Patent Publication Number: US-2004053824-A1

Title: Extracellular matrix and cell adhesion molecules

Description:
TECHNICAL FIELD  
       [0001] This invention relates to nucleic acid and amino acid sequences of extracellular matrix and cell adhesion molecules and to the use of these sequences in the diagnosis, treatment, and prevention of genetic, immune/inflammatory, developmental, neurological, connective tissue, and cell proliferative disorders, including cancer and in the assessment of the effects of exogenous compounds on the expression of nucleic acid and amino acid sequences of extracellular matrix and cell adhesion molecules.  
       BACKGROUND OF THE INVENTION  
       Extracellular Matrix Proteins  
       [0002] The extracellular matrix (ECM) is a complex network of glycoproteins, polysaccharides, proteoglycans, and other macromolecules that are secreted from the cell into the extracellular space. The ECM remains in close association with the cell surface and provides a supportive meshwork that profoundly influences cell shape, motility, strength, flexibility, and adhesion. In fact, adhesion of a cell to its surrounding matrix is required for cell survival except in the case of metastatic tumor cells, which have overcome the need for cell-ECM anchorage. This phenomenon suggests that the ECM plays a critical role in the molecular mechanisms of growth control and metastasis. (Reviewed in Ruoslahti, E. (I 996) Sci. Am. 275:72-77.) Furthermore, the ECM determines the structure and physical properties of connective tissue and is particularly important for morphogenesis and other processes associated with embryonic development and pattern formation.  
       [0003] The collagens comprise a family of ECM proteins that provide structure to bone, teeth, skin, ligaments, tendons, cartilage, blood vessels, and basement membranes. Multiple collagen proteins have been identified. Three collagen molecules fold together in a triple helix stabilized by interchain disulfide bonds. Bundles of these triple helices then associate to form fibrils.  
       [0004] Elastin and related proteins confer elasticity to tissues such as skin, blood vessels, and lungs. Elastin is a highly hydrophobic protein of about 750 amino acids that is rich in proline and glycine residues. Elastin molecules are highly cross-linked, forming an extensive extracellular network of fibers and sheets. Elastin fibers are surrounded by a sheath of microfibrilins which are composed of a number of glycoproteins, including fibrillin.  
       [0005] Fibronectin is a large ECM glycoprotein found in all vertebrates. Fibronectin exists as a dimer of two subunits, each containing about 2,500 amino acids. Each subunit folds into a rod-like structure containing multiple domains. The domains each contain multiple repeated modules, the most common of which is the type III fibronectin repeat. The type III fibronectin repeat is about 90 amino acids in length and is also found in other ECM proteins and in some plasma membrane and cytoplasmic proteins. Furthermore, some type III fibronectin repeats contain a characteristic tripeptide consisting of Arginine-Glycine-Aspartic acid (RGD). The RGD sequence is recognized by the integrin family of cell surface receptors and is also found in other ECM proteins. (Reviewed in Alberts, et al. (1994)  Molecular Biology of the Cell,  Garland Publishing, New York, N.Y., pp. 986-987.)  
       [0006] Laminin is a major glycoprotein component of the basal lamina which underlies and supports epithelial cell sheets. Laminin is one of the first ECM proteins synthesized in the developing embryo. Laminin is an 850 kilodalton protein composed of three polypeptide chains joined in the shape of a cross by disulfide bonds. Laminin is especially important for angiogenesis and, in particular, for guiding the formation of capillaries. (Reviewed in Alberts, supra, pp. 990-991.)  
       [0007] Many proteinaceous ECM components are proteoglycans. Proteoglycans are composed of unibranched polysaccharide chains (glycosaminoglycans) attached to protein cores. Common proteoglycans include aggrecan, betaglycan, decorin, perlecan, serglycin, and syndecan-1. Some of these molecules not only provide mechanical support, but also bind to extracellular signaling molecules, such as fibroblast growth factor and transforming growth factor β, suggesting a role for proteoglycans in cell-cell communication. (Reviewed in Alberts, supra, pp. 973-978.)  
       [0008] Dentin phosphoryn (DPP) is a major component of the dentin ECM. DPP is a proteoglycan that is synthesized and expressed by odontoblasts (Gu, K., et al. (1998) Eur. J. Oral Sci. 106:1043-1047). DPP is believed to nucleate or modulate the formation of hydroxyapatite crystals.  
       [0009] Mucins are highly glycosylated glycoproteins that are the major structural component of the mucus gel. The physiological functions of mucins are cytoprotection, mechanical protection, maintenance of viscosity in secretions, and cellular recognition. MUC6 is a human gastric mucin that is also found in gall bladder, pancreas, seminal vesicles, and female reproductive tract (Toribara, N. W., et al. (1997) J. Biol. Chem. 272:16398-16403). The MUC6 gene has been mapped to human chromosome 11 (Toribara, N. W., et al. (1993) J. Biol. Chem. 268:5879-5885). Hemomucin is a novel Drosophila surface mucin that may be involved in the induction of antibacterial effector molecules (Theopold, U., et al. (1996) J. Biol. Chem. 217:12708-12715).  
       [0010] Olfactomedin was originally identified as the major component of the mucus layer surrounding the chemosensory dendrites of olfactory neurons. Olfactomedin-related proteins are secreted glycoproteins with conserved C-terminal motifs. The TIGR/myocilin protein, an olfactomedin-related protein expressed in the eye, is associated with the pathogenesis of glaucoma (Kulkarni, N. H. et al. (2000) Genet. Res. 76:41-50).  
       [0011] Ankyrin (ANK) repeats mediate protein-protein interactions associated with diverse intracellular functions. ANK repeats are composed of about 33 amino acids that form a helix-turn-helix core preceded by a protruding “tip.” These tips are of variable sequence and may play a role in protein-protein interactions. The helix-turn-helix region of the ANK repeats stack on top of one another and are stabilized by hydrophobic interactions (Yang, Y. et al. (I 998) Structure 6:619-626).  
       [0012] Sushi repeats, also called short consensus repeats (SCR), are found in a number of proteins that share the common feature of binding to other proteins. For example, in the C-terminal domain of versican, the sushi domain is important for heparin binding. Sushi domains contain basic amino acid residues, which may play a role in binding (Oleszewski, M. et al. (2000) J. Biol. Chem. 275:34478-34485).  
       [0013] Link, or X-link, modules are hyaluronan-binding domains found in proteins involved in the assembly of extracellular matrix, cell adhesion, and migration. The Link module superfamily includes CD44, cartilage link protein, and aggrecan. There is close similarity between the Link module and the C-type lectin domain, with the predicted hyaluronan-binding site at an analogous position to the carbohydrate-binding pocket in E-selectin (Kohda, D. et al. (1996) Cell, Vol. 86, 767-775).  
       [0014] Multidomain or mosaic proteins play an important role in the diverse functions of the extracellular matrix (Engel, J. et al. (1994) Development (Camb.) S35-42). ECM proteins are frequently characterized by the presence of one or more domains which may contain a number of potential intracellular disulfide bridge motifs. For example, domains which match the epidermal growth factor (EGF) tandem repeat consensus are present within several known extracellular proteins that promote cell growth, development, and cell signaling. This signature sequence is about forty amino acid residues in length and includes six conserved cysteine residues, and a calcium-binding site near the N-terminus of the signature sequence. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet. Subdomains between the conserved cysteines vary in length (Davis, C. G. New Biol (1990) May;2(5):410-9). Post-translational hydroxylation of aspartic acid or asparagine residues has been associated with EGF-like domains in several proteins (Prosite PDOC00010 Aspartic acid and asparagine hydroxylation site).  
       [0015] A number of proteins that contain calcium-binding EGF-like domain signature sequences are involved in growth and differentiation. Examples include bone morphogenic protein 1, which induces the formation of cartilage and bone; crumbs, which is a Drosophila epithelial development protein; Notch and a number of its homologs, which are involved in neural growth and differentiation, and transforming growth factor beta-1 binding protein (Expasy PROSITE document PDOC00913; Soler, C. and Carpenter, G., in Nicola, N. A. (1994)  The Cytokine Facts Book,  Oxford University Press, Oxford, UK, pp 193-197). EGF-like domains mediate protein-protein interactions for a variety of proteins. For example, EGF-like domains in the ECM glycoprotein fibulin-1 have been shown to mediate both self-association and binding to fibronectin (Tran, H. et al. (1997) J. Biol. Chem. 272:22600-22606). Point mutations in the EGF-like domains of ECM proteins have been identified as the cause of human disorders such as Marfan syndrome and pseudochondroplasia (Maurer, P. et al. (1996) Curr. Opin. Cell Biol. 8:609-617).  
       [0016] The CUB domain is an extracellular domain of approximately 110 amino acid residues found mostly in developmentally regulated proteins. The CUB domain contains four conserved cysteine residues and is predicted to have a structure similar to that of immunoglobulins. Vertebrate bone morphogenic protein 1, which induces cartilage and bone formation, and fibropellins I and III from sea urchin, which form the apical lamina component of the ECM, are examples of proteins that contain both CUB and EGF domains (PROSITE PDOC00908 CUB domain profile).  
       [0017] Other ECM proteins are members of the type A domain of von Willebrand factor (vWFA)-like module superfamily, a diverse group of proteins with a module sharing high sequence similarity. The vWFA-like module is found not only in plasma proteins but also in plasma membrane and ECM proteins (Colombatti, A. and Bonaldo, P. (1991) Blood 77:2305-2315). Crystal structure analysis of an integrin vWFA-like module shows a classic “Rossmann” fold and suggests a metal ion-dependent adhesion site for binding protein ligands (Lee, J.-O. et al. (1995) Cell 80:631-638). This family includes the protein matrilin-2, an extracellular matrix protein that is expressed in a broad range of mammalian tissues and organs. Matrilin-2 is thought to play a role in ECM assembly by bridging collagen fibrils and the aggrecan network (Deak, F. et al. (1997) J. Biol. Chem. 272:9268-9274).  
       [0018] The thrombospondins are multimeric, calcium-binding extracellular glycoproteins found widely in the embryonic extracellular matrix. These proteins are expressed in the developing nervous system or at specific sites in the adult nervous system after injury. Thrombospondins contain multiple EGF-type repeats, as well as a motif known as the thrombospondin type 1 repeat (TSR). The TSR is approximately 60 amino acids in length and contains six conserved cysteine residues. Motifs within TSR domains are involved in mediating cell adhesion through binding to proteoglycans and sulfated glycolipids. Thrombospondin-1 inhibits angiogenesis and modulates endothelial cell adhesion, motility, and growth. TSR domains are found in a diverse group of other proteins, most of which are expressed in the developing nervous system and have potential roles in the guidance of cell and growth cone migration Proteins that share TSRs include the F-spondin gene family, the semapholin 5 family, UNC-5, and SCO-spondin. The TSR superfamily includes the ADAMTS proteins which contain an ADAM (A Disintegin and Metalloproteinase) domain as well as one or more TSRS. The ADAMTS proteins have roles in regulating the turnover of cartilage, matrix, regulation of blood vessel garowth, and possibly development of the nervous system. (Reviewed in Adams, J. C. and Tucker, R. P. (2000) Dev. Dyn. 218:280-299).  
       [0019] Fibrinogen, the principle protein of vertebrate blood clotting, is a hexamer consisting of two sets of three different chains (alpha, beta, and gamma). The C-terminal domain of the beta and gamma chains comprises about 270 amino acid residues and contains four cysteines involved in two disulfide bonds. This domain has also been found in mammalian tenascin-X, an ECM protein that appears to be involved in cell adhesion (Pro site PDOC00445 Fibrinogen beta and gamma chains C-terminal domain signature).  
       Adhesion-Associated Proteins  
       [0020] The surface of a cell is rich in transmembrane proteoglycans, glycoproteins, glycolipids, and receptors. These macromolecules mediate adhesion with other cells and with components of the ECM. The interaction of the cell with its surroundings profoundly influences cell shape, strength, flexibility, motility, and adhesion. These dynamic properties are intimately associated with signal transduction pathways controlling cell proliferation and differentiation, tissue construction, and embryonic development. Families of cell adhesion molecules include the cadherins, integrins, lectins, neural cell adhesion proteins, and some members of the proline-rich proteins.  
       [0021] Cadherins comprise a family of calcium-dependent glycoproteins that function in mediating cell-cell adhesion in virtually all solid tissues of multicellular organisms. These proteins share multiple repeats of a cadherin-specific motif, and the repeats form the folding units of the cadherin extracellular domain. Cadherin molecules cooperate to form focal contacts, or adhesion plaques, between adjacent epithelial cells. The cadherin family includes the classical cadherins and protoeadherins. Classical cadherins include the E-cadherin, N-cadherin, and P-cadherin subfamilies. E-cadherin is present on many types of epithelial cells and is especially important for embryonic    
       [0022] Integrins are ubiquitous transmembrane adhesion molecules that link the ECM to the internal cytoskeleton. Integrins are composed of two noncovalently associated transmembrane glycoprotein subunits called α and β. Integrins function as receptors that play a role in signal transduction. For example, binding of integrin to its extracellular ligand may stimulate changes in intracellular calcium levels or protein kinase activity (Sjaastad, M. D. and Nelson, W. J. (1997) BioEssays 19:47-55). At least ten cell surface receptors of the integrin family recognize the ECM component fibronectin, which is involved in many different biological processes including cell migration and embryogenesis (Johansson, S. et al. (1997) Front. Biosci. 2:D126-D146).  
       [0023] Lectins comprise a ubiquitous family of extracellular glycoproteins which bind cell surface carbohydrates specifically and reversibly, resulting in the agglutination of cells (reviewed in Drickamer, K. and Taylor, M. E. (1993) Annu. Rev. Cell Biol. 9:237-264). This function is particularly important for activation of the immune response. Lectins mediate the agglutination and mitogenic stimulation of lymphocytes at sites of inflammation (Lasky, L. A. (1991) J. Cell. Biochem. 45:139-146; Paietta, E. et al. (1989) J. Immunol. 143:2850-2857).  
       [0024] Lectins are further classified into subfamilies based on carbohydrate-binding specificity and other criteria. The galectin subfamily, in particular, includes lectins that bind β-galactoside carbohydrate moieties in a thiol-dependent manner (reviewed in Hadari, Y. R. et al. (1998) J. Biol. Chem. 270:3447-3453). Galectins are widely expressed and developmentally regulated. Galectins contain a characteristic carbohydrate recognition domain (CRD). The CRD is about 140 amino acids and contains several stretches of about 1 - 10 amino acids which are highly conserved among all galectins. A particular 6-amino acid motif within the CRD contains conserved tryptophan and arginine residues which are critical for carbohydrate binding. The CRD of some galectins also contains cysteine residues which may be important for disulfide bond formation. Secondary structure predictions indicate that the CRD forms several β-sheets.  
       [0025] Galectins play a number of roles in diseases and conditions associated with cell-cell and cell-matrix interactions. For example, certain galectins associate with sites of inflammation and bind to cell surface immunoglobulin E molecules. In addition, galectins may play an important role in cancer metastasis. Galectin overexpression is correlated with the metastatic potential of cancers in humans and mice. Moreover, anti-galectin antibodies inhibit processes associated with cell transformation, such as cell aggregation and anchorage-independent growth (see, for example, Su, Z.-Z. et al. (1996) Proc. Natl. Acad. Sci. USA 93:7252-7257).  
       [0026] Selectins, or LEC-CAMs, comprise a specialized lectin subfamily involved primarily in inflammation and leukocyte adhesion (Reviewed in Lasky, supra). Selectins mediate the recruitment of leukocytes from the circulation to sites of acute inflammation and are expressed on the surface of vascular endothelial cells in response to cytokine signaling. Selectins bind to specific ligands on the leukocyte cell membrane and enable the leukocyte to adhere to and migrate along the endothelial surface. Binding of selectin to its ligand leads to polarized rearrangement of the actin cytoskeleton and stimulates signal transduction within the leukocyte (Breiner, B. et al. (1997) Biochem. Biophys. Res. Commun. 231:802-807; Hidati, K. I. et al. (1997) J. Biol. Chem. 272:28750-28756). Members of the selectin family possess three characteristic motifs: a lectin or carbohydrate recognition domain; an epidermal growth factor-like domain; and a variable number of short consensus repeats (scr or “sushi” repeats) which are also present in complement regulatory proteins.  
       [0027] Neural cell adhesion proteins (NCAPs) play roles in the establishment of neural networks during development and regeneration of the nervous system (Uyemura et al. (1996) Essays Biochem. 31:37-48; Blummendorf and Rathjen (1996) Curr. Opin. Neurobiol. 6:584-593). NCAP participates in neuronal cell migration, cell adhesion, neurite outgrowth, axonal fasciculation, pathfinding, synaptic target-recognition. synaptic formation, myelination and regeneration. NCAPs are expressed on the surfaces of neurons associated with learning and memory. Mutations in genes encoding NCAPS are linked with neurological diseases, including hereditary neuropathy Charcot-Marie-Tooth disease, Dejerine-Sottas disease, X-linked hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait and adducted thumbs), and spastic paraplegia type I. In some cases, expression of NCAP is not restricted to the nervous system. L1, for example, is expressed in melanoma cells and hematopoiatic tumor cells where it is implicated in cell spreading and migration, and may play a role in tumor progression (Montgomery et al. (1996) J. Cell Biol. 132:475-485).  
       [0028] NCAPs have at least one immunoglobulin constant or variable domain (Uyemura et al., supra). They are generally linked to the plasma membrane through a transmembrane domain and/or a glycosyl-phosphatidylinositol (GPI) anchor. The GPI linkage can be cleaved by GPI phospholipase C. Most NCAPs consist of an extracellular region made up of one or more immunoglobulin domains, a membrane spanning domain, and an intracellular region. Many NCAPs contain post-translational modifications including covalently attached oligosaccharide, glucuronic acid, and sulfate. NCAPs fall into three subgroups: simple-type, complex-type, and mixed-type. Simple-type NCAPs contain one or more variable or constant immunoglobulin domains, but lack other types of domains. Members of the simple-type subgroup include Schwann cell myclin protein (SMP), limbic system-associated membrane protein (LAMP), opiate-binding cell-adhesion molecule (OBCAM), and myelin-associated glycoprotein (MAG). The complex-type NCAPs contain fibronectin type III domains in addition to the immunoglobulin domains. The complex-type subgroup includes neural cell-adhesion molecule (NCAM), axonin-1, F11, Bravo, and L1. Mixed-type NCAPs contain a combination of immunoglobulin domains and other motifs such as tyrosine kinase and epidermal growth factor-like domains. This subgroup includes Trk receptors of nerve growth factors such as nerve growth factor (NGF) and neurotropin 4 (NT4), Neu differentiation factors such as glial growth factor II (GGFUI) and acctylcholinc receptor-inducing factor (ARIA), and the semaphorin/collapsin family such as semaphorin B and collapsin.  
       [0029] Semaphorins are a large group of axonal guidance molecules consisting of at least 30 different members and are found in vertebrates, invertebrates, and even certain viruses. All semaphorins contain the soma domain which is approximately 500 amino acids in length. Neuropilin, a semaphorin receptor has been shown to promote neurite outgrowth in vitro. The extracellular region of neuropilins consists of three different domains: CUB, discoidin, and MAM domains. The CUB and the MAM motifs of neuropilin have been suggested as having roles in protein-protein interactions and are suggested to be involved in the binding of semaphorins through the sema and the C-terminal domains (reviewed in Raper, J. A. (2000) Curr. Opin. Neurobiol. 10:88-94).  
       [0030] An NCAP subfamily, the NCAP-LON subgroup, includes cell adhesion proteins expressed on distinct subpopulations of brain neurons. Members of the NCAP-LON subgroup possess three immunoglobulin domains and bind to cell membranes through GPI anchors. Kilon (a kindred of NCAP-LON), for example, is expressed in the brain cerebral cortex and hippocampus (Funatsu et al. (1999) J. Biol. Chem. 274:8224-8230). Immunostaining localizes Kilon to the dendrites and soma of pyramidal neurons. Kilon has three C2 type immunoglobulin-like domains, six predicted glycosylation sites, and a GPI anchor. Expression of Kilon is developmentally regulated. It is expressed at higher levels in adult brain in comparison to embryonic and early postnatal brains. Confocal microscopy shows the presence of Kilon in dendrites of hypothalamic magnocellular neurons secreting neuropeptides, oxytocin or arginine vasopressin (Miyata et al. (2000) J. Comp. Neurol. 424:74-85). Arginine vasopressin regulates body fluid homeostasis, extracellular osmolarity and intravascular volume. Oxytocin induces contractions of uterine smooth muscle during child birth and of myoepithelial cells in mammary glands during lactation. In magnocellular neurons, Kilon is proposed to play roles in the reorganization of dendritic connections during neuropeptide secretion.  
       [0031] Cell adhesion proteins also include some members of the proline-rich proteins (PRPs). PRPs are defined by a high frequency of proline, ranging from 20-50% of the total amuino acid content. Some PRPs have short domains which are rich in proline. These proline-rich regions are associated with protein-protein interactions. One family of PRPs are the proline-rich synapse-associated proteins (ProSAPs) which have been shown to bind to members of the postsynaptic density (PSD) protein family and subtypes of the somatostatin receptor (Yao, I. et al. (1999) J. Biol. Chem. 274: 27463-27466; Zitzer, H. et al. (1999) J. Biol. Chem. 274:32997-33001). Members of ProSAP contain at the N-terminus six to seven ankyrin repeats, followed by an SH3 domain, a PDZ domain, then by seven proline-rich regions and a SAM domain at the C terminus. Several groups of ProSAP are important structural constituents of synaptic structures in human brain (Ziter et al., supra). Another member of PRP is the HLA-B-associated transcript 2 protein (BAT2) which is rich in proline and include short tracts of polyproline, polyglycine, and charged amino acids. BAT2 also contains four RGD (Arg-Gly-Asp) motifs typical of integrins (Bancrji, J. et al. (1990) Proc. Natl. Acad. Sci. USA 87:2374-2378).  
       [0032] There are additional specific domains characteristic of cell adhesion proteins. One such domain is the MAM domain, a domain of about 170 amino acids found in the extracellular region of diverse proteins. These proteins all share a receptor-like architecture comprising a signal peptide, followed by a large N-terminal extracellular domain, a transmembrane region, and an intracellular domain. (PROSITE document PDOC00604 MAM domain signature and profile). MAM domain proteins include zonadhesin, a sperm-specific membrane protein that binds to the zona pellucida of the egg; neuropilin, a cell adhesion molecule that functions during the formation of certain neuronal circuits, and  Xenonus laevis  thyroid hormone induced protein B, which contains four MAM domains and is involved in metamorphosis (Brown, D. D. et al. (1996) Proc. Natl. Acad. Sci. USA 93:1924-1929).  
       [0033] The WSC domain was originally found in the yeast WSC (cell-wall integrity and stress response component) proteins which act as sensors of environmental stress. The WSC domains are extracellular and are thought to possess a carbohydrate binding role (Ponting, C. P. et al. (1999) Curr. Biol. 9:S1-S2). A WSC domain has recently been identified in polycystin-1, a human plasma membrane protein. Mutations in polycystin-1 are the cause of the commonest form of autosonial dominant polycystic kidney disease (Ponting, C. P. et al. (1999) Curr. Biol. 9:R585-R588).  
       [0034] Toposome is a cell-adhesion glycoprotein isolated from mesenchyme-blastula embryos. Toposome precursors including vitellogenin promote cell adhesion of dissociated blastula cells.  
       [0035] Leucine rich repeats (LRR) are short motifs found in numerous proteins from a wide range of species. LRR motifs are of variable length, most commonly 20-29 amino acids and multiple repeats are typically present in tandem. LRR is important for protein/protein interactions and cell adhesion, and LRR proteins are involved in cell/cell interactions, morphogenesis, and development (Kobe, B. and Deisenhofer, J. (1 995) Curr. Opin. Struct. Biol. 5:409-416). The human ISLR (immunoglobulin superfamnily containing leucine-rich repeat) protein contains a C2-type immunoglobulin domain as well as LRR. The ISLR gene is linked to the critical region for Bardet-Biedl syndrome, a developmental disorder of which the most common feature is retinal dystrophy (Nagasawa, A. et al. (1999) Genomics 61:37-43).  
       [0036] The sterile alpha motif (SAM) domain is a conserved protein binding domain, approximately 70 amino acids in length, and is involved in the regulation of many developmental processes in many eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to form homo- or hetero-oligomers with other SAM domains (Schultz, J. et al. (1997) Protein Sci. 6:249-253).  
       [0037] The discovery of new extracellular matrix and cell adhesion molecules and the polynucleotides encoding them satisfies a need in the art by providing new compositions which are useful in the diagnosis, prevention, and treatment of genetic, immune/inflammatory, developmental, neurological, connective tissue, and cell proliferative disorders, including cancer, and in the assessment of the effects of exogenous compounds on the expression of nucleic acid and amino acid sequences of extracellular matrix and cell adhesion molecules.  
       SUMMARY OF THE INVENTION  
       [0038] The invention features purified polypeptides, extracellular matrix and cell adhesion molecules, referred to collectively as “ECMCAD” and individually as “ECMCAD-1,” “ECMCAD-2,” “ECMCAD-3,” “ECMCAD-4,” “ECMCAD-5,” “ECMCAD-6,” “ECMCAD-7,” “ECMCAD-8,” “ECMCAD-9,” “ECMCAD-10,” “ECMCAD-11,” “ECMCAD-12,” “ECMCAD-13,” “ECMCAD-14,” “ECMCAD-15,” “ECMCAD-16,” “ECMCAD-17,” “ECMCAD-18,” “ECMCAD-19,” “ECMCAD-20,” “ECMCAD-21,” “ECMCAD-22,” “ECMCAD-23,” “ECMCAD-24,” “ECMCAD-25,” “ECMCAD-26,” “ECMCAD-27,” “ECMCAD-28,” “ECMCAD-29,” “ECMCAD-30,” “ECMCAD-31,” “ECMCAD-32,” “ECMCAD-33,” “ECMCAD-34,” “ECMCAD-35,” and “ECMCAD-36.” In one aspect, the invention provides an isolated polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. In one alternative, the invention provides an isolated polypeptide comprising the amino acid sequence of SEQ ID NO:1-36.  
       [0039] The invention further provides an isolated polynucleotide encoding a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. In one alternative, the polynucleotide encodes a polypeptide selected from the group consisting of SEQ ID NO:1-36. In another alternative, the polynucleotide is selected from the group consisting of SEQ ID NO:37-72.  
       [0040] Additionally, the invention provides a recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide encoding a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. In one alternative, the invention provides a cell transformed with the recombinant polynucleotide. In another alternative, the invention provides a transgenic organism comprising the recombinant polynucleotide.  
       [0041] The invention also provides a method for producing a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The method comprises a) culturing a cell under conditions suitable for expression of the polypeptide, wherein said cell is transformed with a recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide encoding the polypeptide, and b) recovering the polypeptide so expressed.  
       [0042] Additionally, the invention provides an isolated antibody which specifically binds to a polypeptide selected from ide group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36.  
       [0043] The invention further provides an isolated polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected forms the group consisting of SEQ ID NO:37-72, b) a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d). In one alternative, the polynucleotide comprises at least 60 contiguous nucleotides.  
       [0044] Additionally, the invention provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID, NO:37-72, b) a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and c) an RNA equivalent of a)-d). The method comprises a) hybridizing the sample with a probe comprising at least 20 contiguous nucleotides comprising a sequence complementary to said target polynucleotide in the sample, and which probe specifically hybridizes to said target polynucleotide, under conditions whereby a hybridization complex is formed between said probe and said target polynucleotide or fragments thereof, and b) detecting the presence or absence of said hybridization complex, and optionally, if present, the amount thereof. In one alternative, the probe comprises at least 60 contiguous nucleotides.  
       [0045] The invention further provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, b) a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d). The method comprises a) amplifying said target polynucleotide or fragment thereof using polymerase chain reaction amplification, and b) detecting the presence or absence of said amplified target polynucleotide or fragment thereof, and, optionally, if present, the amount thereof.  
       [0046] The invention further provides a composition comprising an effective amount of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1 -36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO: 1 -36, and a pharmaceutically acceptable excipient. In one embodiment, the composition comprises an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The invention additionally provides a method of treating a disease or condition associated with decreased expression of functional ECMCAD, comprising administering to a patient in need of such treatment the composition.  
       [0047] The invention also provides a method for screening a compound for effectiveness as an agonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1 -36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting agonist activity in the sample. In one alternative, the invention provides a composition comprising an agonist compound identified by the method and a pharmaceutically acceptable excipient. In another alternative, the invention provides a method of treating a disease or condition associated with decreased expression of functional ECMCAD, comprising administering to a patient in need of such treatment the composition.  
       [0048] Additionally, the invention provides a method for screening a compound for effectiveness as an antagonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting antagonist activity in the sample. In one alternative, the invention provides a composition comprising an antagonist compound identified by the method and a pharmaceutically acceptable excipient. In another alternative, the invention provides a method of treating a disease or condition associated with overexpression of functional ECMCAD, comprising administering to a patient in need of such treatment the composition.  
       [0049] The invention further provides a method of screening for a compound that specifically binds to a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the, group consisting of SEQ ID NO: 1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The method comprises a) combining the polypeptide with at least one test compound under suitable conditions, and b) detecting binding of the polypeptide to the test compound, thereby identifying a compound that specifically binds to the polypeptide.  
       [0050] The invention further provides a method of screening for a compound that modulates the activity of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1-36, b) a naturally occurring polypeptide comprising an amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:1-36. The method comprises a) combining the polypeptide with at least one test compound under conditions permissive for the activity of the polypeptide, b) assessing the activity of the polypeptide in the presence of the test compound, and c) comparing the activity of the polypeptide in the presence of the test compound with the activity of the polypeptide in the absence of the test compound, wherein a change in the activity of the polypeptide in the presence of the test compound is indicative of a compound that modulates the activity of the polypeptide.  
       [0051] The invention further provides a method for screening a compound for effectiveness in altering expression of a target polynucleotide, wherein said target polynucleotide comprises a sequence selected from the group consisting of SEQ ID NO:37-72, the method comprising a) exposing a sample comprising the target polynucleotide to a compound, and b) detecting altered expression of the target polynucleotide.  
       [0052] The invention further provides a method for assessing toxicity of a test compound, said method comprising a) treating a biological sample containing nucleic acids with the test compound; b) hybridizing the nucleic acids of the treated biological sample with a probe comprising at least 20 contiguous nucleotides of a polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, ii) a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, iii) a polynucleotide having a sequence complementary to i), iv) a polynucleotide complementary to the polynucleotide of ii), and v) an RNA equivalent of i)-iv). Hybridization occurs under conditions whereby a specific hybridization complex is formed between said probe and a target polynucleotide in the biological sample, said target polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, ii) a naturally occurring polynucleotide comprising a polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NO:37-72, iii) a polynucleotide complementary to the polynucleotide of i), iv) a polynucleotide complementary to the polynucleotide of ii), and v) an RNA equivalent of i)-iv). Alternatively, the target polynucleotide comprises a fragment of a polynucleotide sequence selected from the group consisting of i)-v) above; c) quantifying the amount of hybridization complex; and d) comparing the amount of hybridization complex in the treated biological sample with the amount of hybridization complex in an untreated biological sample, wherein a difference in the amount of hybridization complex in the treated biological sample is indicative of toxicity of the test compound.  
       BRIEF DESCRIPTION OF THE TABLES  
       [0053] Table 1 summarizes the nomenclature for the full length polynucleotide and polypeptide sequences of the present invention.  
       [0054] Table 2 shows the GenBank identification number and annotation of the nearest GenBank homolog for polypeptides of the invention. The probability score for the match between each polypeptide and its GenBank homolog is also shown.  
       [0055] Table 3 shows structural features of polypeptide sequences of the invention, including predicted motifs and domains, along with the methods, algorithms, and searchable databases used for analysis of the polypeptides.  
       [0056] Table 4 lists the cDNA and/or genomic DNA fragments which were used to assemble polynucleotide sequences of the invention, along with selected fragments of the polynucleotide sequences.  
       [0057] Table 5 shows the representative cDNA library for polynucleotides of the invention.  
       [0058] Table 6 provides an appendix which describes the tissues and vectors used for construction of the cDNA libraries shown in Table 5.  
       [0059] Table 7 shows the tools, programs, and algorithims used to analyze the polynucleotides and polypeptides of the invention, along with applicable descriptions, references, and threshold parameters.  
       DESCRIPTION OF THE INVENTION  
       [0060] Before the present proteins, nucleotide sequences, and methods are described, it is understood that this invention is not limited to the particular machines, materials and methods described, as these may vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention which will be limited only by the appended claims.  
       [0061] It must be noted that as used herein and in the appended claims, the singular forms “a,” “an,” and “the” include plural reference unless the context clearly dictates otherwise. Thus, for example, a reference to “a host cell” includes a plurality of such host cells, and a reference to “an antibody” is a reference to one or more antibodies and equivalents thereof known to those skilled in the art, and so forth.  
       [0062] Unless defined otherwise, all technical and scientific terms used herein have the same meanings as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any machines, materials, and methods similar or equivalent to those described herein can be used to practice or test the present invention, the preferred machines, materials and methods are now described. All publications mentioned herein are cited for the purpose of describing and disclosing the cell lines, protocols, reagents and vectors which are reported in the publications and which might be used in connection with the invention. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.  
       DEFINITIONS  
       [0063] “ECMCAD” refers to the amino acid sequences of substantially purified ECMCAD obtained from any species, particularly a mammalian species, including bovine, ovine, porcine, murine, equine, and human, and from any source, whether natural, synthetic, semi-synthetic, or recombinant.  
       [0064] The term “agonist” refers to a molecule which intensifies or mimics the biological activity of ECMCAD. Agonists may include proteins, nucleic acids, carbohydrates, small molecules, or any other compound or composition which modulates the activity of ECMCAD either by directly interacting with ECMCAD or by acting oil components of the biological pathway in which ECMCAD participates.  
       [0065] An “allelic variant” is an alternative form of the gene encoding ECMCAD. Allelic variants may result from at least one mutation in the nucleic acid sequence and may result in altered mRNAs or in polypeptidcs whose structure or function may or may not be altered. A gene may have none, one, or many allelic variants of its naturally occurring form. Common mutational changes which give rise to allelic variants are generally ascribed to natural deletions, additions, or substitutions of nucleotides. Each of these types of changes may occur alone, or in combination with the others, one or more times in a given sequence.  
       [0066] “Altered” nucleic acid sequences encoding ECMCAD include those sequences with deletions, insertions, or substitutions of different nucleotides, resulting in a polypeptide the same as ECMCAD or a polypeptide with at least one functional characteristic of ECMCAD. Included within this definition are polymorphisms which may or may not be readily detectable using a particular oligonucleotide probe of the polynucleotide encoding ECMCAD, and improper or unexpected hybridization to allelic variants, with a locus other than the normal chromosomal locus for the polynucleotide sequence encoding ECMCAD. The encoded protein may also be “altered,” and may contain deletions, insertions, or substitutions of amino acid residues which produce a silent change and result in a functionally equivalent ECMCAD. Deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues, as long as the biological or immunological activity of ECMCAD is retained. For example, negatively charged amino acids may include aspailtic acid and glutamic acid, and positively charged amino acids may include lysine and arginine. Amino acids with uncharged polar side chains having similar hydrophilicity values may include: asparagine and glutamine; and serine and threonine. Amino acids with uncharged side chains having similar hydrophilicity values may include: leucine, isoleucine, and valine; glycine and alanine; and phenylalanine and tyrosine.  
       [0067] The terms “amino acid” and “amino acid sequence” refer to an oligopeptide, peptide, polypeptide, or protein sequence, or a fragment of any of these, and to naturally occurring or synthetic molecules. Where “amino acid sequence” is recited to refer to a sequence of a naturally occurring protein molecule, “amino acid sequence” and like terms are not meant to limit the amino acid sequence to the complete native amino acid sequence associated with the recited protein molecule.  
       [0068] “Amplification” relates to the production of additional copies of a nucleic acid sequence. Amplification is generally carried out using polymerase chain reaction (PCR) technologies well known in the art.  
       [0069] The term “antagonist” refers to a molecule which inhibits or attenuates the biological activity of ECMCAD. Antagonists may include proteins such as antibodies, nucleic acids, carbohydrates, small molecules, or any other compound or composition which modulates the activity of ECMCAD either by directly interacting with ECMCAD or by acting on components of the biological pathway in which ECMCAD participates.  
       [0070] The term “antibody” refers to intact immunoglobulin molecules as well as to fragments thereof, such as Fab, F(ab′) 2 , and Fv fragments, which are capable of binding an epitopic determinant. Antibodies that bind ECMCAD polypeptides can be prepared using intact polypeptides or using fragments containing small peptides of interest as the immunizing antigen. The polypeptide or oligopeptide used to immunize an animal (e.g., a mouse, a rat, or a rabbit) can be derived from the translation of RNA, or synthesized chemically, and can be conjugated to a carrier protein if desired. Commonly used carriers that are chemically coupled to peptides include bovine serum albumin, thyroglobulin, and keyhole limpet hemocyanin (KLH). The coupled peptide is then used to immunize the animal.  
       [0071] The term “antigenic determinant” refers to that region of a molecule (i.e., an epilope) that makes contact with a particular antibody. When a protein or a fragment of a protein is used to immunize a host animal, numerous regions of the protein may induce the production of antibodies which bind specifically to antigenic determinants (particular regions or three-dimensional structures on the protein). An antigenic determinant may compete with the intact antigen (i.e., the immunogen used to elicit the immune response) for binding to an antibody.  
       [0072] The term “antisense” refers to any composition capable of base-pairing with the “sense” (coding) strand of a specific nucleic acid sequence. Antisense compositions may include DNA; RNA; peptide nucleic acid (PNA); oligonucleotides having modified backbone linkages such as phosphorothioates, methylphosphonates, or benzylphosphonates; oligonucleotides having modified sugar groups such as 2′-methoxyethyl sugars or 2′-methoxyethoxy sugars; or oligonucleotides having modified bases such as 5-methyl cytosine, 2′-deoxyuracil, or 7-deaza-2′-deoxyguanosine. Antisense molecules may be produced by any method including chemical synthesis or transcription. Once introduced into a cell, the complementary antisense molecule base-pairs with a naturally occurring nucleic acid sequence produced by the cell to form duplexes which block either transcription or translation. The designation “negative” or “minus” can refer to the antisense strand, and the designation “positive” or “plus” can refer to the sense strand of a reference DNA molecule.  
       [0073] The term “biologically active” refers to a protein having structural, regulatory, or biochemical functions of a naturally occurring molecule. Likewise, “immunologically active” or “immunogenic” refers to the capability of the natural, recombinant, or synthetic ECMCAD, or of any oligopeptide thereof, to induce a specific immune response in appropriate animals or cells and to bind with specific antibodies.  
       [0074] “Complementary” describes the relationship between two single-stranded nucleic acid sequences that anneal by base-pairing. For example, 5′-AGT-3′ pairs with its complement, 3′-TCA-5′.  
       [0075] A “composition comprising a given polynucleotide sequence” and a “composition comprising a given amino acid sequence” refer broadly to any composition containing the given polynucleotide or amino acid sequence. The composition may comprise a dry formulation or an aqueous solution. Compositions comprising polynucleotide sequences encoding ECMCAD or fragments of ECMCAD may be employed as hybridization probes. The probes may be stored in freeze-dried form and may be associated with a stabilizing agent such as a carbohydrate. In hybridizations, the probe may be deployed in an aqueous solution containing salts (e.g., NaCl), detergents (e.g., sodium dodecyl sulfate; SDS), and other components (e.g., Denhardt&#39;s solution, dry milk, salmon sperm DNA, etc.).  
       [0076] “Consensus sequence” refers to a nucleic acid sequence which has been subjected to repeated DNA sequence analysis to resolve uncalled bases, extended using the XL-PCR kit (Applied Biosystems, Foster City Calif.) in the 5′ and/or the 3′ direction, and resequenced, or which has been assembled from one or more overlapping cDNA, EST, or genomic DNA fragments using a computer program for fragment assembly, such as the GELVIEW fragment assembly system (GCG, Madison Wis.) or Phrap (University of Washington, Seattle Wash.). Some sequences have been both extended and assembled to produce the consensus sequence.  
       [0077] “Conservative amino acid substitutions” are those substitutions that are predicted to least interfere with the properties of the original protein, i.e., the structure and especially the function of the protein is conserved and not significantly changed by such substitutions. The table below shows amino acids which may be substituted for an original amino acid in a protein and which are regarded as conservative amino acid substitutions.  
                                                   Original Residue   Conservative Substitution                          Ala   Gly, Ser           Arg   His, Lys           Asn   Asp, Gln, His           Asp   Asn, Glu           Cys   Ala, Ser           Gln   Asn, Glu, His           Glu   Asp, Gln, His           Gly   Ala           His   Asn, Arg, Gln, Glu           Ile   Leu, Val           Leu   Ile, Val           Lys   Arg, Gln, Glu           Met   Leu, Ile           Phe   His, Met, Leu, Trp, Tyr           Ser   Cys, Thr           Thr   Ser, Val           Trp   Phe, Tyr           Tyr   His, Phe, Trp           Val   Ile, Leu, Thr                      
 
