drall Parathyroid hoπnone V00597 168450 G-C, +1 EX2DEL Parathyroid hormone V00597 168450 (AAAT)n intron 1 Parathyroid hormone V00597 168450 BstB I Parathyroid hormone V00597 168450 Pst l Parathyroid hormone V00597 168450 Taq l Parathyroid hormone V00597 168450 Xmnl Parathyroid hormone V00597 168450 CYS 18 ARG Peroxidase (thyoid) Y00406 274500 1-BP INS Peroxidase (thyoid) Y00406 274500 1 -BP INS, 2505C Peroxidase (thyoid) Y00406 274500 20-BP DUP frameshift Peroxidase (thyoid) Y00406 274500 2612 (GTG->GCG) Val->Ala Peroxidase (thyoid) Y00406 274500 4-BP INS frameshift Peroxidase (thyoid) Y00406 274500 50 bp repeat in intron 10 Peroxidase (thyoid) Y00406 274500 Acyl intron 8 Peroxidase (thyoid) Y00406 274500 Eco RI SD- 144141.1 Page 153 Peroxidase (thyoid) Y00406 274500 ARG648GLN Peroxidase (thyoid) Y00406 274500 GLU799LYS Peroxidase (thyoid) Y00406 274500 GLY590SER Peroxidase (thyoid) Y00406 274500 ILE447PHE Peroxidase (thyoid) Y00406 274500 TYR453ASP Peroxidase (thyoid) Y00406 274500 ARG540TER Peroxisome NM_0050 601487 1 -BP DEL, 472A Frameshift proliferative activated 37 receptor, gamma PPARG Peroxisome NM_0050 601487 PR01 15GLN proliferative activated 37 receptor, gamma/PPARG Peroxisome NM_0050 601487 ARG288HIS proliferative activated 37 receptor, gamma/PPARG Peroxisome NM_0050 601487 GLN286PRO proliferative activated 37 receptor, gamma/PPARG Peroxisome NM 0050 601487 LYS319TER proliferative activated 37 receptor, gamma/PPARG Peroxisome NM_0050 601487 PRO 12 ALA proliferative activated 37 receptor, gamma/PPARG phospholipid transfer NM_0062 172425 TaqlB SD-144141.1 Page 153 protein/PLTP 27 plasma cholesterol NM_0000 118470 A1503G ester transfer 78 protein CETP plasma cholesterol NM X-00 1 18470 G-A splice junction alternative ester transfer 78 splice protein/CETP plasma cholesterol NM_0000 118470 G1696A ester transfer 78 protein/CETP plasma cholesterol NM 0000 1 18470 C-T transition in ester transfer 78 intron 12 protein/CETP plasma cholesterol NM 0000 118470 EcoNI ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 G~>A intron 14 ester transfer 78 protein/CETP plasma cholesterol NM 0000 18470 G-A transition in ester transfer 78 intron 15 protein/CETP plasma cholesterol NM 0000 18470 G1533A ester transfer 78 protein CETP plasma cholesterol NM 0000 118470 INS T alternative ester transfer 78 (intron exonl4) splice protein/CETP plasma cholesterol NM 0000 118470 Stul ester transfer 78 protein/CETP SD-144141.1 Page 153 plasma cholesterol NMJ3000 1 18470 T->G tyr57stop ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 TaqlA ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 TaqlB in intron 1 ester transfer 78 protein/CETP plasma cholesterol NM_0000 1 18470 268 Arg- ester transfer 78 >STOP protein/CETP plasma cholesterol NM_0000 118470 G181X ester transfer 78 protein/CETP plasma cholesterol NMJ3000 118470 Asp 442 to Gly ester transfer 78 protein/CETP plasma cholesterol NM_0000 1 18470 I405V ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 Lys309-Stop ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 Val421-Ile ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 R451Q ester transfer 78 protein/CETP plasma cholesterol NM 0000 18470 ASP442GLY SD-144141.1 Page 1535 ester transfer 78 r p.rrvo-Nti»eiirn- -V 1--.- ' -RC,'T iP -r potassium channel beta U25138 603951 none found subunit POTASSIUM 600937 LEU147PRO CHANNEL INWARDLY RECTIFYING SUBFAMILY .1 MEMBER 1 1 ; KCNJ 1 1 Potassium channel X83582 600734 none found Kir3.4 PRO-MELANIN- 176795 none found CONCENTRATING HORMONE progesterone receptor M15716 264080 none found Prolactin V00566 176760 Bg/II Prolactin receptor M31661 176761 none found protein kinase C beta 1 X06318 176970 none found Pyridoxine (Pyridoxal U89606 179020 none found Kinase) RAR related orphan NM 0029 600825 none found receptor A/RORA 43 RAR related orphan ****** 601972 none found receptor B/RORB RAR related orphan NM 0050 602943 none found receptor C/RORC 60 REGUCALCIN 300212 none found retinoic acid receptor NM 0009 180240 7-base deletion frameshift alpha/RARA 64 SD-144141.1 Page 153 retinoic acid receptor NM 0009 180240 codon 411 C to T alpha/RARA 64 retinoic acid receptor NM 0009 180240 Arg272Gln alpha/RARA 64 retinoic acid receptor NM 0009 180240 Met297Leu alpha/RARA 64 RETINOIC ACID X07282 180220 none found RECEPTOR BETA-2 retinoic acid receptor M57707 180190 none found gama/RARG Retinoic acid receptor, M38258 180190 none found gamma 1 retinoid X receptor NM 0029 180245 none found alpha/RXRA 57 retinoid X receptor U38480 180247 none found gamma/RXRG Retinoid X receptor- U38480 180247 none found gamma serotonin 5-HT U49516 312861 2831 T > G in the 3' receptors 5-HT1C, G protein-coupled serotonin 5-HT U49516 312861 CYS23SER receptors 5-HT1C, G protein-coupled SODIUM-IODIDE 601843 THR354PRO SYMPORTER SODIUM-IODIDE 601843 CYS272TER SYMPORTER SODIUM-IODIDE 601843 GLN267GLU SYMPORTER SODIUM-IODIDE 601843 TYR531TER SD-144141.1 Page 153 SYMPORTER SODIUM-IODIDE 601843 GLY93ARG SYMPORTER SODIUM-IODIDE 601843 GLY543GLU SYMPORTER Solute caπier family 9 X76180 600228 2-BP DEL frameshift (sodium/hydrogen exchanger), isoform 1 (antiporter, Na+/H+, amiloride sensitive) Solute carrier family 9 X76180 600228 2-BP DEL ARG508TER (sodium/hydrogen exchanger), isoform 1 (antiporter, Na+/H+, amiloride sensitive) Somatostatin receptor M81829 182451 (CA)n 5' 1/G protein-coupled Somatostatin receptor 2 M81830 182452 TRP188TER Somatostatin receptor M96738 182453 none found 3/adenyl cyclase coupled Somatostatin receptor 5 D16827 182455 2 RFLP's promoter somatostatin receptor L05521 none found subtype 2 Steroid 5 alpha M32313 184753 none found reductase 1 STEROID X51416 601998 none found HORMONE RECEPTOR ERR 1 Steroid receptor U40396 602691 none found coactivator (SRC-1) SD-144141.1 Page 153 Sucrase-isomaltase X63597 222900 GLN1098PRO Tachykinin NKl M81797 162323 none found receptor/TACRl thyroid stimulating NM 0003 603372 18-BP DEL, 4-BP frameshift hormone receptor 69 INS thyroid stimulating NM 0003 603372 1953-1957 deletion Asp at 619 hormone receptor 69 deleted thyroid stimulating NM 0003 603372 2 bases deleted of hormone receptor 69 codon 655 thyroid stimulating NM 0003 603372 C253A hoπnone receptor 69 thyroid stimulating NM 0003 603372 duplication of hormone receptor 69 nucleotides -346 to - 330 thyroid stimulating NM 0003 603372 G to C +3 intron 6 hormone receptor 69 thyroid stimulating NM 0003 603372 G-A -4 intron hormone receptor 69 thyroid stimulating NM 0003 603372 Taql hormone receptor 69 thyroid stimulating NM 0003 603372 P52T hormone receptor 69 thyroid stimulating NM 0003 603372 leu677val hormone receptor 69 thyroid stimulating NM 0003 603372 Asn715Asp hormone receptor 69 thyroid stimulating NM 0003 603372 Asp219Glu hormone receptor 69 thyroid stimulating NM 0003 603372 Asp727Glu hormone receptor 69 thyroid stimulating NM 0003 603372 Lys723 Met SD-144141.1 Page 153 hormone receptor 69 thyroid stimulating NM_0003 603372 Phel97Ile hormone receptor 69 thyroid stimulating NM_0003 603372 LYS 183 ARG hormone receptor 69 thyroid stimulating NM_0003 603372 ILE167ASN hormone receptor 69 thyroid stimulating NM_0003 603372 PRO 162 ALA hormone receptor 69 thyroid stimulating NM_0003 603372 PHE631 LEU hormone receptor 69 thyroid stimulating NM_0003 603372 CYS672TYR hormone receptor 69 thyroid stimulating NM_0003 603372 VAL509ALA hormone receptor 69 thyroid stimulating NM_0003 603372 ALA623ILE hormone receptor 69 thyroid stimulating NM_0003 603372 ASP619GLY hoπnone receptor 69 thyroid stimulating NM_0003 603372 ALA553THR hormone receptor 69 thyroid stimulating NM_0003 603372 SER281ILE hormone receptor 69 thyroid stimulating NM .003 603372 SER281ASN hormone receptor 69 thyroid stimulating NM_0003 603372 ASP633HIS hormone receptor 69 thyroid stimulating NM_0003 603372 LEU629PHE hormone receptor 69 thyroid stimulating NM_0003 603372 SER505ASN hormone receptor 69 SD-144141.1 Page 1540 thyroid stimulating NM_0003 603372 TRP546TER hormone receptor 69 thyroid stimulating NM_0003 603372 MET453THR hormone receptor 69 thyroid stimulating NM_0003 603372 ASP36HIS hormone receptor 69 thyroid stimulating NM_0003 603372 alanine 623 to homione receptor 69 valine thyroid stimulating NM_0003 603372 asp727glu hoπnone receptor 69 thyroid stimulating NM_0003 603372 CAG hormone receptor 69 [Glu]227CAT [His] thyroid stimulating NM_0003 603372 GCG hoπnone receptor 69 [Ala]460GCA [Ala] thyroid stimulating NM_0003 603372 GGT[Arg]201C hormone receptor 69 AT [His] thyroid stimulating NM_0003 603372 ARG109GLN hormone receptor 69 thyroid stimulating NM_0003 603372 CYS41SER hormone receptor 69 thyroid stimulating NM -003 603372 ASP410ASN hormone receptor 69 thyroid stimulating NM_0003 603372 CYS390TRP hormone receptor 69 thyroid stimulating NM_0003 603372 GLN324TER hormone receptor 69 thyroid stimulating NM _0003 603372 PHE525LEU hoπnone receptor 69 Transferrin receptor X01060 190010 Bell SD-144141.1 Page 1541 (p90, CD71) Transferrin receptor X01060 190010 Rsal (p90, CD71) Transferrin receptor X01060 190010 Serl42->Gly (p90, CD71) transforming growth M85079 190182 2-BP INS frameshift factor, beta receptor II (70-80kD)/TGFBR2 transforming growth M85079 190182 a-4t intron 3 factor, beta receptor II (70-80kD)/TGFBR2 transfoπning growth M85079 190182 a7g intron 2 factor, beta receptor II (70-80kD)/TGFBR2 transforming growth M85079 190182 ACA to GCA Thr to Ala factor, beta receptor II (70-80kD)/TGFBR2 transforming growth M85079 190182 base in the factor, beta receptor II polyadenine tract of (70-80kD)/TGFBR2 exon 3 transforming growth M85079 190182 GG to TT Stop codon factor, beta receptor II (70-80kD)/TGFBR2 transforming growth M85079 190182 THR315MET factor, beta receptor II (70-80kD)/TGFBR2 transforming growth M85079 190182 codon 128 factor, beta receptor II (70-80kD)/TGFBR2 TUBBY, MOUSE, 601197 none found HOMOLOG SD-144141 - 1 Page 154 type I 5 iodothyronine S48220 147892 none found deiodinase [human, mRNA, 2222 nt] Type V cyclic AJ004865 603310 none found nucleotide phosphodiesterase vitamin D NM 0003 601769 A(T/C)G putative receptor/VDR 76 translation start site vitamin D NM 0003 601769 Apal receptor/VDR 76 vitamin D NM 0003 601769 Bsml receptor/VDR 76 vitamin D NM 0003 601769 Fokl receptor/VDR 76 vitamin D NM 0003 601769 PvuII receptor/VDR 76 vitamin D NM 0003 601769 Taql receptor/VDR 76 vitamin D NM 0003 601769 Xbal receptor/VDR 76 vitamin D NM 0003 601769 ARG-GLY receptor/VDR 76 vitamin D NM 0003 601769 GLY30ASP receptor/VDR 76 vitamin D NM 0003 601769 TYR292TER receptor/VDR 76 vitamin D NM 0003 601769 ARG77GLN receptor/VDR 76 vitamin D NM 0003 601769 ARG391CYS receptor/VDR 76 SD-144141.1 Page 1543 vitamin D NM_0003 601769 ILE314SER receptor/VDR 76 vitamin D NM_0003 601769 ARG271LEU receptor/VDR 76 vitamin D NM 0003 601769 GLN149TER receptor/VDR 76 vitamin D NM_0003 601769 ARG30TER receptor/VDR 76 vitamin D NM_0003 601769 GLY46ASP receptor/VDR 76 vitamin D NM_0003 601769 codon 352 receptor/VDR 76 vitamin D NM_0003 601769 HIS305GLN receptor/VDR 76 vitamin D NM_0003 601769 ARG47GLN receptor/VDR 76 Table 23. Identified Variances in Genes or Related Pathways involved in Cardiovascular and Renal Disease 3beta hydroxysteroid M27137 109715 none found dehydrogenase 5,10- U09806 236250 1027T-G METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 1084C-T SD-144141.1 Page 154 METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 1298A-C METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 171 1C-T METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 677C-T ala — > val METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 983A-G METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 exon 7 Ala->Glu METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 A225V METHYLENETETRA HYDROFOLATE REDUCTASE 5,10- U09806 236250 ARG158GLN METHYLENETETRA HYDROFOLATE REDUCTASE SD-144141.1 Page 154 5,10- U09806 236250 ARG184TER METHYLENETETRA HYDROFOLATE REDUCTASE Adenosine A 1 L22214 102775 1777C/A Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 1827C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 1904C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2126G/T Receptor; Adoral/G protein-coupled Adenosine A 1 L22214 102775 2294insT Receptor; Adoral/G protein-coupled Adenosine A 1 L22214 102775 267 + 275C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2776C/T Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2777del36 Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 2819T/G Receptor; Adoral/G protein-coupled SD-144141.1 Page 154 Adenosine Al L22214 102775 805T/G Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 48T/A Receptor; Adoral/G protein-coupled Adenosine Al L22214 102775 716T/G Receptor; Adoral/G protein-coupled Adenosine A2 X68486 102776 1083 C/T Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 405C/T Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 432C/T Receptor; Adora2a/G protein-coupled Adenosine A2 X68486 102776 Gly-340-Ser Receptor; Adora2a/G protein-coupled Adenosine A2b X68487 600446 none found Receptor; Adora2b/G protein-coupled Adenosine A3 L20463 600445 none found Receptor; Adora3/G protein-coupled alpha- lb-adrenergic L31773 104220 none found receptor; ADRA1B alpha-2a-adrenergic Ml 8415 104210 -1291 receptor; ADRA2A SD-144141.1 Page 1547 alpha-2a-adrenergic M18415 104210 Dral receptor; ADRA2A alpha-2a-adrenergic M18415 104210 Hhal receptor; ADRA2A alpha-2 a- adrenergi c M18415 104210 Mspl promoter receptor; ADRA2A alpha-2b-adrenergic AF005900 104260 none found receptor; ADRA2B alpha-2c-adrenergic J03853 104250 (CA)n receptor; ADRA2C androgen receptor M20132 313700 Hind III androgen receptor M20132 313700 (CAA)n androgen receptor M20132 313700 (CAG)n androgen receptor M20132 313700 (GGN)n androgen receptor M20132 313700 5-KB DEL, EX F,G androgen receptor M20132 313700 5-KB DEL,EX E androgen receptor M20132 313700 C>T within exon B silent androgen receptor M20132 313700 CAG340TAG Gln>Ter androgen receptor M20132 313700 Del T at 3286 frameshift androgen receptor M20132 313700 del 1893 frameshift androgen receptor M20132 313700 G Codon 210 A androgen receptor M20132 313700 G Codon 21 1 A androgen receptor M20132 313700 G2314A ala>thr androgen receptor M20132 313700 G2677A glu629arg androgen receptor M20132 313700 Hhal androgen receptor M20132 313700 Hpall androgen receptor M20132 313700 Insert of 69 nucleotides androgen receptor M20132 313700 Maelll androgen receptor M20132 313700 PARTIAL DEL androgen receptor M20132 313700 Stu I SD-144141.1 Page 15 androgen receptor M20132 313700 598 or 599 ter androgen receptor M20132 313700 ALA721THR androgen receptor M20132 313700 ALA771THR androgen receptor M20132 313700 ARG607GLN androgen receptor M20132 313700 ARG608LYS androgen receptor M20132 313700 Arg615His androgen receptor M20132 313700 arg7261eu androgen receptor M20132 313700 Arg752Gln androgen receptor M20132 313700 ARG772CYS androgen receptor M20132 313700 ARG773CYS androgen receptor M20132 313700 ARG773HIS androgen receptor M20132 313700 ARG839CYS androgen receptor M20132 313700 ARG839HIS androgen receptor M20132 313700 arg840his androgen receptor M20132 313700 ARG846HIS androgen receptor M20132 313700 ARG855HIS androgen receptor M20132 313700 CYS579PHE androgen receptor M20132 313700 G214R androgen receptor M20132 313700 GLN60TER androgen receptor M20132 313700 Gln798Glu androgen receptor M20132 313700 GLN902ARG androgen receptor M20132 313700 GLU2LYS androgen receptor M20132 313700 gly743val androgen receptor M20132 313700 HIS874TYR androgen receptor M20132 313700 ILE869MET androgen receptor M20132 313700 LEU172TER androgen receptor M20132 313700 LEU676PRO androgen receptor M20132 313700 LEU707ARG androgen receptor M20132 313700 LYS588TER androgen receptor M20132 313700 LYS882TER androgen receptor M20132 3 13700 MET780ILE SD-144141.1 Page 154 androgen receptor M20132 313700 MET786VAL androgen receptor M20132 313700 PHE582TYR androgen receptor M20132 313700 PR0546SER androgen receptor M20132 313700 pro892ser androgen receptor M20132 313700 SER647ASN androgen receptor M20132 313700 THR877ALA androgen receptor M20132 313700 THR877SER androgen receptor M20132 313700 TRP717TER androgen receptor M20132 313700 TRP794TER androgen receptor M20132 313700 TYR761 CYS androgen receptor M20132 313700 val 581 phe androgen receptor M20132 313700 VAL730MET androgen receptor M20132 313700 VAL865LEU androgen receptor M20132 313700 VAL865MET androgen receptor M20132 313700 VAL866MET angiotensin converting NM 0007 106180 250-bp in/del enzyme/dipeptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 3 in the 3' UTR enzyme/dipeptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 5 in the 5' region enzyme/dipeptidyl 89 carboxypeptidase angiotensin converting NM 0007 106180 Pst I RFLP enzyme/dipeptidyl 89 carboxypeptidase angiotensin receptor M87290 106165 1166A-C 1/AGTR1A Anticoagulant Protein X02750 176860 -1641 A/G C (inactivator of SD-144141. Page 15 coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 (6376 G/T) in intron C (inactivator of 7 coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 -1654 C/T C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 1-BP DEL 42 AA frameshift C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 1432 C->T C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 2-BP INS, TT, C (inactivator of NT6139 coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 3350insA C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 3351del4 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 40 T->G SD-144141 1 Page 15 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 5-bp deletion C (inactivator of nucleotides 3455 to coagulation factors Va 3459 and Villa) Anticoagulant Protein X02750 176860 6128 T->C C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 6216 C->T C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 6246 G->A C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 7253 C->T C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 8589 G->A C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 8631 C->T C (inactivator of coagulation factors Va and Villa) SD- 144141.1 Page 15 Anticoagulant Protein X02750 176860 A/G at -641 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 A/T at -1476 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 A/T at -476 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 C insertion: CAT- C (inactivator of >CCAT coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 C/T at -654 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 CCT to CCC Pro-21Pro C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 deletion of 5 C (inactivator of nucleotides (nt) coagulation factors Va (CCCGC) in the end and Villa) of exon VI Anticoagulant Protein X02750 176860 G3079A C (inactivator of coagulation factors Va SD- 144141 Page 15 and Villa) Anticoagulant Protein X02750 176860 G8857 deletion C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 IVS G, C-T, +9 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Mspl C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 T-C -14 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 230 Arg-Lys C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 254 Thr-Ile C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 