36 HUMAN SECRETED PROTEINS

Abstract: The present invention relates to novel human secreted proteins and isolated nucleic acids containing the coding regions of the genes encoding such proteins. Also provided are vectors, host cells, antibodies, and recombinant methods for producing human secreted proteins. The invention further relates to diagnostic and therapeutic methods useful for diagnosing and treating disorders related to these novel human secreted proteins.

Description: 36 Human Secreted Proteins Field of the Invention This invention relates to newly identified polynucleotides and the polypeptides encoded by these polynucleotides, uses of such polynucleotides and polypeptides, and their production. Background of the Invention Unlike bacterium, which exist as a single compartment surrounded by a membrane, human cells and other eucaryotes are subdivided by membranes into many functionally distinct compartments. Each membrane-bounded compartment, or organelle, contains different proteins essential for the function of the organelle. The cell uses "sorting signals," which are amino acid motifs located within the protein, to target proteins to particular cellular organelles. One type of sorting signal, called a signal sequence, a signal peptide, or a leader sequence, directs a class of proteins to an organelle called the endoplasmic reticulum (ER). The ER separates the membrane-bounded proteins from all other types of proteins. Once localized to the ER, both groups of proteins can be further directed to another organelle called the Golgi apparatus. Here, the Golgi distributes the proteins to vesicles, including secretory vesicles, the cell membrane, lysosomes, and the other organelles. Proteins targeted to the ER by a signal sequence can be released into the extracellular space as a secreted protein. For example, vesicles containing secreted proteins can fuse with the cell membrane and release their contents into the extracellular space - a process called exocytosis. Exocytosis can occur constitutively or after receipt of a triggering signal. In the latter case, the proteins are stored in secretory vesicles (or secretory granules) until exocytosis is triggered. Similarly, proteins residing on the cell membrane can also be secreted into the extracellular space by proteolytic cleavage of a "linker" holding the protein to the membrane. Despite the great progress made in recent years, only a small number of genes encoding human secreted proteins have been identified. These secreted proteins include the commercially valuable human insulin, interferon, Factor Niπ, human growth hormone, tissue plasminogen activator, and erythropoeitin. Thus, in light of the pervasive role of secreted proteins in human physiology, a need exists for identifying and characterizing novel human secreted proteins and the genes that encode them. This knowledge will allow one to detect, to treat, and to prevent medical disorders by using secreted proteins or the genes that encode them. Summary of the Invention The present invention relates to novel polynucleotides and the encoded polypeptides. Moreover, the present invention relates to vectors, host cells, antibodies, and recombinant methods for producing the polypeptides and polynucleotides. Also provided are diagnostic methods for detecting disorders related to the polypeptides, and therapeutic methods for treating such disorders. The invention further relates to screening methods for identifying binding partners of the polypeptides. Detailed Description Definitions The following definitions are provided to facilitate understanding of certain terms used throughout this specification. In the present invention, "isolated" refers to material removed from its original environment (e.g., the natural environment if it is naturally occurring), and thus is altered "by the hand of man" from its natural state. For example, an isolated polynucleotide could be part of a vector or a composition of matter, or could be contained within a cell, and still be "isolated" because that vector, composition of matter, or particular cell is not the original environment of the polynucleotide. In the present invention, a "secreted" protein refers to those proteins capable of being directed to the ER, secretory vesicles, or the extracellular space as a result of a signal sequence, as well as those proteins released into the extracellular space without necessarily containing a signal sequence. If the secreted protein is released into the extracellular space, the secreted protein can undergo extracellular processing to produce a "mature" protein. Release into the extracellular space can occur by many mechanisms, including exocytosis and proteolytic cleavage. In specific embodiments, the polynucleotides of the invention are less than 300 kb, 200 kb, 100 kb, 50 kb, 15 kb, 10 kb, or 7.5 kb in length. In a further embodiment, polynucleotides of the invention comprise at least 15 contiguous nucleotides of the coding sequence, but do not comprise all or a portion of any intron. In another embodiment, the nucleic acid comprising the coding sequence does not contain coding sequences of a genomic flanking gene (i.e., 5' or 3' to the gene in the genome). As used herein , a "polynucleotide" refers to a molecule having a nucleic acid sequence contained in SEQ ID NO:X or the cDNA contained within the clone deposited with the ATCC. For example, the polynucleotide can contain the nucleotide sequence of the full length cDNA sequence, including the 5' and 3' untranslated sequences, the coding region, with or without the signal sequence, the secreted protein coding region, as well as fragments, epitopes, domains, and variants of the nucleic acid sequence. Moreover, as used herein, a "polypeptide" refers to a molecule having the translated amino acid sequence generated from the polynucleotide as broadly defined. In the present invention, the full length sequence identified as SEQ ID NO:X was often generated by overlapping sequences contained in multiple clones (contig analysis). A representative clone containing all or most of the sequence for SEQ LD NO:X was deposited with the American Type Culture Collection ("ATCC"). As shown in Table 1, each clone is identified by a cDNA Clone ID (Identifier) and the ATCC Deposit Number. The ATCC is located at 10801 University Boulevard, Manassas, Virginia 20110-2209, USA. The ATCC deposit was made pursuant to the terms of the Budapest Treaty on the international recognition of the deposit of microorganisms for purposes of patent procedure. A "polynucleotide" of the present invention also includes those polynucleotides capable of hybridizing, under stringent hybridization conditions, to sequences contained in SEQ ID NO:X, the complement thereof, or the cDNA within the clone deposited with the ATCC. "Stringent hybridization conditions" refers to an overnight incubation at 42° C in a solution comprising 50% formamide, 5x SSC (750 mM NaCl, 75 mM sodium citrate), 50 mM sodium phosphate (pH 7.6), 5x Denhardt's solution, 10% dextran sulfate, and 20 μg/ml denatured, sheared salmon sperm DNA, followed by washing the filters in O.lx SSC at about 65°C. Also contemplated are nucleic acid molecules that hybridize to the polynucleotides of the present invention at lower stringency hybridization conditions. Changes in the stringency of hybridization and signal detection are primarily accomplished through the manipulation of formamide concentration (lower percentages of formamide result in lowered stringency); salt conditions, or temperature. For example, lower stringency conditions include an overnight incubation at 37°C in a solution comprising 6X SSPE (20X SSPE = 3M NaCl; 0.2M NaH 2 PO 4 ; 0.02M EDTA, pH 7.4), 0.5% SDS, 30% formamide, 100 ug/ml salmon sperm blocking DNA; followed by washes at 50°C with 1XSSPE, 0.1% SDS. In addition, to achieve even lower stringency, washes performed following stringent hybridization can be done at higher salt concentrations (e.g. 5X SSC). Note that variations in the above conditions may be accomplished through the inclusion and/or substitution of alternate blocking reagents used to suppress background in hybridization experiments. Typical blocking reagents include Denhardt's reagent, BLOTTO, heparin, denatured salmon sperm DNA, and commercially available proprietary formulations. The inclusion of specific blocking reagents may require modification of the hybridization conditions described above, due to problems with compatibility. Of course, a polynucleotide which hybridizes only to polyA+ sequences (such as any 3' terminal polyA+ tract of a cDNA shown in the sequence listing), or to a complementary stretch of T (or U) residues, would not be included in the definition of "polynucleotide," since such a polynucleotide would hybridize to any nucleic acid molecule containing a poly (A) stretch or the complement thereof (e.g., practically any double-stranded cDNA clone). The polynucleotide of the present invention can be composed of any polyribonucleotide or polydeoxribonucleotide, which may be unmodified RNA or DNA or modified RNA or DNA. For example, polynucleotides can be composed of single- and double-stranded DNA, DNA that is a mixture of single- and double-stranded regions, single- and double-stranded RNA, and RNA that is mixture of single- and double-stranded regions, hybrid molecules comprising DNA and RNA that may be single-stranded or, more typically, double-stranded or a mixture of single- and double- stranded regions. In addition, the polynucleotide can be composed of triple-stranded regions comprising RNA or DNA or both RNA and DNA. A polynucleotide may also contain one or more modified bases or DNA or RNA backbones modified for stability or for other reasons. "Modified" bases include, for example, tritylated bases and unusual bases such as inosine. A variety of modifications can be made to DNA and RNA; thus, "polynucleotide" embraces chemically, enzymatically, or metabolically modified forms. The polypeptide of the present invention can be composed of amino acids joined to each other by peptide bonds or modified peptide bonds, i.e., peptide isosteres, and may contain amino acids other than the 20 gene-encoded amino acids. The polypeptides may be modified by either natural processes, such as posttranslational processing, or by chemical modification techniques which are well known in the art. Such modifications are well described in basic texts and in more detailed monographs, as well as in a voluminous research literature. Modifications can occur anywhere in a polypeptide, including the peptide backbone, the amino acid side-chains and the amino or carboxyl termini. It will be appreciated that the same type of modification may be present in the same or varying degrees at several sites in a given polypeptide. Also, a given polypeptide may contain many types of modifications. Polypeptides may be branched , for example, as a result of ubiquitination, and they may be cyclic, with or without branching. Cyclic, branched, and branched cyclic polypeptides may result from posttranslation natural processes or may be made by synthetic methods. Modifications include acetylation, acylation, ADP-ribosylation, amidation, covalent attachment of flavin, covalent attachment of a heme moiety, covalent attachment of a nucleotide or nucleotide derivative, covalent attachment of a lipid or lipid derivative, covalent attachment of phosphotidylinositol, cross-linking, cyclization, disulfide bond formation, demethylation, formation of covalent cross-links, formation of cysteine, formation of pyroglutamate, formylation, gamma-carboxylation, glycosylation, GPI anchor formation, hydroxylation, iodination, methylation, myristoylation, oxidation, pegylation, proteolytic processing, phosphorylation, prenylation, racemization, selenoylation, sulfation, transfer-RNA mediated addition of amino acids to proteins such as arginylation, and ubiquitination. (See, for instance, PROTEINS - STRUCTURE AND MOLECULAR PROPERTIES, 2nd Ed., T. E. Creighton, W. H. Freeman and Company, New York (1993); POSTTRANSLATIONAL COVALENT MODIFICATION OF PROTEINS, B. C. Johnson, Ed., Academic Press, New York, pgs. 1-12 (1983); Seifter et al., Meth Enzymol 182:626-646 (1990); Rattan et al., Ann NY Acad Sci 663:48-62 (1992).) "SEQ ID NO:X" refers to a polynucleotide sequence while "SEQ LD NO:Y" refers to a polypeptide sequence, both sequences identified by an integer specified in Table 1. "A polypeptide having biological activity" refers to polypeptides exhibiting activity similar, but not necessarily identical to, an activity of a polypeptide of the present invention, including mature forms, as measured in a particular biological assay, with or without dose dependency. In the case where dose dependency does exist, it need not be identical to that of the polypeptide, but rather substantially similar to the dose-dependence in a given activity as compared to the polypeptide of the present invention (i.e., the candidate polypeptide will exhibit greater activity or not more than about 25-fold less and, preferably, not more than about tenfold less activity, and most preferably, not more than about three-fold less activity relative to the polypeptide of the present invention.) Polynucleotides and Polypeptides of the Invention FEATURES OF PROTEIN ENCODED BY GENE NO: 1 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: HSSLPHFSSRI (SEQ ID NO:85). Polynucleotides encoding these polypeptides are also encompassed by the invention. Contact of cells with supernatant expressing the product of this gene induces the expression of osteocalcin in human SOAS-2 osteoblastic cells. Osteocalcin is a protein attributed to influencing the bone mineralization of skeletal tissue, and is also thought to be useful in inhibiting osteoblast function. Thus, polynucleotides and polypeptides have uses which include, but are not limited to, inducing the expression of osteocalcin. This gene is expressed primarily in B-cell lymphoma, and to a lesser extent in brain tissue. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, diseases of the hematopoietic system and brain, including cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune and central nervous system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, central nervous system, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in B-cell lymphoma and brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the hematopoietic system and the central nervous system, as well as cancers thereof. The expression of this gene in B-cell lymphoma indicates that this gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Alternatively, the tissue distribution in brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 11 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1427 of SEQ ID NO: 11, b is an integer of 15 to 1441, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 11 , and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 2 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: RDSNGRGDSSLLKFVCPVPLKK (SEQ ID NO:86). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 2. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 2. This gene is expressed primarily in brain and embryonic tissues, and to a lesser extent in several other tissues and organs. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, neurological and developmental diseases and cancers. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the neural and developing systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., neurological, developing, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:49 as residues: Ile-35 to Lys-40. The tissue distribution in brain and embryonic tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the neural system, as well as cancer. The tissue distribution in brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection/treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Furthermore, expression within embryonic tissue and other cellular sources marked by proliferating cells indicates that this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, embryonic development also involves decisions involving cell differentiation and/or apoptosis in pattern formation. Thus, this protein may also be involved in apoptosis or tissue differentiation and could again be useful in cancer therapy. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 12 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2146 of SEQ ID NO: 12, b is an integer of 15 to 2160, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 12, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 3 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: IPEYTFRRRWFH (SEQ ID NO:87). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in breast lymph nodes, brain tissue, hematopoietic cells and cancerous tissues. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, cancer and diseases of the hematopoietic and central nervous systems. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the hematopoietic and central nervous systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, neurological, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in hematopoietic and neural tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the hematopoietic system, the central nervous system, and cancers thereof, particularly leukemias. Expression of this gene product in normal and cancerous lymph nodes indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other 10 processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Alternatively, the tissue distribution in brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection/treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 13 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1188 of SEQ ID NO: 13, b is an integer of 15 to 1202, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 13, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 4 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: LCVSMKIEWGRESCEKK (SEQ ID NO:88). Polynucleotides encoding these polypeptides are also encompassed by the invention. 11 This gene is expressed primarily in leukemia cells. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, diseases of the hematopoietic system and cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the hematopoietic system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in leukemia cells indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the hematopoietic system and cancers thereof, particularly leukemia, as well as cancers of other tissues where expression has been observed. Furthermore, this gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 14 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more 12 polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1540 of SEQ ID NO: 14, b is an integer of 15 to 1554, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 14, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 5 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: RLKTTRAYSSQFWRPEVQNQGVRKV (SEQ LD NO:89). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in CD-34 Positive cord blood cells. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, diseases and disorders of the immune and hematopoietic system, in addition to developing cells and tissues. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune and hematopoietic system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, amniotic fluid, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in CD34 (+) cells indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the hematopoietic and immune systems, including cancers thereof. Furthermore, expression of this gene product in CD34 (+) cells indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor 13 marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ LD NO: 15 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1526 of SEQ ID NO: 15, b is an integer of 15 to 1540, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 15, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 6 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: LTLCLPRSLYALPQCPGPHVHPCPALLWDRAGLPLPLPG CfflGRSQVPWHELHSPAAFNQGMMGMCTYPTPPLGRVMLRCGFLTVPRLSQE AWNVVNPTVGAGVISYLRRPPFLPVLCAPTPTLELPRFSVFVKELTLCCLPLSQCP CHSCEPAAGEVGADLCVAG (SEQ ID ΝO:90), LTLCLPRSLYALPQCPGPHVHP CPALLWDRAGLPLPLPGCI (SEQ ID NO:91), HGRSQVPWHELHSPAAFNQGM MGMCTYPTPPLGRVMLR (SEQ ID NO:92), CGϊ^TVPRLSQEAWVWNPTVGA GVISYLRRPPFLPVLCAPT (SEQ ID ΝO:93), and/or PTLELPRFSVFVKELTLCC LPLSQCPCHSCEPAAGEVGADLCVAG (SEQ ID NO:94). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in lymph nodes, thymus and chronic synovitis tissues, and to a lesser extent in several other tissues and organs. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are 14 not limited to, immune and inflammatory disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune and hematopoietic system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, musculo-skeletal, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in immune tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of inflammatory and hematopoietic disorders. Furthermore, expression of this gene product in thymus and lymph nodes indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 16 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1043 of SEQ ID NO: 16, b is an integer of 15 15 to 1057, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 16, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 7 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: IRHETFRVRGCSISRALSPFPLPFPHPGRSGWSGPEAK (SEQ ID NO:95). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 6. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 6. This gene is expressed primarily in embryonic, placental and umbilical vein tissues, and to a lesser extent in several other tissues and organs, including cancerous tissues. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, ~ tsut are not limited to, disorders of developing organs, growth disorders, and cancer(s). Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the developing and fetal systems, highly vascularized tissues and cancer, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., embryonic, placental, developing, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in placental and embryonic tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of diseases of developing, embryonic, and/or fetal systems, as well as growth disorders and cancer(s). Furthermore, the tissue distribution in placental tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis and/or treatment of disorders of the placenta. Specific expression within the placenta indicates that this gene product may play a role in the proper establishment and maintenance of placental function. 16 Alternatively, this gene product may be produced by the placenta and then transported to the embryo, where it may play a crucial role in the development and/or survival of the developing embryo or fetus. Expression of this gene product in a vascular-rich tissue such as the placenta also indicates that this gene product may be produced more generally in endothelial cells or within the circulation. In such instances, it may play more generalized roles in vascular function, such as in angiogenesis. It may also be produced in the vasculature and have effects on other cells within the circulation, such as hematopoietic cells. It may serve to promote the proliferation, survival, activation, and/or differentiation of hematopoietic cells, as well as other cells throughout the body. Likewise, expression within embryonic tissue and other cellular sources marked by proliferating cells indicates that this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, embryonic development also involves decisions involving cell differentiation and/or apoptosis in pattern formation. Thus, this protein may also be involved in apoptosis or tissue differentiation and could again be useful in cancer therapy. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 17 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2066 of SEQ ID NO: 17, b is an integer of 15 to 2080, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 17, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 8 This gene is expressed primarily in the hematopoietic system, the central nervous system, and developing systems, as well as in cancer(s), and to a lesser extent in several other tissues and organs. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a 17 biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, hematopoietic diseases, developmental disorders, central nervous system, and cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the central nervous system, hematopoietic system, and cancer, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, neurological, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:55 as residues: Lys-37 to Ile-45. The tissue distribution in immune and neurological tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis, treatment, and/or prevention of disorders of the hematopoietic system, the central nervous system, and cancer(s). This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Alternatively, the tissue distribution indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection/treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 18 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 588 of SEQ ID NO: 18, b is an integer of 15 to 602, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 18, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 9 This gene is expressed primarily in fetal skin. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, growth and skin abnormalities. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of epithelial structures, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., epithelial, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in fetal epithelium indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of growth and skin disorders. Furthermore, the tissue distribution indicates that polynucleotides and polypeptides corresponding to this gene are useful for the treatment, diagnosis, and/or prevention of various skin disorders including congenital disorders (i.e. nevi, moles, freckles, Mongolian spots, hemangiomas, port-wine 19 syndrome), integumentary tumors (i.e. keratoses, Bowen's disease, basal cell carcinoma, squamous cell carcinoma, malignant melanoma, Paget's disease, mycosis fungoides, and Kaposi's sarcoma), injuries and inflammation of the skin (i.e., wounds, rashes, prickly heat disorder, psoriasis, dermatitis), atherosclerosis, uticaria, eczema, photosensitivity, autoimmune disorders (i.e. lupus erythematosus, vitiligo, dermatomyositis, morphea, scleroderma, pemphigoid, and pemphigus), keloids, striae, erythema, petechiae, purpura, and xanthelasma. Moreover, such disorders may predispose an individual (i.e. increase an individuals susceptibility) to viral and bacterial infections of the skin (i.e. cold sores, warts, chickenpox, molluscum contagiosum, herpes zoster, boils, cellulitis, erysipelas, impetigo, tinea, althletes foot, and ringworm). Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and immunotherapy targets for the above listed tumors and tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 19 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 615 of SEQ ID NO: 19, b is an integer of 15 to 629, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 19, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 10 When tested against sensory neuronal cell lines, supernatants removed from cells containing this gene activated the EGR1 assay. Thus, it is likely that this gene activates sensory neuron cells, and to a lesser extent other neuronal cells, through a signal transduction pathway. Early growth response 1 (EGR1) is a promoter associated with certain genes that induces various tissues and cell types upon activation, leading the cells to undergo differentiation and proliferation. This gene is expressed primarily in epileptic frontal cortex tissue of the brain, and to a lesser extent in fetal heart tissue. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a 20 biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, neurological and cardiovascular abnormalities. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the central nervous and vascular systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., neurological, vascular, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ED NO:57 as residues: Pro-43 to Pro-50, Asn-65 to Gly-70. The tissue distribution in frontal cortex tissue of the brain and fetal heart tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of nervous system and cardiovascular disorders. The tissue distribution in frontal cortex tissue, in conjunction with the observed biological activity data, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis and/or treatment of disorders of the brain and nervous system. Elevated expression of this gene product within the frontal cortex of the brain indicates that it may be involved in neuronal survival; synapse formation; conductance; neural differentiation, etc. Such involvement may impact many processes, such as learning and cognition. It may also be useful in the treatment of such neurodegenerative disorders as schizophrenia; ALS; or Alzheimer's. Alternatively, the tissue distribution in fetal heart tissue indicates that the protein product of this gene is useful for the diagnosis and treatment of conditions and pathologies of the cardiovascular system, such as heart disease, restenosis, atherosclerosis, stoke, angina, thrombosis, and wound healing. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:20 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more 21 polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2053 of SEQ ID NO:20, b is an integer of 15 to 2067, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:20, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 11 The translation product of this gene shares sequence homology with the polypeptide sequence of a novel protein ETI-1, which has cytostatic activity. ETI-1 is thought to be useful as an anti-tumor agent. Based on the sequence similarity, the translation product of this clone is expected to share biological activities with cytostatic proteins. Such activities are known in the art and described elsewhere herein. When tested against U937 Myeloid cell lines, supernatants removed from cells containing this gene activated the GAS assay. Thus, it is likely that this gene activates myeloid cells, and to a lesser extent other immune cells, through the Jak-STAT signal transduction pathway. The gamma activating sequence (GAS) is a promoter element found upstream of many genes which are involved in the Jak-STAT pathway. The Jak-STAT pathway is a large, signal transduction pathway involved in the differentiation and proliferation of cells. Therefore, activation of the Jak-STAT pathway, reflected by the binding of the GAS element, can be used to indicate proteins involved in the proliferation and differentiation of cells. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: PDSRPEARGDHWRPSRGLRVTGATRSLMGPWGEPELLV WRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVLRRPGANHEGSASR QKAI^LVSCFAC jVFLAT(XLDLLPDYLAAroEALAALHNrLQFPLQEFILA (SEQ LD ΝO:96), PDSRPEARGDHVVRPSRGLRVTGATRSIMGPWGEP (SEQ ID NO:97), ELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLC (SEQ ID NO:98), SLVPICVLRRPGANHEGSASRQKALSLVSCFAGGVF (SEQ ID NO:99), and/or LATCLLDLLPDYLAAIDEALAALHNrLQFPLQEFILA (SEQ ID NO: 100). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 1. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 1. 22 This gene is expressed primarily in endocrine organs and cancerous tissues, such as pancreas and endometrial tumors, as well as neuroblastomas, and to a lesser extent in various normal and transformed cell types. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, hormonal abnormalities and tumors. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the endocrine and immune systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., endocrine, immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ LD NO:58 as residues: Lys-17 to Glu-27, Gln-40 to Gly-47. The tissue distribution in cancerous tissues such as pancreatic and endometrial tumors, in conjunction with the observed biological activity data and the homology to a protein known to have cytostatic activity, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of tumors of various tissue types, such as pancreas and endometrium, as well as cancers of other tissues where expression has been observed. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and immunotherapy targets for the above listed tumors and tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:21 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 983 of SEQ ID NO:21, b is an integer of 15 to 997, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:21, and where b is greater than or equal to a + 14. 23 FEATURES OF PROTEIN ENCODED BY GENE NO: 12 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: KYILSSPLLDSLAEHKNLVWKSFLPRNF (SEQ ID NO: 101). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in leukemic spleen tissue. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, leukemia and other cancers. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid frorrran individual not having the disorder. The tissue distribution in leukemic spleen tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for study and treatment of immune disorders and neoplasias, as well as cancers of other tissues where expression has been observed. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and immunotherapy targets for the above listed tumors and tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:22 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1369 of SEQ ID NO:22, b is an integer of 15 to 1383, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:22, and where b is greater than or equal to a + 14. 24 FEATURES OF PROTEIN ENCODED BY GENE NO: 13 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: YGKVNDLAPLHLDARISLSTLQQQLGQPEKALEALEPM YDPDTLAQDAΝAAQXELKLLLHRSTLLFSQGK (SEQ ID NO: 102). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 2. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 2. This gene is expressed primarily in hematopoietic tissues such as fetal liver/spleen, and to a lesser extent in several other normal and transformed cell types. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune and growth abnormalities. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, liver, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:60 as residues: Ser-31 to Arg-36, Ser-44 to Glu-55, Asp-112 to Glu-119, Lys-132 to Asn-139, Asn-148 to Leu-154, Thr-214 to Leu-220, Gly-260 to Ser-265. The tissue distribution in immune tissues such as fetal liver/spleen indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of immune disorders. Expression of this gene product in fetal liver/spleen tissue indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). 25 Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:23 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1499 of SEQ ID NO:23, b is an integer of 15 to 1513, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:23, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 14 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: DFMETFPDFCLPLAPHYLGKAALWAMCPGRAWAGCGPV LRTSHLGPHSALPSWCNICXQAIVGAGRQRGLSEDPTCASHWDTKTGLVPSCG AGKGI (SEQ ID NO: 103), DFMETFPDFCLPLAPHYLGKAALWAMCPGRAWAG CGPVLRTSHL (SEQ ID NO: 104), and/or GPHSALPSWCNICXQAIVGAGRQRGL SEDPTCASHWDTKTGLVPSCGAGKGI (SEQ ID NO: 105). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 7. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 7. This gene is expressed primarily in cerebellum tissue, and to a lesser extent in fetal liver, synovial sarcoma and glioblastoma. 26 Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a. biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, neurodegenerative diseases and brain tumors. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the nervous and immune systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., nervous, immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution and in cerebellum tissue and fetal liver tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of immune, neurodegenerative and cognitive disorders and neoplasias. The tissue distribution in cerebellum tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Alternatively, expression of this gene product in fetal liver indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have 27 commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 24 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1030 of SEQ ID NO:24, b is an integer of 15 to 1044, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:24, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 15 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: RLPQRGQWAWVLQDALGIAFCLYMLKTIRLPTFKACTL LLLVLFLYDIFFVFITPFLTKSGSSLMVEVATGPSDSATREKLPMVLKVPRLNSSP LALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVGLLVTF VALALMQRGQPALLYLVPCTLVTSCANALWRRELGNFWTGSGFAKVLPPSPW APAPADGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMRE PGSPAESEGRDQAQPSPVTQPGASA (SEQ ID NO: 106), RLPQRGQWAWVLQD ALGIAFCLYMLKTIRLPTFKACTLLLLVL (SEQ ID NO: 107), FLYDIFFVFITPF LTKSGSSIMVEVATGPSDSATREKLPMVLKV (SEQ ID NO: 108), PRLNSSPL ALCDRPFSLLGFGDLLVPGLLVAYCHRFDIQVQSSR (SEQ ID NO: 109), VYFV ACTIAYGVGLLNrFVALALMQRGQPALLYLVPCTLVTSC (SEQ ID NO: 110), AVALWRRELGVFWTGSGFAKVLPPSPWAPAPADGPQPPKD (SEQ ID NO: 111 ), SATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMRE (SEQ ID NO: 112), and/or PGSPAESEGRDQAQPSPVTQPGASA(SEQ ID NO: 113). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 19. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 19. 28 This gene is expressed primarily in brain and placental tissue, and to a lesser extent in various other normal and transformed tissues. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, placental, neurological and cancerous abnormalities. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the placenta and central nervous system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., neurological, placental, lung, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:62 as residues: Gly-127 to Asp-134, Gly-194 to Arg-201, His-205 to Glu-217, Pro-275 to Arg-280, Pro-287 to Gln-294, Arg-315 to Arg-325. The tissue distribution in brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or treatment of central nervous system disorders and neoplasias. Furthermore, the tissue distribution in brain tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection/treatment of neurodegenerative disease states and behavioral disorders such as Alzheimers Disease, Parkinsons Disease, Huntingtons Disease, Tourette Syndrome, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, the gene or gene product may also play a role in the treatment and/or detection of developmental disorders associated with the developing embryo, or sexually-linked disorders. Alternatively, the tissue distribution in placental tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis and/or treatment of disorders of the placenta. Specific expression within the placenta indicates that this gene product may play a role in the proper establishment and maintenance of placental function. Alternately, this gene product may be produced by 29 the placenta and then transported to the embryo, where it may play a crucial role in the development and/or survival of the developing embryo or fetus. Moreover, expression of this gene product in a vascular-rich tissue such as the placenta also indicates that this gene product may be produced more generally in endothelial cells or within the circulation. In such instances, it may play more generalized roles in vascular function, such as in angiogenesis. It may also be produced in the vasculature and have effects on other cells within the circulation, such as hematopoietic cells. It may serve to promote the proliferation, survival, activation, and/or differentiation of hematopoietic cells, as well as other cells throughout the body. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ LD NO: 25 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2561 of SEQ ID NO:25, b is an integer of 15 to 2575, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:25, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 16 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: ESSGLPALGPRRRPWEQRWSDPITLK (SEQ ID NO: 114), and/or LTLALDEIRLLKKDLGLIEMKKTDSEKRFGSVSFGRSCRLIPHALASWL QTLLLCFCCRIC (SEQ ID NO: 115). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 12. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 12. This gene is expressed primarily in placental and embryonic tissues and PHA activated T-cells. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are 30 not limited to, growth and immune disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the developing and immune systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., developing, immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ LD NO:63 as residues: Arg-21 to Leu-26. The tissue distribution in placental and embryonic tissues, as well as in T-cells, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study and/or diagnosis of growth and immune disorders. Furthermore, the tissue distribution in placental and embryonic tissues indicates that polynucleotides and polypeptides corresponding to this gene are useful for the diagnosis and/or treatment of disorders of the placenta. Specific expression within the placenta indicates that this gene product may play a role in the proper establishment and maintenance of placental function. Alternately, this gene product may be produced by the placenta and then transported to the embryo, where it may play a crucial role in the development and or survival of the developing embryo or fetus. Moreover, expression of this gene product in a vascular-rich tissue such as the placenta also indicates that this gene product may be produced more generally in endothelial cells or within the circulation. In such instances, it may play more generalized roles in vascular function, such as in angiogenesis. It may also be produced in the vasculature and have effects on other cells within the circulation, such as hematopoietic cells. It may serve to promote the proliferation, survival, activation, and/or differentiation of hematopoietic cells, as well as other cells throughout the body. Expression within embryonic tissue and other cellular sources marked by proliferating cells indicates that this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, embryonic development also involves decisions involving cell differentiation and/or apoptosis in pattern formation. Thus, this protein may also be involved in apoptosis or tissue differentiation and could again be useful in cancer therapy. 31 Alternatively, expression of this gene product in T-cells indicates a role in the regulation of the proliferation; survival; differentiation; and/or activation of potentially all hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are relatedTo SEQ ID NO:26 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 704 of SEQ ID NO:26, b is an integer of 15 to 718, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:26, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 17 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: GRPTRPVMAIQSLHPCPSELCCRACVXFYHWA (SEQ ID NO: 116). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in activated monocytes, primary dendritic cells, and GM-CSF stimulated macrophages, and to a lesser extent in activated T-cells and adult brain. 32 Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune regulation and immune disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:64 as residues: Thr-24 to Gly-42, Glu-53 to Gly-58. The tissue distribution in immune cells and leukocytes such as monocytes, macrophage, primary dendritic cells, and T-cells, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study, diagnosis and/or treatment of immune dysfunction and other immune disorders. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes that may also suggest a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the gene or protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immune deficiency diseases such as AIDS, leukemia, rheumatoid arthritis, inflammatory bowel disease, sepsis, acne, and psoriasis. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Expression of this gene product in T cells and primary dendritic cells also strongly indicates a role for this protein in immune function and immune surveillance. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:27 and may have been publicly available prior to conception of the present 33 invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 640 of SEQ ID NO:27, b is an integer of 15 to 654, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:27, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 18 The translation product of this gene shares sequence homology with NADH ubiquinone oxidoreductase B15 complex, which is thought to be important in cellular respiration and metabolism. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: NSKNTRNERSFLKLFRNIHDIPLTV LENK (SEQ ID NO: 117). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in fetal liver/spleen and infant brain tissues, and to a lesser extent in fetal kidney and adipose tissues. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, growth and developmental disorders, and adult metabolic disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the developmental and metabolic systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, renal, neurological, metabolic, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in a number of fetal and infant tissues, as well as the homology to NADH ubiquinone oxidoreductase B 15 complex, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study, diagnosis and/or treatment of various developmental and growth disorders, and adult 34 metabolic disorders, such as Tay-Sachs disease, phenylkenonuria, galactosemia, hyperlipidemias, porphyrias, and Hurler's syndrome. Furthermore, the tissue distribution in adipose tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the treatment of obesity and other metabolic and endocrine conditions or disorders. Furthermore, the protein product of this gene may show utility in ameliorating conditions which occur secondary to aberrant fatty-acid metabolism (e.g. aberrant myelin sheath development), either directly or indirectly. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:28 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1431 of SEQ ID NO: 28, b is an integer of 15 to 1445, where both a and b correspond to the positions of nucleotide residues shown in SEQ LD NO:28, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 19 The translation product of this gene shares sequence similarity with neuronal olfactomedin-related ER localized protein isolated from the rat (Genbank accession no. gil442370). In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: PRVRGEGNRCWTQGALCHRM (SEQ ID NO: 118). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is thought to reside on chromosome 11. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 11. This gene is expressed primarily in synovial sarcoma tissue, and to a lesser extent in fetal dura mater, adipose, and Hodgkin's' lymphoma tissues. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are 35 not limited to, cancers and other metabolic disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the metabolic system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., musculo-skeletal, metabolic, cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:66 as residues: Tyr-76 to Lys-81, Glu-92 to Asp-99, Glu-125 to He- 132, Asp- 197 to Arg-204, Gln-241 to Glu-246, Pro-310 to Ala-316, Thr-332 to His-338, Pro-361 to Ser-366, Leu-392 to Thr-399. The tissue distribution in musculo-skeletal and metabolic tissues, and the sequence similarity to neuronal olfactomedin-related ER localized protein, indicates that polynucleotides and polypeptides corresponding to this gene are useful for the study, diagnosis and/or treatment of cancers and other metabolic disorders. Furthermore, the tissue distribution indicates that polynucleotides and polypeptides corresponding to this gene are useful for the detection, treatment, and/or prevention of various endocrine disorders and cancers, particularly Addison's disease, Cushing's Syndrome, and disorders and/or cancers of the pancreas (e.g. diabetes mellitus), adrenal cortex, ovaries, pituitary (e.g., hyper-, hypopituitarism), thyroid (e.g. hyper-, hypothyroidism), parathyroid (e.g. hyper-, hypoparathyroidism) , hypothallamus, and testes. Furthermore, expression within embryonic tissue and other cellular sources marked by proliferating cells indicates that this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, embryonic development also involves decisions involving cell differentiation and/or apoptosis in pattern formation. Thus, this protein may also be involved in apoptosis or tissue differentiation and could again be useful in cancer therapy. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ LD NO: 29 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the 36 scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2006 of SEQ ID NO:29, b is an integer of 15 to 2020, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:29, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 20 The translation product of this gene shares sequence homology with tissue plasminogen activator gene enhancer element which is thought to play a role in blood clotting. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: FPCICLSGLLDLLIWRPFSEELTKTFG (SEQ ID NO: 119). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in rhabdomyosarcoma and to a lesser extent in lymphocytic leukemia. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, cancers and clotting disorders, such as hemophilia. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the metabolic and blood clotting systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., hematopoietic, developmental, metabolic disorders, and cancerous and wounded tissues) or bodily fluids (e.g., serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ LD NO:67 as residues: Cys-38 to Cys-45, Leu-49 to Ala-54. The homology to the conserved tissue plasminogen activator gene enhancer element indicates that the protein product of this gene is useful for the study, treatment and diagnosis of cancers and blood clotting disorders. The protein is useful for the treatment, detection, and/or prevention of metabolic and developmental disorders which 37 include, but are not limited to diabetes, or placental aberrations. The protein is also useful for the treating and ameliorating cardiovascular conditions such as coronary artery disease, atherosclerosis, or arteriosclerosis. Moreover, the protein is useful in the detection, treatment, and/or prevention of vascular conditions, which include, but are not limited to, microvascular disease, vascular leak syndrome, aneurysm, stroke, atherosclerosis, arteriosclerosis, or embolism. Alternatively, the expression within lymphocytic leukemia cells, combined with its homology to tissue plasminogen activator indicates this gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes suggesting a usefulness in the treatment of cancer (e.g. by boosting immune responses). Since the gene is expressed in cells of lymphoid origin, the natural gene product may be involved in immune functions. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immunodeficiency diseases such as AIDS, leukemia, rheumatoid arthritis, granulomatous disease, inflammatory bowel disease, sepsis, acne, neutropenia, neutrophilia, psoriasis, hypersensitivities, such as T-cell mediated cytotoxicity; immune reactions to transplanted organs and tissues, such as host-versus-graft and graft-versus-host diseases, or autoimmunity disorders, " such as autoimmune infertility, lense tissue injury, demyelination, systemic lupus erythematosis, drug induced hemolytic anemia, rheumatoid arthritis, Sjogren's disease, scleroderma and tissues. Furthermore, the protein may represent a secreted factor that influences the differentiation or behavior of other blood cells, or that recruits hematopoietic cells to sites of injury (i.e. through modulating integrin function). In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:30 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1069 of SEQ ID NO:30, b is an integer of 15 38 to 1083, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:30, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 21 The gene encoding the disclosed cDNA is believed to reside on chromosome 12. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 12. This gene is expressed primarily in fetal liver, fetal spleen and infant brain and to a lesser extent in human epididymus tissue. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, developmental, hematopoietic, immune, CNS, and/or reproductive disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the reproductive, developmental, and central nervous systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., developmental, hematopoietic, immune, CNS, reproductive, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, amniotic fluid, urine, bile, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ED NO:68 as residues: Pro-29 to Pro-35. The tissue distribution in fetal liver, fetal spleen and infant brain indicates that the protein product of this gene is useful for the study, diagnosis and treatment of reproductive, developmental, and CNS disorders. Moreover, this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, developmental tissues rely on decisions involving cell differentiation and/or apoptosis in pattern formation. Dysregulation of apoptosis can result in inappropriate suppression of cell death, as occurs in the development of some cancers, or in failure to control the extent of cell death, as is believed to occur in acquired 39 immunodeficiency and certain neurodegenerative disorders, such as spinal muscular atrophy (SMA). Therefore, the polynucleotides and polypeptides of the present invention are useful in treating, detecting, and/or preventing said disorders and conditions, in addition to other types of degenerative conditions. Thus this protein may modulate apoptosis or tissue differentiation and is useful in the detection, treatment, and/or prevention of degenerative or proliferative conditions and diseases. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:31 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1566 of SEQ ID NO:31, b is an integer of 15 to 1580, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:31, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 22 The translation product of this gene shares sequence homology with human beta-casein which is thought to be important as a milk component. This sequence encodes a homolog of the human milk protein, beta-casein. This sequence can be used in the production of recombinant human beta- casein for use as a constituent of infant formulae. Beta-casein is a phosphorylated protein which is present in milk of several species including humans in which it is the major casein subunit. This protein is believed to enhance calcium absorption by chelating calcium to its phosphorylated residues and thereby keeping it in an adsorbable form. Human beta- casein is easily digestible by newborn infants and the digestive products have been found to play an important part in calcium uptake, and thus in the mineralisation of the skeleton. A digestion product of human beta-casein has been found to have opiod activity and may be involved in the sleeping patterns of breast-fed infants. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: KDTCTRMXIAALFTIAKIWNQPKX (SEQ ID NO: 120), RHM 40 HTYNYCGTIHNSKDLEPTQM XDXIKKMWHLYTTKYYAAIKKD (SEQ ID NO:121), RKCGTYIPRNTMQP (SEQ ID NO: 122), and/or KRTEFMSFXGTWM KLEAΠLSKLTQEEKTKHLMFSLISGS (SEQ ID NO: 123). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in adult heart. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, reproductive and/or vascular disorders and diseases, particularly deficiency in milk production, atherosclerosis, or coronary artery disease. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the reproductive system and mammary glands, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., reproductive, vascular, and cancerous and wounded tissues) or bodily fluids (e.g., serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The homology to human beta-casein indicates that the protein product of this gene is useful as a constituent of infant formulae. Moreover, the protein is useful for the detection, treatment, and/or prevention of aberrant mammary gland function and diseases, in addition to a possible use in the developmental of novel protein expression for the isolation of heterologous proteins using the beta-casein enhancer, promoter, and encoding nucleotide sequences. Alternatively, the expression in adult heart indicates the protein is useful in the detection, treatment, and/or prevention of a variety of vascular disorders and conditions, which include, but are not limited to miscrovascular disease, vascular leak syndrome, aneurysm, stroke, embolism, thrombosis, and/or atherosclerosis. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:32 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more 41 polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 782 of SEQ ID NO:32, b is an integer of 15 to 796, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:32, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 23 The translation product of this gene shares sequence homology with a rat protein, dendrin, which is distributed in the dendrites of neurons of the forebrain. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: PKSDTSPASSR (SEQ LD NO: 124), PKSDTSPASSRLCWD (SEQ LD NO: 125), YVPSFLPKATGSIPSRKGGVGSEKPEVPLQTYKEIVHCCEEQVLTL ATEQTYAVEGETPINRLSLLLSGRVRVSQDGQFLHYIFPYQFMDSPEWESLQP SEEGVFQVTLTAETSCS YISWPRKSLHLLLTKERYISCLFS ALLGYDISEKLYT LNDKLFAKFGLRFDIRLPSLYHVLGPTAADAGPESEKGDEEVCEPAVSPPQATP TSLQQTPPCSTPPATTNFPAPPTRARLSRPDSGLLASRIPLQSYSQVISRGQAP LAPTHTPEL (SEQ ID NO: 126), ATGSIPSRKGGVGSEKPEVPL (SEQ ID NO: 127), IVHCCEEQVLTLATEQTYAVEGETP (SEQ ID NO: 128), QDGQFLHYIFPYQFM DSPEWESL (SEQ LD NO: 129), TLTAETSCSYISWPRKSLHLLLT (SEQ ID NO: 130), DISEKLYTLNDKLFAKFGLRFDIRL (SEQ ID NO: 131), SLYHVLGPTA ADAGPESEKGDEEVCE (SEQ ID NO: 132), and/or TTNFPAPPTRARLSRPDSGILA SRIPLQ (SEQ ID NO: 133). Polynucleotides encoding these polypeptides are also encompassed by the invention.The gene encoding the disclosed cDNA is believed to reside on chromosome 3. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 3. This gene is expressed primarily in the heart and to a lesser extent, in tonsil. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, cardiovascular disorders and conditions, particularly congestive heart failure. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the vascular and neural systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., cardiovascular, vascular, immune, hematopoietic, and cancerous and wounded tissues) or bodily fluids 42 (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:70 as residues: Met-1 to Ser-7, Asp-41 to Met-48, Pro-61 to Ser-67, Pro-121 to Trp- 130, His- 161 to Lys-181. The homology to dendrin indicates that the protein product of this gene is useful for the detection, treatment, and/or prevention of neuronal diseases such as memory loss. Moreover, polynucleotides and polypeptides corresponding to this gene are useful for the detection, treatment, and/or prevention of neurodegenerative disease states, behavioral disorders, or inflammatory conditions which include, but are not limited to Alzheimer's Disease, Parkinson's Disease, Huntington's Disease, Tourette Syndrome, meningitis, encephalitis, demyelinating diseases, peripheral neuropathies, neoplasia, trauma, congenital malformations, spinal cord injuries, ischemia and infarction, aneurysms, hemorrhages, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, depression, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, elevated expression of this gene product in regions of the brain indicates it plays a role in normal neural function. Potentially, this gene product is involved in synapse formation, neurotransmission, learning, cognition, homeostasis, or neuronal differentiation or survival. Alternatively, the expression in heart tissue indicates the protein is useful in the detection, treatment, and/or prevention of a variety of vascular disorders and conditions, which include, but are not limited to miscrovascular disease, vascular leak syndrome, aneurysm, stroke, embolism, thrombosis, coronary artery disease, arteriosclerosis, and/or atherosclerosis. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:33 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1242 of SEQ ID NO:33, b is an integer of 15 43 to 1256, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:33, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 24 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: YFSHGICSHA (SEQ ID NO: 134). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in peripheral mononuclear cells, and to a lesser extent in other white blood cells such as neutrophils and lymphocytes from lymphomas. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, hematopoietic or immune disorders and conditions, particularly leukemia and lymphomas. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., hematopoietic, immune, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:71 as residues: Leu-41 to Pro-48. The tissue distribution in blood cells indicates that the protein product of this gene is useful for diagnosis and treatment of blood diseases such as leukemia and lymphomas. Moreover, the tissue distribution indicates polynucleotides and polypeptides corresponding to this gene are useful for the treatment and diagnosis of hematopoietic related disorders such as anemia, pancytopenia, leukopenia, thrombocytopenia or leukemia since stromal cells are important in the production of cells of hematopoietic lineages. The uses include bone marrow cell ex- vivo culture, bone marrow transplantation, bone marrow reconstitution, radiotherapy or chemotherapy of neoplasia. The gene product may also be involved in lymphopoiesis, therefore, it can be used in immune disorders such as infection, inflammation, allergy, 44 immunodeficiency etc. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:34 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1050 of SEQ ID NO:34, b is an integer of 15 to 1064, where both a and b correspond to the positions of nucleotide residues shown in SEQ ED NO:34, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 25 The translation product of this gene was shown to have homology to a conserved ubiquitin thiolesterase (deubiquitinating enzyme) (See Genbank Accession No. splQ09738IUBPA_SCHPO) which is thought to be important in protein metabolism, processing, and/or regulation. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: NSEDISQTRQELGLCISQ RCLSDRKKSRRSGVWVRACT MQFMKHVFPRLISPRRP (SEQ ID NO: 135), PTRHFCGTSSCLTGTAVRCRAP APVWSVRCPHCFRSSDAWVDPGIPDRYLQ AYLL (SEQ ID NO: 136), GEAMDA EXAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCICHVC GVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYI YDKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNC TIGLRGLINLGNTCFMNCLVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMS SLFQEFGRVGRPGNSGPVPAGVPSIV SPE (SEQ ID NO: 137), VAPPGCSHLGS FKVDNWKQNLRAI (SEQ ID NO: 138), TAEARKRKAKSCICHVCGVHLNR (SEQ ID NO: 139), FTKKHIHEHAKAKRHN LALDLMY (SEQ LD NO: 140), YDKDMEIIA KEEQRKAWKMQG (SEQ LD NO: 141), ELLKHNPKRRKITSNCTIGLRGLINLGN (SEQ ID NO: 142), GNTCFMNCIVQALTHTPLLRDFFLSD (SEQ ID NO: 143), 45 and/or EFGRVGRPGNSGPVPAGVPS (SEQ ID NO: 144). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in L428 cells, and to a lesser extent, in osteoblasts. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, skeletal diseases and disorders, particularly osteosarcoma or other bone diseases. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the skeletal system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., skeletal, metabolic, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. — The tissue distribution in osteoblasts indicates that the protein product of this gene is useful for diagnosis and treatment of bone disorders such as osteoporosis. Moreover, the homology to the ubiquitin thiolesterase indicates the protein can be used to arrest proliferation of haematopoietic cells for treating or preventing e.g. cancer especially leukaemias or lymphomas (in addition to other proliferative conditions in other cells or cell types). The protein can also be used to stimulate haematopoietic cell proliferation e.g. to produce blood cells for replacing blood cell depletion due to disease or condition e.g., immune suppression from AIDS or therapy such as chemotherapy or dialysis. The protein may also be used to suppress the immune system e.g. during organ or cell transplantation. The polynucleotides of the present invention can be used to transform cells for screening agents which inhibit DUB enzyme activity. Furthermore, the protein is useful for the detection and treatment of disorders and conditions affecting the skeletal system, in particular bone cancer, as well as, disorders afflicting connective tissues (e.g. arthritis, trauma, tendonitis, chrondomalacia and inflammation), such as in the diagnosis or treatment of various autoimmune disorders such as rheumatoid arthritis, lupus, scleroderma, and dermatomyositis as well as dwarfism, spinal deformation, and specific joint abnormalities as well as chondrodysplasias (i.e. spondyloepiphyseal dysplasia congenita, familial osteoarthritis, Atelosteogenesis type π, metaphyseal 46 chondrodysplasia type Schmid). Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO: 35 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 741 of SEQ ID NO:35, b is an integer of 15 to 755, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:35, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 26 This gene is expressed primarily in cells from Hodgkin's lymphoma. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, hematopoietic or immune diseases and conditions, particularly Hodgkin's lymphoma. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., hematopoietic, immune, and cancerous and wounded tissues) or bodily fluids (e.g., serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:73 as residues: Arg-47 to His-52, Gly-64 to Leu-71. The tissue distribution in Hodgkin's lymphoma indicates that the protein product of this gene is useful for diagnosis and treatment of hematopoietic and immune disorders and conditions. Moreover, polynucleotides and polypeptides corresponding 47 to this gene are useful for the treatment and diagnosis of hematopoietic related disorders such as anemia, pancytopenia, leukopenia, thrombocytopenia or leukemia since stromal cells are important in the production of cells of hematopoietic lineages. The uses include bone marrow cell ex- vivo culture, bone marrow transplantation, bone marrow reconstitution, radiotherapy or chemotherapy of neoplasia. The gene product may also be involved in lymphopoiesis, therefore, it can be used in immune disorders such as infection, inflammation, allergy, immunodeficiency etc. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:36 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 590 of SEQ ID NO:36, b is an integer of 15 to 604, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:36, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 27 The translation product of this gene shares sequence homology with 'AP2' tumor-specific DNA, which is thought to be important in detecting insertions or deletions in DNA sequences in tumor cells. Such mutations are markers of cancer and can be used in the diagnosis of cancer, esp. colorectal, stomach or pancreatic tumors. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: AFPWPTS (SEQ ID NO: 145). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in breast lymph nodes from a breast cancer patient, and to a lesser extent in adrenal gland and tonsils. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a 48 biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, reproductive and/or immune diseases and disorders, particularly cancers, such as breast cancer, colorectal cancer, and pancreatic cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the endocrine and digestive system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., reproductive, immune, and cancerous and wounded tissues) or bodily fluids (e.g., serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:74 as residues: Ile-25 to Trp-30. The tissue distribution breast lymph nodes, combined with the homology to 'AP2 tumor-specific DNA sequence' indicates that the protein product or the DNA sequence of this gene is useful for detecting insertions or deletions in DNA sequences in tumor cells. Such mutations are markers of cancer and can be used in the diagnosis of cancer, esp. colorectal, stomach and pancreatic tumors. Expression within cellular sources marked by proliferating cells indicates this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, developmental tissues rely on decisions involving cell differentiation and/or apoptosis in pattern formation. Dysregulation of apoptosis can result in inappropriate suppression of cell death, as occurs in the development of some cancers, or in failure to control the extent of cell death, as is believed to occur in acquired immunodeficiency and certain neurodegenerative disorders, such as spinal muscular atrophy (SMA). Therefore, the polynucleotides and polypeptides of the present invention are useful in treating, detecting, and/or preventing said disorders and conditions, in addition to other types of degenerative conditions. Thus this protein may modulate apoptosis or tissue differentiation and is useful in the detection, treatment, and/or prevention of degenerative or proliferative conditions and diseases, particularly those of the immune and/or hematopoietic systems. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ 49 ID NO:37 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 798 of SEQ ID NO:37, b is an integer of 15 to 812, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:37, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 28 The translation product of this gene was shown to have homology to a conserved reverse transcriptase homolog which may implicate this protein as playing a role in various DNA processing and modulatory activities (See Genbank Accession No.bbsl80120). In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: ESNFFYPYDSQLALLSSVTCSAS (SEQ ID NO: 146), KLKMF AFYVQVLNQSKSLFVYSRNLIFHHMIVSWPSFLQLPAVHQCHQSSVHICGVSGL FPSSNYQCL SLCQNHTVLIITTL (SEQ ID NO: 147), SILNVIPNLSKQSFEEFDRLI LKYMQKSKSKRLA KLLLSNKKTCPTKY (SEQ ID NO: 148), LPQILRWLKYHQS VWGKQTPNTLHYLTLDLIQEFTP (SEQ ID NO: 149), and/or IFVYSRNLIFFIHMIV SWPSFLQLPAVHQCHQS (SEQ ID NO: 150). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in B-cell lymphoma. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune or hematopoietic disorders and conditions, particularly B-cell lymphoma. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, hematopoietic, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene 50 expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in B-cell lymphoma tissue indicates that the protein product of this gene is useful for diagnosis and treatment of immune or hematopoietic disorders. Moreover, the expression of this gene product indicates a role in regulating the proliferation; survival; differentiation; and/or activation of hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes suggesting a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the natural gene product may be involved in immune functions. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immunodeficiency diseases such as AIDS, leukemia, rheumatoid arthritis, granulomatous disease, inflammatory bowel disease, sepsis, acne, neutropenia, neutrophilia, psoriasis, hypersensitivities, such as T-cell mediated cytotoxicity; immune reactions to transplanted organs and tissues, such as host-versus-graft and graft-versus-host diseases, or autoimmunity disorders, such as autoimmune infertility, lense tissue injury, demyelination, systemic lupus erythematosis, drug induced hemolytic anemia, rheumatoid arthritis, Sjogren's disease, scleroderma and tissues. Furthermore, the protein may represent a secreted factor that influences the differentiation or behavior of other blood cells, or that recruits hematopoietic cells to sites of injury. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. In addition, the homology to a reverse transcriptase protein indicates the protein may play a vital role in DNA metabolism, processing, and/or regulatory roles which would have utility in treating or detecting developmental and proliferative disorders and conditions. The protein is useful in, but not limited to, the inhibition or enhancement of apoptosis, transcription, translation, trafficking, and other cellular functions. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:38 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more 51 polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1135 of SEQ ID NO:38, b is an integer of 15 to 1149, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:38, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 29 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: PTGNDLVYVFPCLLSVFSRMEEPSVFCLFFPLSILISSASRT FPGTQQVFSIVHGVTDVSAKKVQSQGRMTSTGLDFNLLPAWFPSPTSLQPTE DLFQTGSLSRSFFCSKAFSSSPLSPGGSPNALTSVKEHLVSPAFLASHSCTAE SFPRVDVIHAVPIAWIPAPLHPIQLINSWFFFFFFFF (SEQ LD NO: 151), DLVY VFPCLLSVFSRMEEPSVFCL (SEQ LD NO: 152), ISSASRTFPGTQQVFSIVH GVTDV (SEQ ED NO: 153), FNLLPAWFPSPTSLQPTEDL (SEQ ID NO: 154), FCSKAFSSSPLSPGGSPNALTSVKE (SEQ ID NO: 155), and/or TAESFPRVDVIHA VPIAWLPAPL (SEQ ED NO: 156). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in B-cell lymphoma. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune or hematopoietic disorders, particularly B-cell lymphoma. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, hematopoietic, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:76 as residues: Glu-16 to Arg-21. The tissue distribution in B-cell lymphoma tissue indicates that the protein product of this gene is useful for diagnosis and treatment of immune or hematopoietic 52 disorders and conditions. Moreover, the expression of this gene product indicates a role in regulating the proliferation; survival; differentiation; and/or activation of hematopoietic cell lineages, including blood stem cells. This gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes suggesting a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the natural gene product may be involved in immune functions. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immunodeficiency diseases such as AIDS, leukemia, rheumatoid arthritis, granulomatous disease, inflammatory bowel disease, sepsis, acne, neutropenia, neutrophilia, psoriasis, hypersensitivities, such as T-cell mediated cytotoxicity; immune reactions to transplanted organs and tissues, such as host-versus-graft and graft-versus-host diseases, or autoimmunity disorders, such as autoimmune infertility, lense tissue injury, demyelination, systemic lupus erythematosis, drug induced hemolytic anemia, rheumatoid arthritis, Sjogren's disease, scleroderma and tissues. Furthermore, the protein may represent a secreted factor that influences the differentiation or behavior of other blood cells, or that recruits hematopoietic cells to sites of injury. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:39 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1073 of SEQ ID NO:39, b is an integer of 15 to 1087, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 39, and where b is greater than or equal to a + 14. 53 FEATURES OF PROTEIN ENCODED BY GENE NO: 30 The translation product of this gene was shown to have homology to histone family of proteins. Based on the sequence similarity, the translation product of this gene is expected to share biological activities with histone proteins, in addition to other proteins having DNA binding activity. Such activities are known in the art and described elsewhere herein. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: FSFLKPLCAPRAPWLWLPPSSKSR VHVGPGDFRS (SEQ ID NO: 157), VCGTGGLEPNLAWVRVDNGSFPSSSPS VPLEHPGCGCLLHPRAESM LGQETSDPCPGAASGFVFPQWAGLGLLVHLYPSLSY AALACCVSGLYSLPFT QALGNQPSFXQERQRRSMPLLWAS (SEQ ID NO: 158), HAGRKTVK (SEQ ID NO: 159), SFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVK PEDLELLMRRQGLVTDQ (SEQ ID NO: 160), PMERKALEMVEKCLDKYFQ (SEQ ID NO: 161), EVFAAHAGRKTVKPEDLELLMR (SEQ ID NO: 162), SFPSSSPSVP LEHPGCGCLLHPRAESMLGQE (SEQ ID NO: 163), and/or YPSLSYAALACCVS GLYSLPFTQALGN (SEQ ID NO: 164). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is " believed to reside on chromosome 16. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 16. This gene is expressed primarily in epididymus and, to a lesser extent, in placenta and fetal liver/spleen . Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, reproductive, hematopoietic, and/or immune disorders and conditions, particularly male infertility. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the reproductive system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., reproductive, hematopoietic, immune, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, seminal fluid, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. 54 Preferred epitopes include those comprising a sequence shown in SEQ ID NO:77 as residues: His-44 to Pro-50, Glu-90 to Glu-96, Gln-111 to Glu-117, Ser-143 to Gly-151, Ala- 154 to Leu- 166, Pro- 199 to Ala-216, Gly-264 to Asp-272. The tissue distribution in epididimus and placental tissue indicates that the protein product of this gene is useful for diagnosis and treatment of various reproductive disorders and conditions which include, but are not limited to infertility. Moreover, the protein is useful for the treatment and diagnosis of conditions concerning proper testicular function (e.g. endocrine function, sperm maturation), as well as cancer. Therefore, this gene product is useful in the treatment of impotence, and could be useful as a contraceptive, either directly or indirectly. Considering the homology to histone proteins, this gene product is also useful in assays designed to identify binding agents, as such agents (antagonists) are useful as male contraceptive agents. Similarly, the protein is believed to be useful in the treatment and/or diagnosis of testicular cancer. The testes are also a site of active gene expression of transcripts that may be expressed, particularly at low levels, in other tissues of the body. Therefore, this gene product may be expressed in other specific tissues or organs where it may play related functional roles in other processes, such as hematopoiesis, inflammation, bone formation, and kidney function, to name a few possible target indications. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:40 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1262 of SEQ ID NO:40, b is an integer of 15 to 1276, where both a and b correspond to the positions of nucleotide residues shown in SEQ LD NO:40, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 31 The translation product of this gene was shown to have homology to serine/threonine phosphatase proteins. Based on the sequence similarity, the translation product of this gene is expected to share biological activities with proteins involved in 55 signal transduction and/or the cell cycle. Such activities are known in the art and described elsewhere herein. In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: APGGVNSEGRGQHLPPPXL AVCLKLHL (SEQ ID NO: 165). Polynucleotides encoding these polypeptides are also encompassed by the invention.The gene encoding the disclosed cDNA is believed to reside on chromosome 9. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 9. This gene is expressed primarily in breast and infant brain and, to a lesser extent, in neutrophils, fetal spleen, and activated monocytes. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, reproductive, developmental, immune, and/or hematopoietic disorders, particularly breast cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune and metabolic systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., reproductive, developmental, immune, hematopoietic, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, breast milk, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:78 as residues: Pro-37 to Ala-42, Leu-44 to Cys-53, Glu-57 to Leu-65, Pro-79 to Pro-85. The tissue distribution in breast tissue and neutrophils indicates that the protein product of this gene is useful for diagnosis and treatment of certain cancers including those of reproductive and immune cell origin. Similarly, polynucleotides and polypeptides corresponding to this gene are useful for the treatment and diagnosis of hematopoietic related disorders such as anemia, pancytopenia, leukopenia, thrombocytopenia or leukemia since stromal cells are important in the production of cells of hematopoietic lineages. The uses include bone marrow cell ex- vivo culture, bone marrow transplantation, bone marrow reconstitution, radiotherapy or chemotherapy of neoplasia. The gene product may also be involved in lymphopoiesis, therefore, it can be used in immune disorders such as infection, inflammation, allergy, 56 immunodeficiency etc. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Moreover, the expression within various fetal and infant tissues indicates this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, developmental tissues rely on decisions involving cell differentiation and/or apoptosis in pattern formation. Dysregulation of apoptosis can result in inappropriate suppression of cell death, as occurs in the development of some cancers, or in failure to control the extent of cell death, as is believed to occur in acquired immunodeficiency and certain neurodegenerative disorders, such as spinal muscular atrophy (SMA). Therefore, the polynucleotides and polypeptides of the present invention are useful in treating, detecting, and or preventing said disorders and conditions, in addition to other types of degenerative conditions. Thus this protein may modulate apoptosis or tissue differentiation and is useful in the detection, treatment, and/or prevention of degenerative or proliferative conditions and diseases. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:41 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2069 of SEQ ID NO:41, b is an integer of 15 to 2083, where both a and b correspond to the positions of nucleotide residues shown in SEQ LD NO:41, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 32 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: NSAEPAWVPVCARGGGAGCGRRRGRRFCAAGAVPAAE RGGENGS (SEQ ID NO: 166), SLVPALKEVVVLWRRQMVLYLVWAFIPESWLN SLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNY AKNQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN (SEQ ID NO: 167), 57 MVLYLVWAFIPESWLNSLGLTYWPQKYW (SEQ ID NO: 168), YWAVALPVYLLI AIVIGYVLLFGIN (SEQ ID NO: 169), and/or QQQKKYQEEAIPALRDISISEV (SEQ ID NO: 170). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in fetal liver/spleen. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune, hematopoietic, and/or developmental disorders and conditions, particularly haemopoiesis, leukemias, and lymphomas. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the hematopoietic system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, hematopoietic, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:79 as residues: Asn-28 to Pro-34. The tissue distribution in feted liver/spleen indicates that the protein product of this gene is useful for diagnosis and treatment of disorders involving haemopoiesis. Moreover, polynucleotides and polypeptides corresponding to this gene are useful for the treatment and diagnosis of hematopoietic related disorders such as anemia, pancytopenia, leukopenia, thrombocytopenia or leukemia since stromal cells are important in the production of cells of hematopoietic lineages. The uses include bone marrow cell ex- vivo culture, bone marrow transplantation, bone marrow reconstitution, radiotherapy or chemotherapy of neoplasia. The gene product may also be involved in lymphopoiesis, therefore, it can be used in immune disorders such as infection, inflammation, allergy, immunodeficiency etc. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Moreover, expression within fetal tissue indicates this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment 58 of cancer and other proliferative disorders. Similarly, developmental tissues rely on decisions involving cell differentiation and/or apoptosis in pattern formation. Dysregulation of apoptosis can result in inappropriate suppression of cell death, as occurs in the development of some cancers, or in failure to control the extent of cell death, as is believed to occur in acquired immunodeficiency and certain neurodegenerative disorders, such as spinal muscular atrophy (SMA). Therefore, the polynucleotides and polypeptides of the present invention are useful in treating, detecting, and/or preventing said disorders and conditions, in addition to other types of degenerative conditions. Thus this protein may modulate apoptosis or tissue differentiation and is useful in the detection, treatment, and/or prevention of degenerative or proliferative conditions and diseases. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:42 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1002 of SEQ ID NO:42, b is an integer of 15 to 1016, where both a and b correspond to the positions of nucleotide residues shown in SEQ LD NO:42, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 33 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: LSPRLFDAGILLWGASVNVTIWEVRXAQSSAS (SEQ ID NO: 171). Polynucleotides encoding these polypeptides are also encompassed by the invention. The gene encoding the disclosed cDNA is believed to reside on chromosome 10. Accordingly, polynucleotides related to this invention are useful as a marker in linkage analysis for chromosome 10. This gene is expressed primarily in Jurkat T-cell Gl phase and to a lesser extent in 12 Week Old Early Stage Human. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a 59 biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, immune, hematopoietic, and/or developmental diseases and conditions. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the immune system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., immune, hematopoietic, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, amniotic fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in Jurkat cells indicates that the protein product of this gene is useful for diagnosis and treatment of certain immune disorders, especially involving Jurkat cells. Moreover, this gene product may be involved in the regulation of cytokine production, antigen presentation, or other processes suggesting a usefulness in the treatment of cancer (e.g. by boosting immune responses). Moreover, since the gene is expressed in cells of lymphoid origin, the natural gene product may be involved in immune functions. Therefore it may be also used as an agent for immunological disorders including arthritis, asthma, immunodeficiency diseases such as AIDS, leukemia, rheumatoid arthritis, granulomatous disease, inflammatory bowel disease, sepsis, acne, neutropenia, neutrophilia, psoriasis, hypersensitivities, such as T-cell mediated cytotoxicity; immune reactions to transplanted organs and tissues, such as host-versus-graft and graft-versus-host diseases, or autoimmunity disorders, such as autoimmune infertility, lense tissue injury, demyelination, systemic lupus erythematosis, drug induced hemolytic anemia, rheumatoid arthritis, Sjogren's disease, scleroderma and tissues. The protein may represent a secreted factor that influences the differentiation or behavior of other blood cells, or that recruits hematopoietic cells to sites of injury. In addition, this gene product may have commercial utility in the expansion of stem cells and committed progenitors of various blood lineages, and in the differentiation and/or proliferation of various cell types. Furthermore, expression within embryonic tissue and other cellular sources marked by proliferating cells indicates this protein may play a role in the regulation of cellular division, and may show utility in the diagnosis and treatment of cancer and other proliferative disorders. Similarly, developmental tissues rely on decisions involving cell differentiation and/or apoptosis in pattern formation. Dysregulation of 60 apoptosis can result in inappropriate suppression of cell death, as occurs in the development of some cancers, or in failure to control the extent of cell death, as is believed to occur in acquired immunodeficiency and certain neurodegenerative disorders, such as spinal muscular atrophy (SMA). Therefore, the polynucleotides and polypeptides of the present invention are useful in treating, detecting, and/or preventing said disorders and conditions, in addition to other types of degenerative conditions. Thus this protein may modulate apoptosis or tissue differentiation and is useful in the detection, treatment, and/or prevention of degenerative or proliferative conditions and diseases. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ LD NO:43 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 2183 of SEQ ID NO:43, b is an integer of 15 to 2197, where both a and b correspond to the positions of nucleotide residues shown in SEQ ED NO:43, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 34 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: NLTSDPRPLALPPPCGDFIKVTSFSPGLETHT (SEQ ID NO: 172), EQQRLRDRETQTGXDSRAKTQRGEDGESERGRWRLREGEDGDSERE EDGDSERWRLRSMESQRGEDGHSGGWRVRRMETHRKGRMESQERLETGEGI ETQRGEDGDSEGGRWRLKEDGNPGERRTEMRQRLGEAG (SEQ ID NO: 173), GHGVAGXCLPQPLLPPSPPDYDERSHLHDTFTQMTHALQELAAAQGSFEVAFP DAAEKMKKVFTQLKEAQACffPCEGLQEFARRFLCSGCYSRVCDLPLDCPVQD VLNTRGDQAMFSCLVNFQLPKEEITYSWKFAGGGLRTQDLSYFRDMPRAEG YLARIRPAQLTHRGTFSCVIKQDQRPLARLYFFLNVTGRPRGRRQSCRPRSGK CCAGRRGMPS (SEQ ID NO: 174), and/or GDHPHFISVLGKVQREGRRGPEGQA EGQTERNSQRRKAQRP (SEQ ID NO: 175). Polynucleotides encoding these polypeptides are also encompassed by the invention. 61 This gene is expressed primarily in uterine cancer and, to a lesser extent, in macrophage and adult testis. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, reproductive diseases and conditions, particularly uterine and testicular cancer. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the reproductive and immune systems, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., reproductive, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, seminal fluid, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:81 as residues: Ser-54 to Arg-64, Lys-70 to Thr-77, Gly-88 to Ser-96. The tissue distribution in uterine and testis tissue indicates that the protein product of this gene is useful for diagnosis and treatment of certain cancers, including uterine cancer. Moreover, the tissue distribution in testis tissue indicates that polynucleotides and polypeptides corresponding to this gene are useful for the treatment and diagnosis of conditions concerning proper testicular function (e.g. endocrine function, sperm maturation), as well as cancer. Therefore, this gene product is useful in the treatment of male infertility and/or impotence. This gene product is also useful in assays designed to identify binding agents, as such agents (antagonists) are useful as male contraceptive agents. Similarly, the protein is believed to be useful in the treatment and/or diagnosis of testicular cancer. The testes are also a site of active gene expression of transcripts that may be expressed, particularly at low levels, in other tissues of the body. Therefore, this gene product may be expressed in other specific tissues or organs where it may play related functional roles in other processes, such as hematopoiesis, inflammation, bone formation, and kidney function, to name a few possible target indications. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ 62 ID NO:44 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1985 of SEQ ID NO:44, b is an integer of 15 to 1999, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:44, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 35 In specific embodiments, polypeptides of the invention comprise the following amino acid sequence: MLVYQNQAQFSSN (SEQ ID NO: 176). Polynucleotides encoding these polypeptides are also encompassed by the invention. This gene is expressed primarily in the cerebellum. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, neurodegenerative disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the central nervous system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the expression level in healthy tissue or bodily fluid from an individual not having the disorder. The tissue distribution in cerebellum indicates that the protein product of this gene is useful for the diagnosis and treatment of neurodegenerative disorders. Moreover, polynucleotides and polypeptides corresponding to this gene are useful for the detection, treatment, and/or prevention of neurodegenerative disease states, behavioral disorders, or inflammatory conditions which include, but are not limited to Alzheimer's Disease, Parkinson's Disease, Huntington's Disease, Tourette Syndrome, meningitis, encephalitis, demyelinating diseases, peripheral neuropathies, neoplasia, trauma, congenital malformations, spinal cord injuries, ischemia and infarction, 63 aneurysms, hemorrhages, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, depression, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, elevated expression of this gene product in regions of the brain indicates it plays a role in normal neural function. Potentially, this gene product is involved in synapse formation, neurotransmission, learning, cognition, homeostasis, or neuronal differentiation or survival. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ED NO:45 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1505 of SEQ ED NO:45, b is an integer of 15 to 1519, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:45, and where b is greater than or equal to a + 14. FEATURES OF PROTEIN ENCODED BY GENE NO: 36 This gene is expressed primarily in cerebellum and whole brain and to a lesser extent in pineal gland, fetal liver/spleen, and ovary. Therefore, polynucleotides and polypeptides of the invention are useful as reagents for differential identification of the tissue(s) or cell type(s) present in a biological sample and for diagnosis of diseases and conditions, which include, but are not limited to, neurodegenerative diseases and/or disorders. Similarly, polypeptides and antibodies directed to these polypeptides are useful in providing immunological probes for differential identification of the tissue(s) or cell type(s). For a number of disorders of the above tissues or cells, particularly of the central nervous system, expression of this gene at significantly higher or lower levels may be routinely detected in certain tissues or cell types (e.g., neural, endocrine, developmental, and cancerous and wounded tissues) or bodily fluids (e.g., lymph, serum, plasma, amniotic fluid, urine, synovial fluid and spinal fluid) or another tissue or cell sample taken from an individual having such a disorder, relative to the standard gene expression level, i.e., the 64 expression level in healthy tissue or bodily fluid from an individual not having the disorder. Preferred epitopes include those comprising a sequence shown in SEQ ID NO:83 as residues: His-3 to Phe-11, Pro-35 to Arg-40. The tissue distribution in cerebellum and whole brain indicates that the protein product of this gene is useful for the diagnosis and treatment of neurodegenerative disorders involving the cerebellum or other brain regions. Moreover, polynucleotides and polypeptides corresponding to this gene are useful for the detection, treatment, and/or prevention of neurodegenerative disease states, behavioral disorders, or inflammatory conditions which include, but are not limited to Alzheimer's Disease, Parkinson's Disease, Huntington's Disease, Tourette Syndrome, meningitis, encephalitis, demyelinating diseases, peripheral neuropathies, neoplasia, trauma, congenital malformations, spinal cord injuries, ischemia and infarction, aneurysms, hemorrhages, schizophrenia, mania, dementia, paranoia, obsessive compulsive disorder, depression, panic disorder, learning disabilities, ALS, psychoses, autism, and altered behaviors, including disorders in feeding, sleep patterns, balance, and perception. In addition, elevated expression of this gene product in regions of the brain indicates it plays a role in normal neural function. Potentially, this gene product is involved in synapse formation, neurotransmission, learning, cognition, homeostasis, or neuronal differentiation or survival. Protein, as well as, antibodies directed against the protein may show utility as a tumor marker and/or immunotherapy targets for the above listed tissues. Many polynucleotide sequences, such as EST sequences, are publicly available and accessible through sequence databases. Some of these sequences are related to SEQ ID NO:46 and may have been publicly available prior to conception of the present invention. Preferably, such related polynucleotides are specifically excluded from the scope of the present invention. To list every related sequence is cumbersome. Accordingly, preferably excluded from the present invention are one or more polynucleotides comprising a nucleotide sequence described by the general formula of a-b, where a is any integer between 1 to 1175 of SEQ ID NO:46, b is an integer of 15 to 1189, where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO:46, and where b is greater than or equal to a + 14. 5' NT * m- o\ NT 5' NT 3' NT of AA First Last m ATCC SEQ of of 5' NT First SEQ AA AA First AA Last Deposit ED Total Clone Clone of AA of ED of of of AA Gene cDNA Nr and NO: NT Seq. Seq. Start Signal NO: Sig Sig Secreted of No. Clone ID Date Vector X Seq. Codon Pep Y Pep Pep Portion ORF 1 HCE1Q30 209626 Uni-ZAP XR 11 1441 1 1441 137 137 48 30 31 55 02/12/98 2 HAGBP70 209626 Uni-ZAP XR 12 2160 163 2142 360 360 49 34 35 40 02/12/98 3 HBCAY27 209626 Uni-ZAP XR 13 1202 447 1202 580 580 50 18 19 93 < 1 02/12/98 4 HCACU58 209626 Uni-ZAP XR 14 1554 1 1554 137 137 51 30 31 83 02/12/98 5 HCWLD74 209626 ZAP Express 15 1540 1 1540 138 138 52 21 22 65 02/12/98 6 HDPFP29 209626 pCMVSport 16 1057 1 1057 293 293 53 30 31 52 02/12/98 3.0 7 HDPPH47 209626 pCMVSport 17 2080 105 2080 116 116 54 35 36 540 o 02/12/98 3.0 1 o m i m β 66 5' NT O VO 0 0 00 CO CO f 3' NT 5' NT o p ^ o oo CO 0 CO CO i AA F Fi 5ff' NTC ATC ttrssr o o CO VO in O VO CN CO co O CM <N CM f f AA f C ll T l C i D tt ooo oneoneao p o s e d S il S S S S NT d A NDN G t tt e cr eea g nae q e qr an r c ene.. 1 <! « * .SP & VO CM O in O in m J ° 00 i P O P C d Sl D C I D N t t ono r e p nooe q aeone CM CO co o H .. CO CM CM CM • £ Ε < < < ° - 0s0? C &U 696 202 /2/98021 ^ ω Q o ^ in VO 00 O CM ^ M z; in in in in in VO VO VO 626 209 m /802/129 VO VO r- co M CM 5 co CM m 0 - - CM CN 66 2092 i → 02/12/98 VO vo CO CM CM 5 co CM m 0 (N N 66 CV S 2092 M t pp or C co O m oM ON CM VO r-- ON 3002/12/98 . 00 VO VO 0 in CN ON co in 0 <N 66 2092 ■ <fr VO CO - - VO • * - O CM /802/129 O - - CM CM ON c-- co c 9626 20 o m o CM VO as 00 t^ VO VO O CO in m CN /1/98022 0 CN ξ N O in CM C CM CM 66 2092 CN CM ^ w 00 ø o x 00 O CN CO M 02/12/98 Qi Pi Pi Pi Pi X X X X 66 2092 2 CU u cu P, Pu o < < < O < < O N & /802/129 > N N 00 N CU N 00 c 3 CU cu ■ 3 " c " 3 P P P P P CO 00 0 CO σ\ ON z < 0 O >—> U < < PU < cu 00 00 00 t E PU i U P O 00 P 00 ON 0 - CN CO m 5' NT NT 5' NT 3' NT of AA First Last m Os ATCC SEQ of of 5' NT First SEQ AA AA First AA Last m Deposit ED Total Clone Clone of AA of LD of of of AA Gene cDNA Nr and NO: NT Seq. Seq. Start Signal NO: Sig Sig Secreted of No. Clone ID Date Vector X Seq. Codon Pep Y Pep Pep Portion ORF 15 HUSIF44 209626 pSportl 47 2584 1 2584 29 29 84 28 29 132 02/12/98 16 H6EDX46 209626 Uni-ZAP XR 26 718 1 718 128 128 63 20 21 84 02/12/98 17 HABAG37 209626 pSportl 27 654 1 639 97 97 64 31 32 62 02/12/98 VI 18 HACBD91 209626 Uni-ZAP XR 28 1445 1 1445 117 1 17 65 42 43 49 02/12/98 19 HADEH21 209626 pSportl 29 2020 1 2020 61 61 66 25 26 401 02/12/98 20 HAGHD57 209626 Uni-ZAP XR 30 1083 97 1083 402 402 67 24 25 57 02/12/98 21 HAGHR69 209626 Uni-ZAP XR 31 1580 1 1450 1 1 1 1 68 21 22 72 02/12/98 O H 22 HAHDB16 209626 Uni-ZAP XR 32 796 1 796 93 93 69 20 21 50 02/12/98 m 5' NT NT 5' NT 3' NT of AA First Last *-. m Os ATCC SEQ of of 5' NT First SEQ AA AA First AA Last m Deposit ID Total Clone Clone of AA of ID of of of AA Gene cDNA Nr and NO: NT Seq. Seq. Start Signal NO: Sig Sig Secreted of No. Clone ID Date Vector X Seq. Codon Pep Y Pep Pep Portion ORF 23 HAHDR32 209626 Uni-ZAP XR 33 1256 365 1256 435 435 70 1 25 26 181 02/12/98 24 HAJAW93 209626 pCMVSport 34 1064 45 1064 218 218 71 1 30 31 48 02/12/98 3.0 25 HAJBR69 209626 pCMVSport 35 755 755 262 262 72 1 19 20 53 02/12/98 3.0 oo 26 HAMGO32 209626 pCMVSport 36 604 604 119 119 73 1 22 23 74 02/12/98 3.0 27 HATBR65 209626 Uni-ZAP XR 37 812 812 252 252 74 1 16 17 64 02/12/98 28 HBJLD29 209626 Uni-ZAP XR 38 1149 1149 142 142 75 1 29 30 43 02/12/98 29 HBJNB 13 209626 Uni-ZAP XR 39 1087 1087 12 12 76 1 17 18 52 O 02/12/98 H 30 HCE2F54 209626 Uni-ZAP XR 40 1276 19 1256 166 166 77 1 19 20 319 >o 02/12/98 m m° ^o 69 5' NT r- o M O VO f T 5 N 3' N ' T o 33 ° 1 O C θN m Fi AA i 5' N f F T f CC AT ttrsrs o o → r- VO 00 00 co CM CM CM O f ff AA C l C ll T i D tt oo ooneoneo as e p o d S il S S S S NT d NNAD G t tt ee cr e g naa qer e qr an cene.. O CO VO m r- _ 3J $ < o ° 00 Λ 0« CN (N C d - co M co Pi P S D C l I D N t t o r one p oone q aenoeo.. £ < « .≥P & £ < ° 00 O H 62609 2 Slag* oo //980212 ON O CM co r- 00 00 00 00 626 209 VO 00 in m O O CM /9802/12 CM ON in 0 626 209 VO OO in m O O CM CM 0/12/982 ON in 0 ■ <fr VO - • O 662 209 N ON as r- ON ON 00 o © ON CN CN /9802/12 in ON 626 209 02/12/98 co vo r- ON ON oo ON ON 26 O 0 96 20 N 0 o © ON m CM <N 02/12/98 _ f a § x CM O in vo ■ <fr • * Pi Pi Pi oi Pi oi X X X X X X -* O— » cu cu CU cu CU Cu u D < < < < < < N N N > N N N a ■ 3 ■ 3 ' 3 ' 3 ' 3 P P P P P P CN 00 VO vo in 00 CN r- ON VO l υ < pq p Pi 03 O P-] PU > pq p ω O q pq U U u p U U X uq X X X X X CM co in VO co co O CO co co 70 Table 1 summarizes the information corresponding to each "Gene No." described above. The nucleotide sequence identified as "NT SEQ ID NO:X" was assembled from partially homologous ("overlapping") sequences obtained from the "cDNA clone ID" identified in Table 1 and, in some cases, from additional related DNA clones. The overlapping sequences were assembled into a single contiguous sequence of high redundancy (usually three to five overlapping sequences at each nucleotide position), resulting in a final sequence identified as SEQ ID NO:X. The cDNA Clone ID was deposited on the date and given the corresponding deposit number listed in "ATCC Deposit No:Z and Date." Some of the deposits contain multiple different clones corresponding to the same gene. "Vector" refers to the type of vector contained in the cDNA Clone ID. "Total NT Seq." refers to the total number of nucleotides in the contig identified by "Gene No." The deposited clone may contain all or most of these sequences, reflected by the nucleotide position indicated as "5' NT of Clone Seq." and the "3' NT of Clone Seq." of SEQ ID NO:X. The nucleotide position of SEQ ID NO:X of the putative start codon (methionine) is identified as "5' NT of Start Codon." Similarly , the nucleotide position of SEQ LD NO:X of the predicted signal sequence is identified as "5' NT of First AA of Signal Pep." The translated amino acid sequence, beginning with the methionine, is identified as "AA SEQ ID NO:Y," although other reading frames can also be easily translated using known molecular biology techniques. The polypeptides produced by these alternative open reading frames are specifically contemplated by the present invention. The first and last amino acid position of SEQ ID NO: Y of the predicted signal peptide is identified as "First AA of Sig Pep" and "Last AA of Sig Pep." The predicted first amino acid position of SEQ ID NO: Y of the secreted portion is identified as "Predicted First AA of Secreted Portion." Finally, the amino acid position of SEQ LD NO:Y of the last amino acid in the open reading frame is identified as "Last AA of ORF." SEQ ID NO:X and the translated SEQ ID NO:Y are sufficiently accurate and otherwise suitable for a variety of uses well known in the art and described further below. For instance, SEQ ID NO:X is useful for designing nucleic acid hybridization probes that will detect nucleic acid sequences contained in SEQ LD NO:X or the cDNA contained in the deposited clone. These probes will also hybridize to nucleic acid molecules in biological samples, thereby enabling a variety of forensic and diagnostic methods of the invention. Similarly, polypeptides identified from SEQ ID NO: Y may be used to generate antibodies which bind specifically to the secreted proteins encoded by the cDNA clones identified in Table 1. 71 Nevertheless, DNA sequences generated by sequencing reactions can contain sequencing errors. The errors exist as misidentified nucleotides, or as insertions or deletions of nucleotides in the generated DNA sequence. The erroneously inserted or deleted nucleotides cause frame shifts in the reading frames of the predicted amino acid sequence. In these cases, the predicted amino acid sequence diverges from the actual amino acid sequence, even though the generated DNA sequence may be greater than 99.9% identical to the actual DNA sequence (for example, one base insertion or deletion in an open reading frame of over 1000 bases). Accordingly, for those applications requiring precision in the nucleotide sequence or the amino acid sequence, the present invention provides not only the generated nucleotide sequence identified as SEQ ID NO:X and the predicted translated amino acid sequence identified as SEQ LD NO: Y, but also a sample of plasmid DNA containing a human cDNA of the invention deposited with the ATCC, as set forth in Table 1. The nucleotide sequence of each deposited clone can readily be determined by sequencing the deposited clone in accordance with known methods. The predicted amino acid sequence can then be verified from such deposits. Moreover, the amino acid sequence of the protein encoded by a particular clone can also be directly determined by peptide sequencing or by expressing the protein in a suitable hosrcell containing the deposited human cDNA, collecting the protein, and determining its sequence. The present invention also relates to the genes corresponding to SEQ ID NO:X, SEQ ED NO:Y, or the deposited clone. The corresponding gene can be isolated in accordance with known methods using the sequence information disclosed herein. Such methods include preparing probes or primers from the disclosed sequence and identifying or amplifying the corresponding gene from appropriate sources of genomic material. Also provided in the present invention are species homologs. Species homologs may be isolated and identified by making suitable probes or primers from the sequences provided herein and screening a suitable nucleic acid source for the desired homologue. The polypeptides of the invention can be prepared in any suitable manner. Such polypeptides include isolated naturally occurring polypeptides, recombinantly produced polypeptides, synthetically produced polypeptides, or polypeptides produced by a combination of these methods. Means for preparing such polypeptides are well understood in the art. The polypeptides may be in the form of the secreted protein, including the mature form, or may be a part of a larger protein, such as a fusion protein (see below). 