       [0078] Conservative amino acid substitutions generally maintain (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a beta sheet or alpha helical conformation, (b) the charge or hydrophobicity of the molecule at the site of the substitution, and/or (c) the bulk of the side chain.  
       [0079] A “deletion” refers to a change in the amino acid or nucleotide sequence that results in the absence of one or more amino acid residues or nucleotides.  
       [0080] The term “derivative” refers to a chemically modified polynucleotide or polypeptide. Chemical modifications of a polynucleotide can include, for example, replacement of hydrogen by an alkyl, acyl, hydroxyl, or amino group. A derivative polynucleotide encodes a polypeptide which retains at least one biological or immunological function of the natural molecule. A derivative polypeptide is one modified by glycosylation, pegylation, or any similar process that retains at least one biological or immunological function of the polypeptide from which it was derived.  
       [0081] A “detectable label” refers to a reporter molecule or enzyme that is capable of generating a measurable signal and is covalently or noncovalently joined to a polynucleotide or polypeptide.  
       [0082] “Differential expression” refers to increased or upregulated; or decreased, downregulated, or absent gene or protein expression, determined by comparing at least two different samples. Such comparisons may be carried out between, for example, a treated and an untreated sample, or a diseased and a normal sample.  
       [0083] A “fragment” is a unique portion of ECMCAD or the polynucleotide encoding ECMCAD which is identical in sequence to but shorter in length than the parent sequence. A fragment may comprise up to the entire length of the defined sequence, minus one nucleotide/amino acid residue. For example, a fragment may comprise from 5 to 1000 continuous nucleotides or amino acid residues. A fragment used as a probe, primer, antigen, therapeutic molecule, or for other purposes, may be at least 5, 10, 15, 16, 20, 25, 30, 40, 50, 60, 75, 100, 150, 250 or at least 500 contiguous nucleotides or amino acid residues in length. Fragments may be preferentially selected from certain regions of a molecule. For example, a polypeptide fragment may comprise a certain length of contiguous amino acids selected from the first 250 or 500 amino acids (or first 25% or 50%) of a polypeptide as shown in a certain defined sequence. Clearly these lengths are exemplary, and any length that is supported by the specification, including the Sequence Listing, tables, and figures, may be encompassed by the present embodiments.  
       [0084] A fragment of SEQ ID NO:37-72 comprises a region of unique polynucleotide sequence that specifically identifies SEQ ID NO :37-72, for example, as distinct from any other sequence in the genome from which the fragment was obtained. A fragment of SEQ ID NO:37-72 is useful, for example, in hybridization and amplification technologies and in analogous methods that distinguish SEQ ID NO:37-72 from related polynucleotide sequences. The precise length of a fragment of SEQ ID NO:37-72 and the region of SEQ ID NO:37-72 to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.  
       [0085] A fragment of SEQ ID NO:1-36 is encoded by a fragment of SEQ ID NO:37-72. A fragment of SEQ ID NO:1-36 comprises a region of unique amino acid sequence that specifically identifies SEQ ID NO:1-36. For example, a fragment of SEQ ID NO:1-36 is useful as an immunogenic peptide for the development of antibodies that specifically recognize SEQ ID NO :1-36. The precise length of a fragment of SEQ ID NO:1-36 and the region of SEQ ID NO:1-36 to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.  
       [0086] A “full length” polynucleotide sequence is one containing at least a translation initiation codon (e.g., methionine) followed by an open reading frame and a translation termination codon. A “full length” polynucleotide sequence encodes a “full length” polypeptide sequence.  
       [0087] “Homology” refers to sequence similarity or, interchangeably, sequence identity, between two or more polynucleotide sequences or two or more polypeptide sequences.  
       [0088] The terms “percent identity” and “% identity,” as applied to polynucleotide sequences, refer to the percentage of residue matches between at least two polynucleotide sequences aligned using a standardized algorithm. Such an algorithm may insert, in a standardized and reproducible way, gaps in the sequences being compared in order to optimize alignment between two sequences, and therefore achieve a more meaningful comparison of the two sequences.  
       [0089] Percent identity between polynucleotide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program. This program is part of the LASERGENE software package, a suite of molecular biological analysis programs (DNASTAR, Madison Wis.). CLUSTAL V is described in Higgins, D. G. and P. M. Sharp (1989) CABIOS 5:151-153 and in Higgins, D. G. et al. (1992) CABIOS 8:189-191. For pairwise alignments of polynucleotide sequences, the default parameters are set as follows: Ktuple=2, gap penalty=5, window=4, and “diagonals saved”=4. The “weighied” residue weight table is selected as the default. Percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polynucleotide sequences.  
       [0090] Alternatively, a suite of commonly used and freely available sequence comparison algorithms is provided by the National Center for Biotechnology Information (NCBI) Basic Local Alignment Search Tool (BLAST) (Altschul, S. F. et al. (1990) J. Mol. Biol. 215:403-410), which is available from several sources, including the NCBI, Bethesda, Md., and on the Internet at http://www.ncbi.nlm.nih.gov/BLAST/. The BLAST software suite includes various sequence analysis programs including “blastn,” that is used to align a known polynucleotide sequence with other polynucleotide sequences from a variety of databases. Also available is a tool called “BLAST 2 Sequences” that is used for direct pairwise comparison of two nucleotide sequences. “BLAST 2 Sequences” can be accessed and used interactively at http://www.ncbi.nlm.nih.gov/gorf/bl2.html. The “BLAST 2 Sequences” tool can be used for both blastn and blastp (discussed below). BLAST programs are commonly used with gap and other parameters set to default settings. For example, to compare two nucleotide sequences, one may use blastn with the “BLAST 2 Sequences” tool Version 2.0.12 (Apr. 21, 2000) set at default parameters. Such default parameters may be, for example:  
       [0091] Matrix: BLOSUM62  
       [0092] Reward for match: 1  
       [0093] Penalty for mismatch: −2  
       [0094] Open Gap: 5 and Extension Gap: 2 penalties  
       [0095] Gap x drop-off: 50  
       [0096] Expect: 10  
       [0097] Word Size: 11  
       [0098] Filter: on  
       [0099] Percent identity may be measured over the length of an entire defined sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined sequence, for instance, a fragment of at least 20, at least 30, at least 40, at least 50, at least 70, at least 100, or at least 200 contiguous nucleotides. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in the tables, figures, or Sequence Listing, may be used to describe a length over which percentage identity may be measured.  
       [0100] Nucleic acid sequences that do not show a high degree of identity may nevertheless encode similar amino acid sequences due to the degeneracy of the genetic code. It is understood that changes in a nucleic acid sequence can be made using this degeneracy to produce multiple nucleic acid sequences that all encode substantially the same protein.  
       [0101] The phrases “percent identity” and “% identity,” as applied to polypeptide sequences, refer to the percentage of residue matches between at least two polypeptide sequences aligned using a standardized algorithm. Methods of polypeptide sequence alignment are well-known. Some alignment methods take into account conservative amino acid substitutions. Such conservative substitutions, explained in more detail above, generally preserve the charge and hydrophobicity at the site of substitution, thus preserving the structure (and therefore function) of the polypeptide.  
       [0102] Percent identity between polypeptide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program (described and referenced above). For pairwise alignments of polypeptide sequences using CLUSTAL V, the default parameters are set as follows: Ktuple=1, gap penalty=3, window=5, and “diagonals saved”=5. The PAM250 matrix is selected as the default residue weight table. As with polynucleotide alignments, the percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polypeptide sequence pairs.  
       [0103] Alternatively the NCBI BLAST software suite may be used. For example, for a pairwise comparison of two polypeptide sequences, one may use the “BLAST 2 Sequences” tool Version 2.0.12 (Apr. 21, 2000) with blastp set at default parameters. Such default parameters may be, for example:  
       [0104] Matrix: BLOSUM62  
       [0105] Open Gap: 11 and Extension Gap: 1 penalties  
       [0106] Gap x drop-off: 50  
       [0107] Expect: 10  
       [0108] Word Size: 3  
       [0109] Filter: on  
       [0110] Percent identity may be measured over the length of an entire defined polypeptide sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined polypeptide sequence, for instance, a fragment of at least 15, at least 20, at least 30, at least 40, at least 50, at least 70 or at least 150 contiguous residues. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in the tables, figures or Sequence Listing, may be used to describe a length over which percentage identity may be measured.  
       [0111] “Human artificial chromosomes” (HACs) are linear microchromosomes which may contain DNA sequences of about 6 kb to 10 Mb in size and which contain all of the elements required for chromosome replication, segregation and maintenance.  
       [0112] The term “humanized antibody” refers to an antibody molecule in which the amino acid sequence in the non-antigen binding regions has been altered so that the antibody more closely resembles a human antibody, and still retains its original binding ability.  
       [0113] “Hybridization” refers to the process by which a polynucleotide strand anneals with a complementary strand through base pairing under defined hybridization conditions. Specific hybridization is an indication that two nucleic acid sequences share a high degree of complementarity. Specific hybridization complexes form under permissive annealing conditions and remain hybridized after the “washing” step(s). The washing step(s) is particularly important in determining the stringency of the hybridization process, with more stringent conditions allowing less non-specific binding, i.e., binding between pairs of nucleic acid strands that are not perfectly matched. Permissive conditions for annealing of nucleic acid sequences are routinely determinable by one of ordinary skill in the art and may be consistent among hybridization experiments, whereas wash conditions may be varied among experiments to achieve the desired stringency, and therefore hybridization specificity. Permissive annealing conditions occur, for example, at 68° C. in the presence of about 6×SSC, about 1% (w/v) SDS, and about 100 μg/ml sheared, denatured salmon sperm DNA.  
       [0114] Generally, stringency of hybridization is expressed, in part, with reference to the temperature under which the wash step is carried out. Such wash temperatures are typically selected to be about 5° C. to 20° C. lower than the thermal melting point (T m ) for the specific sequence at a defined ionic strength and pH. The T m  is the temperature (under defined ionic strength and pH) at which 50% of the target sequence hybridizes to a perfectly matched probe. An equation for calculating T m  and conditions for nucleic acid hybridization are well known and can be found in Sambrook, J. et al. (1989)  Molecular Cloning: A Laboratory Manual,  2 nd  ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; specifically see volume 2, chapter 9.  
       [0115] High stringency conditions for hybridization between polynucleotides of the present invention include wash conditions of 68° C. in the presence of about 0.2×SSC and about 0.1% SDS, for 1 hour. Alternatively, temperatures of about 65° C., 60° C., 55° C., or 42° C. may be used. SSC concentration may be varied from about 0.1 to 2×SSC, with SDS being present at about 0.1%. Typically, blocking reagents are used to block non-specific hybridization. Such blocking reagents include, for instance, sheared and denatured salmon sperm DNA at about 100-200 μg/ml. Organic solvent, such as formaride at a concentration of about 35-50% v/v, may also be used under particular circumstances, such as for RNA:DNA hybridizations. Useful variations on these wash conditions will be readily apparent to those of ordinary skill in the art. Hybridization, particularly under high stringency conditions, may be suggestive of evolutionary similarity between the nucleotides. Such similarity is strongly indicative of a similar role for the nucleotides and their encoded potypeptides.  
       [0116] The term “hybridization complex” refers to a complex formed between two nucleic acid sequences by virtue of the formation of hydrogen bonds between complementary bases. A hybridization complex may be formed in solution (e.g., C 0 t or R 0 t analysis) or formed between one nucleic acid sequence present in solution and another nucleic acid sequence immobilized on a solid support (e.g., paper, membranes, filters, chips, pins or glass slides, or any other appropriate substrate to which cells or their nucleic acids have been fixed).  
       [0117] The words “insertion” and “addition” refer to changes in an amino acid or nucleotide sequence resulting in the addition of one or more amino acid residues or nucleotides, respectively.  
       [0118] “Immune response” can refer to conditions associated with inflammation, trauma, immune disorders, or infectious or genetic disease, etc. These conditions can be characterized by expression of various factors, e.g., cytokines, chemokines, and other signaling molecules, which may affect cellular and systemic defense systems.  
       [0119] An “immunogenic fragment” is a polypeptide or oligopeptide fragment of ECMCAD which is capable of eliciting an immune response when introduced into a living organism, for example, a mammal. The term “immunogenic fragment” also includes any polypeptide or oligopeptide fragment of ECMCAD which is useful in any of the antibody production methods disclosed herein or known in the art.  
       [0120] The term “microarray” refers to an arrangement of a plurality of polynucleotides, polypeptides, or other chemical compounds on a substrate.  
       [0121] The terms “element” and “array element” refer to a polynucleotide, polypeptide, or other chemical compound having a unique and defined position on a microarray.  
       [0122] The term “modulate” refers to a change in the activity of ECMCAD. For example, modulation may cause an increase or a decrease in protein activity, binding characteristics, or any other biological, functional, or immunological properties of ECMCAD.  
       [0123] The phrases “nucleic acid” and “nucleic acid sequence” refer to a nucleotide, oligonucleotide, polynucleotide, or any fragment thereof. These phrases also refer to DNA or RNA of genomic or synthetic origin which may be single-stranded or double-stranded and may represent the sense or the antisense strand, to peptide nucleic acid (PNA), or to any DNA-like or RNA-like material.  
       [0124] “Operably linked” refers to the situation in which a first nucleic acid sequence is placed in a functional relationship with a second nucleic acid sequence. For instance, a promoter is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence. Operably linked DNA sequences may be in close proximity or contiguous and, where necessary to join two protein coding regions in the same reading frame.  
       [0125] “Peptide nucleic acid” (PNA) refers to an antisense molecule or anti-gene agent which comprises an oligonucleotide of at least about 5 nucleotides in length linked to a peptide backbone of amino acid residues ending in lysine. The terminal lysine confers solubility to the composition. PNAs preferentially bind complementary single stranded DNA or RNA and stop transcript elongation, and may be pegylated to extend their lifespan in the cell.  
       [0126] “Post-translational modification” of an ECMCAD may involve lipidation, glycosylation, phosphorylation, acetylation, racemization, proteolytic cleavage, and other modifications known in the art. These processes may occur synthetically or biochemically. Biochemical modifications will vary by cell type depending on the enzymatic milieu of ECMCAD.  
       [0127] “Probe” refers to nucleic acid sequences encoding ECMCAD, their complements, or fragments thereof, which are used to detect identical, allelic or related nucleic acid sequences. Probes are isolated oligonucleotides or polynucleotides attached to a detectable label or reporter molecule. Typical labels include radioactive isotopes, ligands, chemiluminescent agents, and enzymes. “Primers” are short nucleic acids, usually DNA oligonucleotides, which may be annealed to a target polynucleotide by complementary base-pairing. The primer may then be extended along the target DNA strand by a DNA polymerase enzyme. Primer pairs can be used for amplification (and identification) of a nucleic acid sequence, e.g., by the polymerase chain reaction (PCR). Probes and primers as used in the present invention typically comprise at least 15 contiguous nucleotides of a known sequence. In order to enhance specificity, longer probes and primers may also be employed, such as probes and primers that comprise at least 20, 25, 30, 40, 50, 60, 70, 80, 90, 100, or at least 150 consecutive nucleotides of the disclosed nucleic acid sequences. Probes and primers may be considerably longer than these examples, and it is understood that any length supported by the specification, including the tables, figures, and Sequence Listing, may be used.  
       [0128] Methods for preparing and using probes and primers are described in the references, for example Sambrook, J. et al. (1989)  Molecular Cloning: A Laboratory Manual,  2 nd  ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; Ausubel, F. M. et al. (1987)  Current Protocols in Molecular Biolog,  Greene Publ. Assoc. &amp; Wiley-Intersciences, New York N.Y.; Innis, M. et al. (1990)  PCR Protocols, A Guide to Methods and Applications,  Academic Press, San Diego Calif. PCR primer pairs can be derived from a known sequence, for example, by using computer programs intended for that purpose such as Primer (Version 0.5, 1991, Whitehead Institute for Biomedical Research, Cambridge Mass.).  
       [0129] Oligonucleotides for use as primers are selected using software known in the art for such purpose. For example, OLIGO 4.06 software is useful for the selection of PCR primer pairs of up to 100 nucleotides each, and for the analysis of oligonucleotides and larger polynucleotides of up to 5,000 nucleotides from an input polynucleotide sequence of up to 32 kilobases. Similar primer selection programs have incorporated additional features for expanded capabilities. For example, the PrimOU primer selection program (available to the public from the Genome Center at University of Texas South West Medical Center, Dallas Tex.) is capable of choosing specific primers from megabase sequences and is thus useful for designing primers on a genome-wide scope. The Primer3 primer selection program (available to the public from the Whitehead Institute/MIT Center for Genonie Research, Cambridge Mass.) allows the user to input a “mispriming library,” in which sequences to avoid as primer binding sites are user-specified. Primer3 is useful, in particular, for the selection of oligonucleotides for microarrays. (The source code for the latter two primer selection programs may also be obtained from their respective sources and modified to meet the user&#39;s specific needs.) The PrimeGen program (available to the public from the UK Human Genome Mapping Project Resource Centre, Cambridge UK) designs primers based on multiple sequence alignments, thereby allowing selection of primers that hybridize to either the most conserved or least conserved regions of aligned nucleic acid sequences. Hence, this program is useful for identification of both unique and conserved oligonucleotides and polynucleotide fragments. The oligonucleotides and polynucleotide fragments identified by any of the above selection methods are useful in hybridization technologies, for example, as PCR or sequencing primers, microarray elements, or specific probes to identify fully or partially complementary polynucleotides in a sample of nucleic acids. Methods of oligonucleotide selection are not limited to those described above.  
       [0130] A “recombinant nucleic acid” is a sequence that is not naturally occurring or has a sequence that is made by an artificial combination of two or more otherwise separated segments of sequence. This artificial combination is often accomplished by chemical synthesis or, more commonly, by the artificial manipulation of isolated segments of nucleic acids, e.g., by genetic engineering techniques such as those described in Sambrook, supra. The term recombinant includes nucleic acids that have been altered solely by addition, substitution, or deletion of a portion of the nucleic acid. Frequently, a recombinant nucleic acid may include a nucleic acid sequence operably linked to a promoter sequence. Such a recombinant nucleic acid may be part of a vector that is used, for example, to transform a cell.  
       [0131] Alternatively, such recombinant nucleic acids may be part of a viral vector, e.g., based on a vaccinia virus, that could be use to vaccinate a mammal wherein the recombinant nucleic acid is expressed, inducing a protective immunological response in the mammal.  
       [0132] A “regulatory element” refers to a nucleic acid sequence usually derived from untranslated regions of a gene and includes enhancers, promoters, introns, and 5′ and 3′ untranslated regions (UTRs). Regulatory elements interact with host or viral proteins which control transcription, translation, or RNA stability.  
       [0133] “Reporter molecules” are chemical or biochemical moieties used for labeling a nucleic acid, amino acid, or antibody. Reporter molecules include radionuclides; enzymes; fluorescent, chemiluminescent, or chromogenic agents; substrates; cofactors; inhibitors; magnetic particles; and other moieties known in the art.  
       [0134] An “RNA equivalent,” in reference to a DNA sequence, is composed of the same linear sequence of nucleotides as the reference DNA sequence with the exception that all occurrences of the nitrogenous base thymine are replaced with uracil, and the sugar backbone is composed of ribose instead of deoxyribose.  
       [0135] The term “sample” is used in its broadest sense. A sample suspected of containing ECMCAD, nucleic acids encoding ECMCAD, or fragments thereof may comprise a bodily fluid; an extract from a cell, chromosome, organelle, or membrane isolated from a cell; a cell; genomic DNA, RNA, or cDNA, in solution or bound to a substrate; a tissue; a tissue print; etc.  
       [0136] The terms “specific binding” and “specifically binding” refer to that interaction between a protein or peptide and an agonist, an antibody, an antagonist, a small molecule, or any natural or synthetic binding composition. The interaction is dependent upon the presence of a particular structure of the protein, e.g., the antigenic determinant or epitope, recognized by the binding molecule. For example, if an antibody is specific for epitope “A,” the presence of a polypeptide comprising the epitope A, or the presence of free unlabeled A, in a reaction containing free labeled A and the antibody will reduce the amount of labeled A that binds to the antibody.  
       [0137] The term “substantially purified” refers to nucleic acid or amino acid sequences that are removed from their natural environment and are isolated or separated, and are at least 60% free, preferably at least 75% free, and most preferably at least 90% free from other components with which they are naturally associated.  
       [0138] A “substitution” refers to the replacement of one or more amino acid residues or nucleotides by different amino acid residues or nucleotides, respectively.  
       [0139] “Substrate” refers to any suitable rigid or semi-rigid support including membranes, filters, chips, slides, wafers, fibers, magnetic or nonmagnetic beads, gels, tubing, plates, polymers, microparticles and capillaries. The substrate can have a variety of surface forms, such as wells, trenches, pins, channels and pores, to which polynucleotides or polypeptides are bound.  
       [0140] A “transcript image” refers to the collective pattern of gene expression by a particular cell type or tissue under given conditions at a given time.  
       [0141] “Transformation” describes a process by which exogenous DNA is introduced into a recipient cell. Transformation may occur under natural or artificial conditions according to various methods well known in the art, and may rely on any known method for the insertion of foreign nucleic acid sequences into a prokaryotic or eukaryotic host cell. The method for transformation is selected based on the type of host cell being transformed and may include, but is not limited to, bacteriophage or viral infection, electroporation, heat shock, lipofection, and particle bombardment. The term “transformed cells” includes stably transformed cells in which the inserted DNA is capable of replication either as an autonomously replicating plasmid or as part of the host chromosome, as well as transiently transformed cells which express the inserted DNA or RNA for limited periods of time.  
       [0142] A “transgenic organism,” as used herein, is any organism. including but not limited to animals and plants, in which one or more of the cells of the organism contains heterologous nucleic acid introduced by way of human intervention, such as by transgenic techniques well known in the art. The nucleic acid is introduced into the cell, directly or indirectly by introduction into a precursor of the cell, by way of deliberate genetic manipulation, such as by microinjection or by infection with a recombinant virus. The term genetic manipulation does not include classical cross-breeding, or in vitro fertilization, but rather is directed to the introduction of a recombinant DNA molecule. The transgenic organisms contemplated in accordance with the present invention include bacteria, cyanobacteria, fungi, plants and animals. The isolated DNA of the present invention can be introduced into the host by methods known in the art for example infection, transfection, transformation or transconjugation. Techniques for transferring the DNA of the present invention into such organisms are widely known and provided in references such as Sambrook et al. (1989), supra.  
       [0143] A “variant” of a particular nucleic acid sequence is defined as a nucleic acid sequence having at least 40% sequence identity to the particular nucleic acid sequence over a certain length of one of the nucleic acid sequences using blastn with the “BLAST 2 Sequences” tool Version 2.0.9 (May 7, 1999) set at default parameters. Such a pair of nucleic acids may show, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length. A variant may be described as, for example, an “allelic” (as defined above), “splice,” “species,” or “polymorphic” variant. A splice variant may have significant identity to a reference molecule, but will generally have a greater or lesser number of polynucleotides due to alternative splicing of exons during mRNA processing. The corresponding polypeptide may possess additional functional domains or lack domains that are present in the reference molecule. Species variants arc polynucleotide sequences that vary from one species to another. The resulting polypeptides will generally have significant amino acid identity relative to each other. A polymorphic variant is a variation in the polynucleotide sequence of a particular gene between individuals of a given species. Polymorphic variants also may encompass “single nucleotide polymorphisms” (SNPs) in which the polynucleotide sequence varies by one nucleotide base. The presence of SNPs may be indicative of, for example, a certain population, a disease state, or a propensity for a disease state.  
       [0144] A “variant” of a particular polypeptide sequence is defined as a polypeptide sequence having at least 40% sequence identity to the particular polypeptidc sequence over a certain length of one of the polypeptide sequences using blastp with the “BLAST 2 Sequences” tool Version 2.0.9 (May 7, 1999) set at default parameters. Such a pair of polypeptides may show, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length of one of the polypeptides.  
       THE INVENTION  
       [0145] The invention is based on the discovery of new human extracellular matrix and cell adhesion molecules (ECMCAD), the polynucleotides encoding ECMCAD, and the use of these compositions for the diagnosis, treatment, or prevention of genetic, immune/inflammatory, developmental, neurological, connective tissue, and cell proliferative disorders, including cancer.  
       [0146] Table 1 summarizes the nomenclatrre for the full length polynucleotide and polypeptide sequences of the invention. Each polynucleotide and its corresponding polypeptide are correlated to a single Incyte project identification number (Incyte Project ID). Each polypeptide sequence is denoted by both a polypeptide sequence identification number (Polypeptide SEQ ID NO:) and an Incyte polypeptide sequence number (Incyte Polypeptide ID) as shown. Each polynucleotide sequence is denoted by both a polynucleotide sequence identification number (Polynucleotide SEQ ID NO:) and an Incyte polynucleotide consensus sequence number (Incyte Polynucleotide ID) as shown.  
       [0147] Table 2 shows sequences with homology to the polypeptides of the invention as identified by BLAST analysis against the GenBank protein (genpept) database. Columns 1 and 2 show the polypeptide sequence identification number (Polypeptide SEQ ID NO:) and the corresponding Incyte polypeptide sequence number (Incyte Polypeptide ID) for polypeptides of the invention. Column 3 shows the GenBank identification number (Genbank ID NO:) of the nearest GenBank homolog. Column 4 shows the probability score for the match between each polypeptide and its GenBank homolog. Column 5 shows the annotation of the GenBank homolog along with relevant citations where applicable, all of which are expressly incorporated by reference herein.  
       [0148] Table 3 shows various structural features of the polypeptides of the invention. Columns 1 and 2 show the polypeptide sequence identification number (SEQ ID NO:) and the corresponding Incyte polypeptide sequence number (Incyte Polypeptide ID) for each polypeptide of the invention. Column 3 shows the number of amino acid residues in each polypeptide. Column 4 shows potential phosphorylation sites, and column 5 shows potential glycosylation sites, as determined by the MOTIFS program of the GCG sequence analysis software package (Genetics Computer Group, Madison Wis.). Column 6 shows amino acid residues comprising signature sequences, domains, and motifs. Column 7 shows analytical methods for protein structure/function analysis and in some cases, searchable databases to which the analytical methods were applied.  
       [0149] Together, Tables 2 and 3 summarize the properties of polypeptides of the invention, and these properties establish that the claimed polypeptides are extracellular matrix and cell adhesion molecules. For example, SEQ ID NO:2 is 48% identical over 46% of its length to mouse procollagen type I alpha chain, (GenBank ID g192264) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 6.9e-46, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:2 also contains a collagen triple helix repeat, as determined by searching for statistically significant matches in the PFAM database. (See Table 3.) HMMER and SPSCAN analyses indicate the presence of a signal peptide at the N-terminus of SEQ ID NO:2. Data from BLAST analysis of the PRODOM and DOMO databases, as well as MOTIFS analysis, provide further corroborative evidence that SEQ ID NO:2 is a cellular matrix protein associated with cell adhesion. In an alternative example, SEQ ID NO:6 is 64% identical to frog MAM domain protein (GenBank ID g1234793) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 4.2e-254, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:6 also contains four MAM domains as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from MOTIFS analysis provide further corroborative evidence that SEQ ID NO:6 is a MAM domain cell adhesion protein. In an alternative example, SEQ ID NO:10 is 80% identical to murine semaphorin B (GenBank ID g854326) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 6.0e-66, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:10 also contains a soma domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) The BLAST and HMMER analyses provide evidence that SEQ ID NO:10 is a semaphorin. SEQ ID NO:12 is 44% identical to human cadherin superfamily protein VR4-11 (GenBank ID g9622240) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 9.9e-170, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:12 also contains a cadherin domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, MOTIFS, and PROFLES CAN analyses provide further corroborative evidence that SEQ ID NO: 12 is a cadherin. SEQ ID NO: 14 is 91% identical to mutin neuronal glycoprotein (GenBank ID g200057) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 0.0, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance, SEQ ID NO: 14 also contains fibronectin type III and immunoglobulin domains as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) The BLAST and HMMER analyses provide evidence that SEQ ID NO:14 is a cell adhesion molecule. In an alternative example, SEQ ID NO:22 is 79% identical to mouse lamidn 5 alpha chain (GenBank ID g2599232) as determined by the Basic Local Alignment Search Tool (BLAST), (See Table 2.) The BLAST probability score is 0.0, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:22 also contains a laminin N-terminal domain, multiple laminin EGF-like domains, a laminin B domain, and laminin G domains, as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, and MOTIFS analyses provide further corroborative evidence that SEQ ID NO:22 is a laminin. In an alternative example, SEQ ID NO:24 is 89% identical to Bos taurus brevican (GenBank ID g452821) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 0.0, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:24 also contains a lectin C-type domain, an extracellular link domain, an EGF-fike domain, a sushi domain, and an immunoglobulin domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, MOTIFS, and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO:24 is a c-type lectin. In an alternative example, SEQ ID NO:31 is 87% identical lo a mouse semaphorin homolog (GenBank ID g1110599) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 0.0, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:31 also contains a Sema domain and a plexin repeat as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLAST analyses against the DOMO and PRODOM databases provide further corroborative evidence that SEQ ID NO:31 is a semaphorin. In an alternative example, SEQ ID NO:35 is 61% identical to murine C-type lectin (GenBank ID g4159801) as determined by the Basic local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 2.9e-75, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO:35 also contains a lectin C-type domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO:35 is a lectin. SEQ ID NO:1, SEQ ID NO:3-5, SEQ ID NO:7-9, SEQ ID NO:11, SEQ ID NO: 13, SEQ ID NO:15-21, SEQ ID NO:23, SEQ ID NO:25-30, SEQ ID NO:32-34 and SEQ ID NO:36 were analyzed and annotated in a similar manner. The algorithims and parameters for the analysis of SEQ ID NO:1-36 are described in Table 7.  
       [0150] As shown in Table 4, the full length polynucleotide sequences of the present invention were assembled using cDNA sequences or coding (exon) sequences derived from genomic DNA, or any combination of these two types of sequences. Columns 1 and 2 list the polynucleotide sequence identification number (Polynucleotide SEQ ID NO:) and the corresponding Incyte polynucleotide consensus sequence number (Incyte Polynucleotide ID) for each polynucleotide of the invention. Column 3 shows the length of each polynucleotide sequence in basepairs. Column 4 lists fragments of the polynucleotide sequences which are useful, for example, in hybridization or amplification technologies that identify SEQ ID NO:37-72 or that distinguish between SEQ ID NO:37-72 and related polynucleotide sequences. Column 5 shows identification numbers corresponding to cDNA sequences, coding sequences (exons) predicted from genomic DNA, and/or sequence assemblages comprised of both cDNA and genomic DNA. These sequences were used to assemble the full length polynucleotide sequences of the invention. Columns 6 and 7 of Table 4 show the nucleotide start (5′) and stop (3′) positions of the cDNA and/or genomic sequences in column 5 relative to their respective full length sequences.  
       [0151] The identification numbers in Column 5 of Table 4 may refer specifically, for example, to Incyte cDNAs along with their corresponding cDNA libraries. For example, 7347284H1 is the identification number of an Incyte cDNA sequence, and LUNLTUE01 is the cDNA library from which it is derived. Incyte cDNAs for which cDNA libraries are not indicated were derived from pooled cDNA libraries (e.g., 71699406V1). Alternatively, the identification numbers in column 5 may refer to GenBank cDNAs or ESTs (e.g., g1242437) which contributed to the assembly of the full length polynucleotide sequences. Alternatively, the identification numbers in column 5 may refer to coding regions predicted by Genscan analysis of genomic DNA. For example, GNN.g7923864 — 002 is the identification number of a Genscan-predicted coding sequence, with g7923864 being the GenBank identification number of the sequence to which Genscan was applied. The Genscan-predicted coding sequences may have been edited prior to assembly. (See Example IV.) Alternatively, the identification numbers in column 5 may refer to assemblages of both cDNA and Genscan-predicted exons brought together by an “exon stitching” algorithm. (See Example V.) Alternatively, the identification numbers in column 5 may refer to assemblages of both cDNA and Genscan-predicted exons brought together by an “exon-stretching” algorithm. For example, FL2428715_g6815043 — 000026_g8052237 — 1 — 3 — 4.edit is the identification number of a “stretched” sequence, with 2428715 being the Incyte project identification number, g6815043 being the GenBank identification number of the human genomic sequence to which the “exon-stretching” algorithm was applied, and g8052237 being the GenBank identification number of the nearest GenBank protein homolog. (See Example V.) In some cases, Incyte cDNA coverage redundant with the sequence coverage shown in column 5 was obtained to confirm the final consensus polynucleotide sequence, but the relevant Incyte cDNA identification numbers are not shown.  
       [0152] Table 5 shows the representative cDNA libraries for those fill length polynucleotide sequences which were assembled using Incyte cDNA sequences. The representative cDNA library is the Incyte cDNA library which is most frequently represented by the Incyte cDNA sequences which were used to assemble and confirm the above polynucleotide sequences. The tissues and vectors which were used to construct the cDNA libraries shown in Table 5 are described in Table 6.  
       [0153] The invention also encompasses ECMCAD variants. A preferred ECMCAD variant is one which has at least about 80%, or alternatively at least about 90%, or even at least about 95% amnino acid sequence identity to the ECMCAD amino acid sequence, and which contains at least one functional or structural characteristic of ECMCAD.  
       [0154] The invention also encompasses polynucleotides which encode ECMCAD. In a particular embodiment, the invention encompasses a polynucleotide sequence comprising a sequence selected from the group consisting of SEQ ID NO:37-72, which encodes ECMCAD. The polynucleotide sequences of SEQ ID NO:37-72, as presented in the Sequence Listing, embrace the equivalent RNA sequences, wherein occurrences of the nitrogenous base thymine are replaced with uracil, and the sugar backbone is composed of ribose instead of deoxyribose.  
       [0155] The invention also encompasses a variant of a polynucleotide sequence encoding ECMCAD. In particular, such a variant polynucleotide sequence will have at least about 70%, or alternatively at least about 85%, or even at least about 95% polynucleotide sequence identity to the polynucleotide sequence encoding ECMCAD. A particular aspect of the invention encompasses a variant of a polynucleotide sequence comprising a sequence selected from the group consisting of SEQ ID NO:37-72 which has at least about 70%, or alternatively at least about 85%, or even at least about 95% polynuclcotidc sequence identity to a nucleic acid sequence selected from the group consisting of SEQ ID NO:37-72. Any one of the polynucleotide variants described above can encode an amino acid sequence which contains at least one functional or structural characteristic of ECMCAD.  
       [0156] It will be appreciated by those skilled in the art that as a result of the degeneracy of the genetic code, a multitude of polynucleotide sequences encoding ECMCAD, some bearing minimal similarity to the polynucleotide sequences of any known and naturally occurring gene, may be produced. Thus, the invention contemplates each and every possible variation of polynucleotide sequence that could be made by selecting combinations based on possible codon choices. These combinations are made in accordance with the standard triplet genetic code as applied to the polynucleotide sequence of naturally occurring ECMCAD, and all such variations arc to be considered as being specifically disclosed.  
       [0157] Although nucleotide sequences which encode ECMCAD and its variants are generally capable of hybridizing to the nucleotide sequence of the naturally occurring ECMCAD under appropriately selected conditions of stringency, it may be advantageous to produce nucleotide sequences encoding ECMCAD or its derivatives possessing a substantially different codon usage, e.g., inclusion of non-naturally occurring codons. Codons may be selected to increase the rate at which expression of the peptide occurs in a particular prokaryotic or eukaryotic host in accordance with the frequency with which particular codons are utilized by the host. Other reasons for substantially altering the nucleotide sequence encoding ECMCAD and its derivatives without altering the encoded amino acid sequences include the production of RNA transcripts having more desirable properties, such as a greater half-life, than transcripts produced from the naturally occurring sequence.  
       [0158] The invention also encompasses production of DNA sequences which encode ECMCAD and ECMCAD derivatives, or fragments thereof, entirely by synthetic chemistry. After production, the synthetic sequence may be inserted into any of the many available expression vectors and cell systems using reagents well known in the art. Moreover, synthetic chemistry may be used to introduce mutations into a sequence encoding ECMCAD or any fragment thereof.  
       [0159] Also encompassed by the invention are polynucleotide sequences that are capable of hybridizing to the claimed polynucleotide sequences, and, in particular, to those shown in SEQ ID NO:37-72 and fragments thereof under various conditions of stringency. (See, e.g., Wahl, G. M. and S. L. Berger (1987) Methods Enzymol. 152:399407; Kimmel, A. R. (1987) Methods Enzymol. 152:507-511.) Hybridization conditions, including annealing and wash conditions, are described in “Definitions.” 
       [0160] Methods for DNA sequencing are well known in the art and may be used to practice any of the embodiments of the invention. The methods may employ such enzymes as the Klenow fragment of DNA polymerase 1, SEQUENASE (US Biochemical, Cleveland Ohio), Taq polymerase (Applied Biosystems), thermostable T7 polymerase (Amersham Pharmacia Biotech, Piscataway N.J.), or combinations of polymerases and proofreading exonucleases such as those found in the ELONGASE amplification system (Life Technologies, Gaithersburg Md.). Preferably, sequence preparation is automated with machines such as the MICROLAB 2200 liquid transfer system (Hamilton, Reno Nev.), PTC200 thermal cycler (MJ Research, Watertown Mass.) and ABI CATALYST 800 thermal cycler (Applied Biosystems), Sequencing is then carried out using either the ABI 373 or 377 DNA sequencing system (Applied Biosystems), the MEGABACE 1000 DNA sequencing system (Molecular Dynamics, Sunnyvale Calif.), or other systems known in the art. The resulting sequences are analyzed using a variety of algorithms which are well known in the art. (See, e.g., Ausubel, F. M. (1997)  Short Protocols in Molecular Biology,  John Wiley &amp; Sons, New York N.Y., unit 7.7; Meyers, R. A. (1995)  Molecular Biology and Biotechnology,  Wiley VCH, New York N.Y., pp. 856-853.)  
       [0161] The nucleic acid sequences encoding ECMCAD may be extended utilizing a partial nucleotide sequence and employing various PCR-based methods known in the art to detect upstream sequences, such as promoters and regulatory elements. For example, one method which may be employed, restriction-site PCR, uses universal and nested primers to amplify unknown sequence from genomic DNA within a cloning vector. (See, e.g., Sarkar, G. (1993) PCR Methods Applic. 2:318-322.) Another method, inverse PCR, uses primers that extend in divergent directions to amplify unknown sequence from a circularized template. The template is derived from restriction fragments comprising a known genomic locus and surrounding sequences. (See, e.g., Triglia, T. et al. (1988) Nucleic Acids Res. 16:8186.) A third method, capture PCR, involves PCR amplification of DNA fragments adjacent to known sequences in human and yeast artificial chromosome DNA. (See, e.g., Lagerstrom, M. et al. (1991) PCR Methods Applic. 1: 111-119.) In this method, multiple restriction enzyme digestions and ligations may be used to insert an engineered double-stranded sequence into a region of unknown sequence before performing PCR. Other methods which may be used to retrieve unknown sequences are known in the art. (See, e.g., Parker, J. D. et al. (1991) Nucleic Acids Res. 19:3055-3060). Additionally, one may use PCR, nested primers, and PROMOTERFINDER libraries (Clontech, Palo Alto Calif.) to walk genomic DNA. This procedure avoids the need to screen libraries and is useful in finding intron/exon junctions. For all PCR-based methods, primers may be designed using commercially available software, such as OLIGO 4.06 primer analysis software (National Biosciences, Plymouth Minn.) or another appropriate program, to be about 22 to 30 nucleotides in length, to have a GC content of about 50% or more, and to anneal to the template at temperatures of about 68° C. to 72° C.  
       [0162] When screening for full length cDNAs, it is preferable to use libraries that have been size-selected to include larger cDNAs. In addition, random-primed libraries, which often include sequences containing the 5′ regions of genes, are preferable for situations in which an oligo d(T) library does not yield a full-length cDNA. Genornic libraries may be useful for extension of sequence into 5′ non-transcribed regulatory regions.  
       [0163] Capillary electrophoresis systems which are commercially available may be used to analyze the size or confirm the nucleotide sequence of sequencing or PCR products. In particular, capillary sequencing may employ flowable polymers for electrophoretic separation, four different nucleotide-specific, laser-stimulated fluorescent dyes, and a charge coupled device camera for detection of the emitted wavelengths. Output/light intensity may be converted to electrical signal using appropriate software (e.g., GENOTYPER and SEQUENCE NAVIGATOR, Applied Biosystems), and the entire process from loading of samples to computer analysis and electronic data display may be computer controlled. Capillary electrophoresis is especially preferable for sequencing small DNA fragments which may be present in limited amounts in a particular sample.  
       [0164] In another embodiment of the invention, polynucleotide sequences or fragments thereof which encode ECMCAD may be cloned in recombinant DNA molecules that direct expression of ECMCAD, or fragments or functional equivalents thereof, in appropriate host cells. Due to the inherent degeneracy of the genetic code, other DNA sequences which encode substantially the same or a functionally equivalent amino acid sequence may be produced and used to express ECMCAD.  
       [0165] The nucleotide sequences of the present invention can be engineered using methods generally known in the art in order to alter ECMCAD-encoding sequences for a variety of purposes including, but not limited to, modification of the cloning, processing, and/or expression of the gene product. DNA shuffling by random fragmentation and PCR reassembly of gene fragments and synthetic oligonucleotides may be used to engineer the nucleotide sequences. For example, oligonucleotide-mediated site-directed mutagenesis may be used to introduce mutations that create new restriction sites, alter glycosylation patterns, change codon preference, produce splice variants, and so forth.  
       [0166] The nucleotides of the present invention may be subjected to DNA shuffling techniques such as MOLECULARBREEDING (Maxygen Inc., Santa Clara Calif.; described in U.S. Pat. No. 5,837,458: Chang, C.-C. et al. (1999) Nat. Biotechnol. 17:793-797; Christians, F. C. et al. (1999) Nat. Biotechnol. 17:259-264; and Crameri, A. et al. (1996) Nat. Biotechnol. 14:315-319) to alter or improve the biological properties of ECMCAD, such as its biological or enzymatic activity or its ability to bind to other molecules or compounds. DNA shuffling is a process by which a library of gene variants is produced using PCR-moediated recombination of gene fragments. The library is then subjected to selection or screening procedures that identify those gene variants with the desired properties. These preferred variants may then be pooled and further subjected to recursive rounds of DNA shuffling and selection/screening. Thus, genetic diversity is created through “artificial” breeding and rapid molecular evolution. For example, fragments of a single gene containing random point mutations may be recombined, screened, and then reshuffled until the desired properties are optimized. Alternatively, fragments of a given gene may be recombined with fragments of homologous genes in the same gene family, either from the same or different species, thereby maximizing the genetic diversity of multiple naturally occurring genes in a directed and controllable manner.  
       [0167] In another embodiment, sequences encoding ECMCAD may be synthesized, in whole or in part, using chemical methods well known in the art. (See, e.g., Caruthers, M. H. et al. (1980) Nucleic Acids Symp. Ser. 7:215-223; and Horn, T. et al. (1980) Nucleic Acids Symp. Ser. 7:225-232.) Alternatively, ECMCAD itself or a fragment thereof may be synthesized using chemical methods. For example, peptide synthesis can be performed using various solution-phase of solid-phase techniques. (See, e.g., Creighton, T. (1984)  Proteins, Structures and Molecular Properties,  WH, Freeman, New York N.Y., pp. 55-60; and Roberge, J. Y. et al. (1995) Science 269:202-204.) Automated synthesis may be achieved using the ABI 431A peptide synthesizer (Applied Biosystems). Additionally, the amino acid sequence of ECMCAD, or any part thereof, may be altered during direct synthesis and/or combined with sequences from other proteins, or any part thereof, to produce a variant polypeptide or a polypeptide having a sequence of a naturally occurring polypeptide.  
       [0168] The peptide may be substantially purified by preparative high performance liquid chromatography. (See, e.g., Chiez, R. M. and F. Z. Regnier (1990) Methods Enzymol. 182:392-421.) The composition of the synthetic peptides may be confirmed by amino acid analysis or by sequencing. (See, e.g., Creighton, supra, pp. 28-53.)  
       [0169] In order to express a biologically active ECMCAD, the nucleotide sequences encoding ECMCAD or derivatives thereof may be inserted into an appropriate expression vector, i.e., a vector which contains the necessary elements for transcriptional and translational control of the inserted coding sequence in a suitable host. These elements include regulatory sequences, such as enhancers, constitutive and inducible promoters, and 5′ and 3′untranslated regions in the vector and in polynucleotide sequences encoding ECMCAD. Such elements may vary in their strength and specificity. Specific initiation signals may also be used to achieve more efficient translation of sequences encoding ECMCAD. Such signals include the ATG initiation codon and adjacent sequences, e.g. the Kozak sequence. In cases where sequences encoding ECMCAD and its initiation codon and upstream regulatory sequences are inserted into the appropriate expression vector, no additional transcriptional or translational control signals may be needed. However, in cases where only coding sequence, or a fragment thereof, is inserted, exogenous translational control signals including an in-frame ATG initiation codon should be provided by the vector. Exogenous translational elements and initiation codons may be of various origins, both natural and synthetic. The efficiency of expression may be enhanced by the inclusion of enhancers appropriate for the particular host cell system used. (See, e.g., Scharf, D. et al. (1994) Results Probl. Cell Differ. 20:125-162.)  
       [0170] Methods which are well known to those skilled in the art may be used to construct expression vectors containing sequences encoding ECMCAD and appropriate transcriptional and translational control elements. These methods include in vitro recombinant DNA tecluiques, synthetic techniques, and in vivo genetic recombination. (See, e.g., Sambrook J. et al. (1989)  Molecular Cloning, A Laboratory Manual,  Cold Spring Harbor Press, Plainview N.Y., ch. 4, 8, and 16-17; Ausubel, F. M. et al. (1995)  Current Protocols in Molecular Biology,  John Wiley &amp; Sons, New York N.Y., ch. 9, 13, and 16.)  
       [0171] A variety of expression vector/host systems may be utilized to contain and express sequences encoding ECMCAD. These include, but are not limited to, microorganisms such as bacteria transformed with recombinant bacteriophage, plasmid, or cosmid DNA expression vectors; yeast transformed with yeast expression vectors; insect cell systems infected with viral expression vectors (e.g., baculovirus); plan( cell systems transformed with viral expression vectors (e.g., cauliflower mosaic virus, CaMV, or tobacco mosaic virus, TMV) or with bacterial expression vectors (e.g., Ti or pBR322 plasmids); or animal cell systems. (See, e.g., Sambrook, supra; Ausubel, supra; Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509; Engelhard, E. K. et al. (1994) Proc. Natl. Acad. Sci. USA 91:3224-3227; Sandig, V. et al. (1996) Hum. Gene Ther. 7:1937-1945; Takamatsu, N. (1987) EMBO J. 6:307-311;  The McGraw Hill Yearbook of Science and Technology  (1992) McGraw Hill, New York N.Y., pp. 191-196; Logan, J. and T. Shenk (1984) Proc. Natl. Acad. Sci. USA 81:3655-3659; and Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355.) Expression vectors derived from retroviruses, adenoviruses, or herpes or vaccinia viruses, or from various bacterial plasmids, may be used for delivery of nucleotide sequences to the targeted organ, tissue, or cell population. (See, e.g., Di Nicola, M. et al. (1998) Cancer Gen. Ther. 5(6):350-356; Yu, M. et al. (1993) Proc. Natl. Acad. Sci. USA 90(13):6340-6344; Buller, R. M. et al. (1985) Nature 317(6040):813-815; McGregor, D. P. et al. (1994) Mol. Immunol. 31(3):219-226; and Verma, I. M. and N. Somia (1997) Nature 389:239-242.) The invention is not limited by the host cell employed.  
       [0172] In bacterial systems, a number of cloning and expression vectors may be selected depending upon the use intended for polynucleotide sequences encoding ECMCAD. For example, routine cloning, subcloning, and propagation of polynucleotide sequences encoding ECMCAD can be achieved using a multifunctional  E. coli  vector such as PBLUESCRIPT (Stratagene, La Jolla Calif.) or PSPORT1 plasmid (Life Technologies). Ligation of sequences encoding ECMCAD into the vector&#39;s multiple cloning site disrupts the lacZ gene, allowing a calorimetric screening procedure for identification of transformed bacteria containing recombinant molecules. In addition, these vectors may be useful for in vitro transcription, didcoxy sequencing, single strand rescue with helper phage, and creation of nested deletions in the cloned sequence. (See, e.g., Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509.) When large quantities of ECMCAD are needed, e.g. for the production of antibodies, vectors which direct high level expression of ECMCAD may be used. For example, vectors containing the strong, inducible SP6 or T7 bacteriophage promoter may be used.  
       [0173] Yeast expression systems may be used for production of ECMCAD. A number of vectors containing constitutive or inducible promoters, such as alpha factor, alcohol oxidase, and PGH promoters, may be used in the yeast  Saccharomyces cerevisiae  or  Pichia pastoris.  In addition, such vectors direct either the secretion or intracellular retention of expressed proteins and enable integration of foreign sequences into the host genome for stable propagation. (See, e.g., Ausubel, 1995, supra; Bitter, G. A. et al. (1987) Methods Enzymol. 153:516-544; and Scorer, C. A. et al. (1994) Bio/Technology 12:181-184.)  
       [0174] Plant systems may also be used for expression of ECMCAD. Transcription of sequences encoding ECMCAD may be driven by viral promoters, e.g., the 35S and 19S promoters of CaMV used alone or in combination with the omega leader sequence from TMV (Takamatsu, N. (1987) EMBO J. 6:307-311). Alternatively, plant promoters such as the small subunit of RUBISCO or heat shock promoters may be used. (See, e.g., Coruzzi, G. et al. (1984) EMBO J. 3:1671-1680; Broglie, R. et al. (1984) Science 224:838-843; and Winter, J. et al. (1991) Results Probl. Cell Differ. 17:85-105.) These constructs can be introduced into plant cells by direct DNA transformation or pathogen-mediated transfection. (See, e.g.,  The McGraw Hill Yearbook of Science and Technology  (1992) McGraw Hill, New York N.Y., pp. 191-196.)  
       [0175] In mammalian cells, a number of viral-based expression systems may be utilized. In cases where an adenovirus is used as an expression vector, sequences encoding ECMCAD may be ligated into an adenovirus transcription/translation complex consisting of the late promoter and tripartite leader sequence. Insertion in a non-essential E1 or E3 region of the viral genome may be used to obtain infective virus which expresses ECMCAD in host cells. (See, e.g., Logan, J. and T. Shenk (1984) Proc. Natl. Acad. Sci. USA 81:3655-3659.) In addition, transcription enhancers, such as the Rous sarcoma virus (RSV) enhancer, may be used to increase expression in mammalian host cells. SV40 or EBV-based vectors may also be used for high-level protein expression.  
       [0176] Human artificial chromosomes (HACs) may also be employed to deliver larger fragments of DNA than can be contained in and expressed from a plasmid. RACs of about 6 kb to 10 Mb are constructed and delivered via conventional delivery methods (liposomes, polycationic amino polymers, or vesicles) for therapeutic purposes. (See, e.g., Harrington, J. J. et al. (I 997) Nat. Genet. 15:345-355.)  
       [0177] For long term production of recombinant proteins in mammalian systems, stable expression of ECMCAD in cell lines is preferred. For example, sequences encoding ECMCAD can be transformed into cell lines using expression vectors which may contain viral origins of replication and/or endogenous expression elements and a selectable marker gene on the same or on a separate vector. Following the introduction of the vector, cells may be allowed to grow for about 1 to 2 days in enriched media before being switched to selective media. The purpose of the selectable marker is to confer resistance to a selective agent, and its presence allows growth and recovery of cells which successfully express the introduced sequences. Resistant clones of stably transformed cells may be propagated using tissue culture techniques appropriate to the cell type.  
       [0178] Any number of selection systems may be used to recover transformed cell lines. These include, but are not limited to, the herpes simplex virus thymidine kinase and adenine phosphoribosyltransferase genes, for use in tk and apr cells, respectively. (See, e.g., Wigler, M. et al. (1977) Cell 11:223-232; Lowy, I. et al. (1980) Cell 22:817-823.) Also, antimetabolite, antibiotic, or herbicide resistance can be used as the basis for selection. For example, dhfr confers resistance to methotrexate; neo confers resistance to the aminoglycosides neomycin and G-418; and als and pat confer resistance to chlorsulfluon and phosphinotricin acetyltransferase, respectively. (See, e.g., Wigler, M. et al. (1980) Proc. Natl. Acad. Sci. USA 77:3567-3570; Colbere-Garapin, F. et al. (1981) J. Mol. Biol. 150:1-14.) Additional selectable genes have been described, e.g., trpB and hisD, which alter cellular requirements for metabolites. (See, e.g., Haitman, S. C. and R. C. Mulligan (1988) Proc. Natl. Acad. Sci. USA 85:8047-8051.) Visible markers, e.g., anthocyanins, green fluorescent proteins (GFP; Clontech), β glucuronidase and its substrate β-glucuronide, or luciferase and its substrate luciferin may be used. These markers can be used not only to identify transformants, but also to quantify the amount of transient or stable protein expression attributable to a specific vector system. (See, e.g., Rhodes, C. A. (1995) Methods Mol. Biol. 55:121-131.)  
       [0179] Although the presence/absence of marker gene expression suggests that the gene of interest is also present, the presence and expression of the gene may need to be confirmed. For example, if the sequence encoding ECMCAD is inserted within a marker gene sequence, transformed cells containing sequences encoding ECMCAD can be identified by the absence of marker gene function. Alternatively, a marker gene can be placed in tandem with a sequence encoding ECMCAD under the control of a single promoter. Expression of the marker gene in response to induction or selection usually indicates expression of the tandem gene as well.  
       [0180] In general, host cells that contain the nucleic acid sequence encoding ECMCAD and that express ECMCAD may be identified by a variety of procedures known to those of skill in the art. These procedures include, but are not limited to, DNA-DNA or DNA-RNA hybridizations, PCR amplification, and protein bioassay or immunoassay techniques which include membrane, solution, or chip based technologies for the detection and/or quantification of nucleic acid or protein sequences.  
       [0181] Immunological methods for detecting and measuring the expression of ECMCAD using either specific polyclonal or monoclonal antibodies are known in the art. Examples of such techniques include enzyme-linked immunosorbent assays (ELISAs), radioimmunoassays (RfAs), and fluorescence activated cell sorting (FACS). A two-site, monoclonal-based immunoassay utilizing monoclonal antibodies reactive to two non-interfering epitopes on ECMCAD is preferred, but a competitive binding assay may be employed. These and other assays are well known in the art. (See, e.g., Hampton, R. et al. (1990)  Serological Methods, a Laboratory Manual,  APS Press, St. Paul Minn., Sect. IV; Coligan, J. E. et al. (1997)  Current Protocols in Immunology,  Greene Pub. Associates and Wiley-Interscience, New York N.Y.; and Pound, J. D. (1998)  Immunochemical Protocols,  Humana Press, Totowa N.J.)  
       [0182] A wide variety of labels and conjugation techniques are known by those skilled in the art and may be used in various nucleic acid and amino acid assays. Means for producing labeled hybridization or PCR probes for detecting sequences related to polynucleotides encoding ECMCAD include oligolabeling, nick translation, end-labeling, or PCR amplification using a labeled nucleotide. Alternatively, the sequences encoding ECMCAD, or any fragments thereof, may be cloned into a vector for the production of an mRNA probe. Such vectors are known in the art, are commercially available, and may be used to synthesize RNA probes in vitro by addition of an appropriate RNA polymerase such as T7, T3, or SP6 and labeled nucleotides. These procedures may be conducted using a variety of commercially available kits, such as those provided by Amersham Pharmacia Biotech, Promega (Madison Wis.), and US Biochemical. Suitable reporter molecules or labels which may be used for ease of detection include radionuclides, enzymes, fluorescent, chemiluminescent, or chromogenic agents, as well as substrates, cofactors, inhibitors, magnetic particles, and the like.  
       [0183] Host cells transformed with nucleotide sequences encoding ECMCAD may be cultured under conditions suitable for the expression and recovery of the protein from cell culture. The protein produced by a transformed cell may be secreted or retained intracellularly depending on the sequence and/or the vector used. As will be understood by those of skill in the art, expression vectors containing polynucleotides which encode ECMCAD may be designed to contain signal sequences which direct secretion of ECMCAD through a prokaryotic or eukaryotic cell membrane.  
       [0184] In addition, a host cell strain may be chosen for its ability to modulate expression of the inserted sequences or to process the expressed protein in the desired fashion. Such modifications of the polypeptide include, but are not limited to, acetylation, carboxylation, glycosylation, phosphorylation, lipidation, and acylation. Post-translational processing which cleaves a “prepro” or “pro” form of the protein may also be used to specify protein targeting, folding, and/or activity. Different host cells which have specific cellular machinery and characteristic mechanisms for post-translational activities (e.g., CHO, HeLa, MDCK, HEK293, and W138) are available from the American Type Culture Collection (ATCC, Manassas Va.) and may be chosen to ensure the correct modification and processing of the foreign protein.  
       [0185] In another embodiment of the invention, natural, modified, or tecombinant nucleic acid sequences encoding ECMCAD may be ligated to a heterologous sequence resulting in translation of a fusion protein in any of the aforementioned host systems. For example, a chimeric ECMCAD protein containing a heterologous moiety that can be recognized by a commercially available antibody may facilitate the screening of peptide libraries for inhibitors of ECMCAD activity. Heterologous protein and peptide moieties may also facilitate purification of fusion proteins using commercially available affinity matrices. Such moieties include, but are not limited to, glutathione S-transferase (GST), maltose binding protein (MBP), tioredoxin (Trx), calmodulin binding peptide (CBP), 6-His, FLAG, c-myc, and hemagglutinin (HA). GST, MBP, Trx, CBP, and 6-His enable purification of their cognate fusion proteins on immobilized glutathione, maltose, phenylarsine oxide, calmodulin, and metal-chelate resins, respectively. FLAG, c-myc, and hemagglutinin (HA) enable immunoaffinity purification of fusion proteins using commercially available monoclonal and polyclonal antibodies that specifically recognize these epitope tags. A fusion protein may also be engineered to contain a proteolytic cleavage site located between the ECMCAD encoding sequence and the heterologous protein sequence, so that ECMCAD may be cleaved away from the heterologous moiety following purification. Methods for fusion protein expression and purification are discussed in Ausubel (1995, supra, ch. 10). A variety of commercially available kits may also be used to facilitate expression and purification of fusion proteins.  
       [0186] In a further embodiment of the invention, synthesis of radiolabeled ECMCAD may be achieved in vitro using the TNT rabbit reticulocyte lysate or wheat germ extract system (Promega). These systems couple transcription and translation of protein-coding sequences operably associated with the T7, T3, or SP6 promoters. Translation takes place in the presence of a radiolabeled amino acid precursor, for example,  35 S-methionine.  
       [0187] ECMCAD of the present invention or fragments thereof may be used to screen for compounds that specifically bind to ECMCAD. At least one and up to a plurality of test compounds may be screened for specific binding to ECMCAD. Examples of test compounds include antibodies, oligonucleotides, proteins (e.g., receptors), or small molecules.  
       [0188] In one embodiment, the compound thus identified is closely related to the natural ligand of ECMCAD. e.g., a ligand or fragment thereof, a natural substrate, a structural or functional mimetic, or a natural binding partner. (See, e.g., Coligan, J. E. et al. (1991)  Current Protocols in Immunology  1(2): Chapter 5.) Similarly, the compound can be closely related to the natural receptor to which ECMCAD binds, or to at least a fragment of the receptor, e.g., the ligand binding site. In either case, the compound can be rationally designed using known techniques. In one embodiment, screening for these compounds involves producing appropriate cells which express ECMCAD, either as a secreted protein or on the cell membrane. Preferred cells include cells from mammals, yeast, Drosophila, or  E. coli.  Cells expressing ECMCAD or cell membrane fractions which contain ECMCAD are then contacted with a test compound and binding, stimulation, or inhibition of activity of either ECMCAD or the compound is analyzed.  
       [0189] An assay may simply test binding of a test compound to the polypeptide, wherein binding is detected by a fluorophore, radioisotope, enzyme conjugate, or other detectable label. For example, the assay may comprise the steps of combining at least one test compound with ECMCAD, either in solution or affixed to a solid support, and detecting the binding of ECMCAD to the compound. Alternatively, the assay may detect or measure binding of a test compound in the presence of a labeled competitor. Additionally, the assay may be carried out using cell-free preparations, chemical libraries, or natural product mixtures, and the test compound(s) may be free in solution or affixed to a solid support.  
       [0190] ECMCAD of the present invention or fragments thereof may be used to screen for compounds that modulate the activity of ECMCAD. Such compounds may include agonists, antagonists, or partial or inverse agonists. In one embodiment, an assay is performed under conditions permissive for ECMCAD activity, wherein ECMCAD is combined with at least one test compound, and the activity of ECMCAD in the presence of a test compound is compared with the activity of ECMCAD in the absence of the test compound. A change in the activity of ECMCAD in the presence of the test compound is indicative of a compound that modulates the activity of ECMCAD. Alternatively, a test compound is combined with an in vitro or cell-free system comprising ECMCAD under conditions suitable for ECMCAD activity, and the assay is performed. In either of these assays, a test compound which modulates the activity of ECMCAD may do so indirectly and need not come in direct contact with the test compound. At least one and up to a plurality of test compounds may be screened.  
       [0191] In another embodiment, polynucleotides encoding ECMCAD or their mammalian homologs may be “knocked out” in an animal model system using homologous recombination in embryonic stem (ES) cells. Such techniques arc well known in the art and are useful for the generation of animal models of human disease. (See, e.g., U.S. Pat. No. 5,175,383 and U.S. Pat. No. 5,767,337.) For example, mouse ES cells, such as the mouse 129/SvJ cell line, are derived from the early mouse embryo and grown in culture. The ES cells are transformed with a vector containing the gene of interest disrupted by a marker gene, e.g., the neomycin phosphotransferase gene (neo; Capecchi, M. R. (1989) Science 244:1288-1292). The vector integrates into the corresponding region of the host genome by homologous recombination. Alternatively, homologous recombination takes place using the Cre-loxP system to knockout a gene of interest in a tissue- or developmental stage-specific manner (Maith, J. D. (1996) Clin. Invest. 97:1999-2002; Wagner, K. U. et al. (1997) Nucleic Acids Res. 25:4323-4330). Transformed ES cells are identified and microinjected into mouse cell blastocysts such as those from the C57BL/6 mouse strain. The blastocysts are surgically transferred to pseudopregnant dams, and the resulting chimeric progeny are genotyped and bred to produce heterozygous or homozygous strains. Transgenic animals thus generated may be tested with potential therapeutic or toxic agents.  
       [0192] Polynucleotides encoding ECMCAD may also be manipulated in vitro in ES cells derived from human blastocysts. Human ES cells have the potential to differentiate into at least eight separate cell lineages including endoderm, mesoderm, and ectodermal cell types. These cell lineages differentiate into, for example, neural cells, hematopoietic lineages, and cardiomyocytes (Thomson, J. A. et al. (1998) Science 282:1145-1147).  
       [0193] Polynucleotides encoding ECMCAD can also be used to create “knockin” humanized animals (pigs) or transgenic animals (mice or rats) to model human disease. With knockin technology, a region of a polynucleotide encoding ECMCAD is injected into animal ES cells, and the injected sequence integrates into the animal cell genome. Transformed cells are injected into blastulae, and the blastulae are implanted as described above. Transgenic progeny or inbred lines are studied and treated with potential pharmaceutical agents to obtain information on treatment of a human disease. Alternatively, a mammal inbred to overexpress ECMCAD, e.g., by secreting ECMCAD in its milk, may also serve as a convenient source of that protein (Janne, J. et al. (1998) Biotechnol. Annu. Rev. 4:55-74).  
       THERAPEUTICS  
       [0194] Chemical and structural similarity, e.g., in the context of sequences and motifs, exists between regions of ECMCAD and extracellular matrix and cell adhesion molecules In addition, the expression of ECMCAD is closely associated with brain, prostate, atrial myxoma, cerebellum, cervical dorsal root ganglion, cardiac muscle, mesentel fat, kidney epithelium, thymus, endothelium, ovary, placenta, smooth muscle, fallopian tube, breast, cartilage, bladder, rib, colon, spine, gall bladder, blood granulocytes, submandibular gland, seminal vesicle, and intestine tissues; with tumors of the brain, prostate, rib, and fallopian tube; and with dermal microvascular endothelial cells, hNT2 cells derived from a human teratocarcinoma, and 293-EBNA transformed embryonal cells derived from kidney epithelial tissue. Therefore, ECMCAD appears to play a role in genetic, immune/inflammatory, developmental, neurological, connective tissue, and cell proliferative disorders, including cancer. In the treatment of disorders associated with increased ECMCAD expression or activity, it is desirable to decrease the expression or activity of ECMCAD. In the treatment of disorders associated with decreased ECMCAD expression or activity, it is desirable to increase the expression or activity of ECMCAD.  
       [0195] Therefore, in one embodiment, ECMCAD or a fragment or derivative thereof may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of ECMCAD. Examples of such disorders include, but are not limited to, a genetic disorder such as adrenoleukodystrophy, Alport&#39;s syndrome, choroideremia, Duchenne and Becker muscular dystrophy, Down&#39;s syndrome, cystic fibrosis, chronic granulomatous disease, Gaucher&#39;s disease, Huntington&#39;s chorea, Marfan&#39;s syndrome, muscular dystrophy, myotonic dystrophy, pyenodysostosis, Refsum&#39;s syndrome, retinoblastoma, sickle cell anemia, thalassemia, Werner syndrome, von Willebrand&#39;s disease, Wilms&#39; tumor, Zellweger syndrome, peroxisomal acyl-CoA oxidase deficiency, peroxisomal thiolase deficiency, peroxisomal bifunctional protein deficiency, mitochondrial carnitine palmitoyl transferase and carnitine deficiency, mitochondrial very-long-chain acyl-CoA dehydrogenase deficiency, mitochondrial medium-chain acyl-CoA dehydrogenase deficiency, mitochondrial short-chain acyl-CoA dehydrogenase deficiency, mitochondrial electron transport flavoprotein and electron transport flavoprotein:ubiquinone oxidoreductase deficiency, mitochondrial trifunctional protein deficiency, and mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency; an immune/inflammatory disorder such as acquired immunodeficiency syndrome (AIDS), X-linked agammaglobinemia of Bruton, common variable immunodeficiency (CVI), DiGeorge&#39;s syndrome (thymic hypoplasia), thymic dysplasia, isolated IgA deficiency, severe combined immunodeficiency disease (SCID), immunodeficiency with thrombocytopenia and eczema (Wiskott-Aldrich syndrome), Chediak-Higashi syndrome, chronic granulomatous diseases, hereditary angioneurotic edema, immunodeficiency associated with Cushing&#39;s disease, Addison&#39;s disease, adult respiratory distress syndrome, allergies, ankylosinig spondylitis, aimyloidosis, anemia, asthma, atherosclerosis, autoimmune hemolytic anemia, autoimmune thyroiditis, autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED), bronchitis, cholecystitis, contact dermatitis, Crohn&#39;s disease, atopic dermatitis, dermatomyositis, diabetes mellitus, emphysema, episodic lymphopenia with lymphocytotoxins, eiytlioblastosis fetalis, erythema nodosum, atrophic gasthitis, glomerulonephritis, Goodpasture&#39;s syndrome, gout, Graves&#39; disease, Hashimoto&#39;s thyroiditis, hypereosinophilia, irritable bowel syndrome, multiple sclerosis, myasthenia gravis, myocardial or pericardial inflammation, osteoarthritis, osteoporosis, pancreatitis, polymyositis, psoriasis, Reiter&#39;s syndrome, rheumatoid arthritis, scleroderma, Sjogren&#39;s syndrome, systemic anaphylaxis, systemic lupus erythematosus, systernic sclerosis, thrombocytopenic purpura, ulcerative colitis, uveitis, Werner syndrome, complications of cancer, hemodialysis, and extracorporeal circulation, viral, bacterial, fungal, parasitic, protozoal, and helminthic infections, and trauma; a developmental disorder such as renal tubular acidosis, anemia, Cushing&#39;s syndrome, achondroplastic dwarfism, Duchenne and Becker muscular dystrophy, epilepsy, gonadal dysgenesis, WAGR syndrome (Wilms&#39; tumor, aniridia, genitourinary abnormalities, and mental retardation), Smith-Magenis syndrome, myelodysplastic syndrome, hereditary mucoepithelial dysplasia, hereditary keratodermas, hereditary neuropathies such as Charcot-Marie-Tooth disease and neurofibromatosis, hypothyroidism, hydrocephalus, seizure disorders such as Syndenham&#39;s chorea and cerebral palsy, spina bifida, anencephaly, craniorachischisis, congenital glaucoma, cataract, and sensorineural hearing loss; a neurological disorder such as epilepsy, ischemic cerebrovascular disease, stroke, cerebral neoplasms, Alzheimer&#39;s disease, Pick&#39;s disease, Huntinigton&#39;s disease, dementia, Parkinson&#39;s disease and other extrapyramidal disorders, amyotrophic lateral sclerosis and other motor neuron disorders, progressive neural muscular atrophy, retinitis pigmentosa, hereditary ataxias, multiple sclerosis and other demyelinating diseases, bacterial and viral meningitis, brain abscess, subdural empyoma, epidural abscess, suppurative intracranial thrombophlebitis, myelitis and radiculitis, viral central nervous system disease, prion diseases including kuru, Creutzfeldt-Jakob disease, and Gerstmann-Straussler-Scheiniker syndrome, fatal familial insomnia, nutritional and metabolic diseases of the nervous system, neurofibromatosis, tuberous sclerosis, cerebelloretinal hemangioblastomatosis, encephalotrigeminal syndrome, mental retardation and other developmental disorders of the central nervous system including Down syndrome, cerebral palsy, neuroskeletal disorders autonomic nervous system disorders, cranial nerve disorders, spinal cord diseases, muscular dystrophy and other neuromuscular disorders, peripheral nervous system disorders, dermatomyositis and polymyositis, inherited, metabolic, endocrine, and toxic myopathies, myasthenia gravis, periodic paralysis, mental disorders including mood, anxiety, and schizophrenic disorders, seasonal affective disorder (SAD), akathesia, amnesia, catatonia, diabetic neuropathy, tardive dyskinesia, dystonias, paranoid psychoses, postheipetic neuralgia, Tourette&#39;s disorder, progressive supranuclear palsy, corticobasal degeneration, and familial frontotemporal dementia; a connective tissue disorder such as osteogenesis imperfecta, Ehlers-Danlos syndrome, chondrodysplasias, Marfan syndrome, Alport syndrome, familial aortic aneurysm, achondroplasia, mucopolysaccharidoses, osteoporosis, osteopetrosis, Paget&#39;s disease, rickets, osteomalacia, hyperparathyroidism, renal osteodystrophy, osteoneciosis, osteomyelitis, osteoma, osteoid osteoma, osteoblastoma, osteosarcoma, osteochondroma, chondroma, chondroblastoma, chondromyxoid fibroma, chondrosarcoma, fibrous cortical defect, nonossifying fibroma, fibrous dysplasia, fibrosarcoma, malignant fibrous histiocytoma, Ewing&#39;s sarcoma, primitive neuroectodermal tumor, giant cell tumor, osteoarthritis, rheumatoid arthritis, ankylosing spondyloarthritis, Reiter&#39;s syndrome, psoriatic arthritis, enteropathic arthritis, infectious arthritis, gout, gouty arthritis, calcium pyrophosphate crystal deposition disease, ganglion, synovial cyst, villonodular synovitis, systemic sclerosis, Dupuytren&#39;s contracture, hepatic fibrosis, lupus erythematosus, mixed connective tissue disease, epidermolysis bullosa simplex, bullous congenital ichthyosiform erythroderma (epiderniolytic hyperkeratosis), non-epidermolytic and epidermolytic palmoplantar keratoderina, ichthyosis bullosa of Siemens, pachyonychia congenital and white sponge nevus; and a cell proliferative disorder such as actinic keratosis, arteriosclerosis, atherosclerosis, bursitis, cirrhosis, hepatitis, mixed connective tissue disease (MCTD), myelofibrosis, paroxysmal nocturnal hemoglobinuria, polycytheima vera, psoriasis, primary thrombocythemia, and cancers including adenocarcinoma, leukemia, lymphoma, melanoma, myeloma, sarcoma, teratocarcinoma, and, in particular, cancers of the adrenal gland, bladder, bone, bone marrow, brain, breast, cervix, gall bladder, ganglia, gastrointestinal tract, heart, kidney, liver, lung, muscle, ovaty, pancreas, parathyroid, penis, prostate, salivary glands, skin, spleen, testis, thymus, thyroid, and uterus.  
       [0196] In another embodiment, a vector capable of expressing ECMCAD or a fragment or derivative thereof may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of ECMCAD including, but not limited to, those described above.  
       [0197] In a further embodiment, a composition comprising a substantially purified ECMCAD in conjunction with a suitable pharmaceutical carrier may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of ECMCAD including, but not limited to, those provided above.  
       [0198] In still another embodiment, an agonist which modulates the activity of ECMCAD may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of ECMCAD including, but not limited to, those listed above.  
       [0199] In a further embodiment, an antagonist of ECMCAD may be administered to a subject to treat or prevent a disorder associated with increased expression or activity of ECMCAD. Examples of such disorders include, but are not limited to, those genetic, immunelinflammatory, developmental, neurological, connective tissue, and cell proliferative disorders, including cancer described above. In one aspect, an antibody which specifically binds ECMCAD may be used directly as an antagonist or indirectly as a targeting or delivery mechanism for bringing a pharmaceutical agent to cells or tissues which express ECMCAD.  
       [0200] In an additional embodiment, a vector expressing the complement of the polynucleotide encoding ECMCAD may be administered to a subject to treat or prevent a disorder associated with increased expression or activity of ECMCAD including, but not limited to, those described above.  
       [0201] In other embodiments, any of the proteins, antagonists, antibodies, agonists, complementary sequences, or vectors of the invention may be administered in combination with other appropriate therapeutic agents. Selection of the appropriate agents for use in combination therapy may be made by one of ordinary skill in the art, according to conventional pharmaceutical principles. The combination of therapeutic agents may act synergistically to effect the treatment or prevention of the various disorders described above. Using this approach, one may be able to aclueve therapeutic efficacy with lower dosages of each agent, thus reducing the potential for adverse side effects.  
       [0202] An antagonist of ECMCAD may be produced using methods which are generally known in the art. In particular, purified ECMCAD may be used to produce antibodies or to screen libraries of pharmaceutical agents to identify those which specifically bind ECMCAD. Antibodies to ECMCAD may also be generated using methods that are well known in the art. Such antibodies may include, but are not limited to, polyclonal, monoclonal, chimeric, and single chain antibodies, Fab fragments, and fragments produced by a Fab expression library. Neutralizing antibodies (i.e., those which inhibit dimer formation) are generally preferred for therapeutic use.  
       [0203] For the production of antibodies, various hosts including goats, rabbits, rats, mice, humans, and others may be immunized by injection with ECMCAD or with any fragment or oligopeptide thereof which has immunogenic properties. Depending on the host species, various adjuvants may be used to increase immunological response. Such adjuvants include, but are not limited to, Freund&#39;s, mineral gels such as aluminum hydroxide, and surface active substances such as lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, KLH, and dinitrophenol. Among adjuvants used in humans, BCG (bacilli Calmette-Guerin) and  Cornebacterium parvum  are especially preferable.  
       [0204] It is preferred that the oligopeptides, peptides, or fragments used to induce antibodies to ECMCAD have an amino acid sequence consisting of at least about 5 amino acids, and generally will consist of at least about 10 amino acids. It is also preferable that these oligopeptides, peptides, or fragments are identical to a portion of the amino acid sequence of the natural protein. Short stretches of ECMCAD amino acids may be fused with those of another protein, such as KLH, and antibodies to the chimeric molecule may be produced.  
       [0205] Monoclonal antibodies to ECMCAD may be prepared using any technique which provides for the production of antibody molecules by continuous cell lines in culture. These include, but are not limited to, the hybridoma technique, the human B-cell hybridoma technique, and the EBV-hybridoma technique. (See, e.g., Kohler, G. et al. (1975) Nature 256:495-497; Kozbor, D. et al. (1985) J. Immunol. Methods 81:31-42; Cote, R. J. et al. (1983) Proc. Natl. Acad. Sci. USA 80:2026-2030; and Cole, S. P. et al. (1984) Mol. Cell Biol. 62:109-120.)  
       [0206] In addition, techniques developed for the production of “chimeric antibodies,” such as the splicing of mouse antibody genes to human antibody genes to obtain a molecule with appropriate antigen specificity and biological activity, can be used. (See, e.g., Morrison, S. L. et al. (1984) Proc. Natl. Acad. Sci. USA 81:6851-6855; Neuberger, M. S. et al. (1984) Nature 312:604-608; and Takeda, S. et al. (1985) Nature 314:452-454.) Alternatively, techniques described for the production of single chain antibodies may be adapted, using methods known in the art, to produce ECMCAD-specific single chain antibodies. Antibodies with related specificity, but of distinct idiotypic composition, may be generated by chain shuffling from random combinatorial immunoglobulin libraries. (See, e.g., Burton, D. R. (1991) Proc. Natl. Acad. Sci. USA 88:10134-10137.)  
       [0207] Antibodies may also be produced by inducing in vivo production in the lymphocyte population or by screening immunoglobulin libraries or panels of highly specific binding reagents as disclosed in the literature. (See, e.g., Orlandi, R. et al. (1989) Proc. Natl. Acad. Sci. USA 86:3833-3837; Winter, G. et al. (1991) Nature 349:293-299.)  
       [0208] Antibody fragments which contain specific binding sites for ECMCAD may also be generated. For example, such fragments include, but are not limited to, F(ab′) 2  fragments produced by pepsin digestion of the antibody molecule and Fab fragments generated by reducing the disulfide bridges of the F(ab)2 fragments. Alternatively, Fab expression libraries may be constructed to allow rapid and easy identification of monoclonal Fab fragments with the desired specificity. (See, e.g., Huse, W. D. et al. (1989) Science 246:1275-1281.)  
       [0209] Various immunoassays may be used for screening to identify antibodies having the desired specificity. Numerous protocols for competitive binding or immunoradiometric assays using either polyclonal or monoclonal antibodies with established specificities are well known in the art. Such immunoassays typically involve the measurement of complex formation between ECMCAD and its specific antibody. A two-site, monoclonal-based immunoassay utilizing monoclonal antibodies reactive to two non-interfering ECMCAD epitopes is generally used, but a competitive binding assay may also be employed (Pound, supra).  
       [0210] Various methods such as Scatchard analysis in conjunction with radioimmunoassay techniques may be used to assess the affinity of antibodies for ECMCAD. Affinity is expressed as an association constant K a , which is defined as the molar concentration of ECMCAD-antibody complex divided by the molar concentrations of free antigen and free antibody under equilibrium conditions. The K a  determined for a preparation of polyclonal antibodies, which are heterogeneous in their affinitics for multiple ECMCAD epitopes, represents the average affinity, or avidity, of the antibodies for ECMCAD. The K a  determined for a preparation of monoclonal antibodies, which are monospecific for a particular ECMCAD epitope, represents a true measure of affinity. High-affinity antibody preparations with K a  ranging from about 10 9  to 10 12  L/mole are preferred for use in immunoassays in which the ECMCAD-antibody complex must withstand rigorous manipulations. Low-affinity antibody preparations with K a  ranging from about 10 6  to 10 7  L/mole are preferred for use in immunopurification and similar procedures which ultimately require dissociation of ECMCAD, preferably in active form, from the antibody (Catty, D. (1988)  Antibodies, Volume I: A Practical Approach,  IRL Press, Washington D.C.; Liddell, J. E. and A. Ciyer (1991)  A Practical Guide to Monoclonal Antibodies,  John Wiley &amp; Sons, New York N.Y.).  
       [0211] The titer and avidity of polyclonal antibody preparations may be further evaluated to determine the quality and suitability of such preparations for certain downstream applications. For example, a polyclonal antibody preparation containing at least 1-2 mg specific antibody/ml, preferably 5-10 mg specific antibody/ml, is generally employed in procedures requiring precipitation of ECMCAD-antibody complexes. Procedures for evaluating antibody specificity, titer, and avidity, and guidelines for antibody quality and usage in various applications, are generally available. (See, e.g., Catty, supra, and Coligan et al. supra.)  
       [0212] In another embodiment of the invention, the polynucleotides encoding ECMCAD, or any fragment or complement thereof, may be used for therapeutic purposes. In one aspect, modifications of gene expression can be achieved by designing complementary sequences or antisense molecules (DNA, RNA, PNA, or modified oligonucleotides) to the coding or regulatory regions of the gene encoding ECMCAD. Such technology is well known in the all, and antisense oligonucleotides or larger fragments can be designed from various locations along the coding or control regions of sequences encoding ECMCAD. (See, e.g., Agrawal, S., ed. (1996)  Antisense Therapeutics,  Humana Press Inc., Totawa N.J.)  
       [0213] In therapeutic use, any gene delivery system suitable for introduction of the antisense sequences into appropriate target cells can be used. Antisense sequences can be delivered intracellularly in the form of an expression plasmid which, upon transcription, produces a sequence complementary to at least a portion of the cellular sequence encoding the taret protein. (See, e.g., Slater, J. E. et al. (1998) J. Allergy Cli. Immunol. 102(3):469-475; and Scanlon, K. J. et al. (1995) 9(13): 1288-1296.) Antisense sequences can also be introduced intracellularly through the use of viral vectors, such as retrovirus and adeno-associated virus vectors. (See, e.g., Miller, A. D. (1990) Blood 76:271; Ausubel, supra; Uckert, W. and W. Walther (1994) Pharmacol. Ther. 63(3):323-347.) Other gene delivery mechanisms include liposome-derived systems, artificial viral envelopes, and other systems known in the alt. (See, e.g., Rossi, J. J. (1995) Br. Med. Bull. 51(1):217-225; Boado, R. J. et al. (1998) J. Pharm. Sci. 87(11):1308-1315; and Morris, M. C. et al. (1997) Nucleic Acids Res. 25(14):2730-2736.)  
       [0214] In another embodiment of the invention, polynucleotides encoding ECMCAD may be used for somatic or germline gene therapy. Gene therapy may be performed to (i) correct a genetic deficiency (e.g., in the cases of severe combined immunodeficiency (SCID)-X1 disease characterized by X-linked inheritance (Cavazzana-Calvo, M. et al. (2000) Science 288:669-672), severe combined immunodeficiency syndrome associated with an inherited adenosine deaminase (ADA) deficiency (Blaese, R. M. et al. (1995) Science 270:475-480; Bordignon. C. et al. (1995) Science 270:470-475), cystic fibrosis (Zabner, J. et al. (1993) Cell 75:207-216; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:643-666; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:667-703). thalassamias, familial hypercholesterolemia, and hemophilia resulting from Factor VIII or Factor IX deficiencies (Crystal, R. G. (1995) Science 270:404-410; Verma, I. M. and N. Somia (1997) Nature 389:239-242)), (ii) express a conditionally lethal gene product (e.g., in the case of cancers which result from unregulated cell proliferation), or (iii) express a protein which affords protection against intracellular parasites (e.g., against human retroviruses, such as human immunodeficiency virus (HIV) (Baltimore, D. (1988) Nature 335:395-396; Poeschla, E. et al. (1996) Proc. Natl. Acad. Sci. USA. 93:1 1395-11399), hepatitis B or C virus (HBV, HCV); fungal parasites, such as  Candida albicans  and  Paracoccidioides brasiliensis;  and protozoan parasites such as  Plasmodium falciparum  and  Trypanosoma cruzi ). In the case where a genetic deficiency in ECMCAD expression or regulation causes disease, the expression of ECMCAD from an appropriate population of transduced cells may alleviate the clinical manifestations caused by the genetic deficiency.  
       [0215] In a further embodiment of the invention, diseases or disorders caused by deficiencies in ECMCAD are treated by constructing mammalian expression vectors encoding ECMCAD and introducing these vectors by mechanical means into ECMCAD-deficient cells. Mechanical transfer technologies for use with cells in vivo or ex vitro include (i) direct DNA microinjection into individual cells, (ii) ballistic gold particle delivery, (iii) liposome-mediated transfection, (iv) receptor-mediated gene transfer, and (v) the use of DNA transposons (Morgan, R. A. and W. F. Anderson (1993) Annu. Rev. Biochem. 62:191-217; Ivics, Z. (1997) Cell 91:501-510; Boulay, J-L. and H. Récipon (1998) Curr. Opin. Biotechnol. 9:445-450).  
       [0216] Expression vectors that may be effective for the expression of ECMCAD include, but are not limited to, the PCDNA 3.1, EPITAG, PRCCMV2, PREP, PVAX vectors (Invitrogen, Carlsbad Calif.), PCMV-SCRIPT, PCMV-TAG, PEGSLYPERV (Stratagene, La Jolla Calif.), and PTET-OFF, PTET-ON, PTRE2, PTRE2-LUC, PTK-HYG (Clontech, Palo Alto Calif.). ECMCAD may be expressed using (i) a constitutively active promoter, (e.g., from cytomegalovirus (CMV), Rous sarcoma virus (RSV), SV40 virus, thymidine kinase (TK), or β-actin genes), (ii) an inducible promoter (e.g., the tetracycime-regulated promoter (Gossen, M. and H. Bujard (1992) Proc. Natl. Acad. Sci. USA 89:5547-5551; Gossen, M. et al. (1995) Science 268:1766-1769; Rossi, F. M. V. and H. M. Blau (1998) Curr. Opin. Biotechnol. 9:451-456), commercially available in the T-REX plasmid (Invitrogen)); the ecdysone-inducible promoter (available in the plasmids PVGRXR and PIND; Invitrogen); the FK506/rapamycin inducible promoter; or the RU486/mifepristone inducible promoter (Rossi, F. M. V. and Blau, H. M. supra)), or (iii) a tissue-specific promoter or the native promoter of the endogenous gene encoding ECMCAD from a normal individual.  
       [0217] Commercially available liposome transformation kits (e.g., the PERFECT LIPID TRANSFECTION KIT, available from Invitrogen) allow one with ordinary skill in the art to deliver polynucleotides to target cells in culture and require minimal effort to optimize experimental parameters. In the alternative, transformation is performed using the calcium phosphate method (Graham, F. L. and A. J. Eb (1973) Virology 52:456-467), or by electroporation (Neumann, E. et al. (1982) EMBO J. 1:841-845). The introduction of DNA to primary cells requires modification of these standardized mammalian transfection protocols.  
       [0218] In another embodiment of the invention, diseases or disorders caused by genetic defects with respect to ECMCAD expression are treated by constructing a retrovirus vector consisting of (i) the polynucleotide encoding ECMCAD under the control of an independent promoter or the retrovirus long terminal repeat (LTR) promoter, (ii) appropriate RNA packaging signals, and (iii) a Rev-responsive element (RRE) along with additional retrovirus cis-acting RNA sequences and coding sequences required for efficient vector propagation. Retrovirus vectors (e.g., PFB and PFBNEO) are commercially available (Stratagene) and are based on published data (Riviere, I. et al. (1995) Proc. Natl. Acad. Sci. USA 92:6733-6737), incorporated by reference herein. The vector is propagated in an appropriate vector producing cell line (VPCL) that expresses an envelope gene with a tropism for receptors on the target cells or a promiscuous envelope protein such as VSVg (Armentano. D. et al. (1987) J. Virol. 61:1647-1650; Bender, M. A. et al. (1987) J. Virol. 61:1639-1646; Adam, M. A. and A. D. Miller(I988) J. Virol. 62:3802-3806: Dull, T. et al. (1998) J. Virol. 72:8463-8471; Zufferey, R. et al. (1998) J. Virol. 72:9873-9880). U.S. Pat. No. 5,910,434 to Rigg (“Method for obtaining retrovirus packaging cell lines producing high transducing efficiency retroviral supernatant”) discloses a method for obtaining retrovirus packaging cell lines and is hereby incorporated by reference. Propagation of retrovirus vectors, transduction of a population of cells (e.g., CD4 +  T-cells), and the return of transduced cells to a patient are procedures well known to persons skilled in the art of gene therapy and have been well documented (Ranga, U. et al. (1997) J. Virol. 71:7020-7029; Bauer, G. et al. (1997) Blood 89:2259-2267; Bonyhadi, M. L. (1997) J. Virol. 71:47074716; Ranga, U. et al. (1998) Proc. Natl. Acad. Sci. USA 95:1201-1206; Su, L. (1997) Blood 89:2283-2290).  
       [0219] In the alternative, an adenovirus-based gene therapy delivery system is used to deliver polynucleotides encoding ECMCAD to cells which have one or more genetic abnormalities with respect to the expression of ECMCAD. The construction and packaging of adenovirus-based vectors are well known to those with ordinary skill in the art. Replication defective adenovirus vectors have proven to be versatile for importing genes encoding immunoregulatory proteins into intact islets in the pancreas (Csete, M. E. et al. (1995) Transplantation 27:263-268). Potentially useful adenoviral vectors are described in U.S. Pat. No. 5,707,618 to Armentano (“Adenoviius vectors for gene therapy”), hereby incorporated by reference. For adenoviral vectors, see also Antinozzi, P. A. et al. (1999) Annu. Rev. Nutr. 19:511-544 and Verma, I. M. and N. Somia (1997) Nature 18:389:239-242, both incorporated by reference herein.  
       [0220] In another alterative, a herpes-based, gene therapy delivery system is used to deliver polynucleotides encoding ECMCAD to target cells which have one or more genetic abnormalities with respect to the expression of ECMCAD. The use of herpes simplex virus (HSV)-based vectors may be especially valuable for introducing ECMCAD to cells of the central nervous system, for which HSV has a tropism. The construction and packaging of herpes-based vectors are well known to those with ordinary skill in the art. A replication-competent herpes simplex virus (HSV) type 1 -based vector has been used to deliver a reporter gene to the eyes of primates (Liu, X. et al. (1999) Exp. Eye Res. 169:385-395). The construction of a HSV-1 virus vector has also been disclosed in detail in U.S. Pat. No. 5,804,413 to DeLuca (“Herpes simplex virus strains for gene transfer”), which is hereby incorporated by reference. U.S. Pat. No. 5,804,413 teaches the use of recombinant HSV d92 which consists of a genome containing at least one exogenous gene to be transferred to a cell under the control of the appropriate promoter for purposes including human gene therapy. Also taught by this patent are the construction and use of recombinant HSV strains deleted for ICP4, ICP27 and ICP22. For HSV vectors, see also Goins, W. F. et al. (1999) J. Virol. 73:519-532 and Xu, H. et al. (1994) Dev. Biol. 163:152-161, hereby incorporated by reference. The manipulation of cloned herpesvirus sequences the generation of recombinant virus following the transfection of multiple plasmids containing different segments of the large herpesvirus genomes, the growth and propagation of herpesvirus, and the infection of cells with herpesvirus are techniques well known to those of ordinary skill in the art.  
       [0221] In another alternative, an alphavirus (positive, single-stranded RNA virus) vector is used to deliver polynucleotides encoding ECMCAD to target cells. The biology of the prototypic alphavirus, Semliki Forest Virus (SFV), has been studied extensively and gene transfer vectors have been based on the SFV genome (Garoff, H. and K.-J. Li (1998) Curr. Opin. Biotechnol. 9:464469). During alphavirus RNA replication, a subgenomic RNA is generated that normally encodes the viral capsid proteins. This subgenomic RNA replicates to higher levels than the full length genomic RNA, resulting in the overproduction of capsid proteins relative to the viral proteins with enzymatic activity (e.g., protease and polymerase). Similarly, inserting the coding sequence for ECMCAD into the alphavirus genome in place of the capsid-coding region results in the production of a large number of ECMCAD-coding RNAs and the synthesis of high levels of ECMCAD in vector transduced cells. While alphavirus infection is typically associated with cell lysis within a few days, the ability to establish a persistent infection in hamster normal kidney cells (BHK-21) with a variant of Sindbis virus (SET) indicates that the lytic replication of alphaviruses can be altered to suit the needs of the gene therapy application (Dryga, S. A. et al. (1997) Virology 228:74-83). The wide host range of alphaviruses will allow the introduction of ECMCAD into a variety of cell types. The specific transduction of a subset of cells in a population may require the sorting of cells prior to transduction. The methods of manipulating infectious cDNA clones of alphaviruses, performing alphavirus cDNA and RNA transfections, and performing alphavirus infections, are well known to those with ordinary skill in the art.  
       [0222] Oligonucleotides derived from the transcription initiation site, e.g., between about positions −10 and +10 from the start site, may also be employed to inhibit gene expression. Similarly, inhibition can be achieved using triple helix base-pairing methodology. Triple helix pairing is useful because it causes inhibition of the ability of the double helix to open sufficiently for the binding of polymerases, transcription factors, or regulatory molecules. Recent therapeutic advances using triplex DNA have been described in the literature. (See, e.g., Gee. J. E. et al. (1994) in Huber, B. E. and B. I. Carr,  Molecular and Immunologic Approaches,  Futura Publishing, Mt. Kisco N.Y., pp. 163-177.) A complementary sequence or antisense molecule may also be designed to block translation of mRNA by preventing the transcript from binding to ribosomes.  
       [0223] Ribozymes, enzymatic RNA molecules, may also be used to catalyze the specific cleavage of RNA. The mechanism of ribozyme action involves sequence-specific hybridization of the ribozyme molecule to complementary target RNA followed by endonucleolytic cleavage. For example, engineered hammerhead motif ribozyme molecules may specifically and efficiently catalyze endonucleolytic cleavage of sequences encoding ECMCAD.  
       [0224] Specific ribozyme cleavage sites within any potential RNA target are initially identified by scanning the target molecule for ribozyme cleavage sites, including the following sequences: GUA, GUU, and GUC. Once identified, short RNA sequences of between 15 and 20 ribonucleotides, corresponding to the region of the target gene containing the cleavage site, may be evaluated for secondary structural features which may render the oligonucleotide inoperable. The suitability of candidate targets may also be evaluated by testing accessibility to hybridization with complementary oligonucleotides using ribonuclease protection assays.  
       [0225] Complementary ribonucleic acid molecules and ribozymes of the invention may be prepared by any method known in the ant for the synthesis of nucleic acid molecules. These include techniques for chemically synthesizing oligonucleotides such as solid phase phosphoramidite chemical synthesis. Alternatively, RNA molecules may be generated by in vitro and in vivo transcription of DNA sequences encoding ECMCAD. Such DNA sequences may be incorporated into a wide variety of vectors with suitable RNA polymerase promoters such as T7 or SP6. Alternatively, these cDNA constructs that synthesize complementary RNA, constitutively or inducibly, can be introduced into cell lines, cells, or tissues.  
       [0226] RNA molecules may be modified to increase intracellular stability and half-life. Possible modifications include, but are not limited to, the addition of flanking sequences at the 5′ and/or 3′ ends of the molecule, or the use of phosphorothioate or 2′O-methyl rather than phospliodiesterase linkages within the backbone of the molecule. This concept is inherent in the production of PNAs and can be extended in all of these molecules by the inclusion of nontraditional bases such as inosine, queosine, and wybutosine, as well as acetyl-, methyl-, thio-, and similarly modified forms of adenine, cytidine, guanine, thymine, and uridine which are not as easily recognized by endogenous endonucleases.  
       [0227] An additional embodiment of the invention encompasses a method for screening for a compound which is effective in altering expression of a polynucleotide encoding ECMCAD. Compounds which may be effective in altering expression of a specific polynucleotide may include, but are not limited to, oligonucleotides, antisense oligonucleotides, triple helix-forming oligonucleotides. transcription factors and other polypeptide transcriptional regulators, and non-macromolecular chemical entities which are capable of interacting with specific polynucleotide sequences. Effective compounds may alter polynucleotide expression by acting as either inhibitors or promoters of polynucleotide expression. Thus, in the treatment of disorders associated with increased ECMCAD expression or activity, a compound which specifically inhibits expression of the polynucleotide encoding ECMCAD may be therapeutically useful, and in the treatment of disorders associated with decreased ECMCAD expression or activity, a compound which specifically promotes expression of the polynucleotide encoding ECMCAD may be therapeutically useful.  
       [0228] At least one, and up to a plurality, of test compounds may be screened for effectiveness in altering expression of a specific polynucleotide. A test compound may be obtained by any method commonly known in the art, including chemical modification of a compound known to be effective in altering polynucleotide expression; selection from an existing, commercially-available or proprietary library of naturally-occurring or non-natural chemical compounds; rational design of a compound based on chemical and/or structural properties of the target polynucleotide; and selection from a, library of chemical compounds created combinatorially or randomly. A sample comprising a polynucleotide encoding ECMCAD is exposed to at least one test compound thus obtained. The sample may comprise, for example, an intact or permeabilized cell, or an in vitro cellfree or reconstituted biochemical system. Alterations in the expression of a polynucleotide encoding ECMCAD are assayed by any method commonly known in the art. Typically, the expression of a specific nucleotide is detected by hybridization with a probe having a nucleotide sequence complementary to the sequence of the polynucleotide encoding ECMCAD. The amount of hybridization may be quantified, thus forming the basis for a comparison of the expression of the polynucleotide both with and without exposure to one or more test compounds. Detection of a change in the expression of a polynucleotide exposed to a test compound indicates that the test compound is effective in altering the expression of the polynucleotide. A screen for a compound effective in altering expression of a specific polynucleotide can be carried out, for example, using a  Schizosaccharomyces pombe  gene expression system (Atkins, D. et al. (1999) U.S. Pat. No. 5,932,435: Arndt, G. M. et al. (2000) Nucleic Acids Res. 28:E15) or a human cell line such as HeLa cell (Clarke, M. L. et al. (2000) Biochem. Biophys. Res. Commun. 268:8-13). A particular embodiment of the present invention involves screening a combinatorial library of oligonucleotides (such as deoxyribonucleotides, ribonucleotides, peptide nucleic acids, and modified oligonucleotides) for antisense activity against a specific polynucleotide sequence (Bruice, T. W. et al. (1997) U.S. Pat. No. 5,686,242; Bruice, T. W. et al. (2000) U.S. Pat. No. 6,022,691).  
       [0229] Many methods for introducing vectors into cells or tissues are available and equally suitable for use in vivo, in vitro, and ex vivo. For ex vivo therapy, vectors may be introduced into stem cells taken from the patient and clonally propagated for autologous transplant back into that same patient. Delivery by transfection, by liposome injections, or by polycationic amino pollers may be achieved using methods which are well known in the art. (See, e.g., Goldman, C. K. et al. (1997) Nat. Biotechnol. 15:462-466.)  
       [0230] Any of the therapeutic methods described above may be applied to any subject in need of such therapy, including, for example, mammals such as humans, dogs, cats, cows, horses, rabbits, and monkeys.  
       [0231] An additional embodiment of the invention relates to the administration of a composition which generally comprises an active ingredient formulated with a pharmaceutically acceptable excipient. Excipients may include, for example, sugars, starches, celluloses, gums, and proteins. Various formulations are commonly known and are thoroughly discussed in the latest edition of Remington&#39;s Pharmaceutical Sciences (Maack Publishing, Easton Pa.). Such compositions may consist of ECMCAD, antibodies to ECMCAD, and mimetics, agonists, antagonists, or inhibitors of ECMCAD.  
       [0232] The compositions utilized in this invention may be administered by any number of routes including, but not limited to, oral, intravenous, intramuscular, intra-aterial, intramedullaty, intrathecal, intravetitricular, pulmonary, transdermal, subcutaneous, intraperitoneal, intranasal, enteral, topical, sublingual, or rectal means.  
       [0233] Compositions for pulmonary administration may be prepared in liquid or dry powder form. These compositions are generally aerosolized immediately prior to inhalation by the patient. In the case of small molecules (e.g. traditional low molecular weight organic drugs), aerosol delivery of fast-acting formulations is well-known in the art. In the case of macromolecules (e.g. larger peptides and proteins), recent developments in the field of pulmonary delivery via the alveolar region of the lung have enabled the practical delivery of drugs such as insulin to blood circulation (see, e.g., Patton, J. S. et al., U.S. Pat. No. 5,997,848). Pulmonary delivery has the advantage of administration without needle injection, and obviates the need for potentially toxic penetration enhancers.  
       [0234] Compositions suitable for use in the invention include compositions wherein the active ingredients are contained in an effective amount to achieve the intended purpose. The determination of an effective dose is well within the capability of those skilled in the art.  
       [0235] Specialized forms of compositions may be prepared for direct intracellular delivery of macromolecules comprising ECMCAD or fragments thereof. For example, liposome preparations containing a cell-impermeable macromolecule may promote cell fusion and intracellular delivery of the macromolecule. Alternatively, ECMCAD or a fragment thereof may be joined to a short cationic N-terminal portion from the HIV Tat-1 protein. Fusion proteins thus generated have been found to transduce into the cells of all tissues, including the brain, in a mouse model system (Schwarze, S. R. et al (1999) Science 285:1569-1572).  
       [0236] For any compound, the therapeutically effective dose can be estimated initially either in cell culture assays, e.g., of neoplastic cells, or in animal models such as mice. rats, rabbits, dogs, monkeys, or pigs. An animal model may also be used to determine the appropriate concentration range and route of administration. Such information can then be used to determine useful doses and routes for administration in humans.  
       [0237] A therapeutically effective dose refers to that amount of active ingredient, for example ECMCAD or fragments thereof, antibodies of ECMCAD, and agonists, antagonists or inhibitors of ECMCAD, which ameliorates the symptoms or condition. Therapeutic efficacy and toxicity may be determined by standard pharmaceutical procedures in cell cultures or with experimental animals, such as by calculating the ED50 (the dose therapeutically effective in 50% of the population) or LD 50  (the dose lethal to 50% of the population) statistics. The dose ratio of toxic to therapeutic effects is the therapeutic index, which can be expressed as the LD 50 /ED 50  ratio. Compositions which exhibit large therapeutic indices are preferred. The data obtained from cell culture assays and animal studies are used to formulate a range of dosage for human use. The dosage contained in such compositions is preferably within a range of circulating concentrations that includes the ED 50  with little or no toxicity. The dosage varies within this range depending upon the dosage form employed the sensitivity of the patient, and the route of administration.  
       [0238] The exact dosage will be determined by the practitioner, in light of factors related to the subject requiring treatment. Dosage and administration are adjusted to provide sufficient levels of the active moiety or to maintain the desired effect. Factors which may be taken into account include the severity of the disease state, the general health of the subject, the age, weight, and gender of the subject, time and frequency of administration, drug combination(s), reaction sensitivities, and response to therapy. Long-acting compositions may be administered every 3 to 4 days, every week, or biweekly depending on the half-life and clearance rate of the particular formulation.  
       [0239] Normal dosage amounts may vary from about 0.1 μg to 100,000 μg, up to a total dose of about 1 gram, depending upon the route of administration. Guidance as to particular dosages and methods of delivery is provided in the literature and generally available to practitioners in the art. Those skilled in the art will employ different formulations for nucleotides than for proteins or their inhibitors. Similarly, delivery of polynucleotides or polypeptides will be specific to particular cells, conditions, locations, etc.  
       DIAGNOSTICS  
       [0240] In another embodiment, antibodies which specifically bind ECMCAD may be used for the diagnosis of disorders characterized by expression of ECMCAD, or in assays to monitor patients being treated with ECMCAD or agonists, antagonists, or inhibitors of ECMCAD. Antibodies useful for diagnostic purposes may be prepared in the same manner as described above for therapeutics. Diagnostic assays for ECMCAD include methods which utilize the antibody and a label to detect ECMCAD in human body fluids or in extracts of cells or tissues. The antibodies may be used with or without modification, and may be labeled by covalent or non-covalent attachment of a reporter molecule. A wide variety of reporter molecules, several of which are described above, are known in the art and may be used.  
       [0241] A variety of protocols for measuring ECMCAD, including ELISAs, RIAs, and FACS, are known in the art and provide a basis for diagnosing altered or abnormal levels of ECMCAD expression. Normal or standard values for ECMCAD expression are established by combining body fluids or cell extracts taken from normal mammalian subjects, for example, human subjects, with antibodies to ECMCAD under conditions suitable for complex formation. The amount of standard complex formation may be quantitated by various methods, such as photometric means. Quantities of ECMCAD expressed in subject, control, and disease samples from biopsied tissues are compared with the standard values. Deviation between standard and subject values establishes the parameters for diagnosing disease.  
       [0242] In another embodiment of the invention, the polynucleotides encoding ECMCAD may be used for diagnostic purposes. The polynucleotides which may be used include oligonucleotide sequences, complementary RNA and DNA molecules, and PNAs. The polynucleotides may be used to detect and quantify gene expression in biopsied tissues in which expression of ECMCAD may be correlated with disease. The diagnostic assay may be used to determine absence, presence, and excess expression of ECMCAD, and to monitor regulation of ECMCAD levels during therapeutic intervention.  
       [0243] In one aspect, hybridization with PCR probes which are capable of detecting polynucleotide sequences, including genomic sequences, encoding ECMCAD or closely related molecules may be used to identify nucleic acid sequences which encode ECMCAD. The specificity of the probe, whether it is made from a highly specific region, e.g., the 5′ regulatory region, or from a less specific region, e.g., a conserved motif, and the stringency of the hybridization or amplification will determine whether the probe identifies only naturally occurring sequences encoding ECMCAD, allelic variants, or related sequences.  
       [0244] Probes may also be used for the detection of related sequences, and may have at least 50% sequence identity to any of the ECMCAD encoding sequences. The hybridization probes of the subject invention may be DNA or RNA and may be derived from the sequence of SEQ ID NO:37-72 or from genomic sequences including promoters, enhancers, and introns of the ECMCAD gene.  
       [0245] Means for producing specific hybridization probes for DNAs encoding ECMCAD include the cloning of polynucleotide sequences encoding ECMCAD or ECMCAD derivatives into vectors for the production of mRNA probes. Such vectors are known in the art, are commercially available, and may be used to synthesize RNA probes in vitro by means of the addition of the appropriate RNA polymerases and the appropriate labeled nucleotides. Hybridization probes may be labeled by a variety of reporter groups, for example, by radionuclides such as  32 P or  35 S, or by enzymatic labels, such as alkaline phosphatase coupled to the probe via avidin/biotin coupling systems, and the like.  
       [0246] Polynucleotide sequences encoding ECMCAD may be used for the diagnosis of disorders associated with expression of ECMCAD. Examples of such disorders include, but are not limited to, a genetic disorder such as adrenoleukodystrophy, Alport&#39;s syndrome, choroideremia, Duchenne and Becker muscular dystrophy, Down&#39;s syndrome, cystic fibrosis, chronic granulomatous disease, Gaucher&#39;s disease, Huntington&#39;s chorea, Marfan&#39;s syndrome, muscular dystrophy, myotonic dystrophy, pycnodysostosis, Refsum&#39;s syndrome, retinoblastoma, sickle cell anemia, thalassenia, Werner syndrome., von Willebrand&#39;s disease, Wilms&#39; tumor, Zellweger syndrome, peroxisomal acyl-CoA oxidase deficiency, peroxisomal thiolase deficiency, peroxisomal bifunctional protein deficiency, mitochondrial carnitine palmitoyl transferase and carnitine deficiency, mitochondrial very-long-chain acyl-CoA dehydrogenase deficiency, mitochondrial medium-chain acyl-CoA dehydrogenase deficiency, mitochondrial short-chain acyl-CoA dehydrogenase deficiency, mitochondnial electron transport flavoprotein and electron transport flavoprotein:ubiquinone oxidoreductase deficiency, mitochondrial trifunctional protein deficiency, and mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency; an immune/inflammatory disorder such as acquired immunodeficiency syndrome (AIDS), X-linked agammaglobinemia of Bruton, common variable immunodeficiency (CVI), DiGeorge&#39;s syndrome (thymic hypoplasia), thynic dysplasia, isolated IgA deficiency, severe combined immunodeficiency disease (SCID), immunodeficiency with thrombocytopenia and eczema (Wiskott-Aldrich syndrome), Chediak-Higashi syndrome, chronic granulomatous diseases, hereditary angioneurotic edema, immunodeficiency associated with Cushing&#39;s disease, Addison&#39;s disease, adult respiratory distress syndrome, allergies, ankrylosing spondylitis, amyloidosis, anemia, asthma, atherosclerosis, autoimmune hemolytic anemia, autoimmune thyroiditis, autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED), bronchitis, cholecystitis, contact dermatitis, Crohn&#39;s disease, atopic dermatitis, dermatomyositis, diabetes mellitus, emphysema, episodic lymphopenia with lymuphocytotoxins, erythoblastosis fetalis, erythema nodosum, atrophic gastritis, glomerulonephritis, Goodpasture&#39;s syndrome, gout, Graves&#39; disease, Hashimoto&#39;s thyroiditis, hypereosinophilia, irritable bowel syndrome, multiple sclerosis, myasthenia gravis, myocardial or pericardial inflammation, osteoarthritis, osteoporosis, pancreatitis, polymyositis, psoriasis, Reiter&#39;s syndrome, rheumatoid arthritis, scleroderma, Sjogren&#39;s syndrome, systemic anaphylaxis, systemic lupus erythematosus, systemic sclerosis, thrombocytopenia puipura, ulcerative colitis, uveitis, Werner syndrome, complications of cancer, hemodialysis, and extracorporeal circulation, viral, bacterial, fungal, parasitic, protozoal, and helminthic infections, and trauma; a developmental disorder such as renal tubular acidosis, anemia, Cushing&#39;s syndrome, achondroplastic dwarfism, Duchenne and Becker muscular dystrophy, epilepsy, gonadal dysgenesis, WAGR syndrome (Wilms&#39; tumor, anriridia, geritourinary abnornalities, and mental retardation), Smith-Magenis syndrome, myelodysplastic syndrome, hereditary mucoepithelial dysplasia, hereditary keratodermas, hereditary neuropathies such as Charcot-Marie-Tooth disease and neurofibromatosis, hypothyroidism, hydrocephalus, seizure disorders such as Syndenham&#39;s chorea and cerebral palsy, spina bifida, anelncephaly, craniorachischisis, congenital glaucoma, cataract, and sensorineural hearing loss; a neurological disorder such as epilepsy, ischemic cerebrovascular disease, stroke, cerebral neoplasms, Alzheimer&#39;s disease, Pick&#39;s disease, Huntington&#39;s disease, dementia, Parkinson&#39;s disease and other extrapyramidal disorders, amyotrophic lateral sclerosis and other motor neuron disorders, progressive neural muscular atrophy, retinitis pigmentosa, hereditary ataxias, multiple sclerosis and other demyelinating diseases, bacterial and viral meningitis, brain abscess, subdural empyema, epidural abscess, suppurative intracranial thrombopwlebitis, myelitis and radiculitis, viral central nervous system disease, prion diseases including kuru, Creutzfeldt-Jakob disease, and Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, nutritional and metabolic diseases of the nervous system, neurofibromatosis, tuberous sclerosis, cerebelloretinal hemangioblastomatosis, encephalotigerinal syndrome, mental retardation and other developmental disorders of the central nervous system including Down syndrome, cerebral palsy, neuroskeletal disorders, autonomic nervous system disorders, cranial nerve disorders, spinal cord diseases, muscular dystrophy and other neuromuscular disorders, peripheral nervous system disorders, dermatomyositis and polymyositis, inherited, metabolic, endocrine, and toxic myopathies, myasthenia gravis, periodic paralysis, mental disorders including mood, anxiety, and schizophrenic disorders, seasonal affective disorder (SAD), akathesia, amnesia, catatonia, diabetic neuropathy, tardive dyskinesia, dystonias, paranoid psychoses, postherpetic neuralgia, Tourette&#39;s disorder, progressive supranuclear palsy, coilticobasal degeneration, and familial frontotemporal dementia; a connective tissue disorder such as osteogenesis imperfecta, Ehlers-Danlos syndrome, chondrodysplasias, Marfan syndrome, Alport syndrome, familial aortic aneurysm, achondroplasia, mucopolysaccharidoses, osteoporosis, osteopetrosis, Paget&#39;s disease, rickets, osteomalacia, hyperparathyroidism, renal osieodystrophy, osteonecrosis, osteomyelitis, osteoma, osteoid osteoma, osteoblastoma, osteosarcoma, osteochondroma, chondroma, chondroblastoma, chondromyxoid fibroma, chondrosarcoma, fibrous cortical defect, nonossifying fibroma, fibrous dysplasia, fibrosarcoma, malignant fibrous histiocetoma, Ewing&#39;s sarcoma, primitive neuroectodermal tumor, giant cell tumor, osteoartbritis, rheumatoid arthritis, ankylosing spondyloartluitis, Reiter&#39;s syndrome, psoriatic arthritis, enteropathic arthritis, infectious arthritis, gout, gouty arthritis, calcium pyrophosphate crystal deposition disease, ganglion, synovial cyst, villonodular synovitis, systemic sclerosis, Dupuytren&#39;s contracture, hepatic fibrosis, lupus erythematosus, mixed connective tissue disease, epidermolysis bullosa simplex, bullous congenital ichthyosiform eiythrodenna (epidermolytic hyperkeratosis), non-epidermlolytic and epidermolytic palmoplantar keratoderma, ichthyosis bullosa of Siemens, pachyonychia congenita, and white sponge nevus; and a cell proliferative disorder such as actinic keratosis, arteriosclerosis, atherosclerosis, bursitis, cirrhosis, hepatitis, mixed connective tissue disease (MCTD), myelofibrosis, paroxysmal nocturnal hemoglobinuria, polycytheinia vera, psoriasis, primary thrombocythemia, and cancers including adenocarcinoma, leukemia, lymphoma, melanoma, myeloma, sarcoma, teratocarcinoma, and, in particular, cancers of the adrenal gland, bladder, bone, bone marrow, brain, breast, cervix, gall bladder, ganglia, gastrointestinal tract, heart, kidney, liver, lung, muscle, ovary, pancreas, parathyroid, penis, prostate, salivary glands, skin, spleen, testis, thymus, thyroid, and uterus. The polynucleotide sequences encoding ECMCAD may be used in Southern or northern analysis, dot blot, or other membrane-based technologies; in PCR technologies; in dipstick, pin, and multiformat ELISA-like assays; and in microarrays utilizing fluids or tissues from patients to detect altered ECMCAD expression. Such qualitative or quantitative methods are well known in the art.  
       [0247] In a particular aspect, the nucleotide sequences encoding ECMCAD may be useful in assays that detect the presence of associated disorders, particularly those mentioned above. The nucleotide sequences encoding ECMCAD may be labeled by standard methods and added to a fluid or tissue sample from a patient under conditions suitable for the formation of hybridization complexes. After a suitable incubation period, the sample is washed and the signal is quantified and compared with a standard value. If the amount of signal in the patient sample is significantly altered in comparison to a control sample then the presence of altered levels of nucleotide sequences encoding ECMCAD in the sample indicates the presence of the associated disorder. Such assays may also be used to evaluate the efficacy of a particular therapeutic treatment regimen in animal studies, in clinical trials, or to monitor the treatment of an individual patient.  
       [0248] In order to provide a basis for the diagnosis of a disorder associated with expression of ECMCAD, a normal or standard profile for expression is established. This may be accomplished by combining body fluids or cell extracts taken from normal subjects, either animal or human, with a sequence, or a fragment thereof, encoding ECMCAD, under conditions suitable for hybridization or amplification. Standard hybridization may be quantified by comparing the values obtained from normal subjects with values from an experiment in which a known amount of a substantially purified polynucleotide is used. Standard values obtained in this manner may be compared with values obtained from samples from patients who are symptomatic for a disorder. Deviation from standard values is used to establish the presence of a disorder.  
       [0249] Once the presence of a disorder is established and a treatment protocol is initiated, hybridization assays may be repeated on a regular basis to determine if the level of expression in the patient begins to approximate that which is observed in the normal subject. The results obtained from successive assays may be used to show the efficacy of treatment over a period ranging from several days to months.  
       [0250] With respect to cancer, the presence of an abnormal amount of transcript (either under- or overexpressed) in biopsied tissue from an individual may indicate a predisposition for the development of the disease, or may provide a means for detecting the disease prior to the appearance of actual clinical symptoms. A more definitive diagnosis of this type may allow health professionals to employ preventative measures or aggressive treatment earlier thereby preventing the development or further progression of the cancer.  
       [0251] Additional diagnostic uses for oligonucleotides designed from the sequences encoding ECMCAD may involve the use of PCR. These oligomers may be chemically synthesized, generated enzymatically, or produced in vitro. Oligomers will preferably contain a fragment of a polynucleotide encoding ECMCAD, or a fragment of a polynucleotide complementary to the polynucleotide encoding ECMCAD, and will be employed under optimized conditions for identification of a specific gene or condition. Oligomers may also be employed under less stringent conditions for detection or quantification of closely related DNA or RNA sequences.  
       [0252] In a particular aspect, oligonucleotide primers derived from the polynucleotide sequences encoding ECMCAD may be used to detect single nucleotide polytheism (SNPs). SNPs are substitutions, insertions and deletions that are a frequent cause of inherited or acquired genetic disease in humans. Methods of SNP detection include, but are not limited to, single-stranded conformation polymorphism (SSCP) and fluorescent SSCP (fSSCP) methods. In SSCP, oligonucleotide primers derived from the polynucleotide sequences encoding ECMCAD are used to amplify DNA using the polymerase chain reaction (PCR). The DNA may be derived, for example, from diseased or normal tissue, biopsy samples, bodily fluids, and the like. SNPs in the DNA cause differences in the secondary and tertiary structures of PCR products in single-stranded form, and these differences are detectable using gel electrophoresis in non-denaturing gels. In fSCCP, the oligonucleotide primers are fluorescently labeled, which allows detection of the amplifiers in high-throughput equipment such as DNA sequencing machines. Additionally, sequence database analysis methods, termed in silico SNP (isSNP), are capable of identifying polymorphisms by comparing the sequence of individual overlapping DNA fragments which assemble into a common consensus sequence. These computer-based methods filter out sequence variations due to laboratory preparation of DNA and sequencing errors using statistical models and automated analyses of DNA sequence chromatogram. In the alterative. SNPs may be detected and characterized by mass spectrometry using, for example, the high throughput MASSARRAY system (Sequenom, Inc., San Diego Calif.).  
       [0253] Methods which may also be used to quantify the expression of ECMCAD include radiolabeling or biotinylating nucleotides, coamplification of a control nucleic acid, and interpolating results from standard curves. (See, e.g., Melby, P. C. et al. (1993) J. Immunol. Methods 159:235-244; Duplaa, C. et al. (1993) Anal. Biochem. 212:229-236.) The speed of quantitation of multiple samples may be accelerated by running the assay in a high-throughput format where the oligomer or polynucleotide of interest is presented in various dilutions and a spectrophotometic or calorimetric response gives rapid quantitation.  
       [0254] In further embodiments, oligonucleotides or longer fragments derived from any of the polynucleotide sequences described herein may be used as elements on a microarray. The microarray can be used in transcript imaging techniques which monitor the relative expression levels of large numbers of genes simultaneously as described below. The microarray may also be used to identify genetic variants, mutations, and polymorphisms. This information may be used to determine gene function, to understand the genetic basis of a disorder, to diagnose a disorder, to monitor progression/regression of disease as a function of gene expression, and to develop and monitor the activities of therapeutic agents in the treatment of disease. In particular, this information may be used to develop a pharmacogenomic profile of a patient in order to select the most appropriate and effective treatment regimen for that patient. For example, therapeutic agents which are highly effective and display the fewest side effects may be selected for a patient based on his/her pharmacogenomic profile.  
       [0255] In another embodiment, ECMCAD, fragments of ECMCAD, or antibodies specific for ECMCAD may be used as elements on a microarray. The microarray may be used to monitor or measure protein-protein interactions, drug-target interactions, and gene expression profiles, as described above.  
       [0256] A particular embodiment relates to the use of the polynucleotides of the present invention to generate a transcript image of a tissue or cell type. A transcript image represents the global pattern of gene expression by a particular tissue or cell type. Global gene expression patterns are analyzed by quantifying the number of expressed genes and their relative abundance under given conditions and at a given time. (See Seilhamer et al., “Comparative Gene Transcript Analysis,” U.S. Pat. No. 5,840,484, expressly incorporated by reference herein.) Thus a transcript image may be generated by hybridizing the polynucleotides of the present invention or their complements to the totality of transcripts or reverse transcripts of a particular tissue or cell type. In one embodiment, the hybridization takes place in high-throughput format, wherein the polynucleotides of the present invention or their complements comprise a subset of a plurality of elements on a microarray. The resultant transcript image would provide a profile of gene activity.  
       [0257] Transcript images may be generated using transcripts isolated from tissues, cell lines, biopsies, or other biological samples. The transcript image may thus reflect gene expression in vivo, as in the case of a tissue or biopsy sample, or in vitro, as in the case of a cell line.  
       [0258] Transcript images which profile the expression of the polynucleotides of the present invention may also be used in conjunction with in vitro model systems and preclinical evaluation of pharmaceuticals, as well as toxicological testing of industrial and naturally-occurring environmental compounds. All compounds induce characteristic gene expression patterns, frequently termed molecular fingerprints or toxicant signatures, which are indicative of mechanisms of action and toxicity (Nuwaysir, E. F. et al. (1999) Mol. Carcinog. 24:153-159; Steiner, S. and N. L. Anderson (2000) Toxicol. Lett. 112-113:467-471, expressly incorporated by reference herein). If a test compound has a signature similar to that of a compound with known toxicity, it is likely to share those toxic properties. These fingerprints or signatures are most useful and refined when they contain expression information from a large number of genes and gene families. Ideally, a genome-wide measurement of expression provides the highest quality signature. Even genes whose expression is not altered by any tested compounds are important as well, as the levels of expression of these genes are used to normalize the rest of the expression data. The normalization procedure is useful for comparison of expression data after treatment with different compounds. While the assignment of gene function to elements of a toxicant signature aids in interpretation of toxicity mechanisms, knowledge of gene function is not necessary for the statistical matching of signatures which leads to prediction of toxicity. (See, for example, Press Release 00-02 from the National Institute of Environmental Health Sciences, released Feb. 29, 2000, available at http://www.niehs.nii.gov/oc/news/toxchip.htm.) Therefore, it is important and desirable in toxicological screening using toxicant signatures to include all expressed gene sequences.  
       [0259] In one embodiment, the toxicity of a test compound is assessed by treating a biological sample containing nucleic acids with the test compound. Nucleic acids that are expressed in the treated biological sample are hybridized with one or more probes specific to the polynucleotides of the present invention, so that transcript levels corresponding to the polynucleotides of the present invention may be quantified. The transcript levels in the treated biological sample are compared with levels in an untreated biological sample. Differences in the transcript levels between the two samples are indicative of a toxic response caused by the test compound in the treated sample.  
       [0260] Another particular embodiment relates to the use of the polypeptide sequences of the present invention to analyze the proteome of a tissue or cell type. The term proteome refers to the global pattern of protein expression in a particular tissue or cell type. Each protein component of a proteome can be subjected individually to further analysis. Proteome expression patterns, or profiles, are analyzed by quantifying the number of expressed proteins and their relative abundance under given conditions and at a given time. A profile of a cell&#39;s proteome may thus be generated by separating and analyzing the polypeptides of a particular tissue or cell type. In one embodiment, the separation is achieved using two-dimensional gel electropholesis, in which proteins from a sample are separated by isoelectric focusing in the first dimension, and then according to molecular weight by sodium dodecyl sulfate slab gel electrophoresis in the second dimension (Steiner and Anderson, supra). The proteins are visualized in the gel as discrete and uniquely positioned spots, typically by staining the gel with an agent such as Coomassie Blue or silver or fluorescent stains. The optical density of each protein spot is generally proportional to the level of the protein in the sample. The optical densities of equivalently positioned protein spots from different samples, for example, from biological samples either treated or untreated with a test compound or therapeutic agent, are compared to identify any changes in protein spot density related to the treatment. The proteins in the spots are partially sequenced using, for example, standard methods employing chemical or enzymatic cleavage followed by mass spectrometry. The identity of the protein in a spot may be determined by compating its partial sequence, preferably of at least 5 contiguous amino acid residues, to the polypeptide sequences of the present invention. In some cases, further sequence data may be obtained for definitive protein identification.  
       [0261] A proteornic profile may also be generated using antibodies specific for ECMCAD to quantify the levels of ECMCAD expression. In one embodiment, the antibodies are used as elements on a microarray, and protein expression levels are quantified by exposing the microarray to the sample and detecting the levels of protein bound to each array element (Lueking, A. et al. (1999) Anal. Biochem. 270:103-111; Mendoze, L. G. et al. (1999) Biotechniques 27:778-788). Detection may be performed by a variety of methods known in the art, for example, by reacting the proteins in the sample with a thiol- or amino-reactive fluorescent compound and detecting the amount of fluorescence bound at each array clement.  
       [0262] Toxicant signatures at the proteome level are also useful for toxicological screening, and should be analyzed in parallel with toxicant signatures at the transcript level. There is a poor correlation between transcript and protein abundances for some proteins in some tissues (Anderson, N. L. and J. Seilhamer (1997) Electrophoresis 18:533-537), so proteome toxicant signatures may be useful in the analysis of compounds which do not significantly affect the transcript image, but which alter the proteotic profile. In addition, the analysis of transcripts in body fluids is difficult, due to rapid degradation of mRNA, so proteomic profiling may be more reliable and informative in such cases.  
       [0263] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins that are expressed in the treated biological sample are separated so that the amount of each protein can be quantified. The amount of each protein is compared to the amount of the corresponding protein in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample. Individual proteins are identified by sequencing the amino acid residues of the individual proteins and comparing these partial sequences to the polypeptides of the present invention.  
       [0264] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins from the biological sample are incubated with antibodies specific to the polypeptides of the present invention. The amount of protein recognized by the antibodies is quantified. The amount of protein in the treated biological sample is compared with the amount in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample.  
       [0265] Microarrays may be prepared, used, and analyzed using methods known in the art. (See, e.g., Brennan, T. M. et al. (1995) U.S. Pat. No. 5,474,796; Schena, M. et al. (1996) Proc. Natl. Acad. Sci. USA 93:10614-10619; Baldeschweiler et al. (1995) PCT application WO95/251116; Shalon, D. et al. (1995) PCT application WO95/35505; Heller, R. A. et al. (1997) Proc. Natl. Acad. Sci. USA 94:2150-2155; and Heller, M. J. et al. (1997) U.S. Pat. No. 5,605,662.) Various types of microarrays are well known and thoroughly described in DNA Microarrays: A Practical Approach, M. Schena, ed. (1999) Oxford University Press, London, hereby expressly incorporated by reference.  
       [0266] In another embodiment of the invention, nucleic acid sequences encoding ECMCAD may be used to generate hybridization probes useful in mapping the naturally occurring genomic sequence. Either coding or noncoding sequences may be used, and in some instances, noncoding sequences may be preferable over coding sequences. For example, conservation of a coding sequence among members of a multi-gene family may potentially cause undesired cross hybridization during chromosomal mapping. The sequences may be mapped to a particular chromosome, to a specific region of a chromosome, or to artificial chromosome constructions, e.g., human artificial chromosomes (HACs), yeast artificial chromosomes (YACs), bacterial artificial chromosomes (BACs), bacterial P1 constructions, or single chromosome cDNA libraries. (See, e.g., Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355; Price, C. M. (1993) Blood Rev. 7:127-134; and Trask, B. J. (1991) Trends Genet. 7:149-154.) Once mapped, the nucleic acid sequences of the invention may be used to develop genetic linkage maps, for example, which correlate the inheritance of a disease state with the inheritance of a particular chromosome region or restiction fragment length polymorphism (RFLP). (See, for example, Lander, E. S. and D. Botstein (1986) Proc. Natl. Acad. Sci. USA 83:7353-7357.)  
       [0267] Fluorescent in situ hybridization (FISH) may be correlated with other physical and genetic map data. (See, e.g., Heinz-Ulrich, et al. (1995) in Meyers, supra, pp. 965-968.) Examples of genetic map data can be found in various scientific journals or at the Online Mendelian Inheritance in Man (OMIM) World Wide Web site. Correlation between the location of the gene encoding ECMCAD on a physical map and a specific disorder, or a predisposition to a specific disorder, may help define the region of DNA associated with that disorder and thus may further positional cloning efforts. In situ hybridization of chromosomal preparations and physical mapping techniques, such as linkage analysis using established chromosomal markers, may be used for extending genetic maps. Often the placement of a gene on the chromosome of another mammalian species, such as mouse, may reveal associated markers even if the exact chromosomal locus is not known. This information is valuable to investigators searching for disease genes using positional cloning or other gene discovery techniques. Once the gene or genes responsible for a disease or syndrome have been crudely localized by genetic linkage to a particular genomic region, e.g., ataxia-telangiectasia to 11q22-23, any sequences mapping to that area may represent associated or regulatory genes for further investigation (See, e.g., Gatti, R. A. et al. (1988) Nature 336:577-580.) The nucleotide sequence of the instant invention may also be used to detect differences in the chromosomal location due to translocation, inversion, etc., among normal, carrier, or affected individuals.  
       [0268] In another embodiment of the invention, ECMCAD, its catalytic or immunogenic fragments, or oligopeptides thereof can be used for screening libraries of compounds in any of a variety of drug screening techniques. The fragment employed in such screening may be free in solution, affixed to a solid support, borne on a cell surface, or located intracellularly. The formation of binding complexes between ECMCAD and the agent being tested may be measured.  
       [0269] Another technique for drug screening provides for high throughput screening of compounds having suitable binding affinity to the protein of interest. (See, e.g., Geysen, et al. (1984) PCT application WO84/03564.) In this method, large numbers of different small test compounds are synthesized on a solid substrate. The test compounds are reacted with ECMCAD, or fragments thereof, and washed. Bound ECMCAD is then detected by methods well known in the art. Purified ECMCAD can also be coated directly onto plates for use in the aforementioned drug screening techniques. Alternatively, non-neutralizing antibodies can be used to capture the peptide and immobilize it on a solid support.  
       [0270] In another embodiment, one may use competitive drug screening assays in which neutralizing antibodies capable of binding ECMCAD specifically compete with a test compound for binding ECMCAD. In this manner, antibodies can be used to detect the presence of any peptide which shares one or more antigenic determinants with ECMCAD.  
       [0271] In additional embodiments, the nucleotide sequences which encode ECMCAD may be used in any molecular biology techniques that have yet to be developed, provided the new techniques rely on properties of nucleotide sequences that are currently known, including, but not limited to, such properties as the triplet genetic code and specific base pair interactions.  
       [0272] Without further elaboration, it is believed that one skilled in the art can, using the preceding description, utilize the present invention to its fullest extent. The following embodiments are, therefore, to be construed as merely illustrative, and not limitative of the remainder of the disclosure in any way whatsoever.  
       [0273] The disclosures of all patents, applications, and publications mentioned above and below, including U.S. Ser. No. 60/215,454, U.S. Ser. No. 60/219,462, U.S. Ser. No. 60/240,111, U.S. Ser. No. 60/240,106, U.S. Ser. No. 60/244,021, U.S. Ser. No. 60/248,887, and U.S. Ser. No. 60/249,570 are hereby expressly incorporated by reference. 
     