325 Val-Ala C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 359 Asp-Asn C (inactivator of SD-144141.1 Page 15 coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 364 Met-Trp, C (inactivator of 378 Stop coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Alal36->Pro C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ALA259VAL C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ALA267THR C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Arg 157-Stop C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG12TRP C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG169TRP C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG178GLN SD- 144141 .1 Page 155 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG178TRP C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG230CYS C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Arg286His C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ARG306TER C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 arg352try C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Asnl 02~>Lys C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Asn329->Thr C (inactivator of coagulation factors Va and Villa) SD-144141.1 Page 155 Anticoagulant Protein X02750 176860 Asp359Asn C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Asp359Asn C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Cys-331 to Arg C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Cys78->Stop C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 GLN184HIS C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 GLU20ALA C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Gly-376 Asp C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Gly282Ser C (inactivator of coagulation factors Va SD-144141.1 Page 155 and Villa) Anticoagulant Protein X02750 176860 GLY292SER C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 GLY301 SER C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Gly350Arg C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 HIS107PRO C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 ILE403MET C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 LEU223PHE C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Lys 150 deletion C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Met365Ile C (inactivator of SD-144141.1 Page 155 coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Phel39Val C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 PR0168LEU C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 PR0247LEU C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Pro279Leu C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Pro327Leu C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Q132X C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Ser270Pro C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Thr298->Met SD-144141.1 Page 155 C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 TRP402CYS C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Tyr399His C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 VAL297MET C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 VAL34MET C (inactivator of coagulation factors Va and Villa) Anticoagulant Protein X02750 176860 Y124C C (inactivator of coagulation factors Va and Villa) Anticoagulant protein Y00692 176880 G to T at codon S Cys598 Anticoagulant protein Y00692 176880 IVSl l , A-G, -9 S Anticoagulant protein Y00692 176880 + 1 G to A in intron d S Anticoagulant protein Y00692 176880 +3 A to C in intron j S SD-144141.1 Page 156 Anticoagulant protein Y00692 176880 1 nt (T) insertion at S codon 265 Anticoagulant protein Y00692 176880 delete T 635 S Anticoagulant protein Y00692 176880 G to A at codon S Trp465 Anticoagulant protein Y00692 176880 IVS10, G-A, +5 S Anticoagulant protein Y00692 176880 Arg410 (CGA)- S ->Stop Anticoagulant protein Y00692 176880 Lys368stop S Anticoagulant protein Y00692 176880 Ala 484->Pro S Anticoagulant protein Y00692 176880 Arg506->Gln S Anticoagulant protein Y00692 176880 ARG520GLY S Anticoagulant protein Y00692 176880 ASN217SER S Anticoagulant protein Y00692 176880 Cysl45Tyr S Anticoagulant protein Y00692 176880 Cys200Ser S Anticoagulant protein Y00692 176880 Cys408Ser S Anticoagulant protein Y00692 176880 Cys625Arg S Anticoagulant protein Y00692 176880 GLN238TER S Anticoagulant protein Y00692 176880 Glu26Ala SD-144141.1 Page 156 Anticoagulant protein Y00692 176880 Gly340Asp ς Anticoagulant protein Y00692 176880 Gly54Glu S Anticoagulant protein Y00692 176880 LYS155GLU S Anticoagulant protein Y00692 176880 Lysl55Glu S Anticoagulant protein Y00692 176880 Lys9Glu S Anticoagulant protein Y00692 176880 Ser283Pro S Anticoagulant protein Y00692 176880 SER406PRO S Anticoagulant protein Y00692 176880 Ser460Pro S Anticoagulant protein Y00692 176880 TER636TYR, S 649TER Anticoagulant protein Y00692 176880 Tyr595stop S Apolipoprotein B J02610 107730 C2316-->A Val703->Ile (including Ag(x) antigen) Apolipoprotein B J02610 107730 (TG)n (including Ag(x) antigen) Apolipoprotein B J02610 107730 1-BP DEL frameshift (including Ag(x) antigen) Apolipoprotein B J02610 107730 1-BP DEL SD-144141.1 Page 15 (including Ag(x antigen Apolipoprotein B J02610 107730 1 -BP DEL, (including Ag(x FS 1425TER antigen Apolipoprotein B J02610 107730 3'NNTR (including Ag(x antigen Apolipoprotein B J02610 107730 A — G second intron (including Ag(x +722 antigen Apolipoprotein B J02610 107730 ApaLI (including Ag(x antigen Apolipoprotein B J02610 107730 Avail (including Ag(x antigen Apolipoprotein B J02610 107730 Ball (including Ag(x antigen Apolipoprotein B J02610 107730 C to T -516 (including Ag(x antigen Apolipoprotein B J02610 107730 C->T change at (including Ag(x nucleotide 7064, antigen Apolipoprotein B J02610 107730 CTT3517->CTG (including Ag(x antigen Apolipoprotein B J02610 107730 EcoRI (including Ag(x) SD-144141.1 Page 15 antigen) Apolipoprotein B J02610 107730 EX21 DEL (including Ag(x antigen Apolipoprotein B J02610 107730 GCC3527->GCT (including Ag(x antigen Apolipoprotein B J02610 107730 Hindi (including Ag(x antigen Apolipoprotein B J02610 107730 INS AND DEL (including Ag(x antigen Apolipoprotein B J02610 107730 Ins/Del (including Ag(x antigen Apolipoprotein B J02610 107730 intron 20 Alu repeat (including Ag(x antigen Apolipoprotein B J02610 107730 Mspl (including Ag(x antigen Apolipoprotein B J02610 107730 PvuII (including Ag(x antigen Apolipoprotein B J02610 107730 Styl second intron (including Ag(x antigen Apolipoprotein B J02610 107730 T-to-C 1981 (including Ag(x antigen SD-144141.1 Page 156 Apolipoprotein B J02610 107730 Xbal (including Ag(x antigen Apolipoprotein B .102610 107730 A3371 V (including Ag(x antigen Apolipoprotein B J02610 107730 Arg— -Glu3611 (including Ag(x antigen Apolipoprotein B J02610 107730 ARG1306TER (including Ag(x antigen Apolipoprotein B J02610 107730 ARG2058TER (including Ag(x antigen Apolipoprotein B J02610 107730 ARG2495TER (including Ag(x antigen Apolipoprotein B J02610 107730 ARG3500GLN (including Ag(x antigen Apolipoprotein B J02610 107730 ARG3531CYS (including Ag(x antigen Apolipoprotein B J02610 107730 ASN1728THR (including Ag(x antigen Apolipoprotein B J02610 107730 Asn431 1— -Ser (including Ag(x antigen Apolipoprotein B J02610 107730 Cys646->Tyr SD- 144141 , Page 156 (including Ag(x) antigen) Apolipoprotein B J02610 107730 Gin 3405 Glu (including Ag(x) antigen) Apolipoprotein B J02610 107730 GLN1450TER (including Ag(x) antigen) Apolipoprotein B J02610 107730 GLN2252TER (including Ag(x) antigen) Apolipoprotein B J02610 107730 Glu207->Lys (including Ag(x) antigen) Apolipoprotein B J02610 107730 GLU4034ARG (including Ag(x) antigen) Apolipoprotein B J02610 107730 Glu4154 (including Ag(x) antigen) Apolipoprotein B J02610 107730 Leu 3350 Leu (including Ag(x) antigen) Apolipoprotein B J02610 107730 Leu-Ala-Leu (including Ag(x) signal peptide antigen) (SP) insertion/deletio n Apolipoprotein B J02610 107730 LEU3041TER (including Ag(x) antigen) SD-144141. Page 156 Apolipoprotein B J02610 107730 Q3405E (including Ag(x) antigen) Apolipoprotein B J02610 107730 Ser 3252 Gl (including Ag(x) antigen) Apolipoprotein B J02610 107730 Ser 3455 Arg (including Ag(x) antigen) Apolipoprotein B J02610 107730 SER1729TER (including Ag(x) antigen) Apolipoprotein B J02610 107730 Thr71— >Ile (including Ag(x) antigen) Apolipoprotein B J02610 107730 Trp66->Gly (including Ag(x) antigen) Apolipoprotein B J02610 107730 Val 3396 Met (including Ag(x) antigen) Apolipoprotein B J02610 107730 VAL1829CYS (including Ag(x) antigen) Apolipoprotein B J02610 107730 Val591 ->Ala (including Ag(x) antigen) apolipoprotein NM 0000 107741 7 AA insertion; E/APOE 41 tandem repeat of residues 121-127 apolipoprotein NM_0000 107741 A178G Threonine42Ala SD- 144141.1 Page 156 E/APOE 41 nine apolipoprotein NM 0000 107741 A490C Lysine 146Gluta E/APOE 41 mine apolipoprotein NM 0000 107741 A490G Lysine 146Gluta E/APOE 41 mic Acid apolipoprotein NM 0000 107741 A940C Serine296Argini E/APOE 41 ne apolipoprotein NM 0000 107741 Aintron3G substitution E/APOE 41 creates 2 abnormally spliced mRNA forms apolipoprotein NM 0000 107741 C305G Proline84Argini E/APOE 41 ne apolipoprotein NM 0000 107741 C460A Argininel36Seri E/APOE 41 ne apolipoprotein NM 0000 107741 C478T Argl42142Cysl E/APOE 41 42 apolipoprotein NM 0000 107741 C487T Arginine 145 Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C526T Arginine 158Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C736T Arginine228Cys E/APOE 41 teine apolipoprotein NM 0000 107741 C805G Arg251251 Gly2 E/APOE 41 51 apolipoprotein NM 0000 107741 G144deletion LeucineόOTermi E/APOE 41 nation Codon (frameshift) apolipoprotein NM 0000 107741 G349A Ala9999Thr99 E/APOE 41 SD-144141.1 Page 15 apolipoprotein NM 0000 107741 G434A Glyl27127Aspl E/APOE 41 27 apolipoprotein NM 0000 107741 G455A Arginine 134Glu E/APOE 41 tamine apolipoprotein NM 0000 107741 G488A Arginine 145His E/APOE 41 tidine apolipoprotein NM 0000 107741 G568C Alal52Proline E/APOE 41 apolipoprotein NM 0000 107741 G61A Glutamic E/APOE 41 Acid3Lysine apolipoprotein NM 0000 107741 G683A Tryptophan210 E/APOE 41 Termination Codon apolipoprotein NM 0000 107741 G725A Arg224224Gln2 E/APOE 41 24 apolipoprotein NM 0000 107741 G875A Arginine274His E/APOE 41 tidine apolipoprotein NM 0000 107741 G91A Glutamic E/APOE 41 Acidl3Lysine apolipoprotein NM 0000 107741 GAG-GAG844- Glu244/Glu245 E/APOE 41 849AAG-AAG 244- 245Lys244/Lys 245 apolipoprotein NM 0000 107741 T137C Leucine28Prolin E/APOE 41 e apolipoprotein NM 0000 107741 T388C Cysteine 1 12Arg E/APOE 41 inine apolipoprotein NM 0000 107741 T761A Valine236Gluta E/APOE 41 mic Acid APOLIPOPROTEIN(a 152200 -773G, +93T, ); LPA +121 G SD-144141.1 Page 15 © r- v-O oo v VO ft X Λ H Λ X C H -fi H o O o o o O o o o o o ^ o o o o o o o o o o o o V o o CN CN CN CN CN CN CN CN CN CN t-- CN oo oo CN CN CN Ol CN CN CN CN CN CN cn O ^ rf i l-O in m m sn in i i o o o VO o cn cn 60 vO vo vo -o v-o v-o v-o O vO v-o - O O CN CN CN CN CN CN CN CN CN CN CN CN CN CN CN CN V O VO O V-O V-O O -D O V-O O O V-O 0 © © © © © 0 0 0 © 0 © 0 © 0 © - . -^ --^ --- .-^ .^ --^ -^ c^ n ^ co n ^ c^ ro © © © © © 0 © © 0 © © 0 © 0 © © τ Ui Uτ Um Um Um Uτ Um τ Um Um UΛ Uτ Ur U. Um < < < < < < < < < < < < < < < < tn tn tn tn tΛ tΛ tΛ tΛ tn tn tn tn tn tn tn tn tn tn tn tn tn tn tn tn cn tn tn tn tn tn tn tn 03 03 03 03 03 03 03 03 03 03 03 03 03 03 03 03 ft ft ft ft ft ft ft ft ft ft ft ft ft ft ft ft O O O O O O O O O O O O O O O O ''" N ^^ CN ** CN > CN > CN CN CN * CN N > CN > CN ^ CN CN ■ CN > CN > CD . CD , CD , (D , CD , CD , CD , <D , CD , CD . CD , 03 , 03 , CD . ( D , CD .fi o .3 o .3 o .3 o .3 o .3 o .5 o .3 o .3 o .3 o .3 o .5 o .3 0.5 o .£ o .3 st ' 0 30 ftD ' 5 ■ *b ftD ' ^δ> fto 'c So 9ft ' δ ! -b ft ω ' t3--o ' H ω< ' 5( D o c CD ' 5 M ft ω ' S00 ft co '5 5"b ft " ' Sc-Λ c <-> ' S00 ε ω_, ' 5 M ft CD ' SQJ) " H CD- ' S00 ft CD ' δ ^ . Q ^ ii ^ E < ui < ui < Um < ui ^ u2 < E < ui < ui < u2 ^ u2 ^ ui < ui < ui < CN 00 o © © © © © © © © © © © © © © © © © © © cn cn cn n cn n oo 00 oo OO oo OO oo - - r-~ r- t-- o "ot ■ - ^r 1- <5-r 00 oo 00 oo Os Os © © o © © o © © © © o c cn cn n n n cn ——' Beta-2-Adrenergic M15169 109690 Fnu4HI Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 A->G -1343 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 C->G -468 Receptor; Adrb2 Beta-2 - Adrenergi c Ml 5169 109690 G->A -1023 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 G->A -654 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 T->A -1429 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 T->C -20 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 T->C -367 Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 T->C -47 Receptor; Adrb2 Beta-2-Adrenergic M 15169 109690 ARG16GLY Receptor; Adrb2 Beta-2-Adrenergic M15169 109690 GLN27GLU Receptor; Adrb2 B eta-2- Adrenergi c M15169 109690 Thrl64Ile Receptor; Adrb2 Beta-2-Adrenergic Ml 5169 109690 val 34 met Receptor; Adrb2 Beta-Adrenergic X691 17 109636 none found Receptor Kinase 2; Adrbk2 beta-adrinergic NM_0016 109635 none found receptor kinase 19 SD-144141.1 Page 157 1/BARKl bradykinin receptor NM 0007 600337 9-base pair deletion Bl/BDKRBl G 10 protein-coupled bradykinin receptor NM 0007 600337 A1098->G Bl/BDKRBl G 10 protein-coupled bradykinin receptor NM 0007 600337 C181->T Bl/BDKRBl G 10 protein-coupled bradykinin receptor NM 0007 600337 G-699->C Bl/BDKRBl G 10 protein-coupled bradykinin receptor NM 0006 113503 -143C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 1 13503 -412C/G B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 1 13503 -536C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -640T/C B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -649insG B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 1 13503 -704C/T B2/BDKRB2 G 23 protein-coupled SD-144141.1 Page 15 bradykinin receptor NM 0006 113503 -78C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 -845C/T B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 9 bp de (-)21 -29 B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 C>T promoter 54 B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 repeat 3'UTR B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 1 13503 tandem repeat near B2/BDKRB2 G 23 promoter protein-coupled bradykinin receptor NM 0006 113503 R14C B2/BDKRB2 G 23 protein-coupled bradykinin receptor NM 0006 113503 T21M B2/BDKRB2 G 23 protein-coupled Ca2+-dependent U03090 601192 none found phospholipase A2 Carbonic anhydrase II J03037 259730 BstNI Carbonic anhydrase II J03037 259730 gt— >tt splice donor site at the 5' end of intron 6 Carbonic anhydrase II J03037 259730 IVS2, G-A, +1 SD-144141.1 Page 15 Carbonic anhydrase II J03037 259730 IVS5, G-C, -1 Carbonic anhydrase II J03037 259730 TAQ1 Carbonic anhydrase II J03037 259730 TYR40TER Carbonic anhydrase II J03037 259730 ASN252ASP Carbonic anhydrase II J03037 259730 HIS107TYR Carbonic anhydrase II J03037 259730 Ile31 Val Carbonic anhydrase II J03037 259730 LYS17GLU Carbonic anhydrase II J03037 259730 PRO237HIS Carbonic anhydrase IV M83670 114760 none found Chloride channel 5 X91906 300008 1-BP DEL , 2085C Chloride channel 5 X91906 300008 tgcag - -> tgaag Chloride channel 5 X91906 300008 Arg704Stop Chloride channel 5 X91906 300008 GLY57VAL Chloride channel 5 X91906 300008 ARG280PRO Chloride channel 5 X91906 300008 Arg34Stop Chloride channel 5 X91906 300008 ARG648TER Chloride channel 5 X91906 300008 ARG704TER Chloride channel 5 X91906 300008 GLY506GLU Chloride channel 5 X91906 300008 LEU200ARG Chloride channel 5 X91906 300008 SER244LEU Chloride channel 5 X91906 300008 SER520PRO Chloride channel 5 X91906 300008 TRP279TER Chloride channel 5 X91906 300008 TRP343TER Cholecystokinin A L13605 1 18444 GLY21ARG receptor/CCKAR Cholecystokinin A L13605 1 18444 VAL365ILE receptor/CCKAR Cholecystokinin B L081 12 118445 1550 G->A Vall25->Ile receptor/CCKBR Cholecystokinin B L08112 118445 CAT 207 CAC His207His receptor/CCKBR SD-144141.1 Page 15 Cholecystokinin B L08112 118445 Arg215His receptor/CCKBR Cholecystokinin B L08112 118445 Vall38Met receptor/CCKBR CHOLINERGIC 100690 Hae III RECEPTOR, NICOTINIC, ALPHA POLYPEPTIDE 1; CHRNA1 CHOLINERGIC 100690 ASN217LYS RECEPTOR, NICOTINIC, ALPHA POLYPEPTIDE 1; CHRNA1 CHOLINERGIC 100690 GLY153SER RECEPTOR, NICOTINIC, ALPHA POLYPEPTIDE 1 ; CHRNA1 CHOLINERGIC 100690 SER269ILE RECEPTOR, NICOTINIC, ALPHA POLYPEPTIDE 1 ; CHRNA1 CHOLINERGIC 100690 THR254ILE RECEPTOR, NICOTINIC, ALPHA POLYPEPTIDE 1 ; CHRNA1 CHOLINERGIC 100690 VAL156MET RECEPTOR, SD-144141 - 1 Page 15 NICOTINIC, ALPHA POLYPEPTIDE 1; CHRNAl CHYMASE 1 ; CMA1 1 18938 none found Complement CIS J04080 120580 4-BP DEL component precursor (Cl esterase) Copper Transport U70660 602270 none found Protein HAH1 CPLA2-GAMMA 603602 none found Cytochrome P450, M14565 118485 5' UTR subfamily XIA pentanucleotide (cholesterol side chain repeat cleavage) dopamine beta Y00096 223360 hydroxylase Dopamine Receptor DI X58987 126449 C/T Isoleucine49 Dopamine Receptor D2 X51362 126450 141 C ins/del Dopamine Receptor D2 X51362 126450 A241G Dopamine Receptor D2 X51362 126450 Ncol RFLP Dopamine Receptor D2 X51362 126450 Taql A, Taql B, Taql D, and (CA)n STRP Dopamine Receptor D2 X51362 126450 Serine 31 1Cysteine Endopeptidase X07166 120520 none found Endothelin 1 Y00749 131240 A at position 138 5'UTR Endothelin 1 Y00749 131240 C at position 121 5'UTR Endothelin 1 Y00749 131240 Dinucleotide repeat Endothelin 1 Y00749 131240 Lys 198 Asn Endothelin 2 M65199 131241 A985G 3 'UTR SD-144141.1 Page 15 Endothelin 3 X52001 131242 1-BP INS Endothelin 3 X52001 131242 1-BP INS, 262G Endothelin 3 X52001 131242 262GC-T Endothelin 3 X52001 131242 ALA17THR Endothelin 3 X52001 131242 ALA224THR Endothelin 3 X52001 131242 CYS159PHE Endothelin Converting Z35307 600423 ARG742CYS Enzyme 1 Endothelin Receptor D90348 131243 none found Type A Endothelin Receptor L06623 131244 1-BP INS, 878T Type B Endothelin Receptor L06623 131244 ALA183GLY Type B Endothelin Receptor L06623 131244 GLY57SER Type B Endothelin Receptor L06623 131244 SER305ASN Type B Endothelin Receptor L06623 131244 TRP275TER Type B Endothelin Receptor L06623 131244 TRP276CYS Type B eosinophil 131399 INS G, NT1537 t pNPcTrnUvXilπUα oo *C->/ / -C/- PT Λ St eosinophil 131399 ARG286HIS peroxidase/EPX Erythropoietin receptor M34986 133171 7-BP DEL frameshift Erythropoietin receptor M34986 133171 1 -BP INS FS444TER Erythropoietin receptor M34986 133171 1-BP INS, 5967T frameshift Erythropoietin receptor M34986 133171 BamHl j Erythropoietin receptor M34986 133171 Bgl II | SD-144141.1 Page 15 Erythropoietin receptor M34986 133171 C to T l ~>435stop Erythropoietin receptor M34986 133171 C6148T Erythropoietin receptor M34986 133171 Hindlll Erythropoietin receptor M34986 133171 Sacl | Erythropoietin receptor M34986 1331 71 ASN487SER Erythropoietin receptor M34986 133171 TRP439TER Erythropoietin receptor M34986 133171 TYR426TER estrogen receptor 1 M12674 133430 RFLP (Pssl enzyme) (ESR1) estrogen receptor 1 M12674 133430 RFLP (PvuII (ESR1) enzyme) estrogen receptor 2 X99101 601663 none found (ESR2) Estrogen-preferring NM 0054 600043 none found sulfotransferase/STE 20 G protein coupled NM 0022 601 534 (CA)n potassium channel, 39 subfamily J, member 3/KCNJ3/GIRK1 GAP JUNCTION 121013 none found PROTEIN, ALPHA-5 GLYCOPROTEIN