72 It is often advantageous to include an additional amino acid sequence which contains secretory or leader sequences, pro-sequences, sequences which aid in purification , such as multiple histidine residues, or an additional sequence for stability during recombinant production. The polypeptides of the present invention are preferably provided in an isolated form, and preferably are substantially purified. A recombinantly produced version of a polypeptide, including the secreted polypeptide, can be substantially purified by the one-step method described in Smith and Johnson, Gene 67:31-40 (1988). Polypeptides of the invention also can be purified from natural or recombinant sources using antibodies of the invention raised against the secreted protein in methods which are well known in the art. Signal Sequences Methods for predicting whether a protein has a signal sequence, as well as the cleavage point for that sequence, are available. For instance, the method of McGeoch, Virus Res. 3:271-286 (1985), uses the information from a short N-terminal charged region and a subsequent uncharged region of the complete (uncleaved) protein. The method of von Heinje, Nucleic Acids Res. 14:4683-4690 (1986) uses the information from the residues surrounding the cleavage site, typically residues -13 to +2, where +1 indicates the amino terminus of the secreted protein. The accuracy of predicting the cleavage points of known mammalian secretory proteins for each of these methods is in the range of 75-80%. (von Heinje, supra.) However, the two methods do not always produce the same predicted cleavage point(s) for a given protein. In the present case, the deduced amino acid sequence of the secreted polypeptide was analyzed by a computer program called SignalP (Henrik Nielsen et al., Protein Engineering 10: 1-6 (1997)), which predicts the cellular location of a protein based on the amino acid sequence. As part of this computational prediction of localization, the methods of McGeoch and von Heinje are incorporated. The analysis of the amino acid sequences of the secreted proteins described herein by this program provided the results shown in Table 1. As one of ordinary skill would appreciate, however, cleavage sites sometimes vary from organism to organism and cannot be predicted with absolute certainty. Accordingly, the present invention provides secreted polypeptides having a sequence shown in SEQ ID NO:Y which have an N-terminus beginning within 5 residues (i.e., + or - 5 residues) of the predicted cleavage point. Similarly, it is also recognized that in some cases, cleavage of the signal sequence from a secreted protein is not entirely 73 uniform, resulting in more than one secreted species. These polypeptides, and the polynucleotides encoding such polypeptides, are contemplated by the present invention. Moreover, the signal sequence identified by the above analysis may not necessarily predict the naturally occurring signal sequence. For example, the naturally occurring signal sequence may be further upstream from the predicted signal sequence. However, it is likely that the predicted signal sequence will be capable of directing the secreted protein to the ER. These polypeptides, and the polynucleotides encoding such polypeptides, are contemplated by the present invention. Polynucleotide and Polypeptide Variants "Variant" refers to a polynucleotide or polypeptide differing from the polynucleotide or polypeptide of the present invention, but retaining essential properties thereof. Generally, variants are overall closely similar, and, in many regions, identical to the polynucleotide or polypeptide of the present invention. By a polynucleotide having a nucleotide sequence at least, for example, 95% "identical" to a reference nucleotide sequence of the present invention, it is intended that the nucleotide sequence of the polynucleotide is identical to the reference sequence except that the polynucleotide sequence may include up to five point mutations per each 100 nucleotides of the reference nucleotide sequence encoding the polypeptide. In other words, to obtain a polynucleotide having a nucleotide sequence at least 95% identical to a reference nucleotide sequence, up to 5% of the nucleotides in the reference sequence may be deleted or substituted with another nucleotide, or a number of nucleotides up to 5% of the total nucleotides in the reference sequence may be inserted into the reference sequence. The query sequence may be an entire sequence shown inTable 1, the ORF (open reading frame), or any fragement specified as described herein. As a practical matter, whether any particular nucleic acid molecule or polypeptide is at least 90%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of the presence invention can be determined conventionally using known computer programs. A preferred method for determing the best overall match between a query sequence (a sequence of the present invention) and a subject sequence, also referred to as a global sequence alignment, can be determined using the FASTDB computer program based on the algorithm of Brutlag et al. (Comp. App. Biosci. (1990) 6:237-245). In a sequence alignment the query and subject sequences are both DNA sequences. An RNA sequence can be compared by converting U's to T's. The result of said global sequence alignment is in percent identity. Preferred parameters used in a FASTDB alignment of DNA sequences to calculate percent identiy are: Matrix=Unitary, k-tuple=4, Mismatch Penalty=l, Joining Penalty =30, Randomization 74 Group Length=0, Cutoff Score=l, Gap Penalty=5, Gap Size Penalty 0.05, Window Size=500 or the lenght of the subject nucleotide sequence, whichever is shorter. If the subject sequence is shorter than the query sequence because of 5' or 3' deletions, not because of internal deletions, a manual correction must be made to the results. This is because the FASTDB program does not account for 5' and 3' truncations of the subject sequence when calculating percent identity. For subject sequences truncated at the 5' or 3' ends, relative to the the query sequence, the percent identity is corrected by calculating the number of bases of the query sequence that are 5' and 3' of the subject sequence, which are not matched/aligned, as a percent of the total bases of the query sequence. Whether a nucleotide is matched/aligned is determined by results of the FASTDB sequence alignment. This percentage is then subtracted from the percent identity, calculated by the above FASTDB program using the specified parameters, to arrive at a final percent identity score. This corrected score is what is used for the purposes of the present invention. Only bases outside the 5' and 3' bases of the subject sequence, as displayed by the FASTDB alignment, which are not matched/aligned with the query sequence, are calculated for the purposes of manually adjusting the percent identity score. For example, a 90 base subject sequence is aligned to a 100 base query sequence to determine percent identity. The deletions occur at the 5' end of the subject sequence and therefore, the FASTDB alignment does not show a matched/alignement of the first 10 bases at 5' end. The 10 unpaired bases represent 10% of the sequence (number of bases at the 5' and 3' ends not matched/total number of bases in the query sequence) so 10% is subtracted from the percent identity score calculated by the FASTDB program. If the remaining 90 bases were perfectly matched the final percent identity would be 90%. In another example, a 90 base subject sequence is compared with a 100 base query sequence. This time the deletions are internal deletions so that there are no bases on the 5' or 3' of the subject sequence which are not matched/aligned with the query. In this case the percent identity calculated by FASTDB is not manually corrected. Once again, only bases 5' and 3' of the subject sequence which are not matched/aligned with the query sequnce are manually corrected for. No other manual corrections are to made for the purposes of the present invention. By a polypeptide having an amino acid sequence at least, for example, 95% "identical" to a query amino acid sequence of the present invention, it is intended that the amino acid sequence of the subject polypeptide is identical to the query sequence except that the subject polypeptide sequence may include up to five amino acid alterations per each 100 amino acids of the query amino acid sequence. In other words, to obtain a polypeptide having an amino acid sequence at least 95% identical to a query 75 amino acid sequence, up to 5% of the amino acid residues in the subject sequence may be inserted, deleted, (indels) or substituted with another amino acid. These alterations of the reference sequence may occur at the amino or carboxy terminal positions of the reference amino acid sequence or anywhere between those terminal positions, interspersed either individually among residues in the reference sequence or in one or more contiguous groups within the reference sequence. As a practical matter, whether any particular polypeptide is at least 90%, 95%, 96%, 97%, 98% or 99% identical to, for instance, the amino acid sequences shown in Table 1 or to the amino acid sequence encoded by deposited DNA clone can be determined conventionally using known computer programs. A preferred method for determing the best overall match between a query sequence (a sequence of the present invention) and a subject sequence, also referred to as a global sequence alignment, can be determined using the FASTDB computer program based on the algorithm of Brutlag et al. (Comp. App. Biosci. (1990) 6:237-245). In a sequence alignment the query and subject sequences are either both nucleotide sequences or both amino acid sequences. The result of said global sequence alignment is in percent identity. Preferred parameters used in a FASTDB amino acid alignment are: Matrix=PAM 0, k-tuple=2, Mismatch Penalty=l, Joining Penal ty=20, Randomization Group Length=0, Cutoff Scored 1, Window Size=sequence length, Gap Penalty=5, Gap Size Penalty=0.05, Window Size=500 or the length of the subject amino acid sequence, whichever is shorter. If the subject sequence is shorter than the query sequence due to N- or C- terminal deletions, not because of internal deletions, a manual correction must be made to the results. This is becuase the FASTDB program does not account for N- and C- terminal truncations of the subject sequence when calculating global percent identity. For subject sequences truncated at the N- and C-termini, relative to the the query sequence, the percent identity is corrected by calculating the number of residues of the query sequence that are N- and C-terminal of the subject sequence, which are not matched/aligned with a corresponding subject residue, as a percent of the total bases of the query sequence. Whether a residue is matched/aligned is determined by results of the FASTDB sequence alignment. This percentage is then subtracted from the percent identity, calculated by the above FASTDB program using the specified parameters, to arrive at a final percent identity score. This final percent identity score is what is used for the purposes of the present invention. Only residues to the N- and C-termini of the subject sequence, which are not matched/aligned with the query sequence, are considered for the purposes of manually adjusting the percent identity score. That is, only query residue positions outside the farthest N- and C-terminal residues of the subject sequence. 76 For example, a 90 amino acid residue subject sequence is aligned with a 100 residue query sequence to determine percent identity. The deletion occurs at the N- terminus of the subject sequence and therefore, the FASTDB alignment does not show a matching/alignment of the first 10 residues at the N-terminus. The 10 unpaired residues represent 10% of the sequence (number of residues at the N- and C- termini not matched/total number of residues in the query sequence) so 10% is subtracted from the percent identity score calculated by the FASTDB program. If the remaining 90 residues were perfectly matched the final percent identity would be 90%. In another example, a 90 residue subject sequence is compared with a 100 residue query sequence. This time the deletions are internal deletions so there are no residues at the N- or C- termini of the subject sequence which are not matched/aligned with the query. In this case the percent identity calculated by FASTDB is not manually corrected. Once again, only residue positions outside the N- and C-terminal ends of the subject sequence, as displayed in the FASTDB alignment, which are not matched/aligned with the query sequnce are manually corrected for. No other manual corrections are to made for the purposes of the present invention. The variants may contain alterations in the coding regions, non-coding regions, or both. Especially preferred are polynucleotide variants containing alterations which produce silent substitutions, additions, or deletions, but do not alter the properties or activities of the encoded polypeptide. Nucleotide variants produced by silent substitutions due to the degeneracy of the genetic code are preferred. Moreover, variants in which 5-10, 1-5, or 1-2 amino acids are substituted, deleted, or added in any combination are also preferred. Polynucleotide variants can be produced for a variety of reasons, e.g., to optimize codon expression for a particular host (change codons in the human mRNA to those preferred by a bacterial host such as E. coli). Naturally occurring variants are called "allelic variants," and refer to one of several alternate forms of a gene occupying a given locus on a chromosome of an organism. (Genes II, Lewin, B., ed., John Wiley & Sons, New York (1985).) These allelic variants can vary at either the polynucleotide and/or polypeptide level. Alternatively, non-naturally occurring variants may be produced by mutagenesis techniques or by direct synthesis. Using known methods of protein engineering and recombinant DNA technology, variants may be generated to improve or alter the characteristics of the polypeptides of the present invention. For instance, one or more amino acids can be deleted from the N-terminus or C-terminus of the secreted protein without substantial loss of biological function. The authors of Ron et al., J. Biol. Chem. 268: 2984-2988 (1993), reported variant KGF proteins having heparin binding activity even after 77 deleting 3, 8, or 27 amino-terminal amino acid residues. Similarly, Interferon gamma exhibited up to ten times higher activity after deleting 8-10 amino acid residues from the carboxy terminus of this protein. (Dobeli et al., J. Biotechnology 7: 199-216 (1988).) Moreover, ample evidence demonstrates that variants often retain a biological activity similar to that of the naturally occurring protein. For example, Gayle and coworkers (J. Biol. Chem 268:22105-22111 (1993)) conducted extensive mutational analysis of human cytokine IL-la. They used random mutagenesis to generate over 3,500 individual IL-la mutants that averaged 2.5 amino acid changes per variant over the entire length of the molecule. Multiple mutations were examined at every possible amino acid position. The investigators found that "[m]ost of the molecule could be altered with little effect on either [binding or biological activity]." (See, Abstract.) In fact, only 23 unique amino acid sequences, out of more than 3,500 nucleotide sequences examined, produced a protein that significantly differed in activity from wild- type. Furthermore, even if deleting one or more amino acids from the N-terminus or C-terminus of a polypeptide results in modification or loss of one or more biological functions, other biological activities may still be retained. For example, the ability of a deletion variant to induce and/or to bind antibodies which recognize the secreted form will likely be retained when less than the majority of the residues of the secreted form are removed from the N-terminus or C-terminus. Whether a particular polypeptide lacking N- or C-terminal residues of a protein retains such immunogenic activities can readily be determined by routine methods described herein and otherwise known in the art. Thus, the invention further includes polypeptide variants which show substantial biological activity. Such variants include deletions, insertions, inversions, repeats, and substitutions selected according to general rules known in the art so as have little effect on activity. For example, guidance concerning how to make phenotypically silent amino acid substitutions is provided in Bowie, J. U. et al., Science 247:1306-1310 (1990), wherein the authors indicate that there are two main strategies for studying the tolerance of an amino acid sequence to change. The first strategy exploits the tolerance of amino acid substitutions by natural selection during the process of evolution. By comparing amino acid sequences in different species, conserved amino acids can be identified. These conserved amino acids are likely important for protein function. In contrast, the amino acid positions where substitutions have been tolerated by natural selection indicates that these positions are not critical for protein function. Thus, positions tolerating amino acid substitution could be modified while still maintaining biological activity of the protein. 78 The second strategy uses genetic engineering to introduce amino acid changes at specific positions of a cloned gene to identify regions critical for protein function. For example, site directed mutagenesis or alanine-scanning mutagenesis (introduction of single alanine mutations at every residue in the molecule) can be used. (Cunningham and Wells, Science 244: 1081-1085 (1989).) The resulting mutant molecules can then be tested for biological activity. As the authors state, these two strategies have revealed that proteins are surprisingly tolerant of amino acid substitutions. The authors further indicate which amino acid changes are likely to be permissive at certain amino acid positions in the protein. For example, most buried (within the tertiary structure of the protein) amino acid residues require nonpolar side chains, whereas few features of surface side chains are generally conserved. Moreover, tolerated conservative amino acid substitutions involve replacement of the aliphatic or hydrophobic amino acids Ala, Val, Leu and He; replacement of the hydroxyl residues Ser and Thr; replacement of the acidic residues Asp and Glu; replacement of the amide residues Asn and Gin, replacement of the basic residues Lys, Arg, and His; replacement of the aromatic residues Phe, Tyr, and Trp, and replacement of the small-sized amino acids Ala, Ser, Thr, Met, and Gly. Besides conservative amino acid substitution, variants of the present invention include (i) substitutions with one or more of the non-conserved amino acid residues, where the substituted amino acid residues may or may not be one encoded by the genetic code, or (ii) substitution with one or more of amino acid residues having a substituent group, or (iii) fusion of the mature polypeptide with another compound, such as a compound to increase the stability and/or solubility of the polypeptide (for example, polyethylene glycol), or (iv) fusion of the polypeptide with additional amino acids, such as an IgG Fc fusion region peptide, or leader or secretory sequence, or a sequence facilitating purification. Such variant polypeptides are deemed to be within the scope of those skilled in the art from the teachings herein. For example, polypeptide variants containing amino acid substitutions of charged amino acids with other charged or neutral amino acids may produce proteins with improved characteristics, such as less aggregation. Aggregation of pharmaceutical formulations both reduces activity and increases clearance due to the aggregate's immunogenic activity. (Pinckard et al., Clin. Exp. Immunol. 2:331-340 (1967); Robbins et al., Diabetes 36: 838-845 (1987); Cleland et al., Crit. Rev. Therapeutic Drug Carrier Systems 10:307-377 (1993).) A further embodiment of the invention relates to a polypeptide which comprises the amino acid sequence of the present invention having an amino acid sequence which contains at least one amino acid substitution, but not more than 50 amino acid 79 substitutions, even more preferably, not more than 40 amino acid substitutions, still more preferably, not more than 30 amino acid substitutions, and still even more preferably, not more than 20 amino acid substitutions. Of course, in order of ever- increasing preference, it is highly preferable for a polypeptide to have an amino acid sequence which comprises the amino acid sequence of the present invention, which contains at least one, but not more than 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 amino acid substitutions. In specific embodiments, the number of additions, substitutions, and/or deletions in the amino acid sequence of the present invention or fragments thereof (e.g., the mature form and/or other fragments described herein), is 1-5, 5-10, 5-25, 5-50, 10- 50 or 50-150, conservative amino acid substitutions are preferable. Polynucleotide and Polypeptide Fragments In the present invention, a "polynucleotide fragment" refers to a short polynucleotide having a nucleic acid sequence contained in the deposited clone or shown in SEQ ID NO:X. The short nucleotide fragments are preferably at least about 15 nt, and more preferably at least about 20 nt, still more preferably at least about 30 nt, and even more preferably, at least about 40 nt in length. A fragment "at least 20 nt in length," for example, is intended to include 20 or more contiguous bases fromTfhe cDNA sequence contained in the deposited clone or the nucleotide sequence shown in SEQ ID NO:X. These nucleotide fragments are useful as diagnostic probes and primers as discussed herein. Of course, larger fragments (e.g., 50, 150, 500, 600, 2000 nucleotides) are preferred. Moreover, representative examples of polynucleotide fragments of the invention, include, for example, fragments having a sequence from about nucleotide number 1-50, 51-100, 101-150, 151-200, 201-250, 251-300, 301-350, 351-400, 401- 450, 451-500, 501-550, 551-600, 651-700, 701-750, 751-800, 800-850, 851-900, 901-950, 951-1000, 1001-1050, 1051-1100, 1101-1150, 1151-1200, 1201-1250, 1251-1300, 1301-1350, 1351-1400, 1401-1450, 1451-1500, 1501-1550, 1551-1600, 1601-1650, 1651-1700, 1701-1750, 1751-1800, 1801-1850, 1851-1900, 1901-1950, 1951 -2000, or 2001 to the end of SEQ ID NO:X or the cDN A contained in the deposited clone. In this context "about" includes the particularly recited ranges, larger or smaller by several (5, 4, 3, 2, or 1) nucleotides, at either terminus or at both termini. Preferably, these fragments encode a polypeptide which has biological activity. More preferably, these polynucleotides can be used as probes or primers as discussed herein. En the present invention, a "polypeptide fragment" refers to a short amino acid sequence contained in SEQ ID NO:Y or encoded by the cDNA contained in the deposited clone. Protein fragments may be "free-standing," or comprised within a 80 larger polypeptide of which the fragment forms a part or region, most preferably as a single continuous region. Representative examples of polypeptide fragments of the invention, include, for example, fragments from about amino acid number 1-20, 21-40, 41-60, 61-80, 81-100, 102-120, 121-140, 141-160, or 161 to the end of the coding region. Moreover, polypeptide fragments can be about 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, or 150 amino acids in length. In this context "about" includes the particularly recited ranges, larger or smaller by several (5, 4, 3, 2, or 1) amino acids, at either extreme or at both extremes. Preferred polypeptide fragments include the secreted protein as well as the mature form. Further preferred polypeptide fragments include the secreted protein or the mature form having a continuous series of deleted residues from the amino or the carboxy terminus, or both. For example, any number of amino acids, ranging from 1- 60, can be deleted from the amino terminus of either the secreted polypeptide or the mature form. Similarly, any number of amino acids, ranging from 1-30, can be deleted from the carboxy terminus of the secreted protein or mature form. Furthermore, any combination of the above amino and carboxy terminus deletions are preferred. Similarly, polynucleotide fragments encoding these polypeptide fragments are also preferred. Also preferred are polypeptide and polynucleotide fragments characterized by structural or functional domains, such as fragments that comprise alpha-helix and alpha- helix forming regions, beta-sheet and beta-sheet-forming regions, turn and turn- forming regions, coil and coil-forming regions, hydrophilic regions, hydrophobic regions, alpha amphipathic regions, beta amphipathic regions, flexible regions, surface- forming regions, substrate binding region, and high antigenic index regions. Polypeptide fragments of SEQ ID NO: Y falling within conserved domains are specifically contemplated by the present invention. Moreover, polynucleotide fragments encoding these domains are also contemplated. Other preferred fragments are biologically active fragments. Biologically active fragments are those exhibiting activity similar, but not necessarily identical, to an activity of the polypeptide of the present invention. The biological activity of the fragments may include an improved desired activity, or a decreased undesirable activity. Epitopes & Antibodies In the present invention, "epitopes" refer to polypeptide fragments having antigenic or immunogenic activity in an animal, especially in a human. A preferred embodiment of the present invention relates to a polypeptide fragment comprising an epitope, as well as the polynucleotide encoding this fragment. A region of a protein molecule to which an antibody can bind is defined as an "antigenic epitope." In contrast, an "immunogenic epitope" is defined as a part of a protein that elicits an antibody response. (See, for instance, Geysen et al., Proc. Natl. Acad. Sci. USA 81:3998- 4002 (1983).) Fragments which function as epitopes may be produced by any conventional means. (See, e.g., Houghten, R. A., Proc. Natl. Acad. Sci. USA 82:5131-5135 (1985) further described in U.S. Patent No. 4,631,211.) In the present invention, antigenic epitopes preferably contain a sequence of at least seven, more preferably at least nine, and most preferably between about 15 to about 30 amino acids. Antigenic epitopes are useful to raise antibodies, including monoclonal antibodies, that specifically bind the epitope. (See, for instance, Wilson et al.. Cell 37:767-778 (1984); Sutcliffe, J. G. et al., Science 219:660-666 (1983).) Similarly, immunogenic epitopes can be used to induce antibodies according to methods well known in the art. (See, for instance, Sutcliffe et al, supra; Wilson et al., supra; Chow, M. et al., Proc. Natl. Acad. Sci. USA 82:910-914; and Bittle, F. J. et al., J. Gen. Virol. 66:2347-2354 (1985).) A preferred immunogenic epitope includes the secreted protein. The immunogenic epitopes may be presented together with a carrier protein, such as an albumin, to an animal system (such as rabbit or mouse) or, if it is long enough (at least about 25 amino acids), without a carrier. However, immunogenic epitopes comprising as few as 8 to 10 amino acids have been shown to be sufficient to raise antibodies capable of binding to, at the very least, linear epitopes in a denatured polypeptide (e.g., in Western blotting.) As used herein, the term "antibody" (Ab) or "monoclonal antibody" (Mab) is meant to include intact molecules as well as antibody fragments (such as, for example, Fab and F(ab')2 fragments) which are capable of specifically binding to protein. Fab and F(ab')2 fragments lack the Fc fragment of intact antibody, clear more rapidly from the circulation, and may have less non-specific tissue binding than an intact antibody. (Wahl et al., J. Nucl. Med. 24:316-325 (1983).) Thus, these fragments are preferred, as well as the products of a FAB or other immunoglobulin expression library. Moreover, antibodies of the present invention include chimeric, single chain, and humanized antibodies. Fusion Proteins Any polypeptide of the present invention can be used to generate fusion proteins. For example, the polypeptide of the present invention, when fused to a second protein, can be used as an antigenic tag. Antibodies raised against the polypeptide of the present invention can be used to indirectly detect the second protein 82 by binding to the polypeptide. Moreover, because secreted proteins target cellular locations based on trafficking signals, the polypeptides of the present invention can be used as targeting molecules once fused to other proteins. Examples of domains that can be fused to polypeptides of the present invention include not only heterologous signal sequences, but also other heterologous functional regions. The fusion does not necessarily need to be direct, but may occur through linker sequences. Moreover, fusion proteins may also be engineered to improve characteristics of the polypeptide of the present invention. For instance, a region of additional amino acids, particularly charged amino acids, may be added to the N-terminus of the polypeptide to improve stability and persistence during purification from the host cell or subsequent handling and storage. Also, peptide moieties may be added to the polypeptide to facilitate purification. Such regions may be removed prior to final preparation of the polypeptide. The addition of peptide moieties to facilitate handling of polypeptides are familiar and routine techniques in the art. Moreover, polypeptides of the present invention, including fragments, and specifically epitopes, can be combined with parts of the constant domain of immunoglobulins (IgG), resulting in chimeric polypeptides. These fusion proteins facilitate purification and show an increased half-life in vivo. One reported example describes chimeric proteins consisting of the first two domains of the human CD4- polypeptide and various domains of the constant regions of the heavy or light chains of mammalian immunoglobulins. (EP A 394,827; Traunecker et al., Nature 331:84-86 (1988).) Fusion proteins having disulfide-linked dimeric structures (due to the IgG) can also be more efficient in binding and neutralizing other molecules, than the monomeric secreted protein or protein fragment alone. (Fountoulakis et al., J. Biochem. 270:3958-3964 (1995).) Similarly, EP-A-O 464 533 (Canadian counterpart 2045869) discloses fusion proteins comprising various portions of constant region of immunoglobulin molecules together with another human protein or part thereof. In many cases, the Fc part in a fusion protein is beneficial in therapy and diagnosis, and thus can result in, for example, improved pharmacokinetic properties. (EP-A 0232 262.) Alternatively, deleting the Fc part after the fusion protein has been expressed, detected, and purified, would be desired. For example, the Fc portion may hinder therapy and diagnosis if the fusion protein is used as an antigen for immunizations. In drug discovery, for example, human proteins, such as hIL-5, have been fused with Fc portions for the purpose of high-throughput screening assays to identify antagonists of hLL-5. (See, D. 83 Bennett et al., J. Molecular Recognition 8:52-58 (1995); K. Johanson et al., J. Biol. Chem. 270:9459-9471 (1995).) Moreover, the polypeptides of the present invention can be fused to marker sequences, such as a peptide which facilitates purification of the fused polypeptide. En preferred embodiments, the marker amino acid sequence is a hexa-histidine peptide, such as the tag provided in a pQE vector (QIAGEN, Inc., 9259 Eton Avenue, Chatsworth, CA, 91311), among others, many of which are commercially available. As described in Gentz et al., Proc. Natl. Acad. Sci. USA 86:821-824 (1989), for instance, hexa-histidine provides for convenient purification of the fusion protein. Another peptide tag useful for purification, the "HA" tag, corresponds to an epitope derived from the influenza hemagglutinin protein. (Wilson et al., Cell 37:767 (1984).) Thus, any of these above fusions can be engineered using the polynucleotides or the polypeptides of the present invention. Vectors. Host Cells, and Protein Production The present invention also relates to vectors containing the polynucleotide of the present invention, host cells, and the production of polypeptides by recombinant techniques. The vector may be, for example, a phage, plasmid, viral, or retroviral vector. Retroviral vectors may be replication competent or replication defective. In the latter case, viral propagation generally will occur only in complementing host cells. The polynucleotides may be joined to a vector containing a selectable marker for propagation in a host. Generally, a plasmid vector is introduced in a precipitate, such as a calcium phosphate precipitate, or in a complex with a charged lipid. If the vector is a virus, it may be packaged in vitro using an appropriate packaging cell line and then transduced into host cells. The polynucleotide insert should be operatively linked to an appropriate promoter, such as the phage lambda PL promoter, the E. coli lac, trp, phoA and tac promoters, the SV40 early and late promoters and promoters of retroviral LTRs, to name a few. Other suitable promoters will be known to the skilled artisan. The expression constructs will further contain sites for transcription initiation, termination, and, in the transcribed region, a ribosome binding site for translation. The coding portion of the transcripts expressed by the constructs will preferably include a translation initiating codon at the beginning and a termination codon (UAA, UGA or UAG) appropriately positioned at the end of the polypeptide to be translated. As indicated, the expression vectors will preferably include at least one selectable marker. Such markers include dihydrofolate reductase, G418 or neomycin resistance for eukaryotic cell culture and tetracycline, kanamycin or ampicillin resistance 84 genes for culturing in E. coli and other bacteria. Representative examples of appropriate hosts include, but are not limited to, bacterial cells, such as E. coli, Streptomyces and Salmonella typhimurium cells; fungal cells, such as yeast cells; insect cells such as Drosophila S2 and Spodoptera Sf9 cells; animal cells such as CHO, COS, 293, and Bowes melanoma cells; and plant cells. Appropriate culture mediums and conditions for the above-described host cells are known in the art. Among vectors preferred for use in bacteria include pQE70, pQE60 and pQE-9, available from QIAGEN, Inc.; pBluescript vectors, Phagescript vectors, pNH8A, pNHlόa, pNH18A, pNH46A, available from Stratagene Cloning Systems, Inc.; and ptrc99a, pKK223-3, pKK233-3, pDR540, pRIT5 available from Pharmacia Biotech, Inc. Among preferred eukaryotic vectors are pWLNEO, pSV2CAT, pOG44, pXTl and pSG available from Stratagene; and pSVK3, pBPV, pMSG and pSVL available from Pharmacia. Other suitable vectors will be readily apparent to the skilled artisan. Introduction of the construct into the host cell can be effected by calcium phosphate transfection, DEAE-dextran mediated transfection, cationic lipid-mediated transfection, electroporation, transduction, infection, or other methods. Such methods are described in many standard laboratory manuals, such as Davis et al., Basic Methods In Molecular Biology (1986). It is specifically contemplated that the polypeptides of the present invention may in fact be expressed by a host cell lacking a recombinant vector. A polypeptide of this invention can be recovered and purified from recombinant cell cultures by well-known methods including ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography, hydroxylapatite chromatography and lectin chromatography. Most preferably, high performance liquid chromatography ("HPLC") is employed for purification. Polypeptides of the present invention, and preferably the secreted form, can also be recovered from: products purified from natural sources, including bodily fluids, tissues and cells, whether directly isolated or cultured; products of chemical synthetic procedures; and products produced by recombinant techniques from a prokaryotic or eukaryotic host, including, for example, bacterial, yeast, higher plant, insect, and mammalian cells. Depending upon the host employed in a recombinant production procedure, the polypeptides of the present invention may be glycosylated or may be non-glycosylated. In addition, polypeptides of the invention may also include an initial modified methionine residue, in some cases as a result of host-mediated processes. Thus, it is well known in the art that the N-terminal methionine encoded by the translation initiation codon generally is removed with high efficiency from any protein 85 after translation in all eukaryotic cells. While the N-terminal methionine on most proteins also is efficiently removed in most prokaryotes, for some proteins, this prokaryotic removal process is inefficient, depending on the nature of the amino acid to which the N-terminal methionine is covalently linked. In addition to encompassing host cells containing the vector constructs discussed herein, the invention also encompasses primary, secondary, and immortalized host cells of vertebrate origin, particularly mammalian origin, that have been engineered to delete or replace endogenous genetic material (e.g., coding sequence), and/or to include genetic material (e.g., heterologous polynucleotide sequences) that is operably associated with the polynucleotides of the invention, and which activates, alters, and/or amplifies endogenous polynucleotides. For example, techniques known in the art may be used to operably associate heterologous control regions (e.g., promoter and/or enhancer) and endogenous polynucleotide sequences via homologous recombination (see, e.g., U.S. Patent No. 5,641,670, issued June 24, 1997; International Publication No. WO 96/29411, published September 26, 1996; Intemational Publication No. WO 94/12650, published August 4, 1994; Koller et al., Proc. Natl. Acad. Sci. USA 86:8932-8935 (1989); and Zijlstra et al., Nature 342:435- 438 (1989), the disclosures of each of which are incorporated by reference in their entireties). Uses of the Polynucleotides Each of the polynucleotides identified herein can be used in numerous ways as reagents. The following description should be considered exemplary and utilizes known techniques. The polynucleotides of the present invention are useful for chromosome identification. There exists an ongoing need to identify new chromosome markers, since few chromosome marking reagents, based on actual sequence data (repeat polymorphisms), are presently available. Each polynucleotide of the present invention can be used as a chromosome marker. Briefly, sequences can be mapped to chromosomes by preparing PCR primers (preferably 15-25 bp) from the sequences shown in SEQ ID NO:X. Primers can be selected using computer analysis so that primers do not span more than one predicted exon in the genomic DNA. These primers are then used for PCR screening of somatic cell hybrids containing individual human chromosomes. Only those hybrids containing the human gene corresponding to the SEQ LD NO:X will yield an amplified fragment. 86 Similarly, somatic hybrids provide a rapid method of PCR mapping the polynucleotides to particular chromosomes. Three or more clones can be assigned per day using a single thermal cycler. Moreover, sublocalization of the polynucleotides can be achieved with panels of specific chromosome fragments. Other gene mapping strategies that can be used include in situ hybridization, prescreening with labeled flow- sorted chromosomes, and preselection by hybridization to construct chromosome specific-cDNA libraries. Precise chromosomal location of the polynucleotides can also be achieved using fluorescence in situ hybridization (FISH) of a metaphase chromosomal spread. This technique uses polynucleotides as short as 500 or 600 bases; however, polynucleotides 2,000-4,000 bp are preferred. For a review of this technique, see Verma et al., "Human Chromosomes: a Manual of Basic Techniques," Pergamon Press, New York (1988). For chromosome mapping, the polynucleotides can be used individually (to mark a single chromosome or a single site on that chromosome) or in panels (for marking multiple sites and/or multiple chromosomes). Preferred polynucleotides correspond to the noncoding regions of the cDNAs because the coding sequences are more likely conserved within gene families, thus increasing the chance of cross hybridization during chromosomal mapping. Once a polynucleotide has been mapped to a precise chromosomal location, the physical position of the polynucleotide can be used in linkage analysis. Linkage analysis establishes coinheritance between a chromosomal location and presentation of a particular disease. (Disease mapping data are found, for example, in V. McKusick, Mendelian Inheritance in Man (available on line through Johns Hopkins University Welch Medical Library) .) Assuming 1 megabase mapping resolution and one gene per 20 kb, a cDNA precisely localized to a chromosomal region associated with the disease could be one of 50-500 potential causative genes. Thus, once coinheritance is established, differences in the polynucleotide and the corresponding gene between affected and unaffected individuals can be examined. First, visible structural alterations in the chromosomes, such as deletions or translocations, are examined in chromosome spreads or by PCR. If no structural alterations exist, the presence of point mutations are ascertained. Mutations observed in some or all affected individuals, but not in normal individuals, indicates that the mutation may cause the disease. However, complete sequencing of the polypeptide and the corresponding gene from several normal individuals is required to distinguish the mutation from a polymorphism. If a new polymorphism is identified, this polymorphic polypeptide can be used for further linkage analysis. 87 Furthermore, increased or decreased expression of the gene in affected individuals as compared to unaffected individuals can be assessed using polynucleotides of the present invention. Any of these alterations (altered expression, chromosomal rearrangement, or mutation) can be used as a diagnostic or prognostic marker. In addition to the foregoing, a polynucleotide can be used to control gene expression through triple helix formation or antisense DNA or RNA. Both methods rely on binding of the polynucleotide to DNA or RNA. For these techniques, preferred polynucleotides are usually 20 to 40 bases in length and complementary to either the region of the gene involved in transcription (triple helix - see Lee et al., Nucl. Acids Res. 6:3073 (1979); Cooney et al., Science 241:456 (1988); and Dervan et al., Science 251:1360 (1991) ) or to the mRNA itself (antisense - Okano, J. Neurochem. 56:560 (1991); Oligodeoxy-nucleotides as Antisense Inhibitors of Gene Expression, CRC Press, Boca Raton, FL (1988).) Triple helix formation optimally results in a shut-off of RNA transcription from DNA, while antisense RNA hybridization blocks translation of an mRNA molecule into polypeptide. Both techniques are effective in model systems, and the information disclosed herein can be used to design antisense or triple helix polynucleotides in an effort to treat disease. Polynucleotides of the present invention are also useful in gene therapy. One goal of gene therapy is to insert a normal gene into an organism having a defective gene, in an effort to correct the genetic defect. The polynucleotides disclosed in the present invention offer a means of targeting such genetic defects in a highly accurate manner. Another goal is to insert a new gene that was not present in the host genome, thereby producing a new trait in the host cell. The polynucleotides are also useful for identifying individuals from minute biological samples. The United States military, for example, is considering the use of restriction fragment length polymorphism (RFLP) for identification of its personnel. In this technique, an individual's genomic DNA is digested with one or more restriction enzymes, and probed on a Southern blot to yield unique bands for identifying personnel. This method does not suffer from the current limitations of "Dog Tags" which can be lost, switched, or stolen, making positive identification difficult. The polynucleotides of the present invention can be used as additional DNA markers for RFLP. The polynucleotides of the present invention can also be used as an alternative to RFLP, by determining the actual base-by-base DNA sequence of selected portions of an individual's genome. These sequences can be used to prepare PCR primers for amplifying and isolating such selected DNA, which can then be sequenced. Using this technique, individuals can be identified because each individual will have a unique set of DNA sequences. Once an unique ID database is established for an individual, positive identification of that individual, living or dead, can be made from extremely small tissue samples. Forensic biology also benefits from using DNA-based identification techniques as disclosed herein. DNA sequences taken from very small biological samples such as tissues, e.g., hair or skin, or body fluids, e.g., blood, saliva, semen, etc., can be amplified using PCR. In one prior art technique, gene sequences amplified from polymorphic loci, such as DQa class II HLA gene, are used in forensic biology to identify individuals. (Erlich, H., PCR Technology, Freeman and Co. (1992).) Once these specific polymorphic loci are amplified, they are digested with one or more restriction enzymes, yielding an identifying set of bands on a Southern blot probed with DNA corresponding to the DQa class IE HLA gene. Similarly, polynucleotides of the present invention can be used as polymorphic markers for forensic purposes. There is also a need for reagents capable of identifying the source of a particular tissue. Such need arises, for example, in forensics when presented with tissue of unknown origin. Appropriate reagents can comprise, for example, DNA probes or primers specific to particular tissue prepared from the sequences of the present invention. Panels of such reagents can identify tissue by species and/or by organ type. In a similar fashion, these reagents can be used to screen tissue cultures for contamination. In the very least, the polynucleotides of the present invention can be used as molecular weight markers on Southern gels, as diagnostic probes for the presence of a specific mRNA in a particular cell type, as a probe to "subtract-out" known sequences in the process of discovering novel polynucleotides, for selecting and making oligomers for attachment to a "gene chip" or other support, to raise anti-DNA antibodies using DNA immunization techniques, and as an antigen to elicit an immune response. Uses of the Polypeptides Each of the polypeptides identified herein can be used in numerous ways. The following description should be considered exemplary and utilizes known techniques. A polypeptide of the present invention can be used to assay protein levels in a biological sample using antibody-based techniques. For example, protein expression in tissues can be studied with classical immunohistological methods. (Jalkanen, M., et al., J. Cell. Biol. 101:976-985 (1985); Jalkanen, M., et al., J. Cell . Biol. 105:3087- 3096 (1987).) Other antibody-based methods useful for detecting protein gene expression include immunoassays, such as the enzyme linked immunosorbent assay 89 (ELISA) and the radioimmunoassay (RIA). Suitable antibody assay labels are known in the art and include enzyme labels, such as, glucose oxidase, and radioisotopes, such as iodine (1251, 1211), carbon (14C), sulfur (35S), tritium (3H), indium (112In), and technetium (99mTc), and fluorescent labels, such as fluorescein and rhodamine, and biotin. In addition to assaying secreted protein levels in a biological sample, proteins can also be detected in vivo by imaging. Antibody labels or markers for in vivo imaging of protein include those detectable by X-radiography, NMR or ESR. For X- radiography, suitable labels include radioisotopes such as barium or cesium, which emit detectable radiation but are not overtly harmful to the subject. Suitable markers for NMR and ESR include those with a detectable characteristic spin, such as deuterium, which may be incorporated into the antibody by labeling of nutrients for the relevant hybridoma. A protein-specific antibody or antibody fragment which has been labeled with an appropriate detectable imaging moiety, such as a radioisotope (for example, 1311, 112In, 99mTc), a radio-opaque substance, or a material detectable by nuclear magnetic resonance, is introduced (for example, parenterally, subcutaneously, or intraperitoneally) into the mammal. It will be understood in the art that the size of the subject and the imaging system used will determine the quantity of imaging moiety needed to produce diagnostic images. In the case of a radioisotope moiety, for a human subject, the quantity of radioactivity injected will normally range from about 5 to 20 millicuries of 99mTc. The labeled antibody or antibody fragment will then preferentially accumulate at the location of cells which contain the specific protein. In vivo tumor imaging is described in S.W. Burchiel et al., "Immunopharmacokinetics of Radiolabeled Antibodies and Their Fragments." (Chapter 13 in Tumor Imaging: The Radiochemical Detection of Cancer, S.W. Burchiel and B. A. Rhodes, eds., Masson Publishing Inc. (1982).) Thus, the invention provides a diagnostic method of a disorder, which involves (a) assaying the expression of a polypeptide of the present invention in cells or body fluid of an individual; (b) comparing the level of gene expression with a standard gene expression level, whereby an increase or decrease in the assayed polypeptide gene expression level compared to the standard expression level is indicative of a disorder. Moreover, polypeptides of the present invention can be used to treat disease. For example, patients can be administered a polypeptide of the present invention in an effort to replace absent or decreased levels of the polypeptide (e.g., insulin), to supplement absent or decreased levels of a different polypeptide (e.g., hemoglobin S for hemoglobin B), to inhibit the activity of a polypeptide (e.g., an oncogene), to 90 activate the activity of a polypeptide (e.g., by binding to a receptor), to reduce the activity of a membrane bound receptor by competing with it for free ligand (e.g., soluble TNF receptors used in reducing inflammation), or to bring about a desired response (e.g., blood vessel growth). Similarly, antibodies directed to a polypeptide of the present invention can also be used to treat disease. For example, administration of an antibody directed to a polypeptide of the present invention can bind and reduce overproduction of the polypeptide. Similarly, administration of an antibody can activate the polypeptide, such as by binding to a polypeptide bound to a membrane (receptor). At the very least, the polypeptides of the present invention can be used as molecular weight markers on SDS-PAGE gels or on molecular sieve gel filtration columns using methods well known to those of skill in the art. Polypeptides can also be used to raise antibodies, which in turn are used to measure protein expression from a recombinant cell, as a way of assessing transformation of the host cell. Moreover, the polypeptides of the present invention can be used to test the following biological activities. Biological Activities The polynucleotides and polypeptides of the present invention can be used in assays to test for one or more biological activities. If these polynucleotides and polypeptides do exhibit activity in a particular assay, it is likely that these molecules may be involved in the diseases associated with the biological activity. Thus, the polynucleotides and polypeptides could be used to treat the associated disease. Immune Activity A polypeptide or polynucleotide of the present invention may be useful in treating deficiencies or disorders of the immune system, by activating or inhibiting the proliferation, differentiation, or mobilization (chemotaxis) of immune cells. Immune cells develop through a process called hematopoiesis, producing myeloid (platelets, red blood cells, neutrophils, and macrophages) and lymphoid (B and T lymphocytes) cells from pluripotent stem cells. The etiology of these immune deficiencies or disorders may be genetic, somatic, such as cancer or some autoimmune disorders, acquired (e.g., by chemotherapy or toxins), or infectious. Moreover, a polynucleotide or polypeptide of the present invention can be used as a marker or detector of a particular immune system disease or disorder. A polynucleotide or polypeptide of the present invention may be useful in treating or detecting deficiencies or disorders of hematopoietic cells. A polypeptide or 91 polynucleotide of the present invention could be used to increase differentiation and proliferation of hematopoietic cells, including the pluripotent stem cells, in an effort to treat those disorders associated with a decrease in certain (or many) types hematopoietic cells. Examples of immunologic deficiency syndromes include, but are not limited to: blood protein disorders (e.g. agammaglobulinemia, dysgammaglobulinemia), ataxia telangiectasia, common variable immunodeficiency, Digeorge Syndrome, HIV infection, HTLV-BLV infection, leukocyte adhesion deficiency syndrome, lymphopenia, phagocyte bactericidal dysfunction, severe combined immunodeficiency (SCIDs), Wiskott-Aldrich Disorder, anemia, thrombocytopenia, or hemoglobinuria. Moreover, a polypeptide or polynucleotide of the present invention could also be used to modulate hemostatic (the stopping of bleeding) or thrombolytic activity (clot formation). For example, by increasing hemostatic or thrombolytic activity, a polynucleotide or polypeptide of the present invention could be used to treat blood coagulation disorders (e.g., afibrinogenemia, factor deficiencies), blood platelet disorders (e.g. thrombocytopenia), or wounds resulting from trauma, surgery, or other causes. Alternatively, a polynucleotide or polypeptide of the present invention that can decrease hemostatic or thrombolytic activity could be used to inhibit or dissolve clotting. These molecules could be important in the treatment of heart attacks (infarction), strokes, or scarring. A polynucleotide or polypeptide of the present invention may also be useful in treating or detecting autoimmune disorders. Many autoimmune disorders result from inappropriate recognition of self as foreign material by immune cells. This inappropriate recognition results in an immune response leading to the destruction of the host tissue. Therefore, the administration of a polypeptide or polynucleotide of the present invention that inhibits an immune response, particularly the proliferation, differentiation, or chemotaxis of T-cells, may be an effective therapy in preventing autoimmune disorders. Examples of autoimmune disorders that can be treated or detected by the present invention include, but are not limited to: Addison's Disease, hemolytic anemia, antiphospholipid syndrome, rheumatoid arthritis, dermatitis, allergic encephalomyelitis, glomerulonephritis, Goodpasture's Syndrome, Graves' Disease, Multiple Sclerosis, Myasthenia Gravis, Neuritis, Ophthalmia, Bullous Pemphigoid, Pemphigus, Polyendocrinopathies, Purpura, Reiter's Disease, Stiff-Man Syndrome, Autoimmune Thyroiditis, Systemic Lupus Erythematosus, Autoimmune Pulmonary Inflammation, Guillain-Barre Syndrome, insulin dependent diabetes mellitis, and autoimmune inflammatory eye disease. 