    
    
     EXAMPLES  
     I. Construction of cDNA Libraries  
     [0274] Incyte cDNAs were derived from cDNA libraries described in the LIFESEQ GOLD database (Incyte Genomics, Palo Alto Calif.) and shown in Table 4, column 5. Some tissues were homogenized and lysed in guanidimiuin isothiocyanate, while others were homogenized and lysed in phenol or in a suitable mixture of denaturants, such as TRIZOL (Life Technologies), a monophasic solution of phenol and guanidine isothiocyanate. The resulting lysates were centrifuged over CsCl cushions or extracted with chloroform. RNA was precipitated from the lysates with either isopropanol or sodium acetate and ethanol, or by other routine methods.  
     [0275] Phenol extraction and precipitation of RNA were repeated as necessary to increase RNA purity. In some cases, RNA was treated with DNase. For most libraries, poly(A)+RNA was isolated using oligo d(T)-coupled paramagnetic particles (Promega), OLIGOTEX latex particles (QIAGEN, Chatsworth Calif.), or an OLIGOTEX mRNA purification kit (QIAGEN). Alternatively, RNA was isolated directly from tissue lysates using other RNA isolation kits, e.g., the POLY(A)PURE mRNA purification kit (Ambion, Austin Tex.).  
     [0276] In some cases, Stratagene was provided with RNA and constructed the corresponding cDNA libraries. Otherwise, cDNA was synthesized and cDNA libraries were constructed with the UNIZAP vector system (Stratagene) or SUPERSCRIPT plasmid system (Life Technologies), using the recommended procedures or similar methods known in the art. (See, e.g., Ausubel, 1997, supra, units 5.1-6.6.) Reverse transcription was initiated using oligo d(T) or random primers. Synthetic oligonucleotide adapters were ligated to double stranded cDNA, and the cDNA was digested with the appropriate restriction enzyme or enzymes. For most libraries, the cDNA was size-selected (300-1000 bp) using SEPHACRYL S1000, SEPHAROSE CL2B, or SEPHAROSE CL4B column chromatography (Amersham Pharmacia Biotech) or preparative agarose gel electrophoresis. cDNAs were ligated into compatible restriction enzyme sites of the polylinker of a suitable plasmid, e.g., PBLUESCRIPT plasmid (Stratagene), PSPORT1 plasmid (Life Technologies), PCDNA2.1 plasmid (Invitrogen, Carlsbad Calif.), PBK-CMV plasmid (Stratagene), or pINCY (Incyte Genomics, Palo Alto Calif.), or derivatives thereof. Recombinant plasmids were transformed into competent  E. coli  cells including XL1-Blue, XL1-BlueMRF, or SOLR from Stratagene or DH5α, DH10B, or ElectroMAX DH10 B from Life Technologies.  
     II. Isolation of cDNA Clones  
     [0277] Plasmnids obtained as described in Example I were recovered from host cells by in vivo excision using the UNIZAP vector system (Stratagene) or by cell lysis. Plasmids were purified using at least one of the following: a Magic or WIZARD Minipreps DNA purification system (Promega); an AGTC Miniprep purification kit (Edge Biosystems, Gaithersburg Md.); and QIAWELL 8 Plasmid, QIAWELL 8 Plus Plasmid, QIAWELL 8 Ultra Plasmid purification systems or the R.E.A.L. PREP 96 plasmid purification kit from QIAGEN. Following precipitation, plasmids were resuspended in 0.1 ml of distilled water and stored, with or without lyophilization, at 4° C.  
     [0278] Alternatively, plasmid DNA was amplified from host cell lysates using direct link PCR in a high-throughput format (Rao, V. B. (1994) Anal. Biochem. 216:1-14). Host cell lysis and thermal cycling steps were carried out in a single reaction mixture. Samples were processed and stored in 384-well plates, and the concentration of amplified plasmid DNA was quantified fluorometrically using PICOGREEN dye (Molecular Probes, Eugene Oreg.) and a FLUOROSKAN II fluorescence scanner (Labsystems Oy, Helsinki, Finland).  
     III. Sequencing and Analysis  
     [0279] Incyte cDNA recovered in plasmids as described in Example II were sequenced as follows. Sequencing reactions were processed using standard methods or high-throughput instrumentation such as the ABI CATALYST 800 (Applied Biosystems) thermal cycler or the PTC-200 thermal cycler (MJ Research) in conjunction with the HYDRA microdispenser (Robbins Scientific) or the MICROLAB 2200 (Hamilton) liquid transfer system. cDNA sequencing reactions were prepared using reagents provided by Amersham Pharmacia Biotech or supplied in ABI sequencing kits such as the ABI PRISM BIGDYE Terminator cycle sequencing ready reaction kit (Applied Biosystems). Electrophoretic separation of cDNA sequencing reactions and detection of labeled polynucleotides were carried out using the MEGABACE 1000 DNA sequencing system (Molecular Dynamics); the ABI PRISM 373 or 377 sequencing system (Applied Biosystems) in conjunction with standard ABI protocols and base calling software; or other sequence analysis systems known in the art. Reading frames within the cDNA sequences were identified using standard methods (reviewed in Ausubel, 1997, supra, unit 7.7). Some of the cDNA sequences were selected for extension using the techniques disclosed in Example VIII.  
     [0280] The polynucleotide sequences derived from Incyte cDNAs were validated by removing vector, linker, and poly(A) sequences and by masking ambiguous bases, using algorithms and programs based on BLAST, dynamic programming, and dinucleotide nearest neighbor analysis. The Incyte cDNA sequences or translations thereof were then queried against a selection of public databases such as the GenBank primate, rodent, mammalian, vertebrate, and eukaryote databases, and BLOCKS, PRINTS, DOMO, PRODOM, and hidden Markov model (HMM)-based protein family databases such as PFAM. (HMM is a probabilistic approach which analyzes consensus primary structures of gene families. See, for example, Eddy, S. R. (1996) Curr. Opin. Struct. Biol. 6:361-365.) The queries were performed using programs based on BLAST, FASTA, BLIMPS, and HMMER. The Incyte cDNA sequences were assembled to produce full length polynucleotide sequences. Alternatively, GenBank cDNAs, GenBank ESTs, stitched sequences, stretched sequences, or Genscan-predicted coding sequences (see Examples IV and V) were used to extend Incyte cDNA assemblages to full length. Assembly was performed using programs based on Phred, Phrap, and Consed, and cDNA assemblages were screened for open reading frames using programs based on GeneMark, BLAST, and FASTA. The full length polynucleotide sequences were translated to derive the corresponding full length polypeptide sequences. Alternatively, a polypeptide of the invention may begin at any of the methionine residues of the full length translated polypeptide. Full length polypeptide sequences were subsequently analyzed by querying against databases such as the Genank protein databases (genpcpt), SwissProt, BLOCKS, PRINTS, DOMO, PRODOM, Prosite, and hidden Markov model (HMM)-based protein family databases such as PFAM. Full length polynucleotide sequences are also analyzed using MACDNASIS PRO software (Hitachi Software Engineering, South San Francisco Calif.) and LASERGENE software (DNASTAR). Polynucleotide and polypeptide sequence alignments are generated using default parameters specified by the CLUSTAL algorithm as incorporated into the MEGALIGN multisequence alignment program (DNASTAR), which also calculates the percent identity between aligned sequences.  
     [0281] Table 7 summarizes the tools, programs, and algorithms used for the analysis and assembly of Incyte cDNA and full length sequences and provides applicable descriptions, references, and threshold parameters. The first column of Table 7 shows the tools, programs, and algorithms used, the second column provides brief descriptions thereof, the third column presents appropriate references, all of which are incorporated by reference herein in their entirety, and the fourth column presents, where applicable, the scores, probability values, and other parameters used to evaluate the strength of a match between two sequences (the higher the score or the lower the probability value, the greater the identity between two sequences).  
     [0282] The programs described above for the assembly and analysis of full length polynucleotide and polypeptide sequences wore also used to identify polynucleotide sequence fragments from SEQ ID NO:37-72 Fragments from about 20 to about 4000 nucleotides which are useful in hybridization and amplification technologies are described in Table 4, column 4.  
     IV. Identification and Editing of Coding Sequences from Genomic DNA  
     [0283] Putative extracellular matrix and cell adhesion molecules were initially identified by running the Genscan gene identification program against public genomic sequence databases (e.g., gbpri and gbhtg). Genscan is a general-purpose gene identification program which analyzes genomic DNA sequences from a variety of organisms (See Burge, C. and S. Karlin (1997) J. Mol. Biol. 268:78-94, and Burge, C. and S. Karlin (1998) Curr. Opin. Struct. Biol. 8:346-354). The program concatenates predicted exons to form an assembled cDNA sequence extending from a methionine to a stop codoe The output of Genscan is a FASTA database of polynucleotide and polypeptide sequences. The maximum range of sequence for Genscan to analyze at once was set to 30 kb. To determine which of these Genscan predicted cDNA sequences encode extracellular matrix and cell adhesion molecules, the encoded polypeptides were analyzed by querying against PFAM models for extracellular matrix and cell adhesion molecules. Potential extracellular matrix and cell adhesion molecules were also identified by homology to Incyte cDNA sequences that had been annotated as extracellular matrix and cell adhesion molecules. These selected Genscan-predicted sequences were then compared by BLAST analysis to the genpept and gbpri public databases. Where necessary, the Genscan-predicted sequences wore then edited by comparison to the top BLAST hit from genpept to correct errors in the sequence predicted by Genscan, such as extra or omitted exons. BLAST analysis was also used to find any Incyte cDNA or public cDNA coverage of the Genscan-predicted sequences, thus providing evidence for transcription. When Incyte cDNA coverage was available, this information was used to correct or confirm the Genscan predicted sequence. Full length polynucleotide sequences were obtained by assembling Genscan-predicted coding sequences with Incyte cDNA sequences and/or public cDNA sequences using the assembly process described in Example III. Alternatively, full length polynucleotide sequences were derived entirely from edited or unedited Genscan-predicted coding sequences.  
     V. Assembly of Genomic Sequence Data with cDNA Sequence Data  
     “Stitched” Sequences  
     [0284] Partial cDNA sequences were extended with exons predicted by the Genscan gene identification program described in Example IV. Partial cDNAs assembled as described in Example III were mapped to genomic DNA and parsed into clusters containing related cDNAs and Genscan exon predictions from one or more genomic sequences. Each cluster was analyzed using an algorithm based on graph theory and dynamic programming to integrate cDNA and genomic information, generating possible splice variants that were subsequently confirmed, edited, or extended to create a full length sequence. Sequence intervals in which the entire length of the interval was present on more than one sequence in the cluster were identified, and intervals thus identified were considered to be equivalent by transitivity. For example, if an interval was present on a cDNA and two genomic sequences, then all three intervals were considered to be equivalent. This process allows unrelated but consecutive genomic sequences to be brought together, bridged by cDNA sequence. Intervals thus identified were then “stitched” together by the stitching algorithm in the order that they appear along their parent sequences to generate the longest possible sequence, as well as sequence variants. Linkages between intervals which proceed along one type of parent sequence (cDNA to cDNA or genomic sequence to genomic sequence) were given preference over linkages which change parent type (cDNA to genomic sequence). The resultant stitched sequences were translated and compared by BLAST analysis to the genpept and gbpri public databases. Incorrect exons predicted by Genscan were corrected by comparison to the top BLAST hit from genpept. Sequences were farther extended with additional cDNA sequences, or by inspection of genomic DNA, when necessary.  
     “Stretched” Sequences  
     [0285] Partial DNA sequences were extended to full length with an algorithm based on BLAST analysis. First, partial cDNAs assembled as described in Example III were queried against public databases such as the GenBank primate, rodent, mammalian, vertebrate, and cukaryote databases using the BLAST program. The nearest GenBank protein homolog was then compared by BLAST analysis to either Incyte cDNA sequences or GenScan exon predicted sequences described in Example IV. A chimeric protein was generated by using the resultant high-scoring segment pairs (HSPs) to map the translated sequences onto the GenBank protein homolog. Insertions or deletions may occur in the chimeric protein with respect to the original GenBank protein homolog. The GenBank protein homolog, the chimeric protein, or both were used as probes to search for homologous genomic sequences from the public human genome databases. Partial DNA sequences were therefore “stretched” or extended by the addition of homologous genomic sequences. The resultant stretched sequences were examined to determine whether it contained a complete gene.  
     VI. Chromosomal Mapping of ECMCAD Encoding Polynucleotides  
     [0286] The sequences which were used to assemble SEQ ID NO:37-72 were compared with sequences from the Incyte LIFESEQ database and public domain databases using BLAST and other implementations of the Smith-Waterman algorithm. Sequences from these databases that matched SEQ ID NO:37-72 were assembled into clusters of contiguous and overlapping sequences using assembly algorithms such as Phrap (Table 7). Radiation hybrid and genetic mapping data available from public resources such as the Stanford Human Genome Center (SHGC), Whitehead Institute for Genome Research (WIGR), and Généthon were used to determine if any of the clustered sequences had been previously mapped. Inclusion of a mapped sequence in a cluster resulted in the assignment of all sequences of that cluster, including its particular SEQ ID NO:, to that map location.  
     [0287] Map locations are represented by ranges, or intervals, of human chromosomes. The map position of an interval, in centiMorgans, is measured relative to the terminus of the chromosome&#39;s p-arm. (The centiMorgan (cM) is a unit of measurement based on recombination frequencies between chromosomal markers. On average, 1 cM is roughly equivalent to 1 megabase (Mb) of DNA in humans, although this can vary widely due to hot and cold spots of recombination.) The cM distances are based on genetic markers mapped by Ginethon which provide boundaries for radiation hybrid markers whose sequences were included in each of the clusters. Human genome maps and other resources available to the public, such as the NCBI “GeneMap&#39;99” World Wide Web site (http://www.ncbi.nlm.nih.gov/genemap/), can be employed to determine if previously identified disease genes map within or in proximity to the intervals indicated above.  
     [0288] In this manner, SEQ ID NO:47 was mapped to chromosome 3 within the interval from 162.00 to 168.30 centiMorgans. SEQ ID NO:49 was mapped to chromosome 4 within the interval from 63.90 to 88.50 centiMorgans.  
     VII. Analysis of Polynucleotide Expression  
     [0289] Northern analysis is a laboratory technique used to detect the presence of a transcript of a gene and involves the hybridization of a labeled nucleotide sequence to a membrane on which RNAs from a particular cell type or tissue have been bound. (See, e.g., Sambrook, supra, ch. 7; Ausubel (1995) supra, ch. 4 and 16.)  
     [0290] Analogous computer techniques applying BLAST were used to search for identical or related molecules in cDNA databases such as GenBank or LIFESEQ (Incyte Genomics). This analysis is much faster than multiple membrane-based hybridizations. In addition, the sensitivity of the computer search can be modified to determine whether any particular match is categorized as exact or similar. The basis of the search is the product score, which is defined as:  
         BLAST                 Score   ×   Percent                 Identity       5   ×   minimum                   {       length        (     Seq   .              1     )       ,     length        (     Seq   .              2     )         }                     
 
     [0291] The product score takes into account both the degree of similarity between two sequences and the length of the sequence match. The product score is a normalized value between 0 and 100, and is calculated as follows: the BLAST score is multiplied by the percent nucleotide identity and the product is divided by (5 times the length of the shorter of the two sequences). The BLAST score is calculated by assigning a score of +5 for every base that matches in a high-scoring segment pair (HSP), and 4 for every mismatch. Two sequences may share more than one HSP (separated by gaps). If there is more than one HSP, then the pair with the highest BLAST score is used to calculate the product score. The product score represents a balance between fractional overlap and quality in a BLAST alignment. For example, a product score of 100 is produced only for 100% identity over the entire length of the shorter of the two sequences being compared. A product score of 70 is produced either by 100% identity and 70% overlap at one end, or by 88% identity and 100% overlap at the other. A product score of 50 is produced either by 100% identity and 50% overlap at one end, of 79% identity and 100% overlap.  
     [0292] Alternatively, polynucleotide sequences encoding ECMCAD are analyzed with respect to the tissue sources from which they were derived. For example, some full length sequences are assembled, at least in part, with overlapping Incyte cDNA sequences (see Example III). Each cDNA sequence is derived from a cDNA library constructed from a human tissue. Each human tissue is classified into one of the following organ/tissue categories: cardiovascular system; connective tissue; digestive system; embryonic structures; endocrine system; exocrine glands; genitalia, female; genitalia, male; germ cells; hemic and immune system; liver; musculoskeletal system; nervous system; pancreas; respiratory system; sense organs; skin; stomatognathic system; unclassified/mixed; or urinary tract. The number of libraries in each category is counted and divided by the total number of libraries across all categories. Similarly, each human tissue is classified into one of the following disease/condition categories: cancer, cell line, developmental, inflammation, neurological, trauma, cardiovascular, pooled, and other, and the number of libraries in each category is counted and divided by the total number of libraries across all categories. The resulting percentages reflect the tissue- and disease-specific expression of cDNA encoding ECMCAD. cDNA sequences and cDNA library/tissue information are found in the LIFESEQ GOLD database (Incyte Genomics, Palo Alto Calif.).  
     VIII. Extension of ECMCAD Encoding Polynucleotides  
     [0293] Full length polynucleotide sequences were also produced by extension of an appropriate fragment of the full length molecule using oligonucleotide primers designed from this fragment. One primer was synthesized to initiate 5′ extension of the known fragment, and the other primer was synthesized to initiate 3′ extension of the known fragment. The initial primers were designed using OLIGO 4.06 software (National Biosciences), or another appropriate program, to be about 22 to 30 nucleotides in length, to have a GC content of about 50% or more, and to anneal to the target sequence at temperatures of about 68° C. to about 72° C. Any stretch of nucleotides which would result in hairpin structures and primer-primer dimerizations was avoided.  
     [0294] Selected human cDNA libraries were used to extend the sequence. If more than one extension was necessary or desired, additional or nested sets of primers were designed.  
     [0295] High fidelity amplification was obtained by PCR using methods well known in the art. PCR was performed in 96-well plates using the PTC-200 thermal cycler (MJ Research, Inc.). The reaction mix contained DNA template, 200 nmol of each primer, reaction buffer containing Mg 2+ , (NH 4 ) 2 SO 4 , and 2-mercaptoethanol, Taq DNA polymerase (Amersham Pharmacia Biotech), ELONGASE enzyme (Life Technologies), and Pfu DNA polymerase (Stratagene), with the following parameters for primer pair PCI A and PCI B: Step 1: 94° C., 3 nin; Step 2: 94° C., 15 sec; Step 3: 60° C., 1 min; Step 4: 68° C., 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C. In the alternative, the parameters for primer pair T7 and SK+ were as follows: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 57° C., 1 min; Step 4: 68° C., 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C.  
     [0296] The concentration of DNA in each well was determined by dispensing 100 μl PICOGREEN quantitation reagent (0.25% (v/v) PICOGREEN; Molecular Probes, Eugene Oreg.) dissolved in 1×TE and 0.5 μl of undiluted PCR product into each well of an opaque fluorimeter plate (Corning Costar, Acton Mass.), allowing the DNA to bind to the reagent. The plate was scanned in a Fluoroskan II (Labsystems Oy, Helsinki, Finland) to measure the fluorescence of the sample and to quantify the concentration of DNA. A 5 μl to 10 μl aliquot of the reaction mixture was analyzed by electrophoresis on a 1% agarose gel to detemine which reactions were successful in extending the sequence.  
     [0297] The extended nucleotides were desalted and concentrated, transferred to 384-well plates, digested with CviJI cholera virus endonuclease (Molecular Biology Research, Madison Wis.), and sonicated or sheared prior to relegation into pUC 18 vector (Amersham Pharmacia Biotech). For shotgun sequencing, the digested nucleotides were separated on low concentration (0.6 to 0.8%) agarose gels, fragments were excised, and agar digested with Agar ACE (Promega). Extended clones were religated using T4 ligase (New England Biolabs, Beverly Mass.) into pUC 18 vector (Amersham Pharmacia Biotech), treated with Pfu DNA polymerase (Stratagene) to fill-in restriction site overhangs, and transfected into competent  E. coli  cells. Transformed cells were selected on antibiotic-containing media, and individual colonies were picked and cultured overnight at 37° C. in 384-well plates in LB/2×carb liquid media.  
     [0298] The cells were lysed, and DNA was amplified by PCR using Taq DNA polymerase (Amersham Pharmacia Biotech) and Pfu DNA polymerase (Stratagene) with the following parameters: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 60° C., 1 min; Step 4: 72° C., 2 min; Step 5: steps 2, 3, and 4 repeated 29 times; Step 6: 72° C., 5 min; Step 7: storage at 4° C. DNA was quantified by PICOGREEN reagent (Molecular Probes) as described above. Samples with low DNA recoveries were reamplified using the same conditions as described above. Samples were diluted with 20% dimethysulfoxide (1:2, v/v), and sequenced using DYENAMIC energy transfer sequencing primers and the DYENAMIC DIRECT kit (Amersham Pharmacia Biotech) or the ABI PRISM BIGDYE Trminator cycle sequencing ready reaction kit (Applied Biosystems).  
     [0299] In like manner, full length polynucleotide sequences are verified using the above procedure or are used to obtain 5 regulatory sequences using the above procedure along with oligonucleotides designed for such extension, and an appropriate genomic library.  
     IX. Labeling and Use of Individual Hybridization Probes  
     [0300] Hybridization probes derived from SEQ ID NO:37-72 are employed to screen cDNAs, gelioulic DNAs, or mRNAs. Although the labeling of oligonicleotides, consisting of about 20 base pairs, is specifically described, essentially the same procedure is used with larger nucleotide fragments. Oligonucleotides are designed using state-of-the-art software such as OLIGO 4.06 software (National Bioscicnces) and labeled by combining 50 pmol of each oligomer, 250 μCi of [γ- 32 P] adenosine tiphosphate (Amersham Pharmacia Biotech), and T4 polynucleotide kinase (DuPont NEN, Boston Mass.). The labeled oligonucleotides are substantially purified using a SEPHADEX G-25 superfine size exclusion dextran bead column (Amersham Pharmacia Biotech). An aliquot containing 10 7  counts per minute of the labeled probe is used in a typical membrane-based hybridization analysis of human genomic DNA digested with one of the following endonucleases: Ase I, Bgl II, Eco RI, Pst I, Xba I, or Pvu II (DuPont NEN).  
     [0301] The DNA from each digest is fractionated on a 0.7% agarose gel and transferred to nylon membranes (Nytran Plus, Schleicher &amp; Schuell, Durham N.H.). Hybridization is carried out for 16 hours at 40° C. To remove nonspecific signals, blots are sequentially washed at room temperature under conditions of up to, for example, 0.1× saline sodium citrate and 0.5% sodium dodecyl sulfate. Hybridization patterns are visualized using autoradiography or an alternative imaging means and compared.  
     X. Microarrays  
     [0302] The linkage or synthesis of array elements upon a microarray can be achieved utilizing photolithography, piezoelectric printing (ink-jet printing, See, e.g., Baldeschweiler, supra.), mechanical microspotting technologies, and derivatives thereof. The substrate in each of the aforementioned technologies should be uniform and solid with a non-porous surface (Schena (1999), supra). Suggested substrates include silicon, silica, glass slides, glass chips, and silicon wafers. Alternatively, a procedure analogous to a dot or slot blot may also be used to arrange and link elements to the surface of a substrate using thermal, UV, chemical, or mechanical bonding procedures. A typical array may be produced using available methods and machines well known to those of ordinary skill in the art and may contain any appropriate number of elements. (See, e.g., Schena, M. et al. (1995) Science 270:467-470; Shalon, D. et al. (1996) Genome Res. 6:639-645; Marshall, A. and J. Hodgson (1998) Nat. Biotechnol. 16:27-31.)  
     [0303] Full length cDNAs, Expressed Sequence Tags (ESTs), or fragments or oligomers thereof may comprise the elements of the microarray. Fragments or oligomers suitable for hybridization can be selected using software well known in the art such as LASERGENE software (DNASTAR). The array elements are hybridized with polynucleotides in a biological sample. The polynucleotides in the biological sample are conjugated to a fluorescent label or other molecular tag for ease of detection. After hybridization, nonhybridized nucleotides from the biological sample are removed, and a fluorescence scanner is used to detect hybridization at each array element. Alternatively, laser desorption and mass spectrometry may be used for detection of hybridization. The degree of complementarity and the relative abundance of each polynucleotide which hybridizes to an element on the microarray may be assessed. In one embodiment, microarray preparation and usage is described in detail below.  
     Tissue or Cell Sample Preparation  
     [0304] Total RNA is isolated from tissue samples using the guanidinium thiocyanate method and poly(A) + RNA is purified using the oligo-(dT) cellulose method. Each poly(A) + RNA sample is reverse transcribed using MMLV reverse-transcriptase, 0.05 pg/μl oligo-(dT) primer (21mer), 1×first strand buffer, 0.03 units/μl RNase inhibitor, 500 μM dATP, 500 μM dGTP, 500 μM dTTP, 40 μM dCTP, 40 μM dCTP-Cy3 (BDS) or dCTP-Cy5 (Amersham Pharmacia Biotech). The reverse transcription reaction is performed in a 25 ml volume containing 200 ng poly(A) + RNA with GEMBRIGHT kits (Incyte). Specific control poly(A) + RNAs are synthesized by in vitro transcription from non-coding yeast genomic DNA. After incubation at 37° C. for 2 hr, each reaction sample (one with Cy3 and another with Cy5 labeling) is treated with 2.5 ml of 0.5M sodium hydroxide and incubated for 20 minutes at 85° C. to the stop the reaction and degrade the RNA. Samples are purified using two successive CHROMA SPIN 30 gel filtration spin columns (CLONTECH Laboratories, Inc. (CLONTECH), Palo Alto Calif.) and after combining, both reaction samples are ethanol precipitated using 1 ml of glycogen (1 mg/ml), 60 ml sodium acetate, and 300 ml of 100% ethanol. The sample is then dried to completion using a SpeedVAC (Savant Instruments Inc., Holbrook N.Y.) and resuspended in 14 μl 5×SSC/0.2% SDS.  
     Microarray Preparation  
     [0305] Sequences of the present invention are used to generate array elements. Each array element is amplified from bacterial cells containing vectors with cloned cDNA inserts. PCR amplification uses primers complementary to the vector sequences flanking the cDNA insert. Array elements are amplified in thirty cycles of PCR from an initial quantity of 1-2 ng to a final quantity greater than 5 μg. Amplified array elements are then purified using SEPHACRYL400 (Amersham Pharmacia Biotech).  
     [0306] Purified array elements are immobilized on polymer-coated glass slides. Glass microscope slides (Corning) are cleaned by ultrasound in 0.1% SDS and acetone, with extensive distilled water washes between and after treatments. Glass slides are etched in 4% hydroIluoric acid (VWR Scientific Products Corporation (VWR), West Chester Pa.), washed extensively in distilled water, and coated with 0.05% aminopropyl silane (Sigma) in 95% ethanol. Coated slides are cured in a 110° C. oven.  
     [0307] Array elements are applied to the coated glass substrate using a procedure described in U.S. Pat. No. 5,807,522, incorporated herein by reference. 1 μl of the array element DNA, at an average concentration of 100 ng/μl, is loaded into the open capillary printing element by a high-speed robotic apparatus. The apparatus then deposits about 5 nl of array element sample per slide.  
     [0308] Microarrays are UV-crosslinked using a STRATALINKER UV-crosslinker (Stratagene). Microarrays are washed at room temperature once in 0.2% SDS and three times in distilled water. Non-specific binding sites are blocked by incubation of microarrays in 0.2% casein in phosphate buffered saline (PBS) (Tropix, Inc., Bedford Mass.) for 30 minutes at 60° C. followed by washes in 0.2% SDS and distilled water as before.  
     Hybridization  
     [0309] Hybridization reactions contain 9 μl of sample mixture consisting of 0.2 μg each of Cy3 and Cy5 labeled cDNA synthesis products in 5×SSC, 0.2% SDS hybridization buffer. The sample mixture is heated to 65° C. for 5 minutes and is aliquoted onto the microarray surface and covered with an 1.8 cm 2  coverslip. The arrays are transferred to a waterproof chamber having a cavity just slightly larger than a microscope slide. The chamber is kept at 100% humidity internally by the addition of 140 μl of 5×SSC in a corner of the chamber. The chamber containing the arrays is incubated for about 6.5 hours at 60° C. The arrays are washed for 10 min at 45° C. in a first wash buffer (1×SSC, 0.1% SDS), three times for 10 minutes each at 45° C. in a second wash buffer (0.1×SSC), and dried.  
     Detection  
     [0310] Reporter-labeled hybridization complexes are detected with a microscope equipped with an Innova 70 mixed gas 10 W laser (Coherent, Inc., Santa Clara Calif.) capable of generating spectral lines at 488 nm for excitation of Cy3 and at 632 nm for excitation of Cy5. The excitation laser light is focused on the array using a 20× microscope objective (Nikon, Inc., Melville N.Y.). The slide containing the array is placed on a computer-controlled X-Y stage on the microscope and raster-scanned past the objective. The 1.8 cm×1.8 cm array used in the present example is scanned with a resolution of 20 micrometers.  
     [0311] In two separate scans, a mixed gas multiline laser excites the two fluorophores sequentially. Emitted light is split, based on wavelength, into two photomultiplier tube detectors (PMT R1477, Hamamatsu Photonics Systems, Bridgewater N.J.) corresponding to the two fluorophores. Appropriate filters positioned between the array and the photomultiplier tubes are used to filter the signals. The emission maxima of the fluorophores used are 565 nm for Cy3 and 650 nm for Cy5. Each array is typically scanned twice, one scan per fluorophore using the appropriate filters at the laser source, although the apparatus is capable of recording the spectra from both fluorophores simultaneously.  
     [0312] The sensitivity of the scans is typically calibrated using the signal intensity generated by a cDNA control species added to the sample mixture at a known concentration. A specific location on the array contains a complementary DNA sequence, allowing the intensity of the signal at that location to be correlated with a weight ratio of hybridizing species of 1:100,000. When two samples from different sources (e.g., representing test and control cells), each labeled with a different fluorophore, are hybridized to a single array for the purpose of identifying genes that are differentially expressed, the calibration is done by labeling samples of the calibrating cDNA with the two fluorophores and adding identical amounts of each to the hybridization mixture.  
     [0313] The output of the photomultiplier tube is digitized using a 12-bit RTI-835H analog-to-digital (A/D) conversion board (Analog Devices, Inc., Norwood Mass.) installed in an IBM-compatible PC computer. The digitized data are displayed as an image where the signal intensity is mapped using a linear 20-color transformation to a pseudocolor scale ranging from blue (low signal) to red (high signal). The data is also analyzed quantitatively. Where two different fluorophores are excited and measured simultaneously, the data are first corrected for optical crosstalk (due to overlapping emission spectra) between the fluorophores using each fluorophore&#39;s emission spectrum.  
     [0314] A grid is superimposed over the fluorescence signal image such that the signal from each spot is centered in each element of the grid. The fluorescence signal within each element is then integrated to obtain a numerical value corresponding to the average intensity of the signal. The software used for signal analysis is the GEMTOOLS gene expression analysis program (Incyte).  
     XI. Complementary Polynucleotides  
     [0315] Sequences complementary to the ECMCAD-encoding sequences, or any parts thereof, are used to detect, decrease, or inhibit expression of naturally occurring ECMCAD. Although use of oligonucleotides comprising from about 15 to 30 base pairs is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonucleotides are designed using OLIGO 4.06 software (National Biosciences) and the coding sequence of ECMCAD. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5′ sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent ribosomal binding to the ECMCAD-encoding transcript.  
     XII. Expression of ECMCAD  
     [0316] Expression and purification of ECMCAD is achieved using bacterial or vitus-based expression systems. For expression of ECMCAD in bacteria, cDNA is subcloned into an appropriate vector containing an antibiotic resistance gene and an inducible promoter that directs high levels of cDNA transcription. Examples of such promoters include, but are not limited to, the trp-lac (tac) hybrid promoter and the T5 or T7 bacteriophage promoter in conjunction with the lac operator regulatory element. Recombinant vectors are transformed into suitable bacterial hosts, e.g., BL21(DE3). Antibiotic resistant bacteria express ECMCAD upon induction with isopropyl beta-D-thiogalactopyranoside (IPTG). Expression of ECMCAD in eukaryotic cells is achieved by infecting insect or mammalian cell lines with recombinant  Autographica californica  nuclear polyhedrosis virus (AcMNPV), commonly known as baculovirus. The nonessential polyhedrin gene of baculovirus is replaced with cDNA encoding ECMCAD by either homologous recombination or bacterial-mediated transposition involving transfer plasmid intermediates. Viral infectivity is maintained and the strong polyhedrin promoter drives high levels of cDNA transcription. Recombinant baculovirus is used to infect  Spodoptera frugiperda  (Sf9) insect cells in most cases, or human hepatocytes, in some cases. Infection of the latter requires additional genetic modifications to baculovirus. (See Engelhard, E. K. et al. (1994) Proc. Natl. Acad. Sci. USA 91:3224-3227; Sandig, V. et al. (1996) Hum. Gene Ther. 7:1937-1945.)  
     [0317] In most expression systems, ECMCAD is synthesized as a fusion protein with, e.g., glutathione S-transferase (GST) or a peptide epitope tag, such as FLAG or 6-His, permitting rapid, single-step, affinity-based purification of recombinant fusion protein from crude cell lysates. GST, a 26-kilodalton enzyme from  Schistosoma japonicum,  enables the purification of fusion proteins on immobilized glutathione under conditions that maintain protein activity and antigenicity (Amersham Pharmacia Biotech). Following purification, the GST moiety can be proteolytically cleaved from ECMCAD at specifically engineered sites. FLAG, an 8-amino acid peptide, enables immunoaffinity purification using commercially available monoclonal and polyclonal anti-FLAG antibodies (Eastman Kodak). 6-His, a stretch of six consecutive histidine residues, enables purification on metal-chelate resins (QIAGEN). Methods for protein expression and purification are discussed in Ausubel (1995, supra, ch. 10 and 16). Purified ECMCAD obtained by these methods can be used directly in the assays shown in Examples XVI and XVI where applicable.  
     XIII. Functional Assays  
     [0318] ECMCAD function is assessed by expressing the sequences encoding ECMCAD at physiologically elevated levels in mammalian cell culture systems. cDNA is subcloned into a mammalian expression vector containing a strong promoter that drives high levels of cDNA expression. Vectors of choice include PCMV SPORT (Life Technologies) and PCR3.1 (Invitrogen, Carlsbad Calif.), both of which contain the cytomegalovirus promoter. 5-10 μg of recombinant vector are transiently transfected into a human cell line, for example, an endothelial or hematopoietic cell line, using either liposome formulations or electroporation. 1-2 μg of an additional plasmid containing sequences encoding a marker protein are co-transfected. Expression of a marker protein provides a means to distinguish transfected cells from nontransfected cells and is a reliable predictor of cDNA expression from the recombinant vector. Marker proteins of choice include, e.g., Green Fluorescent Protein (GFP; Clontech), CD64, or a CD64-GFP fusion protein. Flow cytometry (FCM), an automated, laser optics-based technique, is used to identify transfected cells expressing GFP or CD64-GFP and to evaluate the apoptotic state of the cells and other cellular properties. FCM detects and quantifies the uptake of fluorescent molecules that diagnose events preceding or coincident with cell death. These events include changes in nuclear DNA content as measured by staining of DNA with propidium iodide; changes in cell size and granularity as measured by forward light scatter and 90 degree side light scatter; down-regulation of DNA synthesis as measured by decrease in bromodeoxyuridine uptake; alterations in expression of cell surface and intracellular proteins as measured by reactivity with specific antibodies; and alterations in plasma membrane composition as measured by the binding of fluorescein-conjugated Annexin V protein to the cell surface. Methods in flow cytometry are discussed in Ormerod, M. G. (1994)  Flow Cytometry,  Oxford, New York N.Y.  
     [0319] The influence of ECMCAD on gene expression can be assessed using highly purified populations of cells transfected with sequences encoding ECMCAD and either CD64 or CD64-GFP. CD64 and CD64-GFP are expressed on the surface of transfected cells and bind to conserved regions of human immunoglobulin G (IgG). Transfected cells are efficiently separated from nontransfected cells using magnetic heads coated with either human IgG or antibody against CD64 (DYNAL, Lake Success N.Y.). mRNA can be purified from the cells using methods well known by those of skill in the art. Expression of mRNA encoding ECMCAD and other genes of interest can be analyzed by northern analysis or microarray techniques.  
     XIV. Production of ECMCAD Specific Antibodies  
     [0320] ECMCAD substantially purified using polyacrylamide gel electrophoresis (PAGE; see, e.g., Harrington. M. G. (1990) Methods Enzymol. 182:488-495), or other purification techniques, is used to immunize rabbits and to produce antibodies using standard protocols.  
     [0321] Alternatively, the ECMCAD amino acid sequence is analyzed using LASERGENE software (DNASTAR) to detentine regions of high immunogenicity, and a corresponding oligopeptide is synthesized and used to raise antibodies by means known to those of skill in the art. Methods for selection of appropriate epitopes, such as those near the C-terminus or in hydrophilic regions are well described in the art. (See, e.g., Ausubel, 1995, supra, ch. 11.)  
     [0322] Typically, oligopeptides of about 15 residues in length are synthesized using an ABI 431 A peptide synthesizer (Applied Biosystems) using FMOC chemistry and coupled to KLH (Sigma-Aldrich, St. Louis Mo.) by reaction with N-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS) to increase immunogenicity. (See, e.g., Ausubel, 1995, supra.) Rabbits are immunized with the oligopeptide-KLH complex in complete Freund&#39;s adjuvant. Resulting antisera are tested for antipeptide and anti-ECMCAD activity by, for example, binding the peptide or ECMCAD to a substrate, blocking with 1% BSA, reacting with rabbit antisera, washing, and reacting with radio-iodinated goat anti-rabbit IgG.  
     XV. Purification of Naturally Occurring ECMCAD Using Specific Antibodies  
     [0323] Naturally occurring or recombinant ECMCAD is substantially purified by immunoaffinity chromatography using antibodies specific for ECMCAD. An immunoaffinity column is constructed by covalently coupling anti-ECMCAD antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer&#39;s instructions.  
     [0324] Media containing ECMCAD are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of ECMCAD (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/ECMCAD binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate ion), and ECMCAD is collected.  
     XVI. Identification of Molecules Which Interact with ECMCAD  
     [0325] ECMCAD, or biologically active fragments thereof, are labeled with  125 Bolton-Hunter reagent. (See, e.g., Bolton A. E. and W. M. Hunter (1973) Biochem. J. 133:529-539.) Candidate molecules previously arrayed in the wells of a multi-well plate are incubated with the labeled ECMCAD, washed, and any wells with labeled ECMCAD complex are assayed. Data obtained using different concentrations of ECMCAD are used to calculate values for the number, affinity, and association of ECMCAD with the candidate molecules.  
     [0326] Alternatively, molecules interacting with ECMCAD are analyzed using the yeast two-hybrid system as described in Fields, S. and O. Song (1989) Nature 340:245-246, or using commercially available kits based on the two-hybrid system, such as the MATCHMAKER system (Clontech).  
     [0327] ECMCAD may also be used in the PATHCALLING process (CuraGen Corp., New Haven Conn.) which employs the yeast two-hybrid system in a high-throughput manner to determine all interactions between the proteins encoded by two large libraries of genes (Nandabalan, K. et al. (2000) U.S. Pat. No. 6,057,101).  
     XVII. Demonstration of ECMCAD Activity  
     [0328] An assay for ECMCAD activity measures the expression of ECMCAD on the cell surface. cDNA encoding ECMCAD is transfected into a non-leukocytic cell line. Cell surface proteins are labeled with biotin (de la Fuente, M. A. et al. (1997) Blood 90:2398-2405). Immunoprecipitations are performed using ECMCAD-specific antibodies, and immunoprecipitated samples are analyzed using SDS-PAGE and immunoblotting techniques. The ratio of labeled immunoprecipitant to unlabeled immunoprecipitant is proportional to the amount of ECMCAD expressed on the cell surface.  
     [0329] Alternatively, an assay for ECMCAD activity measures the amount of cell aggregation induced by overexpression of ECMCAD. In this assay, cultured cells such as NIH3T3 are transfected with cDNA encoding ECMCAD contained within a suitable mammalian expression vector under control of a strong promoter. Cotransfection with cDNA encoding a fluorescent marker protein, such as Green Fluorescent Protein (CLONTECH), is useful for identifying stable transfectants. The amount of cell agglutination, or clumping, associated with transfected cells is compared with that associated with untransfected cells. The amount of cell agglutination is a direct measure of ECMCAD activity.  
     [0330] Alternatively, an assay for ECMCAD activity measures the disruption of cytoskeletal filament networks upon overexpression of ECMCAD in cultured cell lines (Rezniczek, G. A. et al. (1998) J. Cell Biol. 141:209-225). cDNA encoding ECMCAD is subcloned into a mammalian expression vector that drives high levels of cDNA expression. This construct is transfected into cultured cells, such as rat kangaroo PtK2 or rat bladder carcinoma 804G cells. Actin filaments and intermediate filaments such as keratin and vimentin are visualized by immunofluorescence microscopy using antibodies and techniques well known in the art. The configuration and abundance of cyoskeletal filaments can be assessed and quantified using confocal imaging techniques. In particular, the bundling and collapse of cytoskeletal filament networks is indicative of ECMCAD activity.  
     [0331] Alternatively, cell adhesion activity in ECMCAD is measured in a 96-well microtiter assay in which wells are first coated with ECMCAD by adding solutions of ECMCAD of varying concentrations to the wells. Excess ECMCAD is washed off with saline, and the wells incubated with a solution of 1% bovine serum albumin to block non-specific cell binding. Aliquots of a cell suspension of a suitable cell type are then added to the microtiter wells and incubated for a period of time at 37° C. Non-adhered cells are washed off with saline and the cells stained with a suitable cell stain such as Coomassie blue. The intensity of staining is measured using a variable wavelength microtiter plate reader and compared to a standard curve to determine the number of cells adhering to the ECMCAD coated plates. The degree of cell staining is proportional to the cell adhesion activity of ECMCAD in the sample.  
     [0332] Various modifications and variations of the described methods and systems of the invention wilt be apparent to those skilled in the art without departing from the scope and spirit of the invention. Although the invention has been described in collection with certain embodiments, it should be understood that the invention as claimed should not he unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the invention which are obvious to those skilled in molecular biology or related fields are intended to be within the scope of the following claims.  
                               TABLE 1                                   Polynucleo-           Incyte   Polypeptide   Incyte   tide SEQ   Incyte Poly-       Project ID   SEQ ID NO:   Polypeptide ID   ID NO:   nucleotide ID                                                    1888682   1   1888682CD1   37   1888682CB1       1794980   2   1794980CD1   38   1794980CB1       5533958   3   5533958CD1   39   5533958CB1       60210196   4   60210196CD1   40   60210196CB1       815125   5   815125CD1   41   815125CB1       1386915   6   1386915CD1   42   1386915CB1       1344495   7   1344495CD1   43   1344495CB1       1485774   8   1485774CD1   44   1485774CB1       7289372   9   7289372CD1   45   7289372CB1       1672338   10   1672338CD1   46   1672338CB1       184661   11   184661CD1   47   184661CB1       3719737   12   3719737CD1   48   3719737CB1       5773251   13   5773251CD1   49   5773251CB1       5426470   14   5426470CD1   50   5426470CB1       7087904   15   7087904CD1   51   7087904CB1       7477312   16   7477312CD1   52   7477312CB1       2739431   17   2739431CD1   53   2739431CB1       7473606   18   7473606CD1   54   7473606CB1       3534918   19   3534918CD1   55   3534918CB1       2428715   20   2428715CD1   56   2428715CB1       3351332   21   3351332CD1   57   3351332CB1       6382722   22   6382722CD1   58   6382722CB1       55022490   23   55022490CD1   59   55022490CB1       6755002   24   6755002CD1   60   6755002CB1       7350907   25   7350907CD1   61   7350907CB1       7474411   26   7474411CD1   62   7474411CB1       4755911   27   4755911CD1   63   4755911CB1       379766   28   379766CD1   64   379766CB1       553744   29   553744CD1   65   553744CB1       1825473   30   1825473CD1   66   1825473CB1       7950094   31   7950094CD1   67   7950094CB1       7479484   32   7479484CD1   68   7479484CB1       6780147   33   6780147CD1   69   6780147CB1       7204554   34   7204554CD1   70   7204554CB1       6833247   35   6833247CD1   71   6833247CB1       4148119   36   4148119CD1   72   4148119CB1                  
 