lb, 231200 (39-base pair)n PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 92-BP DUP SER399- PLATELET, ALPHA THR411 DUP POLYPEPTIDE GLYCOPROTEIN lb, 231200 Arg342 (A --> G) silent PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 T --> C 2nd SD-144141.1 Page 15 PLATELET, ALPHA nucleotide exon 2 POLYPEPTIDE GLYCOPROTEIN lb, 231200 Tyr492 (TAT->T) PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 ALA156VAL PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 GLY233VAL PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 LEU57PHE PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 MET239VAL PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 TRP126TER PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 231200 TRP343TER PLATELET, ALPHA POLYPEPTIDE GLYCOPROTEIN lb, 31200 TRP498TER PLATELET, ALPHA POLYPEPTIDE Granulocyte colony- M64592 20420 none found stimulating factor Guanine nucleotide J03004 39360 PHE200LEU binding protein (G protein), alpha SD-144141.1 Page 15 inhibiting activity polypeptide 2 Guanine nucleotide J03004 139360 ARG179CYS binding protein (G protein), alpha inhibiting activity polypeptide 2 Guanine nucleotide J03004 139360 ARG179GLY binding protein (G protein), alpha inhibiting activity polypeptide 2 Guanine nucleotide J03004 139360 ARG179HIS binding protein (G protein), alpha inhibiting activity polypeptide 2 Guanine nucleotide M31328 139130 C825T binding protein (G protein), beta polypeptide 3 Guanine nucleotide U40038 600998 none found binding protein (G protein), q polypeptide GUANINE 13931 none found NUCLEOTIDE- BINDING PROTEIN ALPHA- ACTIVATING ACTIVITY POLYPEPTIDE O; SD-144141.1 Page 15 GNAOl Guanylate cyclase 1 , X63282 601244 none found soluble, alpha 2 GUANYLATE 603695 none found CYCLASE 1. SOLUBLE, BETA-2 Guanylate cyclase X66534 139396 none found soluble, alpha-3 chain Guanylate cyclase X66533 139397 none found soluble, beta-1 chain H.sapiens 40 kDa Z1 1695 176948 none found protein kinase related to rat ERK2 H.sapiens 44kDa Z1 1696 601795 none found protein kinase related to rat ERK1 H.sapiens encoding Z22555 601040 none found CLA-1 mRNA H.sapiens gene for X68793 107300 AAG — AAA antithrombin III transition at Lys 176 H.sapiens gene for X68793 107300 Ddel antithrombin III H.sapiens gene for X68793 107300 Hae III antithrombin III H.sapiens gene for X68793 107300 Nhel antithrombin III H.sapiens gene for X68793 107300 Pst l antithrombin III H.sapiens gene for X68793 107300 Trinucleotide repeat antithrombin III H.sapiens gene for X68793 107300 GLU245FS SD-144141.1 Page 158 antithrombin III H.sapiens gene for X68793 107300 ILE7ASN antithrombin III H.sapiens gene for X68793 107300 ALA382THR antithrombin III H.sapiens gene for X68793 107300 ala382thr antithrombin III H.sapiens gene for X68793 107300 ALA384PRO antithrombin III H.sapiens gene for X68793 107300 ALA384SER antithrombin III H.sapiens gene for X68793 107300 ALA387VAL antithrombin III H.sapiens gene for X68793 107300 ALA404THR antithrombin III H.sapiens gene for X68793 107300 ARG129TER antithrombin III H.sapiens gene for X68793 107300 ARG24CYS antithrombin III H.sapiens gene for X68793 107300 ARG393CYS antithrombin III H.sapiens gene for X68793 107300 ARG393HIS antithrombin III H.sapiens gene for X68793 107300 ARG393PRO antithrombin III H.sapiens gene for X68793 107300 arg406met antithrombin III H.sapiens gene for X68793 107300 ARG47CYS antithrombin III H.sapiens gene for X68793 107300 ARG47HIS antithrombin III SD- 144141 Page 158 H.sapiens gene for X68793 107300 ARG47SER antithrombin III H.sapiens gene for X68793 107300 ASN208LYS antithrombin III H.sapiens gene for X68793 107300 ASP309LYS antithrombin III H.sapiens gene for X68793 107300 GLY392ASP antithrombin III H.sapiens gene for X68793 107300 Hisl20->Tyr antithrombin III H.sapiens gene for X68793 107300 LEU-10PRO antithrombin III H.sapiens gene for X68793 107300 LEU99PHE antithrombin III H.sapiens gene for X68793 107300 LYS228FS antithrombin III H.sapiens gene for X68793 107300 LYS370ARG antithrombin III H.sapiens gene for X68793 107300 PRO407LEU antithrombin III H.sapiens gene for X68793 107300 PRO41LEU antithrombin III H.sapiens gene for X68793 107300 PRO429LEU antithrombin III H.sapiens gene for X68793 107300 Pro80->Thr antithrombin III H.sapiens gene for X68793 107300 SER291PRO antithrombin III H.sapiens gene for X68793 107300 SER349PRO antithrombin III H.sapiens gene for X68793 107300 SER394LEU SD-144141.1 Page 158 antithrombin III H.sapiens gene for X68793 107300 Tyrl58->Cys antithrombin III H.sapiens gene for X68793 107300 VAL-3GLU antithrombin III H.sapiens gene for X68793 107300 VAL48CYS antithrombin III H.sapiens HTNT4 X79857 191045 IVS 15, G-A, +1 mRNA for cardiac troponin T H.sapiens HTNT4 X79857 191045 Argl02Leu mRNA for cardiac troponin T H.sapiens HTNT4 X79857 191045 ARG278CYS mRNA for cardiac troponin T H.sapiens HTNT4 X79857 191045 ARG92GLN mRNA for cardiac troponin T H.sapiens HTNT4 X79857 191045 ILE79ASN mRNA for cardiac troponin T H.sapiens mRNA for Z69881 601929 none found adenosine triphosphatase, calcium H.sapiens mRNA for X95520 602047 1389 (A/G) cyclic nucleotide phosphodiesterase H.sapiens mRNA for X95520 602047 dinucleotide repeat cyclic nucleotide introns 12 phosphodiesterase SD-144141.1 Page 15 H.sapiens mRNA for X95520 602047 dinucleotide repeat cyclic nucleotide introns 5 phosphodiesterase H.sapiens mRNA for X95191 601411 1-BP DEL, 656C delta-sarcoglycan H.sapiens mRNA for X95191 601411 ARG165TER delta-sarcoglycan H.sapiens mRNA for X95191 601411 GLU262LYS delta-sarcoglycan H.sapiens mRNA for X95191 601411 TRP30TER delta-sarcoglycan H.sapiens mRNA for X61656 191306 none found growth factor receptor tyrosine kinase H.sapiens mRNA for X73029 163730 (CCTTT)n nitric oxide synthase H.sapiens mRNA for X76079 173490 none found platelet derived growth factor alpha receptor H.sapiens mRNA for X98330 180902 none found ryanodine receptor 2 H.sapiens mRNA for Z19585 600715 none found thrombospondin-4 H.sapiens tropomyosin Z24727 191010 ASP175ASN isoform mRNA, complete CDS H.sapiens tropomyosin Z24727 191010 GLU180GLY isoform mRNA, complete CDS Histamine receptor HI AF026261 600167 none found HMGCoA NM_0008 142910 HgiAI SD-144141.1 Page 15 reductase/HMGCR 59 HMGCoA NM 0008 142910 ScrFI polymorphism reductase/HMGCR 59 in the 2nd intron Homo sapiens (clone L17128 137167 LEU394ARG H4/H16) gamma- glutamic carboxylase mRNA, complete cds Homo sapiens ADDL D67031 601568 none found mRNA for adducin- like protein, complete cds Homo sapiens beta- AF084040 107940 none found arrestin 1 A mRNA, complete cds Homo sapiens beta- M58018 160760 2.4-KB DEL myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG249GLN myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG403GLN myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG403LEU myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG453CYS SD-144141.1 Page 15 myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG719TRP myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ARG723CYS myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 ASP778GLY myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 GLU924LYS myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 GLU949LYS myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 GLY256GLU myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 GLY584ARG myosin heavy chain (MYH7) mRNA, complete cds SD- 144141.1 Page 158 Homo sapiens beta- M58018 160760 GLY741ARG myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 LEU908VAL myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 PHE513CYS myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens beta- M58018 160760 VAL606MET myosin heavy chain (MYH7) mRNA, complete cds Homo sapiens calcium- M23114 108740 18-BP INS, IVS2, ATPase (HK1) mRNA, 12 complete cds Homo sapiens calcium- M23114 108740 IVS6DS, G-A, ATPase (HK1) mRNA, + 1 complete cds Homo sapiens calcium- M231 14 108740 ASN754 DEL ATPase (HK1 ) mRNA, complete cds Homo sapiens calcium- M23114 108740 ASN767SER ATPase (HK1) mRNA, complete cds Homo sapiens calcium- M23114 108740 CYS268PHE ATPase (HK1) mRNA, complete cds SD-144141 - 1 Page 15 Homo sapiens calcium- M231 14 108740 CYS560ARG ATPase (HKl) mRNA, complete cds Homo sapiens calcium- M23114 108740 GLN108TER ATPase (HK1) mRNA, complete cds Homo sapiens calcium- M23114 108740 GLY23GLU ATPase (HK1) mRNA, complete cds Homo sapiens calcium- AF064594 603604 none found independent phospholipase A2 mRNA, complete cds Homo sapiens carbonic AF037335 603263 none found anhydrase precursor (CA 12) mRNA, complete cds Homo sapiens focal L05186 600758 none found adhesion kinase mRNA, complete cds Homo sapiens GATA- L34357 600576 none found 4 mRNA, complete cds Homo sapiens integrin L36531 604063 none found alpha 8 subunit mRNA, 3' end Homo sapiens integrin AF032108 600536 1-bp frameshift alpha-7 mRNA, deletion at cDNA complete cds nucleotide 1204 Homo sapiens integrin AF032108 600536 21-BP INS alpha-7 mRNA, complete cds SD-144141.1 Page 159 Homo sapiens integrin AF032108 600536 98-BP DEL alpha-7 mRNA, complete cds Homo sapiens mRNA AB005289 300135 ILE400MET for ABC transporter 7 protein, complete cds Homo sapiens mRNA AB022017 602739 none found for AMP-activated protein kinase alpha-1, complete cds Homo sapiens mRNA AJ224515 602740 none found for AMP-activated protein kinase beta 1 Homo sapiens mRNA AJ224538 602741 none found for AMP-activated protein kinase beta 2 subunit Homo sapiens mRNA AB001025 180903 none found for brain ryanodine receptor, complete cds Homo sapiens p21- AF068864 300142 ARG419TER activated kinase 3 (PAK3) mRNA, complete cds Homo sapiens L48513 602447 ALA148GLY paraoxonase 2 (PON2) mRNA, complete cds Homo sapiens L48513 602447 CYS311SER paraoxonase 2 (PON2) mRNA, complete cds Homo sapiens L48516 602720 none found SD-144141.1 Page 159 paraoxonase 3 (PON3) mRNA, 3' end of cds Homo sapiens M95678 604114 none found phospholipase C-beta-2 mRNA, complete cds Homo sapiens AF033850 602384 none found phospholipase D2 (PLD2) mRNA, complete cds Homo sapiens receptor L06139 600221 ARG849TRP protein-tyrosine kinase (TEK) mRNA, complete cds Human 47-kD M55067 233700 1-BP DEL, 502G frameshift autosomal chronic granulomatous disease protein mRNA, complete cds Human 47-kD M55067 233700 2-BP DEL, EX2, -2, autosomal chronic GT granulomatous disease protein mRNA, complete cds Human 47-kD M55067 233700 2-BP INS frameshift autosomal chronic granulomatous disease protein mRNA, complete cds Human 47-kD M55067 233700 ASP 161 VAL autosomal chronic granulomatous disease SD-144141.1 Page 159 protein mRNA, complete cds Human 47-kD M55067 233700 LYS160GLU autosomal chronic granulomatous disease protein mRNA, complete cds Human 5'-AMP- U42412 602742 none found activated protein kinase, gamma- 1 subunit mRNA, complete cds Human activin LI 1695 190181 S387Y receptor-like kinase (ALK-5) mRNA, complete cds Human alpha adducin L07261 102680 G460W mRNA, partial cds including alternate exons A and B Human apolipoprotein M27875 107680 1-BP DEL, CODON A-I mRNA, complete 202 cds Human apolipoprotein M27875 107680 1-BP INS A-I mRNA, complete cds Human apolipoprotein M27875 107680 1 121 C/T in intron 3 A-I mRNA, complete cds Human apolipoprotein M27875 107680 12-BP DEL AND 2- A-I mRNA, complete BP INS SD-144141.1 Page 159 cds Human apolipoprotein M27875 107680 A/G at position 78 A-I mRNA, complete bp upstream cds Human apolipoprotein M27875 107680 DELETION OF A-I mRNA, complete APOA1/APOC3/AP COMPLEX Human apolipoprotein M27875 107680 EX4/IVS1 A-I mRNA, complete cds Human apolipoprotein M27875 107680 G-to-A -75 bp A-I mRNA, complete cds Human apolipoprotein M27875 107680 IVS2, G-C, +1 A-I mRNA, complete cds Human apolipoprotein M27875 107680 Msp I A-I mRNA, complete cds Human apolipoprotein M27875 107680 Pst-I A-I mRNA, complete cds Human apolipoprotein M27875 107680 Sstl A-I mRNA, complete cds Human apolipoprotein M27875 107680 Xmnl A-I mRNA, complete cds Human apolipoprotein M27875 107680 Lys- 107 A-I mRNA, complete deletion SD-144141.1 Page 15 cds Human apolipoprotein M27875 107680 Ala-95~>Asp A-I mRNA, complete cds Human apolipoprotein M27875 107680 ARG10LEU A-I mRNA, complete cds Human apolipoprotein M27875 107680 ARG173CYS A-I mRNA, complete cds Human apolipoprotein M27875 107680 ARG173PRO A-I mRNA, complete cds Human apolipoprotein M27875 107680 Asp 103— -Asn A-I mRNA, complete cds Human apolipoprotein M27875 107680 GLN-2TER A-I mRNA, complete cds Human apolipoprotein M27875 107680 GLN32TER A-I mRNA, complete cds Human apolipoprotein M27875 107680 GLN84TER A-I mRNA, complete cds Human apolipoprotein M27875 107680 GLU136LYS A-I mRNA, complete cds Human apolipoprotein M27875 107680 GLU198LYS A-I mRNA, complete cds SD-144141.1 Page 159 Human apolipoprotein M27875 107680 GLY26ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 LEU60ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 LEU90PRO A-I mRNA, complete cds Human apolipoprotein M27875 107680 LYS107DEL A-I mRNA, complete cds Human apolipoprotein M27875 107680 PRO 143 ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 Prol65->Arg A-I mRNA, complete cds Human apolipoprotein M27875 107680 PRO 165 ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 PRO3ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 PRO4ARG A-I mRNA, complete cds Human apolipoprotein M27875 107680 Trp-108-->Arg A-I mRNA, complete cds Human apolipoprotein M27875 107680 TRP50ARG SD-144141.1 Page 159 A-I mRNA, complete cds Human apolipoprotein M27875 107680 VAL156GLU A-I mRNA, complete cds Human ARF-activated U38545 602382 none found phosphatidylcholine- specific phospholipase Dla (hPLDl) mRNA, complete cds Human beta 4 adducin U43959 102681 none found mRNA, alternatively spliced partial cds Human bumetanide- U58130 600839 ASP648ASN sensitive Na-K-2C1 cotransporter (NKCC2) mRNA, complete cds Human bumetanide- U58130 600839 TRP625TER sensitive Na-K-2C1 cotransporter (NKCC2) mRNA, complete cds Human bumetanide- U58130 600839 VAL272PHE sensitive Na-K-2C1 cotransporter (NKCC2) mRNA, complete cds Human bumetanide- U30246 600840 none found sensitive Na-K-Cl cotransporter (NKCC1) mRNA, complete cds Human c-sis/platelet- M l 2783 190040 135-BP DEL, IVS5 derived growth factor 2 SD-144141.1 Page 15 (SIS/PDGF2) mRNA, complete cds Human c-sis/platelet- M12783 190040 FUSION WITH derived growth factor 2 COLI A (SIS/PDGF2) mRNA, complete cds Human calcium- U95301 603603 none found dependent group X phospholipase A2 mRNA, complete cds Human cAMP- M33336 188830 none found dependent protein kinase type l-alpha subunit (PRKARIA) mRNA, complete cds Human cellular LI 0844 1 16952 none found growth-regulating protein mRNA, complete cds Human cGMP- M91667 123805 none found inhibited cAMP phosphodiesterase mRNA, complete cds Human complement M14058 216950 none found Clr mRNA, complete cds Human desmin mRNA, U59167 125660 21 -BP DEL complete cds Human desmin mRNA, U59167 125660 EcoRV complete cds Human desmin mRNA, U59167 125660 ALA337PRO SD-144141.1 Page 159 complete cds Human desmin mRNA, U59167 125660 ALA360PRO complete cds Human desmin mRNA, U59167 125660 ASN393ILE complete cds Human desmin mRNA, U59167 125660 ILE451 MET complete cds Human DNA sequence AL023653 300145 none found from clone 753P9 on chromosome Xq25- 26.1. Contains the gene coding for Aminopeptidase P (EC 3.4.1 1.9, XAA-Pro/X- Pro/Proline/Aminoacyl proline Aminopeptidase) and a novel gene. Contains ESTs, STSs, GSSs and a gaaa repeat polymorphism Human ERK5 mRNA, U25278 602521 none found complete cds Human ferritin H chain M11146 134770 none found mRNA, complete cds Human ferritin L chain M l 1 147 134790 22T-G mRNA, complete cds Human ferritin L chain M 1 1 147 134790 146A-G mRNA, complete cds Human ferritin L chain M11147 134790 147G-C mRNA, complete cds SD-144141.1 Page 160 Human ferritin L chain Ml 1 147 134790 18C-T mRNA, complete cds Human ferritin L chain M1 1147 134790 29-BP DEL IRE DEL mRNA, complete cds Human ferritin L chain M1 1 147 134790 32G-A mRNA, complete cds Human ferritin L chain Ml 1 147 134790 32G-T mRNA, complete cds Human ferritin L chain M11147 134790 36C-A mRNA, complete cds Human ferritin L chain Ml 1 147 134790 39C-T mRNA, complete cds Human fit mRNA for X51602 165070 Dinucleotide repeat receptor-related tyrosine kinase Human heparin- M32977 192240 none found binding vascular endothelial growth factor (VEGF) mRNA, complete cds Human hepatic lipase J03540 151670 SER267PHE mRNA, complete cds Human hepatic lipase J03540 151670 THR383MET mRNA, complete cds Human hormone- U40002 151750 dinucleotide repeat sensitive lipase testicular isoform mRNA, complete cds Human hormone- U40002 151750 Arg309Cys sensitive lipase testicular isoform SD-144141.1 Page 16 mRNA, complete cds Human integrin alpha 9 L24158 603963 none found protein mRNA, 3'end Human IP gene for D38128 600022 none found prostacyclin receptor, exon 3 Human kidney mRNA X00063 179820 ARG387TER fragment for renin (aa 105-401) Human lipid-activated, U33052 602549 none found protein kinase PRK2 mRNA, complete cds Human mRNA for D 14874 103275 none found adrenomedullin, complete cds Human mRNA for X52947 121014 GCG->GTG Ala253Val cardiac gap junction protein Human mRNA for D26309 601329 none found LIMK (LIM kinase), complete cds Human mRNA for D45906 601988 none found LIMK-2, complete cds Human mRNA for X15357 108960 none found natriuretic peptide receptor (ANP-A receptor) Human mRNA for X05199 173350 IVS 17, 1-BP DEL, plasminogen G, +1 Human mRNA for X05199 173350 Taql plasminogen SD-144141.1 Page 16 Human mRNA for X05199 173350 GLU460TER plasminogen Human mRNA for X05199 173350 ALA600THR plasminogen Human mRNA for X05199 173350 Ala675Thr plasminogen Human mRNA for X05199 173350 ARG216HIS plasminogen Human mRNA for X05199 173350 D676N plasminogen Human mRNA for X05199 173350 GLY732ARG plasminogen Human mRNA for X05199 173350 LYS19GLU plasminogen Human mRNA for X05199 173350 LYS212DEL plasminogen Human mRNA for X05199 173350 SER572PRO plasminogen Human mRNA for X05199 173350 TRP597TER plasminogen Human mRNA for X05199 173350 VAL355PHE plasminogen Human mRNA for X06374 173430 none found Dlatelet-derived growth factor PDGF-A Human mRNA for X04665 188060 none found thrombospondin Human mRNA for X02812 190180 72 transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 -509 SD-144141.1 Page 16 transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 -800 transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 -988 transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 713-8delC intron 4 transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 C788-T thr263iso transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 Arg25~>Pro transforming growth factor-beta (TGF-beta) Human mRNA for X02812 190180 Leul 0->Pro transforming growth factor-beta (TGF-beta) Human mRNA for type Y07512 176894 none found I beta cGMP- dependent protein kinase (EC 2.7.1.37) Human myoadenylate M60092 102770 C143->T PRO48LEU deaminase (AMPD1) mRNA, complete cds Human myoadenylate M60092 102770 C34-T Gln->Stop deaminase (AMPD1) mRNA, complete cds Human neuronal nitric U17327 163731 none found SD-144141.1 Page 16 oxide synthase (NOSl) mRNA, complete cds Human neutrophil M21 186 233690 1 -BP DEL, 272C cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21186 233690 10-KB DEL cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21186 233690 IVS4DS, G-A, +1 cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21186 233690 ARG90GLN cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21186 233690 HIS72TYR cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21 186 233690 HIS94ARG cytochrome b light chain p22 phagocyte b- cytochrome mRNA, SD-144141.1 Page 16 complete cds Human neutrophil M21 186 233690 PRO156GLN cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M21186 233690 SER118ARG cytochrome b light chain p22 phagocyte b- cytochrome mRNA, complete cds Human neutrophil M3201 1 233710 5-nucleotide del nts oxidase factor (p67- 1 169-1 173 phox) mRNA, complete cds Human neutrophil M32011 233710 9-nt in-frame oxidase factor (p67- deletion in exon 2 phox) mRNA, (nts 55-63) complete cds Human neutrophil M32011 233710 C(304) -> T oxidase factor (ρ67- phox) mRNA, complete cds Human neutrophil M3201 1 233710 del A(728) oxidase factor (p67- phox) mRNA, complete cds Human neutrophil M32011 233710 intron 4 (G --> A) oxidase factor (p67- phox) mRNA, complete cds SD- 144141 1 Page 16 Human p21 -activated U24152 602590 none found protein kinase (Pakl) gene, complete cds Human M63603 172405 none found phospholamban mRNA, complete cds Human platelet M25827 173515 Alal39(ACC)~ glycoprotein IX >Thr(GCC) mRNA, 3' end Human platelet M25827 173515 ASN45SER glycoprotein IX mRNA, 3' end Human platelet M25827 173515 ASP21GLY glycoprotein IX mRNA, 3' end Human platelet M25827 173515 LEU40PRO glycoprotein IX mRNA, 3' end Human platelet M25827 173515 PHE55SER glycoprotein IX mRNA, 3' end Human platelet-derived M21616 173410 none found growth factor (PDGF) receptor mRNA, complete cds Human protein kinase L18964 300094 none found C iota isoform (PRKCI) mRNA, complete cds Human RASF-A PLA2 M22430 172411 2-BP DEL frameshift mRNA, complete cds SD- 144141.1 Page 160 Human receptor for M9121 1 600214 none found advanced glycosylation end products (RAGE) mRNA, partial cds Human steroid 5-alpha- M74047 264600 1-BP DEL PRO251 DEL reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 null allele reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY196SER reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 LEU55GLN reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 ARG227TER reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 ARG246TRP reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY1 15ASP reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 GLY183SER reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 HIS231ARG reductase 2 (SRD5A2) mRNA, complete cds SD-144141.1 Page 160 Human steroid 5-alpha- M74047 264600 MET157DEL reductase 2 (SRD5A2) mRNA, complete cds Human steroid 5-alpha- M74047 264600 THR228ALA reductase 2 (SRD5A2) mRNA, complete cds Human steroidogenic U17280 600617 840delA acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 IVS4AS, T-A, -11 acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 IVS2, 1 -BP acute regulatory INS, T, +3 protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 1-BP DEL, acute regulatory 261T protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 ARG182LEU acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U 17280 600617 D203A acute regulatory protein (StAR) mRNA, complete cds Human steroidogenic U17280 600617 GLN258TER SD-144141.1 Page 16 acute regulatory protein (StAR) mRNA, complete cds Human TGF-beta type M85079 190182 2-BP INS Frameshift II receptor mRNA, complete cds Human TGF-beta type M85079 190182 THR315MET II receptor mRNA, complete cds Human fhiazide- U44128 600968 3-BP DEL sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 1 19-bp insertion sensitive Na-Cl between exons 3 and cotransporter (hTSC) 4 mRNA, complete cds Human thiazide- U44128 600968 exon 24 was deleted sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 intron 24, GGT --> sensitive Na-Cl GTT cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 intron 3, CAG --> sensitive Na-Cl CAA cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 IVS 15 AS, G-T, -1 sensitive Na-Cl SD-144141.1 Page 16 cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 IVS23DS, G-T, +1 sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 ALA588VAL sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 ARG209TRP sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 ARG653LEU sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 ARG655HIS sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 CYS421ARG sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 GLY630VAL sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 LEU623PRO SD-144141.1 Page 16 sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 LEU850PRO sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thiazide- U44128 600968 PRO349LEU sensitive Na-Cl cotransporter (hTSC) mRNA, complete cds Human thrombopoietin U68162 159530 none found receptor (MPL) gene Human M81339 188061 none found thrombospondin mRNA Human tie mRNA for X60957 600222 none found putative receptor tyrosine kinase Human transferrin M12530 190000 Aval mRNA, complete cds Human transferrin M12530 190000 ASP277GLY mRNA, complete cds Human transferrin M12530 190000 GLY652GLU mRNA, complete cds Human transferrin M12530 190000 HIS300ARG mRNA, complete cds Human transferrin M12530 190000 LYS627GLU mRNA, complete cds Human transferrin M12530 190000 PRO570SER mRNA, complete cds SD- 144141.1 Page 16 Human transforming L07594 600742 none found growth factor-beta type III receptor (TGF-beta) mRNA, complete cds Human urokinase gene, K02286 191840 BamHl 3 * end Human urokinase gene, K02286 191840 C to T change near 3' end ' the beginning of exon 8 Human urokinase gene, K02286 191840 Leu residue by 3' end a Pro, in the kringle domain Human vascular U43142 601528 none found endothelial growth factor related protein VRP mRNA, complete cds Human VEGF related U43368 601398 none found factor isoform VRF186 precursor (VRF) mRNA, complete cds Hydroxy-delta-5- M67466 201810 1-BP INS steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 Dinucleotide repeat steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 ARG249TER steroid dehydrogenase, SD-144141.1 Page 16 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 TRP171TER steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 Hydroxy-delta-5- M67466 201810 VAL248ASN steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 interleukin 1 beta K02770 147720 +5887 C -> T (ILlb) interleukin 1 beta K02770 147720 exon 5 (position (ILlb) +3953) interleukin 1 beta K02770 147720 position -511 (ILlb) interleukin 1 beta K02770 147720 Taql (ILlb) interleukin 1 beta K02770 147720 Aspl 06Asn (ILl b) INTERLEUKIN 1 X65019 147678 none found BETA CONVERTASE PRECURSOR interleukin 1 receptor M27492 147810 Pstl (IL-1R) interleukin 12a (ILl 2a) M65271 161560 none found interleukin 12b (ILl 2b) M65272 161561 4.4-KB DEL interleukin 2 (IL2) X01586 147680 -330 interleukin 2 (IL2) X01586 147680 166 interleukin 2 (IL2) X01586 147680 AUUUA motif deleted SD-144141.1 Page 16 interleukin 2 (IL2) X01586 147680 Dinucleotide Repeat interleukin 2 receptor M26062 146710 CA repeat beta (IL-2Rb) interleukin 2 receptor D1 1086 308380 690-691 hotspot gamma (IL-2Rg) interleukin 2 receptor D11086 308380 9-BP DUP GLN-HIS-TRP gamma (IL-2Rg) INS interleukin 2 receptor D1 1086 308380 G-to-A first position gamma (IL-2Rg) of intron 3 interleukin 2 receptor DI 1086 308380 ARG222CYS gamma (IL-2Rg) interleukin 2 receptor D11086 308380 ARG267TER gamma (IL-2Rg) interleukin 2 receptor D1 1086 308380 ARG285GLN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 CYS115ARG gamma (IL-2Rg) interleukin 2 receptor D1 1086 308380 CYS62TER gamma (IL-2Rg) interleukin 2 receptor DI 1086 308380 GLY1 14ASP gamma (IL-2Rg) interleukin 2 receptor D1 1086 308380 ILE153ASN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 LEU271GLN gamma (IL-2Rg) interleukin 2 receptor D11086 308380 LYS97TER gamma (IL-2Rg) interleukin 2 receptor D1 1086 308380 SER286TER gamma (IL-2Rg) interleukin 4 (IL4) M 13982 147780 -285 C-T interleukin 4 (IL4) M 13982 147780 -81 A-G SD-144141.1 Page 16 interleukin 4 (IL4) M13982 147780 C-589T interleukin 4 (IL4) M13982 147780 Dinucleotide Repeat intron 2 interleukin 4 receptor X52425 147781 GLN576ARG interleukin 4 (IL-4R) interleukin 4 receptor X52425 147781 S503P (IL-4R) interleukin 6 (IL6) M14584 147620 CA repeat interleukin 6 (IL6) M14584 147620 174G-C interleukin 6 (IL6) M14584 147620 AT repeat interleukin 6 (IL6) M14584 147620 Bgll interleukin 6 (IL6) M14584 147620 Bglll interleukin 6 (IL6) M14584 147620 Mspl interleukin 6 (IL6) M14584 147620 Nlalll promoter interleukin 6 receptor M20566 147880 dinucleotide (CA) (IL-6R) (20) interleukin receptor 1 1 U32324 600939 none found alpha (IL-1 l a) interleukin receptor 12 U03187 601642 none found beta2 (IL-12b2) K+ channel (KvLQTI) AF000571 192500 7-BP DEL AND 8- BP INS K+ channel (KvLQTI) AF000571 192500 1-BP INS, 282G K+ channel (KvLQTI) AF000571 192500 3-BP DEL K+ channel (KvLQTI) AF000571 192500 9-BP DEL, NT373 K+ channel (KvLQTI) AF000571 192500 ALA300THR K+ channel (KvLQTI) AF000571 192500 ALA341GLU K+ channel (KvLQTI ) AF000571 192500 ALA341 VAL K+ channel (KvLQTI ) AF000571 192500 ALA529THR SD-144141.1 Page 16 K+ channel (KvLQTI) AF000571 192500 ALA83PRO K+ channel (KvLQTI) AF000571 192500 ARG518TER K+ channel (KvLQTI) AF000571 192500 ARG555CYS K+ channel (KvLQTI) AF000571 192500 ARG95GLN K+ channel (KvLQTI) AF000571 192500 GLY189ARG K+ channel (KvLQTI ) AF000571 192500 GLY21 1ARG K+ channel (KvLQTI) AF000571 192500 GLY219SER K+ channel (KvLQTI) AF000571 192500 GLY250GLU K+ channel (KvLQTI) AF000571 192500 LEU178PHE K+ channel (KvLQTI) AF000571 192500 PHE339DEL K+ channel (KvLQTI) AF000571 192500 THR217ILE K+ channel (KvLQTI) AF000571 192500 TRP305SER K+ channel (KvLQTI) AF000571 192500 VAL159MET L-type voltage NM 0007 114205 none found dependent calcium 19 channel alpha 1 C subunit/CACNAl C Leukocyte integrin U28252 135630 none found beta-1 Leukocyte integrin M35999 173470 11.2-KB DEL beta-3 Leukocyte integrin M35999 173470 G-T, EXiDEL beta-3 Leukocyte integrin M35999 173470 ARG143GLN beta-3 Leukocyte integrin M35999 173470 ARG214GLN beta-3 Leukocyte integrin M35999 173470 ARG214TRP beta-3 Leukocyte integrin M35999 173470 ARG489GLN beta-3 SD-144141 - 1 Page 16 Leukocyte integrin M35999 173470 ARG724TER beta-3 Leukocyte integrin M35999 173470 ASP1 19TYR beta-3 Leukocyte integrin M35999 173470 CYS374TYR beta-3 Leukocyte integrin M35999 173470 GLU616TER beta-3 Leukocyte integrin M35999 173470 LEU33PRO beta-3 Leukocyte integrin M35999 173470 PRO407ALA beta-3 Leukocyte integrin M35999 173470 SER752PRO beta-3 Lipoprotein lipase M15856 238600 INS Lipoprotein lipase M15856 238600 (TTTA)n Lipoprotein lipase M15856 238600 -39T-C Lipoprotein lipase M15856 238600 -93T-G Lipoprotein lipase M15856 238600 1-BP DEL frameshift Lipoprotein lipase M15856 238600 1-BP DEL, 22 IG frameshift Lipoprotein lipase M15856 238600 2-KB DUP Lipoprotein lipase M15856 238600 6-KB DEL Lipoprotein lipase M15856 • 238600 C->A -3 intron 6 Lipoprotein lipase M15856 238600 C-to-T -480 Lipoprotein lipase M15856 238600 C1338->A Thr361 Thr Lipoprotein lipase M15856 238600 C1595->G S447X Lipoprotein lipase M15856 238600 G579->A V108V Lipoprotein lipase M15856 238600 Hindlll Lipoprotein lipase M15856 238600 IVS 1, G-C, +1 Lipoprotein lipase M15856 238600 IVS2DS, G-A Lipoprotein lipase M15856 238600 IVS2DS, G-A, +1 SD-144141.1 Page 16 Lipoprotein lipase M15856 238600 ILE194THR Lipoprotein lipase M15856 238600 ILE225THR Lipoprotein lipase M15856 238600 TRP382TER Lipoprotein lipase M 15856 238600 TYR61TER Lipoprotein lipase M15856 238600 ALA176THR Lipoprotein lipase M15856 238600 ALA334THR Lipoprotein lipase M15856 238600 ARG243CYS Lipoprotein lipase M15856 238600 ARG243HIS Lipoprotein lipase M15856 238600 ARG75SER Lipoprotein lipase M15856 238600 ASN291SER Lipoprotein lipase M15856 238600 ASP156GLY Lipoprotein lipase M15856 238600 ASP180GLU Lipoprotein lipase M15856 238600 ASP204GLU Lipoprotein lipase M15856 238600 ASP250ASN Lipoprotein lipase M15856 238600 ASP9ASN Lipoprotein lipase M15856 238600 Cys239->stop Lipoprotein lipase M15856 238600 CYS418TYR Lipoprotein lipase M15856 238600 E163G Lipoprotein lipase M15856 238600 E410K Lipoprotein lipase M15856 238600 GLN106TER Lipoprotein lipase M15856 238600 Glul lδ Glu Lipoprotein lipase M15856 238600 Glu421Lys Lipoprotein lipase M15856 238600 GLY142GLU Lipoprotein lipase M15856 238600 GLY188GLU Lipoprotein lipase M15856 238600 GLY195GLU Lipoprotein lipase M15856 238600 Hisl83->Gln Lipoprotein lipase M15856 238600 LEU365VAL Lipoprotein lipase M15856 238600 Pro 157 Arg Lipoprotein lipase M15856 238600 PRO207LEU Lipoprotein lipase M15856 238600 SER172CYS Lipoprotein lipase M15856 238600 SER244THR SD-144141.1 Page 161 Lipoprotein lipase M15856 238600 SER447TER Lipoprotein lipase M15856 238600 TRP64TER Lipoprotein lipase M 15856 238600 TRP86ARG Lipoprotein lipase M15856 238600 Tyr262->His Lipoprotein lipase M15856 238600 TYR73TER Lipoxygenases: 5- J03571 152390 none found lipoxygenase (leukocytes) Mineralocorticoid M16801 600983 1-BP DEL frameshift at receptor (aldosterone codon 337 receptor) Mineralocorticoid M16801 600983 1-BP DEL frameshift at receptor (aldosterone codon 459 receptor) Mineralocorticoid M16801 600983 760->G760 lieu 180-- receptor (aldosterone >Vall80 receptor) Mineralocorticoid M16801 600983 A DEL, +3 intron 5 receptor (aldosterone receptor) Mineralocorticoid M16801 600983 C944-NT944 Ala241- receptor (aldosterone >Val241 receptor) Mineralocorticoid M16801 600983 ARG537TER receptor (aldosterone receptor) myeloperoxidase X04876 254600 C8089T ARG569TRP myeloperoxidase X04876 254600 Dinucleotide Repeat myeloperoxidase X04876 254600 EcoRV myeloperoxidase X04876 254600 G to A (promoter) myeloperoxidase X04876 254600 Kpnl SD-144141 - 1 Page 16 myeloperoxidase X04876 254600 Pstl myeloperoxidase X04876 254600 MET251THR myeloperoxidase X04876 254600 TYR173CYS MYOSIN-BINDING 600958 5-BP DEL, EX25 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 IVS, G-A, +1 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 12-BP DUP/4-BP PROTEIN C, DEL CARDIAC MYOSIN-BINDING 600958 18-BP DUP PROTEIN C, CARDIAC MYOSIN-BINDING 600958 BRANCH POINT, PROTEIN C, IVS23, A-G, TGAT- CARDIAC TGGT MYOSIN-BINDING 600958 IVS, A-G PROTEIN C, CARDIAC MYOSIN-BINDING 600958 IVS, G-C, +5 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 IVS23, G-A, +1 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 IVS7, G-A, +5 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 Arg654His SD- 144141.1 Page 16 PROTEIN C, CARDIAC MYOSIN-BINDING 600958 Glu 1096 PROTEIN C, termination CARDIAC codon MYOSIN-BINDING 600958 GLU542GLN PROTEIN C, CARDIAC NEPHRIN 602716 1-BP INS, , 3250G NEPHRIN 602716 2-BP DEL, 121CT NEPHRIN 602716 2-BP INS, 1306AC NEPHRP 602716 ARG1 109TER Neuropeptide Y M84755 162641 none found receptor Yl /NPY IR Nicotinic, Cholinergic X14830 100710 LEU263MET receptor beta 1 Nicotinic, Cholinergic X14830 100710 VAL266MET receptor beta 1 Nicotinic, Cholinergic X66403 100725 ARG147LEU receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 ARG64TER receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 LEU269PHE receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 PROI 21 LEU receptor epsilon polypeptide Nicotinic, Cholinergic X66403 100725 THR264PRO SD-144141 Page 16 receptor epsilon polypeptide NITRIC OXIDE 163729 GLU298ASP SYNTHASE 3 NITRIC OXIDE 600719 none found SYNTHASE, MACROPHAGE, TYPE 2B NITRIC OXIDE 600720 none found SYNTHASE, MACROPHAGE, TYPE 2C; NOS2C paraoxonase 1/PONl AH00419 168820 CA repeat intron 4. (arylesterase) 3 paraoxonase 1/PONl AH00419 168820 GLN192ARG (arylesterase) 3 paraoxonase 1/PONl AH00419 168820 Leu55Met (arylesterase) 3 paraoxonase 1/PONl AH00419 168820 MET54LEU (arylesterase) 3 phenylethanolamine N- NM 0026 171190 BANI methyltransferase/PN 86 MT Phospholipase A-2 M21054 172410 none found (PLA-2) lung Phospholipase A2, M68874 600522 none found group IV Phospholipase C beta-3 Z26649 600230 none found Phospholipase C, beta L41349 600810 none found 4 plasma cholesterol NM_0000 118470 A1503G SD-144141.1 Page 16 ester transfer 78 protein/CETP plasma cholesterol NM_0000 118470 G-A splice junction alternative ester transfer 78 splice protein/CETP plasma cholesterol NM_0000 118470 G1696A ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 C-T transition in ester transfer 78 intron 12 protein/CETP plasma cholesterol NM 0000 1 18470 EcoNI ester transfer 78 protein/CETP plasma cholesterol NM 0000 1 18470 G~>A intron 14 ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 G-A transition in ester transfer 78 intron 15 protein/CETP plasma cholesterol NM 0000 1 18470 G1533A ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 INS T alternative ester transfer 78 (intron/exonl4) splice protein/CETP plasma cholesterol NM 0000 118470 Stul ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 T->G tyr57stop ester transfer 78 SD-144141.1 Page 16 protein/CETP plasma cholesterol NM_0000 118470 TaqlA ester transfer 78 protein/CETP plasma cholesterol NMJ3000 118470 TaqlB in intron 1 ester transfer 78 protein CETP plasma cholesterol NM_0000 118470 268 Arg- ester transfer 78 >STOP protein/CETP plasma cholesterol NM_0000 1 18470 Asp 442 to Gly ester transfer 78 protein CETP plasma cholesterol NM_0000 118470 ASP442GLY ester transfer 78 protein CETP plasma cholesterol NM_0000 118470 G181X ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 I405V ester transfer 78 protein/CETP plasma cholesterol NM 0000 1 18470 Lys309-Stop ester transfer 78 protein CETP plasma cholesterol NM 0000 118470 R451Q ester transfer 78 protein/CETP plasma cholesterol NM 0000 118470 Val421-Ile ester transfer 78 protein/CETP SD-144141.1 Page 16 Platelet glycoprotein X06831 273800 1 1 -BP DEL, EX12 Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 13-BP DEL AT Ilb/IIIa (fibrogen INTRON-EXON receptor) BOUNDARY OF EXON 4 Platelet glycoprotein X06831 273800 4.5-KB DEL, EX2-9 Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 IVS15DS, G-A, +1 Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 IVS25AS, C-G, -3 Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 ARG327HIS Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 ARG584TER Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 ASP426DEL Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 GLU324LYS Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 GLY273ASP Ilb/IIIa (fibrogen receptor) SD- 144141.1 Page 1 Platelet glycoprotein X06831 273800 GLY418ASP Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 ILE565THR Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 ILE843SER Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 LEU214PRO Ilb/IIIa (fibrogen receptor) Platelet glycoprotein X06831 273800 VAL425DEL Ilb/IIIa (fibrogen receptor) Platelet-activating M76674 173393 none found factor receptor Potassium channel U04270 152427 1-BP DEL subunit (h-erg) Potassium channel U04270 152427 27-BP DEL subunit (h-erg) Potassium channel U04270 152427 IVS3, G-C, +1 subunit (h-erg) Potassium channel U04270 152427 