92 Similarly, allergic reactions and conditions, such as asthma (particularly allergic asthma) or other respiratory problems, may also be treated by a polypeptide or polynucleotide of the present invention. Moreover, these molecules can be used to treat anaphylaxis, hypersensitivity to an antigenic molecule, or blood group incompatibility. A polynucleotide or polypeptide of the present invention may also be used to treat and/or prevent organ rejection or graft-versus-host disease (GVHD). Organ rejection occurs by host immune cell destruction of the transplanted tissue through an immune response. Similarly, an immune response is also involved in GVHD, but, in this case, the foreign transplanted immune cells destroy the host tissues. The administration of a polypeptide or polynucleotide of the present invention that inhibits an immune response, particularly the proliferation, differentiation, or chemotaxis of T- cells, may be an effective therapy in preventing organ rejection or GVHD. Similarly, a polypeptide or polynucleotide of the present invention may also be used to modulate inflammation. For example, the polypeptide or polynucleotide may inhibit the proliferation and differentiation of cells involved in an inflammatory response. These molecules can be used to treat inflammatory conditions, both chronic and acute conditions, including inflammation associated with infection (e.g., septic shock, sepsis, or systemic inflammatory response syndrome (SIRS)), ischemia- reperfusion injury, endotoxin lethality, arthritis, complement-mediated hyperacute rejection, nephritis, cytokine or chemokine induced lung injury, inflammatory bowel disease, Crohn's disease, or resulting from over production of cytokines (e.g., TNF or IL-1.) Hvperproliferative Disorders A polypeptide or polynucleotide can be used to treat or detect hvperproliferative disorders, including neoplasms. A polypeptide or polynucleotide of the present invention may inhibit the proliferation of the disorder through direct or indirect interactions. Alternatively, a polypeptide or polynucleotide of the present invention may proliferate other cells which can inhibit the hyperproliferative disorder. For example, by increasing an immune response, particularly increasing antigenic qualities of the hyperproliferative disorder or by proliferating, differentiating, or mobilizing T-cells, hyperproliferative disorders can be treated. This immune response may be increased by either enhancing an existing immune response, or by initiating a new immune response. Alternatively, decreasing an immune response may also be a method of treating hypeφroliferative disorders, such as a chemotherapeutic agent. 93 Examples of hypeφroliferative disorders that can be treated or detected by a polynucleotide or polypeptide of the present invention include, but are not limited to neoplasms located in the: abdomen, bone, breast, digestive system, liver, pancreas, peritoneum, endocrine glands (adrenal, parathyroid, pituitary, testicles, ovary, thymus, thyroid), eye, head and neck, nervous (central and peripheral), lymphatic system, pelvic, skin, soft tissue, spleen, thoracic, and urogenital. Similarly, other hypeφroliferative disorders can also be treated or detected by a polynucleotide or polypeptide of the present invention. Examples of such hypeφroliferative disorders include, but are not limited to: hypergammaglobulinemia, lymphoproliferative disorders, paraproteinemias, puφura, sarcoidosis, Sezary Syndrome, Waldenstron's Macroglobulinemia, Gaucher's Disease, histiocytosis, and any other hypeφroliferative disease, besides neoplasia, located in an organ system listed above. Infectious Disease A polypeptide or polynucleotide of the present invention can be used to treat or detect infectious agents. For example, by increasing the immune response, particularly increasing the proliferation and differentiation of B and/or T cells, infectious diseases may be treated. The immune response may be increased by either enhancing an existing immune response, or by initiating a new immune response. Alternatively, the polypeptide or polynucleotide of the present invention may also directly inhibit the infectious agent, without necessarily eliciting an immune response. Viruses are one example of an infectious agent that can cause disease or symptoms that can be treated or detected by a polynucleotide or polypeptide of the present invention. Examples of viruses, include, but are not limited to the following DNA and RNA viral families: Arbovirus, Adenoviridae, Arenaviridae, Arterivirus, Birnaviridae, Bunyaviridae, Caliciviridae, Circoviridae, Coronaviridae, Flaviviridae, Hepadnaviridae (Hepatitis), Heφesviridae (such as, Cytomegalovirus, Heφes Simplex, Heφes Zoster), Mononegavirus (e.g., Paramyxoviridae, Morbillivirus, Rhabdoviridae), Orthomyxoviridae (e.g., Influenza), Papovaviridae, Parvoviridae, Picornaviridae, Poxviridae (such as Smallpox or Vaccinia), Reoviridae (e.g., Rotavirus), Retroviridae (HTLV-I, HTLV-II, Lentivirus), and Togaviridae (e.g., Rubivirus). Viruses falling within these families can cause a variety of diseases or symptoms, including, but not limited to: arthritis, bronchiollitis, encephalitis, eye infections (e.g., conjunctivitis, keratitis), chronic fatigue syndrome, hepatitis (A, B, C, E, Chronic Active, Delta), meningitis, opportunistic infections (e.g., AIDS), pneumonia, Burkitt's Lymphoma, chickenpox , hemorrhagic fever, Measles, Mumps, 94 Parainfluenza, Rabies, the common cold, Polio, leukemia, Rubella, sexually transmitted diseases, skin diseases (e.g., Kaposi's, warts), and viremia. A polypeptide or polynucleotide of the present invention can be used to treat or detect any of these symptoms or diseases. Similarly, bacterial or fungal agents that can cause disease or symptoms and that can be treated or detected by a polynucleotide or polypeptide of the present invention include, but not limited to, the following Gram-Negative and Gram-positive bacterial families and fungi: Actinomycetales (e.g., Corynebacterium, Mycobacterium, Norcardia), Aspergillosis, Bacillaceae (e.g., Anthrax, Clostridium), Bacteroidaceae, Blastomycosis, Bordetella, Borrelia, Brucellosis, Candidiasis, Campylobacter, Coccidioidomycosis, Cryptococcosis, Dermatocycoses, Enterobacteriaceae (Klebsiella, Salmonella, Serratia, Yersinia), Erysipelothrix, Helicobacter, Legionellosis, Leptospirosis, Listeria, Mycoplasmatales, Neisseriaceae (e.g., Acinetobacter, Gonorrhea, Menigococcal), Pasteurellacea Infections (e.g., Actinobacillus, Heamophilus, Pasteurella), Pseudomonas, Rickettsiaceae, Chlamydiaceae, Syphilis, and Staphylococcal. These bacterial or fungal families can cause the following diseases or symptoms, including, but not limited to: bacteremia, endocarditis, eye infections (conjunctivitis, tuberculosis, uveitis), gingivitis, opportunistic infections (e.g., AIDS related infections), paronychia, prosthesis-related infections, Reiter's Disease, respiratory tract infections, such as Whooping Cough or Empyema, sepsis, Lyme Disease, Cat-Scratch Disease, Dysentery, Paratyphoid Fever, food poisoning, Typhoid, pneumonia, Gonorrhea, meningitis, Chlamydia, Syphilis, Diphtheria, Leprosy, Paratuberculosis, Tuberculosis, Lupus, Botulism, gangrene, tetanus, impetigo, Rheumatic Fever, Scarlet Fever, sexually transmitted diseases, skin diseases (e.g., cellulitis, dermatocycoses), toxemia, urinary tract infections, wound infections. A polypeptide or polynucleotide of the present invention can be used to treat or detect any of these symptoms or diseases. Moreover, parasitic agents causing disease or symptoms that can be treated or detected by a polynucleotide or polypeptide of the present invention include, but not limited to, the following families: Amebiasis, Babesiosis, Coccidiosis, Cryptosporidiosis, Dientamoebiasis, Dourine, Ectoparasitic, Giardiasis, Helminthiasis, Leishmaniasis, Theileriasis, Toxoplasmosis, Trypanosomiasis, and Trichomonas. These parasites can cause a variety of diseases or symptoms, including, but not limited to: Scabies, Trombiculiasis, eye infections, intestinal disease (e.g., dysentery, giardiasis), liver disease, lung disease, opportunistic infections (e.g., AIDS related), Malaria, pregnancy complications, and toxoplasmosis. A polypeptide or polynucleotide 95 of the present invention can be used to treat or detect any of these symptoms or diseases. Preferably, treatment using a polypeptide or polynucleotide of the present invention could either be by administering an effective amount of a polypeptide to the patient, or by removing cells from the patient, supplying the cells with a polynucleotide of the present invention, and returning the engineered cells to the patient (ex vivo therapy). Moreover, the polypeptide or polynucleotide of the present invention can be used as an antigen in a vaccine to raise an immune response against infectious disease. Regeneration A polynucleotide or polypeptide of the present invention can be used to differentiate, proliferate, and attract cells, leading to the regeneration of tissues. (See, Science 276:59-87 (1997).) The regeneration of tissues could be used to repair, replace, or protect tissue damaged by congenital defects, trauma (wounds, burns, incisions, or ulcers), age, disease (e.g. osteoporosis, osteocarthritis, periodontal disease, liver failure), surgery, including cosmetic plastic surgery, fibrosis, reperfusion injury, or systemic cytokine damage. Tissues that could be regenerated using the present invention include organs (e.g., pancreas, liver, intestine, kidney, skin, endothelium), muscle (smooth, skeletal or cardiac), vasculature (including vascular and lymphatics), nervous, hematopoietic, and skeletal (bone, cartilage, tendon, and ligament) tissue. Preferably, regeneration occurs without or decreased scarring. Regeneration also may include angiogenesis. Moreover, a polynucleotide or polypeptide of the present invention may increase regeneration of tissues difficult to heal. For example, increased tendon/ligament regeneration would quicken recovery time after damage. A polynucleotide or polypeptide of the present invention could also be used prophylactically in an effort to avoid damage. Specific diseases that could be treated include of tendinitis, caφal tunnel syndrome, and other tendon or ligament defects. A further example of tissue regeneration of non-healing wounds includes pressure ulcers, ulcers associated with vascular insufficiency, surgical, and traumatic wounds. Similarly, nerve and brain tissue could also be regenerated by using a polynucleotide or polypeptide of the present invention to proliferate and differentiate nerve cells. Diseases that could be treated using this method include central and peripheral nervous system diseases, neuropathies, or mechanical and traumatic disorders (e.g., spinal cord disorders, head trauma, cerebrovascular disease, and stoke). Specifically, diseases associated with peripheral nerve injuries, peripheral neuropathy (e.g., resulting from chemotherapy or other medical therapies), localized 96 neuropathies, and central nervous system diseases (e.g., Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and Shy- Drager syndrome), could all be treated using the polynucleotide or polypeptide of the present invention. Chemotaxis A polynucleotide or polypeptide of the present invention may have chemotaxis activity. A chemotaxic molecule attracts or mobilizes cells (e.g., monocytes, fibroblasts, neutrophils, T-cells, mast cells, eosinophils, epithelial and/or endothelial cells) to a particular site in the body, such as inflammation, infection, or site of hypeφroliferation. The mobilized cells can then fight off and/or heal the particular trauma or abnormality. A polynucleotide or polypeptide of the present invention may increase chemotaxic activity of particular cells. These chemotactic molecules can then be used to treat inflammation, infection, hypeφroliferative disorders, or any immune system disorder by increasing the number of cells targeted to a particular location in the body. For example, chemotaxic molecules can be used to treat wounds and other trauma to tissues by attracting immune cells to the injured location. Chemotactic molecules of the present invention can also attract fibroblasts, which can be used to treat wounds. It is also contemplated that a polynucleotide or polypeptide of the present invention may inhibit chemotactic activity. These molecules could also be used to treat disorders. Thus, a polynucleotide or polypeptide of the present invention could be used as an inhibitor of chemotaxis. Binding Activity A polypeptide of the present invention may be used to screen for molecules that bind to the polypeptide or for molecules to which the polypeptide binds. The binding of the polypeptide and the molecule may activate (agonist), increase, inhibit (antagonist), or decrease activity of the polypeptide or the molecule bound. Examples of such molecules include antibodies, oligonucleotides, proteins (e.g., receptors),or small molecules. Preferably, the molecule is closely related to the natural ligand of the polypeptide, e.g., a fragment of the ligand, or a natural substrate, a ligand, a structural or functional mimetic. (See, Coligan et al., Current Protocols in Immunology l(2):Chapter 5 (1991).) Similarly, the molecule can be closely related to the natural receptor to which the polypeptide binds, or at least, a fragment of the receptor capable 97 of being bound by the polypeptide (e.g., active site). In either case, the molecule can be rationally designed using known techniques. Preferably, the screening for these molecules involves producing appropriate cells which express the polypeptide, either as a secreted protein or on the cell membrane. Preferred cells include cells from mammals, yeast, Drosophila, or E. coli. Cells expressing the polypeptide (or cell membrane containing the expressed polypeptide) are then preferably contacted with a test compound potentially containing the molecule to observe binding, stimulation, or inhibition of activity of either the polypeptide or the molecule. The assay may simply test binding of a candidate compound to the polypeptide, wherein binding is detected by a label, or in an assay involving competition with a labeled competitor. Further, the assay may test whether the candidate compound results in a signal generated by binding to the polypeptide. Alternatively, the assay can be carried out using cell-free preparations, polypeptide/molecule affixed to a solid support, chemical libraries, or natural product mixtures. The assay may also simply comprise the steps of mixing a candidate compound with a solution containing a polypeptide, measuring polypeptide/molecule activity or binding, and comparing the polypeptide/molecule activity or binding to a standard. Preferably, an ΕLISA assay can measure polypeptide level or activity in a sample (e.g., biological sample) using a monoclonal or polyclonal antibody. The antibody can measure polypeptide level or activity by either binding, directly or indirectly, to the polypeptide or by competing with the polypeptide for a substrate. All of these above assays can be used as diagnostic or prognostic markers. The molecules discovered using these assays can be used to treat disease or to bring about a particular result in a patient (e.g., blood vessel growth) by activating or inhibiting the polypeptide/molecule. Moreover, the assays can discover agents which may inhibit or enhance the production of the polypeptide from suitably manipulated cells or tissues. Therefore, the invention includes a method of identifying compounds which bind to a polypeptide of the invention comprising the steps of: (a) incubating a candidate binding compound with a polypeptide of the invention; and (b) determining if binding has occurred. Moreover, the invention includes a method of identifying agonists/antagonists comprising the steps of: (a) incubating a candidate compound with a polypeptide of the invention, (b) assaying a biological activity , and (b) determining if a biological activity of the polypeptide has been altered. 98 Other Activities A polypeptide or polynucleotide of the present invention may also increase or decrease the differentiation or proliferation of embryonic stem cells, besides, as discussed above, hematopoietic lineage. A polypeptide or polynucleotide of the present invention may also be used to modulate mammalian characteristics, such as body height, weight, hair color, eye color, skin, percentage of adipose tissue, pigmentation, size, and shape (e.g., cosmetic surgery). Similarly, a polypeptide or polynucleotide of the present invention may be used to modulate mammalian metabolism affecting catabolism, anabolism, processing, utilization, and storage of energy. A polypeptide or polynucleotide of the present invention may be used to change a mammal's mental state or physical state by influencing biorhythms, caricadic rhythms, depression (including depressive disorders), tendency for violence, tolerance for pain, reproductive capabilities (preferably by Activin or Inhibin-like activity), hormonal or endocrine levels, appetite, libido, memory, stress, or other cognitive qualities. A polypeptide or polynucleotide of the present invention may also be used as a food additive or preservative, such as to increase or decrease storage capabilities, fat content, lipid, protein, carbohydrate, vitamins, minerals, cofactors or other nutritional components. Other Preferred Embodiments Other preferred embodiments of the claimed invention include an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a sequence of at least about 50 contiguous nucleotides in the nucleotide sequence of SEQ ID NO:X wherein X is any integer as defined in Table 1. Also preferred is a nucleic acid molecule wherein said sequence of contiguous nucleotides is included in the nucleotide sequence of SEQ LD NO:X in the range of positions beginning with the nucleotide at about the position of the 5' Nucleotide of the Clone Sequence and ending with the nucleotide at about the position of the 3' Nucleotide of the Clone Sequence as defined for SEQ ID NO:X in Table 1. Also preferred is a nucleic acid molecule wherein said sequence of contiguous nucleotides is included in the nucleotide sequence of SEQ LD NO:X in the range of positions beginning with the nucleotide at about the position of the 5' Nucleotide of the Start Codon and ending with the nucleotide at about the position of the 3' Nucleotide of the Clone Sequence as defined for SEQ ED NO:X in Table 1. 99 Similarly preferred is a nucleic acid molecule wherein said sequence of contiguous nucleotides is included in the nucleotide sequence of SEQ ED NO:X in the range of positions beginning with the nucleotide at about the position of the 5' Nucleotide of the First Amino Acid of the Signal Peptide and ending with the nucleotide at about the position of the 3' Nucleotide of the Clone Sequence as defined for SEQ ID NO:X in Table 1. Also preferred is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a sequence of at least about 150 contiguous nucleotides in the nucleotide sequence of SEQ ID NO:X. Further preferred is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a sequence of at least about 500 contiguous nucleotides in the nucleotide sequence of SEQ ID NO:X. A further preferred embodiment is a nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to the nucleotide sequence of SEQ ID NO:X beginning with the nucleotide at about the position of the 5' Nucleotide of the First Amino Acid of the Signal Peptide and ending with the nucleotide at about the position of the 3' Nucleotide of the Clone Sequence as defined for SEQ LD NO:X in Table 1. A further preferred embodiment is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to the complete nucleotide sequence of SEQ ID NO:X. Also preferred is an isolated nucleic acid molecule which hybridizes under stringent hybridization conditions to a nucleic acid molecule, wherein said nucleic acid molecule which hybridizes does not hybridize under stringent hybridization conditions to a nucleic acid molecule having a nucleotide sequence consisting of only A residues or of only T residues. Also preferred is a composition of matter comprising a DNA molecule which comprises a human cDNA clone identified by a cDNA Clone Identifier in Table 1, which DNA molecule is contained in the material deposited with the American Type Culture Collection and given the ATCC Deposit Number shown in Table 1 for said cDNA Clone Identifier. Also preferred is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a sequence of at least 50 contiguous nucleotides in the nucleotide sequence of a human cDNA clone identified by a cDNA Clone Identifier in Table 1, which DNA molecule is contained in the deposit given the ATCC Deposit Number shown in Table 1. 100 Also preferred is an isolated nucleic acid molecule, wherein said sequence of at least 50 contiguous nucleotides is included in the nucleotide sequence of the complete open reading frame sequence encoded by said human cDNA clone. Also preferred is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to sequence of at least 150 contiguous nucleotides in the nucleotide sequence encoded by said human cDNA clone. A further preferred embodiment is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to sequence of at least 500 contiguous nucleotides in the nucleotide sequence encoded by said human cDNA clone. A further preferred embodiment is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to the complete nucleotide sequence encoded by said human cDNA clone. A further preferred embodiment is a method for detecting in a biological sample a nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from the group consisting of: a nucleotide sequence of SEQ ID NO:X wherein X is any integer as defined in Table 1; and a nucleotide sequence encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1 ; which method comprises a step of comparing a nucleotide sequence of at least one nucleic acid molecule in said sample with a sequence selected from said group and determining whether the sequence of said nucleic acid molecule in said sample is at least 95% identical to said selected sequence. Also preferred is the above method wherein said step of comparing sequences comprises determining the extent of nucleic acid hybridization between nucleic acid molecules in said sample and a nucleic acid molecule comprising said sequence selected from said group. Similarly, also preferred is the above method wherein said step of comparing sequences is performed by comparing the nucleotide sequence determined from a nucleic acid molecule in said sample with said sequence selected from said group. The nucleic acid molecules can comprise DNA molecules or RNA molecules. A further preferred embodiment is a method for identifying the species, tissue or cell type of a biological sample which method comprises a step of detecting nucleic acid molecules in said sample, if any, comprising a nucleotide sequence that is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from the group consisting of: a nucleotide sequence of SEQ ID NO:X wherein X is any integer as defined in Table 1; and a nucleotide sequence encoded by a human cDNA 101 clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. The method for identifying the species, tissue or cell type of a biological sample can comprise a step of detecting nucleic acid molecules comprising a nucleotide sequence in a panel of at least two nucleotide sequences, wherein at least one sequence in said panel is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from said group. Also preferred is a method for diagnosing in a subject a pathological condition associated with abnormal structure or expression of a gene encoding a secreted protein identified in Table 1 , which method comprises a step of detecting in a biological sample obtained from said subject nucleic acid molecules, if any, comprising a nucleotide sequence that is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from the group consisting of: a nucleotide sequence of SEQ ID NO:X wherein X is any integer as defined in Table 1 ; and a nucleotide sequence encoded by a human cDN A clone identified by a cDN A Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. The method for diagnosing a pathological condition can comprise a step of detecting nucleic acid molecules comprising a nucleotide sequence in a panel of at least two nucleotide sequences, wherein at least one sequence in said panel is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from said group. Also preferred is a composition of matter comprising isolated nucleic acid molecules wherein the nucleotide sequences of said nucleic acid molecules comprise a panel of at least two nucleotide sequences, wherein at least one sequence in said panel is at least 95% identical to a sequence of at least 50 contiguous nucleotides in a sequence selected from the group consisting of: a nucleotide sequence of SEQ LD NO:X wherein X is any integer as defined in Table 1; and a nucleotide sequence encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. The nucleic acid molecules can comprise DNA molecules or RNA molecules. Also preferred is an isolated polypeptide comprising an amino acid sequence at least 90% identical to a sequence of at least about 10 contiguous amino acids in the amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1. Also preferred is a polypeptide, wherein said sequence of contiguous amino acids is included in the amino acid sequence of SEQ ID NO:Y in the range of positions beginning with the residue at about the position of the First Amino Acid of the Secreted 102 Portion and ending with the residue at about the Last Amino Acid of the Open Reading Frame as set forth for SEQ ID NO: Y in Table 1. Also preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to a sequence of at least about 30 contiguous amino acids in the amino acid sequence of SEQ ED NO:Y. Further preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to a sequence of at least about 100 contiguous amino acids in the amino acid sequence of SEQ ID NO:Y. Further preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to the complete amino acid sequence of SEQ ID NO:Y. Further preferred is an isolated polypeptide comprising an amino acid sequence at least 90% identical to a sequence of at least about 10 contiguous amino acids in the complete amino acid sequence of a secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is a polypeptide wherein said sequence of contiguous amino acids is included in the amino acid sequence of a secreted portion of the secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to a sequence of at least about 30 contiguous amino acids in the amino acid sequence of the secreted portion of the protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to a sequence of at least about 100 contiguous amino acids in the amino acid sequence of the secreted portion of the protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is an isolated polypeptide comprising an amino acid sequence at least 95% identical to the amino acid sequence of the secreted portion of the protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Further preferred is an isolated antibody which binds specifically to a polypeptide comprising an amino acid sequence that is at least 90% identical to a 103 sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Further preferred is a method for detecting in a biological sample a polypeptide comprising an amino acid sequence which is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1 ; which method comprises a step of comparing an amino acid sequence of at least one polypeptide molecule in said sample with a sequence selected from said group and determining whether the sequence of said polypeptide molecule in said sample is at least 90% identical to said sequence of at least 10 contiguous amino acids. Also preferred is the above method wherein said step of comparing an amino acid sequence of at least one polypeptide molecule in said sample with a sequence- selected from said group comprises determining the extent of specific binding of polypeptides in said sample to an antibody which binds specifically to a polypeptide comprising an amino acid sequence that is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is the above method wherein said step of comparing sequences is performed by comparing the amino acid sequence determined from a polypeptide molecule in said sample with said sequence selected from said group. Also preferred is a method for identifying the species, tissue or cell type of a biological sample which method comprises a step of detecting polypeptide molecules in said sample, if any, comprising an amino acid sequence that is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. 104 Also preferred is the above method for identifying the species, tissue or cell type of a biological sample, which method comprises a step of detecting polypeptide molecules comprising an amino acid sequence in a panel of at least two amino acid sequences, wherein at least one sequence in said panel is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the above group. Also preferred is a method for diagnosing in a subject a pathological condition associated with abnormal structure or expression of a gene encoding a secreted protein identified in Table 1, which method comprises a step of detecting in a biological sample obtained from said subject polypeptide molecules comprising an amino acid sequence in a panel of at least two amino acid sequences, wherein at least one sequence in said panel is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO:Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDN A clone in Table 1. In any of these methods, the step of detecting said polypeptide molecules includes using an antibody. Also preferred is an isolated nucleic acid molecule comprising a nucleotide sequence which is at least 95% identical to a nucleotide sequence encoding a polypeptide wherein said polypeptide comprises an amino acid sequence that is at least 90% identical to a sequence of at least 10 contiguous amino acids in a sequence selected from the group consisting of: an amino acid sequence of SEQ ID NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. Also preferred is an isolated nucleic acid molecule, wherein said nucleotide sequence encoding a polypeptide has been optimized for expression of said polypeptide in a prokaryotic host. Also preferred is an isolated nucleic acid molecule, wherein said polypeptide comprises an amino acid sequence selected from the group consisting of: an amino acid sequence of SEQ LD NO: Y wherein Y is any integer as defined in Table 1 ; and a complete amino acid sequence of a secreted protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. 105 Further preferred is a method of making a recombinant vector comprising inserting any of the above isolated nucleic acid molecule into a vector. Also preferred is the recombinant vector produced by this method. Also preferred is a method of making a recombinant host cell comprising introducing the vector into a host cell, as well as the recombinant host cell produced by this method. Also preferred is a method of making an isolated polypeptide comprising culturing this recombinant host cell under conditions such that said polypeptide is expressed and recovering said polypeptide. Also preferred is this method of making an isolated polypeptide, wherein said recombinant host cell is a eukaryotic cell and said polypeptide is a secreted portion of a human secreted protein comprising an amino acid sequence selected from the group consisting of: an amino acid sequence of SEQ ED NO: Y beginning with the residue at the position of the First Amino Acid of the Secreted Portion of SEQ ID NO:Y wherein Y is an integer set forth in Table 1 and said position of the First Amino Acid of the Secreted Portion of SEQ ID NO: Y is defined in Table 1 ; and an amino acid sequence of a secreted portion of a protein encoded by a human cDNA clone identified by a cDNA Clone Identifier in Table 1 and contained in the deposit with the ATCC Deposit Number shown for said cDNA clone in Table 1. The isolated polypeptide produced by this method is also preferred. Also preferred is a method of treatment of an individual in need of an increased level of a secreted protein activity, which method comprises administering to such an individual a pharmaceutical composition comprising an amount of an isolated polypeptide, polynucleotide, or antibody of the claimed invention effective to increase the level of said protein activity in said individual. Having generally described the invention, the same will be more readily understood by reference to the following examples, which are provided by way of illustration and are not intended as limiting. Examples Example 1: Isolation of a Selected cDNA Clone From the Deposited Sample Each cDNA clone in a cited ATCC deposit is contained in a plasmid vector. Table 1 identifies the vectors used to construct the cDNA library from which each clone was isolated. In many cases, the vector used to construct the library is a phage vector from which a plasmid has been excised. The table immediately below correlates the related plasmid for each phage vector used in constructing the cDNA library. For 106 example, where a particular clone is identified in Table 1 as being isolated in the vector "Lambda Zap," the corresponding deposited clone is in "pBluescript." Vector Used to Construct Library Corresponding Deposited Plasmid Lambda Zap pBluescript (pBS) Uni-Zap XR pBluescript (pBS) Zap Express pBK lafmid BA plafmid B A pSportl pSportl pCMVSport 2.0 pCMVSport 2.0 pCMVSport 3.0 pCMVSport 3.0 pCR ® 2.1 pCR ® 2.1 Vectors Lambda Zap (U.S. Patent Nos. 5,128,256 and 5,286,636), Uni-Zap XR (U.S. Patent Nos. 5,128, 256 and 5,286,636), Zap Express (U.S. Patent Nos. 5,128,256 and 5,286,636), pBluescript (pBS) (Short, J. M. et al., Nucleic Acids Res. 16:7583-7600 (1988); Alting-Mees, M. A. and Short, J. M., Nucleic Acids Res. 17:9494 (1989)) and pBK (Alting-Mees, M. A. et al., Strategies 5:58-61 (1992)) are commercially available from Stratagene Cloning Systems, Inc., 11011 N. Torrey Pines Road, La Jolla, CA, 92037. pBS contains an ampicillin resistance gene and pBK contains a neomycin resistance gene. Both can be transformed into E. coli strain XL-1 Blue, also available from Stratagene. pBS comes in 4 forms SK+, SK-, KS+ and KS. The S and K refers to the orientation of the polylinker to the T7 and T3 primer sequences which flank the polylinker region ("S" is for Sad and "K" is for Kpnl which are the first sites on each respective end of the linker). "+" or "-" refer to the orientation of the fl origin of replication ("ori"), such that in one orientation, single stranded rescue initiated from the f 1 ori generates sense strand DNA and in the other, antisense. Vectors pSportl, pCMVSport 2.0 and pCMVSport 3.0, were obtained from Life Technologies, Inc., P. O. Box 6009, Gaithersburg, MD 20897. All Sport vectors contain an ampicillin resistance gene and may be transformed into E. coli strain DH10B, also available from Life Technologies. (See, for instance, Gruber, C. E., et al., Focus 15:59 (1993).) Vector lafmid BA (Bento Soares, Columbia University, NY) contains an ampicillin resistance gene and can be transformed into E. coli strain XL-1 Blue. Vector pCR ® 2.1, which is available from Invitrogen, 1600 Faraday Avenue, Carlsbad, CA 92008, contains an ampicillin resistance gene and may be transformed into E. coli strain DH10B, available from Life Technologies. (See, for instance, Clark, J. M., Nuc. Acids Res. 16:9677-9686 (1988) and Mead, D. et al., Bio/Technology 9: (1991).) Preferably, a polynucleotide of the present invention does not comprise the 107 phage vector sequences identified for the particular clone in Table 1 , as well as the corresponding plasmid vector sequences designated above. The deposited material in the sample assigned the ATCC Deposit Number cited in Table 1 for any given cDNA clone also may contain one or more additional plasmids, each comprising a cDNA clone different from that given clone. Thus, deposits sharing the same ATCC Deposit Number contain at least a plasmid for each cDNA clone identified in Table 1. Typically, each ATCC deposit sample cited in Table 1 comprises a mixture of approximately equal amounts (by weight) of about 50 plasmid DNAs, each containing a different cDNA clone; but such a deposit sample may include plasmids for more or less than 50 cDNA clones, up to about 500 cDNA clones. Two approaches can be used to isolate a particular clone from the deposited sample of plasmid DNAs cited for that clone in Table 1. First, a plasmid is directly isolated by screening the clones using a polynucleotide probe corresponding to SEQ ID NO:X. Particularly, a specific polynucleotide with 30-40 nucleotides is synthesized using an Applied Biosystems DNA synthesizer according to the sequence reported. The oligonucleotide is labeled, for instance, with 32 P-γ-ATP using T4 polynucleotide kinase and purified according to routine methods. (E.g., Maniatis et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Press, Cold Spring, NY (1982).) The plasmid mixture is transformed into a suitable host, as indicated above (such as XL-1 Blue (Stratagene)) using techniques known to those of skill in the art, such as those provided by the vector supplier or in related publications or patents cited above. The transformants are plated on 1.5% agar plates (containing the appropriate selection agent, e.g., ampicillin) to a density of about 150 transformants (colonies) per plate. These plates are screened using Nylon membranes according to routine methods for bacterial colony screening (e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Edit., (1989), Cold Spring Harbor Laboratory Press, pages 1.93 to 1.104), or other techniques known to those of skill in the art. Alternatively, two primers of 17-20 nucleotides derived from both ends of the SEQ ID NO:X (i.e., within the region of SEQ ID NO:X bounded by the 5' NT and the 3' NT of the clone defined in Table 1) are synthesized and used to amplify the desired cDNA using the deposited cDNA plasmid as a template. The polymerase chain reaction is carried out under routine conditions, for instance, in 25 μl of reaction mixture with 0.5 ug of the above cDNA template. A convenient reaction mixture is 1.5-5 mM MgCl 2 , 0.01% (w/v) gelatin, 20 μM each of dATP, dCTP, dGTP, dTTP, 25 pmol of each primer and 0.25 Unit of Taq polymerase. Thirty five cycles of PCR (denaturation 108 at 94°C for 1 min; annealing at 55°C for 1 min; elongation at 72°C for 1 min) are performed with a Perkin-Elmer Cetus automated thermal cycler. The amplified product is analyzed by agarose gel electrophoresis and the DNA band with expected molecular weight is excised and purified. The PCR product is verified to be the selected sequence by subcloning and sequencing the DNA product. Several methods are available for the identification of the 5' or 3' non-coding portions of a gene which may not be present in the deposited clone. These methods include but are not limited to, filter probing, clone enrichment using specific probes, and protocols similar or identical to 5' and 3' "RACE" protocols which are well known in the art. For instance, a method similar to 5' RACE is available for generating the missing 5' end of a desired full-length transcript. (Fromont-Racine et al., Nucleic Acids Res. 21(7): 1683-1684 (1993).) Briefly, a specific RNA oligonucleotide is ligated to the 5' ends of a population of RNA presumably containing full-length gene RNA transcripts. A primer set containing a primer specific to the ligated RNA oligonucleotide and a primer specific to a known sequence of the gene of interest is used to PCR amplify the 5' portion of the desired full-length gene. This amplified product may then be sequenced and used to generate the full length gene. This above method starts with total RNA isolated from the desired source, although poly-A-i- RNA can be used. The RNA preparation can then be treated with phosphatase if necessary to eliminate 5' phosphate groups on degraded or damaged RNA which may interfere with the later RNA ligase step. The phosphatase should then be inactivated and the RNA treated with tobacco acid pyrophosphatase in order to remove the cap structure present at the 5' ends of messenger RNAs. This reaction leaves a 5' phosphate group at the 5' end of the cap cleaved RNA which can then be ligated to an RNA oligonucleotide using T4 RNA ligase. This modified RNA preparation is used as a template for first strand cDNA synthesis using a gene specific oligonucleotide. The first strand synthesis reaction is used as a template for PCR amplification of the desired 5' end using a primer specific to the ligated RNA oligonucleotide and a primer specific to the known sequence of the gene of interest. The resultant product is then sequenced and analyzed to confirm that the 5' end sequence belongs to the desired gene. Example 2: Isolation of Genomic Clones Corresponding to a Polynucleotide 109 A human genomic PI library (Genomic Systems, Inc.) is screened by PCR using primers selected for the cDNA sequence corresponding to SEQ ID NO:X., according to the method described in Example 1. (See also, Sambrook.) Example 3: Tissue Distribution of Polypeptide Tissue distribution of mRNA expression of polynucleotides of the present invention is determined using protocols for Northern blot analysis, described by, among others, Sambrook et al. For example, a cDNA probe produced by the method described in Example 1 is labeled with P 32 using the rediprime™ DNA labeling system (Amersham Life Science), according to manufacturer's instructions. After labeling, the probe is purified using CHROMA SPEN-100™ column (Clontech Laboratories, Inc.), according to manufacturer's protocol number PT 1200-1. The purified labeled probe is then used to examine various human tissues for mRNA expression. Multiple Tissue Northern (MTN) blots containing various human tissues (H) or human immune system tissues (IM) (Clontech) are examined with the labeled probe using ExpressHyb™ hybridization solution (Clontech) according to manufacturer's protocol number PT1190-1. Following hybridization and washing, the blots are mounted and exposed to film at -70°C overnight, and the films developed according to standard procedures. Example 4: Chromosomal Mapping of the Polynucleotides An oligonucleotide primer set is designed according to the sequence at the 5' end of SEQ ID NO:X. This primer preferably spans about 100 nucleotides. This primer set is then used in a polymerase chain reaction under the following set of conditions : 30 seconds, 95°C; 1 minute, 56°C; 1 minute, 70°C. This cycle is repeated 32 times followed by one 5 minute cycle at 70°C. Human, mouse, and hamster DNA is used as template in addition to a somatic cell hybrid panel containing individual chromosomes or chromosome fragments (Bios, Inc). The reactions is analyzed on either 8% polyacrylamide gels or 3.5 % agarose gels. Chromosome mapping is determined by the presence of an approximately 100 bp PCR fragment in the particular somatic cell hybrid. Example 5: Bacterial Expression of a Polypeptide A polynucleotide encoding a polypeptide of the present invention is amplified using PCR oligonucleotide primers corresponding to the 5' and 3' ends of the DNA 110 sequence, as outlined in Example 1, to synthesize insertion fragments. The primers used to amplify the cDNA insert should preferably contain restriction sites, such as BamHI and Xbal, at the 5' end of the primers in order to clone the amplified product into the expression vector. For example, BamHI and Xbal correspond to the restriction enzyme sites on the bacterial expression vector pQE-9. (Qiagen, Inc., Chatsworth, CA). This plasmid vector encodes antibiotic resistance (Amp r ), a bacterial origin of replication (ori), an IPTG-regulatable promoter/operator (P/O), a ribosome binding site (RBS), a 6-histidine tag (6-His), and restriction enzyme cloning sites. The pQE-9 vector is digested with BamHI and Xbal and the amplified fragment is ligated into the pQE-9 vector maintaining the reading frame initiated at the bacterial RBS. The ligation mixture is then used to transform the E. coli strain M15/rep4 (Qiagen, Inc.) which contains multiple copies of the plasmid pREP4, which expresses the lad repressor and also confers kanamycin resistance (Kan r ). Transformants are identified by their ability to grow on LB plates and ampicillin/kanamycin resistant colonies are selected. Plasmid DNA is isolated and confirmed by restriction analysis. Clones containing the desired constructs are grown overnight (O/N) in liquid culture in LB media supplemented with both Amp (100 ug/ml) and Kan (25 ug/ml). The O/N culture is used to inoculate a large culture at a ratio of 1 : 100 to 1 :250. The cells are grown to an optical density 600 (O.D. 600 ) of between 0.4 and 0.6. IPTG (Isopropyl-B-D-thiogalacto pyranoside) is then added to a final concentration of 1 mM. IPTG induces by inactivating the lad repressor, clearing the P/O leading to increased gene expression. Cells are grown for an extra 3 to 4 hours. Cells are then harvested by centrifugation (20 mins at 6000Xg). The cell pellet is solubilized in the chaotropic agent 6 Molar Guanidine HC1 by stirring for 3-4 hours at 4°C. The cell debris is removed by centrifugation, and the supernatant containing the polypeptide is loaded onto a nickel-nitrilo-tri-acetic acid ("Ni-NTA") affinity resin column (available from QIAGEN, Inc., supra). Proteins with a 6 x His tag bind to the Ni-NTA resin with high affinity and can be purified in a simple one-step procedure (for details see: The QIAexpressionist (1995) QIAGEN, Inc., supra). Briefly, the supernatant is loaded onto the column in 6 M guanidine-HCl, pH 8, the column is first washed with 10 volumes of 6 M guanidine-HCl, pH 8, then washed with 10 volumes of 6 M guanidine-HCl pH 6, and finally the polypeptide is eluted with 6 M guanidine-HCl, pH 5. The purified protein is then renatured by dialyzing it against phosphate-buffered saline (PBS) or 50 mM Na-acetate, pH 6 buffer plus 200 mM NaCl. Alternatively, the 111 protein can be successfully refolded while immobilized on the Ni-NTA column. The recommended conditions are as follows: renature using a linear 6M-1M urea gradient in 500 mM NaCl, 20% glycerol, 20 mM Tris/HCl pH 7.4, containing protease inhibitors. The renaturation should be performed over a period of 1.5 hours or more. After renaturation the proteins are eluted by the addition of 250 mM immidazole. Immidazole is removed by a final dialyzing step against PBS or 50 mM sodium acetate pH 6 buffer plus 200 mM NaCl. The purified protein is stored at 4° C or frozen at -80° C. In addition to the above expression vector, the present invention further includes an expression vector comprising phage operator and promoter elements operatively linked to a polynucleotide of the present invention, called pHE4a. (ATCC Accession Number 209645, deposited on February 25, 1998.) This vector contains: 1) a neomycinphosphotransferase gene as a selection marker, 2) an E. coli origin of replication, 3) a T5 phage promoter sequence, 4) two lac operator sequences, 5) a Shine -Delgarno sequence, and 6) the lactose operon repressor gene (laclq). The origin of replication (oriC) is derived from pUC19 (LTI, Gaithersburg, MD). The promoter sequence and operator sequences are made synthetically. DNA can be inserted into the pHEa by restricting the vector with Ndel and Xbal, BamHI, Xhol, or Asp718, running the restricted product on a gel, and isolating the larger fragment (the stuffer fragment should be about 310 base pairs). The DNA insert is generated according to the PCR protocol described in Example 1, using PCR primers having restriction sites for Ndel (5' primer) and Xbal, BamHI, Xhol, or Asp718 (3' primer). The PCR insert is gel purified and restricted with compatible enzymes. The insert and vector are ligated according to standard protocols. The engineered vector could easily be substituted in the above protocol to express protein in a bacterial system. Example 6: Purification of a Polypeptide from an Inclusion Body The following alternative method can be used to purify a polypeptide expressed in E coli when it is present in the form of inclusion bodies. Unless otherwise specified, all of the following steps are conducted at 4-10°C. Upon completion of the production phase of the E. coli fermentation, the cell culture is cooled to 4-10°C and the cells harvested by continuous centrifugation at 15,000 φm (Heraeus Sepatech). On the basis of the expected yield of protein per unit weight of cell paste and the amount of purified protein required, an appropriate amount of cell paste, by weight, is suspended in a buffer solution containing 100 mM Tris, 50 112 mM EDTA, pH 7.4. The cells are dispersed to a homogeneous suspension using a high shear mixer. The cells are then lysed by passing the solution through a microfluidizer (Microfuidics, Coφ. or APV Gaulin, Inc.) twice at 4000-6000 psi. The homogenate is then mixed with NaCl solution to a final concentration of 0.5 M NaCl, followed by centrifugation at 7000 xg for 15 min. The resultant pellet is washed again using 0.5M NaCl, 100 mM Tris, 50 mM EDTA, pH 7.4. The resulting washed inclusion bodies are solubilized with 1.5 M guanidine hydrochloride (GuHCl) for 2-4 hours. After 7000 xg centrifugation for 15 min., the pellet is discarded and the polypeptide containing supernatant is incubated at 4°C overnight to allow further GuHCl extraction. Following high speed centrifugation (30,000 xg) to remove insoluble particles, the GuHCl solubilized protein is refolded by quickly mixing the GuHCl extract with 20 volumes of buffer containing 50 mM sodium, pH 4.5, 150 mM NaCl, 2 mM EDTA by vigorous stirring. The refolded diluted protein solution is kept at 4°C without mixing for 12 hours prior to further purification steps. To clarify the refolded polypeptide solution, a previously prepared tangential filtration unit equipped with 0.16 μm membrane filter with appropriate surface area (e.g., Filtron), equilibrated with 40 mM sodium acetate, pH 6.0 is employed. The filtered sample is loaded onto a cation exchange resin (e.g., Poros HS-50, Perseptive Biosystems). The column is washed with 40 mM sodium acetate, pH 6.0 and eluted with 250 mM, 500 mM, 1000 mM, and 1500 mM NaCl in the same buffer, in a stepwise manner. The absorbance at 280 nm of the effluent is continuously monitored. Fractions are collected and further analyzed by SDS-PAGE. Fractions containing the polypeptide are then pooled and mixed with 4 volumes of water. The diluted sample is then loaded onto a previously prepared set of tandem columns of strong anion (Poros HQ-50, Perseptive Biosystems) and weak anion (Poros CM-20, Perseptive Biosystems) exchange resins. The columns are equilibrated with 40 mM sodium acetate, pH 6.0. Both columns are washed with 40 mM sodium acetate, pH 6.0, 200 mM NaCl. The CM-20 column is then eluted using a 10 column volume linear gradient ranging from 0.2 M NaCl, 50 mM sodium acetate, pH 6.0 to 1.0 M NaCl, 50 mM sodium acetate, pH 6.5. Fractions are collected under constant A 280 monitoring of the effluent. Fractions containing the polypeptide (determined, for instance, by 16% SDS-PAGE) are then pooled. 