     [0333]                               TABLE 2                       Polypeptide   Incyte   GenBank   Probability           SEQ ID NO:   Polypeptide ID   ID NO:   score   GenBank Homolog                                                    2   1794980CD1   g192264   6.9e−46   procollagen type I alpha chain                       Grant, S. F. et al. (1996)                       Nat. Genet. 14: 203-205       3   5533958CD1   g4091819   2.2e−54   glioma-inactivated protein precursor                       Chernova, O. B. et al. (1998)                       Oncogene 17: 2873-2882       4   60210196CD1   g3132522    8.0e−144   carcinogenesis-associated protein                       ICB-1 (induced by cell-matrix                       interactions)                       Treeck, O. et al. (1998) FEBS Lett.                       425: 426-430       5   815125CD1   g9652103   0   [ Mus musculus ] netrin 4                       Yin, Y. et al. (2000) Identification                       and expression of mouse netrin-4                       Mech. Dev. 96: 115-119               g4388541   3.3e−96   laminin B1 chain                       Durkin, M. E. et al. (1988)                       Biochemistry 27: 5198-5204       6   1386915CD1   g1234793    4.2e−254   [ Xenopus laevis ] MAM domain protein                       Brown, D. D. et al. (1996) The                       thyroid hormone-induced tail                       resorption program during Xenopus                       laevis metamorphosis. Proc. Natl.                       Acad. Sci. U.S.A. 93, 1924-1929       9   7289372CD1   g2554604   6.1e−88   [ Homo sapiens ] ISLR                       Nagasawa, A. et al. (1997) Cloning                       of the cDNA for a new member of the                       immunoglobulin superfamily (ISLR)                       containing leucine-rich repeat                       (LRR). Genomics 44, 273-279       10   1672338CD1   g854326   6.0e−66   [ Mus musculus ] semaphorin B                       (Puschel, A. W. et al. (1995) Neuron                       14: 941-948)       11   184661CD1   g2367641   2.9e−26   [ Rattus norvegicus ] neuropilin-2                       (Kolodkin, A. L. et al. (1997) Cell                       90: 753-762)       12   3719737CD1   g9622242   0   [ Homo sapiens ] [5′ incom]                       protocadherin 13               g6978935    9.9e−170   [ Homo sapiens ] protocadherin-Xa                       (Yoshida, K. and Sugano, S. (1999)                       Genomics 62: 540-543)       13   5773251CD1   g1304387   5.4e−27   [ Saccharomyces cerevisiae  var.                       diastaticus] Glucoamylase                       (Lambrechts, M. G. et al. (1996) Proc.                       Natl. Acad. Sci. U.S.A. 93: 8419-8424)       14   5426470CD1   g200057   0.0   [ Mus musculus ] neuronal glycoprotein                       Connelly, M. A. et al. (1994) Proc.                       Natl. Acad. Sci. U.S.A. 91: 1337-1341       15   7087904CD1   g4519558    1.4e−181   [ Rattus norvegicus ] Kilon                       Funatsu, N. et al. (1999) J. Biol.                       Chem. 274: 8224-8230       16   7477312CD1   g5262748   0.0   [ Rattus norvegicus ] Proline rich                       synapse associated protein 2                       Boeckers, T. M. et al. (1999) Biochem.                       Biophys. Res. Commun. 264: 2476-2528;                       Boeckers, T. M. et al. (1999) J.                       Neurosci. 19: 6506-6518       17   2739431CD1   g2708626   5.7e−34   [ Mus musculus ] fibrinogen-like                       protein       18   7473606CD1   g3928000   3.5e−07   [ Homo sapiens ] procollagen I N-                       proteinase       19   3534918CD1   g13872813   0   [5′ incom] [ Homo sapiens ] (AJ306906)                       fibulin-6               g2947314   8.6e−63   [ Gallus gallus ] fibulin-1, isoform D                       precursor       20   2428715CD1   g10998440   0   [ Mus musculus ] EGF-related protein                       SCUBE1                       Grimmond, S. et al. (2000) Cloning,                       Mapping, and Expression Analysis of                       a Gene Encoding a Novel Mammalian                       EGF-Related Protein (SCUBE1)                       Genomics 70: 74-81               g2072792   3.1e−64   [ Mus musculus ] matrilin-2 precursor                       Deak, F. et al. (1997) Primary                       structure and expression of                       matrilin-2, the closest relative of                       cartilage matrix protein within the                       von Willebrand                       factor type A-like module                       superfamily. J. Biol. Chem. 272,                       9268-9274       21   3351332CD1   g3449294   0   [ Rattus norvegicus ] MEGF6                       Nakayama, M. et al. (1998)                       Identification of high-molecular-                       weight proteins with multiple EGF-                       like motifs by motif-trap screening                       Genomics 51, 27-34               g483581    1.1e−111   [ Mus musculus ] Notch 3                       Lardelli, M. et al. (1994) The novel                       Notch homologue mouse Notch 3 lacks                       specific epidermal growth factor-                       repeats and is expressed in                       proliferating Neuroepithelium. Mech.                       Dev. 46, 123-136       22   6382722CD1   g2599232   0.0   [ Mus musculus ] laminin alpha 5 chain                       Miner, J. H. et al. (1995) Molecular                       cloning of a novel laminin chain,                       alpha 5, and widespread                       expression in adult mouse tissues.                       J. Biol. Chem. 270, 28523-28526       23   55022490CD1   g8977890    9.3e−256   [ Homo sapiens ] ADAMTS7,                       alternatively spliced product       24   6755002CD1   g452821   0.0   [ Bos taurus ] Brevican                       Yamada, H. et al. (1994) J. Biol.                       Chem. 269: 10119-10126       25   7350907CD1   g442368    4.1e−246   [ Rattus norvegicus ] Neuronal                       olfactomedin-related ER localized                       protein                       Danielson, P. E. et al. (1994) J.                       Neurosci. Res. 38: 468-478       26   7474411CD1   g6164595   4.0e−95   [ Manduca sexta ] Lacunin                       (Extracellular matrix protein)                       Nardi, J. B. et al. (1999) Insect                       Biochem. Mol. Biol. 29: 883-897       27   4755911CD1   g1504038   7.1e−41   [ Homo sapiens ] Similar to human                       ankyrin 1       28   379766CD1   g13183078   1.00E−163   [3′ incom] [ Homo sapiens ] a                       disintegrin-like and metalloprotease                       domain with thrombospondin type I                       motifs-like 3               g5923786   1.4e−44   [ Homo sapiens ] Zinc metalloprotease                       ADAMTS6                       Hurskainen, T. L. et al. (1999) J.                       Biol. Chem. 274: 25555-25563       29   553744CD1   g8572538   7.0e−14   [ Homo sapiens ] Mucin                       Gerard, C. et al. (1990) J. Clin.                       Invest. 86: 1921-1927       30   1825473CD1   g188864   9.2e−47   [ Homo sapiens ] Mucin                       Toribara, N. W. et al. (1991) J.                       Clin. Invest. 88: 1005-1013       31   7950094CD1   g1110599   0.0   [Mus sp.] Semaphorin homolog                       Inagaki, S. et al. (1995) FEBS Lett.                       370: 269-272       32   7479484CD1   g4322670   l.7e−28   [ Homo sapiens ] Dentin phosphoryn                       Gu, K. et al. (1998) Eur. J. Oral                       Sci. 106: 1043-1047       33   6780147CD1   g5805194   0.0   [ Rattus norvegicus ] Leprecan                       Wassenhove-McCarthy, D. J. and K. J.                       McCarthy (1999) J. Biol. Chem.                       274: 25004-25017       34   7204554CD1   g1665757   0.0   [ Mus musculus ] Plexin 1                       Kameyama, T. et al. (1996) Biochem.                       Biophys. Res. Commun. 226: 524-529       35   6833247CD1   g4159801   2.9e−75   [ Mus musculus ] C-type lectin                       Balch, S. G. et al. (1998) J. Biol.                       Chem. 273: 18656-18664       36   4148119CD1   g6579191   6.5e−35   [ Rattus norvegicus ] SLIT-2                       Liang Y. et al. (1999) J. Biol.                       Chem. 274: 17885-17892                    
     [0334]                                       TABLE 3                       SEQ   Incyte   Amino   Potential   Potential       Analytical       ID   Polypeptide   Acid   Phosphorylation   Glycosylation   Signature Sequences,   Methods and       NO:   ID   Residues   Sites   Sites   Domains and Motifs   Databases                                                            1   1888682CD1   234   S141 S150 T137   N147 N197 N52   Signal cleavage: M1-A44   SPSCAN                   T99   N97   Transmembrane domain: G168-F187   HMMER                           Rgd cell surface interaction motif: R14-D16   MOTIFS                           Fibronectin type III domain: P47-G130   HMMER_PFAM                           Fibronectin type III PR00014:   BLIMPS_PRINTS                           N61-P70, V96-Y114, Y114-P128       2   1794980CD1   443   S103 S188 S31   N138 N51   Signal cleavage: M1-A21   SPSCAN                   S438 S72 T122       Signal peptide: M1-A22   HMMER                   T146 T160 T172       Glycosaminoglycan attchment site: S407-G410   MOTIFS                   T242 T282 T80       Transmembrane domain: A8-F30   HMMER                   T89       Collagen triple helix repeat:   HMMER_PFAM                           G208-P267 G299-R358                           COLLAGEN ALPHA PRECURSOR CHAIN   BLAST_PRODOM                           REPEAT PD000007: G223-G332                           FIBRILLAR COLLAGEN CARBOXYL-TERMINAL   BLAST_DOMO                           DM00019/P20908/1300-1524): P176-G374       3   5533958CD1   261   S243 S89 T151   N177   Leucine_Zipper: L129-L150   MOTIFS                   T203       Atp_Gtp binding site: A239-T246   MOTIFS                           Signal cleavage: M1-A19   SPSCAN                           Signal peptide: M1-A19   HMMER                           Leucine rich repeat: T53-Q171   HMMER_PFAM                           Leucine rich repeat C-terminal domain:   HMMER_PFAM                           N158-R207                           Leucine-rich repeat signature PR00019:   BLIMPS_PRINTS                           L126-L139                           NEUROGENIC TRKB RECEPTOR DM01983|   BLAST_DOMO                           B39667|24-197: W20-L169       4   60210196CD1   643   S103 S143 S162       ICB1 membrane carcinogenesis-associated   BLAST_PRODOM                   S225 S237 S304       protein PD121395: M150-G403                   S33 S38 S388                   S429 S437 S441                   S45 S567 T114                   T333 T527 T593                   T92       5   815125CD1   628   S108 S136 S212   N163 N353   Signal cleavage: M1-L20   SPSCAN                   S27 S28 S387   N483 N56   Egf (epidermal growth factor) motif:   MOTIFS                   S416 S465 S503       C293-C304, C420-C431                   S534 S554 S570       Signal peptide: M1-G25   HMMER                   S98 T153 T182       Transmembrane domain: M1-V23   HMMER                   T192 T331 T411       Laminin N-terminal (Domain VI)   HMMER_PFAM                   T467 T540 T572       laminin_Nterm: C34-G260                   T597 T71       Laminin EGF-like (Domains III and V):   HMMER_PFAM                           C262-C329, C332-C392, C395-C446                           Laminin-type EGF-like domain BL01248:   BLIMPS_BLOCKS                           C295-C307                           Type III EGF-like signature PR00011:   BLIMPS_PRINTS                           C413-C431                           EGFLIKE LAMININ PRECURSOR DOMAIN   BLAST_PRODOM                           REPEAT PD002082: C34-G260, C262-A319                           LAMININ CHAIN B1 DM01003|P07942|27-259:   BLAST_DOMO                           E31-K230       6   1386915CD1   686   S117 S135 S136   N134 N329   Signal peptide:   HMMER; SPSCAN                   S196 S336 S445   N524   M1-A18                   S449 S477 S497       MAM domains:   HMMER_PFAM                   S499 S578 S647       C26-E169; C170-N329; C342-S498;                   S93 T209 T460       C509-E666                   T89       PRECURSOR GLYCOPROTEIN SIGNAL   BLAST_PRODOM                           TRANSMEMBRANE HYDROLASE PROTEIN                           REPEAT RECEPTOR PHOSPHATASE                           NEUROPILIN PD001482: C170-C327; C509-E666                           MAM DM01344|A55620|618-796:   BLAST_DOMO                           C509-R644                           MAM domain motif:   MOTIFS                           G551-F585       7   1344495CD1   296   S115 S38 S39   N253 N259 N30   Transmembrane domain:   HMMER                   S43 T129 T207       W218-F235                   T282       Putative peptidoglycan binding domain:   HMMER_PFAM                           R76-P119       8   1485774CD1   575   S240 S281 S402   N257 N270   Signal peptide:   SPSCAN                   S413 S511 S527   N348 N509   M1-P45                   T157 T170 T245   N564   WSC domain:   HMMER_PFAM                   T247 T301 T341       Y145-A224                   T500       9   7289372CD1   592   S151 S19 S198   N121 N337   Signal peptide:   HMMER; SPSCAN                   S202 S289 S346   N364 N474 N52   M1-P21                   S367 S395 S411   N563   Leucine rich repeat N-terminal domain:   HMMER_PFAM                   S440 S544 S587       S19-P50                   T267 T329 T354       Leucine Rich Repeats:   HMMER_PFAM                   T400 T431 T433       N52-T75; Q76-S99; Q100-S123; A124-P147;                           D148-S171                           Leucine rich repeat C-terminal domain:   HMMER_PFAM                           N181-A231                           Immunoglobulin domain:   HMMER_PFAM                           G253-A357                           ISLR PRECURSOR SIGNAL PD103127:   BLAST_PRODOM                           P229-P286; P321-I417                           ISLR PRECURSOR SIGNAL PD167884:   BLAST_PRODOM                           S19-V74       10   1672338CD1   255   S106 S111 S119   N120 N135   signal peptide: M1-A31   HMMER                   S180 T233       Sema domain: F64-V155   HMMER_PFAM                           SEMAPHORIN B IMMUNOGLOBULIN FOLD   BLAST_PRODOM                           NEUROGENESIS DEVELOPMENTAL PROTEIN                           PD107003: M1-D63                           SEMAPHORIN PROTEIN RECEPTOR KINASE   BLAST_PRODOM                           SIGNAL TYROSINE FAMILY HEPATOCYTE                           PD001844: L67-H167                           SEMAPHORIN; FASCICLIN; COLLAPSIN; II   BLAST_DOMO                           DM01606|I48745|1-619: M1-I154,                           C217-L255                           DM01606|I48748|1-589: G34-I154                           DM01606|I48747|1-646: L24-I154                           DM01606|A49069|1-646: F64-I154       11   184661CD1   641   S103 S139 S226   N124 N277   signal_cleavage: M1-A34   SPSCAN                   S242 S244 S275   N351 N418   signal peptide: M1-A34   HMMER                   S427 S433 S488   N455 N64   transmembrane domain: T458-F480   HMMER                   S556 S615 S634       F5/8 type C domain (discoidin (DS) domain   HMMER_PFAM                   T129 T157 T325       family): S258-L409                   T357 T434 T46       CUB domain: C41-Y147   HMMER_PFAM                   T527 T54 T552       GLYCOPROTEIN NEUROPILIN COAGULATION   BLAST_PRODOM                   T557 T563 T600       PD000875: D264-L409                   T66       GLYCOPROTEIN EGF-LIKE FACTORB12   BLAST_PRODOM                           PD000165: C41-Y147                           DISCOIDIN I N-TERMINAL   BLAST_DOMO                           DM00516|P12259|2095-2223: H284-I414                           DM00516|A42580|2085-2210: P287-I414                           DM00516|P00451|2221-2347: W285-Q413                           DM00516|A44258|86-212: W285-Q413       12   3719737CD1   924   S116 S12 S144   N108 N299   signal_cleavage: M1-G33   SPSCAN                   S333 S362 S366   N305 N653   transmembrane domain: L866-I884   HMMER                   S44 S57 S609   N721 N776   Cadherin domain:   HMMER_PFAM                   S635 S767 S824   N817 N822   I187-S284, I298-I390, I513-L603,                   T219 T428 T464       F617-L706, Y724-N817                   T516 T533 T568       Cadherin:   MOTIFS                   T581 T601 T637       I170-P180 I281-P291 V496-P506                   T662 T698 T778       L600-P610 I703-P713                   T82 T850 Y43       Cadherins extracellular repeated domain   PROFILESCAN                   Y436 Y580 Y802       signature:                           V260-I312, T581-I631, V685-P733                           CADHERIN SIGNATURE   BLIMPS_PRINTS                           PR00205: Q678-P693, S696-P713,                           V168-F182                           CADHERIN REPEAT   BLAST_DOMO                           DM00030|P33450|1079-1181: E539-D640                           DM00030|P33450|187-298: N215-L322                           DM00030|P33450|1952-2055: E539-A641                           DM00030|P34616|1682-1783: G642-D746       13   5773251CD1   987   S111 S115 S15   N14 N213 N337   KH domain: K113-G161   HMMER_PFAM                   S16 S165 S32   N391 N404   OTOGELIN ALPHA POLYPEPTIDE ALPHANAC   BLAST_PRODOM                   S324 S33 S377   N410 N478   MUSCLESPECIFIC FORM GP220                   S443 S457 S459   N581 N628   PD147940: A206-S772                   S5 S52 S56 S662   N729 N770   MUCIN; MUC5; TRACHEOBRONCHIAL   BLAST_DOMO                   S669 S795 S816   N800 N833   DM05454|S55316|1-317: I287-P530,                   S93 S959 T158       V384-S666, S317-P530,                   T246 T249 T417       T355-S617, F311-S583                   T554 T62 T640       EPSTEIN; BARR; MEMBRANE   BLAST_DOMO                   T686 T813       DM06222|P03200|1-906: G203-S588,                           S339-A768       14   5426470CD1   1028   S133 S164 S170   N193 N375   Fibronectin type III domain:   HMMER_PFAM                   S184 S270 S279   N468 N489 N65   P598-S687, P700-S790, P802-S891,                   S342 S348 S377   N765 N860   P903-S986                   S397 S406 S436   N895 N913   Immunoglobulin domain:   HMMER_PFAM                   S442 S449 S507   N931 N956   D43-A102, G137-V198, G242-A299,                   S512 S549 S558       C339-A388, G424-A481, G514-V579                   S572 S588 S617       CONTACTIN CELL ADHESION NEUROFASCIN   BLAST_PRODOM                   S67 S678 S690       GLYCOPROTEIN GP135 IMMUNOGLOBULIN                   S713 S772 S797       PD001890: L688-P802                   S815 S817 S852       ADHESION IMMUNOGLOBULIN   BLAST_PRODOM                   S863 T244 T364       GLYCOPROTEIN GPI ANCHOR REPEAT                   T47 T470 T581       CONTACTIN PD005229: V894-I991                   T648 T661 T754       FIBRONECTIN TYPEIII   BLAST_PRODOM                   T758 T897 T898       PD073047: N301-G560                   T955 T958 T984       NEURAL CELL ADHESION MOLECULE CLOSE   BLAST_PRODOM                   T995 Y98       HOMOLOGUE OF L1 L1LIKE PROTEIN                           PD066559: E482-G596                           IMMUNOGLOBULIN   BLAST_DOMO                           DM00001|A53449|497-587: T497-S588                           DM00001|A53449|405-495: A405-V496                           DM00001|A53449|32-110: P32-S111                           DM00001|A53449|126-206: T126-V207       15   7087904CD1   354   S171 S178 S210   N155 N275   signal_cleavage: M1-P33   SPSCAN                   S277 T125 T149   N286 N294   Immunoglobulin domain:   HMMER_PFAM                   T163 T226 Y187   N307 N73   G53-V120, G153-A205, G238-A299                           Receptor tyrosine kinase class III   PROFILESCAN                           signature: V135-A198                           PRECURSOR SIGNAL GLYCOPROTEIN   BLAST_PRODOM                           IMMUNOGLOBULIN FOLD CELL ADHESION GPI                           ANCHOR ALTERNATIVE                           PD005605: F40-T128                           IMMUNOGLOBULIN   BLAST_DOMO                           DM00001|P32736|39-125: A44-T128                           DM00001|P32736|139-212: D143-V214                           DM00001|P32736|226-306: I227-A308       16   7477312CD1   1829   S1050 S1124   N122 N239   signal_cleavage: M1-A15   SPSCAN                   T948 S1150 S124   N358 N531   Ank repeat:   HMMER_PFAM                   S477 S1260       S226-R259 D260-S292 R293-E326                   S1285 S57       N327-A359 S360-Y392                   S1295 S484 T279       SAM domain (Sterile alpha motif):   HMMER_PFAM                   S1351 S667       Q1764-D1827                   S1370 S1371       SH3 domain: R580-V634   HMMER_PFAM                   S844 S1389       CORTACTINBINDING PROTEIN 1   BLAST_PRODOM                   S1390 S870       D0148775: P1333-L1765, V768-A1305,                   S1391 S1436       P912-T1495, P17-R223, E16-A74,                   S952 S1449       P27-A128, S454-P569, A6-P64,                   S1453 S996       A60-P94, P1739-W1766, P478-L504,                   S1462 S1496       P25-S38                   S880 S1536       LARGE STRUCTURAL PHOSPHOPROTEIN   BLAST_PRODOM                   S1596 S854       PD145465: R1021-R1560                   S1608 S1619       BAT2 (HLA-B-associated transcript 2)   BLAST_DOMO                   S889 S1637       DM05517|S37671|1-1870: P896-D1201,                   S1660 S900       A12-A79, G1610-P1762                   S1664 S1729       PROLINE-RICH PROTEIN 3   BLAST_DOMO                   S1767 S503 S608       DM00215|S14972|7-90: P912-P941,                   T1011 T1086       P556-P566                   T1125 T415                   T1196 T1360                   T848 S38                   T1395 T443                   T1526 T1801                   T206 T323 T618                   T641 T645 T650                   T699 T771 T796                   T823 T837 T843       17               N173 N264 N53   Signal peptide: M1-A22   SPSCAN                           Signal peptide: M1-A22   HMMER                           Fibrinogen beta and gamma chains, C-term   HMMER_PFAM                           domain:                           Q115-M317                           Fibrinogen beta and gamma chains C-terminal   BLIMPS_BLOCKS                           domain signature BL00514:                           V116-G152, E157-V169, F206-A220                           Fibrinogen beta and gamma chains C-terminal   PROFILESCAN                           domain signature:                           T237-S303                           PRECURSOR GLYCOPROTEIN SIGNAL   BLAST_PRODOM                           FIBRINOGEN BLOOD COAGULATION CHAIN                           PLASMA PROTEIN PLATELET PD001241:                           Q115-R315 FIBRINOGEN BETA/GAMMA   BLAST_DOMO                           DM00531|P12804|145-428: N45-P320                           S47273|152-435: N26-P320                           JN0596|27-305: V116-R315                           P12799|106-414: S31-I314                           Fibrin_Ag_C_Domain motif:   MOTIFS                           W268-G280       18   7473606CD1   644   S171 S214 S270   N574   Transmembrane domain:   HMMER                   S290 S363 S405       M228-F248                   S425 S535 S581       Reprolysin family propeptide domain:   HMMER_PFAM                   S592 S630 T167       Q502-Q615                   T266 T315 T377       Glycosaminoglycan attachment sites:   MOTIFS                   T620 Y534       S86-G89, S125-G128       19   3534918CD1   881   S362 S387 S425   N257 N403   EGF-like domains:   HMMER_PFAM                   S447 S533 S548   N630 N861   C682-C716, C722-C762, C474-C508,                   S552 S60 S658       C514-C553, C559-C591, C597-C633,                   S8 S91 T199       C639-C676                   T259 T300 T322       Thrombospondin type 1 domains:   HMMER_PFAM                   T367 T39 T507       S124-C174, G181-C231                   T626 T632 T715       Calcium-binding EGF-like domain BL01187:   BLIMPS_BLOCKS                   T793 T839 T848       C633-H644, C692-Y707                   Y849       Type II EGF-like signature PR00010:   BLIMPS_PRINTS                           D593-P604, N630-D637, G697-Y707                           HEMICENTIN PRECURSOR SIGNAL   BLAST_PRODOM                           GLYCOPROTEIN EGFLIKE DOMAIN HIM4                           PROTEIN ALTERNATIVE SPLICING                           PD083049: Q725-Y881                           EGF-LIKE DOMAIN DM00864|I55476|159-241:   BLAST_DOMO                           N649-C722, C480-E561, D525-N600                           THROMBOSPONDIN TYPE 1 REPEAT DM00275|   BLAST_DOMO                           P35440|485-548: Q165-C226                           P07996|477-540: Q165-C226                           Q03350|479-542: C169-C226                           Glycosaminoglycan attachment site:   MOTIFS                           S127-G130                           Aspartic acid and asparagine hydroxylation   MOTIFS                           sites:                           C484-C495, C569-C580, C652-C663,                           C692-C703       20   2428715CD1   957   S216 S258 S444   N255 N400   Signal peptide: M1-L22   SPSCAN                   S525 S526 S56   N674 N745   Signal peptide: M1-G25   HMMER                   S594 S728 S880   N774 N784   EGF-like domains:   HMMER_PFAM                   S894 T101 T180       C37-C72, C78-C115, C121-C156,                   T240 T285 T309       C166-C202, C206-C241, C275-C310,                   T350 T434 T505       C316-C351, C357-C390, C396-C431                   T520 T53 T551       CUB domain: C793-Y902   HMMER_PFAM                   T579 T596 T648       Calcium-binding EGF-like signature BL01187:   BLIMPS_BLOCKS                   T721 T748 T775       C115-G126, C407-R422                   T777 T862 T877       THROMBOMODULIN SIGNATURE PR00907:   BLIMPS_PRINTS                   T904       C282-P298, L344-C367, G372-S397,                           C50-D76                           GLYCOPROTEIN THYROGLOBULIN   BLAST_PRODOM                           PRECURSOR REPEAT THYROID HORMONE                           IODINATION SIGNAL EGFLIKE PROTEIN                           PD009765: C641-C788                           EGF-LIKE DOMAIN DM00864|I55476|159-241:   BLAST_DOMO                           N320-C396, N279-C357, N84-C156,                           C363-C437, I49-N124                           EGF DM00003|   BLAST_DOMO                           P98163|1373-1460: C87-C156,                           C323-L384                           P98063|706-753: D117-C156                           Glycosaminoglycan attachment site:   MOTIFS                           S894-G897                           Aspartic acid and asparagine hydroxylation   MOTIFS                           sites:                           C50-C61, C91-C102, C132-C143,                           C327-C338, C367-C378, C407-C418       21   3351332CD1   1393   S1008 S1018   N1098 N1109   Signal peptide: M1-G26   SPSCAN                   S1158 S1206   N1169 N1204   Signal peptide: M1-A22   HMMER                   S1255 S1277   N147 N447   EGF-like domains:   HMMER_PFAM                   S1380 S201 S313   N458 N634   C60-C95, C101-C137, C143-C178,                   S347 S49 S567   N769 N856   C184-C219, C230-C265, C271-C305,                   T1179 T1214   N867 N893   C311-C346, C415-C446, C459-C489,                   T1354 T1384       C502-C532, C536-C577, C635-C664,                   T264 T399 T401       C677-C708, C721-C751, C764-C795,                   T418 T487 T660       C808-C838, C851-C881, C894-C924,                   T836 T953       C937-C967, C980-C1010, C1067-C1097,                           C1110-C1140, C1153-C1183, C1196-C1226,                           C1239-C1269, C1282-C1312, C1325-C1355,                           Type III EGF-like signature PR00011:   BLIMPS_PRINTS                           C471-C489, C1337-C1355, Q797-G825,                           C690-C708                           THROMBOMODULIN SIGNATURE PR00907:   BLIMPS_PRINTS                           G758-C777, C237-P253, C108-L130                           MEGF6 GLYCOPROTEIN EGFLIKE DOMAIN   BLAST_PRODOM                           PD169326: L349-D414                           PD165309: N507-C536                           SURFACE ANTIGEN PROTEIN PRECURSOR   BLAST_PRODOM                           SIGNAL REPEAT MEMBRANE GPIANCHOR                           156G 168G PD001714: H774-C1215                           EGF   BLAST_DOMO                           DM00003|P98163|1373-1460: S229-V308,                           C143-E223 DM00003|P35556|2219-2292:                           S274-C346 DM00003|A57278|2213-2286:                           S274-C346                           EGF-LIKE DOMAIN DM00864|I55476|159-241:   BLAST_DOMO                           N234-C311                           EGF domain motifs:   MOTIFS                           C435-C446, C478-C489, C521-C532,                           C566-C577, C653-C664, C697-C708,                           C740-C751, C784-C795, C827-C838,                           C870-C881, C913-C924, C956-C967,                           C999-C1010, C1043-C1054,                           C1086-C1097, C1129-C1140,                           C1172-C1183, C1215-C1226,                           C1258-C1269, C1301-C1312,                           C1344-C1355                           Aspartic acid and asparagine hydroxylation   MOTIFS                           sites:                           C71-C82, C195-206, C281-292, C322-333       22   6382722CD1   3695   S1093 S111   N1330 N143   Signal peptide: M1-A35   SPSCAN                   S1172 S164   N1529 N1555   Signal peptide: M1-A35   HMMER                   S1731 S1779   N2019 N2196   Laminin N-terminal (Domain VI): L45-G298   HMMER_PFAM                   S1807 S1826   N2209 N2303                   S1836 S1841   N2423 N243   Laminin EGF-like (Domains III and V):   HMMER_PFAM                   S1870 S190   N2501 N2568   C300-C356, C359-C426,                   S1901 S1902   N2707 N3107   C429-C471, C494-C538, C541-C584,                   S191 S1982   N3209 N3257   C587-C629, C632-C674, C677-C720,                   S2211 S2358   N3287 N3626   E721-C773, C776-C826, C829-D870,                   S2626 S2684   N452 N479   C1438-C1481, C1484-C1525, C1528-C1574,                   S2698 S2798   N900 N921 N95   C1577-C1625, C1864-C1910,                   S2819 S290   N959   C1913-C1966, C1969-C2020, C2023-C2067,                   S2934 S2944       C2070-C2114, C2117-C2167                   S3035 S3076       Laminin B (Domain IV): Y1693-E1829   HMMER_PFAM                   S3086 S3155       Laminin G domain;   HMMER_PFAM                   S3316 S3349       F2876-S2911, L2970-D3102,                   S3374 S3429       V3370-G3502, V3549-A3676                   S3478 S352 S380       Laminin-type EGF-like signature BL01248:   BLIMPS_BLOCKS                   S477 S697 S73       C1883-C1895                   S768 S810 S828       Type III EGF-like signature PR00011:   BLIMPS_PRINTS                   S902 S943 S947       C1589-C1607, C2033-C2051, C1596-G1624,                   T1032 T1091       C1543-C1561                   T1154 T124       LAMININ DOMAIN   BLAST_PRODOM                   T1269 T1355       PD035152: S2731-C3292, P3301-F3353                   T1362 T1557       PD025440: L871-A1435                   T1634 T1643       PD002082: H46-G298                   T1658 T1711       PD155637: E1687-L1858                   T1720 T1745       LAMININ CHAIN B1 DM01003|P25391|14-258:   BLAST_DOMO                   T2021 T2047       L45-Y289                   T208 T2128       DM01003|S53868|27-271: L45-Y289                   T2288 T2315       DM01003|I49077|27-271: L45-Y289                   T2515 T2570       DM01003|S50829|1-208: P94-Y289                   T2625 T2749       TNFR/NGFR motif: C2051-C2090   MOTIFS                           Glycosaminoglycan attachment sites:   MOTIFS                           S1531-G1534, S1972-G1975, S3149-G3152                           RGD motifs:   MOTIFS                           R1722-D1724, R1838-D1840                           EGF domain motifs:   MOTIFS                           C322-C333, C447-C458, C515-C526, C560-C571,                           C605-C616, C650-C661, C696-C707,                           C744-C755, C797-C808, C848-C859, C1457-C1468,                           C1550-C1561, C1596-C1607, C1831-C1842                           C1937-C1948, C2040-C2051, C2070-C2081,                           C2088-C2099, C2131-C2142       23   55022490CD1   1255   S1009 S1052   N1039 N1129   Signal peptide: M1-G27   SPSCAN                   S1097 S1188   N262 N347   Thrombospondin type 1 domain:   HMMER_PFAM                   S167 S174 S444   N519 N540   S111-C161, W394-C448, G518-C563,                   S470 S486 S580   N981 N988   W984-C1032, W1035-C1090,                   S604 S74 S761       W1093-C1139, T1140-C1197,                   S877 S939 S954       PROTEIN F25H8.3 F53B6.2 KIAA0605   BLAST_PRODOM                   S966 T1115       PROCOLLAGEN C37C3.6 SERINE                   T1130 T1217       PROTEASE INHIBITOR ALTERNATIVE                   T1228 T138 T272       PD007018: W394-P512, W1093-P1203                   T31 T526 T531       PROTEIN PROCOLLAGEN THROMBOSPONDIN   BLAST_PRODOM                   Y316       MOTIFS NPROTEINASE A DISINTEGRIN                           METALLOPROTEASE WITH ADAMTS1                           PD011654: C198-C266                           PD014161: V269-E380                           Glycosaminoglycan attachment site:   MOTIFS                           S575-G578       24   6755002CD1   911   S116 S165 S29   N130 N337   Signal peptide: M1-A22   HMMER                   S310 S319 S419       Signal cleavage: M1-A22   SPSCAN                   S446 S615 S67       C_Type_Lectin C784-C808   MOTIFS                   S704 S708 S727       Egf C670-C681   MOTIFS                   S74 T212 T219       Ig_Mhc Y135-H141   MOTIFS                   T269 T382 T386       Lectin C-type domain lectin_c: T714-C808   HMMER_PFAM                   T397 T420 T430       Extracellular link domain Xlink:   HMMER_PFAM                   T545 T558 T660       G156-Y251, G257-F353                   T705 T728 T807       Immunoglobulin domain ig: G50-V139   HMMER_PFAM                   Y135 Y459       EGF-like domain EGF: C650-C681   HMMER_PFAM                           Sushi domain (SCR repeat) sushi: C815-C871   HMMER_PFAM                           C-type lectin domain signature   PROFILESCAN                           c_type_lectin.prf: P763-G828                           C-type lectin domain protein BL00615:   BLIMPS_BLOCKS                           C699-C716, W795-C808                           Link domain proteins BL01241: E272-G324   BLIMPS_BLOCKS                           TYPE II ANTIFREEZE PROTEIN (lectin-like)   BLIMPS_PRINTS                           PR00356:                           F687-C699, C699-C716, R717-F734,                           W744-D760, W795-C808                           C-TYPE LECTIN DM00035|A54423|689-811:   BLAST_DOMO                           C688-G811                           COMPLEMENT FACTOR H REPEAT DM00260   BLAST_DOMO                           A54423|142-252: G142-E253                           BREVICAN CORE PROTEIN PRECURSOR (brain-   BLAST_PRODOM                           specific lectican)                           PD022317: L479-V651 PD021260: R354-E455                           EGFLIKE DOMAIN REPEAT   BLAST_PRODOM                           PD150847: D28-V154, PD000918: K267-F353       25   7350907CD1   467   S124 S194 S261   N169 N270   Signal cleavage: M1-T31   SPSCAN                   S273 S335 S362   N289 N376   GLYCOPROTEIN OLFACTOMEDIN   BLAST_PRODOM                   S383 S415 S432   N413 N455 N85   MESHWORK-INDUCED RESPONSE SIGNAL                   S47 T220 T36       PROTEIN PRECURSOR PD006897: E258-I452                   T97 Y103 Y323       NEURONAL OLFACTOMEDIN RELATED   BLAST_PRODOM                           ER LOCALIZED PRECURSOR                           PD037534: A135-R257, PD020721: M11-K134       26   7474411CD1   1018   S117 S195 S206   N373 N441   Signal cleavage: M1-P25   SPSCAN                   S309 S312 S394   N709   Receptor_Cytokines_2 G57-S63   MOTIFS                   S458 S557 S648       Transmembrane domain: M1-F20   HMMER                   S656 S661 S803       Thrombospondin type 1 domain tsp_1:   HMMER_PFAM                   S84 S896 T368       S737-C793                   T483 T493 T649       PROCOLLAGEN THROMBOSPONDIN MOTIFS   BLAST_PRODOM                   T665 T843 T851       PD011654: K344-C411, PD014161: Q412-I527                           PROCOLLAGEN SERINE PROTEASE INHIBITOR   BLAST_PRODOM                           PD007018: W856-P969       27   4755911CD1   1458   S1014 S1027   N1199 N215   Ankyrin repeat ank: P108-D140, E141-N173,   HMMER_PFAM                   S104 S1073   N354 N958   S174-L204, N215-K247, S248-T279                   S1131 S1254       (SAM) protein interaction domain SAM:   HMMER_PFAM                   S1274 S1298       E497-S560, H568-A630                   S1391 S1395       PROLINE-RICH PROTEIN DM03894|A39066|   BLAST_DOMO                   S1429 S1437       1-159: P1216-P1358                   S1444 S174 S367                   S447 S450 S560                   S673 S732 S777                   S782 S79 S846                   S916 S918 S946                   S981 T1056                   T1092 T1103                   T1122 T1150                   T1170 T1174                   T1203 T1273                   T177 T283 T337                   T356 T534 T604                   T667 T678 T702                   T712 T716 T717                   T80 T828 T841                   T855 Y363 Y594       28   379766CD1   323           Signal peptide: M1-T24   HMMER                           Thrombospondin type 1 domain: D79-C123   HMMER-PFAM                           Thrombospondin, procollagen, N-proteinase   BLAST-PRODOM                           A, disintegrin, metalloprotease with                           ADAMTS1 PD011654:                           P157-C227, Q133-G203       29   553744CD1   234   S231 T140       30   1825473CD1   377   S120 S140 S18   N128 N135   Signal peptide: M1-S18   HMMER                   S38 S41 S62   N146 N97   Signal peptide: M1-G22   SPScan                   T267 T343 Y48       Mucin, MUC5, tracheobronchial:   BLAST-DOMO                           DM05454|S55316|1-317:                           P91-A350, C70-T348, S150-P351,                           Q163-A350, P203-A350                           Salivary glue protein:   BLAST-DOMO                           DM02055|P02840|17-234:                           S149-K355, S120-T330, P85-T291       31   7950094CD1   833   S200 S34 S364   N106 N121   Signal peptide: M1-V23   HMMER                   S382 S46 S480   N310 N419   Transmembrane domain: L667-R687   HMMER                   S505 S555 S685   N522 N564   Plexin repeat: D499-N551   HMMER-PFAM                   S742 S826 T229       Sema domain: F53-K481   HMMER-PFAM                   T276 T302 T418       Semaphorin, fasciclin, collapsin:   BLAST-DOMO                   T429 T523 T561       DM01606|I48747|1-646: L10-W519                   T57 T701 Y249       Semaphorin, fasciclin, collapsin:   BLAST-DOMO                   Y345 Y736       DM01606|A49069|1-646: N26-W519                           Semaphorin, fasciclin, collapsin:   BLAST-DOMO                           DM01606|I48744|1-639: A12-G592                           Semaphorin, fasciclin, collapsin:   BLAST-DOMO                           DM01606|I48748|1-589: D52-G530                           Semaphorin I (neural development factor):   BLAST-PRODOM                           PD129812: H540-V833                           Semaphorin, receptor, kinase, tyrosin   BLAST-PRODOM                           protein PD001844:                           F145-E351, R242-S453, L56-E204,                           P754-G764                           Semaphorin I:   BLAST-PRODOM                           PD166847: M1-D52       32   7479484CD1   1291   S1037 S113   N394 N500 N54   Cell attachment sequence: R844-D846   MOTIFS                   S1279 S216 S224       Tumor recognition, prolyl:   BLAST-DOMO                   S225 S272 S324       DM08077|P30414|230-1403:                   S380 S396 S434       S613-P1098, E398-P896                   S445 S450 S453       Acidic serine cluster repeat:   BLAST-DOMO                   S465 S466 S480       DM03496|P32583|57-405:                   S481 S489 S508       S539-Q824, N500-K819, S557-V878,                   S535 S547 S558       S421-S754, A474-R765, S465-W800,                   S563 S585 S589       A378-Y718                   S595 S596 S606       Type B repeat:   BLAST-DOMO                   S618 S635 S652       DM05511|S26650|1-1203:                   S655 S656 S662       E400-P826, D534-Q791, Q593-D842                   S678 S683 S688       Type B repeat:   BLAST- DOMO                   S691 S695 S708       DM05511|P18583|113-1296:                   S713 S719 S720       S585-P826, D475-D842, D534-S783                   S721 S760 S764                   S785 S790 S795                   S799 S804 S810                   S831 S866 S871                   S889 S947 S954                   S965 S971 T1102                   T118 T175 T243                   T268 T341 T371                   T41 T439 T862                   T879 T944       33   6780147CD1   736   S131 S144 S20   N316 N467   Signal peptide: M1-A22   HMMER                   S361 S369 S409   N540   Signal peptide: M1-A22   SPScan                   S469 S479 S653       Cell attachment sequence: R48-D50   MOTIFS                   S683 S699 S726       Leucine zipper pattern: L445-L466   MOTIFS                   T394 T430 T495       CD4, GNB3, mouse BAC library PD043366:   BLAST-PRODOM                   T508 T542 T570       L445-K733, H176-E412, C79-E234,                   T608 T630 Y250       Q97-E135                           CASP, cartilage-associated PD023886:   BLAST-PRODOM                           Y46-C282, E201-S361       34   7204554CD1   1896   S1004 S1115 S45   N1043 N1098   Signal peptide: M1-A26   SPScan                   S1271 S1382   N1140 N1187   Signal peptide: M1-A28   HMMER                   S1435 S1487   N1212 N1609   Transmembrane domains:   HMMER                   S1546 S1621   N1612 N572   V10-A28, P1244-Y1267                   S1631 S1635   N597 N660   Plexin repeat:   HMMER-PFAM                   S1767 S1785   N672 N701   S514-V564, N660-P707, K808-T862                   S1797 S1811   N761 N769 N77   Sema domain:   HMMER-PFAM                   S1827 S1883   N785   L51-N495                   S202 S203 S249       IPT/TIG domain:   HMMER-PFAM                   S294 S454 S542       P864-V959, P961-T1045, P1048-Y1147,                   S599 S608 S621       P1150-Y1236                   S838 S858 S908       ATP/GTP-binding site motif A (P-loop):   MOTIFS                   S929 S952 T1036       G188-S195                   S162 T1075       Hepatocyte tyrosine kinase:   BLAST-DOMO                   T1200 T1220       DM03653|P08581|14-526:                   T1277 T1363       L51-C521, T647-C667                   T1574 T1575       Tyrosine kinase:   BLAST-DOMO                   T1739 T1779       DM01368|P51805|796-899:                   T189 T268 T279       C819-I924                   T361 T503 T519       Tyrosine kinase:   BLAST-DOMO                   T604 T647 T957       DM02937|P51805|991-1085:                   Y1540 Y1817       P1021-V1109                           Hepatocyte tyrosine kinase:   BLAST-DOMO                           DM03653|A48196|13-528:                           L19-E522                           Plexin precursor PD008852:   BLAST-PRODOM                           A1262-S1672, T1504-S1896, E482-N495                           Receptor, tyrosine kinase PD003981:   BLAST-PRODOM                           R892-N1212, M502-H531                           Plexin precursor PD010132:   BLAST-PRODOM                           P570-C843                           Plexin precursor PD003973:   BLAST-PRODOM                           R372-Y498       35   6833247CD1   215   S108 S140 S177   N102 N111 N45   signal peptide:   SPSCAN                   S8 T104 T124       M1-C39                   T53       Transmembrane domain:   HMMER                           Q17-A37                           Lectin C-type domain:   HMMER_PFAM                           R110-C207                           C-type lectin domain protein   BLIMPS_BLOCKS                           BL00615A: C95-C112                           BL00615B: W194-C207                           C-type lectin domain signature:   PROFILESCAN                           Q159-T213                           TYPE II ANTIFREEZE PROTEIN   BLIMPS_PRINTS                           PR00356: S113-F130, F142-D158,                           W194-C207, C83-C95,                           C95-C112                           C-TYPE LECTIN   BLAST_DOMO                           DM00035|A54423|689-811: C83-I209                           DM00035|P10716|405-536: D87-K208                           DM00035|P16112|2205-2327: C84-K208                           DM00035|A46274|248-377: C84-K208       36   4148119CD1   579   S144 S253 S394   N69   signal_cleavage:   SPSCAN                   S485 T162 T472       M1-G24                   T521 T570       signal peptide:   HMMER                           M1-G24                           Leucine Rich Repeat:   HMMER_PFAM                           Q239-H264, S265-A288, G310-R335,                           G336-R359, G381-R406, A407-P426,                           G428-D451, Q452-Q477, A478-P497,                           A499-P522, R523-P548, A73-S96,                           G97-T122, Q123-R146, V168-E193,                           A194-P213, S215-T238                           Leucine zipper pattern:   MOTIFS                           L198-L219 L269-L290 L340-L361                           L411-L432 L418-L439 L482-L503                    
     [0335]                                       TABLE 4                       Polynucleotide   Incyte   Sequence   Selected                   SEQ ID NO:   Polynucleotide ID   Length   Fragment(s)   Sequence Fragments   5′ Position   3′ Position                                                            37   1888682CB1   1211       7347284H1 (LUNLTUE01)   315   905                       2110746R6 (BRAITUT03)   749   1211                       7016843H1 (KIDNNOC01)   1   625       38   1794980CB1   1523   1403-1523, 1-121,   6775891H1 (OVARDIR01)   1   700                   409-454,   4955572H1 (ENDVUNT01)   1202   1523                   833-907   6149683H1 (BRANDIT03)   780   1450                       2149263F6 (BRAINOT09)   678   1313       39   5533958CB1   1368   1-589   6552411H1 (BRAFNON02)   878   1368                       7237564H1 (BRAINOY02)   850   1358                       6976222H1 (BRAHTDR04)   579   1333                       7182163H1 (BONRFEC01)   1   604       40   60210196CB1   3157   1-2311   71699406V1   2592   3157                       71699506V1   2085   2898                       71699453V1   1611   2165                       7050851H1 (BRACNOK02)   1   792                       70810715V1   2310   2955                       71699537V1   1393   2080                       3767657F7 (BRSTNOT24)   769   1492                       5436183F6 (SPLNNOT17)   882   1623       41   815125CB1   3264   1879-1968, 1-938   70506843V1   512   1131                       71182375V1   1999   2553                       6764263H1 (BRAUNOR01)   1   646                       71149313V1   2520   3264                       60205342U1   1305   1932                       1376122F1 (LUNGNOT10)   2143   2654                       6488119H1 (MIXDUNB01)   1453   2026                       70483405V1   702   1342       42   1386915CB1   3383   1-1510   6841587H1 (BRSTNON02)   3124   3376                       70772013V1   1247   1875                       70773009V1   663   1266                       1350440F1 (LATRTUT02)   2451   3007                       5797946H1 (PLACFET04)   2547   3041                       6428723H1 (LUNGNON07)   1   338                       6481347H1 (PROSTMC01)   319   991                       3326918T6 (HEAONOT04)   2914   3333                       843210H1 (PROSTUT05)   3173   3383                       70772645V1   1958   2562                       70771297V1   1319   1951                       70772890V1   1852   2483       43   1344495CB1   2741   1-361, 2693-2741   70267334V1   657   1209                       1860069T6 (PROSNOT18)   1944   2667                       g2577445   2437   2741                       1344495F6 (PROSNOT11)   1   566                       1860069F6 (PROSNOT18)   1083   1873                       70269146V1   2051   2687                       70266807V1   1211   1944                       70270212V1   539   1172                       70267638V1   1803   2365       44   1485774CB1   2076   524-976, 303-332   1617862H1 (BRAITUT12)   1776   2006                       744054R6 (BRAITUT01)   1413   1972                       1485774F6 (CORPNOT02)   1028   1467                       6904024H1 (MUSLTDR02)   1   703                       g3043569_CD   356   1842                       1290195H1 (BRAINOT11)   562   837                       g1242437   1607   2076       45   7289372CB1   2957   1214-1324, 1-236,   7289157H1 (BRAIFER06)   2467   2957                   991-1098,   7252620H2 (BRAIFEE04)   1964   2575                   1803-2480,   7675562J2 (NOSETUE01)   972   1527                   464-920   g772391   1   495                       7290371H1 (BRAIFER06)   1579   2105                       7288441H1 (BRAIFER06)   342   788                       7292572R8 (BRAIFER06)   747   1443                       5090004R8 (UTRSTMR01)   1440   1948       46   1672338CB1   1223   1196-1223,   6609653H1 (EPIGTMC01)   1   609                   652-678   71743918V1   558   1223       47   184661CB1   2888   1331-1592, 1-596,   70160946V1   2386   2888                   2355-2401   7703219J1 (UTRETUE01)   1520   2162                       70160174V1   2176   2810                       71401492V1   620   1168                       70154040V1   2020   2637                       6153426H1 (ENDMUNT04)   1   544                       7192494H2 (BRATDIC01)   1062   1709                       71142234V1   449   1137       48   3719737CB1   3142   3067-3142, 1-409,   71046117V1   2277   2807                   1301-1659,   71047416V1   1375   1784                   761-822   71046670V1   1676   2317                       70064096V1   2614   3142                       4027661F8 (BRAINOT23)   916   1327                       7455730H1 (LIVRTUE01)   1156   1582                       7431827H1 (UTRMTMR02)   543   1071                       7189788H2 (BRATDIC01)   1   603       49   5773251CB1   4749   3194-3442, 1-1545,   71699127V1   1649   2386                   4114-4749,   7091322H1 (BRAUTDR03)   963   1558                   2497-2543   71698165V1   2430   3198                       6981926H1 (BRAIFER05)   1221   1633                       594160T6 (BRAVUNT02)   3989   4604                       7733307H2 (COLDDIE01)   3460   4056                       g3927714   326   712                       71698388V1   2348   3102                       7733307J2 (COLDDIE01)   4181   4749                       70089831V1   3135   3978                       71699024V1   1512   2271                       7754525J1 (SPLNTUE01)   1   570                       7285547H1 (BRAIFEJ01)   650   1140       50   5426470CB1   4155   2222-2681,   6991563H1 (BRAIFER05)   1   478                   4067-4086, 1-171,   6122067H1 (BRAHNON05)   3604   4155                   3250-3606,   5814755F8 (PROSTUS23)   2969   3555                   301-1873   7177748H1 (BRAXDIC01)   2416   3023                       g7959252_CD   442   3284                       5426470T6 (PROSTMT07)   3210   4048                       5426470F6 (PROSTMT07)   2219   2938                       7035583R8 (SINTFER03)   1610   1786                       4329672H1 (KIDNNOT32)   2110   2361                       7178436H1 (BRAXDIC01)   949   1498       51   7087904CB1   1327   943-1327,   7946383H1 (BRABNOE02)   151   976                   267-490   7087904H1 (BRAUTDR03)   1   392                       6312090H1 (NERDTDN03)   605   1327       52   7477312CB1   5529   4005-4070, 1-246,   GNN.g7923864_002   90   2347                   3475-3746,   7102261F8 (BRAWTDR02)   5148   5529                   688-2835,   7314180H1 (LIVRNOE07)   1803   2384                   4856-5529   7719744J1 (SINTFEE02)   2885   3567                       8023704J1 (BRABDIE02)   2342   3058                       7398367H1 (KIDEUNE02)   596   1224                       6953114H1 (BRAITDR02)   3429   4052                       7231729H1 (BRAXTDR15)   4267   4889                       6772109J1 (BRAUNOR01)   4599   5255                       7228637H1 (BRAXTDR15)   3676   4218                       6880723J1 (BRAHTDR03)   4193   4837                       GBI: g7923864.edit   1   503                       7070679R8 (BRAUTDR02)   239   650                       6034612H1 (PITUNOT06)   4974   5501                       7647642J1 (UTRSTUE01)   1362   1642       53   2739431CB1   1623   1-1302   2819460F6 (BRSTNOT14)   1503   1623                       70563142V1   627   1142                       1388139T6 (CARGDIT02)   303   1023                       1388139F6 (CARGDIT02)   1   587                       2737908T6 (OVARNOT09)   975   1599       54   7473606CB1   2242   1053-1326,   2618950T6 (GBLANOT01)   666   863                   252-776, 1-167,   5624160R8 (THYMNOR02)   1892   2242                   864-955,   2618950F6 (GBLANOT01)   1   667                   1401-1490   6770895J1 (BRAUNOR01)   1610   1865                       g5545559   1602   2085                       GNN.g6454068_000018_002.edit   29   1865       55   3534918CB1   3751   854-1195,   6483020H1 (MIXDUNB01)   1355   1880                   593-646, 1-129,   70882296V1   2517   3054                   3709-3751,   70880032V1   3139   3751                   1706-2129   6819410H1 (OVARDIR01)   513   1170                       3736613T6 (SMCCNOS01)   3127   3701                       70879201V1   1925   2526                       GNN.g6634914_000002_002   1   1672                       70879032V1   2483   3011                       70879778V1   1833   2470                       1404901T6 (LATRTUT02)   2984   3670       56   2428715CB1   3579   1-94, 2957-3167   71902796V1   2452   3184                   599-2309   71907111V1   2725   3295                       7362261H1 (BRAIFEE05)   2407   2663                       GNN.g5911819_008.edit   1051   2966                       2428715H1 (SCORNON02)   2359   2590                       6925281R8 (PLACFER06)   2767   3579                       55037058H2   1632   2403                       8186336H1 (EYERNON01)   1   648                       GBI.g5911819_000001.edit   600   1412                       7287205F8 (BRAIFER06)   984   1517                       FL2428715_g6815043_000026_g8052237_1_3-4.edit   466   726                       1736320T6 (COLNNOT22)   4260   4888       57   3351332CB1   5178   4912-5178, 1-3036   71990942V1   3479   4113                   3143-3274,   72036025V1   2484   3377                   3855-4182   71992140V1   2434   3066                       8006270H1 (PENIFEC01)   1743   2484                       7715524H1 (SINTFEE02)   1197   1736                       1736320F6 (COLNNOT22)   4066   4603                       8037780H1 (SMCRUNE01)   1715   2099                       7715524J1 (SINTFEE02)   666   1078                       GNN.g9187279_000012_002.edit   644   1978                       1437833F1 (PANCNOT08)   4690   5178                       GBI.g9844022_000020_000016_000015.edit   272   766                       8037316H1 (SMCRUNE01)   854   1588                       71990329V1   3204   4032                       8037316J1 (SMCRUNE01)   1   639       58   6382722CB1   11367   1-5178   7104534H1 (BRAWTDR02)   4529   5108                       6808001J1 (SKIRNOR01)   5941   6661                       7000837H1 (HEALDIR01)   3133   3749                       7324406H1 (COLRTUE01)   2301   2916                       2778756T6 (OVARTUT03)   10822   11353                       1675050F6 (BLADNOT05)   10293   10903                       6938286R8 (FTUBTUR01)   834   1498                       2951540F6 (KIDNFET01)   10075   10675                       6942017H1 (FTUBTUR01)   2091   2548                       7663312J1 (UTRSTME01)   8747   9415                       7705507H1 (UTRETUE01)   3523   4235                       7716415J1 (SINTFEE02)   8632   9160                       7755720H1 (SPLNTUE01)   4863   5504                       8037265J1 (SMCRUNE01)   3740   4494                       8045466H1 (OVARTUE01)   1434   2165                       7641932J1 (SEMVTDE01)   9355   10078                       7751563H1 (HEAONOE01)   6986   7768                       7076128F6 (BRAUTDR04)   121   881                       7970390H1 (MIXDDIA01)   10912   11367                       7713737H1 (TESTTUE02)   9483   10150                       7755720J1 (SPLNTUE01)   4429   5069                       8045466J1 (OVARTUE01)   1075   1528                       7763930J1 (URETTUE01)   7298   8008                       6975271H1 (BRAHTDR04)   6667   7261                       GNN.g8670608_000002_002.edit   1   297                       7644864J1 (UTRSTUE01)   7987   8616                       7699541H1 (KIDPTDE01)   5176   5894                       6765766H1 (BRAUNOR01)   2543   3057                       6948079H1 (BRAITDR02)   2765   3434                       6759347J1 (HEAONOR01)   5801   6513                       7699541J1 (KIDPTDE01)   6468   7236                       55145718J1   8102   8728       59   55022490CB1   4255   2644-2898, 1-436,   8110806H1 (OSTEUNC01)   1231   1882                   1179-1891   7201271F8 (LUNGFER04)   2265   2964                       8213356H1 (FIBRTXC01)   3680   4255                       7953052H1 (SYNONOC01)   2062   2558                       55022495H1   1   645                       55022496H1   1316   1961                       2939061F6 (THYMFET02)   3185   3774                       55022495J1   608   1248                       55022496J1   661   1310                       7704179H1 (UTRETUE01)   1886   2338                       7346573H1 (SYNODIN02)   2630   3219                       7577135H1 (ADIPUNS02)   3426   4023                       g1382343   3648   4255       60   6755002CB1   3438   1-37, 1548-1618,   5879324F6 (BRAUNOT01)   617   1285                   2405-2610   7630423H1 (BRAFTUE03)   177   711                       6755102H1 (SINTFER02)   84   702                       6337127H1 (BRANDIN01)   1351   1904                       5968891H1 (BRAZNOT01)   2185   2887                       8126594H1 (SCOMDIC01)   863   1538                       1290035H1 (BRAINOT11)   3190   3438                       6555447H1 (BRAFNON02)   2732   3317                       1305462H1 (PLACNOT02)   1   182                       71389138V1   1524   2121                       71185765V1   2086   2672       61   7350907CB1   1683       7350907H1 (COLNNON05)   1299   1683                       6631669J1 (BMARTXR02)   567   1302                       7750841J1 (HEAONOE01)   1   603                       6443310H1 (BRAENOT02)   718   1366       62   7474411CB1   6886   6622-6886,   7222381H1 (PLACFEC01)   2499   3017                   5389-5509, 1-1582,   7737011J1 (BRAITUE01)   6219   6886                   6439-6474,   70870035V1   3823   4452                   1894-1951,   7633045H1 (SINTDIE01)   2306   2579                   2850-4036   8037283J1 (SMCRUNE01)   1014   1741                       2483734F6 (SMCANOT01)   4465   5002                       7755056H1 (SPLNTUE01)   3653   4411                       1603055T6 (BLADNOT03)   5780   6443                       70743936V1   5077   5667                       6822892H1 (SINTNOR01)   1766   2503                       7931495H1 (COLNDIS02)   4915   5652                       8053929J1 (FTUBTUE01)   132   720                       7689270H1 (PROSTME06)   1   458                       6822892J1 (SINTNOR01)   1481   2273                       7644647J1 (UTRSTUE01)   632   1115                       7738773H1 (BRAITUE01)   3004   3655                       7738657H1 (BRAITUE01)   4306   4946                       7688349J1 (PROSTME06)   2589   3035                       71230141V1   3125   3768                       2695328T6 (UTRSNOT12)   5562   6252       63   4755911CB1   4457   1-324, 750-1798,   6773194J1 (BRAUNOR01)   336   1095                   3657-3747,   4755911H1 (BRAHNOT01)   1769   2034                   2407-3438,   g7242966_CD   913   4457                   2273-2326,   6880647J1 (BRAHTDR03)   3285   4044                   3912-4457   6773172H1 (BRAUNOR01)   3132   3908                       6765836H1 (BRAUNOR01)   1902   2429                       7076957H1 (BRAUTDR04)   689   1321                       g953650   311   699                       7371978H2 (BRAIFEE04)   1207   1591                       GNN.g7454228_000009_004.edit   1   4172       64   379766CB1   1943   1-260, 922-1565   71913768V1   1049   1755                       71225395V1   529   1072                       71912043V1   1122   1769                       71910219V1   1291   1943                       1672013H1 (BLADNOT05)   1   221                       7082633R8 (STOMTMR02)   192   957       65   553744CB1   4111   1-580, 2777-2939   3918424H1 (BRAINOT14)   3588   3876                       6610359H2 (MUSTTMC01)   2323   2934                       71249585V1   1666   2217                       3294472T6 (TLYJINT01)   3163   3801                       6338521F7 (BRANDIN01)   1   427                       8016583J1 (BMARTXE01)   531   895                       7467954H1 (LUNGNOE02)   1059   1601                       553744R6 (SCORNOT01)   3799   4110                       1799062T6 (COLNNOT27)   2193   2814                       7167059H1 (PLACNOR01)   147   755                       1304490H1 (PLACNOT02)   3030   3251                       71066496V1   1496   2151                       2219161H1 (LUNGNOT18)   3947   4111                       71065885V1   2537   3206                       7608285J1 (COLRTUE01)   807   1308       66   1825473CB1   1604   1186-1222, 1-662,   71671748V1   957   1604                   697-1075   7977810H1 (LSUBDMC01)   1   614                       7978864H1 (LSUBDMC01)   642   1276                       7978667H1 (LSUBDMC01)   482   1181       67   7950094CB1   2646   1887-1962,   7751102H1 (HEAONOE01)   477   1191                   1358-1427, 1-716,   71824138V1   1889   2577                   2117-2176   1674661F6 (BLADNOT05)   1   503                       71495047V1   608   1350                       7721119H2 (THYRDIE01)   1991   2646                       7675220H1 (NOSETUE01)   1248   1912                       6252635H1 (LUNPTUT02)   529   1205       68   7479484CB1   3876   1855-1892,   GBI.g8569175_000028.edit   580   3876                   1380-1714,   GNN.g8569175_000028_002.edit   1   3579                   2489-2791       69   6780147CB1   2583   720-1210,   6081718H1 (LUNLTUT11)   1909   2583                   2237-2583   2417167F6 (HNT3AZT01)   674   1192                       7220328H1 (SPLNDIC01)   586   1176                       4603304F8 (BRSTNOT07)   1242   1889                       6780147H1 (OVARDIR01)   1111   1709                       3282558T6 (HEAONOT05)   1836   2558                       8116139H1 (TONSDIC01)   1   630       70   7204554CB1   6147   4831-5200,   6321562F6 (LUNGDIN02)   3284   3732                   2698-3091, 1-557,   7655014H1 (UTREDME06)   2035   2634                   3609-4067,   8036632H1 (SMCRUNE01)   1   593                   1239-2254   7655014J1 (UTREDME06)   1286   1880                       6804453H1 (COLENOR03)   762   1352                       7631942H1 (BLADTUE01)   5282   5852                       7292462H1 (BRAIFER06)   2334   2853                       4099025F8 (BRAITUT26)   5241   5762                       6832366H1 (BRSTNON02)   3821   4567                       GBI.g10518389_000002_CDS_5.edit   162   5852                       6814168J1 (ADRETUR01)   4696   5261                       7721587H2 (THYRDIE01)   5641   6147                       6883267J1 (BRAHTDR03)   3504   4216                       7698650J1 (KIDPTDE01)   572   1196                       8239939J1 (LIVRTMR01)   2589   3255                       8076958J1 (ADRETUE02)   4407   5152                       7383235R8 (FTUBTUE01)   1551   2326       71   6833247CB1   888   331-430   498875H1 (NEUTLPT01)   692   888                       6128926H1 (BRAHNON05)   1   432                       6833247T8 (BRSTNON02)   265   879       72   4148119CB1   3582   1681-1740, 1-1470,   g6465050   2274   2694                   2944-3582   7412335H1 (BONMTUE02)   2052   2514                       70776200V1   1409   2028                       1539263R6 (SINTTUT01)   3199   3582                       2212958H1 (SINTFET03)   2452   2684                       4148119F6 (SINITUT04)   2704   3290                       5984846F6 (MCLDTXT02)   1   732                       70776601V1   1053   1616                       7765150J1 (URETTUE01)   614   1285                       70776341V1   1632   2115                    
     [0336]                       TABLE 5                       Polynucleotide   Incyte   Representative       SEQ ID NO:   Project ID   Library                  37   1888682CB1   BRAITUT08       38   1794980CB1   BRAINOT09       39   5533958CB1   CONNTUT04       40   60210196CB1   BRACNOK02       41   815125CB1   BRAENOK01       42   1386915CB1   LATRTUT02       43   1344495CB1   SINTFET03       44   1485774CB1   BRAITUT01       45   7289372CB1   BRAIFER06       46   1672338CB1   CONNNOT01       47   184661CB1   CARDNOT01       48   3719737CB1   KIDETXS02       49   5773251CB1   PLACFER06       50   5426470CB1   PROSTUS23       51   7087904CB1   NERDTDN03       52   7477312CB1   BRABDIE02       53   2739431CB1   OVARNOT09       54   7473606CB1   GBLADIT03       55   3534918CB1   BONRTUT01       56   2428715CB1   PLACFER06       57   3351332CB1   ENDCNOT03       58   6382722CB1   FTUBTUR01       59   55022490CB1   BRAIFEE05       60   6755002CB1   BRAITUT12       61   7350907CB1   BRAENOT02       62   7474411CB1   BRAITUT26       63   4755911CB1   BRAUNOR01       64   379766CB1   NEUTFMT01       65   553744CB1   SEMVNOT01       66   1825473CB1   LSUBDMC01       67   7950094CB1   BLADNOT05       68   7479484CB1   LUNPTUT02       69   6780147CB1   HNT3AZT01       70   7204554CB1   COLENOR03       71   6833247CB1   BRSTNON02       72   4148119CB1   CARGDIT01                    
     [0337]                       TABLE 6                       Library   Vector   Library Description                  BLADNOT05   pINCY   Library was constructed using RNA isolated from bladder tissue removed from a 60-year-               old Caucasian male during a radical cystectomy, prostatectomy, and vasectomy. Pathology               for the associated tumor tissue indicated grade 3 transitional cell carcinoma. Carcinoma               in-situ was identified in the dome and trigone. Patient history included tobacco use.       BONRTUT01   pINCY   Library was constructed using RNA isolated from rib tumor tissue removed from a 16-year-               old Caucasian male during a rib osteotomy and a wedge resection of the lung. Pathology               indicated a metastatic grade 3 (of 4) osteosarcoma, forming a mass involving the chest               wall.       BRABDIE02   pINCY   This 5′ biased random primed library was constructed using RNA isolated from diseased               cerebellum tissue removed from the brain of a 57-year-old Caucasian male who died from a               cerebrovascular accident. Serologies were negative. Patient history included               Huntington&#39;s disease, emphysema, and tobacco abuse (3-4 packs per day, for 40 years).       BRACNOK02   PSPORT1   This amplified and normalized library was constructed using RNA isolated from posterior               cingulate tissue removed from an 85-year-old Caucasian female who died from myocardial               infarction and retroperitoneal hemorrhage. Pathology indicated atherosclerosis, moderate               to severe, involving the circle of Willis, middle cerebral, basilar and vertebral               arteries; infarction, remote, left dentate nucleus; and amyloid plaque deposition               consistent with age. There was mild to moderate leptomeningeal fibrosis, especially over               the convexity of the frontal lobe. There was mild generalized atrophy involving all               lobes. The white matter was mildly thinned. Cortical thickness in the temporal lobes,               both maximal and minimal, was slightly reduced. The substantia nigra pars compacta               appeared mildly depigmented. Patient history included COPD, hypertension, and recurrent               deep venous thrombosis. 6.4 million independent clones from this amplified library were               normalized in one round using conditions adapted Soares et al., PNAS (1994) 91: 9228-9232               and Bonaldo et al., Genome Research 6 (1996): 791.       BRAENOK01   PSPORT1   This amplified and normalized library was constructed using RNA isolated from inferior               parietal cortex tissue removed from a 35-year-old Caucasian male who died from cardiac               failure. Pathology indicated moderate leptomeningeal fibrosis and multiple               microinfarctions of the cerebral neocortex. There was evidence of shrunken and slightly               eosinophilic pyramidal neurons throughout the cerebral hemispheres. There were multiple               small microscopic areas of cavitation with surrounding gliosis scattered throughout the               cerebral cortex. Patient history included dilated cardiomyopathy, congestive heart               failure, and cardiomegaly. Patient medications included simethicone, Lasix, Digoxin,               Colace, Zantac, captopril, and Vasotec. 1.08 million independent clones from this               amplified library were normalized in one round using conditions adapted from Soares et               al., PNAS (1994) 91: 9228-9232 and Bonaldo et al., Genome Research 6 (1996): 791, except               that a significantly longer (48 hours/round) reannealing hybridization was used.       BRAENOT02   pINCY   Library was constructed using RNA isolated from posterior parietal cortex tissue removed               from the brain of a 35-year-old Caucasian male who died from cardiac failure.       BRAIFEE05   PCDNA2.1   This 5′ biased random primed library was constructed using RNA isolated from brain               tissue removed from a Caucasian male fetus who was stillborn with a hypoplastic left               heart at 23 weeks&#39; gestation.       BRAIFER06   PCDNA2.1   This random primed library was constructed using RNA isolated from brain tissue removed               from a Caucasian male fetus who was stillborn with a hypoplastic left heart at 23 weeks&#39;               gestation. Serologies were negative.       BRAINOT09   pINCY   Library was constructed using RNA isolated from brain tissue removed from a Caucasian               male fetus, who died at 23 weeks&#39; gestation.       BRAITUT01   PSPORT1   Library was constructed using RNA isolated from brain tumor tissue removed from a 50-               year-old Caucasian female during a frontal lobectomy. Pathology indicated recurrent               grade 3 oligoastrocytoma with focal necrosis and extensive calcification. Patient               history included a speech disturbance and epilepsy. The patient&#39;s brain had also been               irradiated with a total dose of 5,082 cyg (Fraction 8). Family history included a brain               tumor.       BRAITUT08   pINCY   Library was constructed using RNA isolated from brain tumor tissue removed from the left               frontal lobe of a 47-year-old Caucasian male during excision of cerebral meningeal               tissue. Pathology indicated grade 4 fibrillary astrocytoma with focal tumoral               radionecrosis. Patient history included cerebrovascular disease, deficiency anemia,               hyperlipidemia, epilepsy, and tobacco use. Family history included cerebrovascular               disease and a malignant prostate neoplasm.       BRAITUT12   pINCY   Library was constructed using RNA isolated from brain tumor tissue removed from the left               frontal lobe of a 40-year-old Caucasian female during excision of a cerebral meningeal               lesion. Pathology indicated grade 4 gemistocytic astrocytoma.       BRAITUT26   pINCY   Library was constructed using RNA isolated from brain tumor tissue removed from the               right posterior fossa, occipital convexity of a 70-year-old Caucasian male during               cerebral meninges lesion excision. Pathology indicated meningioma. Patient history               included a benign colon neoplasm and unspecified personality disorder. Family history               included chronic proliferative nephritis, acute myocardial infarction, atherosclerotic               coronary artery disease, and chronic proliferative nephritis.       BRAUNOR01   pINCY   This random primed library was constructed using RNA isolated from striatum, globus               pallidus and posterior putamen tissue removed from an 81-year-old Caucasian female who               died from a hemorrhage and ruptured thoracic aorta due to atherosclerosis. Pathology               indicated moderate atherosclerosis involving the internal carotids, bilaterally;               microscopic infarcts of the frontal cortex and hippocampus; and scattered diffuse               amyloid plaques and neurofibrillary tangles, consistent with age. Grossly, the               leptomeninges showed only mild thickening and hyalinization along the superior sagittal               sinus. The remainder of the leptomeninges was thin and contained some congested blood               vessels. Mild atrophy was found mostly in the frontal poles and lobes, and temporal               lobes, bilaterally. Microscopically, there were pairs of Alzheimer type II astrocytes               within the deep layers of the neocortex. There was increased satellitosis around neurons               in the deep gray matter in the middle frontal cortex. The amygdala contained rare               diffuse plaques and neurofibrillary tangles. The posterior hippocampus contained a               microscopic area of cystic cavitation with hemosiderin-laden macrophages surrounded by               reactive gliosis. Patient history included sepsis, cholangitis, post-operative               atelectasis, pneumonia CAD, cardiomegaly due to left ventricular hypertrophy,               splenomegaly, arteriolonephrosclerosis, nodular colloidal goiter, emphysema, CHF,               hypothyroidism, and peripheral vascular disease.       BRSTNON02   pINCY   This normalized breast tissue library was constructed from 6.2 million independent               clones from a pool of two libraries from two different donors. Starting RNA was made               from breast tissue removed from a 46-year-old Caucasian female during a bilateral               reduction mammoplasty (donor A), and from breast tissue removed from a 60-year-old               Caucasian female during a bilateral reduction mammoplasty (donor B). Pathology indicated               normal breast parenchyma, bilaterally (A) and bilateral mammary hypertrophy (B). Patient               history included hypertrophy of breast, obesity, lumbago, and glaucoma (A) and joint               pain in the shoulder, thyroid cyst, colon cancer, normal delivery and cervical cancer               (B). Family history included cataract, osteoarthritis, uterine cancer, benign               hypertension, hyperlipidemia, and alcoholic cirrhosis of the liver, cerebrovascular               disease, and type II diabetes (A) and cerebrovascular accident, atherosclerotic coronary               artery disease, colon cancer, type II diabetes, hyperlipidemia, depressive disorder, and               Alzheimer&#39;s Disease. The library was normalized in two rounds using conditions adapted               from Soares et al., PNAS (1994) 91: 9228-9232 and Bonaldo et al., Genome Research 6               (1996): 791, except that a significantly longer (48 hours/round) reannealing               hybridization was used.       CARDNOT01   PBLUESCRIPT   Library was constructed using RNA isolated from the cardiac muscle of a 65-year-old               Caucasian male, who died from a gunshot wound.               CARGDIT01 pINCY Library was constructed using RNA isolated from diseased cartilage               tissue. Patient history included osteoarthritis.       COLENOR03   PCDNA2.1   Library was constructed using RNA isolated from colon epithelium tissue removed from a               13-year-old Caucasian female who died from a motor vehicle accident.       CONNNOT01   pINCY   Library was constructed using RNA isolated from mesentery fat tissue obtained from a 71-               year-old Caucasian male during a partial colectomy and permanent colostomy. Family               history included atherosclerotic coronary artery disease, myocardial infarction, and               extrinsic asthma.       CONNTUT04   pINCY   Library was constructed using RNA isolated from tumorous spinal tissue removed from a               35-year-old Caucasian male during an exploratory laparotomy. Pathology indicated               schwannoma with degenerative changes. Patient history included anxiety, depression,               neurofibromatosis and benign neoplasm of the scrotum. Previously the patient had a               spinal fusion. Family history included brain cancer, liver disease, and multiple               sclerosis.       ENDCNOT03   pINCY   Library was constructed using RNA isolated from dermal microvascular endothelial cells               removed from a neonatal Caucasian male.       FTUBTUR01   PCDNA2.1   This random primed library was constructed using RNA isolated from fallopian tube tumor               tissue removed from an 85-year-old Caucasian female during bilateral salpingo-               oophorectomy and hysterectomy. Pathology indicated poorly differentiated mixed               endometrioid (80%) and serous (20%) adenocarcinoma, which was confined to the mucosa               without mural involvement. Endometrioid carcinoma in situ was also present. Pathology               for the associated uterus tumor indicated focal endometrioid adenocarcinoma in situ and               moderately differentiated invasive adenocarcinoma arising in an endometrial polyp.               Metastatic endometrioid and serous adenocarcinoma was present at the cul-de-sac tumor.               Patient history included medullary carcinoma of the thyroid and myocardial infarction.       GBLADIT03   pINCY   Library was constructed using RNA isolated from diseased gallbladder tissue removed from               a 53-year-old Caucasian female during cholecystectomy. Pathology indicated mild chronic               cholecystitis and cholelithiasis with approximately 150 mixed stones ranging in size               from 0.1 cm to 0.5 cm. The patient presented with abdominal pain and nausea and               vomiting. Patient history included hyperlipidema and tobacco and alcohol abuse. Previous               surgeries included adenotonsillectomy. Patient medications included Zantac, Provera,               Premarin, and calcium. Family history included benign hypertension in the mother and the               father.       HNT3AZT01   pINCY   Library was constructed using RNA isolated from the hNT2 cell line (derived from a human               teratocarcinoma that exhibited properties characteristic of a committed neuronal               precursor). Cells were treated for three days with 0.35 micromolar 5-aza-2′-               deoxycytidine (AZ).       KIDETXS02   pINCY   This subtracted, transformed embryonal cell line library was constructed using 9 million               clones from a treated, transformed embryonal cell line (293-EBNA) derived from kidney               epithelial tissue and was subjected to two rounds of subtraction hybridization with 1.9               million clones from an untreated transformed embryonal cell line (293-EBNA) derived from               a kidney epithelial tissue library. The starting library for subtraction was constructed               using RNA isolated from the treated, transformed embryonal cell line (293-EBNA). The               cells were treated with 5-aza-2′-deoxycytidine and transformed with adenovirus 5 DNA.               The hybridization probe for subtraction was derived from a similarly constructed library               from RNA isolated from untreated 293-EBNA cells from the same cell line. Subtractive               hybridization conditions were based on the methodologies of Swaroop et al., NAR 19               (1991): 1954 and Bonaldo, et al. Genome Research (1996) 6: 791.       LATRTUT02   pINCY   Library was constructed using RNA isolated from a myxoma removed from the left atrium of               a 43-year-old Caucasian male during annuloplasty. Pathology indicated atrial myxoma.               Patient history included pulmonary insufficiency, acute myocardial infarction,               atherosclerotic coronary artery disease, hyperlipidemia, and tobacco use. Family history               included benign hypertension, acute myocardial infarction, atherosclerotic coronary               artery disease, and type II diabetes.       LSUBDMC01   PSPORT1   This large size fractionated library was constructed using RNA isolated from               submandibular gland tissue removed from a 49-year-old Caucasian female during               sialoadenectomy. Pathology indicated unremarkable gland. The patient presented with               sialoadenitis. Patient history included vericose veins and normal delivery. Previous               surgeries included cholecystectomy and total abdominal hysterectomy. Patient medications               included vitamins, phentermine HCL, and Pondimin. Family history included               atherosclerotic coronary artery disease and acute myocardial infarction in the mother;               benign hypertension, cerebrovascular accident, atherosclerotic coronary artery disease,               and hyperlipidemia in the sibling(s); and alcohol abuse and depressive disorder in the               grandparent(s).       LUNPTUT02   pINCY   Library was constructed using RNA isolated from pleura tumor tissue removed from a 55-               year-old Caucasian female during complete pneumonectomy. Pathology indicated grade 3               sarcoma most consistent with leiomyosarcoma, uterine primary, forming a bosellated mass               replacing the right lower lobe and a portion of the middle lobe. The tumor involved the               adjacent parietal pleura and pericardium. Multiple nodules comprising the tumor show               near total necrosis. The right upper lobe was atelectic but uninvolved by tumor.               Microsections of cellular nodules show brisk mitotic activity. The pericardium shows               direct involvement but its margins were tumor free. Smooth muscle actin was positive.               Estrogen receptor was negative and progesterone receptor was positive. Patient history               included shortness of breath, peptic ulcer disease, lung cancer, uterine cancer, normal               delivery, tobacco abuse, and deficiency anemia. Previous surgeries included endoscopic               excision of a lung lesion. Family history included atherosclerotic coronary artery               disease, breast cancer, type II diabetes, and multiple sclerosis.       NERDTDN03   pINCY   This normalized dorsal root ganglion tissue library was constructed from 1.05 million               independent clones from a dorsal root ganglion tissue library. Starting RNA was made               from dorsal root ganglion tissue removed from the cervical spine of a 32-year-old               Caucasian male who died from acute pulmonary edema, acute bronchopneumonia, bilateral               pleural effusions, pericardial effusion, and malignant lymphoma (natural killer cell               type). The patient presented with pyrexia of unknown origin, malaise, fatigue, and               gastrointestinal bleeding. Patient history included probable cytomegalovirus infection,               liver congestion, and steatosis, splenomegaly, hemorrhagic cystitis, thyroid hemorrhage,               respiratory failure, pneumonia of the left lung, natural killer cell lymphoma of the               pharynx, Bell&#39;s palsy, and tobacco and alcohol abuse. Previous surgeries included               colonoscopy, closed colon biopsy, adenotonsillectomy, and nasopharyngeal endoscopy and               biopsy. Patient medications included Diflucan (fluconazole), Deltasone (prednisone),               hydrocodone, Lortab, Alprazolam, Reazodone, ProMace-Cytabom, Etoposide, Cisplatin,               Cytarabine, and dexamethasone. The patient received radiation therapy and multiple blood               transfusions. The library was normalized in 2 rounds using conditions adapted from               Soares et al., PNAS (1994) 91: 9228-9232 and Bonaldo et al., Genome Research 6               (1996): 791, except that a significantly longer (48 hours/round) reannealing               hybridization was used.       NEUTFMT01   PBLUESCRIPT   Library was constructed using total RNA isolated from peripheral blood granulocytes               collected by density gradient centrifugation through Ficoll-Hypaque. The cells were               isolated from buffy coat units obtained from unrelated male and female donors. Cells               were cultured in 10 nM fMLP for 30 minutes, lysed in GuSCN, and spun through CsCl to               obtain RNA for library construction. Because this library was made from total RNA, it               has an unusually high proportion of unique singleton sequences, which may not all come               from polyA RNA species.       OVARNOT09   pINCY   Library was constructed using RNA isolated from ovarian tissue removed from a 28-year-               old Caucasian female during a vaginal hysterectomy and removal of the fallopian tubes               and ovaries. Pathology indicated multiple follicular cysts ranging in size from 0.4 to               1.5 cm in the right and left ovaries, chronic cervicitis and squamous metaplasia of the               cervix, and endometrium in weakly proliferative phase. Family history included benign               hypertension, hyperlipidemia, and atherosclerotic coronary artery disease.       PLACFER06   pINCY   This random primed library was constructed using RNA isolated from placental tissue               removed from a Caucasian fetus who died after 16 weeks&#39; gestation from fetal demise and               hydrocephalus. Patient history included umbilical cord wrapped around the head (3 times)               and the shoulders (1 time). Serology was positive for anti-CMV. Family history included               multiple pregnancies and live births, and an abortion.       PROSTUS23   pINCY   This subtracted prostate tumor library was constructed using 10 million clones from a               pooled prostate tumor library that was subjected to 2 rounds of subtractive               hybridization with 10 million clones from a pooled prostate tissue library. The starting               library for subtraction was constructed by pooling equal numbers of clones from 4               prostate tumor libraries using mRNA isolated from prostate tumor removed from Caucasian               males at ages 58 (A), 61 (B), 66 (C) , and 68 (D) during prostatectomy with lymph node               excision. Pathology indicated adenocarcinoma in all donors. History included elevated               PSA, induration and tobacco abuse in donor A; elevated PSA, induration, prostate               hyperplasia, renal failure, osteoarthritis, renal artery stenosis, benign HTN,               thrombocytopenia, hyperlipidemia, tobacco/alcohol abuse and hepatitis C (carrier) in               donor B; elevated PSA, induration, and tobacco abuse in donor C; and elevated PSA,               induration, hypercholesterolemia, and kidney calculus in donor D. The hybridization               probe for subtraction was constructed by pooling equal numbers of cDNA clones from 3               prostate tissue libraries derived from prostate tissue, prostate epithelial cells, and               fibroblasts from prostate stroma from 3 different donors. Subtractive hybridization               conditions were based on the methodologies of Swaroop et al., NAR 19 (1991): 1954 and               Bonaldo, et al. Genome Research 6 (1996): 791.       SEMVNOT01   pINCY   Library was constructed using RNA isolated from seminal vesicle tissue removed from a               58-year-old Caucasian male during radical prostatectomy. Pathology for the associated               tumor tissue indicated adenocarcinoma (Gleason grade 3 + 2) of the prostate.               Adenofibromatous hyperplasia was also present. The patient presented with elevated               prostate specific antigen (PSA). Family history included a malignant breast neoplasm.       SINTFET03   pINCY   Library was constructed using RNA isolated from small intestine tissue removed from a               Caucasian female fetus, who died at 20 weeks&#39; gestation.       CARGDIT01   pINCY   Library was constructed using RNA isolated from diseased cartilage tissue. Patient               history included osteoarthritis.                    
     [0338]                           TABLE 7                       Program   Description   Reference   Parameter Threshold                  ABI   A program that removes vector sequences and   Applied Biosystems, Foster City, CA.           FACTURA   masks ambiguous bases in nucleic acid sequences.       ABI/   A Fast Data Finder useful in comparing and   Applied Biosystems, Foster City, CA;   Mismatch &lt; 50%       PARACEL   annotating amino acid or nucleic acid sequences.   Paracel Inc., Pasadena, CA.       FDF       ABI Auto-   A program that assembles nucleic acid sequences.   Applied Biosystems, Foster City, CA.       Assembler       BLAST   A Basic Local Alignment Search Tool useful in   Altschul, S. F. et al. (1990) J. Mol. Biol.   ESTs: Probability value =           sequence similarity search for amino acid and   215: 403-410; Altschul, S. F. et al. (1997)   1.0E−8 or less           nucleic acid sequences. BLAST includes five   Nucleic Acids Res. 25: 3389-3402.   Full Length sequences:           functions: blastp, blastn, blastx, tblastn, and tblastx.       Probability value = 1.0E−10                   or less       FASTA   A Pearson and Lipman algorithm that searches for   Pearson, W. R. and D. J. Lipman (1988) Proc.   ESTs: fasta E value =           similarity between a query sequence and a group of   Natl. Acad Sci. USA 85: 2444-2448; Pearson,   1.06E−6 Assembled ESTs:           sequences of the same type. FASTA comprises as   W. R. (1990) Methods Enzymol. 183: 63-98;   fasta Identity = 95% or           least five functions: fasta, tfasta, fastx, tfastx, and   and Smith, T. F. and M. S. Waterman (1981)   greater and Match length =           ssearch.   Adv. Appl. Math. 2: 482-489.   200 bases or greater;                   fastx E value = 1.0E−8 or less                   Full Length sequences:                   fastx score = 100 or greater       BLIMPS   A BLocks IMProved Searcher that matches a   Henikoff, S. and J. G. Henikoff (1991) Nucleic   Probability value = 1.0E−3           sequence against those in BLOCKS, PRINTS,   Acids Res. 19: 6565-6572; Henikoff, J. G. and   or less           DOMO, PRODOM, and PFAM databases to search   S. Henikoff (1996) Methods Enzymol.           for gene families, sequence homology, and   266: 88-105; and Attwood, T. K. et al. (1997)           structural fingerprint regions.   J. Chem. Inf. Comput. Sci. 37: 417-424.       HMMER   An algorithm for searching a query sequence against   Krogh, A. et al. (1994) J. Mol. Biol.   PFAM hits: Probability           hidden Markov model (HMM)-based databases of   235: 1501-1531; Sonnhammer, E. L. L. et al.   value = 1.0E−3 or less           protein family consensus sequences, such as PFAM.   (1988) Nucleic Acids Res. 26: 320-322;   Signal peptide hits: Score = 0               Durbin, R. et al. (1998) Our World View, in a   or greater               Nutshell, Cambridge Univ. Press, pp. 1-350.       ProfileScan   An algorithm that searches for structural and sequence   Gribskov, M. et al. (1988) CABIOS 4: 61-66;   Normalized quality score ≧           motifs in protein sequences that match sequence patterns   Gribskov, M. et al. (1989) Methods Enzymol.   GCG-specified “HIGH” value           defined in Prosite.   183: 146-159; Bairoch, A. et al. (1997)   for that particular Prosite               Nucleic Acids Res. 25: 217-221.   motif. Generally, score =                   1.4-2.1.       Phred   A base-calling algorithm that examines automated   Ewing, B. et al. (1998) Genome Res.           sequencer traces with high sensitivity and probability.   8: 175-185; Ewing, B. and P. Green               (1998) Genome Res. 8: 186-194.       Phrap   A Phils Revised Assembly Program including SWAT and   Smith, T. F. and M. S. Waterman (1981) Adv.   Score = 120 or greater;           CrossMatch, programs based on efficient implementation   Appl. Math. 2: 482-489; Smith, T. F. and M.   Match length = 56 or greater           of the Smith-Waterman algorithm, useful in searching   S. Waterman (1981) J. Mol. Biol. 147: 195-           sequence homology and assembling DNA sequences.   197; and Green, P., University of Washington,               Seattle, WA.       Consed   A graphical tool for viewing and editing Phrap   Gordon, D. et al. (1998) Genome Res. 8:           assemblies.   195-202.       SPScan   A weight matrix analysis program that scans protein   Nielson, H. et al. (1997) Protein Engineering   Score = 3.5 or greater           sequences for the presence of secretory signal peptides.   10: 1-6; Claverie, J. M. and S. Audic (1997)               CABIOS 12: 431-439.       TMAP   A program that uses weight matrices to delineate   Persson, B. and P. Argos (1994) J. Mol. Biol.           transmembrane segments on protein sequences and   237: 182-192; Persson, B. and P. Argos (1996)           determine orientation.   Protein Sci. 5: 363-371.       TMHMMER   A program that uses a hidden Markov model (HMM) to   Sonnhammer, E. L. et al. (1998) Proc. Sixth           delineate transmembrane segments on protein sequences   Intl. Conf. on Intelligent Systems for Mol.           and determine orientation.   Biol., Glasgow et al., eds., The Am. Assoc.               for Artificial Intelligence Press, Menlo Park,               CA, pp. 175-182.       Motifs   A program that searches amino acid sequences for   Bairoch, A. et al. (1997) Nucleic Acids Res.           patterns that matched those defined in Prosite.   25: 217-221; Wisconsin Package Program               Manual, version 9, page M51-59, Genetics               Computer Group, Madison, WI.                    
     [0339] 
    