VAL822MET subunit (h-erg) Potassium channel U04270 152427 ALA561VAL subunit (h-erg) Potassium channel U04270 152427 ARG582CYS subunit (h-erg) Potassium channel U04270 152427 ASN470ASP subunit (h-erg) SD-144141.1 Page 1 Potassium channel U04270 152427 GLY628SER subunit (h-erg) Potassium channel U04270 152427 ILE593ARG subunit (h-erg) POTASSIUM 603796 GLN9GLU CHANNEL, VOLTAGE-GATED, ISK-RELATED SUBFAMILY, MEMBER 2 POTASSIUM 603796 ILE57THR CHANNEL, VOLTAGE-GATED, ISK-RELATED SUBFAMILY, MEMBER 2 POTASSRJM 603796 MET54THR CHANNEL, VOLTAGE-GATED, ISK-RELATED SUBFAMILY, MEMBER 2 progesterone receptor M 15716 264080 none found PROTEIN KINASE C, 176975 none found EPSILON PROTEIN KINASE, 600497 none found AMP-ACTIVATED, CATALYTIC, ALPHA-2 PROTEIN KINASE, 602743 none found AMP-ACTIVATED, SD- 144141.1 Page 16 NONCATALYTIC, GAMMA-2; PRKAG2 S-adenosyl M61831 180960 none found homocysteine hydrolase serotonin 5-HT X57829 109760 Rsal receptors 5-HT 1 A, G protein-coupled serotonin 5-HT Y08756 602164 none found receptors 5-HT4, G protein-coupled small inducible M28226 158105 -2076 (A or T) cytokine subfamily A (Cys-Cys), member 2/monocyte chemotactic protein 1/MCP1/SCYA2 small inducible M28226 158105 -2518 (G or A) cytokine subfamily A (Cys-Cys), member 2/monocyte chemotactic protein 1/MCP1/SCYA2 Solute carrier family 9 M81768 107310 none found (sodium/hydrogen exchanger) Steroid 5 alpha M32313 184753 none found reductase 1 Superoxide dismutase X02317 147450 1 (Cu/Zn) Superoxide Dismutase NM_0004 147450 T-G, -10, 9-BP INS SD-144141.1 Page 1 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 VS4AS, A-G, -1 1 1 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ALA145THR 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ALA4THR 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ALA4VAL 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ASP90ALA 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 CYS6PHE 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLUIOOGLY 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLU21LYS 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY16SER 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY37ARG 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY41 ASP 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY41SER 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY72SER 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY85ARG 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 GLY93ALA 1/SODl (soluble) 54 SD- 144141.1 Page 163 Superoxide Dismutase NM 0004 147450 GLY93CYS 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 HIS43ARG 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 HIS46ARG 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ILE104THE 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 ILE1 13THR 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU 106 VAL 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU126TER 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU144SER 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU38VAL 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 LEU84VAL 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 SER134ASN 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 THR151ILE 1/SODl (soluble) 54 Superoxide Dismutase NM 0004 147450 Val7->Glu 1/SODl (soluble) 54 Superoxide Dismutase X65965 147460 ALA16VAL 2/SOD2 (mitochondrial) Tafazzin 300069 none found Thimet oligopeptidase Z501 15 601 1 17 none found SD-144141.1 Page 163 Thrombopoietin U70136 600044 1-BP DEL, 3252G Thrombopoietin U70136 600044 IVS3, G-C +l THROMBOSPONDIN 188062 none found III Thromboxane synthase M80646 274180 (CA)n intron 9 Tissue Plasminogen M 18182 173370 BgW activator, tissue type (t- PA) Tissue Plasminogen M18182 173370 EcoRI activator, tissue type (t- PA) Tissue Plasminogen M18182 173370 Hindi activator, tissue type (t- PA) Tissue Plasminogen M18182 173370 polymoφhic activator, tissue type (t- dinucleotide intron 1 PA) Tissue Plasminogen M 18182 173370 Pstl activator, tissue type (t- PA) Tissue Plasminogen M18182 173370 Taql activator, tissue type (t- PA) Tissue Plasminogen M18182 173370 Xmnl activator, tissue type (t- PA) Transferrin receptor X01060 190010 Bell (p90, CD71 ) Transferrin receptor X01060 190010 Rsal (p90, CD71) tRNA-LEU, 590050 3243A-G SD- 144141.1 Page 16 MITOCHONDRIAL tRNA-LEU, 590050 3250T-C MITOCHONDRIAL tRNA-LEU, 590050 3251 A-G MITOCHONDRIAL tRNA-LEU, 590050 3252T-C MITOCHONDRIAL tRNA-LEU, 590050 3256C-T MITOCHONDRIAL tRNA-LEU, 590050 3260A-G MITOCHONDRIAL tRNA-LEU, 590050 3271T-C MITOCHONDRIAL tRNA-LEU, 590050 3303C-T MITOCHONDRIAL tRNA-LEU, 590050 A3288G MITOCHONDRIAL tRNA-LEU, 590050 G -> A 12301 MITOCHONDRIAL Type V cyclic AJ004865 603310 none found nucleotide phosphodiesterase type V voltage NM_0003 600163 1-BP DEL frameshift dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM_0003 600163 2-BP INS dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM 0003 600163 SD-144141 , 1 Page 163 dependent sodium 35 LYS1505/PRO1 channel alpha 506/GLN1507D subunit/SCN5A EL type V voltage NM_0003 600163 ARG1232TRP dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM_0003 600163 ARG1623GLN dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM_0003 600163 ARG1644HIS] dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM_0003 600163 GLU1784LYS dependent sodium 35 channel alpha subunit/SCN5A type V voltage NM_0003 600163 THR1620MET dependent sodium 35 channel alpha subunit/SCN5A Vascular cell adhesion M60335 192225 none found molecule 1 vitamin B12 NM_0010 602997 IVS6, C-G receptor/cubilin/CUBN 81 vitamin B12 NM_0010 602997 PRO1297LEU receptor/cubilin/CUBN 81 SD-144141 1 Page 163 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110-1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-1441101 Page 16 SD-144110.1 Page 1 SD-144110-1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110-1 Page 16 SD-1441101 Page 16 SD-1441I0.1 Page 1 cn ST) vo SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-1441101 Page 16 oo V σs IT) SD-144110-1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110-1 Page 16 SD-144110-1 Page 16 SD-144110-1 Page 16 SD-144110-1 Page 16 SD-1441101 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-1441101 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110-1 Page 1 SD-1441101 Page 16 SD-1441101 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-1441101 Page 1 SD-1441101 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 16 SD-144110.1 Page 1 SD-1441 10 i Page 16 SD-144110.1 Page 16 SD-1441101 Page 1 SD-144110.1 Page 16 SD-144110 1 Page 1 o Os SO ω w- re ft Q n SD-1441101 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 16 SD-144110.1 Page 1 SD-1441101 Page 1 SD-144110.1 Page 1 SD-144110-1 Page 16 Os Os so ω oo re ft SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-1441101 Page 17 SD-144110-1 Page 1 SD-144110 1 Page 17 SD-144110.1 Page 17 SD-1441101 Page 1 SD-144110-1 Page 17 SD-1441 10 1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110-1 Page 1 SD-144110 1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-1441 10 1 Page 17 SD-144110-1 Page 17 SD-144110-1 Page 17 SD-144110.1 Page 17 SD-1441101 Page 17 SD-144110.1 Page 1 SD-1441101 Page 17 SD-144110.1 Page 1 SD-144110 1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110 1 Page 1 - Pa e 1 SD-144110.1 Page 1 SD-1441101 Page 1 SD-1441101 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-1441101 Page 17 SD-144110 1 Page 17 SD-1441101 Page 17 SD-1441101 Page 17 SD-1441101 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-1441101 Page 1 SD-144110-1 Page 17 SD-144110.1 Page 1 SD-14110.1 Page 17 SD-M4110.1 Page 1 SD-1441 10.1 Page 1 SD-144110.1 Page 17 SD-1441101 Page 17 SD-1441101 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110 1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-1441 10.1 Page 17 SD-144110.1 Page 17 SD-1441101 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 176 SD-144110.1 Page 17 SD-144110 1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-1441101 Page 17 SD-144110 1 Page 17 SD-1441101 Page 17 SD-1441101 Page 1 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-144110 1 Page 1 SD-144110 1 Page 1 SD-1441101 Page 17 SD-144110.1 Page 17 SD-144110 1 Page 17 SD-144110.1 Page 17 SD-144110- Page 1 SD-144110.1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-1441101 Page 17 SD-144110.1 Page 1 SD-144110-1 Page 17 SD-144110 1 Page 17 SD-144110.1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-1441101 Page 17 SD-144110 1 Page 17 SD-144110.1 Page 1 SD-144110.1 Page 17 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-1441101 Page 18 SD-144110.1 Page 1 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD- 144110-1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.I Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-144110 1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110 1 Page 18 SD-144110.1 Page 183 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-I UIOI Page 18 SD-144110.I Page 1 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110-1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 1 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-14 4 110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110.1 Page 1 SD-144110 1 Page 18 SD-144110.1 Page 18 - SD-144110 1 Page 188 SD-1441101 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 18 SD-144110.1 Page 1 SD-1441101 Page 18 SD-144110.1 Page 18 SD-144110,1 Page 18 SD-144110.1 Pa e 18 kietirelix; RS 68439 Discontinued N-acetyl-3-(2- gonadorelin antagonist contraception; canceη naphthalenyl)-D- alanyl-4-chloro-D- Phenylalanyl-D- tryptophyl-L-seryl-L- tyrosyl-N6- [bis(ethylamino)meth ylene]-D-lysyl-L- leucyl-L-arginyl-L- prolyl-D-alaninamide drug delivery system, Discontinued gonadorelin antagonist cancer; ATRIGEL sustained endometriosis release ganirelix; ganirelix ATRIGEL drug delivery system, (Discontinued gonadorelin antagonist endometriosis; ATRIGEL sustained cancer release GnRH antagonists drug delivery system, [Preclinical gonadorelin antagonist cancer; contraception microcapsule SB 75; SB 75 microcapsule gonadotropin Preclinical gonadorelin antagonist contraception; canceη releasing hormone antagonists, Alanex gonadotropin- [Preclinical [gonadorelin antagonist cancer releasing hormone antagonist, Agouron; GnRH antagonist, Agouron HOE 2013 Suspended gonadorelin antagonist cancer; endometriosis SD-1441 10.1 Page 18 SD-144110.1 Page 18 SD-144110 1 Page 18 SD-144110-1 Page 19 SD-1441101 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 1 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110 1 Page 191 SD-144110.1 Page 19 SD-144110.1 Page 191 SD-144110.1 Page 19 SD-1441101 Page 191 SD-1441101 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 191 SD-144110.1 Page 19 SD-144110 1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 193 SD-144110.1 Page 19 SD-144110.1 Page 193 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 193 SD-144110.1 Page 193 SD-144110.1 Page 19 SD-144110.1 Page 19 CN SD-14 4 110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 195 SD-144110.1 Page 19 SD-144110 1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 actinoplanone B; R [Discontinued [1S- polycyclic xanthone; bacterial infection; 304H (lalfa,3alfa,4beta,8aal antibiotic cancer fa)]-l l-chloro- 3,4,8a, 13-tetrahydro- 3,15,16-trihydroxy- l,4-dimethoxy-12- methyl-lH- xantheno[4',3',2':4,5][ 1 ,3]benzodioxino[7,6- g]isoquinoline- 14,17(2H,9H)-dione actinoplanone C; R Discontinued [IS- polycyclic xanthone; bacterial infection; 304J (lalfa,3alfa,4beta,8aal antibiotic cancer fa)]-13-amino- 3,4,8a, 13-tetrahydro- 3,15,16-trihydroxy- 1 ,4-dimethoxy- 12- methyl-lH- xantheno[4',3',2':4,5][ l,3]benzodioxino[7,6- g]isoquinolone- 14,17(2H,9H)-dione SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110. Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110 1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 19 SD-144110.1 Page 199 SD-144110.1 Page 19 SD-144110.1 Page 19 SD-144110-1 Page 19 SD-144110.1 Page 19 SD-144110.I Page 19 SD-144110 1 Page 199 SD-144110.1 Page 19 SanDiego-144144.1 Page 2000 SanDiego-144144.1 Page 2001 SanDiego-144144.1 Page 2002 SanDiego-144144.1 Page 2003 SanDiego-144144.1 Page 2004 SanDiego-144144.1 Page 2005 SanDiego-144144.1 Page 2006 SanDiego-144144.1 Page 2007 SanDiego-144144.1 Page 2008 SanDiego-144144.1 Page 2009 SanDiego-144144.1 Page 2010 SanDiego-144144.1 Page 2011 SanDiego-144144.1 Page 2012 SanDiego-144144.1 Page 2013 SanDiego-144144.1 Page 2014 SanDiego-144144.1 Page 2015 SanDiego-144144.1 Page 2016 SanDiego-144144.1 Page 2017 SanDiego-144144.1 Page 2018 SanDiego-144144.1 Page 2019 SanDiego-144144.1 Page 2020 SanDiego-144144.1 Page 2021 SanDiego-144144.1 Page 2022 SanDiego-144144.1 Page 2023 SanDiego-144144.1 Page 2024 SanDiego-144144.1 Page 2025 SanDiego-144144.1 Page 2026 Table 27. Current Candidate Therapeutic Interventions for the Treatment of Dementia San Diego-144144.1 Page 2027 SanDiego-144144.1 Page 2028 SanDiego-144144.1 Page 2029 SanDiego-144144.1 Page 2030 SanDiego-144144.1 Page 2031 SanDiego-144144.1 Page 2032 SanDiego-144144.1 Page 2033 SanDiego-144144.1 Page 2034 SanDiego-144144.1 Page 2035 SanDiego-144144.1 Page 2036 SanDiego-144144.1 Page 2037 SanDiego-144144.1 Page 2038 SanDiego-144144.1 Page 2039 SanDiego-144144.1 Page 2040 SanDiego-144144.1 Page 2041 SanDiego-144144.1 Page 2042 SanDiego-144144.1 Page 2043 SanDiego-144144.1 Page 2044 SanDiego-144144.1 Page 2045 SanDiego-144144.1 Page 2046 SanDiego-144144.1 Page 2047 SanDiego-144144.1 Page 2048 SanDiego-144144.1 Page 2049 SanDiego-144144.1 Page 2050 SanDiego-144144.1 Page 2051 SanDiego-144144.1 Page 2052 SanDiego-144144.1 Page 2053 SanDiego-144144.1 Page 2054 SanDiego-144144.1 Page 2055 SanDiego-144144.1 Page 2056 SanDiego-144144.1 Page 2057 SanDiego-144144.1 Page 2058 SanDiego-144144.1 Page 2059 SanDiego-144144.1 Page 2060 SanDiego-144144.1 Page 2061 SanDiego-144144.1 Page 2062 SanDiego-144144.1 Page 2063 SanDiego-144144.1 Page 2064 SanDiego-144144.1 Page 2065 SanDiego-144144.1 Page 2066 Sa Diego-144144.1 Page 2067 SanDiego-144144.1 Page 2068 SanDiego-144144.1 Page 2069 SanDiego-144144.1 Page 2070 SanDiego-144144.1 Page 2071 SanDiego-144144.1 Page 2072 SanDiego-144144.1 Page 2073 SanDiego-144144.1 Page 2074 SanDiego-144144.1 Page 2075 SanDiego-144144.1 Page 2076 SanDiego-144144.1 Page 2077 SanDiego-144144.1 Page 2078 Sa Diego-144144.1 Page 2079 SanDiego-144144.1 Page 2080 SanDiego-144144.1 Page 2081 SanDiego-144144.1 Page 2082 SanDiego-144144.1 Page 2083 SanDiego-144144.1 Page 2084 SanDiego-144144.1 Page 2085 SanDiego-144144.1 Page 2086 SanDiego-144144.1 Page 2087 SanDiego-144144.1 Page 2088 Table 30. Current Candidate Therapeutic Interventions for the Treatment of Huntington's Disease San Diego-144144.1 Page 2089 SanDiego-144144.1 Page 2090 SanDiego-144144.1 Page 2091 SanDiego-144144.1 Page 2092 SanDiego-144144.1 Page 2093 SanDiego-144144.1 Page 2094 SanDiego-144144.1 Page 2095 SanDiego-144144.1 Page 2096 SanDiego-144144.1 Page 2097 Table 32. Cunent Candidate Therapeutic Interventions for the Treatment of Multiple Sclerosis San Diego-144144.1 Page 2098 SanDiego-144144.1 Page 2099 SanDiego-144144.1 Page 2100 SanDiego-144144.1 Page 2101 SanDiego-144144.1 Page 2102 SanDiego-144144.1 Page 2103 SanDiego-144144.1 Page 2104 SanDiego-144144.1 Page 2105 SanDiego-144144.1 Page 2106 SanDiego-144144.1 Page 2107 SanDiego-144144.1 Page 2108 SanDiego-144144.1 Page 2109 SanDiego-144144.1 Page 2110 SanDiego-144144.1 Page 2111 SanDiego-144144.1 Page 2112 SanDiego-144144.1 Page 2113 SanDiego-144144.1 Page 2114 SanDiego-144144.1 Page 2115 SanDiego-144144.1 Page 2116 SanDiego-144144.1 Page 2117 SanDiego-144144.1 Page 2118 SanDiego-144144.1 Page 2119 SanDiego-144144.1 Page 2120 SanDiego-144144.1 Page 2121 SanDiego-144144.1 Page 2122 SanDiego-144144.1 Page 2123 SanDiego-144144.1 Page 2124 SanDiego-144144.1 Page 2125 SanDiego-144144.1 Page 2126 SanDiego-144144.1 Page 2127 SanDiego-144144.1 Page 2128 SanDiego-144144.1 Page 2129 SanDiego-144144.1 Page 2130 SanDiego-144144.1 Page 2131 Table 34: Current Candidate Therapeutic Interventions for the Treatment of Parkinson's Disease San Diego-144144.1 Page 2132 SanDiego-144144.1 Page 2133 SanDiego-144144.1 Page 2134 SanDiego-144144.1 Page 2135 SanDiego-144144.1 Page 2136 SanDiego-144144.1 Page 2137 SanDiego-144144.1 Page 2138 SanDiego-144144.1 Page 2139 SanDiego-144144.1 Page 2140 SanDiego-144144.1 Page 2141 Table 35. Current Candidate Therapeutic Interventions for the Treatment of Schizophrenia (and Other Psychoses) San Diego-144144.1 Page 2142 SanDiego-144144.1 Page 2143 SanDiego-144144.1 Page 2144 SanDiego-144144.1 Page 2145 SanDiego-144144.1 Page 2146 SanDiego-144144.1 Page 2147 SanDiego-144144.1 Page 2148 SanDiego-144144.1 Page 2149 SanDiego-144144.1 Page 2150 SanDiego-144144.1 Page 2151 SanDiego-144144.1 Page 2152 SanDiego-144144.1 Page 2153 SanDiego-144144.1 Page 2154 SanDiego-144144.1 Page 2155 SanDiego-144144.1 Page 2156 SanDiego-144144.1 Page 2157 SanDiego-144144.1 Page 2158 SanDiego-144144.1 Page 2159 SanDiego-144144.1 Page 2160 SanDiego-144144.1 Page 2161 San Diego- 144144.1 Page 2162 SanDiego-144144.1 Page 2163 SanDiego-144144.1 Page 2164 SanDiego-144144.1 Page 2165 SanDiego-144144.1 Page 2166 SanDiego-144144.1 Page 2167 Sa Diego-144144.1 Page 2168 SanDiego-144144.1 Page 2169 SanDiego-144144.1 Page 2170 SanDiego-144144.1 Page 2171 SanDiego-144144.1 Page 2172 SanDiego-144144.1 Page 2173 SanDiego-144144.1 Page 2174 Table 38. Cunent Candidate Therapeutic Interventions for the Treatment of Arthritis. SD-144133.1 Page 2175 SD-144133.1 Page 2176 SD-144133.1 Page 2177 SD-144133.1 Page 2178 SD-144133. Page 2179 SD-144133.1 Page 2180 SD-144133.1 Page 2181 SD-144133.1 Page 2182 SD-144133.1 Page 2183 SD-144133.1 Page 2184 SD-144133.1 Page 2185 SD-144133.1 Page 2186 SD-144133.1 Page 2187 SD-144133.1 Page 2 IS SD-144133.1 Page 2189 SD-144133.1 Pat>e2190 SD-144133.1 Page 2191 SD-144133.1 Page 2192 SD-144133.1 Page 2193 SD-144133.1 Page 2194 SD-144133.1 Page 2195 SD-144133. Page 2196 SD-144133.1 Page 2197 SD-144133.1 Page 2198 SD-144133.1 Page 2199 SD-144133.1 Page 2200 SD-144133.1 Page 2201 SD-144133.1 Pase 2202 SD-144133.1 Page 2203 Table 39. Cunent Candidate Therapeutic Interventions for the Treatment of COPD SD-144133.1 Page 2204 SD-144133.1 Page 2205 SD-144133.1 Page 2206 SD-144133.1 Page 2207 SD-144133.1 Page 2208 SD-144133.1 Page 2209 SD-144133.1 Page 2210 SD-144133.1 Page 2211 SD-144133.1 Page 2212 SD-144133.1 Page 2213 SD-144133.1 Page 2214 SD-144133.1 Page 2215 SD-144133.1 Page 2216 SD-144133.1 Page 2217 SD-144133.1 Page 2218 SD-144133.1 Page 2219 SD-144133.1 Page 2220 SD-144133.1 Page 2221 SD-144133.1 Paee 2222 SD-144133 1 Page 2223 SD-144133. Page 2224 SD-144133.1 Page 2225 SD-144133.1 Page 2226 SD-144133.1 Page 2227 SD-144133.1 Page 2228 SD-144133.1 Page 2229 SD-144133.1 Page 2230 SD-144133.1 Page 2231 SD-144133.1 Page 2232 SD-144133.1 Page 2233 SD-144133 1 Page 2234 SD-144133 1 Page 2235 SD-144133.1 Page 2236 SD-144133.1 Page 2237 SD-144133.1 Page 2238 SD-144133.1 Page 2239 SD-144133.1 Page 2240 SD-144133.1 Page 2241 SD-144133.1 Page 2242 SD-144133. Page 2243 SD-144133.1 Page 2244 SD-144133.1 Page 2245 SD-144133.1 Page 2246 SD-144133.1 Page 2247 