113 The resultant polypeptide should exhibit greater than 95% purity after the above refolding and purification steps. No major contaminant bands should be observed from Commassie blue stained 16% SDS-PAGE gel when 5 μg of purified protein is loaded. The purified protein can also be tested for endotoxin/LPS contamination, and typically the LPS content is less than 0.1 ng/ml according to LAL assays. Example 7: Cloning and Expression of a Polypeptide in a Baculovirus Expression System In this example, the plasmid shuttle vector pA2 is used to insert a polynucleotide into a baculovirus to express a polypeptide. This expression vector contains the strong polyhedrin promoter of the Autographa californica nuclear polyhedrosis virus (AcMNPV) followed by convenient restriction sites such as BamHI, Xba I and Asp718. The polyadenylation site of the simian virus 40 ("SV40") is used for efficient polyadenylation. For easy selection of recombinant virus, the plasmid contains the beta-galactosidase gene from E. coli under control of a weak Drosophila promoter in the same orientation, followed by the polyadenylation signal of the polyhedrin gene. The inserted genes are flanked on both sides by viral sequences for cell-mediated homologous recombination with wild-type viral DNA to generate a viable virus that express the cloned polynucleotide. Many other baculovirus vectors can be used in place of the vector above, such as pAc373, pVL941, and pAcIMl, as one skilled in the art would readily appreciate, as long as the construct provides appropriately located signals for transcription, translation, secretion and the like, including a signal peptide and an in-frame AUG as required. Such vectors are described, for instance, in Luckow et al., Virology 170:31- 39 (1989). Specifically, the cDNA sequence contained in the deposited clone, including the AUG initiation codon and the naturally associated leader sequence identified in Table 1, is amplified using the PCR protocol described in Example 1. If the naturally occurring signal sequence is used to produce the secreted protein, the pA2 vector does not need a second signal peptide. Alternatively, the vector can be modified (pA2 GP) to include a baculovirus leader sequence, using the standard methods described in Summers et al., "A Manual of Methods for Baculovirus Vectors and Insect Cell Culture Procedures," Texas Agricultural Experimental Station Bulletin No. 1555 (1987). The amplified fragment is isolated from a 1% agarose gel using a commercially available kit ("Geneclean," BIO 101 Inc., La Jolla, Ca.). The fragment then is digested with appropriate restriction enzymes and again purified on a 1% agarose gel. 114 The plasmid is digested with the corresponding restriction enzymes and optionally, can be dephosphorylated using calf intestinal phosphatase, using routine procedures known in the art. The DNA is then isolated from a 1% agarose gel using a commercially available kit ("Geneclean" BIO 101 Inc., La Jolla, Ca.). The fragment and the dephosphorylated plasmid are ligated together with T4 DNA ligase. E. coli HB101 or other suitable E. coli hosts such as XL-1 Blue (Stratagene Cloning Systems, La Jolla, CA) cells are transformed with the ligation mixture and spread on culture plates. Bacteria containing the plasmid are identified by digesting DNA from individual colonies and analyzing the digestion product by gel electrophoresis. The sequence of the cloned fragment is confirmed by DNA sequencing. Five μg of a plasmid containing the polynucleotide is co-transfected with 1.0 μg of a commercially available linearized baculovirus DNA ("BaculoGold™ baculovirus DNA", Pharmingen, San Diego, CA), using the lipofection method described by Feigner et al., Proc. Natl. Acad. Sci. USA 84:7413-7417 (1987). One μg of BaculoGold™ virus DNA and 5 μg of the plasmid are mixed in a sterile well of a microtiter plate containing 50 μl of serum-free Grace's medium (Life Technologies Inc., Gaithersburg, MD). Afterwards, 10 μl Lipofectin plus 90 μl Grace's medium are added, mixed and incubated for 15 minutes at room temperature. Then the transfection mixture is added drop- wise to Sf9 insect cells (ATCC CRL 1711) seeded in a 35 mm tissue culture plate with 1 ml Grace's medium without serum. The plate is then incubated for 5 hours at 27° C. The transfection solution is then removed from the plate and 1 ml of Grace's insect medium supplemented with 10% fetal calf serum is added. Cultivation is then continued at 27° C for four days. After four days the supernatant is collected and a plaque assay is performed, as described by Summers and Smith, supra. An agarose gel with "Blue Gal" (Life Technologies Inc., Gaithersburg) is used to allow easy identification and isolation of gal-expressing clones, which produce blue-stained plaques. (A detailed description of a "plaque assay" of this type can also be found in the user's guide for insect cell culture and baculovirology distributed by Life Technologies Inc., Gaithersburg, page 9-10.) After appropriate incubation, blue stained plaques are picked with the tip of a micropipettor (e.g., Εppendorf). The agar containing the recombinant viruses is then resuspended in a microcentrifuge tube containing 200 μl of Grace's medium and the suspension containing the recombinant baculovirus is used to infect Sf9 cells seeded in 35 mm dishes. Four days later the supematants of these culture dishes are harvested and then they are stored at 4° C. 115 To verify the expression of the polypeptide, Sf9 cells are grown in Grace's medium supplemented with 10% heat-inactivated FΕS. The cells are infected with the recombinant baculovirus containing the polynucleotide at a multiplicity of infection ("MOI") of about 2. If radiolabeled proteins are desired, 6 hours later the medium is removed and is replaced with SF900 II medium minus methionine and cysteine (available from Life Technologies Inc., Rockville, MD). After 42 hours, 5 μCi of 5 S- methionine and 5 μCi 3:, S-cysteine (available from Amersham) are added. The cells are further incubated for 16 hours and then are harvested by centrifugation. The proteins in the supernatant as well as the intracellular proteins are analyzed by SDS-PAGE followed by autoradiography (if radiolabeled). Microsequencing of the amino acid sequence of the amino terminus of purified protein may be used to determine the amino terminal sequence of the produced protein. Example 8: Expression of a Polypeptide in Mammalian Cells The polypeptide of the present invention can be expressed in a mammalian cell. A typical mammalian expression vector contains a promoter element, which mediates the initiation of transcription of mRNA, a protein coding sequence, and signals required for the termination of transcription and polyadenylation of the transcript. Additional elements include enhancers, Kozak sequences and intervening sequences flanked by donor and acceptor sites for RNA splicing. Highly efficient transcription is achieved with the early and late promoters from SV40, the long terminal repeats (LTRs) from Retroviruses, e.g., RSV, HTLVI, HIVI and the early promoter of the cytomegalovirus (CMV). However, cellular elements can also be used (e.g., the human actin promoter). Suitable expression vectors for use in practicing the present invention include, for example, vectors such as pSVL and pMSG (Pharmacia, Uppsala, Sweden), pRSVcat (ATCC 37152), pSV2dhfr (ATCC 37146), pBC12MI (ATCC 67109), pCMVSport 2.0, and pCMVSport 3.0. Mammalian host cells that could be used include, human Hela, 293, H9 and Jurkat cells, mouse NIH3T3 and C127 cells, Cos 1, Cos 7 and CV1, quail QC1-3 cells, mouse L cells and Chinese hamster ovary (CHO) cells. Alternatively, the polypeptide can be expressed in stable cell lines containing the polynucleotide integrated into a chromosome. The co-transfection with a selectable marker such as dhfr, gpt, neomycin, hygromycin allows the identification and isolation of the transfected cells. The transfected gene can also be amplified to express large amounts of the encoded protein. The DHFR (dihydrofolate reductase) marker is useful in developing cell lines that carry several hundred or even several thousand copies of the gene of 116 interest. (See, e.g., Alt, F. W., et al., J. Biol. Chem. 253: 1357-1370 (1978); Hamlin, J. L. and Ma, C, Biochem. et Biophys. Acta, 1097:107-143 (1990); Page, M. J. and Sydenham, M. A., Biotechnology 9:64-68 (1991).) Another useful selection marker is the enzyme glutamine synthase (GS) (Muφhy et al., Biochem J. 227:277-279 (1991); Bebbington et al., Bio/Technology 10: 169-175 (1992). Using these markers, the mammalian cells are grown in selective medium and the cells with the highest resistance are selected. These cell lines contain the amplified gene(s) integrated into a chromosome. Chinese hamster ovary (CHO) and NSO cells are often used for the production of proteins. Derivatives of the plasmid pSV2-dhfr (ATCC Accession No. 37146), the expression vectors pC4 (ATCC Accession No. 209646) and pC6 (ATCC Accession No.209647) contain the strong promoter (LTR) of the Rous Sarcoma Virus (Cullen et al., Molecular and Cellular Biology, 438-447 (March, 1985)) plus a fragment of the CMV-enhancer (Boshart et al., Cell 41:521-530 (1985).) Multiple cloning sites, e.g., with the restriction enzyme cleavage sites BamHI, Xbal and Asp718, facilitate the cloning of the gene of interest. The vectors also contain the 3' intron, the polyadenylation and termination signal of the rat preproinsulin gene, and the mouse DHI^R gene under control of the SV40 early promoter. Specifically, the plasmid pC6, for example, is digested with appropriate restriction enzymes and then dephosphorylated using calf intestinal phosphates by procedures known in the art. The vector is then isolated from a 1% agarose gel. A polynucleotide of the present invention is amplified according to the protocol outlined in Example 1. If the naturally occurring signal sequence is used to produce the secreted protein, the vector does not need a second signal peptide. Alternatively, if the naturally occurring signal sequence is not used, the vector can be modified to include a heterologous signal sequence. (See, e.g., WO 96/34891.) The amplified fragment is isolated from a 1% agarose gel using a commercially available kit ("Geneclean," BIO 101 Inc., La Jolla, Ca.). The fragment then is digested with appropriate restriction enzymes and again purified on a 1% agarose gel. The amplified fragment is then digested with the same restriction enzyme and purified on a 1% agarose gel. The isolated fragment and the dephosphorylated vector are then ligated with T4 DNA ligase. E. coli HB101 or XL-1 Blue cells are then transformed and bacteria are identified that contain the fragment inserted into plasmid pC6 using, for instance, restriction enzyme analysis. Chinese hamster ovary cells lacking an active DHFR gene is used for transfection. Five μg of the expression plasmid pC6 is cotransfected with 0.5 μg of the plasmid pSVneo using lipofectin (Feigner et al., supra). The plasmid pSV2-neo 117 contains a dominant selectable marker, the neo gene from Tn5 encoding an enzyme that confers resistance to a group of antibiotics including G418. The cells are seeded in alpha minus MEM supplemented with 1 mg/ml G418. After 2 days, the cells are trypsinized and seeded in hybridoma cloning plates (Greiner, Germany) in alpha minus MEM supplemented with 10, 25, or 50 ng/ml of metothrexate plus 1 mg/ml G418. After about 10-14 days single clones are trypsinized and then seeded in 6-well petri dishes or 10 ml flasks using different concentrations of methotrexate (50 nM, 100 nM, 200 nM, 400 nM, 800 nM). Clones growing at the highest concentrations of methotrexate are then transferred to new 6-well plates containing even higher concentrations of methotrexate (1 μM, 2 μM, 5 μM, 10 mM, 20 mM). The same procedure is repeated until clones are obtained which grow at a concentration of 100 - 200 μM. Expression of the desired gene product is analyzed, for instance, by SDS- PAGE and Western blot or by reversed phase HPLC analysis. Example 9: Protein Fusions The polypeptides of the present invention are preferably fused to other proteins. These fusion proteins can be used for a variety of applications. For example, fusion of the present polypeptides to His-tag, HA-tag, protein A, IgG domains, and maltose binding protein facilitates purification. (See Example 5; see also EP A 394,827; Traunecker, et al., Nature 331:84-86 (1988).) Similarly, fusion to IgG-1, IgG-3, and albumin increases the halflife time in vivo. Nuclear localization signals fused to the polypeptides of the present invention can target the protein to a specific subcellular localization, while covalent heterodimer or homodimers can increase or decrease the activity of a fusion protein. Fusion proteins can also create chimeric molecules having more than one function. Finally, fusion proteins can increase solubility and or stability of the fused protein compared to the non-fused protein. All of the types of fusion proteins described above can be made by modifying the following protocol, which outlines the fusion of a polypeptide to an IgG molecule, or the protocol described in Example 5. Briefly, the human Fc portion of the IgG molecule can be PCR amplified, using primers that span the 5' and 3' ends of the sequence described below. These primers also should have convenient restriction enzyme sites that will facilitate cloning into an expression vector, preferably a mammalian expression vector. For example, if pC4 (Accession No. 209646) is used, the human Fc portion can be ligated into the BamHI cloning site. Note that the 3' BamHI site should be destroyed. Next, the vector containing the human Fc portion is re-restricted with BamHI, linearizing the vector, and a polynucleotide of the present invention, isolated 118 by the PCR protocol described in Example 1, is ligated into this BamHI site. Note that the polynucleotide is cloned without a stop codon, otherwise a fusion protein will not be produced. If the naturally occurring signal sequence is used to produce the secreted protein, pC4 does not need a second signal peptide. Alternatively, if the naturally occurring signal sequence is not used, the vector can be modified to include a heterologous signal sequence. (See, e.g., WO 96/34891.) Human IgG Fc region: GGGATCCGGAGCCC AAATCTTCTGAC AAAACTC AC AC ATGCCC ACCGTGCC CAGCACCTGAATTCGAGGGTGCACCGTCAGTCTTCCTCTTCCCCCCAAAACC CAAGGACACCCTCATGATCTCCCGGACTCCTGAGGTCACATGCGTGGTGGT GGACGTAAGCCACGAAGACCCTGAGGTCAAGTTCAACTGGTACGTGGACG GCGTGGAGGTGCATAATGCCAAGACAAAGCCGCGGGAGGAGCAGTACAAC AGCACGTACCGTGTGGTC AGCGTCCTC ACCGTCCTGC ACC AGGACTGGCTG AATGGCAAGGAGTACAAGTGCAAGGTCTCCAACAAAGCCCTCCCAACCCCC ATCGAGAAAACCATCTCCAAAGCCAAAGGGCAGCCCCGAGAACCACAGGT GTACACCCTGCCCCCATCCCGGGATGAGCTGACCAAGAACCAGGTCAGCCT GACCTGCCTGGTCAAAGGCTTCTATCCAAGCGACATCGCCGTGGAGTGGGA GAGCAATGGGCAGCCGGAGAACAACTACAAGACCACGCCTCCCGTGCTGG ACTCCGACGGCTCCTTCTTCCTCTACAGCAAGCTCACCGTGGACAAGAGCA GGTGGCAGCAGGGGAACGTCTTCTCATGCTCCGTGATGCATGAGGCTCTGC ACAACCACTACACGCAGAAGAGCCTCTCCCTGTCTCCGGGTAAATGAGTGC GACGGCCGCGACTCTAGAGGAT (SEQ ID NO: 1) Example 10: Production of an Antibody from a Polypeptide The antibodies of the present invention can be prepared by a variety of methods. (See, Current Protocols, Chapter 2.) For example, cells expressing a polypeptide of the present invention is administered to an animal to induce the production of sera containing polyclonal antibodies. In a preferred method, a preparation of the secreted protein is prepared and purified to render it substantially free of natural contaminants. Such a preparation is then introduced into an animal in order to produce polyclonal antisera of greater specific activity. In the most preferred method, the antibodies of the present invention are monoclonal antibodies (or protein binding fragments thereof). Such monoclonal antibodies can be prepared using hybridoma technology. (Kohler et al., Nature 256:495 (1975); Kohler et al., Eur. J. Immunol. 6:511 (1976); Kohler et al., Eur. J. 119 Immunol. 6:292 (1976); Hammerling et al., in: Monoclonal Antibodies and T-Cell Hybridomas, Elsevier, N.Y., pp. 563-681 (1981).) In general, such procedures involve immunizing an animal (preferably a mouse) with polypeptide or, more preferably, with a secreted polypeptide-expressing cell. Such cells may be cultured in any suitable tissue culture medium; however, it is preferable to culture cells in Earle's modified Eagle's medium supplemented with 10% fetal bovine serum (inactivated at about 56°C), and supplemented with about 10 g/1 of nonessential amino acids, about 1,000 U/ml of penicillin, and about 100 μg/ml of streptomycin. The splenocytes of such mice are extracted and fused with a suitable myeloma cell line. Any suitable myeloma cell line may be employed in accordance with the present invention; however, it is preferable to employ the parent myeloma cell line (SP2O), available from the ATCC. After fusion, the resulting hybridoma cells are selectively maintained in HAT medium, and then cloned by limiting dilution as described by Wands et al. (Gastroenterology 80:225-232 (1981).) The hybridoma cells obtained through such a selection are then assayed to identify clones which secrete antibodies capable of binding the polypeptide. Alternatively, additional antibodies capable of binding to the polypeptide can be produced in a two-step procedure using anti-idiotypic antibodies. Such a method makes use of the fact that antibodies are themselves antigens, and therefore, it is possible to obtain an antibody which binds to a second antibody. In accordance with this method, protein specific antibodies are used to immunize an animal, preferably a mouse. The splenocytes of such an animal are then used to produce hybridoma cells, and the hybridoma cells are screened to identify clones which produce an antibody whose ability to bind to the protein-specific antibody can be blocked by the polypeptide. Such antibodies comprise anti-idiotypic antibodies to the protein-specific antibody and can be used to immunize an animal to induce formation of further protein-specific antibodies. It will be appreciated that Fab and F(ab')2 and other fragments of the antibodies of the present invention may be used according to the methods disclosed herein. Such fragments are typically produced by proteolytic cleavage, using enzymes such as papain (to produce Fab fragments) or pepsin (to produce F(ab')2 fragments). Alternatively, secreted protein-binding fragments can be produced through the application of recombinant DNA technology or through synthetic chemistry. For in vivo use of antibodies in humans, it may be preferable to use "humanized" chimeric monoclonal antibodies. Such antibodies can be produced using genetic constructs derived from hybridoma cells producing the monoclonal antibodies 120 described above. Methods for producing chimeric antibodies are known in the art. (See, for review, Morrison, Science 229: 1202 (1985); Oi et al., BioTechniques 4:214 (1986); Cabilly et al., U.S. Patent No. 4,816,567; Taniguchi et al., EP 171496; Morrison et al., EP 173494; Neuberger et al., WO 8601533; Robinson et al., WO 8702671 ; Boulianne et al, Nature 312:643 (1984); Neuberger et al., Nature 314:268 (1985).) Example 11: Production Of Secreted Protein For High-Throughput Screening Assays The following protocol produces a supernatant containing a polypeptide to be tested. This supernatant can then be used in the Screening Assays described in Examples 13-20. First, dilute Poly-D-Lysine (644 587 Boehringer-Mannheim) stock solution (lmg/ml in PBS) 1:20 in PBS (w/o calcium or magnesium 17-516F Biowhittaker) for a working solution of 50ug/ml. Add 200 ul of this solution to each well (24 well plates) and incubate at RT for 20 minutes. Be sure to distribute the solution over each well (note: a 12-channel pipetter may be used with tips on every other channel). Aspirate off the Poly-D-Lysine solution and rinse with 1ml PBS (Phosphate Buffered Saline). The PBS should remain in the well until just prior to plating the cells and plates may be poly-lysine coated in advance for up to two weeks. Plate 293T cells (do not carry cells past P+20) at 2 x 10 5 cells/well in .5ml DMEM(Dulbecco's Modified Eagle Medium)(with 4.5 G/L glucose and L-glutamine (12-604F Biowhittaker))/10% heat inactivated FBS(14-503F Biowhittaker)/lx Penstrep(17-602E Biowhittaker). Let the cells grow overnight. The next day, mix together in a sterile solution basin: 300 ul Lipofectamine (18324-012 Gibco/BRL) and 5ml Optimem I (31985070 Gibco/BRL)/96-well plate. With a small volume multi-channel pipetter, aliquot approximately 2ug of an expression vector containing a polynucleotide insert, produced by the methods described in Examples 8 or 9, into an appropriately labeled 96-well round bottom plate. With a multi-channel pipetter, add 50ul of the Lipofectamine/Optimem I mixture to each well. Pipette up and down gently to mix. Incubate at RT 15-45 minutes. After about 20 minutes, use a multi-channel pipetter to add 150ul Optimem I to each well. As a control, one plate of vector DNA lacking an insert should be transfected with each set of transfections. Preferably, the transfection should be performed by tag-teaming the following tasks. By tag-teaming, hands on time is cut in half, and the cells do not spend too much time on PBS. First, person A aspirates off the media from four 24-well plates of 121 cells, and then person B rinses each well with .5-lml PBS. Person A then aspirates off PBS rinse, and person B, using al2-channel pipetter with tips on every other channel, adds the 200ul of DNA/Lipofectamine/Optimem I complex to the odd wells first, then to the even wells, to each row on the 24-well plates. Incubate at 37°C for 6 hours. While cells are incubating, prepare appropriate media, either 1 %BS A in DMEM with lx penstrep, or CHO-5 media (116.6 mg/L of CaC12 (anhyd); 0.00130 mg/L CuSO 4 -5H 2 O; 0.050 mg/L of Fe(NO 3 ) 3 -9H 2 O; 0.417 mg/L of FeSO 4 -7H 2 O; 311.80 mg/L of Kcl; 28.64 mg L of MgCl 2 ; 48.84 mg/L of MgSO 4 ; 6995.50 mg/L of NaCl; 2400.0 mg/L of NaHCO 3 ; 62.50 mg/L of NaH 2 PO 4 -H 2 0; 71.02 mg/L of Na 2 HPO4; .4320 mg/L of ZnSO 4 -7H 2 O; .002 mg/L of Arachidonic Acid ; 1.022 mg/L of Cholesterol; .070 mg/L of DL-alpha-Tocopherol- Acetate; 0.0520 mg/L of Linoleic Acid; 0.010 mg/L of Linolenic Acid; 0.010 mg/L of Myristic Acid; 0.010 mg/L of Oleic Acid; 0.010 mg/L of Palmitric Acid; 0.010 mg/L of Palmitic Acid; 100 mg/L of Pluronic F-68; 0.010 mg/L of Stearic Acid; 2.20 mg/L of Tween 80; 4551 mg/L of D- Glucose; 130.85 mg/ml of L- Alanine; 147.50 mg/ml of L-Arginine-HCL; 7.50 mg/ml of L-Asparagine-H 2 0; 6.65 mg/ml of L-Aspartic Acid; 29.56 mg/ml of L-Cystine- 2HCL-H 2 0; 31.29 mg/ml of L-Cystine-2HCL; 7.35 mg/ml of L-Glutamic Acidj_365.0 mg/ml of L-Glutamine; 18.75 mg/ml of Glycine; 52.48 mg/ml of L-Histidine-HCL- H 2 0; 106.97 mg/ml of L-Isoleucine; 111.45 mg/ml of L-Leucine; 163.75 mg/ml of L- Lysine HCL; 32.34 mg/ml of L-Methionine; 68.48 mg/ml of L-Phenylalainine; 40.0 mg/ml of L-Proline; 26.25 mg/ml of L-Serine; 101.05 mg/ml of L-Threonine; 19.22 mg/ml of L-Tryptophan; 91.79 mg/ml of L-Tryrosine-2Na-2H 2 0; 99.65 mg/ml of L- Valine; 0.0035 mg/L of Biotin; 3.24 mg/L of D-Ca Pantothenate; 11.78 mg/L of Choline Chloride; 4.65 mg/L of Folic Acid; 15.60 mg/L of i-Inositol; 3.02 mg/L of Niacinamide; 3.00 mg/L of Pyridoxal HCL; 0.031 mg/L of Pyridoxine HCL; 0.319 mg/L of Riboflavin; 3.17 mg/L of Thiamine HCL; 0.365 mg/L of Thymidine; and 0.680 mg/L of Vitamin B 12 ; 25 mM of HEPES Buffer; 2.39 mg/L of Na Hypoxanthine; 0.105 mg/L of Lipoic Acid; 0.081 mg/L of Sodium Putrescine-2HCL; 55.0 mg/L of Sodium Pyruvate; 0.0067 mg/L of Sodium Selenite; 20uM of Ethanolamine; 0.122 mg/L of Ferric Citrate; 41.70 mg/L of Methyl-B-Cyclodextrin complexed with Linoleic Acid; 33.33 mg/L of Methyl-B-Cyclodextrin complexed with Oleic Acid; and 10 mg/L of Methyl-B-Cyclodextrin complexed with Retinal) with 2mm glutamine and lx penstrep. (BSA (81-068-3 Bayer) lOOgm dissolved in 1L DMEM for a 10% BSA stock solution). Filter the media and collect 50 ul for endotoxin assay in 15ml polystyrene conical. 122 The transfection reaction is terminated, preferably by tag-teaming, at the end of the incubation period. Person A aspirates off the transfection media, while person B adds 1.5ml appropriate media to each well. Incubate at 37°C for 45 or 72 hours depending on the media used: 1%BSA for 45 hours or CHO-5 for 72 hours. On day four, using a 300ul multichannel pipetter, aliquot 600ul in one 1ml deep well plate and the remaining supernatant into a 2ml deep well. The supematants from each well can then be used in the assays described in Examples 13-20. It is specifically understood that when activity is obtained in any of the assays described below using a supernatant, the activity originates from either the polypeptide directly (e.g., as a secreted protein) or by the polypeptide inducing expression of other proteins, which are then secreted into the supernatant. Thus, the invention further provides a method of identifying the protein in the supernatant characterized by an activity in a particular assay. Example 12: Construction of GAS Reporter Construct One signal transduction pathway involved in the differentiation and proliferation of cells is called the Jaks-STATs pathway. Activated proteins in the Jaks-STATs pathway bind to gamma activation site "GAS" elements or interferon-sensitive responsive element ("ISRE"), located in the promoter of many genes. The binding of a protein to these elements alter the expression of the associated gene. GAS and ISRE elements are recognized by a class of transcription factors called Signal Transducers and Activators of Transcription, or "STATs." There are six members of the STATs family. Statl and Stat3 are present in many cell types, as is Stat2 (as response to IFN-alpha is widespread). Stat4 is more restricted and is not in many cell types though it has been found in T helper class I, cells after treatment with LL-12. Stat5 was originally called mammary growth factor, but has been found at higher concentrations in other cells including myeloid cells. It can be activated in tissue culture cells by many cytokines. The STATs are activated to translocate from the cytoplasm to the nucleus upon tyrosine phosphorylation by a set of kinases known as the Janus Kinase ("Jaks") family. Jaks represent a distinct family of soluble tyrosine kinases and include Tyk2, Jakl, Jak2, and Jak3. These kinases display significant sequence similarity and are generally catalytically inactive in resting cells. The Jaks are activated by a wide range of receptors summarized in the Table below. (Adapted from review by Schidler and Darnell, Ann. Rev. Biochem. 64:621-51 (1995).) A cytokine receptor family, capable of activating Jaks, is divided into two 123 groups: (a) Class 1 includes receptors for IL-2, IL-3, IL-4, IL-6, EL-7, EL-9, IL-11, LL- 12, EL- 15, Epo, PRL, GH, G-CSF, GM-CSF, LIF, CNTF, and thrombopoietin; and (b) Class 2 includes IFN-a, IFN-g, and IL-10. The Class 1 receptors share a conserved cysteine motif (a set of four conserved cysteines and one tryptophan) and a WSXWS motif (a membrane proximal region encoding Tφ-Ser-Xxx-Tφ-Ser (SEQ ID NO:2)). Thus, on binding of a ligand to a receptor, Jaks are activated, which in turn activate STATs, which then translocate and bind to GAS elements. This entire process is encompassed in the Jaks-STATs signal transduction pathway. Therefore, activation of the Jaks-STATs pathway, reflected by the binding of the GAS or the ISRE element, can be used to indicate proteins involved in the proliferation and differentiation of cells. For example, growth factors and cytokines are known to activate the Jaks-STATs pathway. (See Table below.) Thus, by using GAS elements linked to reporter molecules, activators of the Jaks-STATs pathway can be identified. 124 JAKs STATS GASfelements or ISRE Ligand tyk2 Jakl Jak2 Jak3 IFN family IFN-a/B + + - - 1 ,2,3 ISRE IFN-g + + - 1 GAS (IRFl>Lys6>IFP) 11-10 + ? 7 - 1,3 gpl30 familv IL-6 (Pleiotrophic) + + + 7 1 ,3 GAS (IRFl>Lys6>IFP) 11- 11 (Pleiotrophic) ? + ? 7 1 ,3 OnM(Pleiotrophic) ? + + 7 1 ,3 LLF(Pleiotrophic) ? + + 7 1 ,3 CNTF(Pleiotrophic) -/+ + + 7 1 ,3 G-CSF(Pleiotrophic) ? + 7 7 1 ,3 IL-12(Pleiotrophic) + - + + 1 ,3 g-C familv IL-2 (lymphocytes) - + - + 1,3,5 GAS IL-4 (lymph/myeloid) - + - + 6 GAS (IRFl = IFP »Ly6)(IgH) LL-7 (lymphocytes) - + - + 5 GAS IL-9 (lymphocytes) - + - + 5 GAS IL-13 (lymphocyte) - + 7 7 6 GAS IL-15 ? + 7 + 5 GAS gp 140 familv EL-3 (myeloid) - - + - 5 GAS (IRFl>EFP»Ly6) LL-5 (myeloid) - - + - 5 GAS GM-CSF (myeloid) - - + - 5 GAS Growth hormone familv GH ? - + - 5 PRL 7 +/- + - 1 ,3,5 EPO ? - + - 5 GAS(B-C AS>IRF1 =IFP»Ly6) Receptor Tvrosine Kinases EGF 7 + + - 1,3 GAS (ERF1) PDGF 7 + + - 1 ,3 CSF-1 7 + + - 1 ,3 GAS (not ERF 1) 125 To construct a synthetic GAS containing promoter element, which is used in the Biological Assays described in Examples 13-14, a PCR based strategy is employed to generate a GAS-SV40 promoter sequence. The 5' primer contains four tandem copies of the GAS binding site found in the IRFl promoter and previously demonstrated to bind STATs upon induction with a range of cytokines (Rothman et al., Immunity 1:457-468 (1994).), although other GAS or ISRE elements can be used instead. The 5' primer also contains 18bp of sequence complementary to the SV40 early promoter sequence and is flanked with an Xhol site. The sequence of the 5' primer is: 5':GCGCCTCGAGATTTCCCCGAAATCTAGATTTCCCCGAAATGATTTCCCCG AAATGATTTCCCCGAAATATCTGCCATCTCAATTAG:3 ' (SEQ ID NO:3) The downstream primer is complementary to the SV40 promoter and is flanked with a Hind III site: 5':GCGGCAAGCTTTTTGCAAAGCCTAGGC:3' (SEQ ID NO:4) PCR amplification is performed using the SV40 promoter template present in the B-gal:promoter plasmid obtained from Clontech. The resulting PCR fragment is digested with Xhol/Hind III and subcloned into BLSK2-. (Stratagene.) Sequencing with forward and reverse primers confirms that the insert contains the following sequence: 5':CTCGAGATTTCCCCGAAATCTAGATTTCCCCGAAATGATTTCCCCGAAATG ATTTCCCCGAAATATCTGCCATCTCAATTAGTCAGCAACCATAGTCCCGCCC CTAACTCCGCCCATCCCGCCCCTAACTCCGCCCAGTTCCGCCCATTCTCCGC CCCATGGCTGACTAATTTTTTTTATTTATGCAGAGGCCGAGGCCGCCTCGGC CTCTGAGCTATTCCAGAAGTAGTGAGGAGGCTTTTTTGGAGGCCTAGGCTTT TGCAAAAAGCTT:3' (SEQ ID NO:5) With this GAS promoter element linked to the SV40 promoter, a GAS :SEAP2 reporter construct is next engineered. Here, the reporter molecule is a secreted alkaline phosphatase, or "SEAP." Clearly, however, any reporter molecule can be instead of SEAP, in this or in any of the other Examples. Well known reporter molecules that can be used instead of SEAP include chloramphenicol acetyltransferase (CAT), luciferase, alkaline phosphatase, B-galactosidase, green fluorescent protein (GFP), or any protein detectable by an antibody. The above sequence confirmed synthetic GAS-SV40 promoter element is subcloned into the pSEAP-Promoter vector obtained from Clontech using Hindlll and Xhol, effectively replacing the SV40 promoter with the amplified GAS:SV40 promoter element, to create the GAS-SEAP vector. However, this vector does not contain a neomycin resistance gene, and therefore, is not preferred for mammalian expression systems. 126 Thus, in order to generate mammalian stable cell lines expressing the GAS- SEAP reporter, the GAS-SEAP cassette is removed from the GAS-SEAP vector using Sail and NotI, and inserted into a backbone vector containing the neomycin resistance gene, such as pGFP-1 (Clontech), using these restriction sites in the multiple cloning site, to create the GAS-SEAP/Neo vector. Once this vector is transfected into mammalian cells, this vector can then be used as a reporter molecule for GAS binding as described in Examples 13-14. Other constructs can be made using the above description and replacing GAS with a different promoter sequence. For example, construction of reporter molecules containing NFK-B and EGR promoter sequences are described in Examples 15 and 16. However, many other promoters can be substituted using the protocols described in these Examples. For instance, SRE, IL-2, NFAT, or Osteocalcin promoters can be substituted, alone or in combination (e.g., GAS/NF-KB/EGR, GAS/NF-KB, II- 2/NFAT, or NF-KB/GAS). Similarly, other cell lines can be used to test reporter construct activity, such as HELA (epithelial), HUVEC (endothelial), Reh (B-cell), Saos-2 (osteoblast), HUVAC (aortic), or Cardiomyocyte. Example 13: High-Throughput Screening Assay for T-cell Activity. The following protocol is used to assess T-cell activity by identifying factors, such as growth factors and cytokines, that may proliferate or differentiate T-cells. T- cell activity is assessed using the GAS/SEAP/Neo construct produced in Example 12. Thus, factors that increase SEAP activity indicate the ability to activate the Jaks-STATS signal transduction pathway. The T-cell used in this assay is Jurkat T-cells (ATCC Accession No. TIB- 152), although Molt-3 cells (ATCC Accession No. CRL- 1552) and Molt-4 cells (ATCC Accession No. CRL- 1582) cells can also be used. Jurkat T-cells are lymphoblastic CD4+ Thl helper cells. In order to generate stable cell lines, approximately 2 million Jurkat cells are transfected with the GAS- SEAP/neo vector using DMRLE-C (Life Technologies)(transfection procedure described below). The transfected cells are seeded to a density of approximately 20,000 cells per well and transfectants resistant to 1 mg/ml genticin selected. Resistant colonies are expanded and then tested for their response to increasing concentrations of interferon gamma. The dose response of a selected clone is demonstrated. Specifically, the following protocol will yield sufficient cells for 75 wells containing 200 ul of cells. Thus, it is either scaled up, or performed in multiple to generate sufficient cells for multiple 96 well plates. Jurkat cells are maintained in RPMI + 10% serum with l%Pen-Strep. Combine 2.5 mis of OPTI-MEM (Life Technologies) 127 with 10 ug of plasmid DNA in a T25 flask. Add 2.5 ml OPTI-MEM containing 50 ul of DMREE-C and incubate at room temperature for 15-45 mins. During the incubation period, count cell concentration, spin down the required number of cells (10 7 per transfection), and resuspend in OPTI-MEM to a final concentration of 10 7 cells/ml. Then add 1ml of 1 x 10 7 cells in OPTI-MEM to T25 flask and incubate at 37°C for 6 hrs. After the incubation, add 10 ml of RPMI + 15% serum. The Jurkat:GAS-SEAP stable reporter lines are maintained in RPMI + 10% serum, 1 mg/ml Genticin, and 1% Pen-Strep. These cells are treated with supematants containing a polypeptide as produced by the protocol described in Example 11. On the day of treatment with the supernatant, the cells should be washed and resuspended in fresh RPMI + 10% serum to a density of 500,000 cells per ml. The exact number of cells required will depend on the number of supematants being screened. For one 96 well plate, approximately 10 million cells (for 10 plates, 100 million cells) are required. Transfer the cells to a triangular reservoir boat, in order to dispense the cells into a 96 well dish, using a 12 channel pipette. Using a 12 channel pipette, transfer 200 ul of cells into each well (therefore adding 100, 000 cells per well). After all the plates have been seeded, 50 ul of the supematants are transferred directly from the 96 well plate containing the supematants into each well using a 12 channel pipette. In addition, a dose of exogenous interferon gamma (0.1, 1.0, 10 ng) is added to wells H9, H10, and HI 1 to serve as additional positive controls for the assay. The 96 well dishes containing Jurkat cells treated with supematants are placed in an incubator for 48 hrs (note: this time is variable between 48-72 hrs). 35 ul samples from each well are then transferred to an opaque 96 well plate using a 12 channel pipette. The opaque plates should be covered (using sellophene covers) and stored at - 20°C until SEAP assays are performed according to Example 17. The plates containing the remaining treated cells are placed at 4°C and serve as a source of material for repeating the assay on a specific well if desired. As a positive control, 100 Unit/ml interferon gamma can be used which is known to activate Jurkat T cells. Over 30 fold induction is typically observed in the positive control wells. The above protocol may be used in the generation of both transient, as well as, stable transfected cells, which would be apparent to those of skill in the art. 128 Example 14: High-Throughput Screening Assay Identifying Myeloid Activity The following protocol is used to assess myeloid activity by identifying factors, such as growth factors and cytokines, that may proliferate or differentiate myeloid cells. Myeloid cell activity is assessed using the GAS/SEAP/Neo construct produced in Example 12. Thus, factors that increase SEAP activity indicate the ability to activate the Jaks-STATS signal transduction pathway. The myeloid cell used in this assay is U937, a pre-monocyte cell line, although TF-1, HL60, or KG1 can be used. To transiently transfect U937 cells with the GAS/SEAP/Neo construct produced in Example 12, a DEAE-Dextran method (Kharbanda et. al, 1994, Cell Growth & Differentiation, 5:259-265) is used. First, harvest 2xl0e^ U937 cells and wash with PBS. The U937 cells are usually grown in RPMI 1640 medium containing 10% heat- inactivated fetal bovine serum (FBS) supplemented with 100 units/ml penicillin and 100 mg/ml streptomycin. Next, suspend the cells in 1 ml of 20 mM Tris-HCl (pH 7.4) buffer containing 0.5 mg/ml DEAE-Dextran, 8 ug GAS-SEAP2 plasmid DNA, 140 mM NaCl, 5 mM KC1, 375 uM Na 2 HPO 4 .7H 2 O, 1 mM MgCl 2 , and 675 uM CaCl 2 . Incubate at 37°C for 45 min. Wash the cells with RPMI 1640 medium containing 10% FBS and then resuspend in 10 ml complete medium and incubate at 37°C for 36 hr. The GAS-SEAP/U937 stable cells are obtained by growing the cells in 400 ug/ml G418. The G418-free medium is used for routine growth but every one to two months, the cells should be re-grown in 400 ug/ml G418 for couple of passages. These cells are tested by harvesting 1x10 cells (this is enough for ten 96- well plates assay) and wash with PBS. Suspend the cells in 200 ml above described growth medium, with a final density of 5xl0 5 cells/ml. Plate 200 ul cells per well in the 96- well plate (or lxl 0 5 cells/well). Add 50 ul of the supernatant prepared by the protocol described in Example 11. Incubate at 37°C for 48 to 72 hr. As a positive control, 100 Unit/ml interferon gamma can be used which is known to activate U937 cells. Over 30 fold induction is typically observed in the positive control wells. SEAP assay the supernatant according to the protocol described in Example 17. Example 15: High-Throughput Screening Assay Identifying Neuronal Activity. 129 When cells undergo differentiation and proliferation, a group of genes are activated through many different signal transduction pathways. One of these genes, EGR1 (early growth response gene 1), is induced in various tissues and cell types upon activation. The promoter of EGR1 is responsible for such induction. Using the EGR1 promoter linked to reporter molecules, activation of cells can be assessed. Particularly, the following protocol is used to assess neuronal activity in PC 12 cell lines. PC 12 cells (rat phenochromocytoma cells) are known to proliferate and/or differentiate by activation with a number of mitogens, such as TPA (tetradecanoyl phorbol acetate), NGF (nerve growth factor), and EGF (epidermal growth factor). The EGR1 gene expression is activated during this treatment. Thus, by stably transfecting PC 12 cells with a construct containing an EGR promoter linked to SEAP reporter, activation of PC 12 cells can be assessed. The EGR/SEAP reporter construct can be assembled by the following protocol. The EGR-1 promoter sequence (-633 to +l)(Sakamoto K et al., Oncogene 6:867-871 (1991)) can be PCR amplified from human genomic DNA using the following primers: 5' GCGCTCGAGGGATGACAGCGATAGAACCCCGG -3' (SEQ ID NO:6) 5' GCGAAGCTTCGCGACTCCCCGGATCCGCCTC-3' (SEQ ID NO:7) Using the GAS:SEAP/Neo vector produced in Example 12, EGR1 amplified product can then be inserted into this vector. Linearize the GAS:SEAP/Neo vector using restriction enzymes Xhol/Hindlll, removing the GAS/SV40 stuffer. Restrict the EGR1 amplified product with these same enzymes. Ligate the vector and the EGR1 promoter. To prepare 96 well-plates for cell culture, two mis of a coating solution (1:30 dilution of collagen type I (Upstate Biotech Inc. Cat#08-115) in 30% ethanol (filter sterilized)) is added per one 10 cm plate or 50 ml per well of the 96-well plate, and allowed to air dry for 2 hr. PC 12 cells are routinely grown in RPMI- 1640 medium (Bio Whittaker) containing 10% horse serum (JRH BIOSCIENCES, Cat. # 12449-78P), 5% heat- inactivated fetal bovine serum (FBS) supplemented with 100 units/ml penicillin and 100 ug/ml streptomycin on a precoated 10 cm tissue culture dish. One to four split is done every three to four days. Cells are removed from the plates by scraping and resuspended with pipetting up and down for more than 15 times. Transfect the EGR/SEAP/Neo construct into PC 12 using the Lipofectamine protocol described in "Example 11. EGR-SEAP/PC12 stable cells are obtained by growing the cells in 300 ug/ml G418. The G418-free medium is used for routine growth but every one to two months, the cells should be re-grown in 300 ug/ml G418 for couple of passages. 130 To assay for neuronal activity, a 10 cm plate with cells around 70 to 80% confluent is screened by removing the old medium. Wash the cells once with PBS (Phosphate buffered saline). Then starve the cells in low serum medium (RPMI- 1640 containing 1% horse serum and 0.5% FBS with antibiotics) overnight. The next morning, remove the medium and wash the cells with PBS. Scrape off the cells from the plate, suspend the cells well in 2 ml low serum medium. Count the cell number and add more low serum medium to reach final cell density as 5x10^ cells/ml. Add 200 ul of the cell suspension to each well of 96-well plate (equivalent to lx 10 5 cells/well). Add 50 ul supernatant produced by Example 11 , 37°C for 48 to 72 hr. As a positive control, a growth factor known to activate PC 12 cells through EGR can be used, such as 50 ng/ul of Neuronal Growth Factor (NGF). Over fifty -fold induction of SEAP is typically seen in the positive control wells. SEAP assay the supematant according to Example 17. Example 16: High-Throughput Screening Assay for T-cell Activity NF-κB (Nuclear Factor KB) is a transcription factor activated by a wide variety of agents including the inflammatory cytokines EL-1 and TNF, CD30 and CD40, lymphotoxin-alpha and lymphotoxin-beta, by exposure to LPS or thrombin, and by expression of certain viral gene products. As a transcription factor, NF-κB regulates the expression of genes involved in immune cell activation, control of apoptosis (NF- KB appears to shield cells from apoptosis), B and T-cell development, anti-viral and antimicrobial responses, and multiple stress responses. In non-stimulated conditions, NF- KB is retained in the cytoplasm with I-κB (Inhibitor KB). However, upon stimulation, I- KB is phosphorylated and degraded, causing NF- KB to shuttle to the nucleus, thereby activating transcription of target genes. Target genes activated by NF- KB include IL-2, IL-6, GM-CSF, ICAM-1 and class 1 MHC. Due to its central role and ability to respond to a range of stimuli, reporter constructs utilizing the NF-κB promoter element are used to screen the supematants produced in Example 11. Activators or inhibitors of NF-kB would be useful in treating 131 diseases. For example, inhibitors of NF-κB could be used to treat those diseases related to the acute or chronic activation of NF-kB, such as rheumatoid arthritis. To construct a vector containing the NF-κB promoter element, a PCR based strategy is employed. The upstream primer contains four tandem copies of the NF-κB binding site (GGGGACTTTCCC) (SEQ ID NO:8), 18 bp of sequence complementary to the 5' end of the SV40 early promoter sequence, and is flanked with an Xhol site: 5 ' :GCGGCCTCGAGGGGACTTTCCCGGGGACTTTCCGGGGACTTTCCGGGAC TTTCCATCCTGCCATCTCAATTAG:3' (SEQ ID NO:9) The downstream primer is complementary to the 3' end of the SV40 promoter and is flanked with a Hind III site: PCR amplification is performed using the S V40 promoter template present in the pB-gal:promoter plasmid obtained from Clontech. The resulting PCR fragment is digested with Xhol and Hind III and subcloned into BLSK2-. (Stratagene) Sequencing with the T7 and T3 primers confirms the insert contains the following sequence: 5 ' :CTCGAGGGGACTTTCCCGGGGACTTTCCGGGGACTTTCCGGGACTTTCC ATCTGCCATCTCAATTAGTCAGCAACCATAGTCCCGCCCCTAACTCCGCCCA TCCCGCCCCTAACTCCGCCCAGTTCCGCCCATTCTCCGCCCCATGGCTGACT AATTTTTTTTATTTATGCAGAGGCCGAGGCCGCCTCGGCCTCTGAGCTATTC CAGAAGTAGTGAGGAGGCTTTTTTC JAGGCCTAGGCTTTTGCAAAAAGCTT: 3' (SEQ ID NO: 10) Next, replace the SV40 minimal promoter element present in the pSEAP2- promoter plasmid (Clontech) with this NF-KB/SV40 fragment using Xhol and Hindlll. However, this vector does not contain a neomycin resistance gene, and therefore, is not preferred for mammalian expression systems. In order to generate stable mammalian cell lines, the NF-KB/S V40/SEAP cassette is removed from the above NF-KB/SEAP vector using restriction enzymes Sail and NotI, and inserted into a vector containing neomycin resistance. Particularly, the NF-KB/SV40/SEAP cassette was inserted into pGFP-1 (Clontech), replacing the GFP gene, after restricting pGFP-1 with Sail and NotI. 132 Once NF-κB/SV40/SEAP/Neo vector is created, stable Jurkat T-cells are created and maintained according to the protocol described in Example 13. Similarly, the method for assaying supematants with these stable Jurkat T-cells is also described in Example 13. As a positive control, exogenous TNF alpha (0.1,1, 10 ng) is added to wells H9, H10, and HI 1, with a 5-10 fold activation typically observed. Example 17: Assay for SEAP Activity As a reporter molecule for the assays described in Examples 13-16, SEAP activity is assayed using the Tropix Phospho-light Kit (Cat. BP-400) according to the following general procedure. The Tropix Phospho-light Kit supplies the Dilution, Assay, and Reaction Buffers used below. Prime a dispenser with the 2.5x Dilution Buffer and dispense 15 μl of 2.5x dilution buffer into Optiplates containing 35 μl of a supematant. Seal the plates with a plastic sealer and incubate at 65°C for 30 min. Separate the Optiplates to avoid uneven heating. Cool the samples to room temperature for 15 minutes. Empty the dispenser and prime with the Assay Buffer. Add 50 μl Assay Buffer and incubate at room temperature 5 min. Empty the dispenser and prime with the Reaction Buffer (see the table below). Add 50 μl Reaction Buffer and incubate at room temperature for 20 minutes. Since the intensity of the chemiluminescent signal is time dependent, and it takes about 10 minutes to read 5 plates on luminometer, one should treat 5 plates at each time and start the second set 10 minutes later. Read the relative light unit in the luminometer. Set H12 as blank, and print the results. An increase in chemiluminescence indicates reporter activity. Reaction Buffer Formulation: # of plates Rxn buffer diluent (ml) CSPD (ml) 10 60 3 11 65 3.25 12 70 3.5 13 75 3.75 14 80 4 15 85 4.25 16 90 4.5 17 95 4.75 18 100 5 19 105 5.25 20 110 5.5 21 115 5.75 22 120 6 133 23 125 6.25 24 130 6.5 25 135 6.75 26 140 7 27 145 7.25 28 150 7.5 29 155 7.75 30 160 8 31 165 8.25 32 170 8.5 33 175 8.75 34 180 9 35 185 9.25 36 190 9.5 37 195 9.75 38 200 10 39 205 10.25 40 210 10.5 41 215 10.75 42 220 11 43 225 1 1.25 44 230 11.5 45 235 1 1.75 46 240 12 47 245 12.25 48 250 12.5 49 255 12.75 50 260 13 Example 18: High-Throughput Screening Assay Identifying Changes in Small Molecule Concentration and Membrane Permeability Binding of a ligand to a receptor is known to alter intracellular levels of small molecules, such as calcium, potassium, sodium, and pH, as well as alter membrane potential. These alterations can be measured in an assay to identify supematants which bind to receptors of a particular cell. Although the following protocol describes an assay for calcium, this protocol can easily be modified to detect changes in potassium, sodium, pH, membrane potential, or any other small molecule which is detectable by a fluorescent probe. The following assay uses Fluorometric Imaging Plate Reader ("FLIPR") to measure changes in fluorescent molecules (Molecular Probes) that bind small molecules. Clearly, any fluorescent molecule detecting a small molecule can be used instead of the calcium fluorescent molecule, fluo-4 (Molecular Probes , Inc . ; catalog no . F-14202 ) , used here. For adherent cells, seed the cells at 10,000 -20,000 cells/well in a Co-star black 96-well plate with clear bottom. The plate is incubated in a CO 2 incubator for 20 hours. 134 The adherent cells are washed two times in Biotek washer with 200 ul of HBSS (Hank's Balanced Salt Solution) leaving 100 ul of buffer after the final wash. A stock solution of 1 mg/ml fluo-4 is made in 10% pluronic acid DMSO. To load the cells with fluo-4 , 50 ul of 12 ug/ml Ωuo-4 is added to each well. The plate is incubated at 37°C in a CO 2 incubator for 60 min. The plate is washed four times in the Biotek washer with HBSS leaving 100 ul of buffer. For non-adherent cells, the cells are spun down from culture media. Cells are re-suspended to 2-5x10 6 cells/ml with HBSS in a 50-ml conical tube. 4 ul of 1 mg/ml fluo-4 solution in 10% pluronic acid DMSO is added to each ml of cell suspension. The tube is then placed in a 37°C water bath for 30-60 min. The cells are washed twice with HBSS, resuspended to lxlO 6 cells/ml, and dispensed into a microplate, 100 ul/well. The plate is centrifuged at 1000 φm for 5 min. The plate is then washed once in Denley CellWash with 200 ul, followed by an aspiration step to 100 ul final volume. For a non-cell based assay, each well contains a fluorescent molecule, such as fluo-4 . The supernatant is added to the well, and a change in fluorescence is detected. To measure the fluorescence of intracellular calcium, the FLIPR is set for the following parameters: (1) System gain is 300-800 mW; (2) Exposure time is 0.4 second; (3) Camera F/stop is F/2; (4) Excitation is 488 nm; (5) Emission is 530 nm; and (6) Sample addition is 50 ul. Increased emission at 530 nm indicates an extracellular signaling event which has resulted in an increase in the intracellular Ca "1-1" concentration. Example 19: High-Throughput Screening Assay Identifying Tyrosine Kinase Activity The Protein Tyrosine Kinases (PTK) represent a diverse group of transmembrane and cytoplasmic kinases. Within the Receptor Protein Tyrosine Kinase RPTK) group are receptors for a range of mitogenic and metabolic growth factors including the PDGF, FGF, EGF, NGF, HGF and Insulin receptor subfamilies. In addition there are a large family of RPTKs for which the corresponding ligand is unknown. Ligands for RPTKs include mainly secreted small proteins, but also membrane-bound and extracellular matrix proteins. Activation of RPTK by ligands involves ligand-mediated receptor dimerization, resulting in transphosphorylation of the receptor subunits and activation of the cytoplasmic tyrosine kinases. The cytoplasmic tyrosine kinases include receptor associated tyrosine kinases of the src -family (e.g., src, yes, lck, lyn, fyn) and non- receptor linked and cytosolic protein tyrosine kinases, such as the Jak family, members 135 of which mediate signal transduction triggered by the cytokine superfamily of receptors (e.g., the Interleukins, Interferons, GM-CSF, and Leptin). Because of the wide range of known factors capable of stimulating tyrosine kinase activity, the identification of novel human secreted proteins capable of activating tyrosine kinase signal transduction pathways are of interest. Therefore, the following protocol is designed to identify those novel human secreted proteins capable of activating the tyrosine kinase signal transduction pathways. Seed target cells (e.g., primary keratinocytes) at a density of approximately 25,000 cells per well in a 96 well Loprodyne Silent Screen Plates purchased from Nalge Nunc (Naperville, LL). The plates are sterilized with two 30 minute rinses with 100% ethanol, rinsed with water and dried overnight. Some plates are coated for 2 hr with 100 ml of cell culture grade type I collagen (50 mg/ml), gelatin (2%) or polylysine (50 mg/ml), all of which can be purchased from Sigma Chemicals (St. Louis, MO) or 10% Matrigel purchased from Becton Dickinson (Bedford,MA), or calf serum, rinsed with PBS and stored at 4°C. Cell growth on these plates is assayed by seeding 5,000 cells/well in growth medium and indirect quantitation of cell number through use of alamarBlue as described by the manufacturer Alamar Biosciences, Inc. (Sacramento, CA) after 48 hr. Falcon plate covers #3071 from Becton Dickinson (Bedford,MA) are used to cover the Loprodyne Silent Screen Plates. Falcon Microtest IEE cell culture plates can also be used in some proliferation experiments. To prepare extracts, A431 cells are seeded onto the nylon membranes of Loprodyne plates (20,000/200ml/well) and cultured overnight in complete medium. Cells are quiesced by incubation in serum-free basal medium for 24 hr. After 5-20 minutes treatment with EGF (60ng/ml) or 50 ul of the supematant produced in Example 11, the medium was removed and 100 ml of extraction buffer ((20 mM HEPES pH 7.5, 0.15 M NaCl, 1% Triton X-100, 0.1% SDS, 2 mM Na3VO4, 2 mM Na4P2O7 and a cocktail of protease inhibitors (# 1836170) obtained from Boeheringer Mannheim (Indianapolis, IN) is added to each well and the plate is shaken on a rotating shaker for 5 minutes at 4°C. The plate is then placed in a vacuum transfer manifold and the extract filtered through the 0.45 mm membrane bottoms of each well using house vacuum. Extracts are collected in a 96-well catch/assay plate in the bottom of the vacuum manifold and immediately placed on ice. To obtain extracts clarified by centrifugation, the content of each well, after detergent solubilization for 5 minutes, is removed and centrifuged for 15 minutes at 4°C at 16,000 x g. Test the filtered extracts for levels of tyrosine kinase activity. Although many methods of detecting tyrosine kinase activity are known, one method is described here. 136 Generally, the tyrosine kinase activity of a supernatant is evaluated by determining its ability to phosphorylate a tyrosine residue on a specific substrate (a biotinylated peptide). Biotinylated peptides that can be used for this puφose include PSK1 (corresponding to amino acids 6-20 of the cell division kinase cdc2-p34) and PSK2 (corresponding to amino acids 1-17 of gastrin). Both peptides are substrates for a range of tyrosine kinases and are available from Boehringer Mannheim. The tyrosine kinase reaction is set up by adding the following components in order. First, add lOul of 5uM Biotinylated Peptide, then lOul ATP/Mg2 + (5mM ATP/50mM MgCl2), then lOul of 5x Assay Buffer (40mM imidazole hydrochloride, pH7.3, 40 mM beta-glycerophosphate, ImM EGTA, lOOmM MgCl2, 5 mM MnC , 0.5 mg/ml BSA), then 5ul of Sodium Vanadate(lmM), and then 5ul of water. Mix the components gently and preincubate the reaction mix at 30°C for 2 min. Initial the reaction by adding lOul of the control enzyme or the filtered supematant. The tyrosine kinase assay reaction is then terminated by adding 10 ul of 120mm EDTA and place the reactions on ice. Tyrosine kinase activity is determined by transferring 50 ul aliquot of reaction mixture to a microtiter plate (MTP) module and incubating at 37°C for 20 min. This allows the streptavadin coated 96 well plate to associate with the biotinylated peptide. Wash the MTP module with 300ul well of PBS four times. Next add 75 ul of anti- phospotyrosine antibody conjugated to horse radish peroxidase(anti-P-Tyr- POD(0.5u/ml)) to each well and incubate at 37°C for one hour. Wash the well as above. Next add lOOul of peroxidase substrate solution (Boehringer Mannheim) and incubate at room temperature for at least 5 mins (up to 30 min). Measure the absorbance of the sample at 405 nm by using ELISA reader. The level of bound peroxidase activity is quantitated using an ELISA reader and reflects the level of tyrosine kinase activity. Example 20: High-Throughput Screening Assay Identifying Phosphorylation Activity As a potential alternative and/or compliment to the assay of protein tyrosine kinase activity described in Example 19, an assay which detects activation (phosphorylation) of major intracellular signal transduction intermediates can also be used. For example, as described below one particular assay can detect tyrosine phosphorylation of the Erk-1 and Erk-2 kinases. However, phosphorylation of other molecules, such as Raf, JNK, p38 MAP, Map kinase kinase (MEK), MEK kinase, 137 Src, Muscle specific kinase (MuSK), IRAK, Tec, and Janus, as well as any other phosphoserine, phosphotyrosine, or phosphothreonine molecule, can be detected by substituting these molecules for Erk-1 or Erk-2 in the following assay. Specifically, assay plates are made by coating the wells of a 96-well ELISA plate with 0.1ml of protein G (lug/ml) for 2 hr at room temp, (RT). The plates are then rinsed with PBS and blocked with 3% BSA/PBS for 1 hr at RT. The protein G plates are then treated with 2 commercial monoclonal antibodies (lOOng/well) against Erk-1 and Erk-2 (1 hr at RT) (Santa Cruz Biotechnology). (To detect other molecules, this step can easily be modified by substituting a monoclonal antibody detecting any of the above described molecules.) After 3-5 rinses with PBS, the plates are stored at 4°C until use. A431 cells are seeded at 20,000/well in a 96-well Loprodyne filteφlate and cultured overnight in growth medium. The cells are then starved for 48 hr in basal medium (DMEM) and then treated with EGF (6ng/well) or 50 ul of the supematants obtained in Example 11 for 5-20 minutes. The cells are then solubilized and extracts filtered directly into the assay plate. After incubation with the extract for l hr at RT, the wells are again rinsed. As a positive control, a commercial preparation of MAP kinase (lOng/well) is used in place of A431 extract. Plates are then treated with a commercial polyclonal (rabbit) antibody (lug/ml) which specifically recognizes the phosphorylated epitope of the Erk-1 and Erk-2 kinases (1 hr at RT). This antibody is biotinylated by standard procedures. The bound polyclonal antibody is then quantitated by successive incubations with Europium-streptavidin and Europium fluorescence enhancing reagent in the Wallac DELFIA instrument (time-resolved fluorescence). An increased fluorescent signal over background indicates a phosphorylation. Example 21: Method of Determining Alterations in a Gene Corresponding to a Polynucleotide RNA isolated from entire families or individual patients presenting with a phenotype of interest (such as a disease) is be isolated. cDNA is then generated from these RNA samples using protocols known in the art. (See, Sambrook.) The cDNA is then used as a template for PCR, employing primers surrounding regions of interest in SEQ ID NO:X. Suggested PCR conditions consist of 35 cycles at 95°C for 30 seconds; 60-120 seconds at 52-58°C; and 60-120 seconds at 70°C, using buffer solutions described in Sidransky, D., et al., Science 252:706 (1991). 