     
       
         1 
         
           
             72  
           
           
             1  
             234  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1888682CD1  
             
           
            1 

Met Pro Ser Gly Cys His Ser Ser Pro Pro Ser Gly Leu Arg Gly 
  1               5                  10                  15 

Asp Met Ala Ser Leu Val Pro Leu Ser Pro Tyr Leu Ser Pro Thr 
                 20                  25                  30 

Val Leu Leu Leu Val Ser Cys Asp Leu Gly Phe Val Arg Ala Asp 
                 35                  40                  45 

Arg Pro Pro Ser Pro Val Asn Val Thr Val Thr His Leu Arg Ala 
                 50                  55                  60 

Asn Ser Ala Thr Val Ser Trp Asp Val Pro Glu Gly Asn Ile Val 
                 65                  70                  75 

Ile Gly Tyr Ser Ile Ser Gln Gln Arg Gln Asn Gly Pro Gly Gln 
                 80                  85                  90 

Arg Val Ile Arg Glu Val Asn Thr Thr Thr Arg Ala Cys Ala Leu 
                 95                 100                 105 

Trp Gly Leu Ala Glu Asp Ser Asp Tyr Thr Val Gln Val Arg Ser 
                110                 115                 120 

Ile Gly Leu Arg Gly Glu Ser Pro Pro Gly Pro Arg Val His Phe 
                125                 130                 135 

Arg Thr Leu Lys Gly Ser Asp Arg Leu Pro Ser Asn Ser Ser Ser 
                140                 145                 150 

Pro Gly Asp Ile Thr Val Glu Gly Leu Asp Gly Glu Arg Pro Leu 
                155                 160                 165 

Gln Thr Gly Glu Val Val Ile Ile Val Val Val Leu Leu Met Trp 
                170                 175                 180 

Ala Ala Val Ile Gly Leu Phe Cys Arg Gln Tyr Asp Ile Ile Lys 
                185                 190                 195 

Asp Asn Asp Ser Asn Asn Asn Pro Lys Glu Lys Gly Lys Gly Pro 
                200                 205                 210 

Glu Gln Ser Pro Gln Gly Arg Pro Val Gly Thr Arg Gln Lys Lys 
                215                 220                 225 

Ser Pro Ser Ile Asn Thr Ile Asp Val 
                230 

 
           
             2  
             443  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1794980CD1  
             
           
            2 

Met Gly Gly Pro Arg Ala Trp Ala Leu Leu Cys Leu Gly Leu Leu 
  1               5                  10                  15 

Leu Pro Gly Gly Gly Ala Ala Trp Ser Ile Gly Ala Ala Pro Phe 
                 20                  25                  30 

Ser Gly Arg Arg Asn Trp Cys Ser Tyr Val Val Thr Arg Thr Ile 
                 35                  40                  45 

Ser Cys His Val Gln Asn Gly Thr Tyr Leu Gln Arg Val Leu Gln 
                 50                  55                  60 

Asn Cys Pro Trp Pro Met Ser Cys Pro Gly Ser Ser Tyr Arg Thr 
                 65                  70                  75 

Val Val Arg Pro Thr Tyr Lys Val Met Tyr Lys Ile Val Thr Ala 
                 80                  85                  90 

Arg Glu Trp Arg Cys Cys Pro Gly His Ser Gly Val Ser Cys Glu 
                 95                 100                 105 

Glu Val Ala Ala Ser Ser Ala Ser Leu Glu Pro Met Trp Ser Gly 
                110                 115                 120 

Ser Thr Met Arg Arg Met Ala Leu Arg Pro Thr Ala Phe Ser Gly 
                125                 130                 135 

Cys Leu Asn Cys Ser Lys Val Ser Glu Leu Thr Glu Arg Leu Lys 
                140                 145                 150 

Val Leu Glu Ala Lys Met Thr Met Leu Thr Val Ile Glu Gln Pro 
                155                 160                 165 

Val Pro Pro Thr Pro Ala Thr Pro Glu Asp Pro Ala Pro Leu Trp 
                170                 175                 180 

Gly Pro Pro Pro Ala Gln Gly Ser Pro Gly Asp Gly Gly Leu Gln 
                185                 190                 195 

Asp Gln Val Gly Ala Trp Gly Leu Pro Gly Pro Thr Gly Pro Lys 
                200                 205                 210 

Gly Asp Ala Gly Ser Arg Gly Pro Met Gly Met Arg Gly Pro Pro 
                215                 220                 225 

Gly Pro Gln Gly Pro Pro Gly Ser Pro Gly Arg Ala Gly Ala Val 
                230                 235                 240 

Gly Thr Pro Gly Glu Arg Gly Pro Pro Gly Pro Pro Gly Pro Pro 
                245                 250                 255 

Gly Pro Pro Gly Pro Pro Ala Pro Val Gly Pro Pro His Ala Arg 
                260                 265                 270 

Ile Ser Gln His Gly Asp Pro Leu Leu Ser Asn Thr Phe Thr Glu 
                275                 280                 285 

Thr Asn Asn His Trp Pro Gln Gly Pro Thr Gly Pro Pro Gly Pro 
                290                 295                 300 

Pro Gly Pro Met Gly Pro Pro Gly Pro Pro Gly Pro Thr Gly Val 
                305                 310                 315 

Pro Gly Ser Pro Gly His Ile Gly Pro Pro Gly Pro Thr Gly Pro 
                320                 325                 330 

Lys Gly Ile Ser Gly His Pro Gly Glu Lys Gly Glu Arg Gly Leu 
                335                 340                 345 

Arg Gly Glu Pro Gly Pro Gln Gly Ser Ala Gly Gln Arg Gly Glu 
                350                 355                 360 

Pro Gly Pro Lys Gly Asp Pro Gly Glu Lys Ser His Trp Gly Glu 
                365                 370                 375 

Gly Leu His Gln Leu Arg Glu Ala Leu Lys Ile Leu Ala Glu Arg 
                380                 385                 390 

Val Leu Ile Leu Glu Thr Met Ile Gly Leu Tyr Glu Pro Glu Leu 
                395                 400                 405 

Gly Ser Gly Ala Gly Pro Ala Gly Thr Gly Thr Pro Ser Leu Leu 
                410                 415                 420 

Arg Gly Lys Arg Gly Gly His Ala Thr Asn Tyr Arg Ile Val Ala 
                425                 430                 435 

Pro Arg Ser Arg Asp Glu Arg Gly 
                440 

 
           
             3  
             261  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5533958CD1  
             
           
            3 

Met Gly Gly Ala Gly Ile Leu Leu Leu Leu Leu Ala Gly Ala Gly 
  1               5                  10                  15 

Val Val Val Ala Trp Arg Pro Pro Lys Gly Lys Cys Pro Leu Arg 
                 20                  25                  30 

Cys Ser Cys Ser Lys Asp Ser Ala Leu Cys Glu Gly Ser Pro Asp 
                 35                  40                  45 

Leu Pro Val Ser Phe Ser Pro Thr Leu Leu Ser Leu Ser Leu Val 
                 50                  55                  60 

Arg Thr Gly Val Thr Gln Leu Lys Ala Gly Ser Phe Leu Arg Ile 
                 65                  70                  75 

Pro Ser Leu His Leu Leu Leu Phe Thr Ser Asn Ser Phe Ser Val 
                 80                  85                  90 

Ile Glu Asp Asp Ala Phe Ala Gly Leu Ser His Leu Gln Tyr Leu 
                 95                 100                 105 

Phe Ile Glu Asp Asn Glu Ile Gly Ser Ile Ser Lys Asn Ala Leu 
                110                 115                 120 

Arg Gly Leu Arg Ser Leu Thr His Leu Ser Leu Ala Asn Asn His 
                125                 130                 135 

Leu Glu Thr Leu Pro Arg Phe Leu Phe Arg Gly Leu Asp Thr Leu 
                140                 145                 150 

Thr His Val Asp Leu Arg Gly Asn Pro Phe Gln Cys Asp Cys Arg 
                155                 160                 165 

Val Leu Trp Leu Leu Gln Trp Met Pro Thr Val Asn Ala Ser Val 
                170                 175                 180 

Gly Thr Gly Ala Cys Ala Gly Pro Ala Ser Leu Ser His Met Gln 
                185                 190                 195 

Leu His His Leu Asp Pro Lys Thr Phe Lys Cys Arg Ala Ile Gly 
                200                 205                 210 

Gly Gly Leu Ser Arg Trp Gly Gly Arg Arg Glu Ile Trp Gly Lys 
                215                 220                 225 

Gly Cys Gln Gly Gln Glu Ala Arg Leu Thr Pro Cys Pro Ala Ile 
                230                 235                 240 

Ser Arg Ser Gly Lys Thr Leu Ser Lys Gln His Cys Leu Pro Glu 
                245                 250                 255 

Pro Gln Phe Ser His Leu 
                260 

 
           
             4  
             643  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 60210196CD1  
             
           
            4 

Met Glu Pro Val Pro Leu Gln Asp Phe Val Arg Ala Leu Asp Pro 
  1               5                  10                  15 

Ala Ser Leu Pro Arg Val Leu Arg Val Cys Ser Gly Val Tyr Phe 
                 20                  25                  30 

Glu Gly Ser Ile Tyr Glu Ile Ser Gly Asn Glu Cys Cys Leu Ser 
                 35                  40                  45 

Thr Gly Asp Leu Ile Lys Val Thr Gln Val Arg Leu Gln Lys Val 
                 50                  55                  60 

Val Cys Glu Asn Pro Lys Thr Ser Gln Thr Met Glu Leu Ala Pro 
                 65                  70                  75 

Asn Phe Gln Gly Tyr Phe Thr Pro Leu Asn Thr Pro Gln Ser Tyr 
                 80                  85                  90 

Glu Thr Leu Glu Glu Leu Val Ser Ala Thr Thr Gln Ser Ser Lys 
                 95                 100                 105 

Gln Leu Pro Thr Cys Phe Met Ser Thr His Arg Ile Val Thr Glu 
                110                 115                 120 

Gly Arg Val Val Thr Glu Asp Gln Leu Leu Met Leu Glu Ala Val 
                125                 130                 135 

Val Met His Leu Gly Ile Arg Ser Ala Arg Cys Val Leu Gly Met 
                140                 145                 150 

Glu Gly Gln Gln Val Ile Leu His Leu Pro Leu Ser Gln Lys Gly 
                155                 160                 165 

Pro Phe Trp Thr Trp Glu Pro Ser Ala Pro Arg Thr Leu Leu Gln 
                170                 175                 180 

Val Leu Gln Asp Pro Ala Leu Lys Asp Leu Val Leu Thr Cys Pro 
                185                 190                 195 

Thr Leu Pro Trp His Ser Leu Ile Leu Arg Pro Gln Tyr Glu Ile 
                200                 205                 210 

Gln Ala Ile Met His Met Arg Arg Thr Ile Val Lys Ile Pro Ser 
                215                 220                 225 

Thr Leu Glu Val Asp Val Glu Asp Val Thr Ala Ser Ser Arg His 
                230                 235                 240 

Val His Phe Ile Lys Pro Leu Leu Leu Ser Glu Val Leu Ala Trp 
                245                 250                 255 

Glu Gly Pro Phe Pro Leu Ser Met Glu Ile Leu Glu Val Pro Glu 
                260                 265                 270 

Gly Arg Pro Ile Phe Leu Ser Pro Trp Val Gly Ser Leu Gln Lys 
                275                 280                 285 

Gly Gln Arg Leu Cys Val Tyr Gly Leu Ala Ser Pro Pro Trp Arg 
                290                 295                 300 

Val Leu Ala Ser Ser Lys Gly Arg Lys Val Pro Arg His Phe Leu 
                305                 310                 315 

Val Ser Gly Gly Tyr Gln Gly Lys Leu Arg Arg Arg Pro Arg Glu 
                320                 325                 330 

Phe Pro Thr Ala Tyr Asp Leu Leu Gly Ala Phe Gln Pro Gly Arg 
                335                 340                 345 

Pro Leu Arg Val Val Ala Thr Lys Asp Cys Glu Gly Glu Arg Glu 
                350                 355                 360 

Glu Asn Pro Glu Phe Thr Ser Leu Ala Val Gly Asp Arg Leu Glu 
                365                 370                 375 

Val Leu Gly Pro Gly Gln Ala His Gly Ala Gln Gly Ser Asp Val 
                380                 385                 390 

Asp Val Leu Val Cys Gln Arg Leu Ser Asp Gln Ala Gly Glu Asp 
                395                 400                 405 

Glu Glu Glu Glu Cys Lys Glu Glu Ala Glu Ser Pro Glu Arg Val 
                410                 415                 420 

Leu Leu Pro Phe His Phe Pro Gly Ser Phe Val Glu Glu Met Ser 
                425                 430                 435 

Asp Ser Arg Arg Tyr Ser Leu Ala Asp Leu Thr Ala Gln Phe Ser 
                440                 445                 450 

Leu Pro Cys Glu Val Lys Val Val Ala Lys Asp Thr Ser His Pro 
                455                 460                 465 

Thr Asp Pro Leu Thr Ser Phe Leu Gly Leu Arg Leu Glu Glu Lys 
                470                 475                 480 

Ile Thr Glu Pro Phe Leu Val Val Ser Leu Asp Ser Glu Pro Gly 
                485                 490                 495 

Met Cys Phe Glu Ile Pro Pro Arg Trp Leu Asp Leu Thr Val Val 
                500                 505                 510 

Lys Ala Lys Gly Gln Pro Asp Leu Pro Glu Gly Ser Leu Pro Ile 
                515                 520                 525 

Ala Thr Val Glu Glu Leu Thr Asp Thr Phe Tyr Tyr Arg Leu Arg 
                530                 535                 540 

Lys Leu Pro Ala Cys Glu Ile Gln Ala Pro Pro Pro Arg Pro Pro 
                545                 550                 555 

Lys Asn Gln Gly Leu Ser Lys Gln Arg Arg His Ser Ser Glu Gly 
                560                 565                 570 

Gly Val Lys Ser Ser Gln Val Leu Gly Leu Gln Gln His Ala Arg 
                575                 580                 585 

Leu Pro Lys Pro Lys Ala Lys Thr Leu Pro Glu Phe Ile Lys Asp 
                590                 595                 600 

Gly Ser Ser Thr Tyr Ser Lys Ile Pro Ala His Arg Lys Gly His 
                605                 610                 615 

Arg Pro Ala Lys Pro Gln Arg Gln Asp Leu Asp Asp Asp Glu His 
                620                 625                 630 

Asp Tyr Glu Glu Ile Leu Glu Gln Phe Gln Lys Thr Ile 
                635                 640 

 
           
             5  
             628  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 815125CD1  
             
           
            5 

Met Gly Ser Cys Ala Arg Leu Leu Leu Leu Trp Gly Cys Thr Val 
  1               5                  10                  15 

Val Ala Ala Gly Leu Ser Gly Val Ala Gly Val Ser Ser Arg Cys 
                 20                  25                  30 

Glu Lys Ala Cys Asn Pro Arg Met Gly Asn Leu Ala Leu Gly Arg 
                 35                  40                  45 

Lys Leu Trp Ala Asp Thr Thr Cys Gly Gln Asn Ala Thr Glu Leu 
                 50                  55                  60 

Tyr Cys Phe Tyr Ser Glu Asn Thr Asp Leu Thr Cys Arg Gln Pro 
                 65                  70                  75 

Lys Cys Asp Lys Cys Asn Ala Ala Tyr Pro His Leu Ala His Leu 
                 80                  85                  90 

Pro Ser Ala Met Ala Asp Ser Ser Phe Arg Phe Pro Arg Thr Trp 
                 95                 100                 105 

Trp Gln Ser Ala Glu Asp Val His Arg Glu Lys Val Gln Leu Asp 
                110                 115                 120 

Leu Glu Ala Glu Phe Tyr Phe Thr His Leu Ile Val Met Phe Lys 
                125                 130                 135 

Ser Pro Arg Pro Ala Ala Met Val Leu Asp Arg Ser Gln Asp Phe 
                140                 145                 150 

Gly Lys Thr Trp Lys Pro Tyr Lys Tyr Phe Ala Thr Asn Cys Ser 
                155                 160                 165 

Ala Thr Phe Gly Leu Glu Asp Asp Val Val Lys Lys Gly Ala Ile 
                170                 175                 180 

Cys Thr Ser Lys Tyr Ser Ser Pro Phe Pro Cys Thr Gly Gly Glu 
                185                 190                 195 

Val Ile Phe Lys Ala Leu Ser Pro Pro Tyr Asp Thr Glu Asn Pro 
                200                 205                 210 

Tyr Ser Ala Lys Val Gln Glu Gln Leu Lys Ile Thr Asn Leu Arg 
                215                 220                 225 

Val Gln Leu Leu Lys Arg Gln Ser Cys Pro Cys Gln Arg Asn Asp 
                230                 235                 240 

Leu Asn Glu Glu Pro Gln His Phe Thr His Tyr Ala Ile Tyr Asp 
                245                 250                 255 

Phe Ile Val Lys Gly Ser Cys Phe Cys Asn Gly His Ala Asp Gln 
                260                 265                 270 

Cys Ile Pro Val His Gly Phe Arg Pro Val Lys Ala Pro Gly Thr 
                275                 280                 285 

Phe His Met Val His Gly Lys Cys Met Cys Lys His Asn Thr Ala 
                290                 295                 300 

Gly Ser His Cys Gln His Cys Ala Pro Leu Tyr Asn Asp Arg Pro 
                305                 310                 315 

Trp Glu Ala Ala Asp Gly Lys Thr Gly Ala Pro Asn Glu Cys Arg 
                320                 325                 330 

Thr Cys Lys Cys Asn Gly His Ala Asp Thr Cys His Phe Asp Val 
                335                 340                 345 

Asn Val Trp Glu Ala Ser Gly Asn Arg Ser Gly Gly Val Cys Asp 
                350                 355                 360 

Asp Cys Gln His Asn Thr Glu Gly Gln Tyr Cys Gln Arg Cys Lys 
                365                 370                 375 

Pro Gly Phe Tyr Arg Asp Leu Arg Arg Pro Phe Ser Ala Pro Asp 
                380                 385                 390 

Ala Cys Lys Pro Cys Ser Cys His Pro Val Gly Ser Ala Val Leu 
                395                 400                 405 

Pro Ala Asn Ser Val Thr Phe Cys Asp Pro Ser Asn Gly Asp Cys 
                410                 415                 420 

Pro Cys Lys Pro Gly Val Ala Gly Arg Arg Cys Asp Arg Cys Met 
                425                 430                 435 

Val Gly Tyr Trp Gly Phe Gly Asp Tyr Gly Cys Arg Pro Cys Asp 
                440                 445                 450 

Cys Ala Gly Ser Cys Asp Pro Ile Thr Gly Asp Cys Ile Ser Ser 
                455                 460                 465 

His Thr Asp Ile Asp Trp Tyr His Glu Val Pro Asp Phe Arg Pro 
                470                 475                 480 

Val His Asn Lys Ser Glu Pro Ala Trp Glu Trp Glu Asp Ala Gln 
                485                 490                 495 

Gly Phe Ser Ala Leu Leu His Ser Gly Lys Cys Glu Cys Lys Glu 
                500                 505                 510 

Gln Thr Leu Gly Asn Ala Lys Ala Phe Cys Gly Met Lys Tyr Ser 
                515                 520                 525 

Tyr Val Leu Lys Ile Lys Ile Leu Ser Ala His Asp Lys Gly Thr 
                530                 535                 540 

His Val Glu Val Asn Val Lys Ile Lys Lys Val Leu Lys Ser Thr 
                545                 550                 555 

Lys Leu Lys Ile Phe Arg Gly Lys Arg Thr Leu Tyr Pro Glu Ser 
                560                 565                 570 

Trp Thr Asp Arg Gly Cys Thr Cys Pro Ile Leu Asn Pro Gly Leu 
                575                 580                 585 

Glu Tyr Leu Val Ala Gly His Glu Asp Ile Arg Thr Gly Lys Leu 
                590                 595                 600 

Ile Val Asn Met Lys Ser Phe Val Gln His Trp Lys Pro Ser Leu 
                605                 610                 615 

Gly Arg Lys Val Met Asp Ile Leu Lys Arg Glu Cys Lys 
                620                 625 

 
           
             6  
             686  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1386915CD1  
             
           
            6 

Met Leu Leu Arg Gly Val Leu Leu Ala Leu Gln Ala Leu Gln Leu 
  1               5                  10                  15 

Ala Gly Ala Leu Asp Leu Pro Ala Gly Ser Cys Ala Phe Glu Glu 
                 20                  25                  30 

Ser Thr Cys Gly Phe Asp Ser Val Leu Ala Ser Leu Pro Trp Ile 
                 35                  40                  45 

Leu Asn Glu Glu Gly His Tyr Ile Tyr Val Asp Thr Ser Phe Gly 
                 50                  55                  60 

Lys Gln Gly Glu Lys Ala Val Leu Leu Ser Pro Asp Leu Gln Ala 
                 65                  70                  75 

Glu Glu Trp Ser Cys Leu Arg Leu Val Tyr Gln Ile Thr Thr Ser 
                 80                  85                  90 

Ser Glu Ser Leu Ser Asp Pro Ser Gln Leu Asn Leu Tyr Met Arg 
                 95                 100                 105 

Phe Glu Asp Glu Ser Phe Asp Arg Leu Leu Trp Ser Ala Lys Glu 
                110                 115                 120 

Pro Ser Asp Ser Trp Leu Ile Ala Ser Leu Asp Leu Gln Asn Ser 
                125                 130                 135 

Ser Lys Lys Phe Lys Ile Leu Ile Glu Gly Val Leu Gly Gln Gly 
                140                 145                 150 

Asn Thr Ala Ser Ile Ala Leu Phe Glu Ile Lys Met Thr Thr Gly 
                155                 160                 165 

Tyr Cys Ile Glu Cys Asp Phe Glu Glu Asn His Leu Cys Gly Phe 
                170                 175                 180 

Val Asn Arg Trp Asn Pro Asn Val Asn Trp Phe Val Gly Gly Gly 
                185                 190                 195 

Ser Ile Arg Asn Val His Ser Ile Leu Pro Gln Asp His Thr Phe 
                200                 205                 210 

Lys Ser Glu Leu Gly His Tyr Met Tyr Val Asp Ser Val Tyr Val 
                215                 220                 225 

Lys His Phe Gln Glu Val Ala Gln Leu Ile Ser Pro Leu Thr Thr 
                230                 235                 240 

Ala Pro Met Ala Gly Cys Leu Ser Phe Tyr Tyr Gln Ile Gln Gln 
                245                 250                 255 

Gly Asn Asp Asn Val Phe Ser Leu Tyr Thr Arg Asp Val Ala Gly 
                260                 265                 270 

Leu Tyr Glu Glu Ile Trp Lys Ala Asp Arg Pro Gly Asn Ala Ala 
                275                 280                 285 

Trp Asn Leu Ala Glu Val Glu Phe Asn Ala Pro Tyr Pro Met Glu 
                290                 295                 300 

Val Ile Phe Glu Val Ala Phe Asn Gly Pro Lys Gly Gly Tyr Val 
                305                 310                 315 

Ala Leu Asp Asp Ile Ser Phe Ser Pro Val His Cys Gln Asn Gln 
                320                 325                 330 

Thr Glu Leu Leu Phe Ser Ala Val Glu Ala Ser Cys Asn Phe Glu 
                335                 340                 345 

Gln Asp Leu Cys Asn Phe Tyr Gln Asp Lys Glu Gly Pro Gly Trp 
                350                 355                 360 

Thr Arg Val Lys Val Lys Pro Asn Met Tyr Arg Ala Gly Asp His 
                365                 370                 375 

Thr Thr Gly Leu Gly Tyr Tyr Leu Leu Ala Asn Thr Lys Phe Thr 
                380                 385                 390 

Ser Gln Pro Gly Tyr Ile Gly Arg Leu Tyr Gly Pro Ser Leu Pro 
                395                 400                 405 

Gly Asn Leu Gln Tyr Cys Leu Arg Phe His Tyr Ala Ile Tyr Gly 
                410                 415                 420 

Phe Leu Lys Met Ser Asp Thr Leu Ala Val Tyr Ile Phe Glu Glu 
                425                 430                 435 

Asn His Val Val Gln Glu Lys Ile Trp Ser Val Leu Glu Ser Pro 
                440                 445                 450 

Arg Gly Val Trp Met Gln Ala Glu Ile Thr Phe Lys Lys Pro Met 
                455                 460                 465 

Pro Thr Lys Val Val Phe Met Ser Leu Cys Lys Ser Phe Trp Asp 
                470                 475                 480 

Cys Gly Leu Val Ala Leu Asp Asp Ile Thr Ile Gln Leu Gly Ser 
                485                 490                 495 

Cys Ser Ser Ser Glu Lys Leu Pro Pro Pro Pro Gly Glu Cys Thr 
                500                 505                 510 

Phe Glu Gln Asp Glu Cys Thr Phe Thr Gln Glu Lys Arg Asn Arg 
                515                 520                 525 

Ser Ser Trp His Arg Arg Arg Gly Glu Thr Pro Thr Ser Tyr Thr 
                530                 535                 540 

Gly Pro Lys Gly Asp His Thr Thr Gly Val Gly Tyr Tyr Met Tyr 
                545                 550                 555 

Ile Glu Ala Ser His Met Val Tyr Gly Gln Lys Ala Arg Leu Leu 
                560                 565                 570 

Ser Arg Pro Leu Arg Gly Val Ser Gly Lys His Cys Leu Thr Phe 
                575                 580                 585 

Phe Tyr His Met Tyr Gly Gly Gly Thr Gly Leu Leu Ser Val Tyr 
                590                 595                 600 

Leu Lys Lys Glu Glu Asp Ser Glu Glu Ser Leu Leu Trp Arg Arg 
                605                 610                 615 

Arg Gly Glu Gln Ser Ile Ser Trp Leu Arg Ala Leu Ile Glu Tyr 
                620                 625                 630 

Ser Cys Glu Arg Gln His Gln Ile Ile Phe Glu Ala Ile Arg Gly 
                635                 640                 645 

Val Ser Ile Arg Ser Asp Ile Ala Ile Asp Asp Val Lys Phe Gln 
                650                 655                 660 

Ala Gly Pro Cys Gly Glu Met Glu Asp Thr Thr Gln Gln Ser Ser 
                665                 670                 675 

Gly Tyr Ser Glu Asp Leu Asn Glu Ile Glu Tyr 
                680                 685 

 
           
             7  
             296  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1344495CD1  
             
           
            7 

Met Arg His Glu Glu Leu Leu Thr Lys Thr Phe Gln Gly Pro Ala 
  1               5                  10                  15 

Val Val Cys Gly Thr Pro Thr Ser His Val Tyr Met Phe Lys Asn 
                 20                  25                  30 

Gly Ser Gly Asp Ser Gly Asp Ser Ser Glu Glu Glu Ser His Arg 
                 35                  40                  45 

Val Val Leu Arg Pro Arg Gly Lys Glu Arg His Lys Ser Gly Val 
                 50                  55                  60 

His Gln Pro Pro Gln Ala Gly Ala Gly Asp Val Val Leu Leu Gln 
                 65                  70                  75 

Arg Glu Leu Ala Gln Glu Asp Ser Leu Asn Lys Leu Ala Leu Gln 
                 80                  85                  90 

Tyr Gly Cys Lys Val Ala Asp Ile Lys Lys Val Asn Asn Phe Ile 
                 95                 100                 105 

Arg Glu Gln Asp Leu Tyr Ala Leu Lys Ser Val Lys Ile Pro Val 
                110                 115                 120 

Arg Asn His Gly Ile Leu Met Glu Thr His Lys Glu Leu Lys Pro 
                125                 130                 135 

Leu Leu Ser Pro Ser Ser Glu Thr Thr Val Thr Val Glu Leu Pro 
                140                 145                 150 

Glu Ala Asp Arg Ala Gly Ala Gly Thr Gly Ala Gln Ala Gly Gln 
                155                 160                 165 

Leu Met Gly Phe Phe Lys Gly Ile Asp Gln Asp Ile Glu Arg Ala 
                170                 175                 180 

Val Gln Ser Glu Ile Phe Leu His Glu Ser Tyr Cys Met Asp Thr 
                185                 190                 195 

Ser His Gln Pro Leu Leu Pro Ala Pro Pro Lys Thr Pro Met Asp 
                200                 205                 210 

Gly Ala Asp Cys Gly Ile Gln Trp Trp Asn Ala Val Phe Ile Met 
                215                 220                 225 

Leu Leu Ile Gly Ile Val Leu Pro Val Phe Tyr Leu Val Tyr Phe 
                230                 235                 240 

Lys Ile Gln Ala Ser Gly Glu Thr Pro Asn Ser Leu Asn Thr Thr 
                245                 250                 255 

Val Ile Pro Asn Gly Ser Met Ala Met Gly Thr Val Pro Gly Gln 
                260                 265                 270 

Ala Pro Arg Leu Ala Val Ala Val Pro Ala Val Thr Ser Ala Asp 
                275                 280                 285 

Ser Gln Phe Ser Gln Thr Thr Gln Ala Gly Ser 
                290                 295 

 
           
             8  
             575  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1485774CD1  
             
           
            8 

Met Ala Lys Pro Phe Phe Arg Leu Gln Lys Phe Leu Arg Arg Thr 
  1               5                  10                  15 

Gln Phe Leu Leu Phe Phe Leu Thr Ala Ala Tyr Leu Met Thr Gly 
                 20                  25                  30 

Ser Leu Leu Leu Leu Gln Arg Val Arg Val Ala Leu Pro Gln Gly 
                 35                  40                  45 

Pro Arg Ala Pro Gly Pro Leu Gln Thr Leu Pro Val Ala Ala Val 
                 50                  55                  60 

Ala Leu Gly Val Gly Leu Leu Asp Ser Arg Ala Leu His Asp Pro 
                 65                  70                  75 

Arg Val Ser Pro Glu Leu Leu Leu Gly Val Asp Met Leu Gln Ser 
                 80                  85                  90 

Pro Leu Thr Arg Pro Arg Pro Gly Pro Arg Trp Leu Arg Ser Arg 
                 95                 100                 105 

Asn Ser Glu Leu Arg Gln Leu Arg Arg Arg Trp Phe His His Phe 
                110                 115                 120 

Met Ser Asp Ser Gln Gly Pro Pro Ala Leu Gly Pro Glu Ala Ala 
                125                 130                 135 

Arg Pro Ala Ile His Ser Arg Gly Thr Tyr Ile Gly Cys Phe Ser 
                140                 145                 150 

Asp Asp Gly His Glu Arg Thr Leu Lys Gly Ala Val Phe Tyr Asp 
                155                 160                 165 

Leu Arg Lys Met Thr Val Ser His Cys Gln Asp Ala Cys Ala Glu 
                170                 175                 180 

Arg Ser Tyr Val Tyr Ala Gly Leu Glu Ala Gly Ala Glu Cys Tyr 
                185                 190                 195 

Cys Gly Asn Arg Leu Pro Ala Val Ser Val Gly Leu Glu Glu Cys 
                200                 205                 210 

Asn His Glu Cys Lys Gly Glu Lys Gly Ser Val Cys Gly Ala Val 
                215                 220                 225 

Asp Arg Leu Ser Val Tyr Arg Val Asp Glu Leu Gln Pro Gly Ser 
                230                 235                 240 

Arg Lys Arg Arg Thr Ala Thr Tyr Arg Gly Cys Phe Arg Leu Pro 
                245                 250                 255 

Glu Asn Ile Thr His Ala Phe Pro Ser Ser Leu Ile Gln Ala Asn 
                260                 265                 270 

Val Thr Val Gly Thr Cys Ser Gly Phe Cys Ser Gln Lys Glu Phe 
                275                 280                 285 

Pro Leu Ala Ile Leu Arg Gly Trp Glu Cys Tyr Cys Ala Tyr Pro 
                290                 295                 300 

Thr Pro Arg Phe Asn Leu Arg Asp Ala Met Asp Ser Ser Val Cys 
                305                 310                 315 

Gly Gln Asp Pro Glu Ala Gln Arg Leu Ala Glu Tyr Cys Glu Val 
                320                 325                 330 

Tyr Gln Thr Pro Val Gln Asp Thr Arg Cys Thr Asp Arg Arg Phe 
                335                 340                 345 

Leu Pro Asn Lys Ser Lys Val Phe Val Ala Leu Ser Ser Phe Pro 
                350                 355                 360 

Gly Ala Gly Asn Thr Trp Ala Arg His Leu Ile Glu His Ala Thr 
                365                 370                 375 

Gly Phe Tyr Thr Gly Ser Tyr Tyr Phe Asp Gly Thr Leu Tyr Asn 
                380                 385                 390 

Lys Gly Phe Lys Gly Glu Lys Asp His Trp Arg Ser Arg Arg Thr 
                395                 400                 405 

Ile Cys Val Lys Thr His Glu Ser Gly Arg Arg Glu Ile Glu Met 
                410                 415                 420 

Ser Asp Ser Ala Ile Leu Leu Ile Arg Asn Pro Tyr Arg Ser Leu 
                425                 430                 435 

Val Ala Glu Phe Asn Arg Lys Cys Ala Gly His Leu Gly Tyr Ala 
                440                 445                 450 

Ala Asp Arg Asn Trp Lys Ser Lys Glu Trp Pro Asp Phe Val Asn 
                455                 460                 465 

Ser Tyr Ala Ser Trp Trp Ser Ser His Val Leu Asp Trp Leu Lys 
                470                 475                 480 

Tyr Gly Lys Arg Leu Leu Val Val His Tyr Glu Glu Leu Arg Arg 
                485                 490                 495 

Ser Leu Val Pro Thr Leu Arg Glu Met Val Ala Phe Leu Asn Val 
                500                 505                 510 

Ser Val Ser Glu Glu Arg Leu Leu Cys Val Glu Asn Asn Lys Glu 
                515                 520                 525 

Gly Ser Phe Arg Arg Arg Gly Arg Arg Ser His Asp Pro Glu Pro 
                530                 535                 540 

Phe Thr Pro Glu Met Lys Asp Leu Ile Asn Gly Tyr Ile Arg Thr 
                545                 550                 555 

Val Asp Gln Ala Leu Arg Asp His Asn Trp Thr Gly Leu Pro Arg 
                560                 565                 570 

Glu Tyr Val Pro Arg 
                575 

 
           
             9  
             592  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7289372CD1  
             
           
            9 

Met Phe Pro Leu Arg Ala Leu Trp Leu Val Trp Ala Leu Leu Gly 
  1               5                  10                  15 

Val Ala Gly Ser Cys Pro Glu Pro Cys Ala Cys Val Asp Lys Tyr 
                 20                  25                  30 

Ala His Gln Phe Ala Asp Cys Ala Tyr Lys Glu Leu Arg Glu Val 
                 35                  40                  45 

Pro Glu Gly Leu Pro Ala Asn Val Thr Thr Leu Ser Leu Ser Ala 
                 50                  55                  60 

Asn Lys Ile Thr Val Leu Arg Arg Gly Ala Phe Ala Asp Val Thr 
                 65                  70                  75 

Gln Val Thr Ser Leu Trp Leu Ala His Asn Glu Val Arg Thr Val 
                 80                  85                  90 

Glu Pro Gly Ala Leu Ala Val Leu Ser Gln Leu Lys Asn Leu Asp 
                 95                 100                 105 

Leu Ser His Asn Phe Ile Ser Ser Phe Pro Trp Ser Asp Leu Arg 
                110                 115                 120 

Asn Leu Ser Ala Leu Gln Leu Leu Lys Met Asn His Asn Arg Leu 
                125                 130                 135 

Gly Ser Leu Pro Arg Asp Ala Leu Gly Ala Leu Pro Asp Leu Arg 
                140                 145                 150 

Ser Leu Arg Ile Asn Asn Asn Arg Leu Arg Thr Leu Ala Pro Gly 
                155                 160                 165 

Thr Phe Asp Ala Leu Ser Ala Leu Ser His Leu Gln Leu Tyr His 
                170                 175                 180 

Asn Pro Phe His Cys Gly Cys Gly Leu Val Trp Leu Gln Ala Trp 
                185                 190                 195 

Ala Ala Ser Thr Arg Val Ser Leu Pro Glu Pro Asp Ser Ile Ala 
                200                 205                 210 

Cys Ala Ser Pro Pro Ala Leu Gln Gly Val Pro Val Tyr Arg Leu 
                215                 220                 225 

Pro Ala Leu Pro Cys Ala Pro Pro Ser Val His Leu Ser Ala Glu 
                230                 235                 240 

Pro Pro Leu Glu Ala Pro Gly Thr Pro Leu Arg Ala Gly Leu Ala 
                245                 250                 255 

Phe Val Leu His Cys Ile Ala Asp Gly His Pro Thr Pro Arg Leu 
                260                 265                 270 

Gln Trp Gln Leu Gln Ile Pro Gly Gly Thr Val Val Leu Glu Pro 
                275                 280                 285 

Pro Val Leu Ser Gly Glu Asp Asp Gly Val Gly Ala Glu Glu Gly 
                290                 295                 300 

Glu Gly Glu Gly Asp Gly Asp Leu Leu Thr Gln Thr Gln Ala Gln 
                305                 310                 315 

Thr Pro Thr Pro Ala Pro Ala Trp Pro Ala Pro Pro Ala Thr Pro 
                320                 325                 330 

Arg Phe Leu Ala Leu Ala Asn Gly Ser Leu Leu Val Pro Leu Leu 
                335                 340                 345 

Ser Ala Lys Glu Ala Gly Val Tyr Thr Cys Arg Ala His Asn Glu 
                350                 355                 360 

Leu Gly Ala Asn Ser Thr Ser Ile Arg Val Ala Val Ala Ala Thr 
                365                 370                 375 

Gly Pro Pro Lys His Ala Pro Gly Ala Gly Gly Glu Pro Asp Gly 
                380                 385                 390 

Gln Ala Pro Thr Ser Glu Arg Lys Ser Thr Ala Lys Gly Arg Gly 
                395                 400                 405 

Asn Ser Val Leu Pro Ser Lys Pro Glu Gly Lys Ile Lys Gly Gln 
                410                 415                 420 

Gly Leu Ala Lys Val Ser Ile Leu Gly Glu Thr Glu Thr Glu Pro 
                425                 430                 435 

Glu Glu Asp Thr Ser Glu Gly Glu Glu Ala Glu Asp Gln Ile Leu 
                440                 445                 450 

Ala Asp Pro Ala Glu Glu Gln Arg Cys Gly Asn Gly Asp Pro Ser 
                455                 460                 465 

Arg Tyr Val Ser Asn His Ala Phe Asn Gln Ser Ala Glu Leu Lys 
                470                 475                 480 

Pro His Val Phe Glu Leu Gly Val Ile Ala Leu Asp Val Ala Glu 
                485                 490                 495 

Arg Glu Ala Arg Val Gln Leu Thr Pro Leu Ala Ala Arg Trp Gly 
                500                 505                 510 

Pro Gly Pro Gly Gly Ala Gly Gly Ala Pro Arg Pro Gly Arg Arg 
                515                 520                 525 

Pro Leu Arg Leu Leu Tyr Leu Cys Pro Ala Gly Gly Gly Ala Ala 
                530                 535                 540 

Val Gln Trp Ser Arg Val Glu Glu Gly Val Asn Ala Tyr Trp Phe 
                545                 550                 555 

Arg Gly Leu Arg Pro Gly Thr Asn Tyr Ser Val Cys Leu Ala Leu 
                560                 565                 570 

Ala Gly Glu Ala Cys His Val Gln Val Val Phe Pro Pro Arg Arg 
                575                 580                 585 

Ser Ser His Arg Cys Trp Ser 
                590 

 
           
             10  
             255  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1672338CD1  
             
           
            10 

Met Ala Leu Pro Ala Leu Gly Leu Asp Pro Trp Ser Leu Leu Gly 
  1               5                  10                  15 

Leu Phe Leu Phe Gln Leu Leu Gln Leu Leu Leu Pro Thr Thr Thr 
                 20                  25                  30 

Ala Gly Gly Gly Gly Gln Gly Pro Met Pro Arg Val Arg Tyr Tyr 
                 35                  40                  45 

Ala Gly Asp Glu Arg Arg Ala Leu Ser Phe Phe His Gln Lys Gly 
                 50                  55                  60 

Leu Gln Asp Phe Asp Thr Leu Leu Leu Ser Gly Asp Gly Asn Thr 
                 65                  70                  75 

Leu Tyr Val Gly Ala Arg Glu Ala Ile Leu Ala Leu Asp Ile Gln 
                 80                  85                  90 

Asp Pro Gly Val Pro Arg Leu Lys Asn Met Ile Pro Trp Pro Ala 
                 95                 100                 105 

Ser Asp Arg Lys Lys Ser Glu Cys Ala Phe Lys Lys Lys Ser Asn 
                110                 115                 120 

Glu Thr Gln Cys Phe Asn Phe Ile Arg Val Leu Val Ser Tyr Asn 
                125                 130                 135 

Val Thr His Leu Tyr Thr Cys Gly Thr Phe Ala Phe Ser Pro Ala 
                140                 145                 150 

Cys Thr Phe Ile Val Ser Ser Leu Val Pro Ser Ala Gln Ala Pro 
                155                 160                 165 

Lys His Pro Phe Ser His Leu Pro Thr Thr Phe Leu Cys Ser Ser 
                170                 175                 180 

Gly Lys Leu Trp Pro Ser Arg Cys Arg Thr Leu Met Asn Phe Leu 
                185                 190                 195 

Ala Pro Asp Gln Phe Pro Ser Met Ser Leu Ser Leu Pro Ser Ser 
                200                 205                 210 

Ser Pro Ser Phe Pro Arg Cys Glu Thr Leu Ala Phe Trp Pro Pro 
                215                 220                 225 

Ser Leu Ser Pro His Leu Gly Thr Ser Arg Phe Leu Pro Val Ala 
                230                 235                 240 

His Leu Gly Gly Gln Gly His Gly Gly Lys Arg Pro Lys Pro Leu 
                245                 250                 255 

 
           
             11  
             641  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 184661CD1  
             
           
            11 

Met Val Pro Gly Ala Arg Gly Gly Gly Ala Leu Ala Arg Ala Ala 
  1               5                  10                  15 

Gly Arg Gly Leu Leu Ala Leu Leu Leu Ala Val Ser Ala Pro Leu 
                 20                  25                  30 

Arg Leu Gln Ala Glu Glu Leu Gly Asp Gly Cys Gly His Leu Val 
                 35                  40                  45 

Thr Tyr Gln Asp Ser Gly Thr Met Thr Ser Lys Asn Tyr Pro Gly 
                 50                  55                  60 

Thr Tyr Pro Asn His Thr Val Cys Glu Lys Thr Ile Thr Val Pro 
                 65                  70                  75 

Lys Gly Lys Arg Leu Ile Leu Arg Leu Gly Asp Leu Asp Ile Glu 
                 80                  85                  90 

Ser Gln Thr Cys Ala Ser Asp Tyr Leu Leu Phe Thr Ser Ser Ser 
                 95                 100                 105 

Asp Gln Tyr Gly Pro Tyr Cys Gly Ser Met Thr Val Pro Lys Glu 
                110                 115                 120 

Leu Leu Leu Asn Thr Ser Glu Val Thr Val Arg Phe Glu Ser Gly 
                125                 130                 135 

Ser His Ile Ser Gly Arg Gly Phe Leu Leu Thr Tyr Ala Ser Ser 
                140                 145                 150 

Asp His Pro Asp Leu Ile Thr Cys Leu Glu Arg Ala Ser His Tyr 
                155                 160                 165 

Leu Lys Thr Glu Tyr Ser Lys Phe Cys Pro Ala Gly Cys Arg Asp 
                170                 175                 180 

Val Ala Gly Asp Ile Ser Gly Asn Met Val Asp Gly Tyr Arg Asp 
                185                 190                 195 

Thr Ser Leu Leu Cys Lys Ala Ala Ile His Ala Gly Ile Ile Ala 
                200                 205                 210 

Asp Glu Leu Gly Gly Gln Ile Ser Val Leu Gln Arg Lys Gly Ile 
                215                 220                 225 

Ser Arg Tyr Glu Gly Ile Leu Ala Asn Gly Val Leu Ser Arg Asp 
                230                 235                 240 

Gly Ser Leu Ser Asp Lys Arg Phe Leu Phe Thr Ser Asn Gly Cys 
                245                 250                 255 

Ser Arg Ser Leu Ser Phe Glu Pro Asp Gly Gln Ile Arg Ala Ser 
                260                 265                 270 

Ser Ser Trp Gln Ser Val Asn Glu Ser Gly Asp Gln Val His Trp 
                275                 280                 285 

Ser Pro Gly Gln Ala Arg Leu Gln Asp Gln Gly Pro Ser Trp Ala 
                290                 295                 300 

Ser Gly Asp Ser Ser Asn Asn His Lys Pro Arg Glu Trp Leu Glu 
                305                 310                 315 

Ile Asp Leu Gly Glu Lys Lys Lys Ile Thr Gly Ile Arg Thr Thr 
                320                 325                 330 

Gly Ser Thr Gln Ser Asn Phe Asn Phe Tyr Val Lys Ser Phe Val 
                335                 340                 345 

Met Asn Phe Lys Asn Asn Asn Ser Lys Trp Lys Thr Tyr Lys Gly 
                350                 355                 360 

Ile Val Asn Asn Glu Glu Lys Val Phe Gln Gly Asn Ser Asn Phe 
                365                 370                 375 

Arg Asp Pro Val Gln Asn Asn Phe Ile Pro Pro Ile Val Ala Arg 
                380                 385                 390 

Tyr Val Arg Val Val Pro Gln Thr Trp His Gln Arg Ile Ala Leu 
                395                 400                 405 

Lys Val Glu Leu Ile Gly Cys Gln Ile Thr Gln Gly Asn Asp Ser 
                410                 415                 420 

Leu Val Trp Arg Lys Thr Ser Gln Ser Thr Ser Val Ser Thr Lys 
                425                 430                 435 

Lys Glu Asp Glu Thr Ile Thr Arg Pro Ile Pro Ser Glu Glu Thr 
                440                 445                 450 

Ser Thr Gly Ile Asn Ile Thr Thr Val Ala Ile Pro Leu Val Leu 
                455                 460                 465 

Leu Val Val Leu Val Phe Ala Gly Met Gly Ile Phe Ala Ala Phe 
                470                 475                 480 

Arg Lys Lys Lys Lys Lys Gly Ser Pro Tyr Gly Ser Ala Glu Ala 
                485                 490                 495 

Gln Lys Thr Asp Cys Trp Lys Gln Ile Lys Tyr Pro Phe Ala Arg 
                500                 505                 510 

His Gln Ser Ala Glu Phe Thr Ile Ser Tyr Asp Asn Glu Lys Glu 
                515                 520                 525 

Met Thr Gln Lys Leu Asp Leu Ile Thr Ser Asp Met Ala Asp Tyr 
                530                 535                 540 

Gln Gln Pro Leu Met Ile Gly Thr Gly Thr Val Thr Arg Lys Gly 
                545                 550                 555 

Ser Thr Phe Arg Pro Met Asp Thr Asp Ala Glu Glu Ala Gly Val 
                560                 565                 570 

Ser Thr Asp Ala Gly Gly His Tyr Asp Cys Pro Gln Arg Ala Gly 
                575                 580                 585 

Arg His Glu Tyr Ala Leu Pro Trp Arg Pro Arg Ser Pro Ser Thr 
                590                 595                 600 

Pro Arg Pro Ser Trp Ser Gly Thr Cys Cys Ala Pro Thr Arg Ser 
                605                 610                 615 

Leu Arg Arg Ala Ala Thr Ala Ser Gln Gly Pro Ser Pro Ala Thr 
                620                 625                 630 

Asn Thr Pro Ser Pro Arg Ala Ala Ser Pro Pro 
                635                 640 

 
           
             12  
             924  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3719737CD1  
             
           
            12 

Met Gly Arg Leu His Arg Pro Arg Ser Ser Thr Ser Tyr Arg Asn 
  1               5                  10                  15 

Leu Pro His Leu Phe Leu Phe Phe Leu Phe Val Gly Pro Phe Ser 
                 20                  25                  30 

Cys Leu Gly Ser Tyr Ser Arg Ala Thr Glu Leu Leu Tyr Ser Leu 
                 35                  40                  45 

Asn Glu Gly Leu Pro Ala Gly Val Leu Ile Gly Ser Leu Ala Glu 
                 50                  55                  60 

Asp Leu Arg Leu Leu Pro Arg Ser Ala Gly Arg Pro Asp Pro Gln 
                 65                  70                  75 

Ser Gln Leu Pro Glu Arg Thr Gly Ala Glu Trp Asn Pro Pro Leu 
                 80                  85                  90 

Ser Phe Ser Leu Ala Ser Arg Gly Leu Ser Gly Gln Tyr Val Thr 
                 95                 100                 105 

Leu Asp Asn Arg Ser Gly Glu Leu His Thr Ser Ala Gln Glu Ile 
                110                 115                 120 

Asp Arg Glu Ala Leu Cys Val Glu Gly Gly Gly Gly Thr Ala Trp 
                125                 130                 135 

Ser Gly Ser Val Ser Ile Ser Ser Ser Pro Ser Asp Ser Cys Leu 
                140                 145                 150 

Leu Leu Leu Asp Val Leu Val Leu Pro Gln Glu Tyr Phe Arg Phe 
                155                 160                 165 

Val Lys Val Lys Ile Ala Ile Arg Asp Ile Asn Asp Asn Ala Pro 
                170                 175                 180 

Gln Phe Pro Val Ser Gln Ile Ser Val Trp Val Pro Glu Asn Ala 
                185                 190                 195 

Pro Val Asn Thr Arg Leu Ala Ile Glu His Pro Ala Val Asp Pro 
                200                 205                 210 

Asp Val Gly Ile Asn Gly Val Gln Thr Tyr Arg Leu Leu Asp Tyr 
                215                 220                 225 

His Gly Met Phe Thr Leu Asp Val Glu Glu Asn Glu Asn Gly Glu 
                230                 235                 240 

Arg Thr Pro Tyr Leu Ile Val Met Gly Ala Leu Asp Arg Glu Thr 
                245                 250                 255 

Gln Asp Gln Tyr Val Ser Ile Ile Ile Ala Glu Asp Gly Gly Ser 
                260                 265                 270 

Pro Pro Leu Leu Gly Ser Ala Thr Leu Thr Ile Gly Ile Ser Asp 
                275                 280                 285 

Ile Asn Asp Asn Cys Pro Leu Phe Thr Asp Ser Gln Ile Asn Val 
                290                 295                 300 

Thr Val Tyr Gly Asn Ala Thr Val Gly Thr Pro Ile Ala Ala Val 
                305                 310                 315 

Gln Ala Val Asp Lys Asp Leu Gly Thr Asn Ala Gln Ile Thr Tyr 
                320                 325                 330 

Ser Tyr Ser Gln Lys Val Pro Gln Ala Ser Lys Asp Leu Phe His 
                335                 340                 345 

Leu Asp Glu Asn Thr Gly Val Ile Lys Leu Phe Ser Lys Ile Gly 
                350                 355                 360 

Gly Ser Val Leu Glu Ser His Lys Leu Thr Ile Leu Ala Asn Gly 
                365                 370                 375 

Pro Gly Cys Ile Pro Ala Val Ile Thr Ala Leu Val Ser Ile Ile 
                380                 385                 390 

Lys Val Ile Phe Arg Pro Pro Glu Ile Val Pro Arg Tyr Ile Ala 
                395                 400                 405 

Asn Glu Ile Asp Gly Val Val Tyr Leu Lys Glu Leu Glu Pro Val 
                410                 415                 420 

Asn Thr Pro Ile Ala Phe Phe Thr Ile Arg Asp Pro Glu Gly Lys 
                425                 430                 435 

Tyr Lys Val Asn Cys Tyr Leu Asp Gly Glu Gly Pro Phe Arg Leu 
                440                 445                 450 

Ser Pro Tyr Lys Pro Tyr Asn Asn Glu Tyr Leu Leu Glu Thr Thr 
                455                 460                 465 

Lys Pro Met Asp Tyr Glu Leu Gln Gln Phe Tyr Glu Val Ala Val 
                470                 475                 480 

Val Ala Trp Asn Ser Glu Gly Phe His Val Lys Arg Val Ile Lys 
                485                 490                 495 

Val Gln Leu Leu Asp Asp Asn Asp Asn Ala Pro Ile Phe Leu Gln 
                500                 505                 510 

Pro Leu Ile Glu Leu Thr Ile Glu Glu Asn Asn Ser Pro Asn Ala 
                515                 520                 525 

Phe Leu Thr Lys Leu Tyr Ala Thr Asp Ala Asp Ser Glu Glu Arg 
                530                 535                 540 

Gly Gln Val Ser Tyr Phe Leu Gly Pro Asp Ala Pro Ser Tyr Phe 
                545                 550                 555 

Ser Leu Asp Ser Val Thr Gly Ile Leu Thr Val Ser Thr Gln Leu 
                560                 565                 570 

Asp Arg Glu Glu Lys Glu Lys Tyr Arg Tyr Thr Val Arg Ala Val 
                575                 580                 585 

Asp Cys Gly Lys Pro Pro Arg Glu Ser Val Ala Thr Val Ala Leu 
                590                 595                 600 

Thr Val Leu Asp Lys Asn Asp Asn Ser Pro Arg Phe Ile Asn Lys 
                605                 610                 615 

Asp Phe Ser Phe Phe Val Pro Glu Asn Phe Pro Gly Tyr Gly Glu 
                620                 625                 630 

Ile Gly Val Ile Ser Val Thr Asp Ala Asp Ala Gly Arg Asn Gly 
                635                 640                 645 

Trp Val Ala Leu Ser Val Val Asn Gln Ser Asp Ile Phe Val Ile 
                650                 655                 660 

Asp Thr Gly Lys Gly Met Leu Arg Ala Lys Val Ser Leu Asp Arg 
                665                 670                 675 

Glu Gln Gln Ser Ser Tyr Thr Leu Trp Val Glu Ala Val Asp Gly 
                680                 685                 690 

Gly Glu Pro Ala Leu Ser Ser Thr Ala Lys Ile Thr Ile Leu Leu 
                695                 700                 705 

Leu Asp Ile Asn Asp Asn Pro Pro Leu Val Leu Phe Pro Gln Ser 
                710                 715                 720 

Asn Met Ser Tyr Leu Leu Val Leu Pro Ser Thr Leu Pro Gly Ser 
                725                 730                 735 

Pro Val Thr Glu Val Tyr Ala Val Asp Lys Asp Thr Gly Met Asn 
                740                 745                 750 

Ala Val Ile Ala Tyr Ser Ile Ile Gly Arg Arg Gly Pro Arg Pro 
                755                 760                 765 

Glu Ser Phe Arg Ile Asp Pro Lys Thr Gly Asn Ile Thr Leu Glu 
                770                 775                 780 

Glu Ala Leu Leu Gln Thr Asp Tyr Gly Leu His Arg Leu Leu Val 
                785                 790                 795 

Lys Val Ser Asp His Gly Tyr Pro Glu Pro Leu His Ser Thr Val 
                800                 805                 810 

Met Val Asn Leu Phe Val Asn Asp Thr Val Ser Asn Glu Ser Tyr 
                815                 820                 825 

Ile Glu Ser Leu Leu Arg Lys Glu Pro Glu Ile Asn Ile Glu Glu 
                830                 835                 840 

Lys Glu Pro Gln Ile Ser Ile Glu Pro Thr His Arg Lys Val Glu 
                845                 850                 855 

Ser Val Ser Cys Met Pro Thr Leu Val Ala Leu Ser Val Ile Ser 
                860                 865                 870 

Leu Gly Ser Ile Thr Leu Val Thr Gly Met Gly Ile Tyr Ile Cys 
                875                 880                 885 

Leu Arg Lys Gly Glu Lys His Pro Arg Glu Asp Glu Asn Leu Glu 
                890                 895                 900 

Val Gln Ile Pro Leu Lys Gly Lys Ile Asp Leu His Met Arg Glu 
                905                 910                 915 

Arg Lys Pro Met Asp Ile Ser Asn Ile 
                920 

 
           
             13  
             987  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5773251CD1  
             
           
            13 

Met Arg Ile Ser Ser Cys Ser Asp Glu Ser Ser Asn Ser Asn Ser 
  1               5                  10                  15 

Ser Arg Lys Ser Asp Asn His Ser Pro Ala Val Val Thr Thr Thr 
                 20                  25                  30 

Val Ser Ser Lys Lys Gln Pro Ser Val Leu Val Thr Phe Pro Lys 
                 35                  40                  45 

Glu Glu Arg Lys Ser Val Ser Gly Lys Ala Ser Ile Lys Leu Ser 
                 50                  55                  60 

Glu Thr Ile Ser Glu Gly Thr Ser Asn Ser Leu Ser Thr Cys Thr 
                 65                  70                  75 

Lys Ser Gly Pro Ser Pro Leu Ser Ser Pro Asn Gly Lys Leu Thr 
                 80                  85                  90 

Val Ala Ser Pro Lys Arg Gly Gln Lys Arg Glu Glu Gly Trp Lys 
                 95                 100                 105 

Glu Val Val Arg Arg Ser Lys Lys Val Ser Val Pro Ser Thr Val 
                110                 115                 120 

Ile Ser Arg Val Ile Gly Arg Gly Gly Cys Asn Ile Asn Ala Ile 
                125                 130                 135 

Arg Glu Phe Thr Gly Ala His Ile Asp Ile Asp Lys Gln Lys Asp 
                140                 145                 150 

Lys Thr Gly Asp Arg Ile Ile Thr Ile Arg Gly Gly Thr Glu Ser 
                155                 160                 165 

Thr Arg Gln Ala Thr Gln Leu Ile Asn Ala Leu Ile Lys Asp Pro 
                170                 175                 180 

Asp Lys Glu Ile Asp Glu Leu Ile Pro Lys Asn Arg Leu Lys Ser 
                185                 190                 195 

Ser Ser Ala Asn Ser Lys Ile Gly Ser Ser Ala Pro Thr Thr Thr 
                200                 205                 210 

Ala Ala Asn Thr Ser Leu Met Gly Ile Lys Met Thr Thr Val Ala 
                215                 220                 225 

Leu Ser Ser Thr Ser Gln Thr Ala Thr Ala Leu Thr Val Pro Ala 
                230                 235                 240 

Ile Ser Ser Ala Ser Thr His Lys Thr Ile Lys Asn Pro Val Asn 
                245                 250                 255 

Asn Val Arg Pro Gly Phe Pro Val Ser Leu Pro Leu Ala Tyr Pro 
                260                 265                 270 

Pro Pro Gln Phe Ala His Ala Leu Leu Ala Ala Gln Thr Phe Gln 
                275                 280                 285 

Gln Ile Arg Pro Pro Arg Leu Pro Met Thr His Phe Gly Gly Thr 
                290                 295                 300 

Phe Pro Pro Ala Gln Ser Thr Trp Gly Pro Phe Pro Val Arg Pro 
                305                 310                 315 

Leu Ser Pro Ala Arg Ala Thr Asn Ser Pro Lys Pro His Met Val 
                320                 325                 330 

Pro Arg His Ser Asn Gln Asn Ser Ser Gly Ser Gln Val Asn Ser 
                335                 340                 345 

Ala Gly Ser Leu Thr Ser Ser Pro Thr Thr Thr Thr Ser Ser Ser 
                350                 355                 360 

Ala Ser Thr Val Pro Gly Thr Ser Thr Asn Gly Ser Pro Ser Ser 
                365                 370                 375 

Pro Ser Val Arg Arg Gln Leu Phe Val Thr Val Val Lys Thr Ser 
                380                 385                 390 

Asn Ala Thr Thr Thr Thr Val Thr Thr Thr Ala Ser Asn Asn Asn 
                395                 400                 405 

Thr Ala Pro Thr Asn Ala Thr Tyr Pro Met Pro Thr Ala Lys Glu 
                410                 415                 420 

His Tyr Pro Val Ser Ser Pro Ser Ser Pro Ser Pro Pro Ala Gln 
                425                 430                 435 

Pro Gly Gly Val Ser Arg Asn Ser Pro Leu Asp Cys Gly Ser Ala 
                440                 445                 450 

Ser Pro Asn Lys Val Ala Ser Ser Ser Glu Gln Glu Ala Gly Ser 
                455                 460                 465 

Pro Pro Val Val Glu Thr Thr Asn Thr Arg Pro Pro Asn Ser Ser 
                470                 475                 480 

Ser Ser Ser Gly Ser Ser Ser Ala His Ser Asn Gln Gln Gln Pro 
                485                 490                 495 

Pro Gly Ser Val Ser Gln Glu Pro Arg Pro Pro Leu Gln Gln Ser 
                500                 505                 510 

Gln Val Pro Pro Pro Glu Val Arg Met Thr Val Pro Pro Leu Ala 
                515                 520                 525 

Thr Ser Ser Ala Pro Val Ala Val Pro Ser Thr Ala Pro Val Thr 
                530                 535                 540 

Tyr Pro Met Pro Gln Thr Pro Met Gly Cys Pro Gln Pro Thr Pro 
                545                 550                 555 

Lys Met Glu Thr Pro Ala Ile Arg Pro Pro Pro His Gly Thr Thr 
                560                 565                 570 

Ala Pro His Lys Asn Ser Ala Ser Val Gln Asn Ser Ser Val Ala 
                575                 580                 585 

Val Leu Ser Val Asn His Ile Lys Arg Pro His Ser Val Pro Ser 
                590                 595                 600 

Ser Val Gln Leu Pro Ser Thr Leu Ser Thr Gln Ser Ala Cys Gln 
                605                 610                 615 

Asn Ser Val His Pro Ala Asn Lys Pro Ile Ala Pro Asn Phe Ser 
                620                 625                 630 

Ala Pro Leu Pro Phe Gly Pro Phe Ser Thr Leu Phe Glu Asn Ser 
                635                 640                 645 

Pro Thr Ser Ala His Ala Phe Trp Gly Gly Ser Val Val Ser Ser 
                650                 655                 660 

Gln Ser Thr Pro Glu Ser Met Leu Ser Gly Lys Ser Ser Tyr Leu 
                665                 670                 675 

Pro Asn Ser Asp Pro Leu His Gln Ser Asp Thr Ser Lys Ala Pro 
                680                 685                 690 

Gly Phe Arg Pro Pro Leu Gln Arg Pro Ala Pro Ser Pro Ser Gly 
                695                 700                 705 

Ile Val Asn Met Asp Ser Pro Tyr Gly Ser Val Thr Pro Ser Ser 
                710                 715                 720 

Thr His Leu Gly Asn Phe Ala Ser Asn Ile Ser Gly Gly Gln Met 
                725                 730                 735 

Tyr Gly Pro Gly Ala Pro Leu Gly Gly Ala Pro Ala Ala Ala Asn 
                740                 745                 750 

Phe Asn Arg Gln His Phe Ser Pro Leu Ser Leu Leu Thr Pro Cys 
                755                 760                 765 

Ser Ser Ala Ser Asn Asp Ser Ser Ala Gln Ser Val Ser Ser Gly 
                770                 775                 780 

Val Arg Ala Pro Ser Pro Ala Pro Ser Ser Val Pro Leu Gly Ser 
                785                 790                 795 

Glu Lys Pro Ser Asn Val Ser Gln Asp Arg Lys Val Pro Val Pro 
                800                 805                 810 