SD-144133.1 Page 2248 SD-144133.1 Page 2249 SD-144133-1 Page 2250 SD-144133.1 Page 2251 SD-144133.1 Page 2252 SD-144133.1 Page 2253 SD-144133.1 Page 2254 SD-144133. Page 2255 SD-144133.1 Page 2256 SD-144133.1 Page 2257 SD-144133.1 Page 2258 SD-144133.1 Page 2259 SD-144133.1 Page 2260 SD-144133.1 Page 2261 PX 3, 7-dihydro-l -methyl- xanthine; asthma 3-(l -methylethyl)- 1H- bronchodilator purine-2,6-dione Table 40. Current Candidate Therapeutic Interventions for the Treatment of Autoimmune Disorders SD-144133.1 Page 2262 SD-144133.1 Page 2263 SD-144133.1 Paee 2264 SD-144133.1 Page 2265 SD-144133.1 Page 2266 SD-144133.1 Page 2267 SD-144133.1 Page 2268 SD-144133.1 Page 2269 SD-144133.1 Page 2270 SD-144133.1 Page 2271 SD-144133.1 Page 2272 SD-144133.1 Page 2273 Table 41. Current Candidate Therapeutic Interventions for the Treatment of Systemic Lupus Erythematosus SD-144133.1 Page 2274 SD-144133.1 Page 2275 SD-144133.1 Page 2276 SD-144133.1 Page 2277 SD-144133.1 Page 2278 SD-144133.1 Page 2279 Table 42. Cunent Candidate Therapeutic Interventions for the Treatment of Immunnosuppression [Product Name Chemical Name [Action Indication SD-144133.1 Page 2280 SD-144133.1 Page 2281 SD-144133.1 Page 2282 SD-144133. Page 2283 SD-144133.1 Page 2284 SD-144133.1 Page 2285 SD-144133.1 Page 2286 SD-144133.1 Page 2287 SD-144133.1 Page 2288 SD-144133.1 Page 2289 SD-144133.1 Page 2290 SD-144133. Page 2291 SD-144133.1 Page 2292 SD-144133.1 Page 2293 SD-144133.1 Page 2294 SD-144133.1 Page 2295 SD-144133.1 Page 2296 SD-144133.1 Page 2297 SD-144133.1 Page 2298 SD-144133.1 Page 2299 SD-144133.1 Page 2300 SD-144133.1 Page 2301 SD-144133.1 Page 2302 SD-144133.1 Page 2303 SD-144133.1 Page 2304 SD-144133.1 Page 2305 SD-144133.1 Page 2306 SD-144133.1 Page 2307 SD-144133.1 Page 2308 SD-144133.1 Page 2309 SD-144133.1 Page 2310 SD-144133.1 Page 231 SD-144133.1 Page 2312 SD-144133.1 Page 2313 SD-144133.1 Page 2314 SD-144133.1 Page 2315 SD-144133.1 Page 2316 SD-144133.1 Page 2317 SD-144133.1 Page 231- SD-144133.1 Page 2319 SD-144133.1 Page 2320 SD-144133.1 Page 2321 SD-144133.1 Page 2322 SD-144133.1 Page 2323 SD-144133.1 Page 2324 SD-144133.1 Page 2325 SD-144133 1 Page 2326 SD-144133.1 Page 2327 SD-144133.1 Page 2328 SD-144133.1 Page 2329 Table 44. Current Candidate Therapeutic Interventions for the Treatment of Pain Related to Inflammation SD-144133.1 Page 2330 SD-144133.1 Page 2331 SD-144133. Page 2332 SD-144133.1 Page 2333 SD-144133.1 Page 2334 SD-144133.1 Page 2335 SD-144133.1 Page 2336 SD-144133. Page 2337 SD-144133.1 Page 2338 SD-144133. Page 2339 SD-144133.1 Page 2340 SD-144133. Page 2341 SD-144133. Page 2342 SD-144133.1 Page 2343 SD-144133.1 Page 2344 SD-144133.1 Page 2345 SD-144133.1 Page 2346 SD-144133.1 Page 2347 SD-144133.1 Page 2348 SD-144133.1 Page 2349 SD-144133.1 Page 2350 SD-144133.1 Page 2351 SD-144133.1 Page 2352 SD-144133.1 Page 2353 SD-144133.1 Page 2354 SD-144133.1 Page 2355 SD-144133.1 Page 2356 SD-144133.1 Page 2357 SD-144133.1 Page 2358 SD-144133.1 Page 2359 SD-144133.1 Page 2360 SD-144133.1 Page 2361 SD-144133.1 Page 2362 SD-144133.1 Page 2363 SD-144133.1 Page 2364 SD-144133.1 Page 2365 SD-144133.1 Page 2366 SD-144133.1 Page 2367 SD-144133.1 Page 2368 SD-144133.1 Page 2369 SD-144133. Page 2370 SD-144133.1 Page 2371 SD-144133.1 Page 2372 SD-144133.1 Page 2373 SD-144133.1 Page 2374 SD-144133.1 Page 2375 SD-144133.1 Page 2376 SD-144133.1 Page 2377 SD-144133.1 Page 2378 SD-144133.1 Page 2379 SD-144133.1 Page 2380 SD-144133.1 Page 2381 SD-144133.1 Page 2382 Table 45. Current Candidate Therapeutic Interventions for the Treatment of Psoriasis SD-144133.1 Page 2383 SD-144133.1 Page 2384 SD-144133.1 Page 2385 SD-144133.1 Page 2386 SD-144133.1 Page 2387 SD-144133.1 Page 2388 SD-144133.1 Page 2389 SD-144133.1 Page 2390 SD-144133.1 Page 2391 SD-144133.1 Page 2392 SD-144133.1 Page 2393 SD-144133.1 Page 2394 SD-144133.1 Page 2395 SD-144133.1 Page 2396 SD-144133.1 Page 2397 SD-144133.1 Page 2398 SD-144133.1 Page 2399 SD-144133.1 Page 2400 SD-144133.1 Page 2401 Table 46. Cunent Candidate Thera eutic Interventions for the Treatment of Athersclerosis SD-144133.1 Page 2402 SD-144133.1 Page 2403 SD-144133.1 Page 2404 SD-144133.1 Page 2405 SD-144133.1 Page 2406 SD-144133.1 Page 2407 SD-144133.1 Page 2408 SD-144133.1 Page 2409 SD-144133.1 Page 2410 SD-144133.1 Page 2411 SD-144133.1 Page 2412 SD-144133.1 Page 2413 SD-144133.1 Page 2414 SD-144133.1 Page 2415 SD-144133.1 Page 2416 SD-144133.1 Page 2417 SD-144133.1 Page 2418 SD-144133.1 Page 2419 SD-144133.1 Page 2420 SD-144133.1 Page 2421 Table 47. Cunent Candidate Therapeutic Interventions for the Treatment of Asthma SD-144133.1 Page 2422 SD-144133.1 Page 2423 SD-144133.1 Page 2424 SD-144133.1 Page 2425 SD-144133.1 Page 2426 SD-144133.1 Page 2427 SD-144133.1 Page 2428 SD-144133.1 Page 2429 SD-144133.1 Page 2430 SD-144133.1 Page 2431 SD-144133.1 Page 2432 SD-144133.1 Page 2433 SD-144133.1 Page 2434 SD-144133.1 Page 2435 SD-144133.1 Page 2436 SD-144133.1 Page 2437 SD-144133.1 Page 2438 SD-144133.1 Page 2439 SD-144133.1 Page 2440 SD-144133.1 Page 2441 SD-144133.1 Paεe 2442 SD-144133.1 Page 2443 SD-144133.1 Page 2444 SD-144133.1 Page 2445 SD-144133.1 Page 2446 SD-144133.1 Page 2447 SD-144133.1 Page 2448 SD-144133.1 Page 2449 SD-144133.1 Page 2450 SD-144133.1 Page 2451 SD-144133.1 Page 2452 SD-144133.1 Page 2453 SD-144133.1 Page 2454 SD-144133.1 Page 2455 SD-144133.1 Page 2456 SD-144133.1 Page 2457 SD-144133.1 Page 2458 SD-144133.1 Page 2459 SD-144133.1 Page 2460 SD-144133.1 Page 2461 SD-144133.1 Page 2462 SD-144133.1 Page 2463 SD-144133.1 Page 2464 SD-144133.1 Page 2465 SD-144133.1 Page 2466 SD-144133.1 Page 2467 SD-144133.1 Page 2468 SD-144133.1 Page 2469 SD-144133.1 Page 2470 SD-144133.1 Page 2471 SD-144133.1 Page 2472 SD-144133.1 Page 2473 SD-144133.1 Page 2474 Table 48. Cunent Candidate Therapeutic Interventions for the Treatment of Inflammatory Bowel Disease SD-144133.1 Page 2475 SD-144133.1 Page 2476 SD-144133.1 Page 2477 SD-144133.1 Page 2478 SD-144133.1 Page 2479 SD-144133.1 Page 2480 SD-144133.1 Page 2481 Table 49. Current Candidate Thera eutic Interventions for the Treatment of Hepatitis SD-144133.1 Page 2482 SD-144133.1 Page 2483 San Diego- 144117.1 Page 2485 San Diego-144117.1 Page 2486 San Diego-144117.1 Page 2487 San Dιego-144117.1 Page 2488 San Diego- 144117.1 Page 2489 San Diego-144117.1 Page 2490 San Diego-144117.1 Page 2491 San Diego-144117.1 Page 2492 San Diego- 144117.1 Page 2493 San Diego-144117.1 Page 2494 San Diego-144117.1 Page 2495 San Diego- 144117.1 Page 2496 San Diego-144117.1 Page 2497 San Diego-144117.1 Page 2498 San Diego-144117.1 Page 2499 San Diego- 144117.1 Page 2500 San Diego- 144117.1 Page 2501 San Diego-144117.1 Page 2502 San Diego- 144117.1 Page 2503 San Diego-144117.1 Page 2504 San Diego- 144117.1 Page 2505 San Diego- 144117.1 Page 2506 San Diego-144117.1 Page 2507 San Diego-144117.1 Page 2508 Table 51. Current Candidate Therapeutic Interventions for the Treatment of Obesity product Name Chemical Name L -ction ttndication obesity therapy Unspecified 5HT agonist; 5HT2C obesity agonist San Diego-144117.1 Page 2509 San Diego-144117.1 Page 2510 San Diego-144117.1 Page 2511 San Diego- 144117.1 Page 2512 San Diego- 144117.1 Page 2513 San Diego-144117.1 Page 2514 San Diego- 144117.1 Page 2515 San Diego-144117.1 Page 2516 San Diego-144117.1 Page 2517 Table 52. Current Candidate Thera eutic Interventions for the Treatment of Contrace tion SanDiego-144117.1 Page 2518 San Diego-144117.1 Page 2519 San Diego-144117.1 Page 2520 San Diego- 144117.1 Page 2521 San Diego- 144117.1 Page 2522 San Diego-144117.1 Page 2523 SanDiego-144117.1 Page 2524 San Diego- 144117.1 Page 2525 San Diego-144117.1 Page 2526 San Diego-144117.1 Page 2527 San Diego-144117.1 Page 2528 San Diego-144117.1 Page 2529 San Diego-144117.1 Page 2530 San Diego-144117.1 Page 2531 San Diego-144117.1 Page 2532 San Diego-144117.1 Page 2533 SanDiego-144117.1 Page 2534 San Diego-144117.1 Page 2535 San Diego-144117.1 Page 2536 San Diego-144117.1 Page 2537 San Diego-144117.1 Page 2538 San Diego-144117.1 Page 2539 secalciferol; 24,25 (3beta,5Z,7E,24R)- Kάtamin D3 analogue osteodystrophy; dihydroxycholecalcif|9 ,10-secocholesta- osteoporosis erol; KDR; Ro 5,7,10(19)-triene- 215816; OSTEO D 3,24,25-triol San Diego-144117.1 Page 2540 San Diego-144117.1 Page 2541 San Diego-144117.1 Page 2542 San Diego-144117.1 Page 2543 San Diego-144117.1 Page 2544 San Diego-144117.1 Page 2545 Table 56. Current Candidate Therapeutic Interventions for the Treatment of Metabolic San Diego-144117.1 Page 2546 San Diego-144117.1 Page 2547 San Diego-144117.1 Page 2548 San Diego-144117.1 Page 2549 San Diego-144117.1 Page 2550 San Diego-144117.1 Page 2551 San Diego-144117.1 Page 2552 San Diego-144117.1 Page 2553 San Diego-144117.1 Page 2554 San Diego-144117.1 Page 2555 San Diego-144117.1 Page 2556 SanDiego-144117.1 Page 2557 San Diego-144117.1 Page 2558 San Diego-144117.1 Page 2559 San Diego-144117.1 Page 2560 San Diego-144117.1 Page 2561 San Diego-144117.1 Page 2562 San Diego-144117.1 Page 2563 San Diego-144117.1 Page 2564 San Diego-144117.1 Page 2565 San Diego-144117.1 Page 2566 San Diego-144117.1 Page 2567 San Diego-144117.1 Page 2568 San Diego-144117.1 Page 2569 San Diego-144117.1 Page 2570 San Diego-144117.1 Page 2571 San Diego-144117.1 Page 2572 San Diego-144117.1 Page 2573 San Diego-144117.1 Page 2574 San Diego-144117.1 Page 2575 San Diego-144117.1 Page 2576 San Diego-144117.1 Page 2577 San Diego-144117.1 Page 2578 San Diego-144117.1 Page 2579 San Diego-144117.1 Page 2580 San Diego-144117.1 Page 2581 San Diego- 144117.1 Page 2582 San Diego-144117.1 Page 2583 San Diego-144117.1 Page 2584 San Diego-144117.1 Page 2585 San Diego-144117.1 Page 2586 San Diego-144117.1 Page 2587 San Diego-144117.1 Page 2588 San Diego-144117.1 Page 2589 San Diego-144117.1 Page 2590 San Diego-144117.1 Page 2591 San Diego-144117.1 Page 2592 San Diego-144117.1 Page 2593 San Diego-144117.1 Page 2594 San Diego-144117.1 Page 2595 San Diego-144117.1 Page 2596 San Diego-144117.1 Page 2597 San Diego-144117.1 Page 2598 San Diego-144117.1 Page 2599 San Diego-144117.1 Page 2600 San Diego-144117.1 Page 2601 San Diego-144117.1 Page 2602 San Diego-144117.1 Page 2603 San Diego-144117.1 Page 2604 San Diego-144117.1 Page 2605 San Diego-144117.1 Page 2606 San Diego-144117.1 Page 2607 San Diego-144117.1 Page 2608 San Diego-144117.1 Page 2609 San Diego-144117.1 Page 2610 San Diego-144117.1 Page 2611 San Diego-144117.1 Page 2612 San Diego-144117.1 Page 2613 San Diego-144117.1 Page 2614 San Diego-144117.1 Page 2615 San Diego-144117.1 Page 2616 San Diego-144117.1 Page 2617 San Diego-144117.1 Page 2618 San Diego-144117.1 Page 2619 San Diego-144117.1 Page 2620 San Diego-144117.1 Page 2621 San Diego-144117.1 Page 2622 Table 57. Current Candidate Thera eutic Interventions for the Treatment of Anemia SD- I441 15 1 Page 2623 SD-1441 15.1 Page 2624 SD-1 4 115.1 Page 2625 SD-144115.1 Page 2626 Table 58. Current Candidate Thera eutic Interventions for the Treatment of -An ina SD-14 11 5 .1 Page 2627 SD-14 4 U5.1 Page 2628 SD-1 44 115.1 Page 2629 SD-I441 15 Page 2630 SD-1441 15 1 Page 2631 SD-1 4 11 5 .1 Page 2633 SD-1 115- Page 2634 SD-1 4 11 5 .1 Page 2635 SD-1441 15 1 Page 2636 SD-1441 15 Page 2637 SD-1441 15 I Page 2638 SD-I441 15 Page 2639 SD-144115.1 Page 2640 SD-l 44115.1 Page 2641 SD-144115.1 Page 2642 SD-144115.1 Page 2643 SD-144115.1 Page 2644 SD-1441151 Page 2645 Table 59. Current Candidate Therapeutic Interventions for the Treatment of Arrh thmia SD-1441 15 ' Page 2646 SD-144115.1 Page 2647 SD-1 4 115.1 Page 2648 SD-144115.1 Page 2649 SD-144115.1 Page 2650 SD-1441 15 I Page 2651 SD-1441151 Page 2652 SD-1441151 Page 2653 SD-1441151 Page 2654 SD-144U51 Page 2655 SD-144115.1 Page 2656 SD-1441151 Page 2657 SD-144115.1 Page 2658 SD-H4115.1 Page 2659 SD-1 44 115.1 Page 2660 SD-1 4 4115-1 Page 2661 SD-1441151 Page 2662 Table 60. Current Candidate Therapeutic Interventions for the Treatment of Hy ertension SD-1441 15 1 Page 2663 SD-1441 15 1 Page 2664 SD-1441I51 Page 2665 SD-1441151 Page 2666 SD-144115.1 Page 2667 SD-144115.1 Page 2668 SD- 4115.1 Page 2669 SD-1441151 Page 2670 SD-144115.1 Page 2671 SD-1441151 Page 2672 SD-1441151 Page 2673 SD-144115 I Page 2674 SD-144115.1 Page 2675 SD-1441151 Page 2676 SD-144115.1 Page 2677 SD-144115.1 Page 2678 SD-144115.1 Page 2679 SD-144115. Page 2680 SD-1441151 Page 2681 SD-1 4 1151 Page 2682 SD-1441 15 1 Page 2683 SD-1441 15 Page 2684 SD-144115 Page 2685 SD-1441151 Page 2686 SD-1441 15 Page 2687 SD-1441151 Page 2688 SD-144115.1 Page 2689 SD-H4U5 1 Page 2690 SD-144115.1 Page 2691 SD-144115.1 Page 2692 SD-1 44 115.1 Page 2693 SD-1441151 Page 2694 SD-1441151 Page 2695 SD-144115.1 Page 2696 SD-14 4 115.1 Page 2697 SD-144115.1 Page 2698 SD-14 4 115 Page 2699 SD-1441151 Page 2700 SD-1441151 Page 2701 SD-1441151 Page 2702 SD-144115 Page 2703 SD-1441151 Page 2704 SD-1441 15 1 Page 2705 SD-144115.1 Page 2706 SD-144115 Page 2707 SD-144115 Page 2708 SD-1441151 Page 2709 SD-144115.1 Page 2710 SD-144U51 Page 2711 SD-1441151 Page 2712 SD-14 115.1 Page 2713 SD-14 4 1151 Page 2714 SD-144115.1 Page 2715 SD-I44115.1 Page 2716 SD-144115.1 Page 2717 SD-144115.1 Page 2718 SD-144115.1 Page 2719 SD-1441151 Page 2720 SD-1 4 4115.1 Page 2721 SD-14 1151 Page 2722 SD-144115 1 Page 2723 SD-I441 15 1 Page 2724 SD-1 4 U51 Page 2725 SD-1441 15.1 Page 2726 SD-1 1151 Page 2727 SD-1441 15.1 Page 2728 SD-1441 15 1 Page 2729 SD-1441 15 1 Page 2730 SD-1 4 1151 Page 2731 SD-M41I5.1 Page 2732 SD-M41151 Page 2733 SD-144115.1 Page 2734 Table 61. Current Candidate Therapeutic Interventions for the Treatment of Hypotension SD-14 1 15 1 Page 2735 SD-14 115.1 Page 2736 SD-1 115.1 Page 2737 Table 62. Current Candidate Therapeutic Interventions for the Treatment of Myocardial Ischemia SD-14 4 1 15.1 Page 2738 SD-144115.1 Page 2739 SD-1 44 115.1 Page 2740 SD-1441151 Page 2741 SD-1441 15 1 Page 2742 SD-1Ψ4115-1 Page 2743 SD-1 4 115.1 Page 2744 SD-1441 15.1 Page 2745 SD-144115.1 Page 2746 SD-1441151 Page 2747 SD-1441151 Page 2748 SD-1441151 Page 2749 Table 63. Current Candidate Therapeutic Interventions for the Treatment of Heart Failure SD-1 4 1 15 1 Page 2750 SD-1441 15 1 Page 2751 SD-1441 15 1 Page 2752 SD-I441 15 1 Page 2753 SD-1441 15.1 Page 2754 SD-1441 15 1 Page 2755 SD-I 4I 15- Page 2756 SD-1441151 Page 2757 SD-1441 15 1 Page 2758 SD-1441151 Page 2759 SD-1441 15 Page 2760 SD-1441 15 1 Page 2761 SD-1441 15 1 Page 2762 SD- 41151 Page 2763 SD-144115 Page 2764 SD-1441 15 Page 2765 SD- 41151 Page 2766 SD-1441 15 1 Page 2767 SD-1441151 Page 2768 SD-1441151 Page 2769 SD-144115 Page 2770 SD-144115.1 Page 2771 SD-14 115.1 Page 2772 SD-1441151 Page 2773 Table 64. Current Candidate Thera eutic Interventions for the Treatment of Thrombosis SD-1441 15 1 Page 2774 SD-144115.1 Page 2775 SD-144115 Page 2776 SD-14 115.1 Page 2777 SD-144115.1 Page 2778 SD-144115.1 Page 2779 SD-1441151 Page 2780 SD-1441151 Page 2781 SD-144115.1 Page 2782 SD-1441151 Page 2783 SD-144115.1 Page 2784 SD-1441 15 1 Page 2785 SD-1441151 Page 2786 SD-1441 15.1 Page 2787 SD-1441151 Page 2788 SD-144115 1 Page 2789 SD-1441151 Page 2790 SD-144115.1 Page 2791 SD-144115.1 Page 2792 SD-144115. Page 2793 SD-1441I51 Page 2794 SD-1441151 Page 2795 SD-1441151 Page 2796 SD-144115.1 Page 2797 SD-144115.1 Page 2798 SD-144115.1 Page 2799 SD-1 4 115.1 Page 2800 SD-144115.1 Page 2801 SD-144115.1 Page 2802 SD-144115.1 Page 2803 SD-144115.1 Page 2804 SD-144115.1 Page 2805 SD-14 4 115.1 Page 2806 SD-144115.1 Page 2807 SD-144115.1 Page 2808 SD-144115-l Page 2809 SD-14 4 115 Page 2810 SD-1Φ41151 Page 2811 SD-1441151 Page 2812 SD-144115 Page 2813 SD-1441151 Page 2814 SD-144115 I Page 2815 SD-1441151 Page 2816 SD-1441 15 1 Page 2817 SD-1441151 Page 2818 SD-1441151 Page 2819 SD-1441151 Page 2820 SD-1441151 Page 2821 SD-1441151 Page 2822 SD-1441151 Page 2823 SD-144115.1 Page 2824 SD-144115.1 Page 2825 SD-144115.1 Page 2826 SD-1441151 Page 2827 SD-144115 I Page 2828 SD-1441 15 1 Page 2829 Table 65. Current Candidate Therapeutic Interventions for the Treatment of Renal Disease, Disorder, or Dysfunction SD-1441 I 5 1 Page 2830 SD-144115 Page 2831 SD-1441151 Page 2832 SD-1441151 Page 2833 SD-144115.1 Page 2834 SD-144115.1 Page 2835 SD-1441151 Page 2836 Table 66. Current Candidate Therapeutic Interventions for the Treatment of Nephritis SD-1441 15.1 Page 2837 SD-144115 Page 2838 SD-1441151 Page 2839 Table 67. Current Candidate Therapeutic Interventions for the Treatment of Restenosis SD-1441 15 Page 2840 SD-1441151 Page 2841 SD-144115 Page 2842 SD-1441151 Page 2843 SD-144115.1 Page 2844 SD-1441151 Page 2845 SD-1441151 Page 2846 SD-1441151 Page 2847 SD-144115.1 Page 2848 Table 68. Current Candidate Therapeutic Interventions for the Treatment of Peripheral Vascular Disease SD-1441 15.1 Page 2849 SD-144115.1 Page 2850 SD-1441151 Page 2851 SD-1441151 Page 2852 SD-1441151 Page 2853 SD-144115.1 Page 2854 SD-144115.1 Page 2855 SD-144115.1 Page 2856 SD-144115.1 Page 2857