138 PCR products are then sequenced using primers labeled at their 5' end with T4 polynucleotide kinase, employing SequiTherm Polymerase. (Epicentre Technologies). The intron-exon borders of selected exons is also determined and genomic PCR products analyzed to confirm the results. PCR products harboring suspected mutations is then cloned and sequenced to validate the results of the direct sequencing. PCR products is cloned into T-tailed vectors as described in Holton, T.A. and Graham, M.W., Nucleic Acids Research, 19:1156 (1991) and sequenced with T7 polymerase (United States Biochemical). Affected individuals are identified by mutations not present in unaffected individuals. Genomic rearrangements are also observed as a method of determining alterations in a gene corresponding to a polynucleotide. Genomic clones isolated according to Example 2 are nick-translated with digoxigenindeoxy-uridine 5'- triphosphate (Boehringer Manheim), and FISH performed as described in Johnson, Cg. et al., Methods Cell Biol. 35:73-99 (1991). Hybridization with the labeled probe is carried out using a vast excess of human cot-1 DNA for specific hybridization to the corresponding genomic locus. Chromosomes are counterstained with 4,6-diamino-2-phenylidole and propidium iodide, producing a combination of C- and R-bands. Aligned images for precise mapping are obtained using a triple-band filter set (Chroma Technology, Brattleboro, VT) in combination with a cooled charge-coupled device camera (Photometries, Tucson, AZ) and variable excitation wavelength filters. (Johnson, Cv. et al., Genet. Anal. Tech. Appl., 8:75 (1991).) Image collection, analysis and chromosomal fractional length measurements are performed using the ISee Graphical Program System. (Inovision Coφoration, Durham, NC.) Chromosome alterations of the genomic region hybridized by the probe are identified as insertions, deletions, and translocations. These alterations are used as a diagnostic marker for an associated disease. Example 22: Method of Detecting Abnormal Levels of a Polypeptide in a Biological Sample A polypeptide of the present invention can be detected in a biological sample, and if an increased or decreased level of the polypeptide is detected, this polypeptide is a marker for a particular phenotype. Methods of detection are numerous, and thus, it is understood that one skilled in the art can modify the following assay to fit their particular needs. For example, antibody-sandwich ELISAs are used to detect polypeptides in a sample, preferably a biological sample. Wells of a microtiter plate are coated with 139 specific antibodies, at a final concentration of 0.2 to 10 ug/ml. The antibodies are either monoclonal or polyclonal and are produced by the method described in Example 10. The wells are blocked so that non-specific binding of the polypeptide to the well is reduced. The coated wells are then incubated for > 2 hours at RT with a sample containing the polypeptide. Preferably, serial dilutions of the sample should be used to validate results. The plates are then washed three times with deionized or distilled water to remove unbounded polypeptide. Next, 50 ul of specific antibody-alkaline phosphatase conjugate, at a concentration of 25-400 ng, is added and incubated for 2 hours at room temperature. The plates are again washed three times with deionized or distilled water to remove unbounded conjugate. Add 75 ul of 4-methylumbelliferyl phosphate (MUP) or p-nitrophenyl phosphate (NPP) substrate solution to each well and incubate 1 hour at room temperature. Measure the reaction by a microtiter plate reader. Prepare a standard curve, using serial dilutions of a control sample, and plot polypeptide concentration on the X-axis (log scale) and fluorescence or absorbance of the Y-axis (linear scale). Inteφolate the concentration of the polypeptide in the sample using the standard ~ curve. Example 23: Formulating a Polypeptide The secreted polypeptide composition will be formulated and dosed in a fashion consistent with good medical practice, taking into account the clinical condition of the individual patient (especially the side effects of treatment with the secreted polypeptide alone), the site of delivery, the method of administration, the scheduling of administration, and other factors known to practitioners. The "effective amount" for puφoses herein is thus determined by such considerations. As a general proposition, the total pharmaceutically effective amount of secreted polypeptide administered parenterally per dose will be in the range of about 1 μg/kg/day to 10 mg/kg/day of patient body weight, although, as noted above, this will be subject to therapeutic discretion. More preferably, this dose is at least 0.01 mg/kg/day, and most preferably for humans between about 0.01 and 1 mg/kg/day for the hormone. If given continuously, the secreted polypeptide is typically administered at a dose rate of about 1 μg/kg/hour to about 50 μg/kg/hour, either by 1-4 injections per day or by continuous subcutaneous infusions, for example, using a mini-pump. An intravenous bag solution may also be employed. The length of treatment needed to observe changes and the interval following treatment for responses to occur appears to vary depending on the desired effect. 140 Pharmaceutical compositions containing the secreted protein of the invention are administered orally, rectally, parenterally, intracistemally, intravaginally, intraperitoneally, topically (as by powders, ointments, gels, drops or transdermal patch), bucally, or as an oral or nasal spray. "Pharmaceutically acceptable carrier" refers to a non-toxic solid, semisolid or liquid filler, diluent, encapsulating material or formulation auxiliary of any type. The term "parenteral" as used herein refers to modes of administration which include intravenous, intramuscular, intraperitoneal, intrasternal, subcutaneous and intraarticular injection and infusion. The secreted polypeptide is also suitably administered by sustained-release systems. Suitable examples of sustained-release compositions include semi-permeable polymer matrices in the form of shaped articles, e.g., films, or mirocapsules. Sustained-release matrices include polylactides (U.S. Pat. No. 3,773,919, EP 58,481), copolymers of L-glutamic acid and gamma-ethyl-L-glutamate (Sidman, U. et al., Biopolymers 22:547-556 (1983)), poly (2- hydroxyethyl methacrylate) (R. Langer et al., J. Biomed. Mater. Res. 15: 167-277 (1981), and R. Langer, Chem. Tech. 12:98- 105 (1982)), ethylene vinyl acetate (R. Langer et al.) or poly-D- (-)-3-hydroxybutyric acid (EP 133,988). Sustained-release compositions also include liposomally entrapped polypeptides. Liposomes containing the secreted polypeptide are prepared by methods known per se: DE 3,218,121; Epstein et al., Proc. Natl. Acad. Sci. USA 82:3688-3692 (1985); Hwang et al., Proc. Natl. Acad. Sci. USA 77:4030-4034 (1980); EP 52,322; EP 36,676; EP 88,046; EP 143,949; EP 142,641; Japanese Pat. Appl. 83-118008; U.S. Pat. Nos. 4,485,045 and 4,544,545; and EP 102,324. Ordinarily, the liposomes are of the small (about 200-800 Angstroms) unilamellar type in which the lipid content is greater than about 30 mol. percent cholesterol, the selected proportion being adjusted for the optimal secreted polypeptide therapy. For parenteral administration, in one embodiment, the secreted polypeptide is formulated generally by mixing it at the desired degree of purity, in a unit dosage injectable form (solution, suspension, or emulsion), with a pharmaceutically acceptable carrier, i.e., one that is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation. For example, the formulation preferably does not include oxidizing agents and other compounds that are known to be deleterious to polypeptides. Generally, the formulations are prepared by contacting the polypeptide uniformly and intimately with liquid carriers or finely divided solid carriers or both. Then, if necessary, the product is shaped into the desired formulation. Preferably the carrier is a parenteral carrier, more preferably a solution that is isotonic with the blood of the recipient. Examples of such carrier vehicles include water, saline, Ringer's 141 solution, and dextrose solution. Non-aqueous vehicles such as fixed oils and ethyl oleate are also useful herein, as well as liposomes. The carrier suitably contains minor amounts of additives such as substances that enhance isotonicity and chemical stability. Such materials are non-toxic to recipients at the dosages and concentrations employed, and include buffers such as phosphate, citrate, succinate, acetic acid, and other organic acids or their salts; antioxidants such as ascorbic acid; low molecular weight (less than about ten residues) polypeptides, e.g., polyarginine or tripeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids, such as glycine, glutamic acid, aspartic acid, or arginine; monosaccharides, disaccharides, and other carbohydrates including cellulose or its derivatives, glucose, manose, or dextiins; chelating agents such as EDTA; sugar alcohols such as mannitol or sorbitol; counterions such as sodium; and/or nonionic surfactants such as polysorbates, poloxamers, or PEG. The secreted polypeptide is typically formulated in such vehicles at a concentration of about OJ mg/ml to 100 mg/ml, preferably 1-10 mg/ml, at a pH of about 3 to 8. It will be understood that the use of certain of the foregoing excipients, carriers, or stabilizers will result in the formation of polypeptide salts. Any polypeptide to be used for therapeutic administration can be sterile. Sterility is readily accomplished by filtration through sterile filtration membranes (e.g., 0.2 micron membranes). Therapeutic polypeptide compositions generally are placed into a container having a sterile access port, for example, an intravenous solution bag or vial having a stopper pierceable by a hypodermic injection needle. Polypeptides ordinarily will be stored in unit or multi-dose containers, for example, sealed ampoules or vials, as an aqueous solution or as a lyophilized formulation for reconstitution. As an example of a lyophilized formulation, 10-ml vials are filled with 5 ml of sterile-filtered 1% (w/v) aqueous polypeptide solution, and the resulting mixture is lyophilized. The infusion solution is prepared by reconstituting the lyophilized polypeptide using bacteriostatic Water-for-Injection. The invention also provides a pharmaceutical pack or kit comprising one or more containers filled with one or more of the ingredients of the pharmaceutical compositions of the invention. Associated with such container(s) can be a notice in the form prescribed by a governmental agency regulating the manufacture, use or sale of pharmaceuticals or biological products, which notice reflects approval by the agency of manufacture, use or sale for human administration. In addition, the polypeptides of the present invention may be employed in conjunction with other therapeutic compounds. 142 Example 24: Method of Treating Decreased Levels of the Polypeptide It will be appreciated that conditions caused by a decrease in the standard or normal expression level of a secreted protein in an individual can be treated by administering the polypeptide of the present invention, preferably in the secreted form. Thus, the invention also provides a method of treatment of an individual in need of an increased level of the polypeptide comprising administering to such an individual a pharmaceutical composition comprising an amount of the polypeptide to increase the activity level of the polypeptide in such an individual. For example, a patient with decreased levels of a polypeptide receives a daily dose OJ-100 ug/kg of the polypeptide for six consecutive days. Preferably, the polypeptide is in the secreted form. The exact details of the dosing scheme, based on administration and formulation, are provided in Example 23. Example 25: Method of Treating Increased Levels of the Polypeptide Antisense technology is used to inhibit production of a polypeptide of the present invention. This technology is one example of a method of decreasing levels of a polypeptide, preferably a secreted form, due to a variety of etiologies, such as cancer. For example, a patient diagnosed with abnormally increased levels of a polypeptide is administered intravenously antisense polynucleotides at 0.5, 1.0, 1.5, 2.0 and 3.0 mg/kg day for 21 days. This treatment is repeated after a 7-day rest period if the treatment was well tolerated. The formulation of the antisense polynucleotide is provided in Example 23. Example 26: Method of Treatment Using Gene Therapy One method of gene therapy transplants fibroblasts, which are capable of expressing a polypeptide, onto a patient. Generally, fibroblasts are obtained from a subject by skin biopsy. The resulting tissue is placed in tissue-culture medium and separated into small pieces. Small chunks of the tissue are placed on a wet surface of a tissue culture flask, approximately ten pieces are placed in each flask. The flask is turned upside down, closed tight and left at room temperature over night. After 24 hours at room temperature, the flask is inverted and the chunks of tissue remain fixed to the bottom of the flask and fresh media (e.g., Ham's F12 media, with 10% FBS, penicillin and streptomycin) is added. The flasks are then incubated at 37°C for approximately one week. 143 At this time, fresh media is added and subsequently changed every several days. After an additional two weeks in culture, a monolayer of fibroblasts emerge. The monolayer is trypsinized and scaled into larger flasks. pMV-7 (Kirschmeier, P.T. et al., DNA, 7:219-25 (1988)), flanked by the long terminal repeats of the Moloney murine sarcoma virus, is digested with EcoRI and HindllE and subsequently treated with calf intestinal phosphatase. The linear vector is fractionated on agarose gel and purified, using glass beads. The cDNA encoding a polypeptide of the present invention can be amplified using PCR primers which correspond to the 5' and 3' end sequences respectively as set forth in Example 1. Preferably, the 5' primer contains an EcoRI site and the 3' primer includes a HindlLI site. Equal quantities of the Moloney murine sarcoma virus linear backbone and the amplified EcoRI and HindEEE fragment are added together, in the presence of T4 DNA ligase. The resulting mixture is maintained under conditions appropriate for ligation of the two fragments. The ligation mixture is then used to transform bacteria HB 101, which are then plated onto agar containing kanamycin for the puφose of confirming that the vector has the gene of interest properly inserted. The amphotropic pA317 or GP+aml2 packaging cells are grown in tissue culture to confluent density in Dulbecco's Modified Eagles Medium (DMEM) with 10% calf serum (CS), penicillin and streptomycin. The MSV vector containing the gene is then added to the media and the packaging cells transduced with the vector. The packaging cells now produce infectious viral particles containing the gene (the packaging cells are now referred to as producer cells). Fresh media is added to the transduced producer cells, and subsequently, the media is harvested from a 10 cm plate of confluent producer cells. The spent media, containing the infectious viral particles, is filtered through a millipore filter to remove detached producer cells and this media is then used to infect fibroblast cells. Media is removed from a sub-confluent plate of fibroblasts and quickly replaced with the media from the producer cells. This media is removed and replaced with fresh media. If the titer of virus is high, then virtually all fibroblasts will be infected and no selection is required. If the titer is very low, then it is necessary to use a retroviral vector that has a selectable marker, such as neo or his. Once the fibroblasts have been efficiently infected, the fibroblasts are analyzed to determine whether protein is produced. The engineered fibroblasts are then transplanted onto the host, either alone or after having been grown to confluence on cytodex 3 microcarrier beads. 144 Example 27: Method of Treatment Using Gene Therapy - In Vivo Another aspect of the present invention is using in vivo gene therapy methods to treat disorders, diseases and conditions. The gene therapy method relates to the introduction of naked nucleic acid (DNA, RNA, and antisense DNA or RNA) sequences into an animal to increase or decrease the expression of the polypeptide. The polynucleotide of the present invention may be operatively linked to a promoter or any other genetic elements necessary for the expression of the polypeptide by the target tissue. Such gene therapy and delivery techniques and methods are known in the art, see, for example, WO90/11092, WO98/11779; U.S. Patent NO. 5693622, 5705151, 5580859; Tabata H. et al. (1997) Cardiovasc. Res. 35(3):470-479, Chao J et al. (1997) Pharmacol. Res. 35(6):517-522, Wolff J. A. (1997) Neuromuscul. Disord. 7(5):314- 318, Schwartz B. et al. (1996) Gene Ther. 3(5):405-411, Tsurumi Y. et al. (1996) Circulation 94(12):3281-3290 (incoφorated herein by reference). The polynucleotide constructs may be delivered by any method that delivers injectable materials to the cells of an animal, such as, injection into the interstitial space of tissues (heart, muscle, skin, lung, liver, intestine and the like). The polynucleotide constructs can be delivered in a pharmaceutically acceptable liquid or aqueous carrier. The term "naked" polynucleotide, DNA or RNA, refers to sequences that are free from any dehvery vehicle that acts to assist, promote, or facihtate entry into the cell, including viral sequences, viral particles, liposome formulations, lipofectin or precipitating agents and the like. However, the polynucleotides of the present invention may also be delivered in liposome formulations (such as those taught in Feigner P.L. et al. (1995) Ann. NY Acad. Sci. 772:126-139 and Abdallah B. et al. (1995) Biol. Cell 85(1): 1-7) which can be prepared by methods well known to those skilled in the art. The polynucleotide vector constructs used in the gene therapy method are preferably constructs that will not integrate into the host genome nor will they contain sequences that allow for replication. Any strong promoter known to those skilled in the art can be used for driving the expression of DNA. Unlike other gene therapies techniques, one major advantage of introducing naked nucleic acid sequences into target cells is the transitory nature of the polynucleotide synthesis in the cells. Studies have shown that non-replicating DNA sequences can be introduced into cells to provide production of the desired polypeptide for periods of up to six months. The polynucleotide construct can be delivered to the interstitial space of tissues within the an animal, including of muscle, skin, brain, lung, liver, spleen, bone marrow, thymus, heart, lymph, blood, bone, cartilage, pancreas, kidney, gall bladder, stomach, intestine, testis, ovary, uterus, rectum, nervous system, eye, gland, and 145 connective tissue. Interstitial space of the tissues comprises the intercellular fluid, mucopolysaccharide matrix among the reticular fibers of organ tissues, elastic fibers in the walls of vessels or chambers, collagen fibers of fibrous tissues, or that same matrix within connective tissue ensheathing muscle cells or in the lacunae of bone. It is similarly the space occupied by the plasma of the circulation and the lymph fluid of the lymphatic channels. Delivery to the interstitial space of muscle tissue is preferred for the reasons discussed below. They may be conveniently delivered by injection into the tissues comprising these cells. They are preferably delivered to and expressed in persistent, non-dividing cells which are differentiated, although delivery and expression may be achieved in non-differentiated or less completely differentiated cells, such as, for example, stem cells of blood or skin fibroblasts. In vivo muscle cells are particularly competent in their ability to take up and express polynucleotides. For the naked polynucleotide injection, an effective dosage amount of DNA or RNA will be in the range of from about 0.05 g/kg body weight to about 50 mg/kg body weight. Preferably the dosage will be from about 0.005 mg/kg to about 20 mg/kg and more preferably from about 0.05 mg/kg to about 5 mg/kg. Of course, as the artisan of ordinary skill will appreciate, this dosage will vary according to the tissue site of injection. The appropriate and effective dosage of nucleic acid sequence can readily be determined by those of ordinary skill in the art and may depend on the condition being treated and the route of administration. The preferred route of administration is by the parenteral route of injection into the interstitial space of tissues. However, other parenteral routes may also be used, such as, inhalation of an aerosol formulation particularly for delivery to lungs or bronchial tissues, throat or mucous membranes of the nose. In addition, naked polynucleotide constructs can be delivered to arteries during angioplasty by the catheter used in the procedure. The dose response effects of injected polynucleotide in muscle in vivo is determined as follows. Suitable template DNA for production of mRNA coding for polypeptide of the present invention is prepared in accordance with a standard recombinant DNA methodology. The template DNA, which may be either circular or linear, is either used as naked DNA or complexed with liposomes. The quadriceps muscles of mice are then injected with various amounts of the template DNA. Five to six week old female and male Balb/C mice are anesthetized by intraperitoneal injection with 0.3 ml of 2.5% Avertin. A 1.5 cm incision is made on the anterior thigh, and the quadriceps muscle is directly visualized. The template DNA is injected in 0J ml of carrier in a 1 cc syringe through a 27 gauge needle over one minute, approximately 0.5 cm from the distal insertion site of the muscle into the knee and about 0.2 cm deep. A suture is placed over the injection site for future localization, 146 and the skin is closed with stainless steel clips. After an appropriate incubation time (e.g., 7 days) muscle extracts are prepared by excising the entire quadriceps. Every fifth 15 um cross-section of the individual quadriceps muscles is histochemically stained for protein expression. A time course for protein expression may be done in a similar fashion except that quadriceps from different mice are harvested at different times. Persistence of DNA in muscle following injection may be determined by Southern blot analysis after preparing total cellular DNA and HIRT supematants from injected and control mice. The results of the above experimentation in mice can be use to extrapolate proper dosages and other treatment parameters in humans and other animals using naked DNA. Example 28: Transgenic Animals. The polypeptides of the invention can also be expressed in transgenic animals. Animals of any species, including, but not limited to, mice, rats, rabbits, hamsters, guinea pigs, pigs, micro-pigs, goats, sheep, cows and non-human primates, e.g., baboons, monkeys, and chimpanzees may be used to generate transgenic animals. In a specific embodiment, techniques described herein or otherwise known in the art, are used to express polypeptides of the invention in humans, as part of a gene therapy protocol. Any technique known in the art may be used to introduce the transgene (i.e., polynucleotides of the invention) into animals to produce the founder lines of transgenic animals. Such techniques include, but are not limited to, pronuclear microinjection (Paterson et al., Appl. Microbiol. Biotechnol. 40:691-698 (1994); Carver et al., Biotechnology (NY) 11:1263-1270 (1993); Wright et al., Biotechnology (NY) 9:830- 834 (1991); and Hoppe et al., U.S. Pat. No. 4,873,191 (1989)); retrovims mediated gene transfer into germ lines (Van der Putten et al., Proc. Natl. Acad. Sci., USA 82:6148-6152 (1985)), blastocysts or embryos; gene targeting in embryonic stem cells (Thompson et al., Cell 56:313-321 (1989)); electroporation of cells or embryos (Lo, 1983, Mol Cell. Biol. 3: 1803-1814 (1983)); introduction of the polynucleotides of the invention using a gene gun (see, e.g., Ulmer et al., Science 259:1745 (1993); introducing nucleic acid constructs into embryonic pleuripotent stem cells and transferring the stem cells back into the blastocyst; and sperm-mediated gene transfer (Lavitrano et al., Cell 57:717-723 (1989); etc. For a review of such techniques, see Gordon, "Transgenic Animals," Intl. Rev. Cytol. 115:171-229 (1989), which is incoφorated by reference herein in its entirety. Any technique known in the art may be used to produce transgenic clones containing polynucleotides of the invention, for example, nuclear transfer into 147 enucleated oocytes of nuclei from cultured embryonic, fetal, or adult cells induced to quiescence (Campell et al., Nature 380:64-66 (1996); Wilmut et al., Nature 385:810- 813 (1997)). The present invention provides for transgenic animals that carry the transgene in all their cells, as well as animals which carry the transgene in some, but not all their cells, i.e., mosaic animals or chimeric. The transgene may be integrated as a single transgene or as multiple copies such as in concatamers, e.g., head-to-head tandems or head-to-tail tandems. The transgene may also be selectively introduced into and activated in a particular cell type by following, for example, the teaching of Lasko et al. (Lasko et al., Proc. Natl. Acad. Sci. USA 89:6232-6236 (1992)). The regulatory sequences required for such a cell-type specific activation will depend upon the particular cell type of interest, and will be apparent to those of skill in the art. When it is desired that the polynucleotide transgene be integrated into the chromosomal site of the endogenous gene, gene targeting is preferred. Briefly, when such a technique is to be utilized, vectors containing some nucleotide sequences homologous to the endogenous gene are designed for the puφose of integrating, via homologous recombination with chromosomal sequences, into and disrupting the function of the nucleotide sequence of the endogenous gene. The transgene may also be selectively introduced into a particular cell type, thus inactivating the endogenous gene in only that cell type, by following, for example, the teaching of Gu et al. (Gu et al., Science 265: 103-106 (1994)). The regulatory sequences required for such a cell-type specific inactivation will depend upon the particular cell type of interest, and will be apparent to those of skill in the art. Once transgenic animals have been generated, the expression of the recombinant gene may be assayed utilizing standard techniques. Initial screening may be accomplished by Southern blot analysis or PCR techniques to analyze animal tissues to verify that integration of the transgene has taken place. The level of mRNA expression of the transgene in the tissues of the transgenic animals may also be assessed using techniques which include, but are not limited to, Northern blot analysis of tissue samples obtained from the animal, in situ hybridization analysis, and reverse transcriptase-PCR (rt-PCR). Samples of transgenic gene-expressing tissue may also be evaluated immunocytochemically or immunohistochemically using antibodies specific for the transgene product. Once the founder animals are produced, they may be bred, inbred, outbred, or crossbred to produce colonies of the particular animal. Examples of such breeding strategies include, but are not limited to: outbreeding of founder animals with more than one integration site in order to establish separate lines; inbreeding of separate lines 148 in order to produce compound transgenics that express the transgene at higher levels because of the effects of additive expression of each transgene; crossing of heterozygous transgenic animals to produce animals homozygous for a given integration site in order to both augment expression and eliminate the need for screening of animals by DNA analysis; crossing of separate homozygous lines to produce compound heterozygous or homozygous lines; and breeding to place the transgene on a distinct background that is appropriate for an experimental model of interest. Transgenic animals of the invention have uses which include, but are not limited to, animal model systems useful in elaborating the biological function of polypeptides of the present invention, studying conditions and/or disorders associated with aberrant expression, and in screening for compounds effective in ameliorating such conditions and/or disorders. Example 29: Knock-Out Animals. Endogenous gene expression can also be reduced by inactivating or "knocking out" the gene and/or its promoter using targeted homologous recombination. (E.g., see Smithies et al., Nature 317:230-234 (1985); Thomas & Capecchi, Cell 51 :503-512 (1987); Thompson et al., Cell 5:313-321 (1989); each of which is incoφorated by reference herein in its entirety). For example, a mutant, non-functional polynucleotide of the invention (or a completely unrelated DNA sequence) flanked by DNA homologous to the endogenous polynucleotide sequence (either the coding regions or regulatory regions of the gene) can be used, with or without a selectable marker and/or a negative selectable marker, to transfect cells that express polypeptides of the invention in vivo. In another embodiment, techniques known in the art are used to generate knockouts in cells that contain, but do not express the gene of interest. Insertion of the DNA construct, via targeted homologous recombination, results in inactivation of the targeted gene. Such approaches are particularly suited in research and agricultural fields where modifications to embryonic stem cells can be used to generate animal offspring with an inactive targeted gene (e.g., see Thomas & Capecchi 1987 and Thompson 1989, supra). However this approach can be routinely adapted for use in humans provided the recombinant DNA constructs are directly administered or targeted to the required site in vivo using appropriate viral vectors that will be apparent to those of skill in the art. In further embodiments of the invention, cells that are genetically engineered to express the polypeptides of the invention, or alternatively, that are genetically engineered not to express the polypeptides of the invention (e.g., knockouts) are administered to a patient in vivo. Such cells may be obtained from the patient (i.e., 149 animal, including human) or an MHC compatible donor and can include, but are not limited to fibroblasts, bone marrow cells, blood cells (e.g.. lymphocytes), adipocytes, muscle cells, endothelial cells etc. The cells are genetically engineered in vitro using recombinant DNA techniques to introduce the coding sequence of polypeptides of the invention into the cells, or alternatively, to disrupt the coding sequence and/or endogenous regulatory sequence associated with the polypeptides of the invention, e.g.. by transduction (using viral vectors, and preferably vectors that integrate the transgene into the cell genome) or transfection procedures, including, but not limited to, the use of plasmids, cosmids, YACs, naked DNA, electroporation, liposomes, etc. The coding sequence of the polypeptides of the invention can be placed under the control of a strong constitutive or inducible promoter or promoter/enhancer to achieve expression, and preferably secretion, of the polypeptides of the invention. The engineered cells which express and preferably secrete the polypeptides of the invention can be introduced into the patient systemically, e.g., in the circulation, or intraperitoneally . Alternatively, the cells can be incoφorated into a matrix and implanted in the body, e.g.. genetically engineered fibroblasts can be implanted as part of a skin graft; genetically engineered endothelial cells can be implanted as part of a lymphatic or vascular graft. (See, for example, Anderson et al. U.S. Patent No. 5,399,349; and Mulligan & Wilson, U.S. Patent No. 5,460,959 each of which is incoφorated by reference herein in its entirety). When the cells to be administered are non-autologous or non-MHC compatible cells, they can be administered using well known techniques which prevent the development of a host immune response against the introduced cells. For example, the cells may be introduced in an encapsulated form which, while allowing for an exchange of components with the immediate extracellular environment, does not allow the introduced cells to be recognized by the host immune system. Transgenic and "knock-out" animals of the invention have uses which include, but are not limited to, animal model systems useful in elaborating the biological function of polypeptides of the present invention, studying conditions and/or disorders associated with aberrant expression, and in screening for compounds effective in ameliorating such conditions and/or disorders. It will be clear that the invention may be practiced otherwise than as particularly described in the foregoing description and examples. Numerous modifications and variations of the present invention are possible in light of the above teachings and, therefore, are within the scope of the appended claims. 150 The entire disclosure of each document cited (including patents, patent applications, journal articles, abstracts, laboratory manuals, books, or other disclosures) in the Background of the Invention, Detailed Description, and Examples is hereby incoφorated herein by reference. Further, the hard copy of the sequence listing submitted herewith and the corresponding computer readable form are both incoφorated herein by reference in their entireties. 151 INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 65 . line N/A B. roENTΪFTCATIONOFDEPOSrr Further deposits are identified on an additional sheet | | Name of depositary institution American Type Culture Collection Address of depositary institution (including postal code and country) 10801 University Boulevard Manassas, Virginia 20110-2209 United States of America Date of deposit Accession Number February 12, 1998 209626 C ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet | | D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATEFURNISHINGOFINDICATIONSf/eαvefc/αn ιyno/αpp/ιcflWeJ The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications e.g., "Accession Number of Deposit") For receiving Office use only For International Bureau use only ^ | This sheet was received with the international application j j This sheet was received by the International Bureau on: PERRY HACKUY ^ INTERNATIONAL DlVSfOW ^705305^6517 Authorized officer usπoαw Form PCT/RO/134 (July 1992)

Claims: 152 What Is Claimed Is: 1 . An isolated nucleic acid molecule comprising a polynucleotide having a nucleotide sequence at least 95% identical to a sequence selected from the group consisting of: (a) a polynucleotide fragment of SEQ ID NO:X or a polynucleotide fragment of the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ED NO:X; (b) a polynucleotide encoding a polypeptide fragment of SEQ ED NO:Y or a polypeptide fragment encoded by the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ID NO:X; (c) a polynucleotide encoding a polypeptide domain of SEQ ID NO: Y or a polypeptide domain encoded by the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ID NO:X; (d) a polynucleotide encoding a polypeptide epitope of SEQ ID NO:Y or a polypeptide epitope encoded by the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ID NO:X; (e) a polynucleotide encoding a polypeptide of SEQ ID NO: Y or the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ID NO:X, having biological activity; (f) a polynucleotide which is a variant of SEQ ID NO:X; (g) a polynucleotide which is an allelic variant of SEQ ED NO:X; (h) a polynucleotide which encodes a species homologue of the SEQ ID NO: Y; (i) a polynucleotide capable of hybridizing under stringent conditions to any one of the polynucleotides specified in (a)-(h), wherein said polynucleotide does not hybridize under stringent conditions to a nucleic acid molecule having a nucleotide sequence of only A residues or of only T residues. 2. The isolated nucleic acid molecule of claim 1 , wherein the polynucleotide fragment comprises a nucleotide sequence encoding a secreted protein. 3. The isolated nucleic acid molecule of claim 1 , wherein the polynucleotide fragment comprises a nucleotide sequence encoding the sequence identified as SEQ ID NO:Y or the polypeptide encoded by the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ED NO:X. 153 4. The isolated nucleic acid molecule of claim 1 , wherein the polynucleotide fragment comprises the entire nucleotide sequence of SEQ ED NO:X or the cDNA sequence included in ATCC Deposit No:Z, which is hybridizable to SEQ ED NO:X. 5. The isolated nucleic acid molecule of claim 2, wherein the nucleotide sequence comprises sequential nucleotide deletions from either the C-terminus or the N- terminus. 6. The isolated nucleic acid molecule of claim 3, wherein the nucleotide sequence comprises sequential nucleotide deletions from either the C-terminus or the N- terminus. 7. A recombinant vector comprising the isolated nucleic acid molecule of claim 1. 8. A method of making a recombinant host cell comprising the isolated nucleic acid molecule of claim 1. 9. A recombinant host cell produced by the method of claim 8. 10. The recombinant host cell of claim 9 comprising vector sequences. 1 1. An isolated polypeptide comprising an amino acid sequence at least 95% identical to a sequence selected from the group consisting of: (a) a polypeptide fragment of SEQ ID NO: Y or the encoded sequence included in ATCC Deposit No:Z; (b) a polypeptide fragment of SEQ YD NO: Y or the encoded sequence included in ATCC Deposit No:Z, having biological activity; (c) a polypeptide domain of SEQ ID NO: Y or the encoded sequence included in ATCC Deposit No:Z; (d) a polypeptide epitope of SEQ ID NO: Y or the encoded sequence included in ATCC Deposit No:Z; (e) a secreted form of SEQ ID NO:Y or the encoded sequence included in ATCC Deposit No:Z; (f) a full length protein of SEQ ID NO: Y or the encoded sequence included in ATCC Deposit No:Z; 154 (g) a variant of SEQ ID NO: Y; (h) an allelic variant of SEQ ID NO: Y; or (i) a species homologue of the SEQ ED NO: Y. 12. The isolated polypeptide of claim 11 , wherein the secreted form or the full length protein comprises sequential amino acid deletions from either the C-terminus or the N-terminus. 13. An isolated antibody that binds specifically to the isolated polypeptide of claim 11. 14. A recombinant host cell that expresses the isolated polypeptide of claim 1 1. 15. A method of making an isolated polypeptide comprising: (a) culturing the recombinant host cell of claim 14 under conditions such that said polypeptide is expressed; and (b) recovering said polypeptide. 16. The polypeptide produced by claim 15. 17. A method for preventing, treating, or ameliorating a medical condition, comprising administering to a mammalian subject a therapeutically effective amount of the polypeptide of claim 11 or the polynucleotide of claim 1. 18. A method of diagnosing a pathological condition or a susceptibility to a pathological condition in a subject comprising: (a) determining the presence or absence of a mutation in the polynucleotide of claim 1; and (b) diagnosing a pathological condition or a susceptibility to a pathological condition based on the presence or absence of said mutation. 19. A method of diagnosing a pathological condition or a susceptibility to a pathological condition in a subject comprising: (a) determining the presence or amount of expression of the polypeptide of claim 11 in a biological sample; and (b) diagnosing a pathological condition or a susceptibility to a pathological condition based on the presence or amount of expression of the polypeptide. 155 20. A method for identifying a binding partner to the polypeptide of claim 11 comprising: (a) contacting the polypeptide of claim 11 with a binding partner; and (b) determining whether the binding partner effects an activity of the polypeptide. 21. The gene corresponding to the cDNA sequence of SEQ ED NO: Y. 22. A method of identifying an activity in a biological assay, wherein the method comprises: (a) expressing SEQ ID NO:X in a cell; (b) isolating the supematant; (c) detecting an activity in a biological assay; and (d) identifying the protein in the supematant having the activity. 23. The product produced by the method of claim 20. <110> Human Genome Sciences, Inc. <120> 36 Human Secreted Proteins <130> PZ025.PCT <140> Unassigned <141> 1999-02-24 <150> 60/076,051 <151> 1998-02-26 <150> 60/076,053 <151> 1998-02-26 <150> 60/076,054 <151> 1998-02-26 <150> 60/076,052 <151> 1998-02-26 <150> 60/076,057 <151> 1998-02-26 <160> 176 <170> Patentln Ver . 2.0 <210> 1 <211> 733 <212> DNA <213> Homo sapiens <400> 1 gggatccgga gcccaaatct tctgacaaaa ctcacacatg cccaccgtgc ccagcacctg 60 aattcgaggg tgcaccgtca gtcttcctct tccccccaaa acccaaggac accctcatga 120 tctcccggac tcctgaggtc acatgcgtgg tggtggacgt aagccacgaa gaccctgagg 180 tcaagttcaa ctggtacgtg gacggcgtgg aggtgcataa tgccaagaca aagccgcggg 240 aggagcagta caacagcacg taccgtgtgg tcagcgtcct caccgtcctg caccaggact 300 ggctgaatgg caaggagtac aagtgcaagg tctccaacaa agccctccca acccccatcg 360 agaaaaccat ctccaaagcc aaagggcagc cccgagaacc acaggtgtac accctgcccc 420 catcccggga tgagctgacc aagaaccagg tcagcctgac ctgcctggtc aaaggcttct 480 atccaagcga catcgccgtg gagtgggaga gcaatgggca gccggagaac aactacaaga 540 ccacgcctcc cgtgctggac tccgacggct ccttcttcct ctacagcaag ctcaccgtgg 600 acaagagcag gtggcagcag gggaacgtct tctcatgctc cgtgatgcat gaggctctgc 660 acaaccacta cacgcagaag agcctctccc tgtctccggg taaatgagtg cgacggccgc 720 gactctagag gat 733 <210> 2 <211> 5 <212> PRT <213> Homo sapiens <220> <221> Site <222> (3) <223> Xaa equals any of the twenty naturally ocurring L-amino acids <400> 2 Trp Ser Xaa Trp Ser 1 5 <210> 3 <211> 86 <212> DNA <213> Homo sapiens <400> 3 gcgcctcgag atttccccga aatctagatt tccccgaaat gatttccccg aaatgatttc 60 cccgaaatat ctgccatctc aattag 86 <210> 4 <211> 27 <212> DNA <213> Homo sapiens <400> 4 gcggcaagct ttttgcaaag cctaggc 27 <210> 5 <211> 271 <212> DNA <213> Homo sapiens <400> 5 ctcgagattt ccccgaaatc tagatttccc cgaaatgatt tccccgaaat gatttccccg 60 aaatatctgc catctcaatt agtcagcaac catagtcccg cccctaactc cgcccatccc 120 gcccctaact ccgcccagtt ccgcccattc tccgccccat ggctgactaa ttttttttat 180 ttatgcagag gccgaggccg cctcggcctc tgagctattc cagaagtagt gaggaggctt 240 ttttggaggc ctaggctttt gcaaaaagct t 271 <210> 6 <211> 32 <212> DNA <213> Homo sapiens <400> 6 gcgctcgagg gatgacagcg atagaacccc gg 32 <210> 7 <211> 31 <212> DNA <213> Homo sapiens <400> 7 gcgaagcttc gcgactcccc ggatccgcct c 31 <210> 8 <211> 12 <212> DNA <213> Homo sapiens <400> 8 ggggactttc cc 12 <210> 9 <211> 73 <212> DNA <213> Homo sapiens <400> 9 gcggcctcga ggggactttc ccggggactt tccggggact ttccgggact ttccatcctg 60 ccatctcaat tag 73 <210> 10 <211> 256 <212> DNA <213> Homo sapiens <400> 10 ctcgagggga ctttcccggg gactttccgg ggactttccg ggactttcca tctgccatct 60 caattagtca gcaaccatag tcccgcccct aactccgccc atcccgcccc taactccgcc 120 cagttccgcc cattctccgc cccatggctg actaattttt tttatttatg cagaggccga 180 ggccgcctcg gcctctgagc tattccagaa gtagtgagga ggcttttttg gaggcctagg 240 cttttgcaaa aagctt 256 <210> 11 <211> 1441 <212> DNA <213> Homo sapiens <400> 11 ggcacgagtt ttatttatct tgcctagggt gtgttgggct tcataaatct gtggattggt 60 atctttcgtc agttctgtaa aagtctcagg tactctttgt taacattcgt ctctgcccca 120 tttttcttct agaattatga tcaaacatgc actaattaga ccttttattg tattctcttt 180 gcttcttagg ctatgctctg aaaatttatt ttgtcctaat actcagttta tagttctgtc 240 ttgtttccaa tctgttgtta aatccctcct ttcaatttta aatctcagtt actgtatttt 300 ttaattctag aaggtcgttt ggttctttca aatccactag atcaagtcac tctctgtgac 360 ttcctacgac ctatattcta gcctttgcct tttattattt tttaacattg taagcaaagt 420 tgttttatag ttgataattc ttgtatctgt ggtctttgtc tcttcatact agctgttatt 480 tcttaacagt tttccctgat cccaccttac ttcctcatag atttgattat ctttgattat 540 gtgctgctta ttttttttaa agataattat ctgtattaat atgagaccta gattttaaga 600 tacttcccct caggattgtg ctgtgtgcct gggcacattg caagtccaaa ttactttaaa 660 gtatcctaga acaccagagg tgaaaattca tgccattctc gtgcatcttt accttatggg 720 tatagcccat tgggaatcct tagtgtcggg agggagttct attacacctt ccacttcggg 780 cagatcctgg gctttgacat tcgtcctctt catcataacc aaatatcaga cttgcctaat 840 gcgtaaatgc ccttggggta aagcatctgt gttctgctta cctctcaggg ttcctgcttt 900 tccctttagc tttggttcca tcacttgtgt gttcaaccag tatgggaaac tgcctctaga 960 agcagtgttt taaaatttta gtctaaccat aaaaatagag aatgcttacc ctctggatat 1020 aaatgccata gcgataactt tgaactccta cattacatgc cttttatgta aggcaaacct 1080 cagtacacat tgagagacag tgtcatatac ttattaagat cacaggctct aaaatcagac 1140 tgccttgttt aaatcctggc cctgccatgt agtagtaacc tgtgttaatt tatgcaagat 1200 acgtaatctc tctgtgcctt ggtttcttcg tttaaaaagc agaataatag cttgcctcat 1260 gtggtcatta tgaaaaacaa acaaggccgg gcaccgtggc ttacgcctgt agtctcagca 1320 ctttgggagg ctgaggtggg cagatgacct gaggtcggga gtttgagacc agcctgccca 1380 acatggagga accccgtctc tactgaaaaa aaaaaaagag agagagagag agagaactag 1440 t 1441 <210> 12 <211> 2160 <212> DNA <213> Homo sapiens <400> 12 ttttgaattc tatagattgt cttggaagga tactgtgtga tgggtcaggc acacagtaat 60 tggagacttt taatgtatgt aatatttcat agattgcatg ctattaatca tctgtgaggg 120 tagtattttt tgttttattg taagtttccc tcttttttta taaattaaaa gatggttggt 180 attaggaatt tcaaatgaat gcagaaaatc ttacatgctg tgtactatta atattataac 240 agacgatcca agtccaaaat ctgaccaata aagcaaccat tttatcaaga tagagggatt 300 ctaatgggag aggggattct tccctcctga agtttgtgtg tccagtcccc ttaaaaaaaa 360 tgaatagttg tcttttcttg tgcatattaa tactcgaaag tgccatggtg gtattaatga 420 aagtacactt tattgttgcc tttgaactta cggccaaggc aataaatcag aaacaaaaat 480 agtgccaatg tgtcaaaatc gacatctgag agattcagcc tcccatttgg aataaatatg 540 aatcttctaa gctatcttgt ttaatatttt ccatcattta gctacttcct atctccctca 600 gaggcgcctg ctgttcccat tttagagttg acagtggcct gctaattttg ctatgttcct 660 aaaagttact gggtgtgaga cattttcatc ccctcctttt tcctactgct ggtgtttatt 720 atccagctag acaatatttt atgcatattt accgtgatgt ctggaccgta cctgtgctcc 780 ttggcagttt atgttgaaga taactaaaga tttttctctt tgggaggcat caaaatgatg 840 gtagtttgct tttatctttt tatgttcatt ttcttttagt aggtgacctt tctgcattaa 900 gaactgtttt tatcttttac taccttttct tttctccttt gtggagacag catgacatgt 960 cctgaaggtc acctttgcct ttgaaaaagg tttgatggag gaattcacag gtgactgaca 1020 agtctttgaa aagaatggga tctgctcact tctggtcttt ttggccggga actcctgatt 1080 ggtgttaagg tggtaatttc ccccatataa gatttagaat cactgagttt gagctagatg 1140 aaatttttaa aatttctggt tgtctcatta gactgatgag gtgagttttc ttcttcatat 1200 gaacagctag ttaataacag cagagttctc actcagtgct cagtacttaa ttttccactg 1260 caccacaact gtcttaacta aatgtgctgt atttttcttt aaaagttaag agttctattt 1320 ggtgttttca ggaatatacg tgaaaagaca tgccatgttt tggtaaatac catcagagtt 1380 gtgtaaaggc gtgtactaag tgcaatctta atttgtggaa ataatcttca tttacccctc 1440 ctaaaactac actcagtata aacactttcc cataaggtgt gtgcagtaaa aatgttatat 1500 tactccaaca ctggcaggag cacagcacag cagccttatt ggagagagcc ttataaaagt 1560 gattaaatgg aggcattgag ctcattacct ttaagtttac tttgtgctga cctttgttcc 1620 tgttttgaga atctcatata attattaaaa aaaaaaaaca attaaaacga aacggcgggg 1680 cctagctgtg tataaatgat ccttgctgaa tatcttaagg ttttttgtaa gaaaaaagaa 1740 aaaccaacaa aaaaagctta ttttcacatt aaaatgaaac ctcttttgca acttaagaat 1800 tctatggaaa agcagttttt atcatatttt gtgtccatgc accatttttc ttaaaatggc 1860 ttacaaaaaa gaatgtaaac aatttgtgat ctggccagtt gtacttttag ctcccagagg 1920 gagagttggt ggtattatga gttgagtaaa aaccatccag gggaacttga gggagcagtc 1980 tgttgccagt aatgttcctt gtgtgccatt aaaccacctc cagatgagtg gaggaacatc 2040 actttttaat tttttaattg tatttggaat tgttgccgtg tactaagaac ttgacctaaa 2100 taaaatccca caaagtataa aaaaaaaaaa aaaaaaaaaa aagggcggcc gctcgcgatc 2160 <210> 13 <211> 1202 <212> DNA <213> Homo sapiens <400> 13 gggtcgaccc acgcgtccgg tttttttaga aatagaagtg cttacagatt tgtttgagca 60 gaatagatac ccatgttcag agagagagag agagagccat tgagaggcas agagtgccga 120 atgtgaattc tgtgtaaatt gaaaagttac ggtccccgtc cataaggaga tggctctggt 180 tgtcttgaat ttagacagct ttccagagga ggaggttctc tcctgcagca gtgtgggaaa 240 aaaatctacc agatttggac cagaatgact gcaatttagg tcagaacatg atacttagag 300 ggaaaaaagt aatcatggct tgaatagctg ccctaaggcc agctacaggg ctgcagggtc 360 tgtggacctt tcttgtcaga actcaggatc cttaggagtc cccacaaggg catggaggct 420 gtggccatca tgagtggaag aaccagcttc caaaggaacc taggattgtt ctggccctgg 480 ctccaggtgc atatctctgc tttccgtgag cattgaatgg gaaatcacgt gttagcagaa 540 taaatcccag aatacacatt caggaggaga tggttccaca tggcacgtaa gtcctttgcc 600 ttattgatgt ttgtctggca gatgtcctta agccttccca tcaagggctt tattctaagg 660 gtggctaact ggctatttaa acctcatctc aatagtgtct gtctaggatg gcaaaatcac 720 accaggttct gctgggcaaa tctcccaggt ggcgtattgc tagaggagag cgccactgca 780 gaggacacac tgtcttggcc actggctttg caaaccatag tggaggaggg agtctggggt 840 caccaaccac ttcctggctg actgcctgag ccacattata caagactgtt tgttgactta 900 gtaatactga agccagagct caccaagatt ctgacatcaa gcatgaaagt gactaattct 960 ttcawttccc agcactttga caaaggggac tctcttaaaa ctcctcatcg gacgttagtg 1020 gaagtcgact catgtatcta aacatgtagc cagcgtaagt tcttggtcag attgatctaa 1080 tgactttttt agcgtgtgtg tgtgtgtgtg tgtgtgtgtt taatcttttt aagtttgggt 1140 gaagtttgac cttctagaat tcctgtttat tcctgagcaa aaaaaaaaaa aaaaaactcg 1200 ag 1202 <210> 14 <211> 1554 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (695) <223> n equals a,t,g, or c <220> <221> SITE <222> (874) <223> n equals a,t,g, or c <220> <221> SITE <222> (1190) <223> n equals a,t,g, or c <400> 14 gctttaatag tgtacactta cacatctgga aggaagagag ttccatatgg cagggatgat 60 tgggacagga gggatctttt gataactttg tgtgagcatg aaaatcgaat ggggaaggga 120 gagctgtgaa aaaaaaatgt tatctctttt tttttgcttc tggaaaccca gctttttggt 180 cagccgtctt gtgatttggc tgggcctggt ttgtgggggt cgctctctga gttgggtagc 240 tcttggagaa gattatctgg gaactcccat ccttatccca aacatacacc aaacctgccc 300 ccatccacca ttatgggaat tagtaccaga gcatccttgc agattagttc tcattttctc 360 tctttgtgag cacacacaca tcaggtagag ttccagaaac ccagctttag gacactgttc 420 acatatcaca ggaggagcaa ggacatgaat acaagagagc tctttcctga ccagcagtgg 480 gargtggttg tactatctat ttawttgttt attwatttat ttattttttg agatggartc 540 tccttctgtc acccaggctg gagtgcagtg gcatgatctc ggctcactgc aatctctgcc 600 tcctgggttc aagcagtcct cctgcctcag ccccccaagt agctgsgatt acaggctgca 660 ccaccatgcc ccgctaattt ttgtattttt agtanagatg gggtttcacc atgttggcca 720 ggctggtctg taactcctga mctcaggtga tccacctgcc ttagcctccc aaggtgctgg 780 gattacaggt gtgagccacc gtgcccggsc tggttccact atttattaaa atgtatatat 840 gtgttttyca cttttttggt aggcatttta ttgntaataa tttggaaatt aaaaaaattt 900 ctccacaagc ttattttttg tggagacaag gtctccctgt gttgcctagg ctggtcttga 960 attcctgggc taagtgattg gtctgccttg gcctctcaaa gtgctgggga ttacaggcat 1020 aagtcaccat gccctgtttg scagcaagkt ttawackgct ctttttggta gggawwtkct 1080 maggtwcagt gatagagaac atgkagttgt ggtgggawac agtggctyat gactgtatcc 1140 gcactttggg aggctgaggc aggaggattg cttgaggctg agagttgagn acaggcctgg 1200 gcaacatagc aagacacctt ctctaaaatg aaaaaaatta gctggatgtg gtgtcatgta 1260 cctgtagtcc cagttgcttg ggaggctgag gcaggaggat cacttgagcc tgggtgttca 1320 agataggcct ggtcaacaca gcaagacccc ttctctaaaa atgaaaataa aaaaattagc 1380 tggttgtggt ggcatgtacc tgtagtccca gttacttggg aggctgagac aggaggattg 1440 cttgagccag gggtttgagg ctgcagtgag ctatgactgc tcccctgcac cccaggctgg 1500 gtgacagagt gagacccagt ctctaaaata aaaaaaaaaa aaaaaaaact cgta 1554 <210> 15 <211> 1540 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (651) <223> n equals a,t,g, or c <220> <221> SITE <222> (1124) <223> n equals a,t,g, or c <400> 15 agaattcggc acgagggcat attactttcc taggactgcc acaacaaact attaccaact 60 agcggcttaa aacaacaaga gcttattcct cacagttctg gaggccagaa