Ile Gly Thr Glu Arg Ser Ala Arg Ile Arg Gln Thr Gly Thr Ser 
                815                 820                 825 

Ala Pro Ser Val Ile Gly Ser Asn Leu Ser Thr Ser Val Gly His 
                830                 835                 840 

Ser Gly Ile Trp Ser Phe Glu Gly Ile Gly Gly Asn Gln Asp Lys 
                845                 850                 855 

Val Asp Trp Cys Asn Pro Gly Met Gly Asn Pro Met Ile His Arg 
                860                 865                 870 

Pro Met Ser Asp Pro Gly Val Phe Ser Gln His Gln Ala Met Glu 
                875                 880                 885 

Arg Asp Ser Thr Gly Ile Val Thr Pro Ser Gly Thr Phe His Gln 
                890                 895                 900 

His Val Pro Ala Gly Tyr Met Asp Phe Pro Lys Val Gly Gly Met 
                905                 910                 915 

Pro Phe Ser Val Tyr Gly Asn Ala Met Ile Pro Pro Val Ala Pro 
                920                 925                 930 

Ile Pro Asp Gly Ala Gly Gly Pro Ile Phe Asn Gly Pro His Ala 
                935                 940                 945 

Ala Asp Pro Ser Trp Asn Ser Leu Ile Lys Met Val Ser Ser Ser 
                950                 955                 960 

Thr Glu Asn Asn Gly Pro Gln Thr Val Trp Thr Gly Pro Trp Ala 
                965                 970                 975 

Pro His Met Asn Ser Val His Met Asn Gln Leu Gly 
                980                 985 

 
           
             14  
             1028  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5426470CD1  
             
           
            14 

Met Met Phe Pro Trp Lys Gln Leu Ile Leu Leu Ser Phe Ile Gly 
  1               5                  10                  15 

Cys Leu Gly Gly Glu Leu Leu Leu Gln Gly Pro Val Phe Ile Lys 
                 20                  25                  30 

Glu Pro Ser Asn Ser Ile Phe Pro Val Gly Ser Glu Asp Lys Lys 
                 35                  40                  45 

Ile Thr Leu His Cys Glu Ala Arg Gly Asn Pro Ser Pro His Tyr 
                 50                  55                  60 

Arg Trp Gln Leu Asn Gly Ser Asp Ile Asp Met Ser Met Glu His 
                 65                  70                  75 

Arg Tyr Lys Leu Asn Gly Gly Asn Leu Val Val Ile Asn Pro Asn 
                 80                  85                  90 

Arg Asn Trp Asp Thr Gly Thr Tyr Gln Cys Phe Ala Thr Asn Ser 
                 95                 100                 105 

Leu Gly Thr Ile Val Ser Arg Glu Ala Lys Leu Gln Phe Ala Tyr 
                110                 115                 120 

Leu Glu Asn Phe Lys Thr Lys Met Arg Ser Thr Val Ser Val Arg 
                125                 130                 135 

Glu Gly Gln Gly Val Val Leu Leu Cys Gly Pro Pro Pro His Ser 
                140                 145                 150 

Gly Glu Leu Ser Tyr Ala Trp Ile Phe Asn Glu Tyr Pro Ser Phe 
                155                 160                 165 

Val Glu Glu Asp Ser Arg Arg Phe Val Ser Gln Glu Thr Gly His 
                170                 175                 180 

Leu Tyr Ile Ser Lys Val Glu Pro Ser Asp Val Gly Asn Tyr Thr 
                185                 190                 195 

Cys Val Val Thr Ser Met Val Thr Asn Ala Arg Val Leu Gly Ser 
                200                 205                 210 

Pro Thr Pro Leu Val Leu Arg Ser Asp Gly Val Met Gly Glu Tyr 
                215                 220                 225 

Glu Pro Lys Ile Glu Val Gln Phe Pro Glu Thr Leu Pro Ala Ala 
                230                 235                 240 

Lys Gly Ser Thr Val Lys Leu Glu Cys Phe Ala Leu Gly Asn Pro 
                245                 250                 255 

Ile Pro Gln Ile Asn Trp Arg Arg Ser Asp Gly Leu Pro Phe Ser 
                260                 265                 270 

Ser Lys Ile Lys Leu Arg Lys Phe Ser Gly Val Leu Glu Ile Pro 
                275                 280                 285 

Asn Phe Gln Gln Glu Asp Ala Gly Ser Tyr Glu Cys Ile Ala Glu 
                290                 295                 300 

Asn Ser Arg Gly Lys Asn Val Ala Arg Gly Arg Leu Thr Tyr Tyr 
                305                 310                 315 

Ala Lys Pro His Trp Val Gln Leu Ile Lys Asp Val Glu Ile Ala 
                320                 325                 330 

Val Glu Asp Ser Leu Tyr Trp Glu Cys Arg Ala Ser Gly Lys Pro 
                335                 340                 345 

Lys Pro Ser Tyr Arg Trp Leu Lys Asn Gly Ala Ala Leu Val Leu 
                350                 355                 360 

Glu Glu Arg Thr Gln Ile Glu Asn Gly Ala Leu Thr Ile Ser Asn 
                365                 370                 375 

Leu Ser Val Thr Asp Ser Gly Met Phe Gln Cys Ile Ala Glu Asn 
                380                 385                 390 

Lys His Gly Leu Val Tyr Ser Ser Ala Glu Leu Lys Val Val Ala 
                395                 400                 405 

Ser Ala Pro Asp Phe Ser Lys Asn Pro Met Lys Lys Leu Val Gln 
                410                 415                 420 

Val Gln Val Gly Ser Leu Val Ser Leu Asp Cys Lys Pro Arg Ala 
                425                 430                 435 

Ser Pro Arg Ala Leu Ser Ser Trp Lys Lys Gly Asp Val Ser Val 
                440                 445                 450 

Gln Glu His Glu Arg Ile Ser Leu Leu Asn Asp Gly Gly Leu Lys 
                455                 460                 465 

Ile Ala Asn Val Thr Lys Ala Asp Ala Gly Thr Tyr Thr Cys Met 
                470                 475                 480 

Ala Glu Asn Gln Phe Gly Lys Ala Asn Gly Thr Thr His Leu Val 
                485                 490                 495 

Val Thr Glu Pro Thr Arg Ile Thr Leu Ala Pro Ser Asn Met Asp 
                500                 505                 510 

Val Ser Val Gly Glu Ser Val Ile Leu Pro Cys Gln Val Gln His 
                515                 520                 525 

Asp Pro Leu Leu Asp Ile Ile Phe Thr Trp Tyr Phe Asn Gly Ala 
                530                 535                 540 

Leu Ala Asp Phe Lys Lys Asp Gly Ser His Phe Glu Lys Val Gly 
                545                 550                 555 

Gly Ser Ser Ser Gly Asp Leu Met Ile Arg Asn Ile Gln Leu Lys 
                560                 565                 570 

His Ser Gly Lys Tyr Val Cys Met Val Gln Thr Gly Val Asp Ser 
                575                 580                 585 

Val Ser Ser Ala Ala Asp Leu Ile Val Arg Gly Ser Pro Gly Pro 
                590                 595                 600 

Pro Glu Asn Val Lys Val Asp Glu Ile Thr Asp Thr Thr Ala Gln 
                605                 610                 615 

Leu Ser Trp Lys Glu Gly Lys Asp Asn His Ser Pro Val Ile Ser 
                620                 625                 630 

Tyr Ser Ile Gln Ala Arg Thr Pro Phe Ser Val Gly Trp Gln Thr 
                635                 640                 645 

Val Thr Thr Val Pro Glu Val Ile Asp Gly Lys Thr His Thr Ala 
                650                 655                 660 

Thr Val Val Glu Leu Asn Pro Trp Val Glu Tyr Glu Phe Arg Val 
                665                 670                 675 

Val Ala Ser Asn Lys Ile Gly Gly Gly Glu Pro Ser Leu Pro Ser 
                680                 685                 690 

Glu Lys Val Arg Thr Glu Glu Ala Val Pro Glu Val Pro Pro Ser 
                695                 700                 705 

Glu Val Asn Gly Gly Gly Gly Ser Arg Ser Glu Leu Val Ile Thr 
                710                 715                 720 

Trp Asp Pro Val Pro Glu Glu Leu Gln Asn Gly Glu Gly Phe Gly 
                725                 730                 735 

Tyr Val Val Ala Phe Arg Pro Leu Gly Val Thr Thr Trp Ile Gln 
                740                 745                 750 

Thr Val Val Thr Ser Pro Asp Thr Pro Arg Tyr Val Phe Arg Asn 
                755                 760                 765 

Glu Ser Ile Val Pro Tyr Ser Pro Tyr Glu Val Lys Val Gly Val 
                770                 775                 780 

Tyr Asn Asn Lys Gly Glu Gly Pro Phe Ser Pro Val Thr Thr Val 
                785                 790                 795 

Phe Ser Ala Glu Glu Glu Pro Thr Val Ala Pro Ser Gln Val Ser 
                800                 805                 810 

Ala Asn Ser Leu Ser Ser Ser Glu Ile Glu Val Ser Trp Asn Thr 
                815                 820                 825 

Ile Pro Trp Lys Leu Ser Asn Gly His Leu Leu Gly Tyr Glu Val 
                830                 835                 840 

Arg Tyr Trp Asn Gly Gly Gly Lys Glu Glu Ser Ser Ser Lys Met 
                845                 850                 855 

Lys Val Ala Gly Asn Glu Thr Ser Ala Arg Leu Arg Gly Leu Lys 
                860                 865                 870 

Ser Asn Leu Ala Tyr Tyr Thr Ala Val Arg Ala Tyr Asn Ser Ala 
                875                 880                 885 

Gly Ala Gly Pro Phe Ser Ala Thr Val Asn Val Thr Thr Lys Lys 
                890                 895                 900 

Thr Pro Pro Ser Gln Pro Pro Gly Asn Val Val Trp Asn Ala Thr 
                905                 910                 915 

Asp Thr Lys Val Leu Leu Asn Trp Glu Gln Val Lys Ala Met Glu 
                920                 925                 930 

Asn Glu Ser Glu Val Thr Gly Tyr Lys Val Phe Tyr Arg Thr Ser 
                935                 940                 945 

Ser Gln Asn Asn Val Gln Val Leu Asn Thr Asn Lys Thr Ser Ala 
                950                 955                 960 

Glu Leu Val Leu Pro Ile Lys Glu Asp Tyr Ile Ile Glu Val Lys 
                965                 970                 975 

Ala Thr Thr Asp Gly Gly Asp Gly Thr Ser Ser Glu Gln Ile Arg 
                980                 985                 990 

Ile Pro Arg Ile Thr Ser Met Asp Ala Arg Gly Ser Thr Ser Ala 
                995                1000                1005 

Ile Ser Asn Val His Pro Met Ser Ser Tyr Met Pro Ile Val Leu 
               1010                1015                1020 

Phe Leu Ile Val Tyr Val Leu Trp 
               1025 

 
           
             15  
             354  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7087904CD1  
             
           
            15 

Met Asp Met Met Leu Leu Val Gln Gly Ala Cys Cys Ser Asn Gln 
  1               5                  10                  15 

Trp Leu Ala Ala Val Leu Leu Ser Leu Cys Cys Leu Leu Pro Ser 
                 20                  25                  30 

Cys Leu Pro Ala Gly Gln Ser Val Asp Phe Pro Trp Ala Ala Val 
                 35                  40                  45 

Asp Asn Met Met Val Arg Lys Gly Asp Thr Ala Val Leu Arg Cys 
                 50                  55                  60 

Tyr Leu Glu Asp Gly Ala Ser Lys Gly Ala Trp Leu Asn Arg Ser 
                 65                  70                  75 

Ser Ile Ile Phe Ala Gly Gly Asp Lys Trp Ser Val Asp Pro Arg 
                 80                  85                  90 

Val Ser Ile Ser Thr Leu Asn Lys Arg Asp Tyr Ser Leu Gln Ile 
                 95                 100                 105 

Gln Asn Val Asp Val Thr Asp Asp Gly Pro Tyr Thr Cys Ser Val 
                110                 115                 120 

Gln Thr Gln His Thr Pro Arg Thr Met Gln Val His Leu Thr Val 
                125                 130                 135 

Gln Val Pro Pro Lys Ile Tyr Asp Ile Ser Asn Asp Met Thr Val 
                140                 145                 150 

Asn Glu Gly Thr Asn Val Thr Leu Thr Cys Leu Ala Thr Gly Lys 
                155                 160                 165 

Pro Glu Pro Ser Ile Ser Trp Arg His Ile Ser Pro Ser Ala Lys 
                170                 175                 180 

Pro Phe Glu Asn Gly Gln Tyr Leu Asp Ile Tyr Gly Ile Thr Arg 
                185                 190                 195 

Asp Gln Ala Gly Glu Tyr Glu Cys Ser Ala Glu Asn Asp Val Ser 
                200                 205                 210 

Phe Pro Asp Val Arg Lys Val Lys Val Val Val Asn Phe Ala Pro 
                215                 220                 225 

Thr Ile Gln Glu Ile Lys Ser Gly Thr Val Thr Pro Gly Arg Ser 
                230                 235                 240 

Gly Leu Ile Arg Cys Glu Gly Ala Gly Val Pro Pro Pro Ala Phe 
                245                 250                 255 

Glu Trp Tyr Lys Gly Glu Lys Lys Leu Phe Asn Gly Gln Gln Gly 
                260                 265                 270 

Ile Ile Ile Gln Asn Phe Ser Thr Arg Ser Ile Leu Thr Val Thr 
                275                 280                 285 

Asn Val Thr Gln Glu His Phe Gly Asn Tyr Thr Cys Val Ala Ala 
                290                 295                 300 

Asn Lys Leu Gly Thr Thr Asn Ala Ser Leu Pro Leu Asn Pro Pro 
                305                 310                 315 

Ser Thr Ala Gln Tyr Gly Ile Thr Gly Ser Ala Asp Val Leu Phe 
                320                 325                 330 

Ser Cys Trp Tyr Leu Val Leu Thr Leu Ser Ser Phe Thr Ser Ile 
                335                 340                 345 

Phe Tyr Leu Lys Asn Ala Ile Leu Gln 
                350 

 
           
             16  
             1829  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477312CD1  
             
           
            16 

Met Gln Leu Ser Arg Ala Ala Ala Ala Ala Ala Ala Ala Pro Ala 
  1               5                  10                  15 

Glu Pro Pro Glu Pro Leu Ser Pro Ala Pro Ala Pro Ala Pro Ala 
                 20                  25                  30 

Pro Pro Gly Pro Leu Pro Arg Ser Ala Ala Asp Gly Ala Pro Ala 
                 35                  40                  45 

Gly Gly Lys Gly Gly Pro Gly Arg Arg Ala Arg Ser Pro Arg Ala 
                 50                  55                  60 

Leu Arg Ser Pro Ala Arg Ala Ala Pro Ala Arg Ala Pro Ala Arg 
                 65                  70                  75 

Gly Trp Thr Ala Pro Gly Pro Gly Ala Ser Ala Val Val Val Arg 
                 80                  85                  90 

Val Gly Ile Pro Asp Leu Gln Gln Thr Lys Cys Leu Arg Leu Asp 
                 95                 100                 105 

Pro Ala Ala Pro Val Trp Ala Ala Lys Gln Arg Val Leu Cys Ala 
                110                 115                 120 

Leu Asn His Ser Leu Gln Asp Ala Leu Asn Tyr Gly Leu Phe Gln 
                125                 130                 135 

Pro Pro Ser Arg Gly Arg Ala Gly Lys Phe Leu Asp Glu Glu Arg 
                140                 145                 150 

Leu Leu Gln Glu Tyr Pro Pro Asn Leu Asp Thr Pro Leu Pro Tyr 
                155                 160                 165 

Leu Glu Phe Arg Tyr Lys Arg Arg Val Tyr Ala Gln Asn Leu Ile 
                170                 175                 180 

Asp Asp Lys Gln Phe Ala Lys Leu His Thr Lys Ala Asn Leu Lys 
                185                 190                 195 

Lys Phe Met Asp Tyr Val Gln Leu His Ser Thr Asp Lys Val Ala 
                200                 205                 210 

Arg Leu Leu Asp Lys Gly Leu Asp Pro Asn Phe His Asp Pro Asp 
                215                 220                 225 

Ser Gly Glu Cys Pro Leu Ser Leu Ala Ala Gln Leu Asp Asn Ala 
                230                 235                 240 

Thr Asp Leu Leu Lys Val Leu Lys Asn Gly Gly Ala His Leu Asp 
                245                 250                 255 

Phe Arg Thr Arg Asp Gly Leu Thr Ala Val His Cys Ala Thr Arg 
                260                 265                 270 

Gln Arg Asn Ala Ala Ala Leu Thr Thr Leu Leu Asp Leu Gly Ala 
                275                 280                 285 

Ser Pro Asp Tyr Lys Asp Ser Arg Gly Leu Thr Pro Leu Tyr His 
                290                 295                 300 

Ser Ala Leu Gly Gly Gly Asp Ala Leu Cys Cys Glu Leu Leu Leu 
                305                 310                 315 

His Asp His Ala Gln Leu Gly Thr Thr Asp Glu Asn Gly Trp Gln 
                320                 325                 330 

Glu Ile His Gln Ala Cys Arg Phe Gly His Val Gln His Leu Glu 
                335                 340                 345 

His Leu Leu Phe Tyr Gly Ala Asp Met Gly Ala Gln Asn Ala Ser 
                350                 355                 360 

Gly Asn Thr Ala Leu His Ile Cys Ala Leu Tyr Asn Gln Glu Ser 
                365                 370                 375 

Cys Ala Arg Val Leu Leu Phe Arg Gly Ala Asn Arg Asp Val Arg 
                380                 385                 390 

Asn Tyr Asn Ser Gln Thr Ala Phe Gln Val Ala Ile Ile Ala Gly 
                395                 400                 405 

Asn Phe Glu Leu Ala Glu Val Ile Lys Thr His Lys Asp Ser Asp 
                410                 415                 420 

Val Gly Gln Asp Ser His Asp Leu Leu His Pro Met Pro Thr Gly 
                425                 430                 435 

Val Pro Glu Trp Gly Leu Tyr Thr Glu Glu Glu Leu Glu Gly Gly 
                440                 445                 450 

Ala Ala Phe Ser Val Pro Phe Arg Glu Thr Pro Ser Tyr Ala Lys 
                455                 460                 465 

Arg Arg Arg Leu Ala Gly Pro Ser Gly Leu Ala Ser Pro Arg Pro 
                470                 475                 480 

Leu Gln Arg Ser Ala Ser Asp Ile Asn Leu Lys Gly Glu Ala Gln 
                485                 490                 495 

Pro Ala Ala Ser Pro Gly Pro Ser Leu Arg Ser Leu Pro His Gln 
                500                 505                 510 

Leu Leu Leu Gln Arg Leu Gln Glu Glu Lys Asp Arg Asp Arg Asp 
                515                 520                 525 

Ala Asp Gln Glu Ser Asn Ile Ser Gly Pro Leu Ala Gly Arg Ala 
                530                 535                 540 

Gly Gln Ser Lys Ile Arg Ser Cys Ile Arg Ile Arg Ala Arg Phe 
                545                 550                 555 

Pro Ala Pro Pro Ala Pro Pro Ala Pro Pro Pro Arg Gly Pro Lys 
                560                 565                 570 

Arg Lys Leu Tyr Ser Ala Val Pro Gly Arg Lys Phe Ile Ala Val 
                575                 580                 585 

Lys Ala His Ser Pro Gln Gly Glu Gly Glu Ile Pro Leu His Arg 
                590                 595                 600 

Gly Glu Ala Val Lys Val Leu Ser Ile Gly Glu Gly Gly Phe Trp 
                605                 610                 615 

Glu Gly Thr Val Lys Gly Arg Thr Gly Trp Phe Pro Ala Asp Cys 
                620                 625                 630 

Val Glu Glu Val Gln Met Arg Gln His Asp Thr Arg Pro Glu Thr 
                635                 640                 645 

Arg Glu Asp Arg Thr Lys Arg Leu Phe Arg His Tyr Thr Val Gly 
                650                 655                 660 

Ser Tyr Asp Ser Leu Thr Ser His Ser Asp Tyr Val Ile Asp Asp 
                665                 670                 675 

Lys Val Ala Val Leu Gln Lys Arg Asp His Glu Gly Phe Gly Phe 
                680                 685                 690 

Val Leu Arg Gly Ala Lys Ala Glu Thr Pro Ile Glu Glu Phe Thr 
                695                 700                 705 

Pro Thr Pro Ala Phe Pro Ala Leu Gln Tyr Leu Glu Ser Val Asp 
                710                 715                 720 

Val Glu Gly Val Ala Trp Arg Ala Gly Leu Arg Thr Gly Asp Phe 
                725                 730                 735 

Leu Ile Glu Val Asn Gly Val Asn Val Val Lys Val Gly His Lys 
                740                 745                 750 

Gln Val Val Ala Leu Ile Arg Gln Gly Gly Asn Arg Leu Val Met 
                755                 760                 765 

Lys Val Val Ser Val Thr Arg Lys Pro Glu Glu Asp Gly Ala Arg 
                770                 775                 780 

Arg Arg Ala Pro Pro Pro Pro Lys Arg Ala Pro Ser Thr Thr Leu 
                785                 790                 795 

Thr Leu Arg Ser Lys Ser Met Thr Ala Glu Leu Glu Glu Leu Glu 
                800                 805                 810 

Lys Leu Asp Glu Met Leu Ala Ala Ala Ala Glu Pro Thr Leu Arg 
                815                 820                 825 

Pro Asp Ile Ala Asp Ala Asp Ser Arg Ala Ala Thr Val Lys Gln 
                830                 835                 840 

Arg Pro Thr Ser Arg Arg Ile Thr Pro Ala Glu Ile Ser Ser Leu 
                845                 850                 855 

Phe Glu Arg Gln Gly Leu Pro Gly Pro Glu Lys Leu Pro Gly Ser 
                860                 865                 870 

Leu Arg Lys Gly Ile Pro Arg Thr Lys Ser Val Gly Glu Asp Glu 
                875                 880                 885 

Lys Leu Ala Ser Leu Leu Glu Gly Arg Phe Pro Arg Ser Thr Ser 
                890                 895                 900 

Met Gln Asp Pro Val Arg Glu Gly Arg Gly Ile Pro Pro Pro Pro 
                905                 910                 915 

Gln Thr Ala Pro Pro Pro Pro Pro Ala Pro Tyr Tyr Phe Asp Ser 
                920                 925                 930 

Gly Pro Pro Pro Ala Phe Ser Pro Pro Pro Pro Pro Gly Arg Ala 
                935                 940                 945 

Tyr Asp Thr Val Arg Ser Ser Phe Lys Pro Gly Leu Glu Ala Arg 
                950                 955                 960 

Leu Gly Ala Gly Ala Ala Gly Leu Tyr Glu Pro Gly Ala Ala Leu 
                965                 970                 975 

Gly Pro Leu Pro Tyr Pro Glu Arg Gln Lys Arg Ala Arg Ser Met 
                980                 985                 990 

Ile Ile Leu Gln Asp Ser Ala Pro Glu Ser Gly Asp Ala Pro Arg 
                995                1000                1005 

Pro Pro Pro Ala Ala Thr Pro Pro Glu Arg Pro Lys Arg Arg Pro 
               1010                1015                1020 

Arg Pro Pro Gly Pro Asp Ser Pro Tyr Ala Asn Leu Gly Ala Phe 
               1025                1030                1035 

Ser Ala Ser Leu Phe Ala Pro Ser Lys Pro Gln Arg Arg Lys Ser 
               1040                1045                1050 

Pro Leu Val Lys Gln Leu Gln Val Glu Asp Ala Gln Glu Arg Ala 
               1055                1060                1065 

Ala Leu Ala Val Gly Ser Pro Gly Pro Gly Gly Gly Ser Phe Ala 
               1070                1075                1080 

Arg Glu Pro Ser Pro Thr His Arg Gly Pro Arg Pro Gly Gly Leu 
               1085                1090                1095 

Asp Tyr Gly Ala Gly Asp Gly Pro Gly Leu Ala Phe Gly Gly Pro 
               1100                1105                1110 

Gly Pro Ala Lys Asp Arg Arg Leu Glu Glu Arg Arg Arg Ser Thr 
               1115                1120                1125 

Val Phe Leu Ser Val Gly Ala Ile Glu Gly Ser Ala Pro Gly Ala 
               1130                1135                1140 

Asp Leu Pro Ser Leu Gln Pro Ser Arg Ser Ile Asp Glu Arg Leu 
               1145                1150                1155 

Leu Gly Thr Gly Pro Thr Ala Gly Arg Asp Leu Leu Leu Pro Ser 
               1160                1165                1170 

Pro Val Ser Ala Leu Lys Pro Leu Val Ser Gly Pro Ser Leu Gly 
               1175                1180                1185 

Pro Ser Gly Ser Thr Phe Ile His Pro Leu Thr Gly Lys Pro Leu 
               1190                1195                1200 

Asp Pro Ser Ser Pro Leu Ala Leu Ala Leu Ala Ala Arg Glu Arg 
               1205                1210                1215 

Ala Leu Ala Ser Gln Ala Pro Ser Arg Ser Pro Thr Pro Val His 
               1220                1225                1230 

Ser Pro Asp Ala Asp Arg Pro Gly Pro Leu Phe Val Asp Val Gln 
               1235                1240                1245 

Ala Arg Asp Pro Glu Arg Gly Ser Leu Ala Ser Pro Ala Phe Ser 
               1250                1255                1260 

Pro Arg Ser Pro Ala Trp Ile Pro Val Pro Ala Arg Arg Glu Ala 
               1265                1270                1275 

Glu Lys Val Pro Arg Glu Glu Arg Lys Ser Pro Glu Asp Lys Lys 
               1280                1285                1290 

Ser Met Ile Leu Ser Val Leu Asp Thr Ser Leu Gln Arg Pro Ala 
               1295                1300                1305 

Gly Leu Ile Val Val His Ala Thr Ser Asn Gly Gln Glu Pro Ser 
               1310                1315                1320 

Arg Leu Gly Gly Ala Glu Glu Glu Arg Pro Gly Thr Pro Glu Leu 
               1325                1330                1335 

Ala Pro Ala Pro Met Gln Ser Ala Ala Val Ala Glu Pro Leu Pro 
               1340                1345                1350 

Ser Pro Arg Ala Gln Pro Pro Gly Gly Thr Pro Ala Asp Ala Gly 
               1355                1360                1365 

Pro Gly Gln Gly Ser Ser Glu Glu Glu Pro Glu Leu Val Phe Ala 
               1370                1375                1380 

Val Asn Leu Pro Pro Ala Gln Leu Ser Ser Ser Asp Glu Glu Thr 
               1385                1390                1395 

Arg Glu Glu Leu Ala Arg Ile Gly Leu Val Pro Pro Pro Glu Glu 
               1400                1405                1410 

Phe Ala Asn Gly Val Leu Leu Ala Thr Pro Leu Ala Gly Pro Gly 
               1415                1420                1425 

Pro Ser Pro Thr Thr Val Pro Ser Pro Ala Ser Gly Lys Pro Ser 
               1430                1435                1440 

Ser Glu Pro Pro Pro Ala Pro Glu Ser Ala Ala Asp Ser Gly Val 
               1445                1450                1455 

Glu Glu Ala Asp Thr Arg Ser Ser Ser Asp Pro His Leu Glu Thr 
               1460                1465                1470 

Thr Ser Thr Ile Ser Thr Val Ser Ser Met Ser Thr Leu Ser Ser 
               1475                1480                1485 

Glu Ser Gly Glu Leu Thr Asp Thr His Thr Ser Phe Ala Asp Gly 
               1490                1495                1500 

His Thr Phe Leu Leu Glu Lys Pro Pro Val Pro Pro Lys Pro Lys 
               1505                1510                1515 

Leu Lys Ser Pro Leu Gly Lys Gly Pro Val Thr Phe Arg Asp Pro 
               1520                1525                1530 

Leu Leu Lys Gln Ser Ser Asp Ser Glu Leu Met Ala Gln Gln His 
               1535                1540                1545 

His Ala Ala Ser Ala Gly Leu Ala Ser Ala Ala Gly Pro Ala Arg 
               1550                1555                1560 

Pro Arg Tyr Leu Phe Gln Arg Arg Ser Lys Leu Trp Gly Asp Pro 
               1565                1570                1575 

Val Glu Ser Arg Gly Leu Pro Gly Pro Glu Asp Asp Lys Pro Thr 
               1580                1585                1590 

Val Ile Ser Glu Leu Ser Ser Arg Leu Gln Gln Leu Asn Lys Asp 
               1595                1600                1605 

Thr Arg Ser Leu Gly Glu Glu Pro Val Gly Gly Leu Gly Ser Leu 
               1610                1615                1620 

Leu Asp Pro Ala Lys Lys Ser Pro Ile Ala Ala Ala Arg Leu Phe 
               1625                1630                1635 

Ser Ser Leu Gly Glu Leu Ser Ser Ile Ser Ala Gln Arg Ser Pro 
               1640                1645                1650 

Gly Gly Pro Gly Gly Gly Ala Ser Tyr Ser Val Arg Pro Ser Gly 
               1655                1660                1665 

Arg Tyr Pro Val Ala Arg Arg Ala Pro Ser Pro Val Lys Pro Ala 
               1670                1675                1680 

Ser Leu Glu Arg Val Glu Gly Leu Gly Ala Gly Ala Gly Gly Ala 
               1685                1690                1695 

Gly Arg Pro Phe Gly Leu Thr Pro Pro Thr Ile Leu Lys Ser Ser 
               1700                1705                1710 

Ser Leu Ser Ile Pro His Glu Pro Lys Glu Val Arg Phe Val Val 
               1715                1720                1725 

Arg Ser Val Ser Ala Arg Ser Arg Ser Pro Ser Pro Ser Pro Leu 
               1730                1735                1740 

Pro Ser Pro Ala Ser Gly Pro Gly Pro Gly Ala Pro Gly Pro Arg 
               1745                1750                1755 

Arg Pro Phe Gln Gln Lys Pro Leu Gln Leu Trp Ser Lys Phe Asp 
               1760                1765                1770 

Val Gly Asp Trp Leu Glu Ser Ile His Leu Gly Glu His Arg Asp 
               1775                1780                1785 

Arg Phe Glu Asp His Glu Ile Glu Gly Ala His Leu Pro Ala Leu 
               1790                1795                1800 

Thr Lys Asp Asp Phe Val Glu Leu Gly Val Thr Arg Val Gly His 
               1805                1810                1815 

Arg Met Asn Ile Glu Arg Ala Leu Arg Gln Leu Asp Gly Ser 
               1820                1825 

 
           
             17  
             323  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2739431CD1  
             
           
            17 

Met Met Ser Pro Ser Gln Ala Ser Leu Leu Phe Leu Asn Val Cys 
  1               5                  10                  15 

Ile Phe Ile Cys Gly Glu Ala Val Gln Gly Asn Cys Val His His 
                 20                  25                  30 

Ser Thr Asp Ser Ser Val Val Asn Ile Val Glu Asp Gly Ser Asn 
                 35                  40                  45 

Ala Lys Asp Glu Ser Lys Ser Asn Asp Thr Val Cys Lys Glu Asp 
                 50                  55                  60 

Cys Glu Glu Ser Cys Asp Val Lys Thr Lys Ile Thr Arg Glu Glu 
                 65                  70                  75 

Lys His Phe Met Cys Arg Asn Leu Gln Asn Ser Ile Val Ser Tyr 
                 80                  85                  90 

Thr Arg Ser Thr Lys Lys Leu Leu Arg Asn Met Met Asp Glu Gln 
                 95                 100                 105 

Gln Ala Ser Leu Asp Tyr Leu Ser Asn Gln Val Met Cys Asp Met 
                110                 115                 120 

Asp Tyr Arg Gly Gly Gly Trp Thr Val Ile Gln Lys Arg Ile Asp 
                125                 130                 135 

Gly Ile Ile Asp Phe Gln Arg Leu Trp Cys Asp Tyr Leu Asp Gly 
                140                 145                 150 

Phe Gly Asp Leu Leu Gly Glu Phe Trp Leu Gly Leu Lys Lys Ile 
                155                 160                 165 

Phe Tyr Ile Val Asn Gln Lys Asn Thr Ser Phe Met Leu Tyr Val 
                170                 175                 180 

Ala Leu Glu Ser Glu Asp Asp Thr Leu Ala Tyr Ala Ser Tyr Asp 
                185                 190                 195 

Asn Phe Trp Leu Glu Asp Glu Thr Arg Phe Phe Lys Met His Leu 
                200                 205                 210 

Gly Arg Tyr Ser Gly Asn Ala Gly Asp Ala Phe Arg Gly Leu Lys 
                215                 220                 225 

Lys Glu Asp Asn Gln Asn Ala Met Pro Phe Ser Thr Ser Asp Val 
                230                 235                 240 

Asp Asn Asp Gly Cys Arg Pro Ala Cys Leu Val Asn Gly Gln Ser 
                245                 250                 255 

Val Lys Ser Cys Ser His Leu His Asn Lys Thr Gly Trp Trp Phe 
                260                 265                 270 

Asn Glu Cys Gly Leu Ala Asn Leu Asn Gly Ile His His Phe Ser 
                275                 280                 285 

Gly Lys Leu Leu Ala Thr Gly Ile Gln Trp Gly Thr Trp Thr Lys 
                290                 295                 300 

Asn Asn Ser Pro Val Lys Ile Lys Ser Val Ser Met Lys Ile Arg 
                305                 310                 315 

Arg Met Tyr Asn Pro Tyr Phe Lys 
                320 

 
           
             18  
             644  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473606CD1  
             
           
            18 

Met Asp Gly Arg Gly Ala Phe Trp Thr Val Ala Ile Pro Arg Ala 
  1               5                  10                  15 

Arg Gln Glu Gly Leu Gly Arg Leu Gly Leu Pro Phe Pro Val Lys 
                 20                  25                  30 

Arg Thr Pro Pro Ala Pro Gln Asn Pro Gly Gly Ser Thr Gln Ala 
                 35                  40                  45 

Pro Gln Arg Val Val Gly Lys Ser His Ser Gly Ile Arg Met Pro 
                 50                  55                  60 

Ala Lys Ser Arg Asn Leu Arg Leu Glu Ser Lys Leu Asn Arg Lys 
                 65                  70                  75 

Val Val Lys Tyr Lys Trp Gly Lys Gln Gly Ser Gly Ala Gly Arg 
                 80                  85                  90 

Glu Leu Val Pro Ala Phe Pro Thr Asn Ala Gly Leu Gly Arg Arg 
                 95                 100                 105 

Asp Arg Cys Arg Pro Pro Pro Ala Gly Gly Asp Val Ala Ser His 
                110                 115                 120 

Gly Leu Pro Gly Ser Gly Val Gly Tyr Ser Cys Asn Gln Arg Glu 
                125                 130                 135 

Glu Gly Leu Arg Gly Gly Cys Gly Gly Ile Pro His Val Pro Leu 
                140                 145                 150 

Phe Leu Ser Pro Leu Pro Leu Asp Ala Ser Gly Gln Arg Pro Ser 
                155                 160                 165 

Ser Thr Tyr Arg Gln Ser Leu Arg Arg Gly Leu Gly Thr Arg Ala 
                170                 175                 180 

His Gln Ser Pro Ala Asn Glu Ile Pro Glu Leu Gly Asp Leu Arg 
                185                 190                 195 

Gly Ser Arg Leu Ala Gln Glu Pro Ala Val Leu Phe Gly Leu Arg 
                200                 205                 210 

Pro Ser Ile Ser Lys Arg Gly Leu Leu Ala Arg Arg Leu Trp Ala 
                215                 220                 225 

Gln Pro Met Leu Leu Ser Gly Trp Val Val Ser Thr Thr Thr Thr 
                230                 235                 240 

Ile Ile Thr Val Thr Val Thr Phe Thr Pro Thr Gly Leu Leu Cys 
                245                 250                 255 

Val Lys His Ser Arg Gly Pro Leu Gln Pro Thr Cys Gln Glu Ser 
                260                 265                 270 

Ala Pro Glu Asn Arg Val Gly Lys Ala Leu Ile Thr Phe Ser Lys 
                275                 280                 285 

Gly Trp Arg Ala Ser Leu Arg Leu Ala Pro Pro Pro Ser Ala Leu 
                290                 295                 300 

Leu Leu Arg Arg His Gly Pro Gly Gly Leu Pro Val Pro Gly Thr 
                305                 310                 315 

Met Cys Asp Gly Ala Leu Leu Pro Pro Leu Val Leu Pro Val Leu 
                320                 325                 330 

Leu Leu Leu Val Trp Gly Leu Asp Pro Gly Thr Gly Ser Ala Pro 
                335                 340                 345 

Ser His Ser Pro Leu His Pro Ala Ser Cys Gly Tyr Leu Pro Ser 
                350                 355                 360 

Ala Phe Ser Arg Arg Pro Gly Gly Pro Gly Ala Ala Ala Gly Pro 
                365                 370                 375 

Leu Thr Ala Pro Glu Arg Arg Arg Arg Gly Pro Arg Pro Glu Tyr 
                380                 385                 390 

Gly Asn Arg Val Ala Pro Trp Gln Ala Arg Arg Arg Arg Val Ser 
                395                 400                 405 

Ala Arg Arg Cys Ala Ala Pro Phe Arg Glu Val Leu Ala Arg Leu 
                410                 415                 420 

Arg Arg Arg Pro Ser Pro Gly Gly Ala Gly Gln Arg Gly Ala Val 
                425                 430                 435 

Gly Asp Ala Ala Ala Asp Val Glu Val Val Leu Pro Trp Arg Val 
                440                 445                 450 

Arg Pro Asp Asp Val His Leu Pro Pro Leu Pro Ala Ala Pro Gly 
                455                 460                 465 

Pro Arg Arg Arg Arg Arg Pro Arg Thr Pro Pro Ala Ala Pro Arg 
                470                 475                 480 

Ala Arg Pro Gly Glu Arg Ala Leu Leu Leu His Leu Pro Ala Phe 
                485                 490                 495 

Gly Arg Asp Leu Tyr Leu Gln Leu Arg Arg Asp Leu Arg Phe Leu 
                500                 505                 510 

Ser Arg Gly Phe Glu Val Glu Glu Ala Gly Ala Ala Arg Arg Arg 
                515                 520                 525 

Gly Arg Pro Ala Glu Leu Cys Phe Tyr Ser Gly Arg Val Leu Gly 
                530                 535                 540 

His Pro Gly Ser Leu Val Ser Leu Ser Ala Cys Gly Ala Ala Gly 
                545                 550                 555 

Gly Leu Val Gly Leu Ile Gln Leu Gly Gln Glu Gln Val Leu Ile 
                560                 565                 570 

Gln Pro Leu Asn Asn Ser Gln Gly Pro Phe Ser Gly Arg Glu His 
                575                 580                 585 

Leu Ile Arg Arg Lys Trp Ser Leu Thr Pro Ser Pro Ser Ala Glu 
                590                 595                 600 

Ala Gln Arg Pro Glu Gln Leu Cys Lys Val Leu Thr Val Pro Gln 
                605                 610                 615 

Cys Leu Gly Leu Thr Trp Glu Asp Leu Lys Ser Gly Gly Trp Ser 
                620                 625                 630 

Asp Leu Glu Val Pro His Ser Cys Val Trp Pro Gly Gly Gly 
                635                 640 

 
           
             19  
             881  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3534918CD1  
             
           
            19 

Met Glu His Gly Ala Leu Gly Ser Leu Gly Glu His Ala Ala Lys 
  1               5                  10                  15 

Val Val Gly Lys Val Leu Arg Gln Glu Gln Asp Phe Val Ile Thr 
                 20                  25                  30 

His His Gln Arg Leu Val Gly Pro Thr Val Met Glu Gln Lys His 
                 35                  40                  45 

Arg Cys Lys Phe Ala Met Lys Glu Ile Val Gln Phe Met Ala Ser 
                 50                  55                  60 

Gly Arg Leu Gly Pro Val Gly Val Pro Val Leu Cys His Val Glu 
                 65                  70                  75 

Glu Val Pro Asp Arg Glu Gln Gly Ala Ala Pro Thr Leu Cys Pro 
                 80                  85                  90 

Ser Met Glu Glu Gly Asn Ala Lys Gly Val Met Ser Arg Val Ile 
                 95                 100                 105 

Phe Ala Thr Val Thr Leu Ala Gln Val Ser Val Gly Asn Thr His 
                110                 115                 120 

Gly Asn Trp Ser Pro Trp Ser Gly Trp Gly Thr Cys Ser Arg Thr 
                125                 130                 135 

Cys Asn Gly Gly Gln Met Arg Arg Tyr Arg Thr Cys Asp Asn Pro 
                140                 145                 150 

Pro Pro Ser Asn Gly Gly Arg Ala Cys Gly Gly Pro Asp Ser Gln 
                155                 160                 165 

Ile Gln Arg Cys Asn Thr Asp Met Cys Pro Val Asp Gly Ser Trp 
                170                 175                 180 

Gly Ser Trp His Ser Trp Ser Gln Cys Ser Ala Ser Cys Gly Gly 
                185                 190                 195 

Gly Glu Lys Thr Arg Lys Arg Leu Cys Asp His Pro Val Pro Val 
                200                 205                 210 

Lys Gly Gly Arg Pro Cys Pro Gly Asp Thr Thr Gln Val Thr Arg 
                215                 220                 225 

Cys Asn Val Gln Ala Cys Pro Gly Gly Pro Gln Arg Ala Arg Gly 
                230                 235                 240 

Ser Val Ile Gly Asn Ile Asn Asp Val Glu Phe Gly Ile Ala Phe 
                245                 250                 255 

Leu Asn Ala Thr Ile Thr Asp Ser Pro Asn Ser Asp Thr Arg Ile 
                260                 265                 270 

Ile Arg Ala Lys Ile Thr Asn Val Pro Arg Ser Leu Gly Ser Ala 
                275                 280                 285 

Met Arg Lys Ile Val Ser Ile Leu Asn Pro Ile Tyr Trp Thr Thr 
                290                 295                 300 

Ala Lys Glu Ile Gly Glu Ala Val Asn Gly Phe Thr Leu Thr Asn 
                305                 310                 315 

Ala Val Phe Lys Arg Glu Thr Gln Val Glu Phe Ala Thr Gly Glu 
                320                 325                 330 

Ile Leu Gln Met Ser His Ile Ala Arg Gly Leu Asp Ser Asp Gly 
                335                 340                 345 

Ser Leu Leu Leu Asp Ile Val Val Ser Gly Tyr Val Leu Gln Leu 
                350                 355                 360 

Gln Ser Pro Ala Glu Val Thr Val Lys Asp Tyr Thr Glu Asp Tyr 
                365                 370                 375 

Ile Gln Thr Gly Pro Gly Gln Leu Tyr Ala Tyr Ser Thr Arg Leu 
                380                 385                 390 

Phe Thr Ile Asp Gly Ile Ser Ile Pro Tyr Thr Trp Asn His Thr 
                395                 400                 405 

Val Phe Tyr Asp Gln Ala Gln Gly Arg Met Pro Phe Leu Val Glu 
                410                 415                 420 

Thr Leu His Ala Ser Ser Val Glu Ser Asp Tyr Asn Gln Ile Glu 
                425                 430                 435 

Glu Thr Leu Gly Phe Lys Ile His Ala Ser Ile Ser Lys Gly Asp 
                440                 445                 450 

Arg Ser Asn Gln Cys Pro Ser Gly Phe Thr Leu Asp Ser Val Gly 
                455                 460                 465 

Pro Phe Cys Ala Asp Glu Asp Glu Cys Ala Ala Gly Asn Pro Cys 
                470                 475                 480 

Ser His Ser Cys His Asn Ala Met Gly Thr Tyr Tyr Cys Ser Cys 
                485                 490                 495 

Pro Lys Gly Leu Thr Ile Ala Ala Asp Gly Arg Thr Cys Gln Asp 
                500                 505                 510 

Ile Asp Glu Cys Ala Leu Gly Arg His Thr Cys His Ala Gly Gln 
                515                 520                 525 

Asp Cys Asp Asn Thr Ile Gly Ser Tyr Arg Cys Val Val Arg Cys 
                530                 535                 540 

Gly Ser Gly Phe Arg Arg Thr Ser Asp Gly Leu Ser Cys Gln Asp 
                545                 550                 555 

Ile Asn Glu Cys Gln Glu Ser Ser Pro Cys His Gln Arg Cys Phe 
                560                 565                 570 

Asn Ala Ile Gly Ser Phe His Cys Gly Cys Glu Pro Gly Tyr Gln 
                575                 580                 585 

Leu Lys Gly Arg Lys Cys Met Asp Val Asn Glu Cys Arg Gln Asn 
                590                 595                 600 

Val Cys Arg Pro Asp Gln His Cys Lys Asn Thr Arg Gly Gly Tyr 
                605                 610                 615 

Lys Cys Ile Asp Leu Cys Pro Asn Gly Met Thr Lys Ala Glu Asn 
                620                 625                 630 

Gly Thr Cys Ile Asp Ile Asp Glu Cys Lys Asp Gly Thr His Gln 
                635                 640                 645 

Cys Arg Tyr Asn Gln Ile Cys Glu Asn Thr Arg Gly Ser Tyr Arg 
                650                 655                 660 

Cys Val Cys Pro Arg Gly Tyr Arg Ser Gln Gly Val Gly Arg Pro 
                665                 670                 675 

Cys Met Asp Ile Asp Glu Cys Glu Asn Thr Asp Ala Cys Gln His 
                680                 685                 690 

Glu Cys Lys Asn Thr Phe Gly Ser Tyr Gln Cys Ile Cys Pro Pro 
                695                 700                 705 

Gly Tyr Gln Leu Thr His Asn Gly Lys Thr Cys Gln Asp Ile Asp 
                710                 715                 720 

Glu Cys Leu Glu Gln Asn Val His Cys Gly Pro Asn Arg Met Cys 
                725                 730                 735 

Phe Asn Met Arg Gly Ser Tyr Gln Cys Ile Asp Thr Pro Cys Pro 
                740                 745                 750 

Pro Asn Tyr Gln Arg Asp Pro Val Ser Gly Phe Cys Leu Lys Asn 
                755                 760                 765 

Cys Pro Pro Asn Asp Leu Glu Cys Ala Leu Ser Pro Tyr Ala Leu 
                770                 775                 780 

Glu Tyr Lys Leu Val Ser Leu Pro Phe Gly Ile Ala Thr Asn Gln 
                785                 790                 795 

Asp Leu Ile Arg Leu Val Ala Tyr Thr Gln Asp Gly Val Met His 
                800                 805                 810 

Pro Arg Thr Thr Phe Leu Met Val Asp Glu Glu Gln Thr Val Pro 
                815                 820                 825 

Phe Ala Leu Arg Asp Glu Asn Leu Lys Gly Val Val Tyr Thr Thr 
                830                 835                 840 

Arg Pro Leu Arg Glu Ala Glu Thr Tyr Arg Met Arg Val Arg Ala 
                845                 850                 855 

Ser Ser Tyr Ser Ala Asn Gly Thr Ile Glu Tyr Gln Thr Thr Phe 
                860                 865                 870 

Ile Val Tyr Ile Ala Val Ser Ala Tyr Pro Tyr 
                875                 880 

 
           
             20  
             957  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2428715CD1  
             
           
            20 

Met Gly Ala Ala Ala Val Arg Trp His Leu Cys Val Leu Leu Ala 
  1               5                  10                  15 

Leu Gly Thr Arg Gly Arg Leu Ala Gly Gly Ser Gly Leu Pro Gly 
                 20                  25                  30 

Ser Val Asp Val Asp Glu Cys Ser Glu Gly Thr Asp Asp Cys His 
                 35                  40                  45 

Ile Asp Ala Ile Cys Gln Asn Thr Pro Lys Ser Tyr Lys Cys Leu 
                 50                  55                  60 

Cys Lys Pro Gly Tyr Lys Gly Glu Gly Lys Gln Cys Glu Asp Ile 
                 65                  70                  75 

Asp Glu Cys Glu Asn Asp Tyr Tyr Asn Gly Gly Cys Val His Glu 
                 80                  85                  90 

Cys Ile Asn Ile Pro Gly Asn Tyr Arg Cys Thr Cys Phe Asp Gly 
                 95                 100                 105 

Phe Met Leu Ala His Asp Gly His Asn Cys Leu Asp Val Asp Glu 
                110                 115                 120 

Cys Gln Asp Asn Asn Gly Gly Cys Gln Gln Ile Cys Val Asn Ala 
                125                 130                 135 

Met Gly Ser Tyr Glu Cys Gln Cys His Ser Gly Phe Phe Leu Ser 
                140                 145                 150 

Asp Asn Gln His Thr Cys Ile His Arg Ser Asn Glu Gly Met Asn 
                155                 160                 165 

Cys Met Asn Lys Asp His Gly Cys Ala His Ile Cys Arg Glu Thr 
                170                 175                 180 

Pro Lys Gly Gly Val Ala Cys Asp Cys Arg Pro Gly Phe Asp Leu 
                185                 190                 195 

Ala Gln Asn Gln Lys Asp Cys Thr Leu Thr Cys Asn Tyr Gly Asn 
                200                 205                 210 

Gly Gly Cys Gln His Ser Cys Glu Asp Thr Asp Thr Gly Pro Thr 
                215                 220                 225 

Cys Gly Cys His Gln Lys Tyr Ala Leu His Ser Asp Gly Arg Thr 
                230                 235                 240 

Cys Ile Glu Lys Asp Glu Ala Ala Ile Glu Arg Ser Gln Phe Asn 
                245                 250                 255 

Ala Thr Ser Val Ala Asp Val Asp Lys Arg Val Lys Arg Arg Leu 
                260                 265                 270 

Leu Met Glu Thr Cys Ala Val Asn Asn Gly Gly Cys Asp Arg Thr 
                275                 280                 285 

Cys Lys Asp Thr Ala Thr Gly Val Arg Cys Ser Cys Pro Val Gly 
                290                 295                 300 

Phe Thr Leu Gln Pro Asp Gly Lys Thr Cys Lys Asp Ile Asn Glu 
                305                 310                 315 

Cys Leu Val Asn Asn Gly Gly Cys Asp His Phe Cys Arg Asn Thr 
                320                 325                 330 

Val Gly Ser Phe Glu Cys Gly Cys Arg Lys Gly Tyr Lys Leu Leu 
                335                 340                 345 

Thr Asp Glu Arg Thr Cys Gln Asp Ile Asp Glu Cys Ser Phe Glu 
                350                 355                 360 

Arg Thr Cys Asp His Ile Cys Ile Asn Ser Pro Gly Ser Phe Gln 
                365                 370                 375 

Cys Leu Cys His Arg Gly Tyr Ile Leu Tyr Gly Thr Thr His Cys 
                380                 385                 390 

Gly Asp Val Asp Glu Cys Ser Met Ser Asn Gly Ser Cys Asp Gln 
                395                 400                 405 

Gly Cys Val Asn Thr Lys Gly Ser Tyr Glu Cys Val Cys Pro Pro 
                410                 415                 420 

Gly Arg Arg Leu His Trp Asn Arg Lys Asp Cys Val Glu Thr Gly 
                425                 430                 435 

Lys Cys Leu Ser Arg Ala Lys Thr Ser Pro Arg Ala Gln Leu Ser 
                440                 445                 450 

Cys Ser Lys Ala Gly Gly Val Glu Ser Cys Phe Leu Ser Cys Pro 
                455                 460                 465 

Ala His Thr Leu Phe Val Pro Asp Ala Pro Thr Thr Pro Ile Lys 
                470                 475                 480 

Gln Lys Ala Arg Phe Lys Ile Arg Asp Ala Lys Cys His Leu Arg 
                485                 490                 495 

Pro His Ser Gln Ala Arg Ala Lys Glu Thr Ala Arg Gln Pro Leu 
                500                 505                 510 

Leu Asp His Cys His Val Thr Phe Val Thr Leu Lys Cys Asp Ser 
                515                 520                 525 

Ser Lys Lys Arg Arg Arg Gly Arg Lys Ser Pro Ser Lys Glu Val 
                530                 535                 540 

Ser His Ile Thr Ala Glu Phe Glu Ile Glu Thr Lys Met Glu Glu 
                545                 550                 555 

Ala Ser Asp Thr Cys Glu Ala Asp Cys Leu Arg Lys Arg Ala Glu 
                560                 565                 570 

Gln Ser Leu Gln Ala Ala Ile Lys Thr Leu Arg Lys Ser Ile Gly 
                575                 580                 585 

Arg Gln Gln Phe Tyr Val Gln Val Ser Gly Thr Glu Tyr Glu Val 
                590                 595                 600 

Ala Gln Arg Pro Ala Lys Ala Leu Glu Gly Gln Gly Ala Cys Gly 
                605                 610                 615 

Ala Gly Gln Val Leu Gln Asp Ser Lys Cys Val Ala Cys Gly Pro 
                620                 625                 630 

Gly Thr His Phe Gly Gly Glu Leu Gly Gln Cys Val Pro Cys Met 
                635                 640                 645 

Pro Gly Thr Tyr Gln Asp Met Glu Gly Gln Leu Ser Cys Thr Pro 
                650                 655                 660 

Cys Pro Ser Ser Asp Gly Leu Gly Leu Pro Gly Ala Arg Asn Val 
                665                 670                 675 

Ser Glu Cys Gly Gly Gln Cys Ser Pro Gly Phe Phe Ser Ala Asp 
                680                 685                 690 

Gly Phe Lys Pro Cys Gln Ala Cys Pro Val Gly Thr Tyr Gln Pro 
                695                 700                 705 

Glu Pro Gly Arg Thr Gly Cys Phe Pro Cys Gly Gly Gly Leu Leu 
                710                 715                 720 

Thr Lys His Glu Gly Thr Thr Ser Phe Gln Asp Cys Glu Ala Lys 
                725                 730                 735 

Val His Cys Ser Pro Gly His His Tyr Asn Thr Thr Thr His Arg 
                740                 745                 750 

Cys Ile Arg Cys Pro Val Gly Thr Tyr Gln Pro Glu Phe Gly Gln 
                755                 760                 765 

Asn His Cys Ile Thr Cys Pro Gly Asn Thr Ser Thr Asp Phe Asp 
                770                 775                 780 

Gly Ser Thr Asn Val Thr His Cys Lys Asn Gln His Cys Gly Gly 
                785                 790                 795 

Glu Leu Gly Asp Tyr Thr Gly Tyr Ile Glu Ser Pro Asn Tyr Pro 
                800                 805                 810 

Gly Asp Tyr Pro Ala Asn Ala Glu Cys Val Trp His Ile Ala Pro 
                815                 820                 825 

Pro Pro Lys Arg Arg Ile Leu Ile Val Val Pro Glu Ile Phe Leu 
                830                 835                 840 

Pro Ile Glu Asp Glu Cys Gly Asp Val Leu Val Met Arg Lys Ser 
                845                 850                 855 

Ala Ser Pro Thr Ser Ile Thr Thr Tyr Glu Thr Cys Gln Thr Tyr 
                860                 865                 870 

Glu Arg Pro Ile Ala Phe Thr Ser Arg Ser Arg Lys Leu Trp Ile 
                875                 880                 885 

Gln Phe Lys Ser Asn Glu Gly Asn Ser Gly Lys Gly Phe Gln Val 
                890                 895                 900 

Pro Tyr Val Thr Tyr Asp Glu Asp Tyr Gln Gln Leu Ile Glu Asp 
                905                 910                 915 

Ile Val Arg Asp Gly Arg Leu Tyr Ala Ser Glu Asn His Gln Glu 
                920                 925                 930 

Ile Leu Lys Asp Lys Lys Leu Ile Lys Ala Leu Phe Asp Val Leu 
                935                 940                 945 

Ala His Pro Gln Asn Arg Gly Leu Val Ser Ser Cys 
                950                 955 

 
           
             21  
             1393  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3351332CD1  
             
           
            21 

Met Gly Ala Ser Arg Asp Arg Gly Leu Ala Ala Leu Trp Cys Leu 
  1               5                  10                  15 

Gly Leu Leu Gly Gly Leu Ala Arg Val Ala Gly Thr His Tyr Arg 
                 20                  25                  30 

Tyr Leu Trp Arg Gly Cys Tyr Pro Cys His Leu Gly Gln Ala Gly 
                 35                  40                  45 

Tyr Pro Val Ser Ala Gly Asp Gln Arg Pro Asp Val Asp Glu Cys 
                 50                  55                  60 

Arg Thr His Asn Gly Gly Cys Gln His Arg Cys Val Asn Thr Pro 
                 65                  70                  75 

Gly Ser Tyr Leu Cys Glu Cys Lys Pro Gly Phe Arg Leu His Thr 
                 80                  85                  90 

Asp Ser Arg Thr Cys Leu Ala Ile Asn Ser Cys Ala Leu Gly Asn 
                 95                 100                 105 

Gly Gly Cys Gln His His Cys Val Gln Leu Thr Ile Thr Arg His 
                110                 115                 120 

Arg Cys Gln Cys Arg Pro Gly Phe Gln Leu Gln Glu Asp Gly Arg 
                125                 130                 135 

His Cys Val Arg Arg Ser Pro Cys Ala Asn Arg Asn Gly Ser Cys 
                140                 145                 150 

Met His Arg Cys Gln Val Val Arg Gly Leu Ala Arg Cys Glu Cys 
                155                 160                 165 

His Val Gly Tyr Gln Leu Ala Ala Asp Gly Lys Ala Cys Pro Asp 
                170                 175                 180 

Val Asp Glu Cys Ala Ala Gly Leu Ala Gln Cys Ala His Gly Cys 
                185                 190                 195 

Leu Asn Thr Gln Gly Ser Phe Lys Cys Val Cys His Ala Gly Tyr 
                200                 205                 210 

Glu Leu Gly Ala Asp Gly Arg Gln Cys Tyr Arg Ile Glu Met Glu 
                215                 220                 225 

Ile Val Asn Ser Cys Glu Ala Asn Asn Gly Gly Cys Ser His Gly 
                230                 235                 240 

Cys Ser His Thr Ser Ala Gly Pro Leu Cys Thr Cys Pro Arg Gly 
                245                 250                 255 

Tyr Glu Leu Asp Thr Asp Gln Arg Thr Cys Ile Asp Val Asp Asp 
                260                 265                 270 

Cys Ala Asp Ser Pro Cys Cys Gln Gln Val Cys Thr Asn Asn Pro 
                275                 280                 285 

Gly Gly Tyr Glu Cys Gly Cys Tyr Ala Gly Tyr Arg Leu Ser Ala 
                290                 295                 300 

Asp Gly Cys Gly Cys Glu Asp Val Asp Glu Cys Ala Ser Ser Arg 
                305                 310                 315 

Gly Gly Cys Glu His His Cys Thr Asn Leu Ala Gly Ser Phe Gln 
                320                 325                 330 

Cys Ser Cys Glu Ala Gly Tyr Arg Leu His Glu Asp Arg Arg Gly 
                335                 340                 345 

Cys Ser Pro Leu Glu Glu Pro Met Val Asp Leu Asp Gly Glu Leu 
                350                 355                 360 

Pro Phe Val Arg Pro Leu Pro His Ile Ala Val Leu Gln Asp Glu 
                365                 370                 375 

Leu Pro Gln Leu Phe Gln Asp Asp Asp Val Gly Ala Asp Glu Glu 
                380                 385                 390 

Glu Ala Glu Leu Arg Gly Glu His Thr Leu Thr Glu Lys Phe Val 
                395                 400                 405 

Cys Leu Asp Asp Ser Phe Gly His Asp Cys Ser Leu Thr Cys Asp 
                410                 415                 420 

Asp Cys Arg Asn Gly Gly Thr Cys Leu Leu Gly Leu Asp Gly Cys 
                425                 430                 435 

Asp Cys Pro Glu Gly Trp Thr Gly Leu Ile Cys Asn Glu Thr Cys 
                440                 445                 450 

Pro Pro Asp Thr Phe Gly Lys Asn Cys Ser Phe Ser Cys Ser Cys 
                455                 460                 465 

Gln Asn Gly Gly Thr Cys Asp Ser Val Thr Gly Ala Cys Arg Cys 
                470                 475                 480 

Pro Pro Gly Val Ser Gly Thr Asn Cys Glu Asp Gly Cys Pro Lys 
                485                 490                 495 

Gly Tyr Tyr Gly Lys His Cys Arg Lys Lys Cys Asn Cys Ala Asn 
                500                 505                 510 

Arg Gly Arg Cys His Arg Leu Tyr Gly Ala Cys Leu Cys Asp Pro 
                515                 520                 525 

Gly Leu Tyr Gly Arg Phe Cys His Leu Thr Cys Pro Pro Trp Ala 
                530                 535                 540 

Phe Gly Pro Gly Cys Ser Glu Glu Cys Gln Cys Val Gln Pro His 
                545                 550                 555 

Thr Gln Ser Cys Asp Lys Arg Asp Gly Ser Cys Ser Cys Lys Ala 
                560                 565                 570 

Gly Phe Arg Gly Glu Arg Cys Gln Ala Glu Cys Glu Leu Gly Tyr 
                575                 580                 585 

Phe Gly Pro Gly Cys Trp Gln Ala Cys Thr Cys Pro Val Gly Val 
                590                 595                 600 

Ala Cys Asp Ser Val Ser Gly Glu Cys Gly Lys Arg Cys Pro Ala 
                605                 610                 615 

Gly Phe Gln Gly Glu Asp Cys Gly Gln Glu Cys Pro Val Gly Thr 
                620                 625                 630 

Phe Gly Val Asn Cys Ser Ser Ser Cys Ser Cys Gly Gly Ala Pro 
                635                 640                 645 

Cys His Gly Val Thr Gly Gln Cys Arg Cys Pro Pro Gly Arg Thr 
                650                 655                 660 

Gly Glu Asp Cys Glu Ala Asp Cys Pro Glu Gly Arg Trp Gly Leu 
                665                 670                 675 

Gly Cys Gln Glu Ile Cys Pro Ala Cys Gln His Ala Ala Arg Cys 
                680                 685                 690 

Asp Pro Glu Thr Gly Ala Cys Leu Cys Leu Pro Gly Phe Val Gly 
                695                 700                 705 

Ser Arg Cys Gln Asp Val Cys Pro Ala Gly Trp Tyr Gly Pro Ser 
                710                 715                 720 

Cys Gln Thr Arg Cys Ser Cys Ala Asn Asp Gly His Cys His Pro 
                725                 730                 735 

Ala Thr Gly His Cys Ser Cys Ala Pro Gly Trp Thr Gly Phe Ser 
                740                 745                 750 

Cys Gln Arg Ala Cys Asp Thr Gly His Trp Gly Pro Asp Cys Ser 
                755                 760                 765 

His Pro Cys Asn Cys Ser Ala Gly His Gly Ser Cys Asp Ala Ile 
                770                 775                 780 

Ser Gly Leu Cys Leu Cys Glu Ala Gly Tyr Val Gly Pro Arg Cys 
                785                 790                 795 

Glu Gln Gln Cys Pro Gln Gly His Phe Gly Pro Gly Cys Glu Gln 
                800                 805                 810 

Leu Cys Gln Cys Gln His Gly Ala Ala Cys Asp His Val Ser Gly 
                815                 820                 825 

Ala Cys Thr Cys Pro Ala Gly Trp Arg Gly Thr Phe Cys Glu His 
                830                 835                 840 

Ala Cys Pro Ala Gly Phe Phe Gly Leu Asp Cys Arg Ser Ala Cys 
                845                 850                 855 

Asn Cys Thr Ala Gly Ala Ala Cys Asp Ala Val Asn Gly Ser Cys 
                860                 865                 870 

Leu Cys Pro Ala Gly Arg Arg Gly Pro Arg Cys Ala Glu Thr Cys 
                875                 880                 885 

Pro Ala His Thr Tyr Gly His Asn Cys Ser Gln Ala Cys Ala Cys 
                890                 895                 900 

Phe Asn Gly Ala Ser Cys Asp Pro Val His Gly Gln Cys His Cys 
                905                 910                 915 

Ala Pro Gly Trp Met Gly Pro Ser Cys Leu Gln Glu Cys Leu Pro 
                920                 925                 930 

Arg Asp Val Arg Ala Gly Cys Arg His Ser Gly Gly Cys Leu Asn 
                935                 940                 945 

Gly Gly Leu Cys Asp Pro His Thr Gly Arg Cys Leu Cys Pro Ala 
                950                 955                 960 

Gly Trp Thr Gly Asp Lys Cys Gln Ser Pro Cys Leu Arg Gly Trp 
                965                 970                 975 

Phe Gly Glu Ala Cys Ala Gln Arg Cys Ser Cys Pro Pro Gly Ala 
                980                 985                 990 

Ala Cys His His Val Thr Gly Ala Cys Arg Cys Pro Pro Gly Phe 
                995                1000                1005 

Thr Gly Ser Gly Cys Glu Gln Ala Cys Pro Pro Gly Ser Phe Gly 
               1010                1015                1020 

Glu Asp Cys Ala Gln Met Cys Gln Cys Pro Gly Glu Asn Pro Ala 
               1025                1030                1035 

Cys His Pro Ala Thr Gly Thr Cys Ser Cys Ala Ala Gly Tyr His 
               1040                1045                1050 

Gly Pro Ser Cys Gln Gln Arg Cys Pro Pro Gly Arg Tyr Gly Pro 
               1055                1060                1065 

Gly Cys Glu Gln Leu Cys Gly Cys Leu Asn Gly Gly Ser Cys Asp 
               1070                1075                1080 

Ala Ala Thr Gly Ala Cys Arg Cys Pro Thr Gly Phe Leu Gly Thr 
               1085                1090                1095 

Asp Cys Asn Leu Thr Cys Pro Gln Gly Arg Phe Gly Pro Asn Cys 
               1100                1105                1110 

Thr His Val Cys Gly Cys Gly Gln Gly Ala Ala Cys Asp Pro Val 
               1115                1120                1125 

Thr Gly Thr Cys Leu Cys Pro Pro Gly Arg Ala Gly Val Arg Cys 
               1130                1135                1140 

Glu Arg Gly Cys Pro Gln Asn Arg Phe Gly Val Gly Cys Glu His 
               1145                1150                1155 

Thr Cys Ser Cys Arg Asn Gly Gly Leu Cys His Ala Ser Asn Gly 
               1160                1165                1170 

Ser Cys Ser Cys Gly Leu Gly Trp Thr Gly Arg His Cys Glu Leu 
               1175                1180                1185 

Ala Cys Pro Pro Gly Arg Tyr Gly Ala Ala Cys His Leu Glu Cys 
               1190                1195                1200 

Ser Cys His Asn Asn Ser Thr Cys Glu Pro Ala Thr Gly Thr Cys 
               1205                1210                1215 

Arg Cys Gly Pro Gly Phe Tyr Gly Gln Ala Cys Glu His Pro Cys 
               1220                1225                1230 

Pro Pro Gly Phe His Gly Ala Gly Cys Gln Gly Leu Cys Trp Cys 
               1235                1240                1245 

Gln His Gly Ala Pro Cys Asp Pro Ile Ser Gly Arg Cys Leu Cys 
               1250                1255                1260 

Pro Ala Gly Phe His Gly His Phe Cys Glu Arg Gly Cys Glu Pro 
               1265                1270                1275 

Gly Ser Phe Gly Glu Gly Cys His Gln Arg Cys Asp Cys Asp Gly 
               1280                1285                1290 

Gly Ala Pro Cys Asp Pro Val Thr Gly Leu Cys Leu Cys Pro Pro 
               1295                1300                1305 

Gly Arg Ser Gly Ala Thr Cys Asn Leu Asp Cys Arg Arg Gly Gln 
               1310                1315                1320 

Phe Gly Pro Ser Cys Thr Leu His Cys Asp Cys Gly Gly Gly Ala 
               1325                1330                1335 

Asp Cys Asp Pro Val Ser Gly Gln Cys His Cys Val Asp Gly Tyr 
               1340                1345                1350 

Met Gly Pro Thr Cys Arg Glu Gly Gly Pro Leu Arg Leu Pro Glu 
               1355                1360                1365 

Asn Pro Ser Leu Ala Gln Gly Ser Ala Gly Thr Leu Pro Ala Ser 
               1370                1375                1380 

Ser Arg Pro Thr Ser Arg Ser Gly Gly Pro Ala Arg His 
               1385                1390 

 
           
             22  
             3695  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6382722CD1  
             
           
            22 

Met Ala Lys Arg Leu Cys Ala Gly Ser Ala Leu Cys Val Arg Gly 
  1               5                  10                  15 

Pro Arg Gly Pro Ala Pro Leu Leu Leu Val Gly Leu Ala Leu Leu 
                 20                  25                  30 

Gly Ala Ala Arg Ala Arg Glu Glu Ala Gly Gly Gly Phe Ser Leu 
                 35                  40                  45 

His Pro Pro Tyr Phe Asn Leu Ala Glu Gly Ala Arg Ile Ala Ala 
                 50                  55                  60 

Ser Ala Thr Cys Gly Glu Glu Ala Pro Ala Arg Gly Ser Pro Arg 
                 65                  70                  75 

Pro Thr Glu Asp Leu Tyr Cys Lys Leu Val Gly Gly Pro Val Ala 
                 80                  85                  90 

Gly Gly Asp Pro Asn Gln Thr Ile Arg Gly Gln Tyr Cys Asp Ile 
                 95                 100                 105 

Cys Thr Ala Ala Asn Ser Asn Lys Ala His Pro Ala Ser Asn Ala 
                110                 115                 120 

Ile Asp Gly Thr Glu Arg Trp Trp Gln Ser Pro Pro Leu Ser Arg 
                125                 130                 135 

Gly Leu Glu Tyr Asn Glu Val Asn Val Thr Leu Asp Leu Gly Gln 
                140                 145                 150 

Val Phe His Val Ala Tyr Val Leu Ile Lys Phe Ala Asn Ser Pro 
                155                 160                 165 

Arg Pro Asp Leu Trp Val Leu Glu Arg Ser Met Asp Phe Gly Arg 
                170                 175                 180 

Thr Tyr Gln Pro Trp Gln Phe Phe Ala Ser Ser Lys Arg Asp Cys 
                185                 190                 195 

Leu Glu Arg Phe Gly Pro Gln Thr Leu Glu Arg Ile Thr Arg Asp 
                200                 205                 210 

Asp Ala Ala Ile Cys Thr Thr Glu Tyr Ser Arg Ile Val Pro Leu 
                215                 220                 225 

Glu Asn Gly Glu Ile Val Val Ser Leu Val Asn Gly Arg Pro Gly 
                230                 235                 240 

Ala Met Asn Phe Ser Tyr Ser Pro Leu Leu Arg Glu Phe Thr Lys 
                245                 250                 255 

Ala Thr Asn Val Arg Leu Arg Phe Leu Arg Thr Asn Thr Leu Leu 
                260                 265                 270 

Gly His Leu Met Gly Lys Ala Leu Arg Asp Pro Thr Val Thr Arg 
                275                 280                 285 

Arg Tyr Tyr Tyr Ser Ile Lys Asp Ile Ser Ile Gly Gly Arg Cys 
                290                 295                 300 

Val Cys His Gly His Ala Asp Ala Cys Asp Ala Lys Asp Pro Thr 
                305                 310                 315 

Asp Pro Phe Arg Leu Gln Cys Thr Cys Gln His Asn Thr Cys Gly 
                320                 325                 330 

Gly Thr Cys Asp Arg Cys Cys Pro Gly Phe Asn Gln Gln Pro Trp 
                335                 340                 345 

Lys Pro Ala Thr Ala Asn Ser Ala Asn Glu Cys Gln Ser Cys Asn 
                350                 355                 360 

Cys Tyr Gly His Ala Thr Asp Cys Tyr Tyr Asp Pro Glu Val Asp 
                365                 370                 375 

Arg Arg Arg Ala Ser Gln Ser Leu Asp Gly Thr Tyr Gln Gly Gly 
                380                 385                 390 

Gly Val Cys Ile Asp Cys Gln His His Thr Ala Gly Val Asn Cys 
                395                 400                 405 

Glu Arg Cys Leu Pro Gly Phe Tyr Arg Ser Pro Asn His Pro Leu 
                410                 415                 420 

Asp Ser Pro His Val Cys Arg Arg Cys Asn Cys Glu Ser Asp Phe 
                425                 430                 435 

Thr Asp Gly Thr Cys Glu Asp Leu Thr Gly Arg Cys Tyr Cys Arg 
                440                 445                 450 

Pro Asn Phe Ser Gly Glu Arg Cys Asp Val Cys Ala Glu Gly Phe 
                455                 460                 465 

Thr Gly Phe Pro Ser Cys Tyr Pro Thr Pro Ser Ser Ser Asn Asp 
                470                 475                 480 

Thr Arg Glu Gln Val Leu Pro Ala Gly Gln Ile Val Asn Cys Asp 
                485                 490                 495 

Cys Ser Ala Ala Gly Thr Gln Gly Asn Ala Cys Arg Lys Asp Pro 
                500                 505                 510 

Arg Val Gly Arg Cys Leu Cys Lys Pro Asn Phe Gln Gly Thr His 
                515                 520                 525 

Cys Glu Leu Cys Ala Pro Gly Phe Tyr Gly Pro Gly Cys Gln Pro 
                530                 535                 540 

Cys Gln Cys Ser Ser Pro Gly Val Ala Asp Asp Arg Cys Asp Pro 
                545                 550                 555 

Asp Thr Gly Gln Cys Arg Cys Arg Val Gly Phe Glu Gly Ala Thr 
                560                 565                 570 

Cys Asp Arg Cys Ala Pro Gly Tyr Phe His Phe Pro Leu Cys Gln 
                575                 580                 585 

Leu Cys Gly Cys Ser Pro Ala Gly Thr Leu Pro Glu Gly Cys Asp 
                590                 595                 600 