Claims: 2858 Claims What is claimed is: 1. A method for selecting a treatment for a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease, disorder, or condition, comprising determining whether cells of said patient contain at least one variance in a gene from a Table herein, wherein the presence or the absence of said at least one variance in said gene is indicative of the effectiveness of said treatment for said disease, disorder, or condition. 2. The method of claim 1, wherein disease, disorder, or condition is listed in an example or Table herein. 3. The method of claim 1, wherein the presence of said at least one variance is indicative that said treatment will be effective for said patient. 4. The method of claim 1 , wherein the presence of said variance is indicative that said treatment will be ineffective or contra-indicated for said patient. 5. The method of claim 1, wherein said at least one variance comprises a plurality of variances. 6. The method of claim 5, wherein said plurality of variances comprise a haplotype or haplotypes. 7. The method of claim 1, wherein said selecting a treatment further comprises identifying a compound differentially active in a patient bearing a form of said gene containing said at least one variance. 8. The method of claim 7, wherein said compound is a compound listed in a Table herein or that belongs to the same chemical class as a compound listed in a said Table. 9. The method of claim 1, wherein said selecting a treatment further comprises excluding or eliminating a treatment, wherein said presence or absence of said at least one variance is indicative that said treatment will be ineffective or contra-indicated. 2859 10. The method of claim 1, wherein said treatment comprises a first treatment and a second treatment, said method comprising the steps of: identifying a said first treatment effective to treat said disease, disorder, or condition; and identifying a said second treatment which reduces a deleterious effect or promotes efficacy of said first treatment. 11. The method of claim 1 , wherein said selecting a treatment further comprises selecting a method of administration of a compound effective to treat said disease in a patient, disorder or condition, wherein said presence or absence of said at least one variance is indicative of the appropriate method of administration for said compound. 12. The method of claim 11 , wherein said selecting the method of administration comprises selecting a suitable dosage level or frequency of administration of a compound. 13. The method of claim 1, further comprising determining the level of expression of said gene or the level of activity of a protein containing a polypeptide expressed from said gene, wherein the combination of the determination of the presence or absence of said at least one variance and the determination of the level of activity or the level of expression provides a further indication of the effectiveness of said treatment. 14. The method of claim 1, further comprising determining the at least one of sex, age, racial origin, ethnic origin, and geopraphic origin of said patient, wherein the combination of the determination of the presence or absence of said at least one variance and the determination of the sex, age, racial origin, ethnic origin, and geopraphic origin of said patient provides a further indication of the effectiveness of said treatment. 15. The method of claim 1, wherein said disease, disorder, or condition is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central 2860 nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, arrhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 16. The method of claim 1, wherein the detection of the presence or absence of said at least one variance comprises amplifying a segment of nucleic acid including at least one of said variances. 17. The method of claim 16, wherein said segment of nucleic acid is 500 nucleotides or less in length. 18. The method of claim 16, wherein said segment of nucleic acid is 100 nucleotides or less in length. 19. The method of claim 16, wherein said segment of nucleic acid is 45 nucleotides or less in length. 20. The method of claim 16, wherein said segment includes a plurality of variances. 21. The method of claim 17, wherein amplification preferentially occurs from one of the two strands of a chromosome. 22. The method of claim 17, wherein said segment of nucleic acid is at least 500 nucleotides in length. 23. The method of claim 1, wherein the detection of the presence or absence of said at least one variance comprises contacting nucleic acid comprising a variance site with at least one nucleic acid probe, wherein said at least one probe preferentially hybridizes with a nucleic acid sequence including said variance site and containing a complementary base at said variance site under selective hybridization conditions. 2861 24. The method of claim 1, wherein the detection of the presence or absence of said at least one variance comprises sequencing at least one nucleic acid sequence. 25. The method of claim 1, wherein the detection of the presence or absence of said at least one variance comprises mass spectrometric determination of at least one nucleic acid sequence. 26. The method of claim 1, wherein the detection of the presence or absence of said at least one variance comprises determining the haplotype of a plurality of variances in a gene. 27. A method for selecting a method of treatment, comprising comparing at least one variance in at least one gene from Tables 1-6, 12-17, and 18-23 in a patient suffering from a neurological or psychiatric disease, dmg- induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition with a list of variances or haplotypes in said at least one gene indicative of the effectiveness of at least one method of treatment. 28. The method of claim 27, wherein said list comprises at least 5 variances. 29. The method of claim 27, wherein said at least one variance comprises a plurality of variances. 30. The method of claim 27, wherein said list of variances comprises a plurality of variances. 31. The method of claim 27, wherein at least one said method of treatment comprises the administration of a compound effective against said disease or condition to a patient. 32. The method of claim 31 , wherein said compound is selected from the group consisting of agonists, antagonists, blockers, partial agonists, partial antagonists, inhibitors, activators, modulators, negative antagonists, inverse agonists, mimetics, or factors that elicit pharmacological activity on a gene product of at least one gene or gene pathway listed in Table 1. 2862 33. The method of claim 27, wherein the presence or absence of at least one variance or haplotype in said gene is indicative that said treatment will be effective in said patient. 34. The method of claim 27, wherein the presence or absence of at least one variance in said gene is indicative that said treatment will be ineffective or contraindicated. 35. The method of claim 27, wherein said treatment is a first treatment and the presence or absence of at least one variance in said gene is indicative that a second treatment will be beneficial to reduce a deleterious effect or promotes efficacy of said first treatment. 36. The method of claim 27, wherein said at least one method of treatment is a plurality of methods of treatment. 37. The method of claim 36, wherein said selecting comprises determining whether any of said plurality of methods of treatment will be more effective than at least one other of said plurality of methods of treatment. 38. The method of claim 27, wherein said disease is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, arrhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 39. A method for selecting a method of administration to a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation 2863 or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition for a compound or compounds effective to treat said condition or disease, comprising determining whether at least one variance in a gene from Tables 1-6, 12-17, and 18-23 is present or absent in cells of said patient, wherein said presence or absence of said at least one variance is indicative of an appropriate method of administration for said compound. 40. The method of claim 39, wherein said neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition is a disease or condition listed in the Detailed Description, an Example, or a Table herein. 41. The method of claim 39, wherein said selecting a method of administration comprises selecting a dosage level or frequency or frequency of administration of said compound. 42. The method of claim 39, wherein said compound is selected from the group consisting of agonists, antagonists, blockers, partial agonists, partial antagonists, inhibitors, activators, modulators, negative antagonists, inverse agonists, mimetics, or factors that elicit pharmacological activity on a gene product of at least one gene or gene pathway listed in Table 1. 43. The method of claim 39, wherein said disease is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, drag-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, 2864 angina, anhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 44. A method for selecting a patient for administration of a treatment, comprising comparing the presence or absence of at least one variance or haplotype in a gene from Tables 1-6, 12-17, and 18-23 in cells of a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition with a list of variances or haplotypes in said at least one gene, wherein the presence or absence of said at least one variance or haplotype in said cells is indicative that said treatment will be effective, more effective, less effective, ineffective, or contra-indicated in said patient; and determining whether said patient will receive said treatment based on the presence or absence of said at least one variance in said cells. 45. The method of claim 44, wherein said list comprises at least 5 variances. 46. The method of claim 44, wherein said method of treatment comprises administration of a compound effective against said disease or condition. 47. The method of claim 46, wherein said compound is selected from the group consisting of agonists, antagonists, blockers, partial agonists, partial antagonists, inhibitors, activators, modulators, negative antagonists, inverse agonists, mimetics, or factors that elicit pharmacological activity on a gene product of at least one gene or gene pathway listed in Table 1. 48. A method for identifying the presence or absence of at least one form of a gene from Tables 1-6, 12-17, and 18-23 in cells of an individual, comprising: determining the presence or absence of at least one variance in said gene in said cells. 49. The method of claim 48, wherein said said at least one variance is a plurality of variances. 50. The method of claim 49, wherein said plurality of variances comprises a haplotype. 2865 51. The method of claim 50, wherein said individual suffers from a disease or condition. 52. The method of claim 50, wherein the presence or absence of said at least one variance is indicative of the effectiveness of a therapeutic treatment in a patient having cells containing said at least one variance. 53. The method of claim 50, wherein said determining comprises amplifying a segment of nucleic acid including a site of at least one variance. 54. The method of claim 50, wherein said determining comprises contacting a nucleic acid sequence containing a variance site conesponding to a said variance with a probe which specifically binds under selective binding conditions to a nucleic acid sequence comprising at least one said variance. 55. The method of claim 50, wherein the detection of the presence or absence of said at least one variance comprises sequencing at least one nucleic acid sequence. 56. The method of claim 50, wherein the detection of the presence or absence of said at least one variance comprises mass spectrometric determination of at least one nucleic acid sequence. 57. The method of claim 50, wherein the detection of the presence or absence of said at least one variance comprises determining the haplotype of a plurality of variances in a gene. 58. A pharmaceutical composition comprising a compound which has a differential effect in patients having at least one copy of a particular form of an identified gene from Tables 1-6, 12-17, and 18-23; and a pharmaceutically acceptable carrier or excipient or diluent, wherein said composition is preferentially effective to treat a patient with cells comprising a form of said gene comprising at least one variance. 59. The method of claim 58, wherein said composition is adapted to be preferentially effective based on the unit dosage, presence of additional active components, complexing of said compound with stabilizing components, or inclusion of components enhancing delivery or slowing excretion of said compound. 2866 60. The composition of claim 58, wherein said compound is deleterious to patients having said at least one copy or in patients not having said at least one copy, but not in both. 61. The composition of claim 58, wherein said patient suffers from a disease or condition selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, arrhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 62. The pharmaceutical composition of claim 58, wherein said composition is subject to a regulatory restriction or recommendation for use of a diagnostic test determining the presence or absence of at least one variance or haplotype in said gene. 63. The pharmaceutical composition of claim 58, wherein said pharmaceutical composition is subject to a regulatory limitation or recommendation restricting or recommending restriction of the use of said pharmaceutical composition to patients having at least one copy of a form of a gene comprising at least one variance. 64. The pharmaceutical composition of claim 58, wherein said pharmaceutical composition is subject to a regulatory limitation or recommendation indicating said pharmaceutical composition is not to be used in patients having at least one copy of a form of a gene comprising at least one variance. 65. The pharmaceutical composition of claim 58, wherein said pharmaceutical composition is packaged, and the packaging includes a label or insert restricting or 2867 recommending the restriction of the use of said pharmaceutical composition to patients having at least one copy of a form of a gene comprising at least one variance or haplotype. 66. The pharmaceutical composition of claim 58, wherein said pharmaceutical composition is packaged, and said packaging includes a label or insert requiring or recommending the use of a test to determine the presence or absence of at least one variance in cells of a said patient. 67. A nucleic acid probe comprising a nucleic acid sequence 7 to 200 nucleotide bases in length that specifically binds under selective binding conditions to a nucleic acid sequence comprising at least one variance in a gene from Tables 1-6, 12-17, and 18-23, or a sequence complementary thereto or an RNA equivalent. 68. The probe of claim 67, wherein said probe comprises a nucleic acid sequence 500 nucleotide bases or fewer in length. 69. The probe of claim 67, wherein said nucleic acid sequence is 100 or fewer nucleotide bases in length. 70. The probe of claim 67, wherein said nucleic acid sequence is 25 or fewer nucleotide bases in length. 71. The probe of claim 67, wherein said probe comprises DNA. 72. The probe of claim 67, wherein said probe comprises DNA and at least one nucleic acid analog. 73. The probe of claim 67, wherein said probe comprises peptide nucleic acid (PNA). 74. The probe of claim 67, further comprising a detectable label. 75. The probe of claim 74, wherein said detectable label is a fluorescent label. 76. A method for determining a genotype of an individual, comprising analyzing at least one nucleic acid sequence from cells of said individual using mass spectrometric analysis, 2868 wherein said nucleic acid sequence is a portion of a gene from Tables 1-6, 12-17, and 18-23 or a sequence complementary thereto. 77. The method of claim 76, wherein said analyzing a nucleic acid sequence comprises determining the presence or absence of a variance in said gene. 78. The method of claim 76, wherein said analyzing a nucleic acid sequence comprises determining the nucleotide sequence of said at least one nucleic acid sequence. 79. The method of claim 76, wherein said at least one nucleic acid sequence is 500 nucleotides or less in length. 80. The method of claim 76, wherein said at least one nucleic acid sequence comprises at least one variance site in said gene. 81. An isolated, purified or enriched nucleic acid sequence of 15 to 500 nucleotides in length, comprising at least one variance site, wherein said sequence has the base sequence of a portion of an allele of a gene from Tables 1-6, 12-17, and 18-23. 82. The nucleic acid sequence of claim 81, wherein said nucleic acid sequence is 15 to 100 nucleotide bases in length. 83. The nucleic acid sequence of claim 81, wherein said nucleic acid sequence sequence is 15 to 25 nucleotide bases in length. 84. A method for determining whether a compound has differential effects on cells containing at least one different form of a gene from Tables 1-6, 12-17, and 18- 23, comprising: contacting a first cell and a second cell with said compound, wherein said first cell and said second cell differ in the presence or absence of at least one variance in said gene; and determining whether the responses of said first cell and said second cell to said compound differ, wherein the difference in said response is due to the presence or absence of said at least one variance. 2869 85. The method of claim 84, wherein said at least one variance comprises a haplotype. 86. The method of claim 84, wherein at least one of said first cell and said second cell are contacted in vivo. 87. The method of claim 85, wherein at least one of said first cell and said second cell are contacted in vitro. 88. The method of claim 87, wherein at least one of said first cell and said second cell is contacted in vivo in a plurality of patients suffering from a disease or condition. 89. A method of treating a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition, comprising: a) determining whether cells of said patient contain a form of a gene from Tables 1-6, 12-17, and 18-23 which comprises at least one variance, wherein the presence or absence of said at least one variance is indicative that a treatment will be effective in said patient; and b) administering said treatment to said patient. 90. The method of claim 89, wherein said gene is listed in Table 1 or is a gene in a pathway listed in Table 1 herein. 91. The method of claim 89, wherein said disease or condition is a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition listed in the Detailed Description, Examples, or Tables herein. 92. The method of claim 89, wherein said disease is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system 2870 toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, anhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 93. The method of claim 89, wherein the presence of said at least one variance is indicative that said treatment will be effective in said patient. 94. The method of claim 93, wherein said treatment comprises the administration of a compound preferentially active for said condition or disease in a said patient having said at least one variance in said gene. 95. The method of claim 94, wherein said compound is selected from the group consisting of agonists, antagonists, blockers, partial agonists, partial antagonists, inhibitors, activators, modulators, negative antagonists, inverse agonists, mimetics, or factors that elicit pharmacological activity on a gene product of at least one gene or gene pathway listed in Table 1. 96. The method of claim 89, wherein the presence of said at least one variance in said gene is indicative of an appropriate dosage or frequency of administration of a compound in said treatment. 97. A method of treating a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition, comprising: a) comparing the presence or absence of at least one variance in a gene from Tables 1-6, 12-17, and 18-23 in cells of a patient suffering from said disease or condition with a list of variances in said gene indicative of the effectiveness of at least one method of treatment; b) selecting a method of treatment from said at least one method of treatment, wherein the presence or absence of at least one of said at least one 2871 variance is indicative that said method of treatment will be effective in said patient; and c) administering said method of treatment to said patient. 98. The method of claim 97, wherein said at least one gene comprises a gene listed in Table 1 or comprises a gene in a pathway listed in Table 1 herein. 99. The method of claim 97, wherein said condition or disease is a condition or disease listed in the Detailed Description, Examples, or Tables herein. 100. The method of claim 97, further comprising determining the presence or absence of said at least one variance in cells of said patient. 101. The method of claim 97, wherein said at least one variance comprises a plurality of variances. 102. The method of claim 97, wherein said list of variances comprises a plurality of variances. 103. The method of claim 102, wherein said plurality of variances comprises a haplotype or haplotypes. 