gtccaaaacc 120 aaggtgtcag gaaggtcatg ctctctccaa agtctccaag gatgctcctt ccttgcctcc 180 tccagcctct ggtcgtggcc aacatcccga gggttccttg gcttgcagat gaatcactta 240 atcccacccc catcatcaca tggcagtccc cctgtgtagc tcagctctgt ccaaatttcc 300 cctttcctac aaggacatta gtcactggat tatgacacag ctcatcttaa ctggattata 360 tctgcaaaga ccctgttata tctgcaaaga cgagttaaca ttcacatgtt ccaggggaga 420 tatgaatttt aaggggacag tattggaccc agtataggag ggcaggcagc agcgagggag 480 ccagggaggg ctggcctgac ttgagcctgt ttgaaaagca tcatcctcct accaagactg 540 ggggctgctg gttctgacaa ggtttgcagg atcagctggg atgatgggtt scamccaytc 600 cttcgagyta cgttggaccc ctgggcccac ttacagcaag gagcttgccc ntycgtgtag 660 ctctycgtca gtgtgggaaa atctgartga gccagagaag ggtgagattc cccctgcaga 720 gcaggcagta ctgagcaaat ccaggatcca gaactccagt tctaatcctg gctcttgcct 780 gctttcctgt gtgaccctgg ggaagtggtt ttccctctct gagactctcc ttccccatgt 840 gagtcacaag ggctgggcct agctgacccc caaggccctt acatgagtgg atagttgcat 900 tttaaacctg gtgctcccca ggataaggga gtcaacccca aggagactgg ggtttctcct 960 gagcctggcc cctggggatg agcactcact gtggaaaaag ctggccactt cttagccctt 1020 gtcatgggca gaaaacatgc ccctccagcc ccaccagcac caacacacag ccaagctcac 1080 tgtttcattt ttagagagaa atcagggctt tcggtgcagc tgantgacac agacaagggg 1140 cggggggaca tgaaagggag cgggcaagga cggaaattac acttctccta gcaacctggt 1200 tctgcagctc ctaggcctgg ggccgcgtga tacatgccat tcccaattaa cgggatgtta 1260 aatatacccc ggctcagcct gccccatgct gagccccgcc tggggcagtg cagggagcca 1320 tgtgatggtg tagagcactc tgcaacaccc catattcatg ttcccactcc tagggccccg 1380 ctcggtcccc aggaggccag agcggtcctg ccctctgcct gagcatggct cagctccagc 1440 ctccacttgc cctcccctat gctggccagc tcgggggtct gcaggcagcc tgtggggcag 1500 ggccagttgg ccaaactctc caagccagaa gcccctcgag 1540 <210> 16 <211> 1057 <212> DNA <213> Homo sapiens <400> 16 tcgacccacg cgtccgctga gattacaggt gtgagccacc aggctcagcc ccctaagatt 60 tgaaacactt taaatggccc atggtagggt tcctgctagg ataaaacatt aagcggctgt 120 taaaagaaat aaaaggagga cacgtctctg tgcactggtg tggacaaatc tccaagtcac 180 tgcaaaatgg aaaaagtata agatgctctt tccctgaacc tcaagggtcc cgcccctctc 240 actttcaggt ctctggacct ctgactgaca ctgtgcctgc ccaggtccct gtatgcactg 300 ccacagtgcc ctgggcccca tgtccacccc tgtcctgccc ttctctggga tagggctggc 360 cttcctctgc ctctgcctgg ctgcatccat ggtcgatctc aagtgccttg gcatgaactc 420 cactctcctg cagccttcaa tcaaggaatg atggggatgt gtacataccc caccccaccc 480 cttggcaggg tgatgctgag gtgtggattt ttaacagttc ccagactttc ccaggaggct 540 tgggtttggg tgcccacagt gggagctggt gtgatatcat accttcgccg gccgcctttc 600 cttcctgttc tctgtgcccc tactcccact ctagagctgc cccgtttctc tgttttcgtg 660 aaagagctga ccctgtgctg cctcccactc tcccaatgcc cctgccactc ctgtgagcct 720 gctgctggtg aggtcggtgc tgacctctgt gttgctggat aatgagtcat ctatctctgg 780 aggagaagaa aggcaggtcc tccacagccc tgataaaatc tccaagtctc ccagtttcgg 840 gtccctctcc tgggatgcag acccactgcc tgcccagctg gtacgatcca catgccctct 900 tcttgggaat aggggcatgg gaaagtgact aaagatactg ttctggctgc tgtgttcact 960 gtgagtaata aactgtccat ttctccgaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa 1020 aaaaaaaaaa aaaaaaaaaa aaaaaaaggg cggccgc 1057 <210> 17 <211> 2080 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (145) <223> n equals a,t,g, or c <400> 17 aattcggcac gagaccttta gggtgcgcgg gtgcagtata tctcgcgctc tctccccttt 60 ccccctcccc tttccccacc ccgggcgctc aggttggtct ggaccggaag cgaagatggc 120 gacttctggc gcggcctcgg cgganctggt gatcggctgg tgcatattcg gcctcttact 180 actggctatt ttggcattct gctggatata tgttcgtaaa taccaaagtc ggcgggaaag 240 tgaagttgtc tccaccataa cagcaatttt ttctctagca attgcactta tcacatcagc 300 acttctacca gtggatatat ttttggtttc ttacatgaaa aatcaaaatg gtacatttaa 360 ggactgggct aatgctaatg tcagcagaca gattgaggac actgtattat acggttacta 420 tactttatat tctgttatat tgttctgtgt gttcttctgg atcccttttg tctacttcta 480 ttatgaagaa aaggatgatg atgatactag taaatgtact caaattaaaa cggcactcaa 540 gtatactttg ggatttgttg tgatttgtgc actgcttctt ttagttggtg cctttgttcc 600 attgaatgtt cccaataaca aaaattctac agagtgggaa aaagtgaagt ccctatttga 660 agaacttgga agtagtcatg gtttagctgc attgtcattt tctatcagtt ctctgacctt 720 gattggaatg ttggcagcta taacttacac agcctatggc atgtctgcgt tacctttaaa 780 tctgataaaa ggcactagaa gcgctgctta tgaacgtttg gaaaacactg aagacattga 840 agaagtagaa caacacattc aaacgattaa atcaaaaagc aaagatggtc gacctttgcc 900 agcaagggat aaacgcgcct taaaacaatt tgaagaaagg ttacgaacac ttaagaagag 960 agagaggcat ttagaattca ttgaaaacag ctggtggaca aaattttgtg gcgctctgcg 1020 tcccctgaag atcgtctggg gaatattttt catcttagtt gcattgctgt ttgtaatttc 1080 tctcttcttg tcaaatttag ataaagctct tcattcagct ggaatagatt ctggtttcat 1140 aatttttgga gctaacctga gtaatccact gaatatgctt ttgcctttac tacaaacagt 1200 tttccctctt gattatattc ttataacaat tattattatg tactttattt ttacttcaat 1260 ggcaggaatt cgaaatattg gcatatggtt cttttggatt agattatata aaatcagaag 1320 aggtagaacc aggccccaag cactcctttt tctctgcatg atacttctgc ttattgtcct 1380 tcacactagc tacatgattt atagtcttgc tccccaatat gttatgtatg gaagccaaaa 1440 ttacttaata gagactaata taacttctga taatcataaa ggcaattcaa ccctttctgt 1500 gccaaagaga tgtgatgcag awgctcctga agatcagtgt actgttaccc ggacatacct 1560 attccttcac aagttctggt tcttcagtgc tgcttactat tttggtaact gggcctttct 1620 tggggtattt ttgattggat taattgtatc ctgttgtaaa gggaagaaat cggttattga 1680 aggagtagat gaagattcag acataagtga tgatgagccc tctgtctatt ctgcttgaca 1740 gccttctgtc ttaaaggttt tataatgctg actgaatatc tgttatgcat ttttaaagta 1800 ttaaactaac attaggattt gctaactagc tttcatcaaa aatgggagca tggctataag 1860 acaactatat tttattatat gttttctgaa gtaacattgt atcatagatt aacattttaa 1920 attaccataa tcatgctatg taaatataag actactggct ttgtgaggga atgtttgtgc 1980 aaaatttttt cctctaatgt ataatagtgt taaattgatt aaaaatcttc cagaattaaa 2040 aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa gggcggccgc 2080 <210> 18 <211> 602 <212> DNA <213> Homo sapiens <400> 18 aattcggcac agkttgtgtt tctmatgttc caggtccggc caggctggca gctcctgctg 60 gtcatgtttt cctcatgtgc tgtttccaac cagctcttgg tctggtaccc agcaactgcc 120 ttagcagaca acaaacctgt agcacctgac cgacgaatca gtgggcatgt gggcatcatc 180 ttcagcatgt catacctgga aagcaaggga ttgctggcta cagyttcaga agaccgaagc 240 gttcgtatct ggaaggtggg cgacctgcga gtgcctgggg gtcgggtgca gaatattggg 300 cactgctttg ggcacagcgc ccgtgtgtgg caggtcaagc ttctagagaa ttaccttatc 360 agtgcaggag aggattgtgt ctgcttggtg tggagccatg aaggtgagat cctccaggcc 420 tttcggggac accaggatgt gtacccggtt gtagtaggag ctgaaatcca tgctgagctg 480 taccaggaac ttgcatatct agagacagag actgagtcac tggcccatct ctttgctctt 540 gtccccaggc cagaataaag aatagagtgt aaaaaaaaaa aaaaaaaaaa aaaaaactcg 600 ag 602 <210> 19 <211> 629 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (533) <223> n equals a,t,g, or c <400> 19 gcacactttg accacttgtg atgagcctta tttgggagca aggtcttcaa ctttgtggtt 60 tttgtttgtt ttatttggtt ttctgcttct gcattagttc acttagggtg atggctttca 120 gctgctycca tgttgcttgc tgcaaaggat atgattttgt ycttttttat ggctgtgtag 180 tattccatgg tgtatatgga ccacattttc tttatccaat ccaccatata tgggcaccta 240 ggttgattcc atgtctttgc tattgtgaat agcactgtga tgaacataga agtggattaa 300 atttcttttt cttgacagtc tcctaattta tgcttgtaca tatatttttc tctcatgcct 360 tgaggttttt aaaagtcctc tcctctttct catggcaata cttttactaa agtacatttc 420 ctgggaatcc ttagggttcc ccttattttg aataggctga atattttcat atgtttggtg 480 atttttatct tttaatcctt taataggttt gaaagtctct cttgatatgg gtngctcaga 540 taggctccat cgtagagtct agaaatcatc ctatgatttt tttttgccca ttcctaggtt 600 aaaaaaaaaa aaaaaaaaaa aaactcgag 629 <210> 20 <211> 2067 <212> DNA <213> Homo sapiens <400> 20 aattcggcac gaggaaaaac aaaagttttt taaaacaata aaagttaaca gtcaataatg 60 tgtttgtcgg caagaagccc tctgttaata atggtctaaa caaataagac attgtttttc 120 tccaataaag aaatccagag gcaggcagta gctggctttg attcagcctc tgactgtcac 180 tgtcagggcc ccaggcccca tgagcctttc gtctttcctg catgttggct tatcttctca 240 tgcttgtgac ttcctggttg caacacggct gctgcaacac cagacatctt gcctgtcttc 300 aaggcaggaa ggagggggaa actatcgcct accagctatt tttcttacct tagctcctcc 360 atgtcttgga tcaaaagcat ctctttgaac ctctccctca ggcataccct gaaatgctgt 420 ggactttaac cttttttctg ttgcaaaggt cgctcacatc tccctggttg tttggtcttc 480 tcttccttgg ctctagtaac acagcagtct gttgcttcct aggacaactt ataatgggac 540 ccaaagggga aagaggattt cccgggcctc caggaagatg tctttgtgga cccactatga 600 atgtgaataa cccttcctac ggggaatctg tgtatgggcc cagttccccg cgagttcctg 660 tggtaaggct ttctgggaga agtctggggt ggttatccgt gaggacctct cacctgatcc 720 ttatggggct ttgtaaaatc ctttcagtaa aactaacttt ttttcacgac tctgagtaca 780 ccctcattat aggaaattgg aaaatatgag aaaatcaaga ggaaaaccaa attgtccatt 840 tgattgtgag tccattttgg ggtattttct ttgtcttatt aaaatctaac ttttatatgg 900 ttgagattat attgtataaa aatgtacttt tggccgggca tggtggctta tgcctgtaat 960 cccagcactt tgggaggcca aggtgggtgg attataaggt caggagttcg agatcagcct 1020 ggccgataca gtgaaacccc atctctacta aaaaatatat ttaaaaaatt agccgggcgc 1080 ggtggtgcac gcctgttgtc tcagctactt gggaggctga ggtgggagaa tcgcttgaac 1140 ccaggaggcg gagattgcag tgagctgaga tagcaccact gcactccagc ctgggcaaca 1200 gagcgagact ccgtctcaaa aaaagttata ctttgktatc ttagttgaaa tcctgccatg 1260 tttccacact ctataaataa cattttaaac tttttattag ggaaaatttc aaatacatat 1320 aaaagcagaa caaatagtgt aatgaacccc tgtgtaccct tcacccaact ttaataatga 1380 tcaactcatg gcgagcctgt gtccttgttt tctctttatg cctactcact cctgcccatt 1440 ctctgttgta ttattttgaa gtaaaccttg gacatctgtt catcataatc atccatctag 1500 tgtggctgtg ctacaattta cttaaccagt gttggtgttt aaccaaccta ttgcttattg 1560 10 gccaccccca agctttttac taatgtaaat aatgctgtaa agaatatctt tgagtaggat 1620 aattttaaga atcacttcca gatgtcaaat tacttgacta tatgacattg ccttttaact 1680 taagtcttgg gaacgtttta aatatttaaa aatgttaaat ccgaggccgg gcgcggtggc 1740 tcatgcctgt aatcccagaa ctttgggagg ccgaggtggg tggatcacct tgaggtcagg 1800 agctcgcaac cagcctggcc aacatggcga aaccctatct ctactaaaaa tacaaaagtt 1860 agccaggcat tgtggtgcac acctgtaatc ccacctactc gagaggctga ggcaggagaa 1920 ttgcttgaac ccgggaggca gaggttgcaa tgagccgaga tcacgctact tcactccagc 1980 ctgggcaacc gcgtgagact ccatctcaaa aacaaaagaa aaaaaaaaaw aaaaaaaccg 2040 gcacgagggg gggcccgtac ccaatcg 2067 <210> 21 <211> 997 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (963) <223> n equals a,t,g, or c <400> 21 cccgactcta ggccggaagc gcgcggagac catgtagtga gaccctcgcg aggtctgaga 60 gtcactggag ctaccagaag catcatgggg ccctggggag agccagagct cctggtgtgg 120 cgccccgagg cggtagcttc agagcctcca gtgcctgtgg ggctggaggt gaagttgggg 180 gccctggtgc tgctgctggt gctcaccctc ctctgcagcc tggtgcccat ctgtgtgctg— 240 cgccggccag gagctaacca tgaaggctca gcttcccgcc agaaagccct gagcctagta 300 agctgtttcg cggggggcgt ctttttggcc acttgtctcc tggacctgct gcctgactac 360 ctggctgcca tagatgaggc cctggcagcc ttgcacgtga cgctccagtt cccactgcaa 420 gagttcatcc tggccatggg cttcttcctg gtcctggtga tggagcagat cacactggct 480 tacaaggagc agtcagggcc gtcacctctg gaggaaacaa gggctctgct gggaacagtg 540 aatggtgggc cgcagcattg gcatgatggg ccaggggtcc cacaggcgag tggagcccca 600 gcaaccccct cagccttgcg tgcctgtgta ctggtgttct ccctggccct ccactccgtg 660 ttcgaggggc tggcggtagg gctgcagcga gaccgggctc gggccatgga gctgtgcctg 720 gctttgctgc tccacaaggg catcctggct gtcagcctgt ccctgcggct gttgcagagc 780 caccttaggg cacaggtggt ggctggctgt gggatcctct tctcatgcat gacacctcta 840 ggcatcgggc tgggtgcagc tctggcagag tcggcaggac ctctgcacca gctggcccag 900 tctgtgctag agggcatggc agctggcacc tttytytata tcacctttyt ggaaatcctg 960 ctntttcatc ccaaatttaa gggggtttca agaagaa 997 <210> 22 <211> 1383 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (556) <223> n equals a,t,g, or c <220> <221> SITE <222> (562) <223> n equals a,t,g, or c 11 <400> 22 ggtgcaaaga acatagaata ttttgaaaaa cataagactg aaaatacatt ctgagctcac 60 ctttgcttga tagtttggct gaacataaaa atctagtttg gaaatctttt ttgcctagaa 120 attttatgac attttcccca ttgtcttcta ccttctggtg gtcttccaga tttcactgtg 180 aaatgctgtg gtttgtatct ttacttgtca cttttactgc acactcagtt gaatactctc 240 aatattaaag ctcatgccct ccagtttggg catattttga tgaatatttt gtgaaaattc 300 cttgcctttt ccaacttcta gaagctgcct ctacactttg attctttggg ctctttcttt 360 ttttctccac cttcaaagcc agcagcatag cacttccaaa tttctctctg cttctgccct 420 agtactaata ttaagtgagg tctccttgtt tcaaagaaaa tggatgtcaa taaagcactg 480 atgcatcagc aaatagtttt aaactccctg gakgwatatc tagtcttcca gaatacctct 540 cttctctact agagtntaga tntattcatt tactcatcay tcmatcattt aamaaacatt 600 ttctaagaaa ctgctttgcc tttgggactg ccctaggywc tggaatataa tagtgagcat 660 gacattgttt gaacttttaa agcagcttac agttaaatag gtgaaacaaa ccaatataca 720 aggacttgcc atatataaca aatacttttg tagagctaag tatagaatgt aaaagaaagg 780 aaatagctca gtcttggagg gggaaaggag atttctcagt gacctgggac acttgaagaa 840 taagtaggag tcatccaaac aaagaacagg caaagctatt gatatagcat gtacaaagac 900 ccagaagtga aagaaggtat agtattttca gagaaattac tcatgtaatc tgagacttag 960 acaagtagag acagagatga atctggagag gcaaagtaat gaaggacctt atgaattggg 1020 tgaccataga atatactatc caaacctata cacttttgaa aatgaaagag atacccgggt 1080 gcagtggctc atgcctgtaa tcccagcact ttgggaggcc aagcaagaca ggccgatcat 1140 ctgaggtcag gagtttgaga ccagcctgac caacatggtg aaaccccatc actactaaca 1200 ttacaaaatt agccaggcat ggtagctcac acctgtattc ccagctactc aggaggctga 1260 ggtagtagaa tcgcttgaac ccgggaagtg gaagttgtca gtgagccaag attgtgccat 1320 tgcactctag cctgggtggc agagcgaaac tctgtctcaa aaaaaaaaaa aaaaagggcg 1380 gcc 1383 <210> 23 <211> 1513 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (1502) <223> n equals a,t,g, or c <220> <221> SITE <222> (1512) <223> n equals a,t,g, or c <400> 23 gcagaatgtt taaaggcctt aggtatatgg agcgagctgc tgaaastatg gcaaggtggt 60 tgatctggcc ccactccatt tggatgcaag gatttcactt tctacccttc agcagcagct 120 gggccagcct gagaaagctc tggaagctct ggaaccaatg tatgatccag atactttagc 180 acaggatgca aatgctgcac agcrggaact gaagttattg cttcatcgtt ctactctgtt 240 gttttcacaa ggcaaaatgt atggttatgt ggatacctta cttactatgt tagccatgct 300 tttaaaggta gcaatgaatc gagcccaagt ttgtttgata tccagttcca agtctggaga 360 gaggcatctt tatcttatta aagtatcgag agacaaaata tcagacagca atgaccaaga 420 gtcagcaaat tgtgatgcaa aagcaatatt tgctgtgctc acaagcgtct tgacaaagga 480 tgactggtgg aatcttctgt tgaaggccat atactcctta tgtgacctat cccgatttca 540 agaggctgag ttgcttgtag attcctcatt ggaatattac tcattttatg atgacaggca 600 aaaacgcaaa gaactagaat actttggtct gtctgctgca attctggaca aaaatttcag 660 12 aaaggcatac aactatatca ggataatggt aatggaaaat gtcaataaac cccagctctg 720 gaacattttc aatcaagtta ccatgcactc ccaagatgta cgacatcatc gcttctgtct 780 ccgtttgatg ctgaaaaacc cagaaaatca tgccctatgt gtcttaaatg gacacaatgc 840 atttgtatct ggtagtttta agcatgcgct tggacagtat gtgcaagcct ttcgcactca 900 ccctgacgaa cctctctata gcttctgtat aggcctaacc tttattcata tggcatctca 960 gaagtatgtg ttacggagac atgctcttat tgtacagggc ttttcctttc ttaatcgata 1020 cctcagttta cgtgggccct gccaggaatc attctacaat ttgggccgtg gccttcatca 1080 gttggggctg attcatcttg caatccacta ttatcagaag gccctggagc tccctccact 1140 tgtggtagag ggtatagaac ttgaccagtt agacttacga agagatattg cctacaactt 1200 gtctctcatc tatcagagca gtgggaatac cggaatggct caaacgcttt tgtataccta 1260 ttgttctata taaagcaccg caactgagaa cagagcaatg gcagctgctg tgtgaggacc 1320 agtgtcttct gtctcagggc ttattatttg taactccaaa atagaaatga caatttcaga 1380 attacctaac aaacagtgta tttattttta atatgtgata atgatcttgt ggtatatatg 1440 caaaattatt cctacaaaaa aaaaaaaaaa aaactcgtag ggggggcccg gtacccaatc 1500 cnaatttttc cnc 1513 <210> 24 <211> 1044 <212> DNA <213> Homo sapiens <400> 24 ggattttcag agacaaaggt ccaagttagg agacgtaatt actcagtgct ttgaagggac 60 atccaaggtg ctcactctta gccatagccg ttggtttcct ggatgctgac tgtgaagatt 120 ctaaagtgct tcctagggtg ggcggtggtg gcaggaggcc ttggacggag tcaggccaga 180 cccagcctcc tgtttaatag gctgagccca agcgtccctc agatgcgaat ccaacagcct 240 tggtgagttg taagatttca tggaaacttt ccctgacttc tgtctccccc ttgctcccca 300 ttacctggga aaggcagctt tgtgggccat gtgtcccgga agggcctggg ctggctgtgg 360 cccagtgctc aggaccagcc atcttggccc tcacagcgcc ctgcccagtt ggtgtaatat 420 ttgtyttcaa gccattgttg gagcaggcag gcaaaggggg ctttctgagg atccaacgtg 480 tgccagccac tgggatacaa agacaggcct ggttcctagc tgtggggctg ggaagggtat 540 ctgacatcaa tggtggcacc tggcagagga cacacagaca acagcaggca gcatggactt 600 ttatgtttgt agcttgagct ggttttaatt ggaagctctg tgatttacat aatcacttac 660 aatctctgta aataaggaac tatttatgag gaattgtaaa tttcctctct cccccttctt 720 accctgtctg tgatcttgtc tgtgatgcag taatgatatt ccactctagg ttcccatgat 780 cagtggtgaa atatagtgat tttcacctgt gcttccattc tgaagttctg gaaagaagta 840 ctggatggac tgaagtccag gacaacgtyc caaagaaagg cagagtccag gtaggcttgg 900 aggaccaagc cctggatgag cactggaggg cagaggcctc agtgtccagc actgtgccct 960 gcacatggaa agcccctacg tttgtggaat gaatgaataa taaaaatgtt ttcataagtg 1020 aaaaaaaaaa aaaaaaaact cgag 1044 <210> 25 <211> 2575 <212> DNA <213> Homo sapiens <400> 25 ccacgcgtcc gcgggcaccg gccgacatgg cggcagcggt ggcggctgcg ctggcgcggc 60 ttttggcggc ctttctgctc ctcgcggccc aggtggcctg tgagtacggc atggtgcacg 120 tggtctccca ggccgggggc cccgaaggca aagactactg catcctctac aacccgcagt 180 gggcccatct tccgcacgac ctcagcaagg catctttcct gcagctgcgc aactggacgg 240 cctccctgct ctgctccgca gccgacctcc ccgcccgtgg cttcagcaac cagatcccgc 300 tggtggcgcg ggggaactgc accttctatg agaaagtgag gctggcccag ggcagcggag 360 13 cacgcgggct gctcatcgtc agcagggaga ggctggtccc cccggggggt aataagacgc 420 agtatgatga gattggcatt cccgtggccc tgctcagcta caaagacatg ctggacatct 480 tcacgcgttt cggccgcacg gtgagggcgg cgctgtatgc gcctaaggag ccggtgctgg 540 actacaacat ggtcatcatc ttcatcatgg ctgtgggcac cgtcgccatc ggcggctact 600 gggccgggag tcgggacgtg aagaaaaggt acatgaagca caagcgcgac gatgggcccg 660 agaagcagga ggacgaggcg gtggacgtga cgccggtgat gacctgcgtg tttgtggtga 720 tgtgctgctc catgctggtg ctgctctact acttctacga cctcctcgtg tgcgtggtca 780 tcgggatctt ctgcctggcc tccgccaccg gcctctacag ctgcctggcg ccctgtgtgc 840 ggcggctgcc cttcggcaag tgcaggatcc ccaacaacag cctgccctac ttccacaagc 900 gcccgcaggc ccgtatgctg ctcctggcgc tcttctgcgt ggccgtcagc gtggtgtggg 960 gcgtcttccg caacgaggac agtgggcctg ggtcctccag gatgccctgg gcatcgcctt 1020 ctgcctctac atgctgaaga ccatccgtct gcccaccttc aaggcctgca cgctgctgct 1080 gctggtgctg ttcctctacg acatcttctt cgtgttcatc acgcccttcc tgaccaagag 1140 tgggagcagc atcatggtgg aggtggccac tgggccctcg gactcagcca cccgtgagaa 1200 gctgcccatg gtcctgaagg tgcccaggct gaactcctca cctctggccc tgtgtgaccg 1260 gcccttctcc ctcctgggtt tcggagacat tttggtgcca gggctgctgg tggcctactg 1320 ccacaggttt gacatccagg tacagtcctc cagggtatac ttcgtggcct gcaccatcgc 1380 ctatggcgtt ggcctccttg tgacattcgt ggcactggcc ctgatgcagc gtggccagcc 1440 cgctctcctc tacctggtgc cctgcacgct ggtgacgagc tgcgctgtgg cgctctggcg 1500 ccgggagctg ggcgtgttct ggacgggcag cggctttgcg aaagtcctac ctccatctcc 1560 gtgggcccca gcaccagccg acggcccgca gcctcccaaa gactctgcca cgccactctc 1620 cccgcagccg cccagcgaag aaccagccac atccccctgg cctgctgagc agtccccaaa 1680 atcacgcacg tccgaggaga tgggggctgg agcccccatg cgggagcctg ggagcccagc 1740 tgaatccgag ggccgggacc aggcccagcc gtccccggta acccagcctg gcgcctcggc 1800 ctaggggagg ggtgagacgc tcgctgccgt gcccgccaca ccaagatgtt ggggctgcct 1860 ggcgcccatg gagacagaca gacagacgct tgtcccccgg gaccgaggcc tgtgccgtcc 1920 ccacccgccc caacatggtg cttatccttg ccgagacccc tgcagtcgtg cccgcgccca 1980 gcccagctgc cccggctgca cgcctgctgc tcccagctcg cccggctgcc acaagctttc 2040 tgcgggtcca tcctccccgc aggaggaggg gtccgtcctt cgcaggcctt gcccggcctc 2100 tctgcagacc ctcaagcgtc gtctgcatga gtgagcaggc gtgggtggac tttggccgcg 2160 gccacacttg gtgctcacca gctgcttcgg ccttcaggtg acctccctcc ccacggcatc 2220 ctgctctccg ggtggaagag cagctttttg tctcccagaa ggcatcgctt ttccctcttg 2280 agcagatcgg agcccctggg aggtttggaa gctgcctcca agcctaggac acggaccggt 2340 ggccggggcg gcctctggcc cctgacgctg gctgagacag gcccgtgggg cggggttttg 2400 gggcgtgaac aaggctggca gtaagtggac aagctgctcc cctggctaag gccctgccct 2460 gccctcagcc agaggtgcct ggccatgcct gcacactcct ccccatttta ataaatggtc 2520 gcaacttcaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaa 2575 <210> 26 <211> 718 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (21) <223> n equals a,t,g, or c <400> 26 aactagggat cccccgggct ncaggaattc gccactggrg ccaaagtgag agtccagcgg 60 tcttccagcg cttgggccac ggcggcggcc ctgggagcag aggtggagcg accccattac 120 gctaaagatg aaaggctggg gttggctggc cctgcttctg ggggccctgc tgggaaccgc 180 ctgggctcgg aggagccagg atctccactg tggagcatgc agggctctgg tggatgaact 240 agaatgggaa attgcccagg tggaccccaa gaagaccatt cagatgggat ctttccggat 300 14 caatccagat ggcagccagt cagtggtgga ggtaactgtt actgttcccc caaacaaagt 360 agctcactct ggctttggat gaaattcgac tgcttaaaaa ggaccttggt ttaatagaaa 420 tgaagaaaac agactcagaa aaaagatttg gctctgtctc atttggaaga agctgcaggc 480 ttattcccca tgcacttgct tcctggctgc aaaccttaat actttgtttc tgctgtagaa 540 tttgttagca aacagggagt cctgatcagc acccttctcc acatccacat gactggtttt 600 taatgtagca ctgtggtata catgcaaaca tccgttcaaa atctgagtcg gagctaaaaa 660 aaaaaaaaaa aaaactcrag ggggggcccg agtacccaat tsgccctaga agaggcga 718 <210> 27 <211> 654 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (613) <223> n equals a,t,g, or c <220> <221> SITE <222> (623) <223> n equals a,t,g, or c <400> 27 ggtcgaccca cgcgtccggt catggccatc cagagcctgc acccttgccc ctcagagctc — 60 tgctgcaggg cctgcgtgas yttttaccac tgggcgatgg tggctgtgac gggcggcgtg 120 ggcgtggccg ctgccctgtg tctctgtagc ctcctgctgt ggccgacccg cctgcgacgc 180 tcccgaggcg gagaacaccg aacacccagt gaaggtgagg ggatcagcac ggcgccgcca 240 ccgtgctgga acgagactca gccacaagga ggtgcgaagc tctgacccag gccacagtgc 300 ggatgcacct tgaggatgtc acgctcagtg agagacacca gacacagaag ggtacgctgt 360 gatcccactt ctatgaaatg tccaggacag accaatccac agaatcaggg agaggattcg 420 tgggtgccgg gactggggag ggggacctgg gggtgactag gtgacataat ggggacaggg 480 ctgccttctg ggtgatgaga atgttctgga atcagatggg atggctgcac ggcgtggtga 540 aggtactgaa cgccacctca ctgtaagacg gtagattttg tattttacca caataaacaa 600 aacaaaacaa aanmaaaaaa aanaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaa 654 <210> 28 <211> 1445 <212> DNA <213> Homo sapiens <400> 28 ggcacgaggg atttgaacaa gatcattaga attcaaaaaa caccagaaat gaaagatctt 60 tcctgaagct gtttaggaat attcatgata tacccttaac tgttctagag aacaaaatgc 120 gtctgtgctc cttcacaaaa gtccctatga atttgtttct caatgtgatc cttcttaagt 180 tctataactt tttgttttca ttaattttag gaaaatcctg ccttgcttcg ttgggcctat 240 gcaagaacaa taaatgtcta tcctaatttc agacccactc ctaaaaactc actcatggga 300 gctctgtgtg gatttgggcc cctcatcttc atttattata ttatcaaaac tgagagggta 360 agtattcaga ccagatgttt agtatttgag tgataggttc actttctagg gaccagctgc 420 agctccttct cttgaagatt gccaccagtg cccctcccac cttggggctg tcctctgcct 480 tcccttcctc tcttctttta tctttattcc tttccagcag gagttaaaac agaaagtttt 540 cagtcacctt tgtctatttt tgttagttca tttgtttttt aaaaagatga tgtttattgg 600 gttaagtatt agcagaatac ataaatcatt tagtacgttt cctgtttgcg tgaattctat 660 15 ttatgttggt cacattttgc aaattaatgt taaaacctat taatactcta cgggacagag 720 aagcacaagc tgcctgtgtg gggaatagct gccgtcagca gcctgggtat atgattggag 780 agaaagtcaa gctgatcttt ggcaccaaac cattccacat ctggtactaa accctgagct 840 gcagccccca ggcttgtgtt gccactggag cccactcgtc tagctttgtc tttaactggc 900 ccatctgcat tcccattaga gttcgtgtat tttgattatc tggtgaatga tctacttaac 960 agaaaggtag tccacatttt cccagaaagt gtttgcattt tgctttcaat atatggtttt 1020 atgggataat atatttctaa tgactaaaat gtgagtaaga tgtttttgaa taggagcatt 1080 ttcttactgt gtctttagtt cctcggatta ctgtttcttc gcacactccc tgggctttag 1140 acagtgggat tgcaattagg tttggagtgt ttcattctgt ttgtcagttg tacggtgggt 1200 tgtgccaaaa tgcagttttt cttacctttt ttatttattt atttttatct aatatagcca 1260 actggcagaa tatattgtct ttaatgtact ttttttctgt ctttacagga taggaaagaa 1320 aaacttatcc aggaaggaaa attggatcga acatttcacc tctcatatta agtctggcaa 1380 tgatgactat atgtattcct gcctaaataa atcatctatt aatcattaaa aaaaaaaaaa 1440 aaaaa 1445 <210> 29 <211> 2020 <212> DNA <213> Homo sapiens <400> 29 ccacgcgtcc ggggtgaggg caacagatgc tggacccagg gagctctctg ccacaggatg 60 atggtggccc ttcgaggagc ttctgcattg ctggttctgt tccttgcagc ttttctgccc 120 ccgccgcagt gtacccagga cccagccatg gtgcattaca tctaccagcg ctttcgagtc 180 ttggagcaag ggctggaaaa atgtacccaa gcaacgaggg catacattca agaattccaa 240 gagttctcaa aaaatatatc tgtcatgctg ggaagatgtc agacctacac aagtgagtac 300 aagagtgcag tgggtaactt ggcactgaga gttgaacgtg cccaacggga gattgactac 360 atacaatacc ttcgagaggc tgacgagtgc atcgaatcag aggacaagac actggcagaa 420 atgttgctcc aagaagctga agaagagaaa aagatccgga ctctgctgaa tgcaagctgt 480 gacaacatgc tgatgggcat aaagtctttg aaaatagtga agaagatgat ggacacacat 540 ggctcttgga tgaaagatgc tgtctataac tctccaaagg tgtacttatt aattggatcc 600 agaaacaaca ctgtttggga atttgcaaac atacgggcat tcatggagga taacaccaag 660 ccagctcccc ggaagcaaat cctaacactt tcctggcagg gaacaggcca agtgatctac 720 aaaggttttc tattttttca taaccaagca acttctaatg agataatcaa atataacctg 780 cagaagagga ctgtggaaga tcgaatgctg ctcccaggag gggtaggccg agcattggtt 840 taccagcact ccccctcaac ttacattgac ctggctgtgg atgagcatgg gctctgggcc 900 atccactctg ggccaggcac ccatagccat ttggttctca caaagattga gccgggcaca 960 ctgggagtgg agcattcatg ggatacccca tgcagaagcc aggatgctga agcctcattc 1020 ctcttgtgtg gggttctcta tgtggtctac agtactgggg gccagggccc tcatcgcatc 1080 acctgcatct atgatccact gggcactatc agtgaggagg acttgcccaa cttgttcttc 1140 cccaagagac caagaagtca ctccatgatc cattacaacc ccagagataa gcagctctat 1200 gcctggaatg aaggaaacca gatcatttac aaactacaga caaagagaaa gctgactctg 1260 aagtaatgca ttacagctgt gagaaagagc actgtggctt tggcagctgt tctacaggac 1320 agtgaggcta tagccccttc acaatatagt atccctctaa tcacacacag gaagagtgtg 1380 tagaagtgga aatacgtatg cctcctttcc caaatgtcac tgccttaggt atcttccaag 1440 agcttagatg agagcatatc atcaggaaag tttcaacaat gtccattact cccccaaacc 1500 tcctggctct caaggatgac cacattctga tacagcctac ttcaagcctt ttgttttact 1560 gctccccagc atttactgta actctgccat cttccctccc acaattagag ttgtatgcca 1620 gcccctaata ttcaccactg gcttttctct cccctggcct ttgctgaagc tcttccctct 1680 ttttcaaatg tctattgata ttctcccatt ttcactgccc aactaaaata ctattaatat 1740 ttctttcttt tctttccttt tttttgagac aaggtctcac tatgttgccc aggctggtct 1800 caaactccag agctcaagag atcctcctgc ctcagcctcc taagtacctg ggattacagg 1860 catgtgccac cacacctggc ttaaaatact atttcttatt gaggtttaac ctctatttcc 1920 cctagccctg tccttccact aagcttggta gatgtaataa taaagtgaaa atattaacat 1980 16 ttgaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa 2020 <210> 30 <211> 1083 <212> DNA <213> Homo sapiens <400> 30 aattcggcag agccctgaac cccgcacccc accctcgagg ccagaaatcg gttgcctctg 60 gggacctgag aagcgagacc actcggcgcc ctgacttgca aagttggggt ctttattggc 120 ctccgggatt ctgctcctgg cggtttctcc aggctggtga tgggcaagcc gggtgtacca 180 agtccaggat gcacatgagg agcgtttgta gcagtcactg aatcacctca tgactagcgg 240 ggcaggcctc taattcaccg caggatttcc ggtaggttgg attgtggggt tggtgtttgc 300 actccaaaga gktgctgtga tttccctgta tctgtctttc tggcttgtta gatcttctca 360 tttggcgtcc tttctccgaa gagttaacca agacgtttgg catggtttcc ttgctttcct 420 cctatctttt gctgctagag ctgctttcga aaagaagtct tttcttgcag tggtatcttt 480 tctttgggtt acagtgttgt tcatcctttc tttgccgaaa gaatgaatcc cagtgcttca 540 caaggttaaa ggaaagatct gctggtagtg tttagtcttt gttctgagct gatatgtgtt 600 agtagctttt tgtttttaaa ttttattagt aaaatttcac cagtgaacca gaagctcttt 660 ttttctgttg tgaaatgcta gctttaagat ttctgagaac tttgtgtcaa agaaatcttt 720 gaaaagttac tgaagtatac agagaggttc acaattttaa atgtgcaggt ggtccgggcg 780 cggtagatca cacctgtaat cccagcactt tgggacgcca aggtgggcgg atcacttgag 840 cccaggattt ccagaccagc ctgggcaacg tgccaaaacc ctatctctac taaaattaca 900 aaagttagct gtgtgtggtg gtgtgtgcct gtagtcccag ctacctggta ggctgaggtg 960 ggaggatcac cagagcccag gaggttgaga ttgcagtgag ccgtgatcat ggcagtgcac 1020 tcccgcctgg gtggcagagt gagaccctgt ctccaaaaaa aaaaaaaaaa aaaaaaactc 1080 gag 1083 <210> 31 <211> 1580 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (1513) <223> n equals a,t,g, or c <220> <221> SITE <222> (1542) <223> n equals a,t,g, or c <400> 31 gctggggaag atgctgcgtc cagcgttacc gtggctgtac cttggcctct gcagcctcct 60 ggtgggggag gcagaggccc cgagccccgt ggatccgctg gagcggagcc ggccgtacgc 120 ggtgctgcga gggcagaacc tggtgttgat gggaaccatt ttcagcatcc tgctggtgac 180 tgtcatcctt atggcatttt gtgtctacaa gcccattcgg cgtcggtgac agccagacaa 240 gttcttcaat gagtatttgg gaataggata agttgtgttg cacacaggcc agtggagaag 300 ttggaaccaa aactttccta cttggaaatg acctttggtc tggacagttg gtaaatgcta 360 aatgaattag aagaaaacat gtactagaca ttattttttc ctaacactgt agcgcaaata 420 attggcccct gagtccgctt ctcagtgttt ctgactgtac ttgttaaaag taagacctga 480 aagctccaaa ggtcagtgta aagatggagt gttcatgaga aagaaaacat ggtaaccttg 540 17 tgagtgcctg taagaaccac actgtaaaga actcatcatt aatgcttgaa aatgttatta 600 agaaggagac ttaccatgca gacattccct atttaagaac catttggtta cagtgggtta 660 agaatcacag attttttttt ttaatctcac ctgagttagc ctagaatgcg ctggttgcaa 720 agtggtgtca gctgtgggga tcttgggccc tcgttcctca cctgcatcct gccctgcact 780 caggtgctcc ccctgaagtc agggtcacat caggtagacc tgttactata tgcacctttg 840 gcctggaatg ctctgaagtt ggactggaaa tgttactagg ttggcctgtt acaaaaagga 900 ccccatcctg cttaaacaca ttgatctccc ttgccctgca tttgagtctt tctagcccac 960 ggtctgaaac ttgaggcagc tttccagatt tggaatgtaa aaggctcagt gggcactctg 1020 ttcatccctg ggtggggagg gcccagccaa cagaagtgca tgtccactgt gcgggccagt 1080 gtgtgtttac acaaatttca tctcagcttt gaaaatgctg ctattagttt ccactgttgg 1140 tgaactggat tttttcctcc tattgaaatg atactttcat acttataaag ctgtcgtcaa 1200 tatttatttc aaggtgctag atttaatttt gttattaaat tgaaatgctt atcttgtgtt 1260 caagcacagc actgatttta acaacctgca tttaatgtga agtaaccgaa gtaggatact 1320 gtaactgtgt aaggattttg tttgtaatct tgtaacattg aaccattgaa atgttcagtt 1380 ctttgctttt gagcaaaacg tcaattaaaa ctaaagtaaa atcctatata ttgttttact 1440 ccaccagtta tttcccaagt gtttgaaatg caggtgtgtg tctgaatttg gatctaatcc 1500 acttaaagga ggnctgtgga ggggaaattc cttttttgag gncgggtttt gggtcccctt 1560 gcccggggaa agggttcccg 1580 <210> 32 <211> 796 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (748) <223> n equals a,t,g, or c <400> 32 tcggcccgag aagaaatgtg acgcactctc accaagatgc tgaagctgac attcatcaat 60 aagcagctgt gcatccacta ggcatttggt aaatgttaac ttatctaccg aggtggtgtt 120 ttcttagcct cccacctcct tgctgtggag cagcttcatg taccatgatg catattcaga 180 tcattcttaa tactcatatt ttgatagaga ggtttttagg ttttctttta aaccaagttt 240 attgagataa actactttgg taggatatgg aacttaggaa taatggtatg aaactagaca 300 gctttttttt ttttattaca ctttaagttc tgggatatgt gttcagaaca tgcaggtttg 360 ttacataggt atacacgtgc catggtggtt tgctgcaccc atcaacctgt catctgtatt 420 cggtgtttct cctaattcta tcccwcccct acccccctgc ccccaaaaag gccccagtgt 480 gtgatggtcc cctccctgtg tccatgtgtt ctcattgttc aactcccact tatgagtgag 540 aacatgaggt gtttggtttt ttcttcctgt gttagtttgc tgagaatgat ggcttccagc 600 ttcatccatg tccctkcaaa ggacatgaac tcagtccttt tttatggctg catagtattt 660 cgtggtatat aagtgccaca ttttctttat ycagtctayc atttgggttg gttccaaatc 720 tttgctattg tgaatagtgc cgcaatanac atacgtgtgc atgtgtcttt aaaaaaaaaa 780 aaaaaaaaaa ctcgag 796 <210> 33 <211> 1256 <212> DNA <213> Homo sapiens <400> 33 ctatgttcca tcattccttc ccaaagccac cggaagcatt ccttctagga aaggtggagt 60 cggtagtgag aagccggagg tgcccctaca gacatacaag gagattgttc actgctgyga 120 ggagcaggtc ttaactctgg ccactgaaca gacctatgct gtggagggtg agacacccat 180 caaccgcctg tccctgctgc tctctggccg ggttcgtgtg agccaggatg ggcagtttct 240 gcactacatc tttccatacc agttcatgga ctctcctgag tgggaatcac tacagccttc 300 tgaggagggg gtgttccagg tcactctgac tgctgagacc tcatgtagct acatttcctg 360 gccccggaaa agtctccatc ttcttctgac caaagagcga tacatctcct gcctcttctc 420 ggctctgctg ggatatgaca tctcggagaa gctctacact ctcaatgaca agctctttgc 480 taagtttggg ctgcgctttg acatccgcct tcccagcctc taccatgtcc tgggtcccac 540 tgctgcagat gctggaccag agtccgagaa gggtgatgag gaagtctgtg agccagctgt 600 gtcccctcct caggccacac ccacctctct ccagcaaaca cccccttgtt ctacccctcc 660 agctaccacc aactttcctg cacctcctac ccgggccagg ttgtccaggc cagacagtgg 720 catactggct tctagaattc ctctccagag ctactctcaa gttatatcca ggggacaggc 780 ccctttggct ccaacccaca cgcctgaact ttaaggatca ttggactatc ttctctgtgg 840 ccagcgcagc tctcttctgt gttcacagaa tggccactga taggcaygcc tcttttccca 900 cccactggaa ggctcacagg caaggtgaga gaggacacag aaggtgccaa cactgtcgct 960 acagtaagga cctgaagtga ctttgagaaa ttcaccctca caaaccttcc ttcaggagca 1020 ggcattggta gtgcagaggc acagattccg tcctttacca gctgcagaat cttgggcaag 1080 ttacatagcc tctgtgagcc tcatcggtaa acagtggggg ttatgaaacc cacctcacag 1140 ggttgttgtg aggatccaat gagttgattt aggtaagcac ctagcacatg ccgtggcacc 1200 aagtaagcac tcaataaatc actcaactcc ttaaaaaaaa aaaaaaaaaa ctcgag 1256 <210> 34 <211> 1064 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (462) <223> n equals a,t,g, or c <220> <221> SITE <222> (1047) <223> n equals a,t,g, or c <220> <221> SITE <222> (1048) <223> n equals a,t,g, or c <220> <221> SITE <222> (1050) <223> n equals a,t,g, or c <400> 34 cttcagcctg ggcaacagag caagaacctg tctcagtcaa tcaataaatg tatgtatata 60 tatatatgta tatatgtcag accaccgtct gaaattgctg ttcatgattg gaaatcgaac 120 tggaaacccg aaggcaggag atgtgtgctc ccttgggatg tatggggaaa tcacacagag 180 ctgttagtac ttcagtcatg ggatttgctc tcatgctatg catatgggcc tcacaacttg 240 taaatgccac tggaagatgg cttatctaag gttccttatt ttgtggtctt tcccccttag 300 ttctgcagtg agtggggcaa agcgtgtcac tgaccttttg aatggaaaac actggaagcc 360 ttagcgttct taattcctga aatgttcatt tttwcttcta agcaactggg cttcasagga 420 gattagggca ggcaataaca gtgttgacac cagggcaact gntttcycct gttatgggat 480 19 tatwcaacat ctgctttctg ctaagctcca tggaaggcac agaggaaaca cagcagagtc 540 catgccttag agactttgta cctgatgaat tgagtggtat caggacaatg ctatttaatg 600 tttgatccat cccttctcta agcacatctc agatttctgt gctacctgat ttaacccttt 660 cagttcatag aacccagaag gataaggtga aaagatagac cgggaaaagt aatgcaagtg 720 gccaagagta gcttccactt caaagttcct catgtgtgtg tgctaacatt gtgacttctg 780 ttcagtcatt gtcagtataa actgtacatt ggaatcattt gtagcttttt aaaaaatgcc 840 tatgcctcac cctagaccta ccacatcaaa atctcaggat agagtctcaa gctaaaaagc 900 ctctatttga gccaggctta ttggcacctg cctgtagtcc cgtactcaga aggctgaagt 960 gagaggatcg cttgaactca ggagtttaac gccagcagag gcaatagggc aaaatagcga 1020 gatctcatct ctttaaaaaa aaaaaanntn aaaagggcgg ccgc 1064 <210> 35 <211> 755 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (1) <223> n equals a,t,g, or c <220> <221> SITE <222> (733) <223> n equals a,t,g, or c <220> <221> SITE <222> (734) <223> n equals a,t,g, or c <400> 35 natttcccgt tcagttattc cggtgacact atagaaggta cgcctgcagg taccggtccg 60 gaattcccgg gtcgacccac gcgtccgaac tcctgaaaca gtgaggacat ctcacagacc 120 agacaggagc tggggctctg catctcacag cggtgcctgt cagacaggaa gaagtcccgc 180 agaagtggcg tgtgggtcag ggcctgcacg atgcagttca tgaagcatgt gttcccaagg 240 ttgatcagcc cacgcagacc tatggtgcag ttcgaggtga tctttctcct tttcgggttg 300 tgcttcagca gttcaagctc ccgtttggtt ggttcccaag ttgaaaactt ctctccaacg 360 ccttgcattt tccaagcttt tcgctgctcc tccttggcga ttatttccat gtctttgtca 420 tagatgtagt cctggcacag aaaacagtag atgcctccgt acatcagatc aatggccagg 480 ttgtgccgct tcgccttcgc atgctcgtga atatgcttct ttgtgaaaca gccgaagaag 540 acacagtaga ggcaggaatg cagcctgttg aggtggacgc cacagacatg gcagatacag 600 gacttggcct tgcgcttgcg ggcctcagcc gtgccgctcc acacgaagca ctggtagatg 660 gcccgcaggt tctgcttcca gttgtccacc ttgaagctgc ccaggtgcga gcagcccggc 720 ggcgctaccg ccnnctcggc gtccatggcc tcgcc 755 <210> 36 <211> 604 <212> DNA <213> Homo sapiens <400> 36 ggcctcccaa agtgctggga ttacaggcgt gagcaagatt atatttcttt aataaagaat 60 20 acgtgacttt tatttaagtt gtcagattta ttggaaatgt tgttcgtaat atcttttgat 120 gtctgtggta cctgtaatga ttcctttttt actactactg ttttttttct ctctctcttc 180 cacccaccat ccccatttac tttatttttc catctttata ttttcaggct ctttattggt 240 cagaattctt agttgtagaa aagagagttc acaccaggta ctcttaagca gaaaatgttt 300 tattaagggg cacagacagc acagacagct tacaaaagtg taggggaccc aaacagaaac 360 cctttaattt tactgattag aatggggagc tcaacagagg caactattaa aatgtgcaga 420 aggtattcag aagattgtga gcaggcatat atgagagatt tcattacaag ctctctacag 480 taaccaacca taatgcagaa tagaaattca ttattttgga cttttgctac ctgtcaattt 540 aactgttacg tttttacgga cttgttaaaa aagtgattag atagactgtt ttagattttc 600 ctta 604 <210> 37 <211> 812 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (17) <223> n equals a,t,g, or c <220> <221> SITE <222> (108) <223> n equals a,t,g, or c <400> 37 gaccattttt agccaanctt ggaattaacc ctcacttaag ggaacaaaag ctggagcttc 60 caccgcgttg gcggccgctc tagaactagt ggatcccccg ggctgcanga attcggccac 120 gagaggactt ccccacctca tgcagctatt tgggccgtgg cgtctgaaat ttattatttc 180 agagtcaccc ctttratgac cttggcagtg ractgcagtc atctgtttag gcctttccat 240 ggcccacgtc aatgccgtta tttctgtttg ttgcacattt gatttccttg ttgttggcat 300 ttagaaggcc ccctgcttcc cagatcacac cacgggcatg gaccacagag attgcatctt 360 gtgagtctgt agaaatggtc aaggccttgt cctctcttag gtccagagct caggtgaatg 420 cagattttcc cggccatctg tgctgaagtc cctgtgggga ggctcctggc tggtttcctg 480 taggtagaca gctacacgtc ctgcccttca ttggcttctt ttcatgaagc tcctgccatc 540 tacaaaacat gtctcccttc ttgaatcaca tctctgttat tgaagctctg gaagtcaacc 600 gggcgtggtg gctatgccta taatcccagc attttgggat gccggggcgg gtggatcacc 660 tgaggtcagg agttcgggac cagcctggcc aacatggcga aaccccgtct ctaatacaag 720 tgcaaaaatt ggccaggcgt ggtggtcact gtgctccagc ctgggtgaca gagcgagctc 780 cgtctcaaaa aaaaaaaaaa aaaaaactcg ag 812 <210> 38 <211> 1149 <212> DNA <213> Homo sapiens <400> 38 gtaaaagtta aaaatgtttg ccttttatgt tcaggtttta aatcaatcta aaagtatttt 60 tgtatacagt aggaatctaa ttttttttat ccatatgata gtcagttggc cctcctttct 120 tcagttacct gcagtgcatc aatgtcatca gtcaagtgtc catatatgtg gtgtttctgg 180 gcttttcccc tcttccaatt atcagtgttt atccctgtgt caaaatcaca cagtattaat 240 tattacaact ttatagtaag tcttaatatt tagtagggca agtcttttta tttgataaga 300 21 gtatctttgc tattctttta cttttactct tctgcatata ttttagaatc agcctgtcaa 360 attcctcaaa agactgtttg gataaatttg gaattacatt caatatagat caatttggga 420 ataaccaaga gttttgggat attgagtctt cattcattaa catagctttt ctcttcattt 480 atttaggtct tattttttca tagagcttta aaaggtttac tataaaatct ttaaggggta 540 aactcttgaa taaggtccag agttaaatag tggagagtta caggtgtctg tttgccccaa 600 acagactgat ggtatttcag ccatctcagg atttggggaa gtcagcacaa ggatcaaaag 660 actgagaaag tttaacttct cctctaggat gtttttagta cacacattat atttataagg 720 aaacatattg taaataatag agtgataatg gccacttacc tgagccttat tataaacaga 780 aacaaatatc caaccaatgc catagagcag aagtacagcc tgaaaccaag aagaaaaaga 840 gcaattaaat caggatctca tctaggccaa gcttgaaaag gaagcttatt tcctatttgt 900 cttctgccta atgaatgtgt cattactggg gaccttacca ataaaggtgc ttggatacat 960 tttccagcac agaaacttaa tttgcaggaa catgatcttt acttgtaaaa ggatacattc 1020 ttaattcggg atggttattt gagctgattt tcaaggcatt tatttttaat ttatttgtca 1080 gatgggaata aaggtggttt ataattaaat ttaaaagata gtttaaaaaa aaaaaaaaaa 1140 aaactcgag 1149 <210> 39 <211> 1087 <212> DNA <213> Homo sapiens <400> 39 gcccactgga aatgatcttg tttatgtgtt tccttgttta ctgtctgtct tcagtagaat 60 ggaagagcca tcggtatttt gtcttttttt ccccttgtcc attcttatat cctcagcttc 120 tagaacattc cctggaacac agcaagtgtt cagtattgtt catggagtga cagatgtctc 180 agccaagaag gtacaatcac agggaagaat gacttcaact ggtcttgact tcaacctgct 240 tccagcctgg ttcccttctc ccacctccct acagcccaca gaagatcttt tccaaactgg 300 aagtctgtcc aggtcattct tctgctctaa ggctttcagt agctccccct tatccccagg 360 aggaagtcca aatgccttaa caagtgtcaa ggaacacttg gtgagccctg ctttccttgc 420 tagtcactcg tgcacagctg agtctttccc cagagtggat gtcattcatg ctgttcccat 480 tgcctggatt cctgctcctc tccaccccat tcaactgata aactcgtggt tttttttttt 540 tttttttttt ttttgagack gagtctcgat ctatcaccca cgctggagyg cagaggttgc 600 tgtgagctga ggtggtgcta gtgccctcca gcctggatga cagagtgaga ctcggtctca 660 ataaataaat aaataataaa gaagaaacca acccttttga ccccggggtc tcagactttt 720 agccaccaca tcagcgagtt atggtgtttg ttatagcagc tctgggaaac taatgcatgt 780 tttcagtgac attttagccc cttctgaatg gtctggatgg ctggttgaca gctaagttca 840 gacccgatgc aaaagcgcag tctatgtagg aatgtcccct gtggacagct gctgtgtagc 900 caaggtgggt tacatactag gaaagggccc tgggggcccc cacagggagc taactctatt 960 gacgggggac ccaggtaaca gatgcaggca tttgctgtga gtcacaagac actgatgtgt 1020 gtttgcttgc ctgggcaaca tagtgagacc ccgtctctat taaaaaaaaa aaaaaaaaaa 1080 actcgag 1087 <210> 40 <211> 1276 <212> DNA <213> Homo sapiens <400> 40 gtgagtgtgt ggcactggtg gcctggagcc aaatttagct tgggtgagag ttgacaatgg 60 tagttttcct tcctcaagcc cctctgtgcc cctagagcac cctggctgtg gctgcctcct 120 tcatccaaga gcagagtcca tgttgggcca ggagacttca gatccatgtc ctggtgctgc 180 ctctggcttt gtctttcctc agtgggcagg actgggtctg ctggtccatc tttacccttc 240 tctgagctat gcagccttgg cctgctgcgt ctccggcctg tattctctcc ccttcactca 300 22 ggccctggga aaccagccca gtttctkgca ggagaggcag aggaggtcaa tgcctttgct 360 ctgggcttcc tgagcaccag cagtggtgtc tctggagaag atgaagtaga gcccttacac 420 gatggagttg aagaggcaga gaaaaagatg gaagaagaag gtgtgagtgt gagtgaaatg 480 gaggcaacag gagcacaagg acccagcagg gtagaagagg ctgagggaca cacagaggtg 540 acagaagcag agggatccca ggggactgct gaggctgacg ggccaggagc atcttcaggg 600 gatgaggatg cctctggcag ggcagcaagt ccagagtcgg cctccagcac ccctgagtct 660 ctccaggcca ggcgacatca tcagtttctt gagccagccc cagcgcctgg tgctgcagtc 720 ttatcttcag agcctgcaga gcctctgttg gtcaggcatc cccctaggcc ccggaccacc 780 ggccccaggc cccggcaaga tccccacaag gctggactga gccactatgt gaaactcttt 840 agcttctatg ccaagatgcc catggagagg aaggctcttg agatggtgga gaagtgccta 900 gataaatatt tccagcatct ttgtgatgat ctggaggtat ttgctgctca tgctggccgc 960 aagactgtga agccagagga cctggagctg ctgatgcggc ggcagggcct ggtcactgac 1020 caagtctcac tgcacgtgct agtggagcgg cacctgcccc tggagtaccg gcagctgctc 1080 atcccctgtg catacagtgg caactctgtc ttccctgccc agtagtggcc aggcttcaac 1140 actttccctg tcccacctgg ggactcttgc ccccacatat ttctccaggt ctcctcccca 1200 cccccccagc atcaataaag tgtcataaac agaaaaaaaa aaaaaaaaaa aaaaaaaaaa 1260 attggggggg ggcccc 1276 <210> 41 <211> 2083 <212> DNA <213> Homo sapiens <400> 41 gccctttacc cccaacccca ggccactggg cccttcccac accacttggg gagctgagaa— 60 gaggaggctg gagtaaggga ggacttgatc atccaagaaa tactttttat tgctgggagt 120 cttctgaacc tcaccaaact gaggccagag ctgagctcct gggggagtta attcagaggg 180 gagaggccag cacctccctc ctccatygct cgctgtgtgc cttaaactcc atctcatgtc 240 cctccccatc ccctggcttt ccctccctcc ttgccccatc ctgggccagc cagcagggct 300 cctcctctgg ctcttcagac ctttcagcca gtgctgtcag tgcccctggg agggaagggc 360 atccctgagg cacccgaatg gtccctcagg gtgcagggag gcagaagcct ggccacagag 420 gagcctccta aggcagcagc tgcagcaagc gcaccctctc cccactctcc ccacgccaga 480 gcggcttcca gagcagatgc tgtttccatc ctcctcgtca aaaccattct cgctgctgag 540 cttgacaatc tgggcaaggc ttgtggggcg cttgacaaac agaatctgcc ctgtgccgcc 600 tggttccgtg gcctccagca tgagcctgca ggcagggcgc tgcgggaacc cagttgtgct 660 gccccagccc atgcctccgg gtctgctgtg catgaatgag tgctcacttg tcccgggttt 720 aggacgtggt caagtgaaca gcagggtcta actgtgctta cttagcccag ttcaaacaga 780 acaaaggaaa aatatagaaa gcaacatctg ttgatcattt aggttttttt ttaaaccacc 840 atgtcacttt gagtccttca tgggtttttg aacagcattt atcaagaaga aaatgtgggc 900 tttttcccct ctcccgtgtt ttgtttgtcc tgtagataga gggaggaaag ccgtgcagtg 960 gcaggcggga ccccctctgg tggcgggacc ccctcttgcg gtggtcttgc ggggccagcc 1020 gggacctgtc actttattat ttaaggagtg tgtgtgtaga gtcgctggct tattaacagt 1080 attgtgtgtg ggttgggttt ttagtttgtt ccttcttttt gaagtccctt catttcaatc 1140 cttgactctc tctccccttc ccttgcccag ctctgttgaa tgctgctgtg cgcgtgtgag 1200 ggccgctctg cacacagggc ccttgggttg tgtgaactga aattctccct gtatttgtga 1260 gactcgcagg agtccccatc tgtagcacag gcaatgccag tgccatgctg cagcctcaga 1320 aaccaggcct ctcactccag cagcaggcag aaccgtgtct gtggtcgggt gctgtccaca 1380 gctctgtctg ccttgttctt gggcttgagc tggatagagg tggggtctct tcaccttccc 1440 tgaattcaga acagaccctg tgcctggccc cagtgtgccc aggcaattcc ccaggccctc 1500 attgggagcc cttggtgttc tgagcagcag ggcccaggca gcacatgagc agtgcccagg 1560 ggctccctgc gtgaggacgg caaggtgcga tgtatgtcta acttattgat ggcaggcagc 1620 cccctgtgcc ccctaagcct ggccctggtt attgctgagc tctgtgctca gtgctgcggc 1680 ctggccgtgg ctcgtctgtt cctttggggg gcccgggcgg gttgtgggaa tcagtcttca 1740 cagacagacg tgagccaggc ggaggactcg ttccttgcag aggtcagtcc tcacctgcag 1800 23 gtgtcggggt ggrggggggc aaggaggggc aggcacacac catgtctgac ctgaacccga 1860 ttctggggag catcttcccg ctccggcccc acgacctcca cagggttaca ttgtaatata 1920 tatgccccag ctaacctgtc tgatggtggc atcttcctgc agacatttca aacatgtaac 1980 ttttatatga aaaaaaataa acacagatga aagctgccca aaaaaaaaaa aaaaaaaaaa 2040 aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa agg 2083 <210> 42 <211> 1016 <212> DNA <213> Homo sapiens <400> 42 taattcggca gagccagcct gggtgcctgt atgcgctcga ggcgggggcg cgggttgcgg 60 acggaggcgc gggaggcggt tctgcgcggc gggggccgta cccgcggcgg agcgaggagg 120 cgagaatgga tcaatggtgt cacggagcac atcgctgacg ctgattgtgt tccttttcca 180 cagattgtct aaagccccag gaaaaatggt ggaaaattca ccgtcgccat tgccagaaag 240 agcgatttat ggctttgttc ttttcttaag ctcccaattt ggcttcaaaa atctgaaggg 300 atctcgtgtt tgctgagtgt tccgtgtgcc agcactagcc taggaggttt tagtctctac 360 aaatatttat acagcaccag acgcgatggc aaagtggata aagcctggtc cctgccctta 420 aggaggtcgt ggtcttgtgg aggagacaga tggtacttta cctcgtgtgg gcctttattc 480 ctgaatcttg gctaaactct ttaggtttaa cctattggcc tcaaaaatat tgggcagttg 540 cattacctgt ctacctcctt attgctatag taattggcta cgtgctcttg tttgggatta 600 acatgatgag tacctctcca ctcgactcca tccatacaat cacagataac tatgcaaaaa 660 atcaacagca gaagaaatac caagaggagg ccattccagc cttaagagat atttctatta 720 gtgaagtaaa ccaaatgttc tttcttgcag ccaaagaact ttacaccaaa aactgaactg 780 tgtgtaacca tagtaacacc aagcacgtat ttatttataa gtttttgcca ttataatttt 840 gaccataaat taatttgacc atctctctta ttaatagaga agtaaaaaat gtaagttgac 900 cttctcttag attatgttca atgaatattg taaatgttca agtattgtta atgaatagaa 960 taaatacaat attgcattcc cataaaaaaa aaaaaaaaaa aaaaaaaaac tcgtag 1016 <210> 43 <211> 2197 <212> DNA <213> Homo sapiens <400> 43 ggtttgagaa actgtagtac ctagctttct ccaaggctgt ttgatgctgg gatcctcttg 60 tggggggcgt ctgtcaacgt caccatttgg gaagtgcgca ragctcarag cagcgcttcc 120 atgcttcctt ctgcttgggg gcccctccag gtagcttctt tcttcttgct atcttttyct 180 ttctgttttc tctcctcttc cccgcacctt gggaggcagg agacccactt kgtkgtgctk 240 gargatgatg agggcgcccc gtgcccagca gaggatgagc tggccctgca ggacaacggg 300 ttcctgagca agaatgaggt gctgcgcaca aggtgtctcg gctcacggag cggctccgca 360 agcgctaccc caccaacaac ttcgggaact gcacgggctg ctcggccacc ttctcagtgc 420 tgaagaagag gcggagctgc agtaattgtg gaaacagctt ctgctctcga tgctgctcct 480 tcaaggtgcc caagtcctcc atgggggcca cagccctgaa gcccagaggg agactgtgtt 540 tgtgtgtgcc tcgtgtaacc agaccttgag caagtgagaa gagaggccag ggtccaacca 600 ggcacccgtc cttggggcca gcagtagacc ccccactctc cccacccctg gcccactgtg 660 gtgtgtgctg ggcaaatgtg gcctgaatgc taggtaggct tccccttcct tcctcactct 720 ctccagctgg attctggagc tgttctccat ccatgagagt ggctggcaat ggctgctctc 780 aatcccttga gggagaagag cccctggagg gcctggcatg tttgccctgc tctgcctggg 840 actgagcgag tggacttagg gctgggcagg cagtagccac cagagggcag cagcgaacta 900 ggccaggcct gactggggtc tgaagatcag ggtcagtgtg gctatgcctg ggaattccag 960 acctgaggtt gggaaaagag gtttttctcc tgcagggtac tgggccaggc cctcagcctc 1020 24 agagagcctg cagaagggct tgggagtgcc acaccccatc tctgctgatt gaatgtccct 1080 ccaggcacca ggatctcatc atttccccat cagagggtgt ggccaggcct aacaagacca 1140 tgggtgcttc tagaaacagg gttgaagttc ccagattccc tgagaggaga atgtgtatag 1200 gagggtttgg ctgagtcctt cagcgttaag tggaggaaag cttggggaag ccccaatagc 1260 tggacagacc tcagcctccc ctcgaagaca cctcaattca cagactctca gcccacacaa 1320 tgccccagtg tccccagctc cgctggagca gctgcagggc acttggatca caacttctgc 1380 accctctgtc cagagtctag ggcagtcctc cactggccca gcactccagt ttcctttccc 1440 tgcctcttgt ccaatggagt gggaggccag gtgagtggag cagaggtcct gaagcccttg 1500 acccctgggg gcctgggtag tgtaggatct cgctgggctg ggtcctggat tccagggcta 1560 ttccctggag gacagtctca gttatgggat aaggccccct gggggtctcc atttctttcc 1620 aacagtttca tgttcactac tggactctta cgggctcagt atctctccct tagccatgag 1680 ctggctcagg catcccttcc cttccctgga gctgccctgc ctttctcaag tatttattta 1740 tttattgcat ggttcctggg aacatgtggc acaagtaatg ggatgaggag gaattggggg 1800 tgggggtctt ctacctagga ctcttccctg gagtcatggg ctgcctggga cccaggaccc 1860 atgagggggc tgagaggttt ctacactcga ggagcagggg tccagagagg caggctgggg 1920 aggcaaggga cccatcctag gcccgctttc ttgccgagcc aagcagctta gctggggctg 1980 tgcagccagg ggcttaccca ggccagtgga ggtgccacag ccctggggag ccagacaggc 2040 tttggtatcg tatcgcctct gtgtcctttt aagagaggag agttcagtac cccgtgcttt 2100 ctttacactg gagaggaact aaaaggatct ctgtgtctat ggagaattgt caataaaaag 2160 gcctcaagct tmaaaaaaaa aaaaaaaaaa ctcgtag 2197 <210> 44 <211> 1999 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (965) <223> n equals a,t,g, or c <220> <221> SITE <222> (973) <223> n equals a,t,g, or c <220> <221> SITE <222> (1110) <223> n equals a,t,g, or c <400> 44 ggcacgagcc caaccacaca cctggggaat tgctggcctg acttctgacc cctgactcct 60 catacccttc ctccagagca tgacatttga ccaccaactg aaacctgacc tctgacccca 120 gaccactggc ccttcccccg ccctgtggtg acttcataaa ggttactagc ttctcccctg 180 gccttgagac ccacacgatg gccctgctgg ctctggccag tgccgtcccg tctgccctgc 240 tggccctggc tgtcttcagg gtgcccgcct gggcctgtct cctctgcttc acaacctact 300 ctgagcgcct ccgcatctgc cagatgtttg ttgggatgcg gagcccaagc ttgaagagtg 360 tgaggaggcc ttcacggccg ccttccaggg cctctctgac accgaaatca gtgaggagac 420 catccacact tcatcagtgt cctggggaag gtgcagaggg agggcaggag aggcccagag 480 ggtcaggctg agggacagac agagagaaac agtcagagga gaaaggctca aagaccatga 540 gaacaacaga gacttaggga cagagagaca cagacagggg asgacagcag ggcaaagact 600 cagagagggg aggatggaga gtcagagagg ggaagatgga gactcagaga gggggaggat 660 ggagactcag agagagagga agatggagac tcggaaagat ggagactcag gagtatggag 720 25 agtcagagag gggaggatgg acactcggga ggatggagag tcaggaggat ggagactcat 780 agaaagggga ggatggagag tcaggagagg ttggagactg gagagggaat agagacccag 840 agaggggagg atggagactc agagggtgga agatggagac tcaaagagga tggaaaccca 900 ggagagagga ggacagagat gaggcagaga ctaggggaag caggatagcg actggtcggg 960 ggcanagact canggaggat agagacttgg gagggactca ggaagcatag cgactgtggg 1020 gcaaagagtc agagagggga ggatacagac ttgggagggc agagactcag aaacagaatg 1080 ttcgcattag ggacatggtg ttgcggggan ctgcctcccc cagcccctgc tccctccctc 1140 accgccagac tatgatgaga gaagccacct gcatgacacc ttcacccaga tgacccatgc 1200 cctgcaggag ctggctgctg cccagggatc ctttgaggtt gccttccctg atgctgcgga 1260 gaaaatgaag aaggtcttta cacagcttaa agaagcccag gcttgcatcc ctccctgcga 1320 aggtctccag gagttcgccc ggcgtttcct ctgcagcggg tgctactcta gggtctgcga 1380 cctcccgctg gactgcccag ttcaggatgt gacagtgact cggggcgacc aggctatgtt 1440 ttcttgcatc gtaaacttcc agctgccaaa ggaggagatc acctattcct ggaagttcgc 1500 aggaggaggt ctccggactc aggacttgtc ctatttccga gatatgccgc gggccgaagg 1560 atacctggcg cggatccggc cggctcagct cacgcaccgc gggacgttct cctgcgtgat 1620 caagcaagac cagcgccccc tggcccggct ctacttcttt cttaacgtga cgggccgccc 1680 ccgcgggcgg agacagagtt gcaggcctcg ttccgggaag tgctgcgctg ggcgccgcgg 1740 gatgccgagc tgatcgagcc ctggaggccc agcctgggcg agctgctggc caggcccgag 1800 gctctgacgc ccagcaatct gttcctgctt gcagtcctcg gggccctcgc atcagcgagt 1860 gcgacagtgt tggcgtggat gttctttcga tggtactgca gtggcaacta acaaaggtat 1920 ctttcctcct tccctatcct atttccatcc tgaaaataaa gaatatattt caactctaaa 1980 aaaaaaaaaa aaaaaaaaa 1999 <210> 45 <211> 1519 <212> DNA <213> Homo sapiens <400> 45 cggcacgagg taaattctgc cttcacccag tatatctttc caatgtagga tgatttattt 60 ttcattacat ttgttctaag attttgtagt gattactcta gtgtttgtca tgtaaatgtt 120 agtttatcaa aatcaggctc agttctccag taatatgtgg ttaaatttca gtgatgtaca 180 cacatatttg tcctctatag ctctattatg tttttgcctt tctggggtac tttgttgcat 240 atgtaacaac tcagtgttcc acattcaaca atatattctt ataattatta cttttccact 300 ggtagtcatt tagttcagtt tttatggtgt tatttataaa tataatacat gtatgttaaa 360 tttttctatg ttgtaggcct aacaatccat tactacttat tactttacac aattgacttg 420 taaatccata acaaggagaa aggtgaagaa acacatattc agtttgtctt ttccacttat 480 atagtcttgc atggtgctct ctgctttttc ctgtggattt tgacagactc aataattttt 540 tttttttttg agatggagtc ttcctctgtt gtcccaggct ggagtgcggt ggctctatct 600 tggccactgc agcctccacc tgccgggttc aaatgattgt cctgcctcag ccccccaagt 660 agctgggact acaggcgtgt gccaccacac ccggctaatt tttgtatttt tttttttttt 720 tgtagagaca gggttttgcc atgtttgcca gggtgctctc aaactcctga cctctagtga 780 tccaccagcc tcggcctccc aaagtgctga gattacagac gcgagccacc gcacctggca 840 ctttggtctt gtagggctgg tgtgccagga aaaattctct caatgttcat atttttaagc 900 ctaggaaaat atttgttttg tctttcattt tgaacatgaa cattgttgga ttctggttaa 960 ggtgtgtttt ggagcagagc atgatgaggg actgggtgag gggcttccca gtgaaaggag 1020 gaacagaacc tagcaaaagc aaatatgtct gtttcactcc aatcacttat tacaataacc 1080 tctattactt aatatcaaaa aaaaagcaat gatcaatatg ttgaaaggga tggaagaagc 1140 aagtatgatg tttgaccata atagcattca ttgcttggga aactaaagac aaaacaactg 1200 gaaaactatt aacactgttg gccaggtgtg gtggctcatg cctgtcatcc cagcactttg 1260 ggaggctggg gtggatggat cgcttgagcc caggagttcg agaccagcct gggcaacatg 1320 gcgaaacctc atctctacaa aaaatacaaa aaattacccg ggtctggtgg tgtgttcctg 1380 tggtcccagc tactcgggag gctgagatgg aaggattgct tgagcctggg aagtcgatgc 1440 tgcagtgagc caggattgca ccactgcact ctagcctgag tgacagagtg agaccctgtc 1500 26 taaaaaaaaa aaaaaaaaa 1519 <210> 46 <211> 1189 <212> DNA <213> Homo sapiens <400> 46 ggcacgagat ttaatacaaa gtttgctttg agacttttca gcatatgatc ttttttccat 60 aaacttgtac agtgcaaaag acattttgaa taccatgatc gatgatgtcc catgcttcga 120 ggaaaaccaa acactttccg cctctcttgc aaaatccatt cctcatgctg accctcctca 180 cgatggctgt gtcagcccag ccccttccct tctccaggcc cagataactc ttccacaaac 240 aagatgagag ccactcggga aaagagccat agtcaactgg gagggcctac atctggatgg 300 cggtggaaaa acttgagggt ttggggttca aagtcagccc atcccacctg gcaaaatcct 360 cctggaagga ggaccttcaa gagcgcatca cctgaatgtc atgaagaagt atctctgaat 420 gtatccagga gaggaactgc ataaccaaag gggtgaccag ccctcagatg tgcttattgg 480 attccagtac aaacgccacc aaagccagcc cactgctctc ctacaaggaa ggaaagatct 540 gcacgtgtaa aacatggggc agccttggaa catggtgttt tttggagttt cctttctcac 600 agttttccat ctccccactt ctttgatcag tcatgtgtcc gtgacctcgt tccatgacat 660 caggatagct gtgtttgcac accatgctgc atgttcattt ggagccagga ggggttctca 720 gtggagcctg gcttagggaa cagggagcga tggaagaatg ccaacattag cgttggtctt 780 ctcttgtcag gaatgaagga tgcttgcaca catgcacccc ctcactctca cacttgcaca 840 catacacaca cacacacacg aaatggttgg tttgtcaaaa ctcactgtag tacataaagc 900 ttgcactctg cgtcctatat ctagcagcat ggggtacgtt tggcagttca ctccattagg 960 gggtaaataa tttatgacca ttcatctgtt tttatgaatt tttttatcta gacaataatt 1020 gtaaataaag aactcaccat ctctgttcat ttaatactat gcaatggtta tgctttcaat 1080 cgctggctct tctgactcgt gcagtgtggt tctgaaatgt ttgtggttta aaaaaaaaag 1140 caaaaaacac tcaacagaac atagtaaata taaaaaaaaa aaaaaaaaa 1189 <210> 47 <211> 2584 <212> DNA <213> Homo sapiens <220> <221> SITE <222> (1389) <223> n equals a,t,g, or c <400> 47 acccacgcgt ccgcgggcac cggccgacat ggcggcagcg gtggcggctg cgctggcgcg 60 gcttttggcg gcctttctgc tcctcgcggc ccaggtggcc tgtgagtacg gcatggtgca 120 cgtggtctcc caggccgggg gccccgaagg caaagactac tgcatcctct acaacccgca 180 gtgggcccat cttccgcacg acctcagcaa ggcatctttc ctgcagctgc gcaactggac 240 ggcctccctg ctctgctccg cagccgacct ccccgcccgt ggcttcagca accagatccc 300 gctggtggcg cgggggaact gcaccttcta tgagaaagtg aggctggccc agggcagcgg 360 acacgcgggc tgctcatcgt cagcagggag argctggtcc ccccgggggg taataagacg 420 catatgatga gattggcatt cccgtggccc tgctcagcta caaagacatg ctggacatct 480 tcacgcgttt cggccgcacg gtgagggcgg cgctgtatgc gcctaaggag ccggtgctgg 540 actacaacat ggtcatcatc ttcatcatgg ctgtgggsac cgtcgccatc ggcggctact 600 gggccgggak tcgggacgtg aagaaaaggt acatgaagca caagcgcgac gatgggcccg 660 agaagcagga ggacgaggcg gtggacgtga cgccggtgat gacctgcgtg tttgtggtga 720 tgtgctgctc catgctggtg ctgctctact ayttctacga cctcctcgtg trcgtggtca 780 27 tcgggatctt ctgcctggcc tccgccaccg gcctctacag ctgcctggcg ccctgtgtgc 840 ggcggctgcc cttcggcaag tgcaggatcc ccaacaacag cctgccctac ttccacaagc 900 gcccgcaggc ccgtatgctg ctcctggcgc tcttctgcgt ggscgtcagc gtggtgtggg 960 gcgtcttccg caacgargac cagtgggcct gggtcctcca ggatgccctg ggcatcgcct 1020 tctgcctcta catgctgaag accatccgtc tgcccacctt caaggcctgc acgctgctgc 1080 tgctggtgct gttcctctac gacatcttct tcgtgttcat cacgcccttc ctgaccaaga 1140 gtgggagcag catcatggtg gaggtggcca ctgggccctc ggactcagcc acccgtgaga 1200 agctgcccat ggtcctgaag gtgcccaggc tgaactcctc acctctggcc ctgtgtgacc 1260 ggcccttctc cctcctgggt ttcggagaca ttttggtgcc agggctgctg gtggcctact 1320 gccacaggtt tgacatccag gtacagtcct ccagggtata cttcgtggcc tgcaccatcg 1380 cctatggynt tggcctcctt gtgacattcg tggcactggc cctgatgcag cgtggccagc 1440 ccgctctcct ctacctggtg ccctgcacgc tggtgacgag ctgcgctgtg gcgctctggc 1500 gcygkgagct gggcgtgttc tggacgggca gcggctttgc gaaagtccta cctccatctc 1560 cgtgggcccc agcaccagcc gacggcccgc agcctcccaa agactctgcc acgccactct 1620 ccccgcagcc gcccagcgaa gaaccagcca catccccctg gcctgctgag cagtccccaa 1680 aatcacgcac gtccgaggag atgggggctg gagccatgct gggascctgg gagcccagct 1740 gaatccgagg gccgggacca ggccagccgt ccccggtaac ccagcctggc gcctcggcct 1800 ag gagggg tgagacgctc gctgccgtgc ccgccacacc aagatgttgg ggctgcctgg 1860 cgcccactgg agacagacag acagacgcyt gtcccccggg accgaggcct gtgccgtccc 1920 cacccgcccc aacatggtgc ttatccttgc cgagacccct gcagtccgtg cccgcgccca 1980 gcccagctgc cccggctgca cgcctgctgc tcccagctcg cccggctgcc acaagctctc 2040 tgcgggtcca tcctccccgc aggaggaggg gtccgtcctc gcaggccytg cccggcctct 2100 ctgcagaccc tcaagcgtcg tctgcatgag tgagcaggcg tgggtggact