Glu Ala Gly Arg Cys Leu Cys Gln Pro Glu Phe Ala Gly Pro His 
                605                 610                 615 

Cys Asp Arg Cys Arg Pro Gly Tyr His Gly Phe Pro Asn Cys Gln 
                620                 625                 630 

Ala Cys Thr Cys Asp Pro Arg Gly Ala Leu Asp Gln Leu Cys Gly 
                635                 640                 645 

Ala Gly Gly Leu Cys Arg Cys Arg Pro Gly Tyr Thr Gly Thr Ala 
                650                 655                 660 

Cys Gln Glu Cys Ser Pro Gly Phe His Gly Phe Pro Ser Cys Val 
                665                 670                 675 

Pro Cys His Cys Ser Ala Glu Gly Ser Leu His Ala Ala Cys Asp 
                680                 685                 690 

Pro Arg Ser Gly Gln Cys Ser Cys Arg Pro Arg Val Thr Gly Leu 
                695                 700                 705 

Arg Cys Asp Thr Cys Val Pro Gly Ala Tyr Asn Phe Pro Tyr Cys 
                710                 715                 720 

Glu Ala Gly Ser Cys His Pro Ala Gly Leu Ala Pro Val Asp Pro 
                725                 730                 735 

Ala Leu Pro Glu Ala Gln Val Pro Cys Met Cys Arg Ala His Val 
                740                 745                 750 

Glu Gly Pro Ser Cys Asp Arg Cys Lys Pro Gly Phe Trp Gly Leu 
                755                 760                 765 

Ser Pro Ser Asn Pro Glu Gly Cys Thr Arg Cys Ser Cys Asp Leu 
                770                 775                 780 

Arg Gly Thr Leu Gly Gly Val Ala Glu Cys Gln Pro Gly Thr Gly 
                785                 790                 795 

Gln Cys Phe Cys Lys Pro His Val Cys Gly Gln Ala Cys Ala Ser 
                800                 805                 810 

Cys Lys Asp Gly Phe Phe Gly Leu Asp Gln Ala Asp Tyr Phe Gly 
                815                 820                 825 

Cys Arg Ser Cys Arg Cys Asp Ile Gly Gly Ala Leu Gly Gln Ser 
                830                 835                 840 

Cys Glu Pro Arg Thr Gly Val Cys Arg Cys Arg Pro Asn Thr Gln 
                845                 850                 855 

Gly Pro Thr Cys Ser Glu Pro Ala Arg Asp His Tyr Leu Pro Asp 
                860                 865                 870 

Leu His His Leu Arg Leu Glu Leu Glu Glu Ala Ala Thr Pro Glu 
                875                 880                 885 

Gly His Ala Val Arg Phe Gly Phe Asn Pro Leu Glu Phe Glu Asn 
                890                 895                 900 

Phe Ser Trp Arg Gly Tyr Ala Gln Met Ala Pro Val Gln Pro Arg 
                905                 910                 915 

Ile Val Ala Arg Leu Asn Leu Thr Ser Pro Asp Leu Phe Trp Leu 
                920                 925                 930 

Val Phe Arg Tyr Val Asn Arg Gly Ala Met Ser Val Ser Gly Arg 
                935                 940                 945 

Val Ser Val Arg Glu Glu Gly Arg Ser Ala Ala Cys Ala Asn Cys 
                950                 955                 960 

Thr Ala Gln Ser Gln Pro Val Ala Phe Pro Pro Ser Thr Glu Pro 
                965                 970                 975 

Ala Phe Ile Thr Val Pro Gln Arg Gly Phe Gly Glu Pro Phe Val 
                980                 985                 990 

Leu Asn Pro Gly Thr Trp Ala Leu Arg Val Glu Ala Glu Gly Val 
                995                1000                1005 

Leu Leu Asp Tyr Val Val Leu Leu Pro Ser Ala Tyr Tyr Glu Ala 
               1010                1015                1020 

Ala Leu Leu Gln Leu Arg Val Thr Glu Ala Cys Thr Tyr Arg Pro 
               1025                1030                1035 

Ser Ala Gln Gln Ser Gly Asp Asn Cys Leu Leu Tyr Thr His Leu 
               1040                1045                1050 

Pro Leu Asp Gly Phe Pro Ser Ala Ala Gly Leu Glu Ala Leu Cys 
               1055                1060                1065 

Arg Gln Asp Asn Ser Leu Pro Arg Pro Cys Pro Thr Glu Gln Leu 
               1070                1075                1080 

Ser Pro Ser His Pro Pro Leu Ile Thr Cys Thr Gly Ser Asp Val 
               1085                1090                1095 

Asp Val Gln Leu Gln Val Ala Val Pro Gln Pro Gly Arg Tyr Ala 
               1100                1105                1110 

Leu Val Val Glu Tyr Ala Asn Glu Asp Ala Arg Gln Glu Val Gly 
               1115                1120                1125 

Val Ala Val His Thr Pro Gln Arg Ala Pro Gln Gln Gly Leu Leu 
               1130                1135                1140 

Ser Leu His Pro Cys Leu Tyr Ser Thr Leu Cys Arg Gly Thr Ala 
               1145                1150                1155 

Arg Asp Thr Gln Asp His Leu Ala Val Phe His Leu Asp Ser Glu 
               1160                1165                1170 

Ala Ser Val Arg Leu Thr Ala Glu Gln Ala Arg Phe Phe Leu His 
               1175                1180                1185 

Gly Val Thr Leu Val Pro Ile Glu Glu Phe Ser Pro Glu Phe Val 
               1190                1195                1200 

Glu Pro Arg Val Ser Cys Ile Ser Ser His Gly Ala Phe Gly Pro 
               1205                1210                1215 

Asn Ser Ala Ala Cys Leu Pro Ser Arg Phe Pro Lys Pro Pro Gln 
               1220                1225                1230 

Pro Ile Ile Leu Arg Asp Cys Gln Val Ile Pro Leu Pro Pro Gly 
               1235                1240                1245 

Leu Pro Leu Thr His Ala Gln Asp Leu Thr Pro Ala Thr Ser Pro 
               1250                1255                1260 

Ala Gly Pro Arg Pro Arg Pro Pro Thr Ala Val Asp Pro Asp Ala 
               1265                1270                1275 

Glu Pro Thr Leu Leu Arg Glu Pro Gln Ala Thr Val Val Phe Thr 
               1280                1285                1290 

Thr His Val Pro Thr Leu Gly Arg Tyr Ala Phe Leu Leu His Gly 
               1295                1300                1305 

Tyr Gln Pro Ala His Pro Thr Phe Pro Val Glu Val Leu Ile Asn 
               1310                1315                1320 

Ala Gly Arg Val Trp Gln Gly His Ala Asn Ala Ser Phe Cys Pro 
               1325                1330                1335 

His Gly Tyr Gly Cys Arg Thr Leu Val Val Cys Glu Gly Gln Ala 
               1340                1345                1350 

Leu Leu Asp Val Thr His Ser Glu Leu Thr Val Thr Val Arg Val 
               1355                1360                1365 

Pro Glu Gly Arg Trp Leu Trp Leu Asp Tyr Val Leu Val Val Pro 
               1370                1375                1380 

Glu Asn Val Tyr Ser Phe Gly Tyr Leu Arg Glu Glu Pro Leu Asp 
               1385                1390                1395 

Lys Ser Tyr Asp Phe Ile Ser His Cys Ala Ala Gln Gly Tyr His 
               1400                1405                1410 

Ile Ser Pro Ser Ser Ser Ser Leu Phe Cys Arg Asn Ala Ala Ala 
               1415                1420                1425 

Ser Leu Ser Leu Phe Tyr Asn Asn Gly Ala Arg Pro Cys Gly Cys 
               1430                1435                1440 

His Glu Val Gly Ala Thr Gly Pro Thr Cys Glu Pro Phe Gly Gly 
               1445                1450                1455 

Gln Cys Pro Cys His Ala His Val Ile Gly Arg Asp Cys Ser Arg 
               1460                1465                1470 

Cys Ala Thr Gly Tyr Trp Gly Phe Pro Asn Cys Arg Pro Cys Asp 
               1475                1480                1485 

Cys Gly Ala Arg Leu Cys Asp Glu Leu Thr Gly Gln Cys Ile Cys 
               1490                1495                1500 

Pro Pro Arg Thr Ile Pro Pro Asp Cys Leu Leu Cys Gln Pro Gln 
               1505                1510                1515 

Thr Phe Gly Cys His Pro Leu Val Gly Cys Glu Glu Cys Asn Cys 
               1520                1525                1530 

Ser Gly Pro Gly Ile Gln Glu Leu Thr Asp Pro Thr Cys Asp Thr 
               1535                1540                1545 

Asp Ser Gly Gln Cys Lys Cys Arg Pro Asn Val Thr Gly Arg Arg 
               1550                1555                1560 

Cys Asp Thr Cys Ser Pro Gly Phe His Gly Tyr Pro Arg Cys Arg 
               1565                1570                1575 

Pro Cys Asp Cys His Glu Ala Gly Thr Ala Pro Gly Val Cys Asp 
               1580                1585                1590 

Pro Leu Thr Gly Gln Cys Tyr Cys Lys Glu Asn Val Gln Gly Pro 
               1595                1600                1605 

Lys Cys Asp Gln Cys Ser Leu Gly Thr Phe Ser Leu Asp Ala Ala 
               1610                1615                1620 

Asn Pro Lys Gly Cys Thr Arg Cys Phe Cys Phe Gly Ala Thr Glu 
               1625                1630                1635 

Arg Cys Arg Ser Ser Ser Tyr Thr Arg Gln Glu Phe Val Asp Met 
               1640                1645                1650 

Glu Gly Trp Val Leu Leu Ser Thr Asp Arg Gln Val Val Pro His 
               1655                1660                1665 

Glu Arg Gln Pro Gly Thr Glu Met Leu Arg Ala Asp Leu Arg His 
               1670                1675                1680 

Val Pro Glu Ala Val Pro Glu Ala Phe Pro Glu Leu Tyr Trp Gln 
               1685                1690                1695 

Ala Pro Pro Ser Tyr Leu Gly Asp Arg Val Ser Ser Tyr Gly Gly 
               1700                1705                1710 

Thr Leu Arg Tyr Glu Leu His Ser Glu Thr Gln Arg Gly Asp Val 
               1715                1720                1725 

Phe Val Pro Met Glu Ser Arg Pro Asp Val Val Leu Gln Gly Asn 
               1730                1735                1740 

Gln Met Ser Ile Thr Phe Leu Glu Pro Ala Tyr Pro Thr Pro Gly 
               1745                1750                1755 

His Val His Arg Gly Gln Leu Gln Leu Val Glu Gly Asn Phe Arg 
               1760                1765                1770 

His Thr Glu Thr Arg Asn Thr Val Ser Arg Glu Glu Leu Met Met 
               1775                1780                1785 

Val Leu Ala Ser Leu Glu Gln Leu Gln Ile Arg Ala Leu Phe Ser 
               1790                1795                1800 

Gln Ile Ser Ser Ala Val Ser Leu Arg Arg Val Ala Leu Glu Val 
               1805                1810                1815 

Ala Ser Pro Ala Gly Gln Gly Ala Leu Ala Ser Asn Val Glu Leu 
               1820                1825                1830 

Cys Leu Cys Pro Ala Ser Tyr Arg Gly Asp Ser Cys Gln Glu Cys 
               1835                1840                1845 

Ala Pro Gly Phe Tyr Arg Asp Val Lys Gly Leu Phe Leu Gly Arg 
               1850                1855                1860 

Cys Val Pro Cys Gln Cys His Gly His Ser Asp Arg Cys Leu Pro 
               1865                1870                1875 

Gly Ser Gly Val Cys Val Asp Cys Gln His Asn Thr Glu Gly Ala 
               1880                1885                1890 

His Cys Glu Arg Cys Gln Ala Gly Phe Met Ser Ser Arg Asp Asp 
               1895                1900                1905 

Pro Ser Ala Pro Cys Val Ser Cys Pro Cys Pro Leu Ser Val Pro 
               1910                1915                1920 

Ser Asn Asn Phe Ala Glu Gly Cys Val Leu Arg Gly Gly Arg Thr 
               1925                1930                1935 

Gln Cys Leu Cys Lys Pro Gly Tyr Ala Gly Ala Ser Cys Glu Arg 
               1940                1945                1950 

Cys Ala Pro Gly Phe Phe Gly Asn Pro Leu Val Leu Gly Ser Ser 
               1955                1960                1965 

Cys Gln Pro Cys Asp Cys Ser Gly Asn Gly Asp Pro Asn Leu Leu 
               1970                1975                1980 

Phe Ser Asp Cys Asp Pro Leu Thr Gly Ala Cys Arg Gly Cys Leu 
               1985                1990                1995 

Arg His Thr Thr Gly Pro Arg Cys Glu Ile Cys Ala Pro Gly Phe 
               2000                2005                2010 

Tyr Gly Asn Ala Leu Leu Pro Gly Asn Cys Thr Arg Cys Asp Cys 
               2015                2020                2025 

Thr Pro Cys Gly Thr Glu Ala Cys Asp Pro His Ser Gly His Cys 
               2030                2035                2040 

Leu Cys Lys Ala Gly Val Thr Gly Arg Arg Cys Asp Arg Cys Gln 
               2045                2050                2055 

Glu Gly His Phe Gly Phe Asn Gly Cys Gly Gly Cys Arg Pro Cys 
               2060                2065                2070 

Ala Cys Gly Pro Ala Ala Glu Gly Ser Glu Cys His Pro Gln Ser 
               2075                2080                2085 

Gly Gln Cys His Cys Arg Pro Gly Thr Met Gly Pro Gln Cys Arg 
               2090                2095                2100 

Glu Cys Ala Pro Gly Tyr Trp Gly Leu Pro Glu Gln Gly Cys Arg 
               2105                2110                2115 

Arg Cys Gln Cys Pro Gly Gly Arg Cys Asp Pro His Thr Gly Arg 
               2120                2125                2130 

Cys Asn Cys Pro Pro Gly Leu Ser Gly Glu Arg Cys Asp Thr Cys 
               2135                2140                2145 

Ser Gln Gln His Gln Val Pro Val Pro Gly Gly Pro Val Gly His 
               2150                2155                2160 

Ser Ile His Cys Glu Val Cys Asp His Cys Val Val Leu Leu Leu 
               2165                2170                2175 

Asp Asp Leu Glu Arg Ala Gly Ala Leu Leu Pro Ala Ile His Glu 
               2180                2185                2190 

Gln Leu Arg Gly Ile Asn Ala Ser Ser Met Ala Trp Ala Arg Leu 
               2195                2200                2205 

His Arg Leu Asn Ala Ser Ile Ala Asp Leu Gln Ser Gln Leu Arg 
               2210                2215                2220 

Ser Pro Leu Gly Pro Arg His Glu Thr Ala Gln Gln Leu Glu Val 
               2225                2230                2235 

Leu Glu Gln Gln Ser Thr Ser Leu Gly Gln Asp Ala Arg Arg Leu 
               2240                2245                2250 

Gly Gly Gln Ala Val Gly Thr Arg Asp Gln Ala Ser Gln Leu Leu 
               2255                2260                2265 

Ala Gly Thr Glu Ala Thr Leu Gly His Ala Lys Thr Leu Leu Ala 
               2270                2275                2280 

Ala Ile Arg Ala Val Asp Arg Thr Leu Ser Glu Leu Met Ser Gln 
               2285                2290                2295 

Thr Gly His Leu Gly Leu Ala Asn Ala Ser Ala Pro Ser Gly Glu 
               2300                2305                2310 

Gln Leu Leu Arg Thr Leu Ala Glu Val Glu Arg Leu Leu Trp Glu 
               2315                2320                2325 

Met Arg Ala Arg Asp Leu Gly Ala Pro Gln Ala Ala Ala Glu Ala 
               2330                2335                2340 

Glu Leu Ala Ala Ala Gln Arg Leu Leu Ala Arg Val Gln Glu Gln 
               2345                2350                2355 

Leu Ser Ser Leu Trp Glu Glu Asn Gln Ala Leu Ala Thr Gln Thr 
               2360                2365                2370 

Arg Asp Arg Leu Ala Gln His Glu Ala Gly Leu Met Asp Leu Arg 
               2375                2380                2385 

Glu Ala Leu Asn Arg Ala Val Asp Ala Thr Arg Glu Ala Gln Glu 
               2390                2395                2400 

Leu Asn Ser Arg Asn Gln Glu Arg Leu Glu Glu Ala Leu Gln Arg 
               2405                2410                2415 

Lys Gln Glu Leu Ser Arg Asp Asn Ala Thr Leu Gln Ala Thr Leu 
               2420                2425                2430 

His Ala Ala Arg Asp Thr Leu Ala Ser Val Phe Arg Leu Leu His 
               2435                2440                2445 

Ser Leu Asp Gln Ala Lys Glu Glu Leu Glu Arg Leu Ala Ala Ser 
               2450                2455                2460 

Leu Asp Gly Ala Arg Thr Pro Leu Leu Gln Arg Met Gln Thr Phe 
               2465                2470                2475 

Ser Pro Ala Gly Ser Lys Leu Arg Leu Val Glu Ala Ala Glu Ala 
               2480                2485                2490 

His Ala Gln Gln Leu Gly Gln Leu Ala Leu Asn Leu Ser Ser Ile 
               2495                2500                2505 

Ile Leu Asp Val Asn Gln Asp Arg Leu Thr Gln Arg Ala Ile Glu 
               2510                2515                2520 

Ala Ser Asn Ala Tyr Ser Arg Ile Leu Gln Ala Val Gln Ala Ala 
               2525                2530                2535 

Glu Asp Ala Ala Gly Gln Ala Leu Gln Gln Ala Asp His Thr Trp 
               2540                2545                2550 

Ala Thr Val Val Arg Gln Gly Leu Val Asp Arg Ala Gln Gln Leu 
               2555                2560                2565 

Leu Ala Asn Ser Thr Ala Leu Glu Glu Ala Met Leu Gln Glu Gln 
               2570                2575                2580 

Gln Arg Leu Gly Leu Val Trp Ala Ala Leu Gln Gly Ala Arg Thr 
               2585                2590                2595 

Gln Leu Arg Asp Val Arg Ala Lys Lys Asp Gln Leu Glu Ala His 
               2600                2605                2610 

Ile Gln Ala Ala Gln Ala Met Leu Ala Met Asp Thr Asp Glu Thr 
               2615                2620                2625 

Ser Lys Lys Ile Ala His Ala Lys Ala Val Ala Ala Glu Ala Gln 
               2630                2635                2640 

Asp Thr Ala Thr Arg Val Gln Ser Gln Leu Gln Ala Met Gln Glu 
               2645                2650                2655 

Asn Val Glu Arg Trp Gln Gly Gln Tyr Glu Gly Leu Arg Gly Gln 
               2660                2665                2670 

Asp Leu Gly Gln Ala Val Leu Asp Ala Gly His Ser Val Ser Thr 
               2675                2680                2685 

Leu Glu Lys Thr Leu Pro Gln Leu Leu Ala Lys Leu Ser Ile Leu 
               2690                2695                2700 

Glu Asn Arg Gly Val His Asn Ala Ser Leu Ala Leu Ser Ala Ser 
               2705                2710                2715 

Ile Gly Arg Val Arg Glu Leu Ile Ala Gln Ala Arg Gly Ala Ala 
               2720                2725                2730 

Ser Lys Val Lys Val Pro Met Lys Phe Asn Gly Arg Ser Gly Val 
               2735                2740                2745 

Gln Leu Arg Thr Pro Arg Asp Leu Ala Asp Leu Ala Ala Tyr Thr 
               2750                2755                2760 

Ala Leu Lys Phe Tyr Leu Gln Gly Pro Glu Pro Glu Pro Gly Gln 
               2765                2770                2775 

Gly Thr Glu Asp Arg Phe Val Met Tyr Met Gly Ser Arg Gln Ala 
               2780                2785                2790 

Thr Gly Asp Tyr Met Gly Val Ser Leu Arg Asp Lys Lys Val His 
               2795                2800                2805 

Trp Val Tyr Gln Leu Gly Glu Ala Gly Pro Ala Val Leu Ser Ile 
               2810                2815                2820 

Asp Glu Asp Ile Gly Glu Gln Phe Ala Ala Val Ser Leu Asp Arg 
               2825                2830                2835 

Thr Leu Gln Phe Gly His Met Ser Val Thr Val Glu Arg Gln Met 
               2840                2845                2850 

Ile Gln Glu Thr Lys Gly Asp Thr Val Ala Pro Gly Ala Glu Gly 
               2855                2860                2865 

Leu Leu Asn Leu Arg Pro Asp Asp Phe Val Phe Tyr Val Gly Gly 
               2870                2875                2880 

Tyr Pro Ser Thr Phe Thr Pro Pro Pro Leu Leu Arg Phe Pro Gly 
               2885                2890                2895 

Tyr Arg Gly Cys Ile Glu Met Asp Thr Leu Asn Glu Glu Val Val 
               2900                2905                2910 

Ser Leu Tyr Asn Phe Glu Arg Thr Phe Gln Leu Asp Thr Ala Val 
               2915                2920                2925 

Asp Arg Pro Cys Ala Arg Ser Lys Ser Thr Gly Asp Pro Trp Leu 
               2930                2935                2940 

Thr Asp Gly Ser Tyr Leu Asp Gly Thr Gly Phe Ala Arg Ile Ser 
               2945                2950                2955 

Phe Asp Ser Gln Ile Ser Thr Thr Lys Arg Phe Glu Gln Glu Leu 
               2960                2965                2970 

Arg Leu Val Ser Tyr Ser Gly Val Leu Phe Phe Leu Lys Gln Gln 
               2975                2980                2985 

Ser Gln Phe Leu Cys Leu Ala Val Gln Glu Gly Ser Leu Val Leu 
               2990                2995                3000 

Leu Tyr Asp Phe Gly Ala Gly Leu Lys Lys Ala Val Pro Leu Gln 
               3005                3010                3015 

Pro Pro Pro Pro Leu Thr Ser Ala Ser Lys Ala Ile Gln Val Phe 
               3020                3025                3030 

Leu Leu Gly Gly Ser Arg Lys Arg Val Leu Val Arg Val Glu Arg 
               3035                3040                3045 

Ala Thr Val Tyr Ser Val Glu Gln Asp Asn Asp Leu Glu Leu Ala 
               3050                3055                3060 

Asp Ala Tyr Tyr Leu Gly Gly Val Pro Pro Asp Gln Leu Pro Pro 
               3065                3070                3075 

Ser Leu Arg Arg Leu Phe Pro Thr Gly Gly Ser Val Arg Gly Cys 
               3080                3085                3090 

Val Lys Gly Ile Lys Ala Leu Gly Lys Tyr Val Asp Leu Lys Arg 
               3095                3100                3105 

Leu Asn Thr Thr Gly Val Ser Ala Gly Cys Thr Ala Asp Leu Leu 
               3110                3115                3120 

Val Gly Arg Ala Met Thr Phe His Gly His Gly Phe Leu Arg Leu 
               3125                3130                3135 

Ala Leu Ser Asn Val Ala Pro Leu Thr Gly Asn Val Tyr Ser Gly 
               3140                3145                3150 

Phe Gly Phe His Ser Ala Gln Asp Ser Ala Leu Leu Tyr Tyr Arg 
               3155                3160                3165 

Ala Ser Pro Asp Gly Leu Cys Gln Val Ser Leu Gln Gln Gly Arg 
               3170                3175                3180 

Val Ser Leu Gln Leu Leu Arg Thr Glu Val Lys Thr Gln Ala Gly 
               3185                3190                3195 

Phe Ala Asp Gly Ala Pro His Tyr Val Ala Phe Tyr Ser Asn Ala 
               3200                3205                3210 

Thr Gly Val Trp Leu Tyr Val Asp Asp Gln Leu Gln Gln Met Lys 
               3215                3220                3225 

Pro His Arg Gly Pro Pro Pro Glu Leu Gln Pro Gln Pro Glu Gly 
               3230                3235                3240 

Pro Pro Arg Leu Leu Leu Gly Gly Leu Pro Glu Ser Gly Thr Ile 
               3245                3250                3255 

Tyr Asn Phe Ser Gly Cys Ile Ser Asn Val Phe Val Gln Arg Leu 
               3260                3265                3270 

Leu Gly Pro Gln Arg Val Phe Asp Leu Gln Gln Asn Leu Gly Ser 
               3275                3280                3285 

Val Asn Val Ser Thr Gly Cys Ala Pro Ala Leu Gln Ala Gln Thr 
               3290                3295                3300 

Pro Gly Leu Gly Pro Arg Gly Leu Gln Ala Thr Ala Arg Lys Ala 
               3305                3310                3315 

Ser Arg Arg Ser Arg Gln Pro Ala Arg His Pro Ala Cys Met Leu 
               3320                3325                3330 

Pro Pro His Leu Arg Thr Thr Arg Asp Ser Tyr Gln Phe Gly Gly 
               3335                3340                3345 

Ser Leu Ser Ser His Leu Glu Phe Val Gly Ile Leu Ala Arg His 
               3350                3355                3360 

Arg Asn Trp Pro Ser Leu Ser Met His Val Leu Pro Arg Ser Ser 
               3365                3370                3375 

Arg Gly Leu Leu Leu Phe Thr Ala Arg Leu Arg Pro Gly Ser Pro 
               3380                3385                3390 

Ser Leu Ala Leu Phe Leu Ser Asn Gly His Phe Val Ala Gln Met 
               3395                3400                3405 

Glu Gly Leu Gly Thr Arg Leu Arg Ala Gln Ser Arg Gln Arg Ser 
               3410                3415                3420 

Arg Pro Gly Arg Trp His Lys Val Ser Val Arg Trp Glu Lys Asn 
               3425                3430                3435 

Arg Ile Leu Leu Val Thr Asp Gly Ala Arg Ala Trp Ser Gln Glu 
               3440                3445                3450 

Gly Pro His Arg Gln His Gln Gly Ala Glu His Pro Gln Pro His 
               3455                3460                3465 

Thr Leu Phe Val Gly Gly Leu Pro Ala Ser Ser His Ser Ser Lys 
               3470                3475                3480 

Leu Pro Val Thr Val Gly Phe Ser Gly Cys Val Lys Arg Leu Arg 
               3485                3490                3495 

Leu His Gly Arg Pro Leu Gly Ala Pro Thr Arg Met Ala Gly Val 
               3500                3505                3510 

Thr Pro Cys Ile Leu Gly Pro Leu Glu Ala Gly Leu Phe Phe Pro 
               3515                3520                3525 

Gly Ser Gly Gly Val Ile Thr Leu Asp Leu Pro Gly Ala Thr Leu 
               3530                3535                3540 

Pro Asp Val Gly Leu Glu Leu Glu Val Arg Pro Leu Ala Val Thr 
               3545                3550                3555 

Gly Leu Ile Phe His Leu Gly Gln Ala Arg Thr Pro Pro Tyr Leu 
               3560                3565                3570 

Gln Leu Gln Val Thr Glu Lys Gln Val Leu Leu Arg Ala Asp Asp 
               3575                3580                3585 

Gly Ala Gly Glu Phe Ser Thr Ser Val Thr Arg Pro Ser Val Leu 
               3590                3595                3600 

Cys Asp Gly Gln Trp His Arg Leu Ala Val Met Lys Ser Gly Asn 
               3605                3610                3615 

Val Leu Arg Leu Glu Val Asp Ala Gln Ser Asn His Thr Val Gly 
               3620                3625                3630 

Pro Leu Leu Ala Ala Ala Ala Gly Ala Pro Ala Pro Leu Tyr Leu 
               3635                3640                3645 

Gly Gly Leu Pro Glu Pro Met Ala Val Gln Pro Trp Pro Pro Ala 
               3650                3655                3660 

Tyr Cys Gly Cys Met Arg Arg Leu Ala Val Asn Arg Ser Pro Val 
               3665                3670                3675 

Ala Met Thr Arg Ser Val Glu Val His Gly Ala Val Gly Ala Ser 
               3680                3685                3690 

Gly Cys Pro Ala Ala 
               3695 

 
           
             23  
             1255  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 55022490CD1  
             
           
            23 

Met Val Arg Gly Gly Arg Trp Glu Gln Ala His Lys Lys Glu Pro 
  1               5                  10                  15 

Leu Gly Val Trp Gly Pro Leu Pro Cys Val Arg Gly Ala Gln Gly 
                 20                  25                  30 

Thr Leu Gly Asp Arg Asn Gly Gly Thr Gly Gly Trp Arg His Trp 
                 35                  40                  45 

Gly Gly Cys Glu Gly Met Pro Met Pro Ser Ser Ser Gln Asn Val 
                 50                  55                  60 

Cys Thr Asn Ser Gly Ala Ser Val Gly Thr Thr Cys His Ser Lys 
                 65                  70                  75 

Leu Asp Ala Ala Val Asp Gly Thr Arg Cys Gly Glu Asn Lys Trp 
                 80                  85                  90 

Cys Leu Ser Gly Glu Cys Val Pro Val Gly Phe Arg Pro Glu Ala 
                 95                 100                 105 

Val Asp Gly Gly Trp Ser Gly Trp Ser Ala Trp Ser Ile Cys Ser 
                110                 115                 120 

Arg Ser Cys Gly Met Gly Val Gln Ser Ala Glu Arg Gln Cys Thr 
                125                 130                 135 

Gln Pro Thr Pro Lys Tyr Lys Gly Arg Tyr Cys Val Gly Glu Arg 
                140                 145                 150 

Lys Arg Phe Arg Leu Cys Asn Leu Gln Ala Cys Pro Ala Gly His 
                155                 160                 165 

Pro Ser Phe Arg His Val Gln Cys Ser His Phe Asp Ala Met Leu 
                170                 175                 180 

Tyr Lys Gly Gln Leu His Thr Trp Val Pro Val Val Asn Asp Val 
                185                 190                 195 

Asn Pro Cys Glu Leu His Cys Arg Pro Ala Asn Glu Tyr Phe Ala 
                200                 205                 210 

Glu Lys Leu Arg Asp Ala Val Val Asp Gly Thr Pro Cys Tyr Gln 
                215                 220                 225 

Val Arg Ala Ser Arg Asp Leu Cys Ile Asn Gly Ile Cys Lys Asn 
                230                 235                 240 

Val Gly Cys Asp Phe Glu Ile Asp Ser Gly Ala Met Glu Asp Arg 
                245                 250                 255 

Cys Gly Val Cys His Gly Asn Gly Ser Thr Cys His Thr Val Ser 
                260                 265                 270 

Gly Thr Phe Glu Glu Ala Glu Gly Leu Gly Tyr Val Asp Val Gly 
                275                 280                 285 

Leu Ile Pro Ala Gly Ala Arg Glu Ile Arg Ile Gln Glu Val Ala 
                290                 295                 300 

Glu Ala Ala Asn Phe Leu Ala Leu Arg Ser Glu Asp Pro Glu Lys 
                305                 310                 315 

Tyr Phe Leu Asn Gly Gly Trp Thr Ile Gln Trp Asn Gly Asp Tyr 
                320                 325                 330 

Gln Val Ala Gly Thr Thr Phe Thr Tyr Ala Arg Arg Gly Asn Trp 
                335                 340                 345 

Glu Asn Leu Thr Ser Pro Gly Pro Thr Lys Glu Pro Val Trp Ile 
                350                 355                 360 

Gln Leu Leu Phe Gln Glu Ser Asn Pro Gly Val His Tyr Glu Tyr 
                365                 370                 375 

Thr Ile His Arg Glu Ala Gly Gly His Asp Glu Val Pro Pro Pro 
                380                 385                 390 

Val Phe Ser Trp His Tyr Gly Pro Trp Thr Lys Cys Thr Val Thr 
                395                 400                 405 

Cys Gly Arg Gly Val Gln Arg Gln Asn Val Tyr Cys Leu Glu Arg 
                410                 415                 420 

Gln Ala Gly Pro Val Asp Glu Glu His Cys Asp Pro Leu Gly Arg 
                425                 430                 435 

Pro Asp Asp Gln Gln Arg Lys Cys Ser Glu Gln Pro Cys Pro Ala 
                440                 445                 450 

Arg Trp Trp Ala Gly Glu Trp Gln Leu Cys Ser Ser Ser Cys Gly 
                455                 460                 465 

Pro Gly Gly Leu Ser Arg Arg Ala Val Leu Cys Ile Arg Ser Val 
                470                 475                 480 

Gly Leu Asp Glu Gln Ser Ala Leu Glu Pro Pro Ala Cys Glu His 
                485                 490                 495 

Leu Pro Arg Pro Pro Thr Glu Thr Pro Cys Asn Arg His Val Pro 
                500                 505                 510 

Cys Pro Ala Thr Trp Ala Val Gly Asn Trp Ser Gln Cys Ser Val 
                515                 520                 525 

Thr Cys Gly Glu Gly Thr Gln Arg Arg Asn Val Leu Cys Thr Asn 
                530                 535                 540 

Asp Thr Gly Val Pro Cys Asp Glu Ala Gln Gln Pro Ala Ser Glu 
                545                 550                 555 

Val Thr Cys Ser Leu Pro Leu Cys Arg Trp Pro Leu Gly Thr Leu 
                560                 565                 570 

Gly Pro Glu Gly Ser Gly Ser Gly Ser Ser Ser His Glu Leu Phe 
                575                 580                 585 

Asn Glu Ala Asp Phe Ile Pro His His Leu Ala Pro Arg Pro Ser 
                590                 595                 600 

Pro Ala Ser Ser Pro Lys Pro Gly Thr Met Gly Asn Ala Ile Glu 
                605                 610                 615 

Glu Glu Ala Pro Glu Leu Asp Leu Pro Gly Pro Val Phe Val Asp 
                620                 625                 630 

Asp Phe Tyr Tyr Asp Tyr Asn Phe Ile Asn Phe His Glu Asp Leu 
                635                 640                 645 

Ser Tyr Gly Pro Ser Glu Glu Pro Asp Leu Asp Leu Ala Gly Thr 
                650                 655                 660 

Gly Asp Arg Thr Pro Pro Pro His Ser Arg Pro Ala Ala Pro Ser 
                665                 670                 675 

Thr Gly Ser Pro Val Pro Ala Thr Glu Pro Pro Ala Ala Lys Glu 
                680                 685                 690 

Glu Gly Val Leu Gly Pro Trp Ser Pro Ser Pro Trp Pro Ser Gln 
                695                 700                 705 

Ala Gly Arg Ser Pro Pro Pro Pro Ser Glu Gln Thr Pro Gly Asn 
                710                 715                 720 

Pro Leu Ile Asn Phe Leu Pro Glu Glu Asp Thr Pro Ile Gly Ala 
                725                 730                 735 

Pro Asp Leu Gly Leu Pro Ser Leu Ser Trp Pro Arg Val Ser Thr 
                740                 745                 750 

Asp Gly Leu Gln Thr Pro Ala Thr Pro Glu Ser Gln Asn Asp Phe 
                755                 760                 765 

Pro Val Gly Lys Asp Ser Gln Ser Gln Leu Pro Pro Pro Trp Arg 
                770                 775                 780 

Asp Arg Thr Asn Glu Val Phe Lys Asp Asp Glu Glu Pro Lys Gly 
                785                 790                 795 

Arg Gly Ala Pro His Leu Pro Pro Arg Pro Ser Ser Thr Leu Pro 
                800                 805                 810 

Pro Leu Ser Pro Val Gly Ser Thr His Ser Ser Pro Ser Pro Asp 
                815                 820                 825 

Val Ala Glu Leu Trp Thr Gly Gly Thr Val Ala Trp Glu Pro Ala 
                830                 835                 840 

Leu Glu Gly Gly Leu Gly Pro Val Asp Ser Glu Leu Trp Pro Thr 
                845                 850                 855 

Val Gly Val Ala Ser Leu Leu Pro Pro Pro Ile Ala Pro Leu Pro 
                860                 865                 870 

Glu Met Lys Val Arg Asp Ser Ser Leu Glu Pro Gly Thr Pro Ser 
                875                 880                 885 

Phe Pro Thr Pro Gly Pro Gly Ser Trp Asp Leu Gln Thr Val Ala 
                890                 895                 900 

Val Trp Gly Thr Phe Leu Pro Thr Thr Leu Thr Gly Leu Gly His 
                905                 910                 915 

Met Pro Glu Pro Ala Leu Asn Pro Gly Pro Lys Gly Gln Pro Glu 
                920                 925                 930 

Ser Leu Ser Pro Glu Val Pro Leu Ser Ser Arg Leu Leu Ser Thr 
                935                 940                 945 

Pro Ala Trp Asp Ser Pro Ala Asn Ser His Arg Val Pro Glu Thr 
                950                 955                 960 

Gln Pro Leu Ala Pro Ser Leu Ala Glu Ala Gly Pro Pro Ala Asp 
                965                 970                 975 

Pro Leu Val Val Arg Asn Ala Ser Trp Gln Ala Gly Asn Trp Ser 
                980                 985                 990 

Glu Cys Ser Thr Thr Cys Gly Leu Gly Ala Val Trp Arg Pro Val 
                995                1000                1005 

Arg Cys Ser Ser Gly Arg Asp Glu Asp Cys Ala Pro Ala Gly Arg 
               1010                1015                1020 

Pro Gln Pro Ala Arg Arg Cys His Leu Arg Pro Cys Ala Thr Trp 
               1025                1030                1035 

His Ser Gly Asn Trp Ser Lys Cys Ser Arg Ser Cys Gly Gly Gly 
               1040                1045                1050 

Ser Ser Val Arg Asp Val Gln Cys Val Asp Thr Arg Asp Leu Arg 
               1055                1060                1065 

Pro Leu Arg Pro Phe His Cys Gln Pro Gly Pro Ala Lys Pro Pro 
               1070                1075                1080 

Ala His Arg Pro Cys Gly Ala Gln Pro Cys Leu Ser Trp Tyr Thr 
               1085                1090                1095 

Ser Ser Trp Arg Glu Cys Ser Glu Ala Cys Gly Gly Gly Glu Gln 
               1100                1105                1110 

Gln Arg Leu Val Thr Cys Pro Glu Pro Gly Leu Cys Glu Glu Ala 
               1115                1120                1125 

Leu Arg Pro Asn Thr Thr Arg Pro Cys Asn Thr His Pro Cys Thr 
               1130                1135                1140 

Gln Trp Val Val Gly Pro Trp Gly Gln Cys Ser Ala Pro Cys Gly 
               1145                1150                1155 

Gly Gly Val Gln Arg Arg Leu Val Lys Cys Val Asn Thr Gln Thr 
               1160                1165                1170 

Gly Leu Pro Glu Glu Asp Ser Asp Gln Cys Gly His Glu Ala Trp 
               1175                1180                1185 

Pro Glu Ser Ser Arg Pro Cys Gly Thr Glu Asp Cys Glu Pro Val 
               1190                1195                1200 

Glu Pro Pro Arg Cys Glu Arg Asp Arg Leu Ser Phe Gly Phe Cys 
               1205                1210                1215 

Glu Thr Leu Arg Leu Leu Gly Arg Cys Gln Leu Pro Thr Ile Arg 
               1220                1225                1230 

Thr Gln Cys Cys Arg Ser Cys Ser Pro Pro Ser His Gly Ala Pro 
               1235                1240                1245 

Ser Arg Gly His Gln Arg Val Ala Arg Arg 
               1250                1255 

 
           
             24  
             911  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6755002CD1  
             
           
            24 

Met Ala Gln Leu Phe Leu Pro Leu Leu Ala Ala Leu Val Leu Ala 
  1               5                  10                  15 

Gln Ala Pro Ala Ala Leu Ala Asp Val Leu Glu Gly Asp Ser Ser 
                 20                  25                  30 

Glu Asp Arg Ala Phe Arg Val Arg Ile Ala Gly Asp Ala Pro Leu 
                 35                  40                  45 

Gln Gly Val Leu Gly Gly Ala Leu Thr Ile Pro Cys His Val His 
                 50                  55                  60 

Tyr Leu Arg Pro Pro Pro Ser Arg Arg Ala Val Leu Gly Ser Pro 
                 65                  70                  75 

Arg Val Lys Trp Thr Phe Leu Ser Arg Gly Arg Glu Ala Glu Val 
                 80                  85                  90 

Leu Val Ala Arg Gly Val Arg Val Lys Val Asn Glu Ala Tyr Arg 
                 95                 100                 105 

Phe Arg Val Ala Leu Pro Ala Tyr Pro Ala Ser Leu Thr Asp Val 
                110                 115                 120 

Ser Leu Ala Leu Ser Glu Leu Arg Pro Asn Asp Ser Gly Ile Tyr 
                125                 130                 135 

Arg Cys Glu Val Gln His Gly Ile Asp Asp Ser Ser Asp Ala Val 
                140                 145                 150 

Glu Val Lys Val Lys Gly Val Val Phe Leu Tyr Arg Glu Gly Ser 
                155                 160                 165 

Ala Arg Tyr Ala Phe Ser Phe Ser Gly Ala Gln Glu Ala Cys Ala 
                170                 175                 180 

Arg Ile Gly Ala His Ile Ala Thr Pro Glu Gln Leu Tyr Ala Ala 
                185                 190                 195 

Tyr Leu Gly Gly Tyr Glu Gln Cys Asp Ala Gly Trp Leu Ser Asp 
                200                 205                 210 

Gln Thr Val Arg Tyr Pro Ile Gln Thr Pro Arg Glu Ala Cys Tyr 
                215                 220                 225 

Gly Asp Met Asp Gly Phe Pro Gly Val Arg Asn Tyr Gly Val Val 
                230                 235                 240 

Asp Pro Asp Asp Leu Tyr Asp Val Tyr Cys Tyr Ala Glu Asp Leu 
                245                 250                 255 

Asn Gly Glu Leu Phe Leu Gly Asp Pro Pro Glu Lys Leu Thr Leu 
                260                 265                 270 

Glu Glu Ala Arg Ala Tyr Cys Gln Glu Arg Gly Ala Glu Ile Ala 
                275                 280                 285 

Thr Thr Gly Gln Leu Tyr Ala Ala Trp Asp Gly Gly Leu Asp His 
                290                 295                 300 

Cys Ser Pro Gly Trp Leu Ala Asp Gly Ser Val Arg Tyr Pro Ile 
                305                 310                 315 

Val Thr Pro Ser Gln Arg Cys Gly Gly Gly Leu Pro Gly Val Lys 
                320                 325                 330 

Thr Leu Phe Leu Phe Pro Asn Gln Thr Gly Phe Pro Asn Lys His 
                335                 340                 345 

Ser Arg Phe Asn Val Tyr Cys Phe Arg Asp Ser Ala Gln Pro Ser 
                350                 355                 360 

Ala Ile Pro Glu Ala Ser Asn Pro Ala Ser Asn Pro Ala Ser Asp 
                365                 370                 375 

Gly Leu Glu Ala Ile Val Thr Val Thr Glu Thr Leu Glu Glu Leu 
                380                 385                 390 

Gln Leu Pro Gln Glu Ala Thr Glu Ser Glu Ser Arg Gly Ala Ile 
                395                 400                 405 

Tyr Ser Ile Pro Ile Met Glu Asp Gly Gly Gly Gly Ser Ser Thr 
                410                 415                 420 

Pro Glu Asp Pro Ala Glu Ala Pro Arg Thr Leu Leu Glu Phe Glu 
                425                 430                 435 

Thr Gln Ser Met Val Pro Pro Thr Gly Phe Ser Glu Glu Glu Gly 
                440                 445                 450 

Lys Ala Leu Glu Glu Glu Glu Lys Tyr Glu Asp Glu Glu Glu Lys 
                455                 460                 465 

Glu Glu Glu Glu Glu Glu Glu Glu Val Glu Asp Glu Ala Leu Trp 
                470                 475                 480 

Ala Trp Pro Ser Glu Leu Ser Ser Pro Gly Pro Glu Ala Ser Leu 
                485                 490                 495 

Pro Thr Glu Pro Ala Ala Gln Glu Lys Ser Leu Ser Gln Ala Pro 
                500                 505                 510 

Ala Arg Ala Val Leu Gln Pro Gly Ala Ser Pro Leu Pro Asp Gly 
                515                 520                 525 

Glu Ser Glu Ala Ser Arg Pro Pro Arg Val His Gly Pro Pro Thr 
                530                 535                 540 

Glu Thr Leu Pro Thr Pro Arg Glu Arg Asn Leu Ala Ser Pro Ser 
                545                 550                 555 

Pro Ser Thr Leu Val Glu Ala Arg Glu Val Gly Glu Ala Thr Gly 
                560                 565                 570 

Gly Pro Glu Leu Ser Gly Val Pro Arg Gly Glu Ser Glu Glu Thr 
                575                 580                 585 

Gly Ser Ser Glu Gly Ala Pro Ser Leu Leu Pro Ala Thr Arg Ala 
                590                 595                 600 

Pro Glu Gly Thr Arg Glu Leu Glu Ala Pro Ser Glu Asp Asn Ser 
                605                 610                 615 

Gly Arg Thr Ala Pro Ala Gly Thr Ser Val Gln Ala Gln Pro Val 
                620                 625                 630 

Leu Pro Thr Asp Ser Ala Ser Arg Gly Gly Val Ala Val Val Pro 
                635                 640                 645 

Ala Ser Gly Asp Cys Val Pro Ser Pro Cys His Asn Gly Gly Thr 
                650                 655                 660 

Cys Leu Glu Glu Glu Glu Gly Val Arg Cys Leu Cys Leu Pro Gly 
                665                 670                 675 

Tyr Gly Gly Asp Leu Cys Asp Val Gly Leu Arg Phe Cys Asn Pro 
                680                 685                 690 

Gly Trp Asp Ala Phe Gln Gly Ala Cys Tyr Lys His Phe Ser Thr 
                695                 700                 705 

Arg Arg Ser Trp Glu Glu Ala Glu Thr Gln Cys Arg Met Tyr Gly 
                710                 715                 720 

Ala His Leu Ala Ser Ile Ser Thr Pro Glu Glu Gln Asp Phe Ile 
                725                 730                 735 

Asn Asn Arg Tyr Arg Glu Tyr Gln Trp Ile Gly Leu Asn Asp Arg 
                740                 745                 750 

Thr Ile Glu Gly Asp Phe Leu Trp Ser Asp Gly Val Pro Leu Leu 
                755                 760                 765 

Tyr Glu Asn Trp Asn Pro Gly Gln Pro Asp Ser Tyr Phe Leu Ser 
                770                 775                 780 

Gly Glu Asn Cys Val Val Met Val Trp His Asp Gln Gly Gln Trp 
                785                 790                 795 

Ser Asp Val Pro Cys Asn Tyr His Leu Ser Tyr Thr Cys Lys Met 
                800                 805                 810 

Gly Leu Val Ser Cys Gly Pro Pro Pro Glu Leu Pro Leu Ala Gln 
                815                 820                 825 

Val Phe Gly Arg Pro Arg Leu Arg Tyr Glu Val Asp Thr Val Leu 
                830                 835                 840 

Arg Tyr Arg Cys Arg Glu Gly Leu Ala Gln Arg Asn Leu Pro Leu 
                845                 850                 855 

Ile Arg Cys Gln Glu Asn Gly Arg Trp Glu Ala Pro Gln Ile Ser 
                860                 865                 870 

Cys Val Pro Arg Arg Pro Ala Arg Ala Leu His Pro Glu Glu Asp 
                875                 880                 885 

Pro Glu Gly Arg Gln Gly Arg Leu Leu Gly Arg Trp Lys Ala Leu 
                890                 895                 900 

Leu Ile Pro Pro Ser Ser Pro Met Pro Gly Pro 
                905                 910 

 
           
             25  
             467  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7350907CD1  
             
           
            25 

Met Pro Gly Arg Trp Arg Trp Gln Arg Asp Met His Pro Ala Arg 
  1               5                  10                  15 

Lys Leu Leu Ser Leu Leu Phe Leu Ile Leu Met Gly Thr Glu Leu 
                 20                  25                  30 

Thr Gln Val Leu Pro Thr Asn Pro Glu Glu Ser Trp Gln Val Tyr 
                 35                  40                  45 

Ser Ser Ala Gln Asp Ser Glu Gly Arg Cys Ile Cys Thr Val Val 
                 50                  55                  60 

Ala Pro Gln Gln Thr Met Cys Ser Arg Asp Ala Arg Thr Lys Gln 
                 65                  70                  75 

Leu Arg Gln Leu Leu Glu Lys Val Gln Asn Met Ser Gln Ser Ile 
                 80                  85                  90 

Glu Val Leu Asp Arg Arg Thr Gln Arg Asp Leu Gln Tyr Val Glu 
                 95                 100                 105 

Lys Met Glu Asn Gln Met Lys Gly Leu Glu Ser Lys Phe Lys Gln 
                110                 115                 120 

Val Glu Glu Ser His Lys Gln His Leu Ala Arg Gln Phe Lys Ala 
                125                 130                 135 

Ile Lys Ala Lys Met Asp Glu Leu Arg Pro Leu Ile Pro Val Leu 
                140                 145                 150 

Glu Glu Tyr Lys Ala Asp Ala Lys Leu Val Leu Gln Phe Lys Glu 
                155                 160                 165 

Glu Val Gln Asn Leu Thr Ser Val Leu Asn Glu Leu Gln Glu Glu 
                170                 175                 180 

Ile Gly Ala Tyr Asp Tyr Asp Glu Leu Gln Ser Arg Val Ser Asn 
                185                 190                 195 

Leu Glu Glu Arg Leu Arg Ala Cys Met Gln Lys Leu Ala Cys Gly 
                200                 205                 210 

Lys Leu Thr Gly Ile Ser Asp Pro Val Thr Val Lys Thr Ser Gly 
                215                 220                 225 

Ser Arg Phe Gly Ser Trp Met Thr Asp Pro Leu Ala Pro Glu Gly 
                230                 235                 240 

Asp Asn Arg Val Trp Tyr Met Asp Gly Tyr His Asn Asn Arg Phe 
                245                 250                 255 

Val Arg Glu Tyr Lys Ser Met Val Asp Phe Met Asn Thr Asp Asn 
                260                 265                 270 

Phe Thr Ser His Arg Leu Pro His Pro Trp Ser Gly Thr Gly Gln 
                275                 280                 285 

Val Val Tyr Asn Gly Ser Ile Tyr Phe Asn Lys Phe Gln Ser His 
                290                 295                 300 

Ile Ile Ile Arg Phe Asp Leu Lys Thr Glu Thr Ile Leu Lys Thr 
                305                 310                 315 

Arg Ser Leu Asp Tyr Ala Gly Tyr Asn Asn Met Tyr His Tyr Ala 
                320                 325                 330 

Trp Gly Gly His Ser Asp Ile Asp Leu Met Val Asp Glu Ser Gly 
                335                 340                 345 

Leu Trp Ala Val Tyr Ala Thr Asn Gln Asn Ala Gly Asn Ile Val 
                350                 355                 360 

Val Ser Arg Leu Asp Pro Val Ser Leu Gln Thr Leu Gln Thr Trp 
                365                 370                 375 

Asn Thr Ser Tyr Pro Lys Arg Ser Ala Gly Glu Ala Phe Ile Ile 
                380                 385                 390 

Cys Gly Thr Leu Tyr Val Thr Asn Gly Tyr Ser Gly Gly Thr Lys 
                395                 400                 405 

Val His Tyr Ala Tyr Gln Thr Asn Ala Ser Thr Tyr Glu Tyr Ile 
                410                 415                 420 

Asp Ile Pro Phe Gln Asn Lys Tyr Ser His Ile Ser Met Leu Asp 
                425                 430                 435 

Tyr Asn Pro Lys Asp Arg Ala Leu Tyr Ala Trp Asn Asn Gly His 
                440                 445                 450 

Gln Ile Leu Tyr Asn Val Thr Leu Phe His Val Ile Arg Ser Asp 
                455                 460                 465 

Glu Leu 

 
           
             26  
             1018  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474411CD1  
             
           
            26 

Met Val Ser His Phe Met Gly Ser Leu Ser Val Leu Cys Phe Leu 
  1               5                  10                  15 

Leu Leu Leu Gly Phe Gln Phe Val Cys Pro Gln Pro Ser Thr Gln 
                 20                  25                  30 

His Arg Lys Val Pro Gln Arg Met Ala Ala Glu Gly Ala Pro Glu 
                 35                  40                  45 

Asp Asp Gly Gly Gly Gly Ala Pro Gly Val Trp Gly Ala Trp Gly 
                 50                  55                  60 

Pro Trp Ser Ala Cys Ser Arg Ser Cys Ser Gly Gly Val Met Glu 
                 65                  70                  75 

Gln Thr Arg Pro Cys Leu Pro Arg Ser Tyr Arg Leu Arg Gly Gly 
                 80                  85                  90 

Gln Arg Pro Gly Ala Pro Ala Arg Ala Phe Ala Asp His Val Val 
                 95                 100                 105 

Ser Ala Val Arg Thr Ser Val Pro Leu His Arg Ser Arg Asp Glu 
                110                 115                 120 

Thr Pro Ala Leu Ala Gly Thr Asp Ala Ser Arg Gln Gly Pro Thr 
                125                 130                 135 

Val Leu Arg Gly Ser Arg His Pro Gln Pro Gln Gly Leu Glu Val 
                140                 145                 150 

Thr Gly Asp Arg Arg Ser Arg Thr Arg Gly Thr Ile Gly Pro Gly 
                155                 160                 165 

Lys Tyr Gly Tyr Gly Lys Ala Pro Tyr Ile Leu Pro Leu Gln Thr 
                170                 175                 180 

Asp Thr Ala His Thr Pro Gln Arg Leu Arg Arg Gln Lys Leu Ser 
                185                 190                 195 

Ser Arg His Ser Arg Ser Gln Gly Ala Ser Ser Ala Arg His Gly 
                200                 205                 210 

Tyr Ser Ser Pro Ala His Gln Val Pro Gln His Gly Pro Leu Tyr 
                215                 220                 225 

Gln Ser Asp Ser Gly Pro Arg Ser Gly Leu Gln Ala Ala Glu Ala 
                230                 235                 240 

Pro Ile Tyr Gln Leu Pro Leu Thr His Asp Gln Gly Tyr Pro Ala 
                245                 250                 255 

Ala Ser Ser Leu Phe His Ser Pro Glu Thr Ser Asn Asn His Gly 
                260                 265                 270 

Val Gly Thr His Gly Ala Thr Gln Ser Phe Ser Gln Pro Ala Arg 
                275                 280                 285 

Ser Thr Ala Ile Ser Cys Ile Gly Ala Tyr Arg Gln Tyr Lys Leu 
                290                 295                 300 

Cys Asn Thr Asn Val Cys Pro Glu Ser Ser Arg Ser Ile Arg Glu 
                305                 310                 315 

Val Gln Cys Ala Ser Tyr Asn Asn Lys Pro Phe Met Gly Arg Phe 
                320                 325                 330 

Tyr Glu Trp Glu Pro Phe Ala Glu Val Lys Gly Asn Arg Lys Cys 
                335                 340                 345 

Glu Leu Asn Cys Gln Ala Met Gly Tyr Arg Phe Tyr Val Arg Gln 
                350                 355                 360 

Ala Glu Lys Val Ile Asp Gly Thr Pro Cys Asp Gln Asn Gly Thr 
                365                 370                 375 

Ala Ile Cys Val Ser Gly Gln Cys Lys Ser Ile Gly Cys Asp Asp 
                380                 385                 390 

Tyr Leu Gly Ser Asp Lys Val Val Asp Lys Cys Gly Val Cys Gly 
                395                 400                 405 

Gly Asp Asn Thr Gly Cys Gln Val Val Ser Gly Val Phe Lys His 
                410                 415                 420 

Ala Leu Thr Ser Leu Gly Tyr His Arg Val Val Glu Ile Pro Glu 
                425                 430                 435 

Gly Ala Thr Lys Ile Asn Ile Thr Glu Met Tyr Lys Ser Asn Asn 
                440                 445                 450 

Tyr Leu Ala Leu Arg Ser Arg Ser Gly Arg Ser Ile Ile Asn Gly 
                455                 460                 465 

Asn Trp Ala Ile Asp Arg Pro Gly Lys Tyr Glu Gly Gly Gly Thr 
                470                 475                 480 

Met Phe Thr Tyr Lys Arg Pro Asn Glu Ile Ser Ser Thr Ala Gly 
                485                 490                 495 

Glu Ser Phe Leu Ala Glu Gly Pro Thr Asn Glu Ile Leu Asp Val 
                500                 505                 510 

Tyr Met Ile His Gln Gln Pro Asn Pro Gly Val His Tyr Glu Tyr 
                515                 520                 525 

Val Ile Met Gly Thr Asn Ala Ile Ser Pro Gln Val Pro Pro His 
                530                 535                 540 

Arg Arg Pro Gly Glu Pro Phe Asn Gly Gln Met Val Thr Glu Gly 
                545                 550                 555 

Arg Ser Gln Glu Glu Gly Glu Gln Lys Gly Arg Asn Glu Glu Lys 
                560                 565                 570 

Glu Asp Leu Arg Gly Glu Ala Pro Glu Met Phe Thr Ser Glu Ser 
                575                 580                 585 

Ala Gln Thr Phe Pro Val Arg His Pro Asp Arg Phe Ser Pro His 
                590                 595                 600 

Arg Pro Asp Asn Leu Val Pro Pro Ala Pro Gln Pro Pro Arg Arg 
                605                 610                 615 

Ser Arg Asp His Asn Trp Lys Gln Leu Gly Thr Thr Glu Cys Ser 
                620                 625                 630 

Thr Thr Cys Gly Lys Gly Ser Gln Tyr Pro Ile Phe Arg Cys Val 
                635                 640                 645 

His Arg Ser Thr His Glu Glu Ala Pro Glu Ser Tyr Cys Asp Ser 
                650                 655                 660 

Ser Met Lys Pro Thr Pro Glu Glu Glu Pro Cys Asn Ile Phe Pro 
                665                 670                 675 

Cys Pro Ala Phe Trp Asp Ile Gly Glu Trp Ser Glu Cys Ser Lys 
                680                 685                 690 

Thr Cys Gly Leu Gly Met Gln His Arg Gln Val Leu Cys Arg Gln 
                695                 700                 705 

Val Tyr Ala Asn Arg Ser Leu Thr Val Gln Pro Tyr Arg Cys Gln 
                710                 715                 720 

His Leu Glu Lys Pro Glu Thr Thr Ser Thr Cys Gln Leu Lys Ile 
                725                 730                 735 

Cys Ser Glu Trp Gln Ile Arg Thr Asp Trp Thr Ser Cys Ser Val 
                740                 745                 750 

Pro Cys Gly Val Gly Gln Arg Thr Arg Asp Val Lys Cys Val Ser 
                755                 760                 765 

Asn Ile Gly Asp Val Val Asp Asp Glu Glu Cys Asn Met Lys Leu 
                770                 775                 780 

Arg Pro Asn Asp Ile Glu Asn Cys Asp Met Gly Pro Cys Ala Lys 
                785                 790                 795 

Ser Trp Phe Leu Thr Glu Trp Ser Glu Arg Cys Ser Ala Glu Cys 
                800                 805                 810 

Gly Ala Gly Val Arg Thr Arg Ser Val Val Cys Met Thr Asn His 
                815                 820                 825 

Val Ser Ser Leu Pro Leu Glu Gly Cys Gly Asn Asn Arg Pro Ala 
                830                 835                 840 

Glu Ala Thr Pro Cys Asp Asn Gly Pro Cys Thr Gly Lys Val Glu 
                845                 850                 855 

Trp Phe Ala Gly Ser Trp Ser Gln Cys Ser Ile Glu Cys Gly Ser 
                860                 865                 870 

Gly Thr Gln Gln Arg Glu Val Ile Cys Val Arg Lys Asn Ala Asp 
                875                 880                 885 

Thr Phe Glu Val Leu Asp Pro Ser Glu Cys Ser Phe Leu Glu Lys 
                890                 895                 900 

Pro Pro Ser Gln Gln Ser Cys His Leu Lys Pro Cys Gly Ala Lys 
                905                 910                 915 

Trp Phe Ser Thr Glu Trp Ser Met Cys Ser Lys Ser Cys Gln Gly 
                920                 925                 930 

Gly Phe Arg Val Arg Glu Val Arg Cys Leu Ser Asp Asp Met Thr 
                935                 940                 945 

Leu Ser Asn Leu Cys Asp Pro Gln Leu Lys Pro Glu Glu Arg Glu 
                950                 955                 960 

Ser Cys Asn Pro Gln Asp Cys Val Pro Glu Val Asp Glu Asn Cys 
                965                 970                 975 

Lys Asp Lys Tyr Tyr Asn Cys Asn Val Val Val Gln Ala Arg Leu 
                980                 985                 990 

Cys Val Tyr Asn Tyr Tyr Lys Thr Ala Cys Cys Ala Ser Cys Thr 
                995                1000                1005 

Arg Val Ala Asn Arg Gln Thr Gly Phe Leu Gly Ser Arg 
               1010                1015 

 
           
             27  
             1458  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4755911CD1  
             
           
            27 

Met Gly Lys Glu Gln Glu Leu Val Gln Ala Val Lys Ala Glu Asp 
  1               5                  10                  15 

Val Gly Thr Ala Gln Arg Leu Leu Gln Arg Pro Arg Pro Gly Lys 
                 20                  25                  30 

Ala Thr Arg Ser Leu Pro Gly Gly Arg Arg Arg Trp Met Asp Gly 
                 35                  40                  45 

Arg Val Asp Gln Pro Arg Val Arg Leu Arg Thr Tyr Ser Arg Val 
                 50                  55                  60 

Ser Val Ser Gly His Leu Cys Gly His Gly Gln Gly Ser Ala Glu 
                 65                  70                  75 

Leu Leu Gly Ser Thr Lys Lys Ile Asn Val Asn Phe Gln Asp Pro 
                 80                  85                  90 

Asp Gly Val Gly Phe Gly Val Lys Gly Gln Leu Pro Ala Ser Pro 
                 95                 100                 105 

Arg Pro Pro Gly Met Arg Pro Leu His Tyr Ala Ala Trp Gln Gly 
                110                 115                 120 

Arg Lys Glu Pro Met Lys Leu Val Leu Lys Ala Gly Ser Ala Val 
                125                 130                 135 

Asn Ile Pro Ser Asp Glu Gly His Ile Pro Leu His Leu Ala Ala 
                140                 145                 150 

Gln His Gly His Tyr Asp Val Ser Glu Met Leu Leu Gln His Gln 
                155                 160                 165 

Ser Asn Pro Cys Met Val Asp Asn Ser Gly Lys Thr Pro Leu Asp 
                170                 175                 180 

Leu Ala Cys Glu Phe Gly Arg Val Gly Val Val Gln Leu Leu Leu 
                185                 190                 195 

Ser Ser Asn Met Cys Ala Ala Leu Leu Glu Pro Arg Pro Gly Asp 
                200                 205                 210 

Ala Thr Asp Pro Asn Gly Thr Ser Pro Leu His Leu Ala Ala Lys 
                215                 220                 225 

Asn Gly His Ile Asp Ile Ile Arg Leu Leu Leu Gln Ala Gly Ile 
                230                 235                 240 

Asp Ile Asn Arg Gln Thr Lys Ser Gly Thr Ala Leu His Glu Ala 
                245                 250                 255 

Ala Leu Cys Gly Lys Thr Glu Val Val Arg Leu Leu Leu Asp Ser 
                260                 265                 270 

Gly Ile Asn Ala His Val Arg Asn Thr Tyr Ser Gln Thr Ala Leu 
                275                 280                 285 

Asp Ile Val His Gln Phe Thr Thr Ser Gln Ala Ser Arg Glu Ile 
                290                 295                 300 

Lys Gln Leu Leu Arg Glu Ala Ser Ala Ala Leu Gln Val Arg Ala 
                305                 310                 315 

Thr Lys Asp Tyr Cys Asn Asn Tyr Asp Leu Thr Ser Leu Asn Val 
                320                 325                 330 

Lys Ala Gly Asp Ile Ile Thr Val Leu Glu Gln His Pro Asp Gly 
                335                 340                 345 

Arg Trp Lys Gly Cys Ile His Asp Asn Arg Thr Gly Asn Asp Arg 
                350                 355                 360 

Val Gly Tyr Phe Pro Ser Ser Leu Gly Glu Ala Ile Val Lys Arg 
                365                 370                 375 

Ala Gly Ser Arg Ala Gly Thr Glu Pro Ser Leu Pro Gln Gly Ser 
                380                 385                 390 

Ser Ser Ser Gly Pro Ser Ala Pro Pro Glu Glu Ile Trp Val Leu 
                395                 400                 405 

Arg Lys Pro Phe Ala Gly Gly Asp Arg Ser Gly Ser Ile Ser Gly 
                410                 415                 420 

Met Ala Gly Gly Arg Gly Ser Gly Gly His Ala Leu His Ala Gly 
                425                 430                 435 

Ser Glu Gly Val Lys Leu Leu Ala Thr Val Leu Ser Gln Lys Ser 
                440                 445                 450 

Val Ser Glu Ser Gly Pro Gly Asp Ser Pro Ala Lys Pro Pro Glu 
                455                 460                 465 

Gly Ser Ala Gly Val Ala Arg Ser Gln Pro Pro Val Ala His Ala 
                470                 475                 480 

Gly Gln Val Tyr Gly Glu Gln Pro Pro Lys Lys Leu Glu Pro Ala 
                485                 490                 495 

Ser Glu Gly Lys Ser Ser Glu Ala Val Ser Gln Trp Leu Thr Ala 
                500                 505                 510 

Phe Gln Leu Gln Leu Tyr Ala Pro Asn Phe Ile Ser Ala Gly Tyr 
                515                 520                 525 

Asp Leu Pro Thr Ile Ser Arg Met Thr Pro Glu Asp Leu Thr Ala 
                530                 535                 540 

Ile Gly Val Thr Lys Pro Gly His Arg Lys Lys Ile Ala Ala Glu 
                545                 550                 555 

Ile Ser Gly Leu Ser Ile Pro Asp Trp Leu Pro Glu His Lys Pro 
                560                 565                 570 

Ala Asn Leu Ala Val Trp Leu Ser Met Ile Gly Leu Ala Gln Tyr 
                575                 580                 585 

Tyr Lys Val Leu Val Asp Asn Gly Tyr Glu Asn Ile Asp Phe Ile 
                590                 595                 600 

Thr Asp Ile Thr Trp Glu Asp Leu Gln Glu Ile Gly Ile Thr Lys 
                605                 610                 615 

Leu Gly His Gln Lys Lys Leu Met Leu Ala Val Arg Lys Leu Ala 
                620                 625                 630 

Glu Leu Gln Lys Ala Glu Tyr Ala Lys Tyr Glu Gly Gly Pro Leu 
                635                 640                 645 

Arg Arg Lys Ala Pro Gln Ser Leu Glu Val Met Ala Ile Glu Ser 
                650                 655                 660 

Pro Pro Pro Pro Glu Pro Thr Pro Ala Asp Cys Gln Ser Pro Lys 
                665                 670                 675 

Met Thr Thr Phe Gln Asp Ser Glu Leu Ser Asp Glu Leu Gln Ala 
                680                 685                 690 

Ala Met Thr Gly Pro Ala Glu Val Gly Pro Thr Thr Glu Lys Pro 
                695                 700                 705 

Ser Ser His Leu Pro Pro Thr Pro Arg Ala Thr Thr Arg Gln Asp 
                710                 715                 720 

Ser Ser Leu Gly Gly Arg Ala Arg His Met Ser Ser Ser Gln Glu 
                725                 730                 735 

Leu Leu Gly Asp Gly Pro Pro Gly Pro Ser Ser Pro Met Ser Arg 
                740                 745                 750 

Ser Gln Glu Tyr Leu Leu Asp Glu Gly Pro Ala Pro Gly Thr Pro 
                755                 760                 765 

Pro Arg Glu Ala Arg Pro Gly Arg His Gly His Ser Ile Lys Arg 
                770                 775                 780 

Ala Ser Val Pro Pro Val Pro Gly Lys Pro Arg Gln Val Leu Pro 
                785                 790                 795 

Pro Gly Thr Ser His Phe Thr Pro Pro Gln Thr Pro Thr Lys Thr 
                800                 805                 810 

Arg Pro Gly Ser Pro Gln Ala Leu Gly Gly Pro His Gly Pro Ala 
                815                 820                 825 

Pro Ala Thr Ala Lys Val Lys Pro Thr Pro Gln Leu Leu Pro Pro 
                830                 835                 840 

Thr Glu Arg Pro Met Ser Pro Arg Ser Leu Pro Gln Ser Pro Thr 
                845                 850                 855 

His Arg Gly Phe Ala Tyr Val Leu Pro Gln Pro Val Glu Gly Glu 
                860                 865                 870 

Val Gly Pro Ala Ala Pro Gly Pro Ala Pro Pro Pro Val Pro Thr 
                875                 880                 885 

Ala Val Pro Thr Leu Cys Leu Pro Pro Glu Ala Asp Ala Glu Pro 
                890                 895                 900 

Gly Arg Pro Lys Lys Arg Ala His Ser Leu Asn Arg Tyr Ala Ala 
                905                 910                 915 

Ser Asp Ser Glu Pro Glu Arg Asp Glu Leu Leu Val Pro Ala Ala 
                920                 925                 930 

Ala Gly Pro Tyr Ala Thr Val Gln Arg Arg Val Gly Arg Ser His 
                935                 940                 945 

Ser Val Arg Ala Pro Ala Gly Ala Asp Lys Asn Val Asn Arg Ser 
                950                 955                 960 

Gln Ser Phe Ala Val Arg Pro Arg Lys Lys Gly Pro Pro Pro Pro 
                965                 970                 975 

Pro Pro Lys Arg Ser Ser Ser Ala Leu Ala Ser Ala Asn Leu Ala 
                980                 985                 990 

Asp Glu Pro Val Pro Asp Ala Glu Pro Glu Asp Gly Leu Leu Gly 
                995                1000                1005 

Val Arg Ala Gln Cys Arg Arg Ala Ser Asp Leu Ala Gly Ser Val 
               1010                1015                1020 

Asp Thr Gly Ser Ala Gly Ser Val Lys Ser Ile Ala Ala Met Leu 
               1025                1030                1035 

Glu Leu Ser Ser Ile Gly Gly Gly Gly Arg Ala Ala Arg Arg Pro 
               1040                1045                1050 

Pro Glu Gly His Pro Thr Pro Arg Pro Ala Ser Pro Glu Pro Gly 
               1055                1060                1065 

Arg Val Ala Thr Val Leu Ala Ser Val Lys His Lys Glu Ala Ile 
               1070                1075                1080 

Gly Pro Gly Gly Glu Val Val Asn Arg Arg Arg Thr Leu Ser Gly 
               1085                1090                1095 

Pro Val Thr Gly Leu Leu Ala Thr Ala Arg Arg Gly Pro Gly Glu 
               1100                1105                1110 

Ser Ala Asp Pro Gly Pro Phe Val Glu Asp Gly Thr Gly Arg Gln 
               1115                1120                1125 

Arg Pro Arg Gly Pro Ser Lys Gly Glu Ala Gly Val Glu Gly Pro 
               1130                1135                1140 

Pro Leu Ala Lys Val Glu Ala Ser Ala Thr Leu Lys Arg Arg Ile 
               1145                1150                1155 

Arg Ala Lys Gln Asn Gln Gln Glu Asn Val Lys Phe Ile Leu Thr 
               1160                1165                1170 

Glu Ser Asp Thr Val Lys Arg Arg Pro Lys Ala Lys Glu Arg Glu 
               1175                1180                1185 

Ala Gly Pro Glu Pro Pro Pro Pro Leu Ser Val Tyr His Asn Gly 
               1190                1195                1200 

Thr Gly Thr Val Arg Arg Arg Pro Ala Ser Glu Gln Ala Gly Pro 
               1205                1210                1215 

Pro Glu Leu Pro Pro Pro Pro Pro Pro Ala Glu Pro Pro Pro Thr 
               1220                1225                1230 

Asp Leu Ala His Leu Pro Pro Leu Pro Pro Pro Glu Gly Glu Ala 
               1235                1240                1245 

Arg Lys Pro Ala Lys Pro Pro Val Ser Pro Lys Pro Val Leu Thr 
               1250                1255                1260 

Gln Pro Val Pro Lys Leu Gln Gly Ser Pro Thr Pro Thr Ser Lys 
               1265                1270                1275 

Lys Val Pro Leu Pro Gly Pro Gly Ser Pro Glu Val Lys Arg Ala 
               1280                1285                1290 

His Gly Thr Pro Pro Pro Val Ser Pro Lys Pro Pro Pro Pro Pro 
               1295                1300                1305 

Thr Ala Pro Lys Pro Val Lys Ala Val Ala Gly Leu Pro Ser Gly 
               1310                1315                1320 

Ser Ala Gly Pro Ser Pro Ala Pro Ser Pro Ala Arg Gln Pro Pro 
               1325                1330                1335 

Ala Ala Leu Ala Lys Pro Pro Gly Thr Pro Pro Ser Leu Gly Ala 
               1340                1345                1350 

Ser Pro Ala Lys Pro Pro Ser Pro Gly Ala Pro Ala Leu His Val 
               1355                1360                1365 

Pro Ala Lys Pro Pro Arg Ala Ala Ala Ala Ala Ala Ala Ala Ala 
               1370                1375                1380 

Ala Ala Pro Pro Ala Pro Pro Glu Gly Ala Ser Pro Gly Asp Ser 
               1385                1390                1395 

Ala Arg Gln Lys Leu Glu Glu Thr Ser Ala Cys Leu Ala Ala Ala 
               1400                1405                1410 

Leu Gln Ala Val Glu Glu Lys Ile Arg Gln Glu Asp Ala Gln Gly 
               1415                1420                1425 

Pro Arg Asp Ser Ala Ala Glu Lys Ser Thr Gly Ser Ile Leu Asp 
               1430                1435                1440 

Asp Ile Gly Ser Met Phe Asp Asp Leu Ala Asp Gln Leu Asp Ala 
               1445                1450                1455 