104. The method of claim 97, wherein said method of treatment comprises the administration of a compound effective against said disease or condition. 105. The method of claim 97, wherein said treatment is a first treatment and the presence or absence of at least one variance in said gene is indicative that a second treatment will be beneficial to reduce a deleterious effect or promotes efficacy of said first treatment. 106. The method of claim 97, wherein said at least one method of treatment is a plurality of methods of treatment. 107. The method of claim 97, wherein said disease or condition is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of 2872 blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, anhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 108. A method of treating a patient suffering from a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition, comprising: a) comparing the presence or absence of at least one variance in a gene from Tables 1-6, 12-17, and 18-23 in cells of a patient suffering from said disease or condition with a list of variances in said gene indicative of the effectiveness of at least one method of treatment; b) eliminating a method of treatment from said at least one method of treatment, wherein the presence or absence of at least one of said at least one variance is indicative that said method of treatment will be ineffective or contraindicated in said patient; c) selecting an alternative method of treatment effective to treat said neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition; and e. administering said alternative method of treatment to said patient. 109. The method of claim 108, further comprising determining the presence or absence of said at least one variance in cells of said patient. 110. The method of claim 108, wherein said at least one gene comprises a gene in the acetylcholine pathway; the CNS lipid transport/membrane repair pathway; the prostaglandin, prostacylin and thromboxane pathway, or is a gene involved in Alzheimer's disease neurofibrillary plaque formation or in susceptibility to Alzheimer's disease. 2873 111. The method of claim 108, wherein said disease or condition is a disease or condition listed in the Detailed Description, Examples, or Tables herein. 112. A method for producing a pharmaceutical composition, comprising: a) identifying a compound which has differential activity against a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition in patients having at least one variance in a gene from Tables 1-6, 12-17, and 18-23; b) compounding said pharmaceutical composition by combining said compound and a pharmaceutically acceptable carrier or excipient or diluent in a manner adapted to be preferentially effective in patients having said at least one variance. 113. A method for producing a pharmaceutical agent, comprising: a) identifying a compound which has differential activity against a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition in patients having at least one variance in a gene from Tables 1-6, 12-17, and 18-23; and b) synthesizing said compound in an amount sufficient to provide a pharmaceutical effect in a patient suffering from said neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition. 1 14. A method for determining whether a variance in a gene from Tables 1-6, 12- 17, and 18-23 provides variable patient response to a method of treatment for a disease or condition, comprising: determining whether the response of a first patient or set of patients suffering from a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition differs from the response of a second patient or set of patients suffering from said disease or condition; determining whether the presence or absence of at least one variance in said gene differs between said first patient or set of patient and said second patient or set of patients; 2874 wherein conelation of said presence or absence of at least one variance and the response of said patient to said treatment is indicative that said at least one variance provides variable patient response. 115. The method of claim 114, further comprising identifying at least one variance in a said gene. 116. The method of claim 114, wherein a plurality of pairwise comparisons of treatment response and the presence or absence of at least one variance are performed for a plurality of patients. 117. The method of claim 114, wherein said determining whether the presence or absence of at least one variance in at least one gene comprises comparing the response of at least one patient homozygous for said at least one variance with at least one patient homozygous for the alternative form of said at least one variance. 118. The method of claim 114, wherein said determining whether the presence or absence of said at least one variance in at least one gene comprises comparing the response of at least one patient heterozygous for said at least one variance with the response of at least one patient homozygous for said at least one variance. 1 19. The method of claim 114, wherein it is previously known that patient response to said method of treatment is variable. 120. The method of claim 114, wherein said disease or condition is a disease or condition listed in the Detailed Description, Examples, or Tables herein. 121. The method of claim 114, wherein said disease or condition is selected from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, spasticity, psychoses, and stroke, dmg-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, 2875 adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, arrhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease. 122. The method of claim 114, wherein said method of treatment comprises administration of a compound effective to treat said disease or condition. 123. A method of treating a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition in a patient, comprising a) selecting a patient whose cells comprise an allele of a gene from Tables 1- 6, 12-17, and 18-23, wherein said allele comprises at least one variance conelated with more effective treatment of said neurological or psychiatric disease, drag- induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or condition; and b) altering the level of activity in cells of said patient of a product said allele, wherein said altering provides a therapeutic effect. 124. A method for determining a method of treatment effective to treat a disease or condition in a sub-population of patients, comprising altering the level of activity of a product of an allele of a gene from Tables 1- 6, 12-17, and 18-23; and determining whether said alteration provides a differential effect related to reducing or alleviating a disease or condition as compared to at least one alternative allele, wherein the presence of a said differential effect is indicative that said altering the level of activity comprises an effective treatment for said disease or condition in said sub-population. 125. A method for performing a clinical trial or study, comprising selecting or stratifying subjects using a variance or variances or haplotypes from one or more genes specified in Tables 1-6, 12-17, and 18-23. 126. The method of claim 125, wherein differential efficacy, tolerance, or safety of a treatment in a subset of patients who have a particular variance, variances, or haplotype in a gene or genes from Tables 1-6, 12-17, and 18-23, comprising 2876 conducting a clinical trial and using a statistical test to assess whether a relationship exists between efficacy, tolerance, or safety with the presence or absence of any of said variances or haplotype in one or more of said genes, wherein results of said clinical trial or study are indicative whether a higher or lower efficacy, tolerance, or safety of said treatment in said subset of patients is associated with any of said variance or variances or haplotype in one or more of said gene. 127. The method of claim 125 wherein normal subjects or patients are prospectively stratified by genotype in different genotype-defined groups, including the use of genotype as a enrollment criterion, using a variance, variances or haplotypes from Tables 1-6, 12-17, and 18-23, and subsequently a biological or clinical response variable is compared between the different genotype-defined groups. 128. The method of claim 125 wherein the normal subjects or patients in a clinical trial or study are stratified by a biological or clinical response variable in different biologically or clinically-defined groups, and subsequently the frequency of a variance, variances or haplotypes from Tables 1-6, 12-17, and 18-23 is measured in the different biologically or clinically defined groups. 129. The method of claim 127 or 128 where the normal subjects or patients in a clinical trial or study are stratified by at least one demographic characteristic selected from the goups consisting of sex, age, racial origin, ethnic origin, or geographic origin. 130. The method of claim 125, wherein said determining comprises assigning said patient to a group to receive said method of treatment or to a control group. 131. A method for determining whether a variance in a gene provides variable patient response to a method of treatment for a disease or condition, comprising: determining whether the response of a first patient or set of patients suffering from a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or 2877 renal disease, or proliferative disease or condition differs from the response of a second patient or set of patients suffering from said disease or condition; determining whether the presence or absence of at least one variance in a gene from Tables 1-6, 12-17, and 18-23 differs between said first patient or set of patient and said second patient or set of patients; wherein conelation of said presence or absence of at least one variance and the response of said patient to said treatment is indicative that said at least one variance provides variable patient response. 132. A method for treating a patient at risk for a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or diagnosed with a neurological or psychiatric disease, drug-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease, comprising identifying a said patient and determining the patient's genotype allele status for a gene from Tables 1-6, 12-17, and 18-23; determining a treatment protocol using the patient's genotype status to provide a prediction of the efficacy and safety of a therapy in light of a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or an associated pathological condition. 133. A method for identifying a patient for participation in a clinical trial of a therapy for the treatment of neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease or disorder, comprising identifying a patient with a disease risk and determining the patient's genotype, allele status for an identified gene from Tables 1-6, 12-17, and 18-23. 134. The method of claim 133, further comprising determining the patient's allele status and selecting those patients having at least one wild type allele of said gene as candidates likely to develop a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease. 2878 135. A method for treating a patient at risk for a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease, comprising identifying a patient with a risk for said disease; determining the genotypic allele status of the patient for at least one gene from Tables 1-6, 12-17, and 18-23; and converting the genotypic allele status into a treatment protocol that comprises a comparison of the genotypic allele status determination with the allele frequency of a control population, thereby allowing a statistical calculation of the patient's risk for having a neurological or psychiatric disease, dmg-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease. 136. A method for treating a patient at risk for or diagnosed with having a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease, comprising identifying a said patient; determining the gene allele load status of the patient for at least one gene from Tables 1-6, 12-17, and 18-23 and converting the gene allele load status into a treatment protocol that includes a comparison of the allele status determinations with the allele frequency of a control population, thereby allowing a statistical calculation of the patient's risk for having having a neurological or psychiatric disease, drag- induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease. 137. A method for improving the safety of candidate therapies associated with having a neurological or psychiatric disease, drag-induced disease or toxicity, inflammation or immune disease, endocrine or metabolic disease, cardiovascular or renal disease, or proliferative disease, comprising comparing the relative safety of the candidate therapeutic intervention in patients having different alleles in one or more than one of the genes listed in Tables 1-6, 12-17, and 18-23, thereby identifying subsets of patients with differing safety of the candidate therapeutic intervention. 138. A kit for determination of the presence or absence of at least one sequence variance in a gene identified in any of Tables 1-6, 12-17, and 18-23, comprising 2879 at least one probe that preferentially hybridizes with a nucleic acid sequence conesponding to a portion of said gene or at least one primer comprising a nucleic acid sequence conesponding to a portion of said gene or a sequence complementary thereto or both said at least one probe and said at least one primer. 139. A method for determining whether there is a genetic component to intersubject variation in a sunogate treatment response, comprising: a. administering said treatment to a group of related normal subjects and a group of unrelated normal subjects; b. measuring a sunogate pharmacodynamic or pharmacokinetic drag response variable in said subjects; c. performing a statistical test measuring the variation in response in said group of related normal subjects and, separately in said group or unrelated normal subjects; d. comparing the magnitude or pattern of variation in response or both between said groups to determine if the responses of said groups are different, using a predetermined statistical measure of difference, wherein a difference in response between said groups is indicative that there is a genetic component to intersubject variation in said sunogate treatment response. 140. The method of claim 129, wherein the size of the related and unrelated groups is set in order to achieve a predetermined degree of statistical power. 141. A method for evaluating the combined contribution of two or more variances to a sunogate drag response phenotype in subjects, comprising: a. genotyping a set of unrelated subjects participating in a clinical trial or study of a compound for two or more variances to identify subjects with specific genotypes, wherein said two or more specific genotypes define two or more genotype-defined groups; b. administering a drag to subjects with two or more of said specific genotypes; 2880 c. measuring a sunogate pharmacodynamic or pharmacokinetic drag response variable in said subjects; d. performing statistical tests to measure response in said groups separately, wherein said statistical tests provide a measurement of variation in response with each said group; e. comparing the magnitude or pattern of variation in response or both between said groups to determine if said groups are different using a predetermined statistical measure of difference. 142. The method of claim 141, wherein said clinical trial or study is a Phase I clinical trial or study. 143. The method of claim 141, wherein said specific genotypes are homozygous genotypes for two variances. 144. The method of claim 141, wherein the comparison is between groups of subjects differing in three or more variances. 145. A method for providing contract research services to a client, comprising: a. enrolling subjects in a clinical drug trial or study unit for the purpose of genotyping said subjects in order to assess the contribution of one or more variances or haplotypes to variation in drag response; b. genotyping said subjects to determine the status of one or more variances in said subjects; c. administering a compound to said subjects and measuring a sunogate dmg response variable; d. comparing responses between two or more genotype-defined groups of said subjects to determine whether there is a genetic component to the interperson variability in response to said compound; and e. reporting the results of said clinical drag trial or study unit to a contracting entity. 2881 146. The method of claim 145, wherein said clinical drag trial or study unit is a Phase I drag trial or study unit. 147. The method of claim 145, wherein at least some of the subjects have disclosed that they are related to each other and said comparing includes comparison of groups of related individuals. 148. The method of claim 147, wherein the related individuals are encouraged to participate by compensation in proportion to the number of their relatives participating. 149. A method for recruiting a clinical trial or study population for studies of the influence of one or more variances or haplotypes on drag response, comprising soliciting subjects to participate in said clinical trial or study; obtaining consent of said subjects for participation in said clinical trial or study; obtaining additional related subjects for participation in said clinical trial by compensating one or more of the related subjects for said participation at a level based on the number of related subjects participating or based on participation of at least a minimum specified number of related subjects. from the group consisting of neoplastic disorders, amyotrophic lateral sclerosis, anxiety, dementia, depression, epilepsy, Huntington's disease, migraine, demyehnating disease, multiple sclerosis, pain, Parkinson's disease, schizophrenia, psychoses, and stroke, drug-induced diseases, disorders, or toxicities consisting of blood dyscrasias, cutaneous toxicities, systemic toxicities, central nervous system toxicities, hepatic toxicities, cardiovascular toxicities, pulmonary toxicities, and renal toxicities, arthritis, chronic obstmctive pulmonary disease, autoimmune disease, transplantation, pain associated with inflammation, psoriasis, atherosclerosis, asthma, inflammatory bowel disease, and hepatitis, diabetes mellitus, metabolic syndrome X, diabetes insipidus, obesity, contraception, infertility, hormonal insufficiency related to aging, osteoporosis, acne, alopecia, adrenal dysfunction, thyroid dysfunction, and parathyroid dysfunction, anemia, angina, anhythmia, hypertension, hypothermia, ischemia, heart failure, thrombosis, renal disease, restenosis, and peripheral vascular disease

Inventors: STANTON VINCENT JR, STANTON, VINCENT, JR.
Applicants: STANTON VINCENT JR, VARIAGENICS INC, STANTON, VINCENT, JR., VARIAGENICS, INC.
Application year: 2000
Main classification: C12Q1
IPC codes: A61K45, A61P1, A61P3, A61P5, A61P7, A61P9, A61P11, A61P13, A61P15, A61P17, A61P19, A61P21, A61P25, A61P29, A61P35, A61P37, C12N15, C12Q1