ctggccgcgg 2160 ccacacttgg tgctcaccag ctgcttcggc cttcaggtga cctccctccc cacggcatcc 2220 tgctctccgg gtggaagagc agctttctgt ctcccagaag gcatcgcttt tccctcttga 2280 gcagatcgga gcccctggga ggtttggaag ctgcctccaa gcctaggaca cggaccggtg 2340 gccggggcgg cctctggccc ctgacgctgg ctgagacagg cccgtggggc ggggttttgg 2400 ggcgtgaaca aggctggcag taagtggaca agctgctccc ctggctaagg ccctgccctg 2460 ccctcagcca gaggtgcctg gccatgcctg cacactcctc cccattttaa taaatggtcg 2520 caacttcaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaagggcgg 2580 ccgc 2584 <210> 48 <211> 56 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (56) <223> Xaa equals stop translation <400> 48 Met lie ys His Ala Leu lie Arg Pro Phe lie Val Phe Ser Leu Leu 1 5 10 15 Leu Arg Leu Cys Ser Glu Asn Leu Phe Cys Pro Asn Thr Gin Phe lie 20 25 30 Val Leu Ser Cys Phe Gin Ser Val Val Lys Ser Leu Leu Ser lie Leu 35 40 45 Asn Leu Ser Tyr Cys lie Phe Xaa 50 55 28 <210> 49 <211> 41 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (41) <223> Xaa equals stop translation <400> 49 Met Asn Ser Cys Leu Phe Leu Cys lie Leu lie Leu Glu Ser Ala Met 1 5 10 15 Val Val Leu Met Lys Val His Phe lie Val Ala Phe Glu Leu Thr Ala 20 25 30 Lys Ala lie Asn Gin Lys Gin Lys Xaa 35 40 <210> 50 <211> 94 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (94) <223> Xaa equals stop translation <400> 50 Met Ala Arg Lys Ser Phe Ala Leu Leu Met Phe Val Trp Gin Met Ser 1 5 10 15 Leu Ser Leu Pro lie Lys Gly Phe lie Leu Arg Val Ala Asn Trp Leu 20 25 30 Phe Lys Pro His Leu Asn Ser Val Cys Leu Gly Trp Gin Asn His Thr 35 40 45 Arg Phe Cys Trp Ala Asn Leu Pro Gly Gly Val Leu Leu Glu Glu Ser 50 55 60 Ala Thr Ala Glu Asp Thr Leu Ser Trp Pro Leu Ala Leu Gin Thr lie 65 70 75 80 Val Glu Glu Gly Val Trp Gly His Gin Pro Leu Pro Gly Xaa 85 90 <210> 51 <211> 84 29 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (84) <223> Xaa equals stop translation <400> 51 Met Leu Ser Leu Phe Phe Cys Phe Trp Lys Pro Ser Phe Leu Val Ser 1 5 10 15 Arg Leu Val lie Trp Leu Gly Leu Val Cys Gly Gly Arg Ser Leu Ser 20 25 30 Trp Val Ala Leu Gly Glu Asp Tyr Leu Gly Thr Pro lie Leu lie Pro 35 40 45 Asn lie His Gin Thr Cys Pro His Pro Pro Leu Trp Glu Leu Val Pro 50 55 60 Glu His Pro Cys Arg Leu Val Leu lie Phe Ser Leu Cys Glu His Thr 65 70 75 80 His lie Arg Xaa <210> 52 <211> 66 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (66) <223> Xaa equals stop translation <400> 52 Met Leu Ser Pro Lys Ser Pro Arg Met Leu Leu Pro Cys Leu Leu Gin 1 5 10 15 Pro Leu Val Val Ala Asn lie Pro Arg Val Pro Trp Leu Ala Asp Glu 20 25 30 Ser Leu Asn Pro Thr Pro lie lie Thr Trp Gin Ser Pro Cys Val Ala 35 40 45 Gin Leu Cys Pro Asn Phe Pro Phe Pro Thr Arg Thr Leu Val Thr Gly 50 55 60 Leu Xaa 65 30 <210> 53 <211> 53 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (53) <223> Xaa equals stop translation <400> 53 Met His Cys His Ser Ala Leu Gly Pro Met Ser Thr Pro Val Leu Pro 1 5 10 15 Phe Ser Gly lie Gly Leu Ala Phe Leu Cys Leu Cys Leu Ala Ala Ser 20 25 30 Met Val Asp Leu Lys Cys Leu Gly Met Asn Ser Thr Leu Leu Gin Pro 35 40 45 Ser lie Lys Glu Xaa 50 <210> 54 <211> 541 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (10) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (469) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (541) <223> Xaa equals stop translation <400> 54 Met Ala Thr Ser Gly Ala Ala Ser Ala Xaa Leu Val lie Gly Trp Cys 1 5 10 15 lie Phe Gly Leu Leu Leu Leu Ala lie Leu Ala Phe Cys Trp lie Tyr 20 25 30 Val Arg Lys Tyr Gin Ser Arg Arg Glu Ser Glu Val Val Ser Thr lie 35 40 45 Thr Ala lie Phe Ser Leu Ala lie Ala Leu lie Thr Ser Ala Leu Leu 31 50 55 60 Pro Val Asp lie Phe Leu Val Ser Tyr Met Lys Asn Gin Asn Gly Thr 65 70 75 80 Phe Lys Asp Trp Ala Asn Ala Asn Val Ser Arg Gin lie Glu Asp Thr 85 90 95 Val Leu Tyr Gly Tyr Tyr Thr Leu Tyr Ser Val lie Leu Phe Cys Val 100 105 110 Phe Phe Trp lie Pro Phe Val Tyr Phe Tyr Tyr Glu Glu Lys Asp Asp 115 120 125 Asp Asp Thr Ser Lys Cys Thr Gin lie Lys Thr Ala Leu Lys Tyr Thr 130 135 140 Leu Gly Phe Val Val lie Cys Ala Leu Leu Leu Leu Val Gly Ala Phe 145 150 155 160 Val Pro Leu Asn Val Pro Asn Asn Lys Asn Ser Thr Glu Trp Glu Lys 165 170 175 Val Lys Ser Leu Phe Glu Glu Leu Gly Ser Ser His Gly Leu Ala Ala 180 185 190 Leu Ser Phe Ser lie Ser Ser Leu Thr Leu lie Gly Met Leu Ala Ala 195 200 205 lie Thr Tyr Thr Ala Tyr Gly Met Ser Ala Leu Pro Leu Asn Leu lie 210 215 220 Lys Gly Thr Arg Ser Ala Ala Tyr Glu Arg Leu Glu Asn Thr Glu Asp 225 230 235 240 lie Glu Glu Val Glu Gin His lie Gin Thr lie Lys Ser Lys Ser Lys 245 250 255 Asp Gly Arg Pro Leu Pro Ala Arg Asp Lys Arg Ala Leu Lys Gin Phe 260 265 270 Glu Glu Arg Leu Arg Thr Leu Lys Lys Arg Glu Arg His Leu Glu Phe 275 280 285 lie Glu Asn Ser Trp Trp Thr Lys Phe Cys Gly Ala Leu Arg Pro Leu 290 295 300 Lys lie Val Trp Gly lie Phe Phe lie Leu Val Ala Leu Leu Phe Val 305 310 315 320 lie Ser Leu Phe Leu Ser Asn Leu Asp Lys Ala Leu His Ser Ala Gly 325 330 335 lie Asp Ser Gly Phe lie lie Phe Gly Ala Asn Leu Ser Asn Pro Leu 340 345 350 32 Asn Met Leu Leu Pro Leu Leu Gin Thr Val Phe Pro Leu Asp Tyr lie 355 360 365 Leu lie Thr lie lie lie Met Tyr Phe lie Phe Thr Ser Met Ala Gly 370 375 380 lie Arg Asn lie Gly lie Trp Phe Phe Trp lie Arg Leu Tyr Lys lie 385 390 395 400 Arg Arg Gly Arg Thr Arg Pro Gin Ala Leu Leu Phe Leu Cys Met lie 405 410 415 Leu Leu Leu lie Val Leu His Thr Ser Tyr Met lie Tyr Ser Leu Ala 420 425 430 Pro Gin Tyr Val Met Tyr Gly Ser Gin Asn Tyr Leu lie Glu Thr Asn 435 440 445 lie Thr Ser Asp Asn His Lys Gly Asn Ser Thr Leu Ser Val Pro Lys 450 455 460 Arg Cys Asp Ala Xaa Ala Pro Glu Asp Gin Cys Thr Val Thr Arg Thr 465 470 475 480 Tyr Leu Phe Leu His Lys Phe Trp Phe Phe Ser Ala Ala Tyr Tyr Phe 485 490 495 Gly Asn Trp Ala Phe Leu Gly Val Phe Leu lie Gly Leu lie Val Ser 500 505 510 Cys Cys Lys Gly Lys Lys Ser Val lie Glu Gly Val Asp Glu Asp Ser 515 520 525 Asp lie Ser Asp Asp Glu Pro Ser Val Tyr Ser Ala Xaa 530 535 540 <210> 55 <211> 178 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (67) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (178) <223> Xaa equals stop translation <400> 55 Met Phe Gin Val Arg Pro Gly Trp Gin Leu Leu Leu Val Met Phe Ser 33 1 5 10 15 Ser Cys Ala Val Ser Asn Gin Leu Leu Val Trp Tyr Pro Ala Thr Ala 20 25 30 Leu Ala Asp Asn Lys Pro Val Ala Pro Asp Arg Arg lie Ser Gly His 35 40 45 Val Gly lie lie Phe Ser Met Ser Tyr Leu Glu Ser Lys Gly Leu Leu 50 55 60 Ala Thr Xaa Ser Glu Asp Arg Ser Val Arg lie Trp Lys Val Gly Asp 65 70 75 80 Leu Arg Val Pro Gly Gly Arg Val Gin Asn lie Gly His Cys Phe Gly 85 90 95 His Ser Ala Arg Val Trp Gin Val Lys Leu Leu Glu Asn Tyr Leu lie 100 105 110 Ser Ala Gly Glu Asp Cys Val Cys Leu Val Trp Ser His Glu Gly Glu 115 120 125 lie Leu Gin Ala Phe Arg Gly His Gin Asp Val Tyr Pro Val Val Val 130 135 140 Gly Ala Glu lie His Ala Glu Leu Tyr Gin Glu Leu Ala Tyr Leu Glu 145 150 155 160 Thr Glu Thr Glu Ser Leu Ala His Leu Phe Ala Leu Val Pro Arg Pro 165 170 175 Glu Xaa <210> 56 <211> 84 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (36) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (84) <223> Xaa equals stop translation <400> 56 Met Ser Leu lie Trp Glu Gin Gly Leu Gin Leu Cys Gly Phe Cys Leu 1 5 10 15 34 Phe Tyr Leu Val Phe Cys Phe Cys lie Ser Ser Leu Arg Val Met Ala 20 25 30 Phe Ser Cys Xaa His Val Ala Cys Cys Lys Gly Tyr Asp Phe Val Leu 35 40 45 Phe Tyr Gly Cys Val Val Phe His Gly Val Tyr Gly Pro His Phe Leu 50 55 60 Tyr Pro lie His His lie Trp Ala Pro Arg Leu lie Pro Cys Leu Cys 65 70 75 80 Tyr Cys Glu Xaa <210> 57 <211> 132 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (132) <223> Xaa equals stop translation <400> 57 Met Leu Trp Thr Leu Thr Phe Phe Leu Leu Gin Arg Ser Leu Thr Ser 1 5 10 15 Pro Trp Leu Phe Gly Leu Leu Phe Leu Gly Ser Ser Asn Thr Ala Val 20 25 30 Cys Cys Phe Leu Gly Gin Leu lie Met Gly Pro Lys Gly Glu Arg Gly 35 40 45 Phe Pro Gly Pro Pro Gly Arg Cys Leu Cys Gly Pro Thr Met Asn Val 50 55 60 Asn Asn Pro Ser Tyr Gly Glu Ser Val Tyr Gly Pro Ser Ser Pro Arg 65 70 75 80 Val Pro Val Val Arg Leu Ser Gly Arg Ser Leu Gly Trp Leu Ser Val 85 90 95 Arg Thr Ser His Leu lie Leu Met Gly Leu Cys Lys lie Leu Ser Val 100 105 110 Lys Leu Thr Phe Phe His Asp Ser Glu Tyr Thr Leu lie lie Gly Asn 115 120 125 Trp Lys lie Xaa 130 35 <210> 58 <211> 187 <212> PRT <213> Homo sapiens <220> <221> SITE <222> ( 167 ) <223> Xaa equals any of the naturally occurring L-amino acids <400> 58 Met Gly Phe Phe Leu Val Leu Val Met Glu Gin lie Thr Leu Ala Tyr 1 5 10 15 Lys Glu Gin Ser Gly Pro Ser Pro Leu Glu Glu Thr Arg Ala Leu Leu 20 25 30 Gly Thr Val Asn Gly Gly Pro Gin His Trp His Asp Gly Pro Gly Val 35 40 45 Pro Gin Ala Ser Gly Ala Pro Ala Thr Pro Ser Ala Leu Arg Ala Cys 50 55 60 Val Leu Val Phe Ser Leu Ala Leu His Ser Val Phe Glu Gly Leu Ala 65 70 75 80 Val Gly Leu Gin Arg Asp Arg Ala Arg Ala Met Glu Leu Cys Leu Ala 85 90 95 Leu Leu Leu His Lys Gly lie Leu Ala Val Ser Leu Ser Leu Arg Leu 100 105 110 Leu Gin Ser His Leu Arg Ala Gin Val Val Ala Gly Cys Gly lie Leu 115 120 125 Phe Ser Cys Met Thr Pro Leu Gly lie Gly Leu Gly Ala Ala Leu Ala 130 135 140 Glu Ser Ala Gly Pro Leu His Gin Leu Ala Gin Ser Val Leu Glu Gly 145 150 155 160 Met Ala Ala Gly Thr Phe Xaa Tyr lie Thr Phe Leu Glu lie Leu Leu 165 170 175 Phe His Pro Lys Phe Lys Gly Val Ser Arg Arg 180 185 <210> 59 <211> 41 <212> PRT <213> Homo sapiens <220> <221> SITE 36 <222> ( 41 ) <223> Xaa equals stop translation <400> 59 Met Thr Phe Ser Pro Leu Ser Ser Thr Phe Trp Trp Ser Ser Arg Phe 1 5 10 15 His Cys Glu Met Leu Trp Phe Val Ser Leu Leu Val Thr Phe Thr Ala 20 25 30 His Ser Val Glu Tyr Ser Gin Tyr Xaa 35 40 <210> 60 <211> 339 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (339) <223> Xaa equals stop translation <400> 60 Met Tyr Gly Tyr Val Asp Thr Leu Leu Thr Met Leu Ala Met Leu Leu 1 5 10 15 Lys Val Ala Met Asn Arg Ala Gin Val Cys Leu lie Ser Ser Ser Lys 20 25 30 Ser Gly Glu Arg His Leu Tyr Leu lie Lys Val Ser Arg Asp Lys lie 35 40 45 Ser Asp Ser Asn Asp Gin Glu Ser Ala Asn Cys Asp Ala Lys Ala lie 50 55 60 Phe Ala Val Leu Thr Ser Val Leu Thr Lys Asp Asp Trp Trp Asn Leu 65 70 75 80 Leu Leu Lys Ala lie Tyr Ser Leu Cys Asp Leu Ser Arg Phe Gin Glu 85 90 95 Ala Glu Leu Leu Val Asp Ser Ser Leu Glu Tyr Tyr Ser Phe Tyr Asp 100 105 110 Asp Arg Gin Lys Arg Lys Glu Leu Glu Tyr Phe Gly Leu Ser Ala Ala 115 120 125 lie Leu Asp Lys Asn Phe Arg Lys Ala Tyr Asn Tyr lie Arg lie Met 130 135 140 Val Met Glu Asn Val Asn Lys Pro Gin Leu Trp Asn lie Phe Asn Gin 145 150 155 160 37 Val Thr Met His Ser Gin Asp Val Arg His His Arg Phe Cys Leu Arg 165 170 175 Leu Met Leu Lys Asn Pro Glu Asn His Ala Leu Cys Val Leu Asn Gly 180 185 190 His Asn Ala Phe Val Ser Gly Ser Phe Lys His Ala Leu Gly Gin Tyr 195 200 205 Val Gin Ala Phe Arg Thr His Pro Asp Glu Pro Leu Tyr Ser Phe Cys 210 215 220 He Gly Leu Thr Phe He His Met Ala Ser Gin Lys Tyr Val Leu Arg 225 230 235 240 Arg His Ala Leu He Val Gin Gly Phe Ser Phe Leu Asn Arg Tyr Leu 245 250 255 Ser Leu Arg Gly Pro Cys Gin Glu Ser Phe Tyr Asn Leu Gly Arg Gly 260 265 270 Leu His Gin Leu Gly Leu He His Leu Ala He His Tyr Tyr Gin Lys 275 280 285 Ala Leu Glu Leu Pro Pro Leu Val Val Glu Gly He Glu Leu Asp Gin 290 295 300 Leu Asp Leu Arg Arg Asp He Ala Tyr Asn Leu Ser Leu He Tyr Gin 305 310 315 320 Ser Ser Gly Asn Thr Gly Met Ala Gin Thr Leu Leu Tyr Thr Tyr Cys 325 330 335 Ser He Xaa <210> 61 <211> 48 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (48) <223> Xaa equals stop translation <400> 61 Met Leu Thr Val Lys He Leu Lys Cys Phe Leu Gly Trp Ala Val Val 1 5 10 15 Ala Gly Gly Leu Gly Arg Ser Gin Ala Arg Pro Ser Leu Leu Phe Asn 20 25 30 Arg Leu Ser Pro Ser Val Pro Gin Met Arg He Gin Gin Pro Trp Xaa 38 35 40 45 <210> 62 <211> 336 <212> PRT <213> Homo sapiens <400> 62 Met Ala Ala Ala Val Ala Ala Ala Leu Ala Arg Leu Leu Ala Ala Phe 1 5 10 15 Leu Leu Leu Ala Ala Gin Val Ala Cys Glu Tyr Gly Met Val His Val 20 25 30 Val Ser Gin Ala Gly Gly Pro Glu Gly Lys Asp Tyr Cys He Leu Tyr 35 40 45 Asn Pro Gin Trp Ala His Leu Pro His Asp Leu Ser Lys Ala Ser Phe 50 55 60 Leu Gin Leu Arg Asn Trp Thr Ala Ser Leu Leu Cys Ser Ala Ala Asp 65 70 75 80 Leu Pro Ala Arg Gly Phe Ser Asn Gin He Pro Leu Val Ala Arg Gly 85 90 95 Asn Cys Thr Phe Tyr Glu Lys Val Arg Leu Ala Gin Gly Ser Gly Ala 100 105 110 Arg Gly Leu Leu He Val Ser Arg Glu Arg Leu Val Pro Pro Gly Gly 115 120 125 Asn Lys Thr Gin Tyr Asp Glu He Gly He Pro Val Ala Leu Leu Ser 130 135 140 Tyr Lys Asp Met Leu Asp He Phe Thr Arg Phe Gly Arg Thr Val Arg 145 150 155 160 Ala Ala Leu Tyr Ala Pro Lys Glu Pro Val Leu Asp Tyr Asn Met Val 165 170 175 He He Phe He Met Ala Val Gly Thr Val Ala He Gly Gly Tyr Trp 180 185 190 Ala Gly Ser Arg Asp Val Lys Lys Arg Tyr Met Lys His Lys Arg Asp 195 200 205 Asp Gly Pro Glu Lys Gin Glu Asp Glu Ala Val Asp Val Thr Pro Val 210 215 220 Met Thr Cys Val Phe Val Val Met Cys Cys Ser Met Leu Val Leu Leu 39 225 230 235 240 Tyr Tyr Phe Tyr Asp Leu Leu Val Cys Val Val He Gly He Phe Cys 245 250 255 Leu Ala Ser Ala Thr Gly Leu Tyr Ser Cys Leu Ala Pro Cys Val Arg 260 265 270 Arg Leu Pro Phe Gly Lys Cys Arg He Pro Asn Asn Ser Leu Pro Tyr 275 280 285 Phe His Lys Arg Pro Gin Ala Arg Met Leu Leu Leu Ala Leu Phe Cys 290 295 300 Val Ala Val Ser Val Val Trp Gly Val Phe Arg Asn Glu Asp Ser Gly 305 310 315 320 Pro Gly Ser Ser Arg Met Pro Trp Ala Ser Pro Ser Ala Ser Thr Cys 325 330 335 <210> 63 <211> 85 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (85) <223> Xaa equals stop translation <400> 63 Met Lys Gly Trp Gly Trp Leu Ala Leu Leu Leu Gly Ala Leu Leu Gly 1 5 10 15 Thr Ala Trp Ala Arg Arg Ser Gin Asp Leu His Cys Gly Ala Cys Arg 20 25 30 Ala Leu Val Asp Glu Leu Glu Trp Glu He Ala Gin Val Asp Pro Lys 35 40 45 Lys Thr He Gin Met Gly Ser Phe Arg He Asn Pro Asp Gly Ser Gin 50 55 60 Ser Val Val Glu Val Thr Val Thr Val Pro Pro Asn Lys Val Ala His 65 70 75 80 Ser Gly Phe Gly Xaa 85 <210> 64 40 <211> 63 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (63) <223> Xaa equals stop translation <400> 64 Met Val Ala Val Thr Gly Gly Val Gly Val Ala Ala Ala Leu Cys Leu 1 5 10 15 Cys Ser Leu Leu Leu Trp Pro Thr Arg Leu Arg Arg Ser Arg Gly Gly 20 25 30 Glu His Arg Thr Pro Ser Glu Gly Glu Gly He Ser Thr Ala Pro Pro 35 40 45 Pro Cys Trp Asn Glu Thr Gin Pro Gin Gly Gly Ala Lys Leu Xaa 50 55 60 <210> 65 <211> 50 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (50) <223> Xaa equals stop translation <400> 65 Met Arg Leu Cys Ser Phe Thr Lys Val Pro Met Asn Leu Phe Leu Asn 1 5 10 15 Val He Leu Leu Lys Phe Tyr Asn Phe Leu Phe Ser Leu He Leu Gly 20 25 30 Lys Ser Cys Leu Ala Ser Leu Gly Leu Cys Lys Asn Asn Lys Cys Leu 35 40 45 Ser Xaa 50 <210> 66 <211> 402 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (402) 41 <223> Xaa equals stop translation <400> 66 Met Val Ala Leu Arg Gly Ala Ser Ala Leu Leu Val Leu Phe Leu Ala 1 5 10 15 Ala Phe Leu Pro Pro Pro Gin Cys Thr Gin Asp Pro Ala Met Val His 20 25 30 Tyr He Tyr Gin Arg Phe Arg Val Leu Glu Gin Gly Leu Glu Lys Cys 35 40 45 Thr Gin Ala Thr Arg Ala Tyr He Gin Glu Phe Gin Glu Phe Ser Lys 50 55 60 Asn He Ser Val Met Leu Gly Arg Cys Gin Thr Tyr Thr Ser Glu Tyr 65 70 75 80 Lys Ser Ala Val Gly Asn Leu Ala Leu Arg Val Glu Arg Ala Gin Arg 85 90 95 Glu He Asp Tyr He Gin Tyr Leu Arg Glu Ala Asp Glu Cys He Glu 100 105 110 Ser Glu Asp Lys Thr Leu Ala Glu Met Leu Leu Gin Glu Ala Glu Glu 115 120 125 Glu Lys Lys He Arg Thr Leu Leu Asn Ala Ser Cys Asp Asn Met Leu 130 135 140 Met Gly He Lys Ser Leu Lys He Val Lys Lys Met Met Asp Thr His 145 150 155 160 Gly Ser Trp Met Lys Asp Ala Val Tyr Asn Ser Pro Lys Val Tyr Leu 165 170 175 Leu He Gly Ser Arg Asn Asn Thr Val Trp Glu Phe Ala Asn He Arg 180 185 190 Ala Phe Met Glu Asp Asn Thr Lys Pro Ala Pro Arg Lys Gin He Leu 195 200 205 Thr Leu Ser Trp Gin Gly Thr Gly Gin Val He Tyr Lys Gly Phe Leu 210 215 220 Phe Phe His Asn Gin Ala Thr Ser Asn Glu He He Lys Tyr Asn Leu 225 230 235 240 Gin Lys Arg Thr Val Glu Asp Arg Met Leu Leu Pro Gly Gly Val Gly 245 250 255 Arg Ala Leu Val Tyr Gin His Ser Pro Ser Thr Tyr He Asp Leu Ala 260 265 270 Val Asp Glu His Gly Leu Trp Ala He His Ser Gly Pro Gly Thr His 42 275 280 285 Ser His Leu Val Leu Thr Lys He Glu Pro Gly Thr Leu Gly Val Glu 290 295 300 His Ser Trp Asp Thr Pro Cys Arg Ser Gin Asp Ala Glu Ala Ser Phe 305 310 315 320 Leu Leu Cys Gly Val Leu Tyr Val Val Tyr Ser Thr Gly Gly Gin Gly 325 330 335 Pro His Arg He Thr Cys He Tyr Asp Pro Leu Gly Thr He Ser Glu 340 345 350 Glu Asp Leu Pro Asn Leu Phe Phe Pro Lys Arg Pro Arg Ser His Ser 355 360 365 Met He His Tyr Asn Pro Arg Asp Lys Gin Leu Tyr Ala Trp Asn Glu 370 375 380 Gly Asn Gin He He Tyr Lys Leu Gin Thr Lys Arg Lys Leu Thr Leu 385 390 395 400 Lys Xaa <210> 67 <211> 58 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (58) <223> Xaa equals stop translation <400> 67 Met Val Ser Leu Leu Ser Ser Tyr Leu Leu Leu Leu Glu Leu Leu Ser 1 5 10 15 Lys Arg Ser Leu Phe Leu Gin Trp Tyr Leu Phe Phe Gly Leu Gin Cys 20 25 30 Cys Ser Ser Phe Leu Cys Arg Lys Asn Glu Ser Gin Cys Phe Thr Arg 35 40 45 Leu Lys Glu Arg Ser Ala Gly Ser Val Xaa 50 55 <210> 68 <211> 73 <212> PRT <213> Homo sapiens 43 <220> <221> SITE <222> (73 ) <223> Xaa equals stop translation <400> 68 Met Leu Arg Pro Ala Leu Pro Trp Leu Tyr Leu Gly Leu Cys Ser Leu 1 5 10 15 Leu Val Gly Glu Ala Glu Ala Pro Ser Pro Val Asp Pro Leu Glu Arg 20 25 30 Ser Arg Pro Tyr Ala Val Leu Arg Gly Gin Asn Leu Val Leu Met Gly 35 40 45 Thr He Phe Ser He Leu Leu Val Thr Val He Leu Met Ala Phe Cys 50 55 60 Val Tyr Lys Pro He Arg Arg Arg Xaa 65 70 <210> 69 <211> 51 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (51) <223> Xaa equals stop translation <400> 69 Met Leu Thr Tyr Leu Pro Arg Trp Cys Phe Leu Ser Leu Pro Pro Pro 1 5 10 15 Cys Cys Gly Ala Ala Ser Cys Thr Met Met His He Gin He He Leu 20 25 30 Asn Thr His He Leu He Glu Arg Phe Leu Gly Phe Leu Leu Asn Gin 35 40 45 Val Tyr Xaa 50 <210> 70 <211> 182 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (182) 44 <223> Xaa equals stop translation <400> 70 Met Thr Ser Arg Arg Ser Ser Thr Leu Ser Met Thr Ser Ser Leu Leu 1 5 10 15 Ser Leu Gly Cys Ala Leu Thr Ser Ala Phe Pro Ala Ser Thr Met Ser 20 25 30 Trp Val Pro Leu Leu Gin Met Leu Asp Gin Ser Pro Arg Arg Val Met 35 40 45 Arg Lys Ser Val Ser Gin Leu Cys Pro Leu Leu Arg Pro His Pro Pro 50 55 60 Leu Ser Ser Lys His Pro Leu Val Leu Pro Leu Gin Leu Pro Pro Thr 65 70 75 80 Phe Leu His Leu Leu Pro Gly Pro Gly Cys Pro Gly Gin Thr Val Ala 85 90 95 Tyr Trp Leu Leu Glu Phe Leu Ser Arg Ala Thr Leu Lys Leu Tyr Pro 100 105 110 Gly Asp Arg Pro Leu Trp Leu Gin Pro Thr Arg Leu Asn Phe Lys Asp 115 120 125 His Trp Thr He Phe Ser Val Ala Ser Ala Ala Leu Phe Cys Val His 130 135 140 Arg Met Ala Thr Asp Arg His Ala Ser Phe Pro Thr His Trp Lys Ala 145 150 155 160 His Arg Gin Gly Glu Arg Gly His Arg Arg Cys Gin His Cys Arg Tyr 165 170 175 Ser Lys Asp Leu Lys Xaa 180 <210> 71 <211> 49 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (49) <223> Xaa equals stop translation <400> 71 Met His Met Gly Leu Thr Thr Cys Lys Cys His Trp Lys Met Ala Tyr 1 5 10 15 Leu Arg Phe Leu He Leu Trp Ser Phe Pro Leu Ser Ser Ala Val Ser 45 20 25 30 Gly Ala Lys Arg Val Thr Asp Leu Leu Asn Gly Lys His Trp Lys Pro 35 40 45 Xaa <210> 72 <211> 54 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (54) <223> Xaa equals stop translation <400> 72 Met Val Gin Phe Glu Val He Phe Leu Leu Phe Gly Leu Cys Phe Ser 1 5 10 15 Ser Ser Ser Ser Arg Leu Val Gly Ser Gin Val Glu Asn Phe Ser Pro 20 25 30 Thr Pro Cys He Phe Gin Ala Phe Arg Cys Ser Ser Leu Ala He He 35 40 45 Ser Met Ser Leu Ser Xaa 50 <210> 73 <211> 75 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (75) <223> Xaa equals stop translation <400> 73 Met Ser Val Val Pro Val Met He Pro Phe Leu Leu Leu Leu Phe Phe 1 5 10 15 Phe Ser Leu Ser Ser Thr His His Pro His Leu Leu Tyr Phe Ser He 20 25 30 Phe He Phe Ser Gly Ser Leu Leu Val Arg He Leu Ser Cys Arg Lys 35 40 45 Glu Ser Ser His Gin Val Leu Leu Ser Arg Lys Cys Phe He Lys Gly 50 55 60 46 His Arg Gin His Arg Gin Leu Thr Lys Val Xaa 65 70 75 <210> 74 <211> 65 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (65) <223> Xaa equals stop translation <400> 74 Met Pro Leu Phe Leu Phe Val Ala His Leu He Ser Leu Leu Leu Ala 1 5 10 15 Phe Arg Arg Pro Pro Ala Ser Gin He Thr Pro Arg Ala Trp Thr Thr 20 25 30 Glu He Ala Ser Cys Glu Ser Val Glu Met Val Lys Ala Leu Ser Ser 35 40 45 Leu Arg Ser Arg Ala Gin Val Asn Ala Asp Phe Pro Gly His Leu Cys 50 55 60 Xaa 65 <210> 75 <211> 44 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (44) <223> Xaa equals stop translation <400> 75 Met Ser Ser Val Lys Cys Pro Tyr Met Trp Cys Phe Trp Ala Phe Pro 1 5 10 15 Leu Phe Gin Leu Ser Val Phe He Pro Val Ser Lys Ser His Ser He 20 25 30 Asn Tyr Tyr Asn Phe He Val Ser Leu Asn He Xaa 35 40 <210> 76 <211> 53 47 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (53) <223> Xaa equals stop translation <400> 76 Met He Leu Phe Met Cys Phe Leu Val Tyr Cys Leu Ser Ser Val Glu 1 5 10 15 Trp Lys Ser His Arg Tyr Phe Val Phe Phe Ser Pro Cys Pro Phe Leu 20 25 30 Tyr Pro Gin Leu Leu Glu His Ser Leu Glu His Ser Lys Cys Ser Val 35 40 45 Leu Phe Met Glu Xaa 50 <210> 77 <211> 320 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (320) <223> Xaa equals stop translation <400> 77 Met Ser Trp Cys Cys Leu Trp Leu Cys Leu Ser Ser Val Gly Arg Thr 1 5 10 15 Gly Ser Ala Gly Pro Ser Leu Pro Phe Ser Glu Leu Cys Ser Leu Gly 20 25 30 Leu Leu Arg Leu Arg Pro Val Phe Ser Pro Leu His Ser Gly Pro Gly 35 40 45 Lys Pro Ala Gin Phe Leu Ala Gly Glu Ala Glu Glu Val Asn Ala Phe 50 55 60 Ala Leu Gly Phe Leu Ser Thr Ser Ser Gly Val Ser Gly Glu Asp Glu 65 70 75 80 Val Glu Pro Leu His Asp Gly Val Glu Glu Ala Glu Lys Lys Met Glu 85 90 95 Glu Glu Gly Val Ser Val Ser Glu Met Glu Ala Thr Gly Ala Gin Gly 100 105 110 Pro Ser Arg Val Glu Glu Ala Glu Gly His Thr Glu Val Thr Glu Ala 48 115 120 125 Glu Gly Ser Gin Gly Thr Ala Glu Ala Asp Gly Pro Gly Ala Ser Ser 130 135 140 Gly Asp Glu Asp Ala Ser Gly Arg Ala Ala Ser Pro Glu Ser Ala Ser 145 150 155 160 Ser Thr Pro Glu Ser Leu Gin Ala Arg Arg His His Gin Phe Leu Glu 165 170 175 Pro Ala Pro Ala Pro Gly Ala Ala Val Leu Ser Ser Glu Pro Ala Glu 180 185 190 Pro Leu Leu Val Arg His Pro Pro Arg Pro Arg Thr Thr Gly Pro Arg 195 200 205 Pro Arg Gin Asp Pro His Lys Ala Gly Leu Ser His Tyr Val Lys Leu 210 215 220 Phe Ser Phe Tyr Ala Lys Met Pro Met Glu Arg Lys Ala Leu Glu Met 225 230 235 240 Val Glu Lys Cys Leu Asp Lys Tyr Phe Gin His Leu Cys Asp Asp Leu 245 250 255 Glu Val Phe Ala Ala His Ala Gly Arg Lys Thr Val Lys Pro Glu Asp 260 265 270 Leu Glu Leu Leu Met Arg Arg Gin Gly Leu Val Thr Asp Gin Val Ser 275 280 285 Leu His Val Leu Val Glu Arg His Leu Pro Leu Glu Tyr Arg Gin Leu 290 295 300 Leu He Pro Cys Ala Tyr Ser Gly Asn Ser Val Phe Pro Ala Gin Xaa 305 310 315 320 <210> 78 <211> 172 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (172) <223> Xaa equals stop translation <400> 78 Met Ser Leu Pro He Pro Trp Leu Ser Leu Pro Pro Cys Pro He Leu 1 5 10 15 49 Gly Gin Pro Ala Gly Leu Leu Leu Trp Leu Phe Arg Pro Phe Ser Gin 20 25 30 Cys Cys Gin Cys Pro Trp Glu Gly Arg Ala Ser Leu Arg His Pro Asn 35 40 45 Gly Pro Ser Gly Cys Arg Glu Ala Glu Ala Trp Pro Gin Arg Ser Leu 50 55 60 Leu Arg Gin Gin Leu Gin Gin Ala His Pro Leu Pro Thr Leu Pro Thr 65 70 75 80 Pro Glu Arg Leu Pro Glu Gin Met Leu Phe Pro Ser Ser Ser Ser Lys 85 90 95 Pro Phe Ser Leu Leu Ser Leu Thr He Trp Ala Arg Leu Val Gly Arg 100 105 110 Leu Thr Asn Arg He Cys Pro Val Pro Pro Gly Ser Val Ala Ser Ser 115 120 125 Met Ser Leu Gin Ala Gly Arg Cys Gly Asn Pro Val Val Leu Pro Gin 130 135 140 Pro Met Pro Pro Gly Leu Leu Cys Met Asn Glu Cys Ser Leu Val Pro 145 150 155 160 Gly Leu Gly Arg Gly Gin Val Asn Ser Arg Val Xaa 165 170 <210> 79 <211> 61 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (61) <223> Xaa equals stop translation <400> 79 Met Val Ser Arg Ser Thr Ser Leu Thr Leu He Val Phe Leu Phe His 1 5 10 15 Arg Leu Ser Lys Ala Pro Gly Lys Met Val Glu Asn Ser Pro Ser Pro 20 25 30 Leu Pro Glu Arg Ala He Tyr Gly Phe Val Leu Phe Leu Ser Ser Gin 35 40 45 Phe Gly Phe Lys Asn Leu Lys Gly Ser Arg Val Cys Xaa 50 55 60 50 <210> 80 <211> 101 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (20) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (37) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (101) <223> Xaa equals stop translation <400> 80 Met Leu Pro Ser Ala Trp Gly Pro Leu Gin Val Ala Ser Phe Phe Leu 1 5 10 15 Leu Ser Phe Xaa Phe Cys Phe Leu Ser Ser Ser Pro His Leu Gly Arg 20 25 30 Gin Glu Thr His Xaa Val Val Leu Glu Asp Asp Glu Gly Ala Pro Cys 35 40 45 Pro Ala Glu Asp Glu Leu Ala Leu Gin Asp Asn Gly Phe Leu Ser Lys 50 55 60 Asn Glu Val Leu Arg Thr Arg Cys Leu Gly Ser Arg Ser Gly Ser Ala 65 70 75 80 Ser Ala Thr Pro Pro Thr Thr Ser Gly Thr Ala Arg Ala Ala Arg Pro 85 90 95 Pro Ser Gin Cys Xaa 100 <210> 81 <211> 98 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (98) <223> Xaa equals stop translation <400> 81 51 Met Ala Leu Leu Ala Leu Ala Ser Ala Val Pro Ser Ala Leu Leu Ala 1 5 10 15 Leu Ala Val Phe Arg Val Pro Ala Trp Ala Cys Leu Leu Cys Phe Thr 20 25 30 Thr Tyr Ser Glu Arg Leu Arg He Cys Gin Met Phe Val Gly Met Arg 35 40 45 Ser Pro Ser Leu Lys Ser Val Arg Arg Pro Ser Arg Pro Pro Ser Arg 50 55 60 Ala Ser Leu Thr Pro Lys Ser Val Arg Arg Pro Ser Thr Leu His Gin 65 70 75 80 Cys Pro Gly Glu Gly Ala Glu Gly Gly Gin Glu Arg Pro Arg Gly Ser 85 90 95 Gly Xaa <210> 82 <211> 53 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (53) <223> Xaa equals stop translation <400> 82 Met Trp Leu Asn Phe Ser Asp Val His Thr Tyr Leu Ser Ser He Ala 1 5 10 15 Leu Leu Cys Phe Cys Leu Ser Gly Val Leu Cys Cys He Cys Asn Asn 20 25 30 Ser Val Phe His He Gin Gin Tyr He Leu He He He Thr Phe Pro 35 40 45 Leu Val Val He Xaa 50 <210> 83 <211> 41 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (41) <223> Xaa equals stop translation 52 <400> 83 Met Ser His Ala Ser Arg Lys Thr Lys His Phe Pro Pro Leu Leu Gin 1 5 10 15 Asn Pro Phe Leu Met Leu Thr Leu Leu Thr Met Ala Val Ser Ala Gin 20 25 30 Pro Leu Pro Phe Ser Arg Pro Arg Xaa 35 40 <210> 84 <211> 133 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (122) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (133) <223> Xaa equals stop translation <400> 84 Met Ala Ala Ala Val Ala Ala Ala Leu Ala Arg Leu Leu Ala Ala Phe 1 5 10 15 Leu Leu Leu Ala Ala Gin Val Ala Cys Glu Tyr Gly Met Val His Val 20 25 30 Val Ser Gin Ala Gly Gly Pro Glu Gly Lys Asp Tyr Cys He Leu Tyr 35 40 45 Asn Pro Gin Trp Ala His Leu Pro His Asp Leu Ser Lys Ala Ser Phe 50 55 60 Leu Gin Leu Arg Asn Trp Thr Ala Ser Leu Leu Cys Ser Ala Ala Asp 65 70 75 80 Leu Pro Ala Arg Gly Phe Ser Asn Gin He Pro Leu Val Ala Arg Gly 85 90 95 Asn Cys Thr Phe Tyr Glu Lys Val Arg Leu Ala Gin Gly Ser Gly His 100 105 110 Ala Gly Cys Ser Ser Ser Ala Gly Arg Xaa Trp Ser Pro Arg Gly Val 115 120 125 He Arg Arg He Xaa 130 53 <210> 85 <211> 11 <212> PRT <213> Homo sapiens <400> 85 His Ser Ser Leu Pro His Phe Ser Ser Arg He 1 5 10 <210> 86 <211> 22 <212> PRT <213> Homo sapiens <400> 86 Arg Asp Ser Asn Gly Arg Gly Asp Ser Ser Leu Leu Lys Phe Val Cys 1 5 10 15 Pro Val Pro Leu Lys Lys 20 <210> 87 <211> 12 <212> PRT <213> Homo sapiens <400> 87 He Pro Glu Tyr Thr Phe Arg Arg Arg Trp Phe His 1 5 10 <210> 88 <211> 17 <212> PRT <213> Homo sapiens <400> 88 Leu Cys Val Ser Met Lys He Glu Trp Gly Arg Glu Ser Cys Glu Lys 1 5 10 15 Lys <210> 89 <211> 25 <212> PRT <213> Homo sapiens <400> 89 Arg Leu Lys Thr Thr Arg Ala Tyr Ser Ser Gin Phe Trp Arg Pro Glu 1 5 10 15 54 Val Gin Asn Gin Gly Val Arg Lys Val 20 25 <210> 90 <211> 165 <212> PRT <213> Homo sapiens <400> 90 Leu Thr Leu Cys Leu Pro Arg Ser Leu Tyr Ala Leu Pro Gin Cys Pro 1 5 10 15 Gly Pro His Val His Pro Cys Pro Ala Leu Leu Trp Asp Arg Ala Gly 20 25 30 Leu Pro Leu Pro Leu Pro Gly Cys He His Gly Arg Ser Gin Val Pro 35 40 45 Trp His Glu Leu His Ser Pro Ala Ala Phe Asn Gin Gly Met Met Gly 50 55 60 Met Cys Thr Tyr Pro Thr Pro Pro Leu Gly Arg Val Met Leu Arg Cys 65 70 75 80 Gly Phe Leu Thr Val Pro Arg Leu Ser Gin Glu Ala Trp Val Trp Val 85 90 95 Pro Thr Val Gly Ala Gly Val He Ser Tyr Leu Arg Arg Pro Pro Phe 100 105 110 Leu Pro Val Leu Cys Ala Pro Thr Pro Thr Leu Glu Leu Pro Arg Phe 115 120 125 Ser Val Phe Val Lys Glu Leu Thr Leu Cys Cys Leu Pro Leu Ser Gin 130 135 140 Cys Pro Cys His Ser Cys Glu Pro Ala Ala Gly Glu Val Gly Ala Asp 145 150 155 160 Leu Cys Val Ala Gly 165 <210> 91 <211> 41 <212> PRT <213> Homo sapiens <400> 91 Leu Thr Leu Cys Leu Pro Arg Ser Leu Tyr Ala Leu Pro Gin Cys Pro 1 5 10 15 Gly Pro His Val His Pro Cys Pro Ala Leu Leu Trp Asp Arg Ala Gly 55 20 25 30 Leu Pro Leu Pro Leu Pro Gly Cys He 35 40 <210> 92 <211> 38 <212> PRT <213> Homo sapiens <400> 92 His Gly Arg Ser Gin Val Pro Trp His Glu Leu His Ser Pro Ala Ala 1 5 10 15 Phe Asn Gin Gly Met Met Gly Met Cys Thr Tyr Pro Thr Pro Pro Leu 20 25 30 Gly Arg Val Met Leu Arg 35 <210> 93 <211> 41 <212> PRT <213> Homo sapiens <400> 93 Cys Gly Phe Leu Thr Val Pro Arg Leu Ser Gin Glu Ala Trp Val Trp 1 5 10 15 Val Pro Thr Val Gly Ala Gly Val He Ser Tyr Leu Arg Arg Pro Pro 20 25 30 Phe Leu Pro Val Leu Cys Ala Pro Thr 35 40 <210> 94 <211> 45 <212> PRT <213> Homo sapiens <400> 94 Pro Thr Leu Glu Leu Pro Arg Phe Ser Val Phe Val Lys Glu Leu Thr 1 5 10 15 Leu Cys Cys Leu Pro Leu Ser Gin Cys Pro Cys His Ser Cys Glu Pro 20 25 30 Ala Ala Gly Glu Val Gly Ala Asp Leu Cys Val Ala Gly 35 40 45 <210> 95 56 <211> 38 <212> PRT <213> Homo sapiens <400> 95 He Arg His Glu Thr Phe Arg Val Arg Gly Cys Ser He Ser Arg Ala 1 5 10 15 Leu Ser Pro Phe Pro Leu Pro Phe Pro His Pro Gly Arg Ser Gly Trp 20 25 30 Ser Gly Pro Glu Ala Lys 35 <210> 96 <211> 145 <212> PRT <213> Homo sapiens <400> 96 Pro Asp Ser Arg Pro Glu Ala Arg Gly Asp His Val Val Arg Pro Ser 1 5 10 15 Arg Gly Leu Arg Val Thr Gly Ala Thr Arg Ser He Met Gly Pro Trp 20 25 30 Gly Glu Pro Glu Leu Leu Val Trp Arg Pro Glu Ala Val Ala Ser Glu 35 40 45 Pro Pro Val Pro Val Gly Leu Glu Val Lys Leu Gly Ala Leu Val Leu 50 55 60 Leu Leu Val Leu Thr Leu Leu Cys Ser Leu Val Pro He Cys Val Leu 65 70 75 80 Arg Arg Pro Gly Ala Asn His Glu Gly Ser Ala Ser Arg Gin Lys Ala 85 90 95 Leu Ser Leu Val Ser Cys Phe Ala Gly Gly Val Phe Leu Ala Thr Cys 100 105 110 Leu Leu Asp Leu Leu Pro Asp Tyr Leu Ala Ala He Asp Glu Ala Leu 115 120 125 Ala Ala Leu His Val Thr Leu Gin Phe Pro Leu Gin Glu Phe He Leu 130 135 140 Ala 145 <210> 97 <211> 35 <212> PRT 57 <213> Homo sapiens <400> 97 Pro Asp Ser Arg Pro Glu Ala Arg Gly Asp His Val Val Arg Pro Ser 1 5 10 15 Arg Gly Leu Arg Val Thr Gly Ala Thr Arg Ser He Met Gly Pro Trp 20 25 30 Gly Glu Pro 35 <210> 98 <211> 37 <212> PRT <213> Homo sapiens <400> 98 Glu Leu Leu Val Trp Arg Pro Glu Ala Val Ala Ser Glu Pro Pro Val 1 5 10 15 Pro Val Gly Leu Glu Val Lys Leu Gly Ala Leu Val Leu Leu Leu Val 20 25 30 Leu Thr Leu Leu Cys 35 <210> 99 <211> 36 <212> PRT <213> Homo sapiens <400> 99 Ser Leu Val Pro He Cys Val Leu Arg Arg Pro Gly Ala Asn His Glu 1 5 10 15 Gly Ser Ala Ser Arg Gin Lys Ala Leu Ser Leu Val Ser Cys Phe Ala 20 25 30 Gly Gly Val Phe 35 <210> 100 <211> 37 <212> PRT <213> Homo sapiens <400> 100 Leu Ala Thr Cys Leu Leu Asp Leu Leu Pro Asp Tyr Leu Ala Ala He 1 5 10 15 Asp Glu Ala Leu Ala Ala Leu His Val Thr Leu Gin Phe Pro Leu Gin 58 20 25 30 Glu Phe He Leu Ala 35 <210> 101 <211> 28 <212> PRT <213> Homo sapiens <400> 101 Lys Tyr He Leu Ser Ser Pro Leu Leu Asp Ser Leu Ala Glu His Lys 1 5 10 15 Asn Leu Val Trp Lys Ser Phe Leu Pro Arg Asn Phe 20 25 <210> 102 <211> 70 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (53) <223> Xaa equals any of the naturally occurring L-amino acids <400> 102 Tyr Gly Lys Val Val Asp Leu Ala Pro Leu His Leu Asp Ala Arg He 1 5 10 15 Ser Leu Ser Thr Leu Gin Gin Gin Leu Gly Gin Pro Glu Lys Ala Leu 20 25 30 Glu Ala Leu Glu Pro Met Tyr Asp Pro Asp Thr Leu Ala Gin Asp Ala 35 40 45 Asn Ala Ala Gin Xaa Glu Leu Lys Leu Leu Leu His Arg Ser Thr Leu 50 55 60 Leu Phe Ser Gin Gly Lys 65 70 <210> 103 <211> 96 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (58) <223> Xaa equals any of the naturally occurring L-amino acids 59 <400> 103 Asp Phe Met Glu Thr Phe Pro Asp Phe Cys Leu Pro Leu Ala Pro His 1 5 10 15 Tyr Leu Gly Lys Ala Ala Leu Trp Ala Met Cys Pro Gly Arg Ala Trp 20 25 30 Ala Gly Cys Gly Pro Val Leu Arg Thr Ser His Leu Gly Pro His Ser 35 40 45 Ala Leu Pro Ser Trp Cys Asn He Cys Xaa Gin Ala He Val Gly Ala 50 55 60 Gly Arg Gin Arg Gly Leu Ser Glu Asp Pro Thr Cys Ala Ser His Trp 65 70 75 80 Asp Thr Lys Thr Gly Leu Val Pro Ser Cys Gly Ala Gly Lys Gly He 85 90 95 <210> 104 <211> 44 <212> PRT <213> Homo sapiens <400> 104 Asp Phe Met Glu Thr Phe Pro Asp Phe Cys Leu Pro Leu Ala Pro His 1 5 10 15 Tyr Leu Gly Lys Ala Ala Leu Trp Ala Met Cys Pro Gly Arg Ala Trp 20 25 30 Ala Gly Cys Gly Pro Val Leu Arg Thr Ser His Leu 35 40 <210> 105 <211> 52 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (14) <223> Xaa equals any of the naturally occurring L-amino acids <400> 105 Gly Pro His Ser Ala Leu Pro Ser Trp Cys Asn He Cys Xaa Gin Ala 1 5 10 15 He Val Gly Ala Gly Arg Gin Arg Gly Leu Ser Glu Asp Pro Thr Cys 60 20 25 30 Ala Ser His Trp Asp Thr Lys Thr Gly Leu Val Pro Ser Cys Gly Ala 35 40 45 Gly Lys Gly He 50 <210> 106 <211> 280 <212> PRT <213> Homo sapiens <400> 106 Arg Leu Pro Gin Arg Gly Gin Trp Ala Trp Val Leu Gin Asp Ala Leu 1 5 10 15 Gly He Ala Phe Cys Leu Tyr Met Leu Lys Thr He Arg Leu Pro Thr 20 25 30 Phe Lys Ala Cys Thr Leu Leu Leu Leu Val Leu Phe Leu Tyr Asp He 35 40 45 Phe Phe Val Phe He Thr Pro Phe Leu Thr Lys Ser Gly Ser Ser He 50 55 60 Met Val Glu Val Ala Thr Gly Pro Ser Asp Ser Ala Thr Arg Glu Lys 65 70 75 80 Leu Pro Met Val Leu Lys Val Pro Arg Leu Asn Ser Ser Pro Leu Ala 85 90 95 Leu Cys Asp Arg Pro Phe Ser Leu Leu Gly Phe Gly Asp He Leu Val 100 105 110 Pro Gly Leu Leu Val Ala Tyr Cys His Arg Phe Asp He Gin Val Gin 115 120 125 Ser Ser Arg Val Tyr Phe Val Ala Cys Thr He Ala Tyr Gly Val Gly 130 135 140 Leu Leu Val Thr Phe Val Ala Leu Ala Leu Met Gin Arg Gly Gin Pro 145 150 155 160 Ala Leu Leu Tyr Leu Val Pro Cys Thr Leu Val Thr Ser Cys Ala Val 165 170 175 Ala Leu Trp Arg Arg Glu Leu Gly Val Phe Trp Thr Gly Ser Gly Phe 180 185 190 Ala Lys Val Leu Pro Pro Ser Pro Trp Ala Pro Ala Pro Ala Asp Gly 195 200 205 Pro Gin Pro Pro Lys Asp Ser Ala Thr Pro Leu Ser Pro Gin Pro Pro 61 210 215 220 Ser Glu Glu Pro Ala Thr Ser Pro Trp Pro Ala Glu Gin Ser Pro Lys 225 230 235 240 Ser Arg Thr Ser Glu Glu Met Gly Ala Gly Ala Pro Met Arg Glu Pro 245 250 255 Gly Ser Pro Ala Glu Ser Glu Gly Arg Asp Gin Ala Gin Pro Ser Pro 260 265 270 Val Thr Gin Pro Gly Ala Ser Ala 275 280 <210> 107 <211> 43 <212> PRT <213> Homo sapiens <400> 107 Arg Leu Pro Gin Arg Gly Gin Trp Ala Trp Val Leu Gin Asp Ala Leu 1 5 10 15 Gly He Ala Phe Cys Leu Tyr Met Leu Lys Thr He Arg Leu Pro Thr 20 25 30 Phe Lys Ala Cys Thr Leu Leu Leu Leu Val Leu 35 40 <210> 108 <211> 44 <212> PRT <213> Homo sapiens <400> 108 Phe Leu Tyr Asp He Phe Phe Val Phe He Thr Pro Phe Leu Thr Lys 1 5 10 15 Ser Gly Ser Ser He Met Val Glu Val Ala Thr Gly Pro Ser Asp Ser 20 25 30 Ala Thr Arg Glu Lys Leu Pro Met Val Leu Lys Val 35 40 <210> 109 <211> 44 <212> PRT <213> Homo sapiens <400> 109 Pro Arg Leu Asn Ser Ser Pro Leu Ala Leu Cys Asp Arg Pro Phe Ser 1 5 10 15 62 Leu Leu Gly Phe Gly Asp He Leu Val Pro Gly Leu Leu Val Ala Tyr 20 25 30 Cys His Arg Phe Asp He Gin Val Gin Ser Ser Arg 35 40 <210> 110 <211> 43 <212> PRT <213> Homo sapiens <400> 110 Val Tyr Phe Val Ala Cys Thr He Ala Tyr Gly Val Gly Leu Leu Val 1 5 10 15 Thr Phe Val Ala Leu Ala Leu Met Gin Arg Gly Gin Pro Ala Leu Leu 20 25 30 Tyr Leu Val Pro Cys Thr Leu Val Thr Ser Cys 35 40 <210> 111 <211> 40 <212> PRT <213> Homo sapiens <400> 111 Ala Val Ala Leu Trp Arg Arg Glu Leu Gly Val Phe Trp Thr Gly Ser 1 5 10 15 Gly Phe Ala Lys Val Leu Pro Pro Ser Pro Trp Ala Pro Ala Pro Ala 20 25 30 Asp Gly Pro Gin Pro Pro Lys Asp 35 40 <210> 112 <211> 41 <212> PRT <213> Homo sapiens <400> 112 Ser Ala Thr Pro Leu Ser Pro Gin Pro Pro Ser Glu Glu Pro Ala Thr 1 5 10 15 Ser Pro Trp Pro Ala Glu Gin Ser Pro Lys Ser Arg Thr Ser Glu Glu 20 25 30 Met Gly Ala Gly Ala Pro Met Arg Glu 35 40 63 <210> 113 <211> 25 <212> PRT <213> Homo sapiens <400> 113 Pro Gly Ser Pro Ala Glu Ser Glu Gly Arg Asp Gin Ala Gin Pro Ser 1 5 10 15 Pro Val Thr Gin Pro Gly Ala Ser Ala 20 25 <210> 114 <211> 26 <212> PRT <213> Homo sapiens <400> 114 Glu Ser Ser Gly Leu Pro Ala Leu Gly Pro Arg Arg Arg Pro Trp Glu 1 5 10 15 Gin Arg Trp Ser Asp Pro He Thr Leu Lys 20 25 <210> 115 <211> 61 <212> PRT <213> Homo sapiens <400> 115 Leu Thr Leu Ala Leu Asp Glu He Arg Leu Leu Lys Lys Asp Leu Gly 1 5 10 15 Leu He Glu Met Lys Lys Thr Asp Ser Glu Lys Arg Phe Gly Ser Val 20 25 30 Ser Phe Gly Arg Ser Cys Arg Leu He Pro His Ala Leu Ala Ser Trp 35 40 45 Leu Gin Thr Leu He Leu Cys Phe Cys Cys Arg He Cys 50 55 60 <210> 116 <211> 32 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (27) <223> Xaa equals any of the naturally occurring L-amino acids 64 <400> 116 Gly Arg Pro Thr Arg Pro Val Met Ala He Gin Ser Leu His Pro Cys 1 5 10 15 Pro Ser Glu Leu Cys Cys Arg Ala Cys Val Xaa Phe Tyr His Trp Ala 20 25 30 <210> 117 <211> 29 <212> PRT <213> Homo sapiens <400> 117 Asn Ser Lys Asn Thr Arg Asn Glu Arg Ser Phe Leu Lys Leu Phe Arg 1 5 10 15 Asn He His Asp He Pro Leu Thr Val Leu Glu Asn Lys 20 25 <210> 118 <211> 20 <212> PRT <213> Homo sapiens <400> 118 Pro Arg Val Arg Gly Glu Gly Asn Arg Cys Trp Thr Gin Gly Ala Leu 1 5 10 15 Cys His Arg Met 20 <210> 119 <211> 27 <212> PRT <213> Homo sapiens <400> 119 Phe Pro Cys He Cys Leu Ser Gly Leu Leu Asp Leu Leu He Trp Arg 1 5 10 15 Pro Phe Ser Glu Glu Leu Thr Lys Thr Phe Gly 20 25 <210> 120 <211> 24 <212> PRT <213> Homo sapiens 65 <220> <221> SITE <222> (8) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (24) <223> Xaa equals any of the naturally occurring L-amino acids <400> 120 Lys Asp Thr Cys Thr Arg Met Xaa He Ala Ala Leu Phe Thr He Ala 1 5 10 15 Lys He Trp Asn Gin Pro Lys Xaa 20 <210> 121 <211> 45 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (24) <223> Xaa equals any of the naturally occurring L-amino acids <220> <221> SITE <222> (26) <223> Xaa equals any of the naturally occurring L-amino acids <400> 121 Arg His Met His Thr Tyr Val Tyr Cys Gly Thr He His Asn Ser Lys 1 5 10 15 Asp Leu Glu Pro Thr Gin Met Xaa Asp Xaa He Lys Lys Met Trp His 20 25 30 Leu Tyr Thr Thr Lys Tyr Tyr Ala Ala He Lys Lys Asp 35 40 45 <210> 122 <211> 14 <212> PRT <213> Homo sapiens <400> 122 Arg Lys Cys Gly Thr Tyr He Pro Arg Asn Thr Met Gin Pro 1 5 10 66 <210> 123 <211> 40 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (9) <223> Xaa equals any of the naturally occurring L-amino acids <400> 123 Lys Arg Thr Glu Phe Met Ser Phe Xaa Gly Thr Trp Met Lys Leu Glu 1 5 10 15 Ala He He Leu Ser Lys Leu Thr Gin Glu Glu Lys Thr Lys His Leu 20 25 30 Met Phe Ser Leu He Ser Gly Ser 35 40 <210> 124 <211> 11 <212> PRT <213> Homo sapiens <400> 124 Pro Lys Ser Asp Thr Ser Pro Ala Ser Ser Arg 1 5 10 <210> 125 <211> 15 <212> PRT <213> Homo sapiens <400> 125 Pro Lys Ser Asp Thr Ser Pro Ala Ser Ser Arg Leu Cys Trp Asp 1 5 10 15 <210> 126 <211> 270 <212> PRT <213> Homo sapiens <400> 126 Tyr Val Pro Ser Phe Leu Pro Lys Ala Thr Gly Ser He Pro Ser Arg 1 5 10 15 Lys Gly Gly Val Gly Ser Glu Lys Pro Glu Val Pro Leu Gin Thr Tyr 20 25 30 Lys Glu He Val His Cys Cys Glu Glu Gin Val Leu Thr Leu Ala Thr 35 40 45 67 Glu Gin Thr Tyr Ala Val Glu Gly Glu Thr Pro He Asn Arg Leu Ser 50 55 60 Leu Leu Leu Ser Gly Arg Val Arg Val Ser Gin Asp Gly Gin Phe Leu 65 70 75 80 His Tyr He Phe Pro Tyr Gin Phe Met Asp Ser Pro Glu Trp Glu Ser 85 90 95 Leu Gin Pro Ser Glu Glu Gly Val Phe Gin Val Thr Leu Thr Ala Glu 100 105 110 Thr Ser Cys Ser Tyr He Ser Trp Pro Arg Lys Ser Leu His Leu Leu 115 120 125 Leu Thr Lys Glu Arg Tyr He Ser Cys Leu Phe Ser Ala Leu Leu Gly 130 135 140 Tyr Asp He Ser Glu Lys Leu Tyr Thr Leu Asn Asp Lys Leu Phe Ala 145 150 155 160 Lys Phe Gly Leu Arg Phe Asp He Arg Leu Pro Ser Leu Tyr His Val 165 170 175 Leu Gly Pro Thr Ala Ala Asp Ala Gly Pro Glu Ser Glu Lys Gly Asp 180 185 190 Glu Glu Val Cys Glu Pro Ala Val Ser Pro Pro Gin Ala Thr Pro Thr 195 200 205 Ser Leu Gin Gin Thr Pro Pro Cys Ser Thr Pro Pro Ala Thr Thr Asn 210 215 220 Phe Pro Ala Pro Pro Thr Arg Ala Arg Leu Ser Arg Pro Asp Ser Gly 225 230 235 240 He Leu Ala Ser Arg He Pro Leu Gin Ser Tyr Ser Gin Val He Ser 245 250 255 Arg Gly Gin Ala Pro Leu Ala Pro Thr His Thr Pro Glu Leu 260 265 270 <210> 127 <211> 21 <212> PRT <213> Homo sapiens <400> 127 Ala Thr Gly Ser He Pro Ser Arg Lys Gly Gly Val Gly Ser Glu Lys 1 5 10 15 Pro Glu Val Pro Leu 20 68 <210> 128 <211> 25 <212> PRT <213> Homo sapiens <400> 128 He Val His Cys Cys Glu Glu Gin Val Leu Thr Leu Ala Thr Glu Gin 1 5 10 15 Thr Tyr Ala Val Glu Gly Glu Thr Pro 20 25 <210> 129 <211> 23 <212> PRT <213> Homo sapiens <400> 129 Gin Asp Gly Gin Phe Leu His Tyr He Phe Pro Tyr Gin Phe Met Asp 1 5 10 15 Ser Pro Glu Trp Glu Ser Leu 20 <210> 130 <211> 23 <212> PRT <213> Homo sapiens <400> 130 Thr Leu Thr Ala Glu Thr Ser Cys Ser Tyr He Ser Trp Pro Arg Lys 1 5 10 15 Ser Leu His Leu Leu Leu Thr 20 <210> 131 <211> 25 <212> PRT <213> Homo sapiens <400> 131 Asp He Ser Glu Lys Leu Tyr Thr Leu Asn Asp Lys Leu Phe Ala Lys 1 5 10 15 Phe Gly Leu Arg Phe Asp He Arg Leu 20 25 <210> 132 69 <211> 26 <212> PRT <213> Homo sapiens <400> 132 Ser Leu Tyr His Val Leu Gly Pro Thr Ala Ala Asp Ala Gly Pro Glu 1 5 10 15 Ser Glu Lys Gly Asp Glu Glu Val Cys Glu 20 25 <210> 133 <211> 28 <212> PRT <213> Homo sapiens <400> 133 Thr Thr Asn Phe Pro Ala Pro Pro Thr Arg Ala Arg Leu Ser Arg Pro 1 5 10 15 Asp Ser Gly He Leu Ala Ser Arg He Pro Leu Gin 20 25 <210> 134 <211> 10 <212> PRT <213> Homo sapiens <400> 134 Tyr Phe Ser His Gly He Cys Ser His Ala 1 5 10 <210> 135 <211> 55 <212> PRT <213> Homo sapiens <400> 135 Asn Ser Glu Asp He Ser Gin Thr Arg Gin Glu Leu Gly Leu Cys He 1 5 10 15 Ser Gin Arg Cys Leu Ser Asp Arg Lys Lys Ser Arg Arg Ser Gly Val 20 25 30 Trp Val Arg Ala Cys Thr Met Gin Phe Met Lys His Val Phe Pro Arg 35 40 45 Leu He Ser Pro Arg Arg Pro 50 55 <210> 136 70 <211> 55 <212> PRT <213> Homo sapiens <400> 136 Pro Thr Arg His Phe Cys Gly Thr Ser Ser Cys Leu Thr Gly Thr Ala 1 5 10 15 Val Arg Cys Arg Ala Pro Ala Pro Val Trp Ser Val Arg Cys Pro His 20 25 30 Cys Phe Arg Ser Ser Asp Ala Trp Val Asp Pro Gly He Pro Asp Arg 35 40 45 Tyr Leu Gin Ala Tyr Leu Leu 50 55 <210> 137 <211> 246 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (8) <223> Xaa equals any of the naturally occurring L-amino acids <400> 137 Gly Glu Ala Met Asp Ala Glu Xaa Ala Val Ala Pro Pro Gly Cys Ser 1 5 10 15 His Leu Gly Ser Phe Lys Val Asp Asn Trp Lys Gin Asn Leu Arg Ala 20 25 30 He Tyr Gin Cys Phe Val Trp Ser Gly Thr Ala Glu Ala Arg Lys Arg 35 40 45 Lys Ala Lys Ser Cys He Cys His Val Cys Gly Val His Leu Asn Arg 50 55 60 Leu His Ser Cys Leu Tyr Cys Val Phe Phe Gly Cys Phe Thr Lys Lys 65 70 75 80 His He His Glu His Ala Lys Ala Lys Arg His Asn Leu Ala He Asp 85 90 95 Leu Met Tyr Gly Gly He Tyr Cys Phe Leu Cys Gin Asp Tyr He Tyr 100 105 110 Asp Lys Asp Met Glu He He Ala Lys Glu Glu Gin Arg Lys Ala Trp 115 120 125 Lys Met Gin Gly Val Gly Glu Lys Phe Ser Thr Trp Glu Pro Thr Lys 130 135 140 71 Arg Glu Leu Glu Leu Leu Lys His Asn Pro Lys Arg Arg Lys He Thr 145 150 155 160 Ser Asn Cys Thr He Gly Leu Arg Gly Leu He Asn Leu Gly Asn Thr 165 170 175 Cys Phe Met Asn Cys He Val Gin Ala Leu Thr His Thr Pro Leu Leu 180 185 190 Arg Asp Phe Phe Leu Ser Asp Arg His Arg Cys Glu Met Gin Ser Pro 195 200 205 Ser Ser Cys Leu Val Cys Glu Met Ser Ser Leu Phe Gin Glu Phe Gly 210 215 220 Arg Val Gly Arg Pro Gly Asn Ser Gly Pro Val Pro Ala Gly Val Pro 225 230 235 240 Ser He Val Ser Pro Glu 245 <210> 138 <211> 24 <212> PRT <213> Homo sapiens <400> 138 Val Ala Pro Pro Gly Cys Ser His Leu Gly Ser Phe Lys Val Asp Asn 1 5 10 15 Trp Lys Gin Asn Leu Arg Ala He 20 <210> 139 <211> 23 <212> PRT <213> Homo sapiens <400> 139 Thr Ala Glu Ala Arg Lys Arg Lys Ala Lys Ser Cys He Cys His Val 1 5 10 15 Cys Gly Val His Leu Asn Arg 20 <210> 140 <211> 23 <212> PRT <213> Homo sapiens <400> 140 72 Phe Thr Lys Lys His He His Glu His Ala Lys Ala Lys Arg His Asn 1 5 10 15 Leu Ala He Asp Leu Met Tyr 20 <210> 141 <211> 21 <212> PRT <213> Homo sapiens <400> 141 Tyr Asp Lys Asp Met Glu He He Ala Lys Glu Glu Gin Arg Lys Ala 1 5 10 15 Trp Lys Met Gin Gly 20 <210> 142 <211> 28 <212> PRT <213> Homo sapiens <400> 142 Glu Leu Leu Lys His Asn Pro Lys Arg Arg Lys He Thr Ser Asn Cys 1 5 10 15 Thr He Gly Leu Arg Gly Leu He Asn Leu Gly Asn 20 25 <210> 143 <211> 26 <212> PRT <213> Homo sapiens <400> 143 Gly Asn Thr Cys Phe Met Asn Cys He Val Gin Ala Leu Thr His Thr 1 5 10 15 Pro Leu Leu Arg Asp Phe Phe Leu Ser Asp 20 25 <210> 144 <211> 20 <212> PRT <213> Homo sapiens <400> 144 Glu Phe Gly Arg Val Gly Arg Pro Gly Asn Ser Gly Pro Val Pro Ala 1 5 10 15 73 Gly Val Pro Ser 20 <210> 145 <211> 7 <212> PRT <213> Homo sapiens <400> 145 Ala Phe Pro Trp Pro Thr Ser 1 5 <210> 146 <211> 23 <212> PRT <213> Homo sapiens <400> 146 Glu Ser Asn Phe Phe Tyr Pro Tyr Asp Ser Gin Leu Ala Leu Leu Ser 1 5 10 15 Ser Val Thr Cys Ser Ala Ser 20 <210> 147 <211> 83 <212> PRT <213> Homo sapiens <400> 147 Lys Leu Lys Met Phe Ala Phe Tyr Val Gin Val Leu Asn Gin Ser Lys 1 5 10 15 Ser He Phe Val Tyr Ser Arg Asn Leu He Phe Phe He His Met He 20 25 30 Val Ser Trp Pro Ser Phe Leu Gin Leu Pro Ala Val His Gin Cys His 35 40 45 Gin Ser Ser Val His He Cys Gly Val Ser Gly Leu Phe Pro Ser Ser 50 55 60 Asn Tyr Gin Cys Leu Ser Leu Cys Gin Asn His Thr Val Leu He He 65 70 75 80 Thr Thr Leu <210> 148 <211> 48 <212> PRT 74 <213> Homo sapiens <400> 148 Ser He Leu Asn Val He Pro Asn Leu Ser Lys Gin Ser Phe Glu Glu 1 5 10 15 Phe Asp Arg Leu He Leu Lys Tyr Met Gin Lys Ser Lys Ser Lys Arg 20 25 30 He Ala Lys He Leu Leu Ser Asn Lys Lys Thr Cys Pro Thr Lys Tyr 35 40 45 <210> 149 <211> 36 <212> PRT <213> Homo sapiens <400> 149 Leu Pro Gin He Leu Arg Trp Leu Lys Tyr His Gin Ser Val Trp Gly 1 5 10 15 Lys Gin Thr Pro Val Thr Leu His Tyr Leu Thr Leu Asp Leu He Gin 20 25 30 Glu Phe Thr Pro 35 <210> 150 <211> 33 <212> PRT <213> Homo sapiens <400> 150 He Phe Val Tyr Ser Arg Asn Leu He Phe Phe He His Met He Val 1 5 10 15 Ser Trp Pro Ser Phe Leu Gin Leu Pro Ala Val His Gin Cys His Gin 20 25 30 Ser <210> 151 <211> 184 <212> PRT <213> Homo sapiens <400> 151 Pro Thr Gly Asn Asp Leu Val Tyr Val Phe Pro Cys Leu Leu Ser Val 75 1 5 10 15 Phe Ser Arg Met Glu Glu Pro Ser Val Phe Cys Leu Phe Phe Pro Leu 20 25 30 Ser He Leu He Ser Ser Ala Ser Arg Thr Phe Pro Gly Thr Gin Gin 35 40 45 Val Phe Ser He Val His Gly Val Thr Asp Val Ser Ala Lys Lys Val 50 55 60 Gin Ser Gin Gly Arg Met Thr Ser Thr Gly Leu Asp Phe Asn Leu Leu 65 70 75 80 Pro Ala Trp Phe Pro Ser Pro Thr Ser Leu Gin Pro Thr Glu Asp Leu 85 90 95 Phe Gin Thr Gly Ser Leu Ser Arg Ser Phe Phe Cys Ser Lys Ala Phe 100 105 110 Ser Ser Ser Pro Leu Ser Pro Gly Gly Ser Pro Asn Ala Leu Thr Ser 115 120 125 Val Lys Glu His Leu Val Ser Pro Ala Phe Leu Ala Ser His Ser Cys 130 135 140 Thr Ala Glu Ser Phe Pro Arg Val Asp Val He His Ala Val Pro He 145 150 155 160 Ala Trp He Pro Ala Pro Leu His Pro He Gin Leu He Asn Ser Trp 165 170 175 Phe Phe Phe Phe Phe Phe Phe Phe 180 <210> 152 <211> 24 <212> PRT <213> Homo sapiens <400> 152 Asp Leu Val Tyr Val Phe Pro Cys Leu Leu Ser Val Phe Ser Arg Met 1 5 10 15 Glu Glu Pro Ser Val Phe Cys Leu 20 <210> 153 <211> 24 <212> PRT <213> Homo sapiens <400> 153 76 He Ser Ser Ala Ser Arg Thr Phe Pro Gly Thr Gin Gin Val Phe Ser 1 5 10 15 He Val His Gly Val Thr Asp Val 20 <210> 154 <211> 20 <212> PRT <213> Homo sapiens <400> 154 Phe Asn Leu Leu Pro Ala Trp Phe Pro Ser Pro Thr Ser Leu Gin Pro 1 5 10 15 Thr Glu Asp Leu 20 <210> 155 <211> 25 <212> PRT <213> Homo sapiens <400> 155 Phe Cys Ser Lys Ala Phe Ser Ser Ser Pro Leu Ser Pro Gly Gly Ser 1 5 10 15 Pro Asn Ala Leu Thr Ser Val Lys Glu 20 25 <210> 156 <211> 23 <212> PRT <213> Homo sapiens <400> 156 Thr Ala Glu Ser Phe Pro Arg Val Asp Val He His Ala Val Pro He 1 5 10 15 Ala Trp He Pro Ala Pro Leu 20 <210> 157 <211> 34 <212> PRT <213> Homo sapiens <400> 157 Phe Ser Phe Leu Lys Pro Leu Cys Ala Pro Arg Ala Pro Trp Leu Trp 1 5 10 15 77 Leu Pro Pro Ser Ser Lys Ser Arg Val His Val Gly Pro Gly Asp Phe 20 25 30 Arg Ser <210> 158 <211> 122 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (108) <223> Xaa equals any of the naturally occurring L-amino acids <400> 158 Val Cys Gly Thr Gly Gly Leu Glu Pro Asn Leu Ala Trp Val Arg Val 1 5 10 15 Asp Asn Gly Ser Phe Pro Ser Ser Ser Pro Ser Val Pro Leu Glu His 20 25 30 Pro Gly Cys Gly Cys Leu Leu His Pro Arg Ala Glu Ser Met Leu Gly 35 40 45 Gin Glu Thr Ser Asp Pro Cys Pro Gly Ala Ala Ser Gly Phe Val Phe 50 55 60 Pro Gin Trp Ala Gly Leu Gly Leu Leu Val His Leu Tyr Pro Ser Leu 65 70 75 80 Ser Tyr Ala Ala Leu Ala Cys Cys Val Ser Gly Leu Tyr Ser Leu Pro 85 90 95 Phe Thr Gin Ala Leu Gly Asn Gin Pro Ser Phe Xaa Gin Glu Arg Gin 100 105 110 Arg Arg Ser Met Pro Leu Leu Trp Ala Ser 115 120 <210> 159 <211> 8 <212> PRT <213> Homo sapiens <400> 159 His Ala Gly Arg Lys Thr Val Lys 1 5 <210> 160 <211> 61 78 <212> PRT <213> Homo sapiens <400> 160 Ser Phe Tyr Ala Lys Met Pro Met Glu Arg Lys Ala Leu Glu Met Val 1 5 10 15 Glu Lys Cys Leu Asp Lys Tyr Phe Gin His Leu Cys Asp Asp Leu Glu 20 25 30 Val Phe Ala Ala His Ala Gly Arg Lys Thr Val Lys Pro Glu Asp Leu 35 40 45 Glu Leu Leu Met Arg Arg Gin Gly Leu Val Thr Asp Gin 50 55 60 <210> 161 <211> 19 <212> PRT <213> Homo sapiens <400> 161 Pro Met Glu Arg Lys Ala Leu Glu Met Val Glu Lys Cys Leu Asp Lys 1 5 10 15 Tyr Phe Gin <210> 162 <211> 22 <212> PRT <213> Homo sapiens <400> 162 Glu Val Phe Ala Ala His Ala Gly Arg Lys Thr Val Lys Pro Glu Asp 1 5 10 15 Leu Glu Leu Leu Met Arg 20 <210> 163 <211> 31 <212> PRT <213> Homo sapiens <400> 163 Ser Phe Pro Ser Ser Ser Pro Ser Val Pro Leu Glu His Pro Gly Cys 1 5 10 15 Gly Cys Leu Leu His Pro Arg Ala Glu Ser Met Leu Gly Gin Glu 20 25 30 79 <210> 164 <211> 27 <212> PRT <213> Homo sapiens <400> 164 Tyr Pro Ser Leu Ser Tyr Ala Ala Leu Ala Cys Cys Val Ser Gly Leu 1 5 10 15 Tyr Ser Leu Pro Phe Thr Gin Ala Leu Gly Asn 20 25 <210> 165 <211> 27 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (18) <223> Xaa equals any of the naturally occurring L-amino acids <400>- 165 Ala Pro Gly Gly Val Asn Ser Glu Gly Arg Gly Gin His Leu Pro Pro 1 5 10 15 Pro Xaa Leu Ala Val Cys Leu Lys Leu His Leu 20 25 <210> 166 <211> 44 <212> PRT <213> Homo sapiens <400> 166 Asn Ser Ala Glu Pro Ala Trp Val Pro Val Cys Ala Arg Gly Gly Gly 1 5 10 15 Ala Gly Cys Gly Arg Arg Arg Gly Arg Arg Phe Cys Ala Ala Gly Ala 20 25 30 Val Pro Ala Ala Glu Arg Gly Gly Glu Asn Gly Ser 35 40 <210> 167 <211> 124 <212> PRT <213> Homo sapiens <400> 167 Ser Leu Val Pro Ala Leu Lys Glu Val Val Val Leu Trp Arg Arg Gin 80 1 5 10 15 Met Val Leu Tyr Leu Val Trp Ala Phe He Pro Glu Ser Trp Leu Asn 20 25 30 Ser Leu Gly Leu Thr Tyr Trp Pro Gin Lys Tyr Trp Ala Val Ala Leu 35 40 45 Pro Val Tyr Leu Leu He Ala He Val He Gly Tyr Val Leu Leu Phe 50 55 60 Gly He Asn Met Met Ser Thr Ser Pro Leu Asp Ser He His Thr He 65 70 75 80 Thr Asp Asn Tyr Ala Lys Asn Gin Gin Gin Lys Lys Tyr Gin Glu Glu 85 90 95 Ala He Pro Ala Leu Arg Asp He Ser He Ser Glu Val Asn Gin Met 100 105 110 Phe Phe Leu Ala Ala Lys Glu Leu Tyr Thr Lys Asn 115 120 <210> 168 <211> 28 <212> PRT <213> Homo sapiens <400> 168 Met Val Leu Tyr Leu Val Trp Ala Phe He Pro Glu Ser Trp Leu Asn 1 5 10 15 Ser Leu Gly Leu Thr Tyr Trp Pro Gin Lys Tyr Trp 20 25 <210> 169 <211> 25 <212> PRT <213> Homo sapiens <400> 169 Tyr Trp Ala Val Ala Leu Pro Val Tyr Leu Leu He Ala He Val He 1 5 10 15 Gly Tyr Val Leu Leu Phe Gly He Asn 20 25 <210> 170 <211> 22 <212> PRT <213> Homo sapiens 81 <400> 170 Gin Gin Gin Lys Lys Tyr Gin Glu Glu Ala He Pro Ala Leu Arg Asp 1 5 10 15 He Ser He Ser Glu Val 20 <210> 171 <211> 32 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (26) <223> Xaa equals any of the naturally occurring L-amino acids <400> 171 Leu Ser Pro Arg Leu Phe Asp Ala Gly He Leu Leu Trp Gly Ala Ser 1 5 10 15 Val Asn Val Thr He Trp Glu Val Arg Xaa Ala Gin Ser Ser Ala Ser 20 25 30 <210> 172 <211> 32 <212> PRT <213> Homo sapiens <400> 172 Asn Leu Thr Ser Asp Pro Arg Pro Leu Ala Leu Pro Pro Pro Cys Gly 1 5 10 15 Asp Phe He Lys Val Thr Ser Phe Ser Pro Gly Leu Glu Thr His Thr 20 25 30 <210> 173 <211> 135 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (14) <223> Xaa equals any of the naturally occurring L-amino acids 82 <400> 173 Glu Gin Gin Arg Leu Arg Asp Arg Glu Thr Gin Thr Gly Xaa Asp Ser 1 5 10 15 Arg Ala Lys Thr Gin Arg Gly Glu Asp Gly Glu Ser Glu Arg Gly Arg 20 25 30 Trp Arg Leu Arg Glu Gly Glu Asp Gly Asp Ser Glu Arg Glu Glu Asp 35 40 45 Gly Asp Ser Glu Arg Trp Arg Leu Arg Ser Met Glu Ser Gin Arg Gly 50 55 60 Glu Asp Gly His Ser Gly Gly Trp Arg Val Arg Arg Met Glu Thr His 65 70 75 80 Arg Lys Gly Arg Met Glu Ser Gin Glu Arg Leu Glu Thr Gly Glu Gly 85 90 95 He Glu Thr Gin Arg Gly Glu Asp Gly Asp Ser Glu Gly Gly Arg Trp 100 105 110 Arg Leu Lys Glu Asp Gly Asn Pro Gly Glu Arg Arg Thr Glu Met Arg 115 120 125 Gin Arg Leu Gly Glu Ala Gly 130 135 <210> 174 <211> 220 <212> PRT <213> Homo sapiens <220> <221> SITE <222> (7) <223> Xaa equals any of the naturally occurring L-amino acids <400> 174 Gly His Gly Val Ala Gly Xaa Cys Leu Pro Gin Pro Leu Leu Pro Pro 1 5 10 15 Ser Pro Pro Asp Tyr Asp Glu Arg Ser His Leu His Asp Thr Phe Thr 20 25 30 Gin Met Thr His Ala Leu Gin Glu Leu Ala Ala Ala Gin Gly Ser Phe 35 40 45 Glu Val Ala Phe Pro Asp Ala Ala Glu Lys Met Lys Lys Val Phe Thr 50 55 60 Gin Leu Lys Glu Ala Gin Ala Cys He Pro Pro Cys Glu Gly Leu Gin 65 70 75 80 83 Glu Phe Ala Arg Arg Phe Leu Cys Ser Gly Cys Tyr Ser Arg Val Cys 85 90 95 Asp Leu Pro Leu Asp Cys Pro Val Gin Asp Val Thr Val Thr Arg Gly 100 105 110 Asp Gin Ala Met Phe Ser Cys He Val Asn Phe Gin Leu Pro Lys Glu 115 120 125 Glu He Thr Tyr Ser Trp Lys Phe Ala Gly Gly Gly Leu Arg Thr Gin 130 135 140 Asp Leu Ser Tyr Phe Arg Asp Met Pro Arg Ala Glu Gly Tyr Leu Ala 145 150 155 160 Arg He Arg Pro Ala Gin Leu Thr His Arg Gly Thr Phe Ser Cys Val 165 170 175 He Lys Gin Asp Gin Arg Pro Leu Ala Arg Leu Tyr Phe Phe Leu Asn 180 185 190 Val Thr Gly Arg Pro Arg Gly Arg Arg Gin Ser Cys Arg Pro Arg Ser 195 200 205 Gly Lys Cys Cys Ala Gly Arg Arg Gly Met Pro Ser 210 215 220 <210> 175 <211> 41 <212> PRT <213> Homo sapiens <400> 175 Gly Asp His Pro His Phe He Ser Val Leu Gly Lys Val Gin Arg Glu 1 5 10 15 Gly Arg Arg Gly Pro Glu Gly Gin Ala Glu Gly Gin Thr Glu Arg Asn 20 25 30 Ser Gin Arg Arg Lys Ala Gin Arg Pro 35 40 <210> 176 <211> 13 <212> PRT <213> Homo sapiens <400> 176 Met Leu Val Tyr Gin Asn Gin Ala Gin Phe Ser Ser Asn 1 5 10

Inventors: BREWER LAURIE A, DUAN ROXANNE D, EBNER REINHARD, FLORENCE KIMBERLY, OLSEN HENRIK S, ROSEN CRAIG A, RUBEN STEVEN M, BREWER, LAURIE, A., DUAN, ROXANNE, D., EBNER, REINHARD, FLORENCE, KIMBERLY, OLSEN, HENRIK, S., ROSEN, CRAIG, A., RUBEN, STEVEN, M.
Applicants: BREWER LAURIE A, DUAN ROXANNE D, EBNER REINHARD, FLORENCE KIMBERLY, HUMAN GENOME SCIENCES INC, OLSEN HENRIK S, ROSEN CRAIG A, RUBEN STEVEN M, BREWER, LAURIE, A., DUAN, ROXANNE, D., EBNER, REINHARD, FLORENCE, KIMBERLY, HUMAN GENOME SCIENCES, INC., OLSEN, HENRIK, S., ROSEN, CRAIG, A., RUBEN, STEVEN, M.
Application year: 1999
Main classification: C07H21
IPC codes: A61K31, A61K38, A61K48, A61P7, A61P11, A61P15, A61P19, A61P25, A61P29, A61P37, C07H21, C07K14, C07K16, C12N1, C12N5, C12N15, G01N33