Met Leu Glu 

 
           
             28  
             323  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 379766CD1  
             
           
            28 

Met Ala Ser Trp Thr Ser Pro Trp Trp Val Leu Ile Gly Met Val 
  1               5                  10                  15 

Phe Met His Ser Pro Leu Pro Gln Thr Thr Ala Glu Lys Ser Pro 
                 20                  25                  30 

Gly Ala Tyr Phe Leu Pro Glu Phe Ala Leu Ser Pro Gln Gly Ser 
                 35                  40                  45 

Phe Leu Glu Asp Thr Thr Gly Glu Gln Phe Leu Thr Tyr Arg Tyr 
                 50                  55                  60 

Asp Asp Gln Thr Ser Arg Asn Thr Arg Ser Asp Glu Asp Lys Asp 
                 65                  70                  75 

Gly Asn Trp Asp Ala Trp Gly Asp Trp Ser Asp Cys Ser Arg Thr 
                 80                  85                  90 

Cys Gly Gly Gly Ala Ser Tyr Ser Leu Arg Arg Cys Leu Thr Gly 
                 95                 100                 105 

Arg Asn Cys Glu Gly Gln Asn Ile Arg Tyr Lys Thr Cys Ser Asn 
                110                 115                 120 

His Asp Cys Pro Pro Asp Ala Glu Asp Phe Arg Ala Gln Gln Cys 
                125                 130                 135 

Ser Ala Tyr Asn Asp Val Gln Tyr Gln Gly Arg Tyr Tyr Glu Trp 
                140                 145                 150 

Leu Pro Arg Tyr Asn Asp Pro Ala Ala Pro Cys Ala Leu Lys Cys 
                155                 160                 165 

His Ala Gln Gly Gln Asn Leu Val Val Glu Leu Ala Pro Lys Val 
                170                 175                 180 

Leu Asp Gly Thr Arg Cys Asn Thr Asp Ser Leu Asp Met Cys Ile 
                185                 190                 195 

Ser Gly Ile Cys Gln Ala Val Gly Cys Asp Arg Gln Leu Gly Ser 
                200                 205                 210 

Asn Ala Lys Glu Asp Asn Cys Gly Val Cys Ala Gly Asp Gly Ser 
                215                 220                 225 

Thr Cys Arg Leu Val Arg Gly Gln Ser Lys Ser His Val Ser Pro 
                230                 235                 240 

Glu Lys Arg Glu Glu Asn Val Ile Ala Val Pro Leu Gly Ser Arg 
                245                 250                 255 

Ser Val Arg Ile Thr Val Lys Gly Pro Ala Tyr Pro Val Ala Trp 
                260                 265                 270 

Ala Leu Ala Ile Ser Ser Asn Thr Asn Cys Leu Val Leu Leu Cys 
                275                 280                 285 

Lys Ala Asn Leu Ala Ser Ser Gly Pro Tyr Phe Ala Leu Ile Pro 
                290                 295                 300 

Val Asn Pro Thr Thr Met Ala Leu Asn Thr Ala Ile Val Ser Gln 
                305                 310                 315 

Ser Ala Val Leu Ile Asp Cys Leu 
                320 

 
           
             29  
             234  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 553744CD1  
             
           
            29 

Met Met Ile His Ser Cys Leu Phe Ser Pro Phe His Ile Ala Phe 
  1               5                  10                  15 

Ser Thr Pro Ala Ser Gln Leu Phe Ser Pro His Gly Ser Asn Pro 
                 20                  25                  30 

Ser Thr Pro Ala Ala Thr Pro Val Pro Thr Ala Ser Pro Val Lys 
                 35                  40                  45 

Ala Ile Asn His Pro Ser Ala Ser Ala Ala Ala Thr Val Ser Gly 
                 50                  55                  60 

Met Asn Leu Leu Asn Thr Val Leu Pro Val Phe Pro Gly Gln Val 
                 65                  70                  75 

Ser Ser Ala Val His Thr Pro Gln Pro Ser Ile Pro Asn Pro Thr 
                 80                  85                  90 

Val Ile Arg Thr Pro Ser Leu Pro Thr Ala Pro Val Thr Ser Ile 
                 95                 100                 105 

His Ser Thr Thr Thr Thr Pro Val Pro Ser Ile Phe Ser Gly Leu 
                110                 115                 120 

Val Ser Leu Pro Gly Pro Ser Ala Thr Pro Thr Ala Ala Thr Pro 
                125                 130                 135 

Thr Pro Gly Pro Thr Pro Arg Ser Thr Leu Gly Ser Ser Glu Ala 
                140                 145                 150 

Phe Ala Ser Thr Ser Ala Pro Phe Thr Ser Leu Pro Phe Ser Thr 
                155                 160                 165 

Ser Ser Ser Ala Ala Ser Thr Ser Asn Pro Asn Ser Ala Ser Leu 
                170                 175                 180 

Ser Ser Val Phe Ala Gly Leu Pro Leu Pro Leu Pro Pro Thr Ser 
                185                 190                 195 

Gln Gly Leu Ser Asn Pro Thr Pro Val Ile Ala Gly Gly Ser Thr 
                200                 205                 210 

Pro Ser Val Ala Gly Pro Leu Gly Val Asn Ser Pro Ser Phe Val 
                215                 220                 225 

Cys Val Lys Arg Phe Ser Asp Ile Gln 
                230 

 
           
             30  
             377  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1825473CD1  
             
           
            30 

Met Lys Thr Leu Pro Leu Phe Val Cys Ile Cys Ala Leu Ser Ala 
  1               5                  10                  15 

Cys Phe Ser Phe Ser Glu Gly Arg Glu Arg Asp His Glu Leu Arg 
                 20                  25                  30 

His Arg Arg His His His Gln Ser Pro Lys Ser His Phe Glu Leu 
                 35                  40                  45 

Pro His Tyr Pro Gly Leu Leu Ala His Gln Lys Pro Phe Ile Arg 
                 50                  55                  60 

Lys Ser Tyr Lys Cys Leu His Lys Arg Cys Arg Pro Lys Leu Pro 
                 65                  70                  75 

Pro Ser Pro Asn Asn Pro Pro Lys Phe Pro Asn Pro His Gln Pro 
                 80                  85                  90 

Pro Lys His Pro Asp Lys Asn Ser Ser Val Val Asn Pro Thr Leu 
                 95                 100                 105 

Val Ala Thr Thr Gln Ile Pro Ser Val Thr Phe Pro Ser Ala Ser 
                110                 115                 120 

Thr Lys Ile Thr Thr Leu Pro Asn Val Thr Phe Leu Pro Gln Asn 
                125                 130                 135 

Ala Thr Thr Ile Ser Ser Arg Glu Asn Val Asn Thr Ser Ser Ser 
                140                 145                 150 

Val Ala Thr Leu Ala Pro Val Asn Ser Pro Ala Pro Gln Asp Thr 
                155                 160                 165 

Thr Ala Ala Pro Pro Thr Pro Ser Ala Thr Thr Pro Ala Pro Pro 
                170                 175                 180 

Ser Ser Ser Ala Pro Pro Glu Thr Thr Ala Ala Pro Pro Thr Pro 
                185                 190                 195 

Ser Ala Thr Thr Gln Ala Pro Pro Ser Ser Ser Ala Pro Pro Glu 
                200                 205                 210 

Thr Thr Ala Ala Pro Pro Thr Pro Pro Ala Thr Thr Pro Ala Pro 
                215                 220                 225 

Pro Ser Ser Ser Ala Pro Pro Glu Thr Thr Ala Ala Pro Pro Thr 
                230                 235                 240 

Pro Ser Ala Thr Thr Pro Ala Pro Leu Ser Ser Ser Ala Pro Pro 
                245                 250                 255 

Glu Thr Thr Ala Val Pro Pro Thr Pro Ser Ala Thr Thr Leu Asp 
                260                 265                 270 

Pro Ser Ser Ala Ser Ala Pro Pro Glu Thr Thr Ala Ala Pro Pro 
                275                 280                 285 

Thr Pro Ser Ala Thr Thr Pro Ala Pro Pro Ser Ser Pro Ala Pro 
                290                 295                 300 

Gln Glu Thr Thr Ala Ala Pro Ile Thr Thr Pro Asn Ser Ser Pro 
                305                 310                 315 

Thr Thr Leu Ala Pro Asp Thr Ser Glu Thr Ser Ala Ala Pro Thr 
                320                 325                 330 

His Gln Thr Thr Thr Ser Val Thr Thr Gln Thr Thr Thr Thr Lys 
                335                 340                 345 

Gln Pro Thr Ser Ala Pro Gly Gln Asn Lys Ile Ser Arg Phe Leu 
                350                 355                 360 

Leu Tyr Met Lys Asn Leu Leu Asn Arg Ile Ile Asp Asp Met Val 
                365                 370                 375 

Glu Gln 

 
           
             31  
             833  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7950094CD1  
             
           
            31 

Met Ala Pro His Trp Ala Val Trp Leu Leu Ala Ala Arg Leu Trp 
  1               5                  10                  15 

Gly Leu Gly Ile Gly Ala Glu Val Trp Trp Asn Leu Val Pro Arg 
                 20                  25                  30 

Lys Thr Val Ser Ser Gly Glu Leu Ala Thr Val Val Arg Arg Phe 
                 35                  40                  45 

Ser Gln Thr Gly Ile Gln Asp Phe Leu Thr Leu Thr Leu Thr Glu 
                 50                  55                  60 

Pro Thr Gly Leu Leu Tyr Val Gly Ala Arg Glu Ala Leu Phe Ala 
                 65                  70                  75 

Phe Ser Met Glu Ala Leu Glu Leu Gln Gly Ala Ile Ser Trp Glu 
                 80                  85                  90 

Ala Pro Val Glu Lys Lys Thr Glu Cys Ile Gln Lys Gly Lys Asn 
                 95                 100                 105 

Asn Gln Thr Glu Cys Phe Asn Phe Ile Arg Phe Leu Gln Pro Tyr 
                110                 115                 120 

Asn Ala Ser His Leu Tyr Val Cys Gly Thr Tyr Ala Phe Gln Pro 
                125                 130                 135 

Lys Cys Thr Tyr Val Asn Met Leu Thr Phe Thr Leu Glu His Gly 
                140                 145                 150 

Glu Phe Glu Asp Gly Lys Gly Lys Cys Pro Tyr Asp Pro Ala Lys 
                155                 160                 165 

Gly His Ala Gly Leu Leu Val Asp Gly Glu Leu Tyr Ser Ala Thr 
                170                 175                 180 

Leu Asn Asn Phe Leu Gly Thr Glu Pro Ile Ile Leu Arg Asn Met 
                185                 190                 195 

Gly Pro His His Ser Met Lys Thr Glu Tyr Leu Ala Phe Trp Leu 
                200                 205                 210 

Asn Glu Pro His Phe Val Gly Ser Ala Tyr Val Pro Glu Ser Val 
                215                 220                 225 

Gly Ser Phe Thr Gly Asp Asp Asp Lys Val Tyr Phe Phe Phe Arg 
                230                 235                 240 

Glu Arg Ala Val Glu Ser Asp Cys Tyr Ala Glu Gln Val Val Ala 
                245                 250                 255 

Arg Val Ala Arg Val Cys Lys Gly Asp Met Gly Gly Ala Arg Thr 
                260                 265                 270 

Leu Gln Arg Lys Trp Thr Thr Phe Leu Lys Ala Arg Leu Ala Cys 
                275                 280                 285 

Ser Ala Pro Asn Trp Gln Leu Tyr Phe Asn Gln Leu Gln Ala Met 
                290                 295                 300 

His Thr Leu Gln Asp Thr Ser Trp His Asn Thr Thr Phe Phe Gly 
                305                 310                 315 

Val Phe Gln Ala Gln Trp Gly Asp Met Tyr Leu Ser Ala Ile Cys 
                320                 325                 330 

Glu Tyr Gln Leu Glu Glu Ile Gln Arg Val Phe Glu Gly Pro Tyr 
                335                 340                 345 

Lys Glu Tyr His Glu Glu Ala Gln Lys Trp Asp Arg Tyr Thr Asp 
                350                 355                 360 

Pro Val Pro Ser Pro Arg Pro Gly Ser Cys Ile Asn Asn Trp His 
                365                 370                 375 

Arg Arg His Gly Tyr Thr Ser Ser Leu Glu Leu Pro Asp Asn Ile 
                380                 385                 390 

Leu Asn Phe Val Lys Lys His Pro Leu Met Glu Glu Gln Val Gly 
                395                 400                 405 

Pro Arg Trp Ser Arg Pro Leu Leu Val Lys Lys Gly Thr Asn Phe 
                410                 415                 420 

Thr His Leu Val Ala Asp Arg Val Thr Gly Leu Asp Gly Ala Thr 
                425                 430                 435 

Tyr Thr Val Leu Phe Ile Gly Thr Gly Asp Gly Trp Leu Leu Lys 
                440                 445                 450 

Ala Val Ser Leu Gly Pro Trp Val His Leu Ile Glu Glu Leu Gln 
                455                 460                 465 

Leu Phe Asp Gln Glu Pro Met Arg Ser Leu Val Leu Ser Gln Ser 
                470                 475                 480 

Lys Lys Leu Leu Phe Ala Gly Ser Arg Ser Gln Leu Val Gln Leu 
                485                 490                 495 

Pro Val Ala Asp Cys Met Lys Tyr Arg Ser Cys Ala Asp Cys Val 
                500                 505                 510 

Leu Ala Arg Asp Pro Tyr Cys Ala Trp Ser Val Asn Thr Ser Arg 
                515                 520                 525 

Cys Val Ala Val Gly Gly His Ser Gly Ser Leu Leu Ile Gln His 
                530                 535                 540 

Val Met Thr Ser Asp Thr Ser Gly Ile Cys Asn Leu Arg Gly Ser 
                545                 550                 555 

Lys Lys Val Arg Pro Thr Pro Lys Asn Ile Thr Val Val Ala Gly 
                560                 565                 570 

Thr Asp Leu Val Leu Pro Cys His Leu Ser Ser Asn Leu Ala His 
                575                 580                 585 

Ala Arg Trp Thr Phe Gly Gly Arg Asp Leu Pro Ala Glu Gln Pro 
                590                 595                 600 

Gly Ser Phe Leu Tyr Asp Ala Arg Leu Gln Ala Leu Val Val Met 
                605                 610                 615 

Ala Ala Gln Pro Arg His Ala Gly Ala Tyr His Cys Phe Ser Glu 
                620                 625                 630 

Glu Gln Gly Ala Arg Leu Ala Ala Glu Gly Tyr Leu Val Ala Val 
                635                 640                 645 

Val Ala Gly Pro Ser Val Thr Leu Glu Ala Arg Ala Pro Leu Glu 
                650                 655                 660 

Asn Leu Gly Leu Val Trp Leu Ala Val Val Ala Leu Gly Ala Val 
                665                 670                 675 

Cys Leu Val Leu Leu Leu Leu Val Leu Ser Leu Arg Arg Arg Leu 
                680                 685                 690 

Arg Glu Glu Leu Glu Lys Gly Ala Lys Ala Thr Glu Arg Thr Leu 
                695                 700                 705 

Val Tyr Pro Leu Glu Leu Pro Lys Glu Pro Thr Ser Pro Pro Phe 
                710                 715                 720 

Arg Pro Cys Pro Glu Pro Asp Glu Lys Leu Trp Asp Pro Val Gly 
                725                 730                 735 

Tyr Tyr Tyr Ser Asp Gly Ser Leu Lys Ile Val Pro Gly His Ala 
                740                 745                 750 

Arg Cys Gln Pro Gly Gly Gly Pro Pro Ser Pro Pro Pro Gly Ile 
                755                 760                 765 

Pro Gly Gln Pro Leu Pro Ser Pro Thr Arg Leu His Leu Gly Gly 
                770                 775                 780 

Gly Arg Asn Ser Asn Ala Asn Gly Tyr Val Arg Leu Gln Leu Gly 
                785                 790                 795 

Gly Glu Asp Arg Gly Gly Leu Gly His Pro Leu Pro Glu Leu Ala 
                800                 805                 810 

Asp Glu Leu Arg Arg Lys Leu Gln Gln Arg Gln Pro Leu Pro Asp 
                815                 820                 825 

Ser Asn Pro Glu Glu Ser Ser Val 
                830 

 
           
             32  
             1291  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7479484CD1  
             
           
            32 

Met Phe Arg Pro Thr Thr Val Ala Val Asp Glu Asp Gly Gly Glu 
  1               5                  10                  15 

Glu Asp Lys Asp Glu Ser Ser Thr Asn Ser Gly Ala Ser Ala Val 
                 20                  25                  30 

Ser Ser Cys Gly Phe Gly Ala Asp Phe Ser Thr Asp Lys Gly Gly 
                 35                  40                  45 

Ser Phe Thr Ser Val Gln Ile Thr Asn Thr Thr Gly Leu Ser Gln 
                 50                  55                  60 

Ala Pro Gly Leu Ala Ser Gln Gly Ile Ser Phe Gly Ile Lys Asn 
                 65                  70                  75 

Asn Leu Gly Pro Pro Leu Gln Lys Leu Gly Val Ser Phe Ser Phe 
                 80                  85                  90 

Ala Lys Lys Ala Pro Val Lys Leu Glu Ser Ile Ala Ser Val Phe 
                 95                 100                 105 

Lys Asp His Ala Glu Glu Gly Ser Ser Glu Asp Gly Thr Lys Ala 
                110                 115                 120 

Asp Glu Lys Ser Ser Asp Gln Gly Val Gln Lys Val Gly Asp Thr 
                125                 130                 135 

Asp Gly Thr Gly Asn Leu Asp Gly Lys Lys Glu Asp Glu Asp Pro 
                140                 145                 150 

Gln Asp Gly Gly Ser Leu Ala Ser Thr Leu Ser Lys Leu Lys Arg 
                155                 160                 165 

Met Lys Arg Glu Glu Gly Thr Gly Ala Thr Glu Pro Glu Tyr Tyr 
                170                 175                 180 

His Tyr Ile Pro Pro Ala His Cys Lys Val Lys Pro Asn Phe Pro 
                185                 190                 195 

Phe Leu Leu Phe Met Arg Ala Ser Glu Gln Met Glu Gly Asp His 
                200                 205                 210 

Ser Ala His Ser Lys Ser Ala Pro Glu Asn Arg Lys Ser Ser Ser 
                215                 220                 225 

Pro Lys Pro Gln Gly Cys Ser Lys Thr Ala Ala Ser Pro Gly Ala 
                230                 235                 240 

Glu Arg Thr Val Ser Glu Ala Ser Glu Leu Gln Lys Glu Ala Ala 
                245                 250                 255 

Val Ala Gly Pro Ser Glu Pro Gly Gly Lys Thr Glu Thr Lys Lys 
                260                 265                 270 

Gly Ser Gly Gly Gly Glu Asp Glu Gln Ser Val Glu Ser Arg Glu 
                275                 280                 285 

Thr Ser Glu Ser Pro Met Cys Glu Ser Asn Pro Lys Asp Ile Ser 
                290                 295                 300 

Gln Ala Thr Pro Ala Thr Lys Ala Gly Gln Gly Pro Lys His Pro 
                305                 310                 315 

Thr Gly Pro Phe Phe Pro Val Leu Ser Lys Asp Glu Ser Thr Ala 
                320                 325                 330 

Leu Gln Trp Pro Ser Glu Leu Leu Ile Phe Thr Lys Ala Glu Pro 
                335                 340                 345 

Ser Ile Ser Tyr Ser Cys Asn Pro Leu Tyr Phe Asp Phe Lys Leu 
                350                 355                 360 

Ser Arg Asn Lys Asp Ala Lys Ala Lys Gly Thr Glu Lys Pro Lys 
                365                 370                 375 

Asp Val Ala Gly Ser Ser Lys Asp His Leu Gln Ser Leu Asp Pro 
                380                 385                 390 

Arg Glu Pro Asn Lys Ser Gln Glu Glu Glu Gln Asp Val Val Leu 
                395                 400                 405 

Ser Ser Glu Gly Arg Val Asp Glu Pro Ala Ser Gly Ala Ala Cys 
                410                 415                 420 

Ser Ser Leu Asn Lys Gln Glu Pro Gly Gly Ser His Met Ser Glu 
                425                 430                 435 

Thr Glu Asp Thr Gly Arg Ser His Pro Ser Lys Lys Glu Pro Ser 
                440                 445                 450 

Gly Lys Ser His Arg His Lys Lys Lys Lys Lys His Lys Lys Ser 
                455                 460                 465 

Ser Lys His Lys Arg Lys His Lys Ala Asp Thr Glu Glu Lys Ser 
                470                 475                 480 

Ser Lys Ala Glu Ser Gly Glu Lys Ser Lys Lys Arg Lys Lys Arg 
                485                 490                 495 

Lys Arg Lys Lys Asn Lys Ser Ser Ala Ala Ala Asp Ser Glu Arg 
                500                 505                 510 

Gly Pro Lys Ser Glu Pro Pro Gly Ser Gly Ser Pro Ala Pro Pro 
                515                 520                 525 

Arg Arg Arg Arg Arg Ala Gln Asp Asp Ser Gln Arg Arg Ser Leu 
                530                 535                 540 

Pro Ala Glu Glu Gly Asn Ser Gly Lys Lys Asp Asp Gly Gly Gly 
                545                 550                 555 

Gly Ser Ser Cys Gln Asp His Ser Gly Arg Lys His Lys Gly Glu 
                560                 565                 570 

Pro Pro Thr Ser Ser Cys Gln Arg Arg Ala Asn Thr Lys His Ser 
                575                 580                 585 

Ser Arg Ser Ser His Arg Ser Gln Pro Ser Ser Gly Asp Glu Asp 
                590                 595                 600 

Ser Asp Asp Ala Ser Ser His Arg Leu His Gln Lys Ser Pro Ser 
                605                 610                 615 

Gln Tyr Ser Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu 
                620                 625                 630 

Glu Asp Glu Asp Ser Gly Ser Glu His Ser Arg Ser Arg Ser Arg 
                635                 640                 645 

Ser Gly His Arg His Ser Ser His Arg Ser Ser Arg Arg Ser Tyr 
                650                 655                 660 

Ser Ser Ser Ser Asp Ala Ser Ser Asp Gln Ser Cys Tyr Ser Arg 
                665                 670                 675 

Gln His Ser Tyr Ser Asp Asp Ser Tyr Ser Asp Tyr Ser Asp Arg 
                680                 685                 690 

Ser Arg Arg His Ser Lys Arg Ser His Asp Ser Asp Asp Ser Asp 
                695                 700                 705 

Tyr Thr Ser Ser Lys His Arg Ser Lys Arg His Lys Tyr Ser Ser 
                710                 715                 720 

Ser Asp Asp Asp Tyr Ser Leu Ser Cys Ser Gln Ser Arg Ser Arg 
                725                 730                 735 

Ser Arg Ser His Thr Arg Glu Arg Ser Arg Ser Arg Gly Arg Ser 
                740                 745                 750 

Arg Ser Ser Ser Cys Ser Arg Ser Arg Ser Lys Arg Arg Ser Arg 
                755                 760                 765 

Ser Thr Thr Ala His Ser Trp Gln Arg Ser Arg Ser Tyr Ser Arg 
                770                 775                 780 

Asp Arg Ser Arg Ser Thr Arg Ser Pro Ser Gln Arg Ser Gly Ser 
                785                 790                 795 

Arg Lys Gly Ser Trp Gly His Glu Ser Pro Glu Glu Arg Arg Ser 
                800                 805                 810 

Gly Arg Arg Asp Phe Ile Arg Ser Lys Ile Tyr Arg Ser Gln Ser 
                815                 820                 825 

Pro His Tyr Phe Gln Ser Gly Arg Gly Glu Gly Pro Gly Lys Lys 
                830                 835                 840 

Glu Asp Gly Arg Gly Asp Asp Ser Lys Gly Ala Gly Leu Pro Ser 
                845                 850                 855 

Gln Asn Ser Asn Thr Gly Thr Gly Arg Gly Ser Glu Ser Asp Cys 
                860                 865                 870 

Ser Pro Glu Asp Lys Asn Ser Val Thr Ala Arg Leu Leu Leu Glu 
                875                 880                 885 

Lys Ile Gln Ser Arg Lys Val Glu Arg Lys Pro Asn Val Cys Glu 
                890                 895                 900 

Glu Val Leu Ala Thr Pro Asn Lys Ala Gly Leu Lys Tyr Lys Asn 
                905                 910                 915 

Pro Pro Gln Gly Tyr Phe Gly Pro Lys Leu Pro Pro Ser Leu Gly 
                920                 925                 930 

Asn Lys Pro Val Leu Pro Met Ile Gly Lys Leu Pro Ala Thr Arg 
                935                 940                 945 

Lys Ser Asn Lys Lys Cys Glu Glu Ser Gly Leu Glu Arg Gly Glu 
                950                 955                 960 

Glu Gln Glu His Ser Glu Pro Glu Glu Gly Ser Pro Arg Ser Ser 
                965                 970                 975 

Asp Ala Pro Phe Gly His Gln Phe Ser Glu Glu Ala Ala Gly Pro 
                980                 985                 990 

Leu Ser Asp Pro Pro Pro Glu Glu Pro Lys Ser Glu Glu Ala Thr 
                995                1000                1005 

Ala Asp His Ser Val Ala Pro Leu Gly Thr Pro Ala His Thr Asp 
               1010                1015                1020 

Cys Tyr Pro Gly Asp Pro Ala Ile Ser His Asn Tyr Leu Pro Asp 
               1025                1030                1035 

Pro Ser Asp Gly Asp Thr Leu Glu Ser Leu Asp Ser Gly Ser Gln 
               1040                1045                1050 

Pro Gly Pro Val Glu Ser Ser Leu Leu Pro Ile Ala Pro Asp Leu 
               1055                1060                1065 

Glu His Phe Pro Asn Tyr Ala Pro Pro Ser Gly Glu Pro Ser Ile 
               1070                1075                1080 

Glu Ser Thr Asp Gly Thr Glu Asp Ala Ser Leu Ala Pro Leu Glu 
               1085                1090                1095 

Ser Gln Pro Ile Thr Phe Thr Pro Glu Glu Met Glu Lys Tyr Ser 
               1100                1105                1110 

Lys Leu Gln Gln Ala Ala Gln Gln His Ile Gln Gln Gln Leu Leu 
               1115                1120                1125 

Ala Lys Gln Val Lys Ala Phe Pro Ala Ser Thr Ala Leu Ala Pro 
               1130                1135                1140 

Ala Thr Pro Ala Leu Gln Pro Ile His Ile Gln Gln Pro Ala Thr 
               1145                1150                1155 

Ala Ser Ala Thr Ser Ile Thr Thr Val Gln His Ala Ile Leu Gln 
               1160                1165                1170 

His His Ala Ala Ala Ala Ala Ala Ala Ile Gly Ile His Pro His 
               1175                1180                1185 

Pro His Pro Gln Pro Leu Ala Gln Val His His Ile Pro Gln Pro 
               1190                1195                1200 

His Leu Thr Pro Ile Ser Leu Ser His Leu Thr His Ser Ile Ile 
               1205                1210                1215 

Pro Gly His Pro Ala Thr Phe Leu Ala Ser His Pro Ile His Ile 
               1220                1225                1230 

Ile Pro Ala Ser Ala Ile His Pro Gly Pro Phe Thr Phe His Pro 
               1235                1240                1245 

Val Pro His Ala Ala Leu Tyr Pro Thr Leu Leu Ala Pro Arg Pro 
               1250                1255                1260 

Ala Ala Ala Ala Ala Thr Ala Leu His Leu His Pro Leu Leu His 
               1265                1270                1275 

Pro Ile Phe Ser Gly Gln Asp Leu Gln His Pro Pro Ser His Gly 
               1280                1285                1290 

Thr 

 
           
             33  
             736  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6780147CD1  
             
           
            33 

Met Ala Val Arg Ala Leu Lys Leu Leu Thr Thr Leu Leu Ala Val 
  1               5                  10                  15 

Val Ala Ala Ala Ser Gln Ala Glu Val Glu Ser Glu Ala Gly Trp 
                 20                  25                  30 

Gly Met Val Thr Pro Asp Leu Leu Phe Ala Glu Gly Thr Ala Ala 
                 35                  40                  45 

Tyr Ala Arg Gly Asp Trp Pro Gly Val Val Leu Ser Met Glu Arg 
                 50                  55                  60 

Ala Leu Arg Ser Arg Ala Ala Leu Arg Ala Leu Arg Leu Arg Cys 
                 65                  70                  75 

Arg Thr Gln Cys Ala Ala Asp Phe Pro Trp Glu Leu Asp Pro Asp 
                 80                  85                  90 

Trp Ser Pro Ser Pro Ala Gln Ala Ser Gly Ala Ala Ala Leu Arg 
                 95                 100                 105 

Asp Leu Ser Phe Phe Gly Gly Leu Leu Arg Arg Ala Ala Cys Leu 
                110                 115                 120 

Arg Arg Cys Leu Gly Pro Pro Ala Ala His Ser Leu Ser Glu Glu 
                125                 130                 135 

Met Glu Leu Glu Phe Arg Lys Arg Ser Pro Tyr Asn Tyr Leu Gln 
                140                 145                 150 

Val Ala Tyr Phe Lys Ile Asn Lys Leu Glu Lys Ala Val Ala Ala 
                155                 160                 165 

Ala His Thr Phe Phe Val Gly Asn Pro Glu His Met Glu Met Gln 
                170                 175                 180 

Gln Asn Leu Asp Tyr Tyr Gln Thr Met Ser Gly Val Lys Glu Ala 
                185                 190                 195 

Asp Phe Lys Asp Leu Glu Thr Gln Pro His Met Gln Glu Phe Arg 
                200                 205                 210 

Leu Gly Val Arg Leu Tyr Ser Glu Glu Gln Pro Gln Glu Ala Val 
                215                 220                 225 

Pro His Leu Glu Ala Ala Leu Gln Glu Tyr Phe Val Ala Tyr Glu 
                230                 235                 240 

Glu Cys Arg Ala Leu Cys Glu Gly Pro Tyr Asp Tyr Asp Gly Tyr 
                245                 250                 255 

Asn Tyr Leu Glu Tyr Asn Ala Asp Leu Phe Gln Ala Ile Thr Asp 
                260                 265                 270 

His Tyr Ile Gln Val Leu Asn Cys Lys Gln Asn Cys Val Thr Glu 
                275                 280                 285 

Leu Ala Ser His Pro Ser Arg Glu Lys Pro Phe Glu Asp Phe Leu 
                290                 295                 300 

Pro Ser His Tyr Asn Tyr Leu Gln Phe Ala Tyr Tyr Asn Ile Gly 
                305                 310                 315 

Asn Tyr Thr Gln Ala Val Glu Cys Ala Lys Thr Tyr Leu Leu Phe 
                320                 325                 330 

Phe Pro Asn Asp Glu Val Met Asn Gln Asn Leu Ala Tyr Tyr Ala 
                335                 340                 345 

Ala Met Leu Gly Glu Glu His Thr Arg Ser Ile Gly Pro Arg Glu 
                350                 355                 360 

Ser Ala Lys Glu Tyr Arg Gln Arg Ser Leu Leu Glu Lys Glu Leu 
                365                 370                 375 

Leu Phe Phe Ala Tyr Asp Val Phe Gly Ile Pro Phe Val Asp Pro 
                380                 385                 390 

Asp Ser Trp Thr Pro Glu Glu Val Ile Pro Lys Arg Leu Gln Glu 
                395                 400                 405 

Lys Gln Lys Ser Glu Arg Glu Thr Ala Val Arg Ile Ser Gln Glu 
                410                 415                 420 

Ile Gly Asn Leu Met Lys Glu Ile Glu Thr Leu Val Glu Glu Lys 
                425                 430                 435 

Thr Lys Glu Ser Leu Asp Val Ser Arg Leu Thr Arg Glu Gly Gly 
                440                 445                 450 

Pro Leu Leu Tyr Glu Gly Ile Ser Leu Thr Met Asn Ser Lys Leu 
                455                 460                 465 

Leu Asn Gly Ser Gln Arg Val Val Met Asp Gly Val Ile Ser Asp 
                470                 475                 480 

His Glu Cys Gln Glu Leu Gln Arg Leu Thr Asn Val Ala Ala Thr 
                485                 490                 495 

Ser Gly Asp Gly Tyr Arg Gly Gln Thr Ser Pro His Thr Pro Asn 
                500                 505                 510 

Glu Lys Phe Tyr Gly Val Thr Val Phe Lys Ala Leu Lys Leu Gly 
                515                 520                 525 

Gln Glu Gly Lys Val Pro Leu Gln Ser Ala His Leu Tyr Tyr Asn 
                530                 535                 540 

Val Thr Glu Lys Val Arg Arg Ile Met Glu Ser Tyr Phe Arg Leu 
                545                 550                 555 

Asp Thr Pro Leu Tyr Phe Ser Tyr Ser His Leu Val Cys Arg Thr 
                560                 565                 570 

Ala Ile Glu Glu Val Gln Ala Glu Arg Lys Asp Asp Ser His Pro 
                575                 580                 585 

Val His Val Asp Asn Cys Ile Leu Asn Ala Glu Thr Leu Val Cys 
                590                 595                 600 

Val Lys Glu Pro Pro Ala Tyr Thr Phe Arg Asp Tyr Ser Ala Ile 
                605                 610                 615 

Leu Tyr Leu Asn Gly Asp Phe Asp Gly Gly Asn Phe Tyr Phe Thr 
                620                 625                 630 

Glu Leu Asp Ala Lys Thr Val Thr Ala Glu Val Gln Pro Gln Cys 
                635                 640                 645 

Gly Arg Ala Val Gly Phe Ser Ser Gly Thr Glu Asn Pro His Gly 
                650                 655                 660 

Val Lys Ala Val Thr Arg Gly Gln Arg Cys Ala Ile Ala Leu Trp 
                665                 670                 675 

Phe Thr Leu Asp Pro Arg His Ser Glu Arg Asp Arg Val Gln Ala 
                680                 685                 690 

Asp Asp Leu Val Lys Met Leu Phe Ser Pro Glu Glu Met Asp Leu 
                695                 700                 705 

Ser Gln Glu Gln Pro Leu Asp Ala Gln Gln Gly Pro Pro Glu Pro 
                710                 715                 720 

Ala Gln Glu Ser Leu Ser Gly Ser Glu Ser Lys Pro Lys Asp Glu 
                725                 730                 735 

Leu 

 
           
             34  
             1896  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7204554CD1  
             
           
            34 

Met Pro Leu Pro Pro Arg Ser Leu Gln Val Leu Leu Leu Leu Leu 
  1               5                  10                  15 

Leu Leu Leu Leu Leu Leu Pro Gly Met Trp Ala Glu Ala Gly Leu 
                 20                  25                  30 

Pro Arg Ala Gly Gly Gly Ser Gln Pro Pro Phe Arg Thr Phe Ser 
                 35                  40                  45 

Ala Ser Asp Trp Gly Leu Thr His Leu Val Val His Glu Gln Thr 
                 50                  55                  60 

Gly Glu Val Tyr Val Gly Ala Val Asn Arg Ile Tyr Lys Leu Ser 
                 65                  70                  75 

Gly Asn Leu Thr Leu Leu Arg Ala His Val Thr Gly Pro Val Glu 
                 80                  85                  90 

Asp Asn Glu Lys Cys Tyr Pro Pro Pro Ser Val Gln Ser Cys Pro 
                 95                 100                 105 

His Gly Leu Gly Ser Thr Asp Asn Val Asn Lys Leu Leu Leu Leu 
                110                 115                 120 

Asp Tyr Ala Ala Asn Arg Leu Leu Ala Cys Gly Ser Ala Ser Gln 
                125                 130                 135 

Gly Ile Cys Gln Phe Leu Arg Leu Asp Asp Leu Phe Lys Leu Gly 
                140                 145                 150 

Glu Pro His His Arg Lys Glu His Tyr Leu Ser Ser Val Gln Glu 
                155                 160                 165 

Ala Gly Ser Met Ala Gly Val Leu Ile Ala Gly Pro Pro Gly Gln 
                170                 175                 180 

Gly Gln Ala Lys Leu Phe Val Gly Thr Pro Ile Asp Gly Lys Ser 
                185                 190                 195 

Glu Tyr Phe Pro Thr Leu Ser Ser Arg Arg Leu Met Ala Asn Glu 
                200                 205                 210 

Glu Asp Ala Asp Met Phe Gly Phe Val Tyr Gln Asp Glu Phe Val 
                215                 220                 225 

Ser Ser Gln Leu Lys Ile Pro Ser Asp Thr Leu Ser Lys Phe Pro 
                230                 235                 240 

Ala Phe Asp Ile Tyr Tyr Val Tyr Ser Phe Arg Ser Glu Gln Phe 
                245                 250                 255 

Val Tyr Tyr Leu Thr Leu Gln Leu Asp Thr Gln Leu Thr Ser Pro 
                260                 265                 270 

Asp Ala Ala Gly Glu His Phe Phe Thr Ser Lys Ile Val Arg Leu 
                275                 280                 285 

Cys Val Asp Asp Pro Lys Phe Tyr Ser Tyr Val Glu Phe Pro Ile 
                290                 295                 300 

Gly Cys Glu Gln Ala Gly Val Glu Tyr Arg Leu Val Gln Asp Ala 
                305                 310                 315 

Tyr Leu Ser Arg Pro Gly Arg Ala Leu Ala His Gln Leu Gly Leu 
                320                 325                 330 

Ala Glu Asp Glu Asp Val Leu Phe Thr Val Phe Ala Gln Gly Gln 
                335                 340                 345 

Lys Asn Arg Val Lys Pro Pro Lys Glu Ser Ala Leu Cys Leu Phe 
                350                 355                 360 

Thr Leu Arg Ala Ile Lys Glu Lys Ile Lys Glu Arg Ile Gln Ser 
                365                 370                 375 

Cys Tyr Arg Gly Glu Gly Lys Leu Ser Leu Pro Trp Leu Leu Asn 
                380                 385                 390 

Lys Glu Leu Gly Cys Ile Asn Ser Pro Leu Gln Ile Asp Asp Asp 
                395                 400                 405 

Phe Cys Gly Gln Asp Phe Asn Gln Pro Leu Gly Gly Thr Val Thr 
                410                 415                 420 

Ile Glu Gly Thr Pro Leu Phe Val Asp Lys Asp Asp Gly Leu Thr 
                425                 430                 435 

Ala Val Ala Ala Tyr Asp Tyr Arg Gly Arg Thr Val Val Phe Ala 
                440                 445                 450 

Gly Thr Arg Ser Gly Arg Ile Arg Lys Ile Leu Val Asp Leu Ser 
                455                 460                 465 

Asn Pro Gly Gly Arg Pro Ala Leu Ala Tyr Glu Ser Val Val Ala 
                470                 475                 480 

Gln Glu Gly Ser Pro Ile Leu Arg Asp Leu Val Leu Ser Pro Asn 
                485                 490                 495 

His Gln Tyr Leu Tyr Ala Met Thr Glu Lys Gln Val Thr Arg Val 
                500                 505                 510 

Pro Val Glu Ser Cys Val Gln Tyr Thr Ser Cys Glu Leu Cys Leu 
                515                 520                 525 

Gly Ser Arg Asp Pro His Cys Gly Trp Cys Val Leu His Ser Ile 
                530                 535                 540 

Cys Ser Arg Arg Asp Ala Cys Glu Arg Ala Asp Glu Pro Gln Arg 
                545                 550                 555 

Phe Ala Ala Asp Leu Leu Gln Cys Val Gln Leu Thr Val Gln Pro 
                560                 565                 570 

Arg Asn Val Ser Val Thr Met Ser Gln Val Pro Leu Val Leu Gln 
                575                 580                 585 

Ala Trp Asn Val Pro Asp Leu Ser Ala Gly Val Asn Cys Ser Phe 
                590                 595                 600 

Glu Asp Phe Thr Glu Ser Glu Ser Val Leu Glu Asp Gly Arg Ile 
                605                 610                 615 

His Cys Arg Ser Pro Ser Ala Arg Glu Val Ala Pro Ile Thr Arg 
                620                 625                 630 

Gly Gln Gly Asp Gln Arg Val Val Lys Leu Tyr Leu Lys Ser Lys 
                635                 640                 645 

Glu Thr Gly Lys Lys Phe Ala Ser Val Asp Phe Val Phe Tyr Asn 
                650                 655                 660 

Cys Ser Val His Gln Ser Cys Leu Ser Cys Val Asn Gly Ser Phe 
                665                 670                 675 

Pro Cys His Trp Cys Lys Tyr Arg His Val Cys Thr His Asn Val 
                680                 685                 690 

Ala Asp Cys Ala Phe Leu Glu Gly Arg Val Asn Val Ser Glu Asp 
                695                 700                 705 

Cys Pro Gln Ile Leu Pro Ser Thr Gln Ile Tyr Val Pro Val Gly 
                710                 715                 720 

Val Val Lys Pro Ile Thr Leu Ala Ala Arg Asn Leu Pro Gln Pro 
                725                 730                 735 

Gln Ser Gly Gln Arg Gly Tyr Glu Cys Leu Phe His Ile Pro Gly 
                740                 745                 750 

Ser Pro Ala Arg Val Thr Ala Leu Arg Phe Asn Ser Ser Ser Leu 
                755                 760                 765 

Gln Cys Gln Asn Ser Ser Tyr Ser Tyr Glu Gly Asn Asp Val Ser 
                770                 775                 780 

Asp Leu Pro Val Asn Leu Ser Val Val Trp Asn Gly Asn Phe Val 
                785                 790                 795 

Ile Asp Asn Pro Gln Asn Ile Gln Ala His Leu Tyr Lys Cys Pro 
                800                 805                 810 

Ala Leu Arg Glu Ser Cys Gly Leu Cys Leu Lys Ala Asp Pro Arg 
                815                 820                 825 

Phe Glu Cys Gly Trp Cys Val Ala Glu Arg Arg Cys Ser Leu Arg 
                830                 835                 840 

His His Cys Ala Ala Asp Thr Pro Ala Ser Trp Met His Ala Arg 
                845                 850                 855 

His Gly Ser Ser Arg Cys Thr Asp Pro Lys Ile Leu Lys Leu Ser 
                860                 865                 870 

Pro Glu Thr Gly Pro Arg Gln Gly Gly Thr Arg Leu Thr Ile Thr 
                875                 880                 885 

Gly Glu Asn Leu Gly Leu Arg Phe Glu Asp Val Arg Leu Gly Val 
                890                 895                 900 

Arg Val Gly Lys Val Leu Cys Ser Pro Val Glu Ser Glu Tyr Ile 
                905                 910                 915 

Ser Ala Glu Gln Ile Val Cys Glu Ile Gly Asp Ala Ser Ser Val 
                920                 925                 930 

Arg Ala His Asp Ala Leu Val Glu Val Cys Val Arg Asp Cys Ser 
                935                 940                 945 

Pro His Tyr Arg Ala Leu Ser Pro Lys Arg Phe Thr Phe Val Thr 
                950                 955                 960 

Pro Thr Phe Tyr Arg Val Ser Pro Ser Arg Gly Pro Leu Ser Gly 
                965                 970                 975 

Gly Thr Trp Ile Gly Ile Glu Gly Ser His Leu Asn Ala Gly Ser 
                980                 985                 990 

Asp Val Ala Val Ser Val Gly Gly Arg Pro Cys Ser Phe Ser Trp 
                995                1000                1005 

Arg Asn Ser Arg Glu Ile Arg Cys Leu Thr Pro Pro Gly Gln Ser 
               1010                1015                1020 

Pro Gly Ser Ala Pro Ile Ile Ile Asn Ile Asn Arg Ala Gln Leu 
               1025                1030                1035 

Thr Asn Pro Glu Val Lys Tyr Asn Tyr Thr Glu Asp Pro Thr Ile 
               1040                1045                1050 

Leu Arg Ile Asp Pro Glu Trp Ser Ile Asn Ser Gly Gly Thr Leu 
               1055                1060                1065 

Leu Thr Val Thr Gly Thr Asn Leu Ala Thr Val Arg Glu Pro Arg 
               1070                1075                1080 

Ile Arg Ala Lys Tyr Gly Gly Ile Glu Arg Glu Asn Gly Cys Leu 
               1085                1090                1095 

Val Tyr Asn Asp Thr Thr Met Val Cys Arg Ala Pro Ser Val Ala 
               1100                1105                1110 

Asn Pro Val Arg Ser Pro Pro Glu Leu Gly Glu Arg Pro Asp Glu 
               1115                1120                1125 

Leu Gly Phe Val Met Asp Asn Val Arg Ser Leu Leu Val Leu Asn 
               1130                1135                1140 

Ser Thr Ser Phe Leu Tyr Tyr Pro Asp Pro Val Leu Glu Pro Leu 
               1145                1150                1155 

Ser Pro Thr Gly Leu Leu Glu Leu Lys Pro Ser Ser Pro Leu Ile 
               1160                1165                1170 

Leu Lys Gly Arg Asn Leu Leu Pro Pro Ala Pro Gly Asn Ser Arg 
               1175                1180                1185 

Leu Asn Tyr Thr Val Leu Ile Gly Ser Thr Pro Cys Thr Leu Thr 
               1190                1195                1200 

Val Ser Glu Thr Gln Leu Leu Cys Glu Ala Pro Asn Leu Thr Gly 
               1205                1210                1215 

Gln His Lys Val Thr Val Arg Ala Gly Gly Phe Glu Phe Ser Pro 
               1220                1225                1230 

Gly Thr Leu Gln Val Tyr Ser Asp Ser Leu Leu Thr Leu Pro Ala 
               1235                1240                1245 

Ile Val Gly Ile Gly Gly Gly Gly Gly Leu Leu Leu Leu Val Ile 
               1250                1255                1260 

Val Ala Val Leu Ile Ala Tyr Lys Arg Lys Ser Arg Asp Ala Asp 
               1265                1270                1275 

Arg Thr Leu Lys Arg Leu Gln Leu Gln Met Asp Asn Leu Glu Ser 
               1280                1285                1290 

Arg Val Ala Leu Glu Cys Lys Glu Ala Phe Ala Glu Leu Gln Thr 
               1295                1300                1305 

Asp Ile His Glu Leu Thr Asn Asp Leu Asp Gly Ala Gly Ile Pro 
               1310                1315                1320 

Phe Leu Asp Tyr Arg Thr Tyr Ala Met Arg Val Leu Phe Pro Gly 
               1325                1330                1335 

Ile Glu Asp His Pro Val Leu Lys Glu Met Glu Val Gln Ala Asn 
               1340                1345                1350 

Val Glu Lys Ser Leu Thr Leu Phe Gly Gln Leu Leu Thr Lys Lys 
               1355                1360                1365 

His Phe Leu Leu Thr Phe Ile Arg Thr Leu Glu Ala Gln Arg Ser 
               1370                1375                1380 

Phe Ser Met Arg Asp Arg Gly Asn Val Ala Ser Leu Ile Met Thr 
               1385                1390                1395 

Ala Leu Gln Gly Glu Met Glu Tyr Ala Thr Gly Val Leu Lys Gln 
               1400                1405                1410 

Leu Leu Ser Asp Leu Ile Glu Lys Asn Leu Glu Ser Lys Asn His 
               1415                1420                1425 

Pro Lys Leu Leu Leu Arg Arg Thr Glu Ser Val Ala Glu Lys Met 
               1430                1435                1440 

Leu Thr Asn Trp Phe Thr Phe Leu Leu Tyr Lys Phe Leu Lys Glu 
               1445                1450                1455 

Cys Ala Gly Glu Pro Leu Phe Met Leu Tyr Cys Ala Ile Lys Gln 
               1460                1465                1470 

Gln Met Glu Lys Gly Pro Ile Asp Ala Ile Thr Gly Glu Ala Arg 
               1475                1480                1485 

Tyr Ser Leu Ser Glu Asp Lys Leu Ile Arg Gln Gln Ile Asp Tyr 
               1490                1495                1500 

Lys Thr Leu Thr Leu Asn Cys Val Asn Pro Glu Asn Glu Asn Ala 
               1505                1510                1515 

Pro Glu Val Pro Val Lys Gly Leu Asp Cys Asp Thr Val Thr Gln 
               1520                1525                1530 

Ala Lys Glu Lys Leu Leu Asp Ala Ala Tyr Lys Gly Val Pro Tyr 
               1535                1540                1545 

Ser Gln Arg Pro Lys Ala Ala Asp Met Asp Leu Glu Trp Arg Gln 
               1550                1555                1560 

Gly Arg Met Ala Arg Ile Ile Leu Gln Asp Glu Asp Val Thr Thr 
               1565                1570                1575 

Lys Ile Asp Asn Asp Trp Lys Arg Leu Asn Thr Leu Ala His Tyr 
               1580                1585                1590 

Gln Val Thr Asp Gly Ser Ser Val Ala Leu Val Pro Lys Gln Thr 
               1595                1600                1605 

Ser Ala Tyr Asn Ile Ser Asn Ser Ser Thr Phe Thr Lys Ser Leu 
               1610                1615                1620 

Ser Arg Tyr Glu Ser Met Leu Arg Thr Ala Ser Ser Pro Asp Ser 
               1625                1630                1635 

Leu Arg Ser Arg Thr Pro Met Ile Thr Pro Asp Leu Glu Ser Gly 
               1640                1645                1650 

Thr Lys Leu Trp His Leu Val Lys Asn His Asp His Leu Asp Gln 
               1655                1660                1665 

Arg Glu Gly Asp Arg Gly Ser Lys Met Val Ser Glu Ile Tyr Leu 
               1670                1675                1680 

Thr Arg Leu Leu Ala Thr Lys Gly Thr Leu Gln Lys Phe Val Asp 
               1685                1690                1695 

Asp Leu Phe Glu Thr Ile Phe Ser Thr Ala His Arg Gly Ser Ala 
               1700                1705                1710 

Leu Pro Leu Ala Ile Lys Tyr Met Phe Asp Phe Leu Asp Glu Gln 
               1715                1720                1725 

Ala Asp Lys His Gln Ile His Asp Ala Asp Val Arg His Thr Trp 
               1730                1735                1740 

Lys Ser Asn Cys Leu Pro Leu Arg Phe Trp Val Asn Val Ile Lys 
               1745                1750                1755 

Asn Pro Gln Phe Val Phe Asp Ile His Lys Asn Ser Ile Thr Asp 
               1760                1765                1770 

Ala Cys Leu Ser Val Val Ala Gln Thr Phe Met Asp Ser Cys Ser 
               1775                1780                1785 

Thr Ser Glu His Lys Leu Gly Lys Asp Ser Pro Ser Asn Lys Leu 
               1790                1795                1800 

Leu Tyr Ala Lys Asp Ile Pro Asn Tyr Lys Ser Trp Val Glu Arg 
               1805                1810                1815 

Tyr Tyr Ala Asp Ile Ala Lys Met Pro Ala Ile Ser Asp Gln Asp 
               1820                1825                1830 

Met Ser Ala Tyr Leu Ala Glu Gln Ser Arg Leu His Leu Ser Gln 
               1835                1840                1845 

Phe Asn Ser Met Ser Ala Leu His Glu Ile Tyr Ser Tyr Ile Thr 
               1850                1855                1860 

Lys Tyr Lys Asp Glu Ile Leu Ala Ala Leu Glu Lys Asp Glu Gln 
               1865                1870                1875 

Ala Arg Arg Gln Arg Leu Arg Ser Lys Leu Glu Gln Val Val Asp 
               1880                1885                1890 

Thr Met Ala Leu Ser Ser 
               1895 

 
           
             35  
             215  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6833247CD1  
             
           
            35 

Met Gly Leu Glu Lys Pro Gln Ser Lys Leu Glu Gly Gly Met His 
  1               5                  10                  15 

Pro Gln Leu Ile Pro Ser Val Ile Ala Val Val Phe Ile Leu Leu 
                 20                  25                  30 

Leu Ser Val Cys Phe Ile Ala Ser Cys Leu Val Thr His His Asn 
                 35                  40                  45 

Phe Ser Arg Cys Lys Arg Gly Thr Gly Val His Lys Leu Glu His 
                 50                  55                  60 

His Ala Lys Leu Lys Cys Ile Lys Glu Lys Ser Glu Leu Lys Ser 
                 65                  70                  75 

Ala Glu Gly Ser Thr Trp Asn Cys Cys Pro Ile Asp Trp Arg Ala 
                 80                  85                  90 

Phe Gln Ser Asn Cys Tyr Phe Pro Leu Thr Asp Asn Lys Thr Trp 
                 95                 100                 105 

Ala Glu Ser Glu Arg Asn Cys Ser Gly Met Gly Ala His Leu Met 
                110                 115                 120 

Thr Ile Ser Thr Glu Ala Glu Gln Asn Phe Ile Ile Gln Phe Leu 
                125                 130                 135 

Asp Arg Arg Leu Ser Tyr Phe Leu Gly Leu Arg Asp Glu Asn Ala 
                140                 145                 150 

Lys Gly Gln Trp Arg Trp Val Asp Gln Thr Pro Phe Asn Pro Arg 
                155                 160                 165 

Arg Val Phe Trp His Lys Asn Glu Pro Asp Asn Ser Gln Gly Glu 
                170                 175                 180 

Asn Cys Val Val Leu Val Tyr Asn Gln Asp Lys Trp Ala Trp Asn 
                185                 190                 195 

Asp Val Pro Cys Asn Phe Glu Ala Ser Arg Ile Cys Lys Ile Pro 
                200                 205                 210 

Gly Thr Thr Leu Asn 
                215 

 
           
             36  
             579  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4148119CD1  
             
           
            36 

Met Gly Arg Pro Thr Gln Trp Pro Ser Leu Leu Leu Leu Leu Leu 
  1               5                  10                  15 

Leu Pro Gly Pro Pro Pro Val Ala Gly Leu Glu Asp Ala Ala Phe 
                 20                  25                  30 

Pro His Leu Gly Glu Ser Leu Gln Pro Leu Pro Arg Ala Cys Pro 
                 35                  40                  45 

Leu Arg Cys Ser Cys Pro Arg Val Asp Thr Val Asp Cys Asp Gly 
                 50                  55                  60 

Leu Asp Leu Arg Val Phe Pro Asp Asn Ile Thr Arg Ala Ala Gln 
                 65                  70                  75 

His Leu Ser Leu Gln Asn Asn Gln Leu Gln Glu Leu Pro Tyr Asn 
                 80                  85                  90 

Glu Leu Ser Arg Leu Ser Gly Leu Arg Thr Leu Asn Leu His Asn 
                 95                 100                 105 

Asn Leu Ile Ser Ser Glu Gly Leu Pro Asp Glu Ala Phe Glu Ser 
                110                 115                 120 

Leu Thr Gln Leu Gln His Leu Cys Val Ala His Asn Lys Leu Ser 
                125                 130                 135 

Val Ala Pro Gln Phe Leu Pro Arg Ser Leu Arg Val Ala Asp Leu 
                140                 145                 150 

Ala Ala Asn Gln Val Met Glu Ile Phe Pro Leu Thr Phe Gly Glu 
                155                 160                 165 

Lys Pro Val Leu Arg Ser Val Tyr Leu His Asn Asn Gln Leu Ser 
                170                 175                 180 

Asn Ala Gly Leu Pro Pro Asp Ala Phe Arg Gly Ser Glu Ala Ile 
                185                 190                 195 

Ala Thr Leu Ser Leu Ser Asn Asn Gln Leu Ser Tyr Leu Pro Pro 
                200                 205                 210 

Ser Leu Pro Pro Ser Leu Glu Arg Leu His Leu Gln Asn Asn Leu 
                215                 220                 225 

Ile Ser Lys Val Pro Arg Gly Ala Leu Ser Arg Gln Thr Gln Leu 
                230                 235                 240 

Arg Glu Leu Tyr Leu Gln His Asn Gln Leu Thr Asp Ser Gly Leu 
                245                 250                 255 

Asp Ala Thr Thr Phe Ser Lys Leu His Ser Leu Glu Tyr Leu Asp 
                260                 265                 270 

Leu Ser His Asn Gln Leu Thr Thr Val Pro Ala Gly Leu Pro Arg 
                275                 280                 285 

Thr Leu Ala Ile Leu His Leu Gly Arg Asn Arg Ile Arg Gln Val 
                290                 295                 300 

Glu Ala Ala Arg Leu His Gly Ala Arg Gly Leu Arg Tyr Leu Leu 
                305                 310                 315 

Leu Gln His Asn Gln Leu Gly Ser Ser Gly Leu Pro Ala Gly Ala 
                320                 325                 330 

Leu Arg Pro Leu Arg Gly Leu His Thr Leu His Leu Tyr Gly Asn 
                335                 340                 345 

Gly Leu Asp Arg Val Pro Pro Ala Leu Pro Arg Arg Leu Arg Ala 
                350                 355                 360 

Leu Val Leu Pro His Asn His Val Ala Ala Leu Gly Ala Arg Asp 
                365                 370                 375 

Leu Val Ala Thr Pro Gly Leu Thr Glu Leu Asn Leu Ala Tyr Asn 
                380                 385                 390 

Arg Leu Ala Ser Ala Arg Val His His Arg Ala Phe Arg Arg Leu 
                395                 400                 405 

Arg Ala Leu Arg Ser Leu Asp Leu Ala Gly Asn Gln Leu Thr Arg 
                410                 415                 420 

Leu Pro Met Gly Leu Pro Thr Gly Leu Arg Thr Leu Gln Leu Gln 
                425                 430                 435 

Arg Asn Gln Leu Arg Met Leu Glu Pro Glu Pro Leu Ala Gly Leu 
                440                 445                 450 

Asp Gln Leu Arg Glu Leu Ser Leu Ala His Asn Arg Leu Arg Val 
                455                 460                 465 

Gly Asp Ile Gly Pro Gly Thr Trp His Glu Leu Gln Ala Leu Gln 
                470                 475                 480 

Met Leu Asp Leu Ser His Asn Glu Leu Ser Phe Val Pro Pro Asp 
                485                 490                 495 

Leu Pro Glu Ala Leu Glu Glu Leu His Leu Glu Gly Asn Arg Ile 
                500                 505                 510 

Gly His Val Gly Pro Glu Ala Phe Leu Ser Thr Pro Arg Leu Arg 
                515                 520                 525 

Ala Leu Phe Leu Arg Ala Asn Arg Leu His Met Thr Ser Ile Ala 
                530                 535                 540 

Ala Glu Ala Phe Leu Gly Leu Pro Asn Leu Arg Val Val Asp Thr 
                545                 550                 555 

Ala Gly Asn Pro Glu Gln Val Leu Ile Arg Leu Pro Pro Thr Thr 
                560                 565                 570 

Pro Arg Gly Pro Arg Ala Gly Gly Pro 
                575 

 
           
             37  
             1211  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1888682CB1  
             
           
            37 

ccgggacggt cacatcccgc tgcaggggcg ggcggaggcc gccgcactgc ctcccgcacc     60 

ggggacccag gccagcgtcc gggcaacgcc ccctgctccc ggacagactc cgtggcccgc    120 

tcgagccctg ggggctccgc agacccgcgc ccgctccgcc cgcagctcgg ccccgcgctg    180 

cccgcgtcgc cgggcccgcg ccgggatggg gtaggggcag cgccaccgag tcgggcgatg    240 

ggccgccctc tgggcaccga gcagcccccc gaggcctgac caaccgcgag gaccggcgga    300 

ggagccccgc ctggatgtca agcggatgcc aagcggatgc cacagttccc cccccagcgg    360 

actccgtggg gacatggctt cgctggtgcc cctttcccca tatctaagcc ccacggtcct    420 

cctgctggtc agctgtgacc tgggcttcgt gcgagcagac cggcctccct ctcctgtgaa    480 

tgtgacggtc actcacctca gagccaactc ggccactgtg tcctgggacg tcccagaagg    540 

caacatcgtc attggctact ccatttccca gcaacggcag aatggccccg ggcagcgtgt    600 

gattcgggag gtgaacacca ccacccgggc ctgtgccctc tggggcctgg ctgaagacag    660 

tgactacaca gtgcaggtca ggagcatcgg ccttcgggga gagagtcccc cagggccccg    720 

ggtgcacttc cgaactctca agggttctga ccggctacct tcaaacagtt caagcccagg    780 

tgacatcaca gtggaaggtc tggatggaga gcggccactg cagactgggg aagtggtcat    840 

cattgtggtg gtgttgctca tgtgggctgc tgtaattggg ctgttctgcc gtcagtatga    900 

catcatcaag gacaatgact ccaacaacaa tcccaaggag aagggaaagg ggccggaaca    960 

gagtcctcag ggaaggccag tggggacaag acagaaaaag tcaccatcta tcaacaccat   1020 

cgacgtttga gtgaagaaac acacccagaa gagagatgca ctaacaactg gggataggga   1080 

tggggtcagg gggagcccaa gatggtgatc tgcccgagac tcccagaggg tattgccact   1140 

cccacaatct caggcctggt acccatcctc tttccactgt gagcagagcc agaaggtagg   1200 

tctgttcaga g                                                        1211 

 
           
             38  
             1523  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1794980CB1  
             
           
            38 

ggcggctggc ggcgcgggca ggcaggcggg gaggacaggc tgggggcggc gaccgcgagg     60 

ggccgcgcgc ggagggcgcc tggtgcagca tgggcggccc gcgggcttgg gcgctgctct    120 

gcctcgggct cctgctcccg ggaggcggcg ctgcgtggag catcggggca gctccgttct    180 

ccggacgcag gaactggtgc tcctatgtgg tgacccgcac catctcatgc catgtgcaga    240 

atggcaccta ccttcagcga gtgctgcaga actgcccctg gcccatgagc tgtccgggga    300 

gcagctacag aactgtggtg agacccacat acaaggtgat gtacaagata gtgaccgccc    360 

gtgagtggag gtgctgccct gggcactcag gagtgagctg cgaggaagtt gcagcttcct    420 

ctgcctcctt ggagcccatg tggtcgggca gtaccatgcg gcggatggcg cttcggccca    480 

cagccttctc aggttgtctc aactgcagca aagtgtcaga gctgacagag cggctgaagg    540 

tgctggaggc caagatgacc atgctgactg tcatagagca gccagtacct ccaacaccag    600 

ctacccctga ggaccctgcc ccgctctggg gtccccctcc tgcccagggc agccccggag    660 

atggaggcct ccaggaccaa gtcggtgctt gggggcttcc cgggcccacc ggccccaagg    720 

gagatgccgg cagtcggggc ccaatgggga tgagaggccc accaggtcca cagggccccc    780 

cagggagccc tggccgggct ggagctgtgg gcacccctgg agagagggga cctcctgggc    840 

caccagggcc tcctggcccc cctgggcccc cagcccctgt tgggccaccc catgcccgga    900 

tctcccagca tggagaccca ttgctgtcca acaccttcac tgagaccaac aaccactggc    960 

cccagggacc cactgggcct ccaggccctc cagggcccat gggtccccct gggcctcctg   1020 

gccccacagg tgtccctggg agtcctggtc acataggacc cccaggcccc actggaccca   1080 

aaggaatctc tggccaccca ggagagaagg gcgagagagg actgcgtggg gagcctggcc   1140 

cccaaggctc tgctgggcag cggggggaac ctggccctaa gggagaccct ggtgagaaga   1200 

gccactgggg ggaggggttg caccagctac gcgaggcttt gaagatttta gctgagaggg   1260 

ttttaatctt ggaaacaatg attgggctct atgaaccaga gctggggtct ggggcgggcc   1320 

ctgccggcac aggcaccccc agcctccttc ggggcaagag gggcggacat gcaaccaact   1380 

accggatcgt ggcccccagg agccgggacg agagaggctg agttggtggc ggcccctgag   1440 

gcagaccagg ccaggcttcc cctcctacct ggactcggcc agctgcctcc agggaccgcc   1500 

cgtccataat tcaggagcgt ccc                                           1523 

 
           
             39  
             1368  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5533958CB1  
             
           
            39 

ctgccgggtg tgccgggtgt ccagcgaacc cctttcccaa accttcgggg agaagggagg     60 

tgggaggagg caaagaaact acaggcaggg agctggaagg gggggtgggg ggggcaggag    120 

acaagaaatc aagacaccag gcagcaggac acacacacac tcacatacac tcacacacat    180 

agagaccaac agatagacag ctacctaaag cctgaaagac tgacagcaac acagaaaaaa    240 

agaaacaggc agaaagagag acaaagacag aaatagaaac agactaacac acagagtcaa    300 

aaatacagag acagaaagac agggagaaag agaaacagaa aattagacac caaagacata    360 

cgaacaggga ggaaggccga ctgaaagaaa gacggagaag aggagagaga agccagggcc    420 

gagcgtgcca gcaggcggat ggagggcggc ctggtggagg aggagacgta gtggcctggg    480 

ctgagctggg tgggccggga gaagcgggtg cctcagagtg ggggtggggg catgggaggg    540 

gcaggcattc tgctgctgct gctggctggg gcgggggtgg tggtggcctg gagaccccca    600 

aagggaaagt gtcccctgcg ctgctcctgc tctaaagaca gcgccctgtg tgagggctcc    660 

ccggacctgc ccgtcagctt ctctccgacc ctgctgtcac tctcactcgt caggacggga    720 

gtcacccagc tgaaggccgg cagcttcctg agaattccgt ctctgcacct gctcctcttc    780 

acctccaact ccttctccgt gattgaggac gatgcatttg cgggcctgtc ccacctgcag    840 

tacctcttca tcgaggacaa tgagattggc tccatctcta agaatgccct cagaggactt    900 

cgctcgctta cacacctaag cctggccaat aaccatctgg agaccctccc cagattcctg    960 

ttccgaggcc tggacaccct tactcacgtg gacctccgcg ggaacccgtt ccagtgtgac   1020 

tgccgcgtcc tctggctcct gcagtggatg cccaccgtga atgccagcgt ggggaccggc   1080 

gcctgtgcgg gccccgcctc cctgagccac atgcagctcc accacctcga ccccaagact   1140 

ttcaagtgca gagccatagg tggggggctt tcccgatggg gtgggaggcg ggagatctgg   1200 

gggaaaggct gccagggcca agaggctcgt ctcactccct gccctgccat ttcccggagt   1260 

gggaagaccc tgagcaagca gcactgcctt cctgagcccc agttttctca tctgtaaagt   1320 

gggggtaata aacagtgata taggagtgcc atggaaaaaa aaaaaaaa                1368 

 
           
             40  
             3157  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 60210196CB1  
             
           
            40 

tggtcgttcc tcggtttgcc atccattggg cccctgccct ccatccccgt ggaggcccct     60 

tgtctgggtg ttcgcactca acgtcgatgt gttgataatg gtgccttttt cgtgaagaaa    120 

ctgcctgagt ctcacttcca gaagtttata ggtccacccg ttctctccag cgtccgccag    180 

cccagatctc gcatgcgcat ctgtgtctgc ccctctttgc cttctgcctg tccctgggtg    240 

cccctcaggg tcagaatcac cctttccgcc cgcactggcc cccacatcac ctgtcttgtc    300 

cccactggcc ttccctgagg actctgttcc ggcccctttc ccttctcctt gggattgttg    360 

ttggagtcat tgtccttgat gatgtcatac tgacggcaga acagcccaat tacagctgaa    420 

acacaataca gtctgagccc agagagccgc ggggaccatg gagccggtgc cgctgcagga    480 

cttcgtgcgc gccttggacc ccgcctccct cccgcgcgtg ctgcgggtct gctcgggggt    540 

ctacttcgag ggctccatct atgagatctc tgggaatgag tgctgcctct ccacggggga    600 

cctgatcaag gtcacccagg tccgcctcca gaaggtggtc tgtgagaacc cgaagaccag    660 

ccagaccatg gagctcgccc ccaacttcca gggctacttc acccccctca acaccccaca    720 

gagctatgaa accctggagg agctggtctc tgccacaact cagagctcca agcagctgcc    780 

cacttgcttc atgtcgaccc acaggattgt cacagagggc agggtggtga ctgaggacca    840 

gctcctcatg cttgaggctg tggtgatgca cctcgggatc cgctctgccc gctgtgtcct    900 

gggcatggag ggtcagcagg tcatcctgca cctgccccta tcccagaagg ggcccttctg    960 

gacatgggag cctagtgccc ctcgaactct gctccaggtc ctacaggatc cagccctgaa   1020 

agacctcgtc ctcacctgcc ccaccctgcc ctggcattcc ctgatcctgc ggccccagta   1080 

tgagatccaa gccatcatgc acatgcgcag gaccattgtc aagatccctt ctaccctgga   1140 

ggtcgacgtg gaggacgtca ccgcctcctc ccggcacgtc cactttatca aaccgctgct   1200 

gctgagcgag gtcctggcct gggaaggccc tttccccctg tccatggaga tcctggaggt   1260 

tcctgagggc cgccccatct tcctcagccc gtgggtgggc tccttgcaaa aaggccagag   1320 

gctttgcgtc tatggcctag cctcaccacc ctggcgggtc ctggcctcaa gcaagggccg   1380 

caaggtgccc aggcacttcc tggtgtcagg gggctaccaa ggcaagctgc ggcggcggcc   1440 

aagggagttc cccacggcct atgacctcct aggtgctttc cagccaggcc ggccactccg   1500 

ggtggtggcc acaaaggact gtgagggcga gagggaggag aatcccgagt tcacgtccct   1560 

ggctgtgggt gaccggctgg aggtgctggg gcctggccag gcccatgggg cccagggcag   1620 

tgacgtggat gtcttggttt gtcagcggct gagtgaccag gctggggagg atgaggagga   1680 

agagtgcaaa gaggaggcag agagcccaga gcgggtcctg ctgcccttcc acttccctgg   1740 

cagtttcgtg gaggagatga gtgacagccg gcgctacagc ctggcagatc tgactgccca   1800 

gttttcactg ccttgtgagg tcaaggtggt ggccaaggac accagccacc ccactgaccc   1860 

tctgacctcc ttcctgggcc tgcggctgga ggagaagatc acagagccat tcttggtggt   1920 

gagcctagac tctgagcctg ggatgtgctt tgagatccct ccccggtggc tggacctgac   1980 

tgttgtgaag gccaaggggc agccagactt gccagagggg tctctcccca tagccacagt   2040 

ggaggagctg acagacacct tctattatcg tcttcggaag ttaccagcct gtgagatcca   2100 

agccccccca cccaggcccc ctaaaaatca gggcctcagc aagcagagga gacacagcag   2160 

tgagggaggc gtcaagtctt ctcaagtctt aggattgcag caacacgctc ggctgcccaa   2220 

acccaaggcg aagaccttgc cagagttcat caaggatggc tccagtacgt acagcaagat   2280 

tcctgcccac aggaagggcc acaggcccgc taagccccaa aggcaggatc tagatgatga   2340 

tgaacatgat tatgaagaaa tacttgagca atttcagaaa accatctaag tgctggagga   2400 

accacgcttc ctaactgctg cttctcaggg aatccgacac cagccaacca ttttaagcct   2460 

ctaaaagacc tcgggcaagt ctcacagaaa ctgagctgca gacggggagt agctttgtgg   2520 

aaactgattt gatggacact gcaccagctt ccttcaggtt ctagattctt gctacttagg   2580 

gcgggctggt ttggacctaa catctcgcac gtgactccct cagcctcaga gccttgggat   2640 

gcagagcagc tggcagggtt cctctcaatc ctgcaacccc agctgtccca ccggtggatg   2700 

cagaggggaa tccgaggcca tcaaccttgg tgacagcagc gcagtgccaa tgctgatcac   2760 

actgcatggg agattttgtt aacgtctgcc acccccactc tcacccccaa gctctaagcc   2820 

cccgggaggc ctggactgtc ttcctcatct ctgtagcacc aagcctgata gatctgtata   2880 

tggtaaacag gggtttaacc acatgtggtt aacatggatt aatgtgggaa tttggcttca   2940 

agaacacaac cttaggacct tgggccccaa aagctggtgg tgaaatgaga ggagccaatt   3000 

taagaagacc cttatggaga cctgaggctg cagaaactgg taggtttcat caggtggtta   3060 

aagtcgtcaa agttgtaagt gactaaccaa gattatttca ttttaaaacc acagaataaa   3120 

aatgacacct gagcttctct aaaaaaaaaa aaaaaaa                            3157 

 
           
             41  
             3264  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 815125CB1  
             
           
            41 

ggagccgggg cagccagaag aggtgggaaa agcggaggag gacgcccagg aggaggcggc     60 

ggcggcggcc gggaagtgaa aggtctcgca aagttcagcg gcggctgcgg gcgccgagcc    120 

ccgggctagc ggcagacgag cccgcagggc cgctccgcgg ggcagcgcag ccaggccggc    180 

tatggtcccg gggctcccgc cgccccccag gtgcccggga cccgccaggc cgggtgcgcg    240 

agggtcaccc cacctccccg cgcggtcccg gcccctggct cccagctgcc ggcgaccgct    300 

gaccgagccc ggcgccccag gaggaggaag aaaccagggc cccgttccct cccgaggacg    360 

gcggcgcttc atcccgcagc ccagaggtct cggctccctc cggcacccgc ccggcccggc    420 

tgctcccggc tcctcccggc catggggagc tgcgcgcggc tgctgctgct ctggggctgc    480 

acggtggtgg ccgcaggact gagtggagta gctggagtga gttcccgctg tgaaaaagcc    540 

tgcaaccctc ggatgggaaa tttggctttg gggcgaaaac tctgggcaga caccacctgc    600 

ggtcagaatg ctaccgaact gtactgcttc tacagtgaga acacggatct gacttgtcgg    660 

cagcccaaat gtgacaagtg caatgctgcc tatcctcacc tggctcacct gccatctgcc    720 

atggcagact catccttccg gtttcctcgc acatggtggc agtctgcgga ggatgtgcac    780 

agagaaaagg tccagttaga cctggaagct gaattctact tcactcacct aattgtgatg    840 

ttcaagtccc ccaggccagc tgccatggtg ctggaccgct cccaggactt tgggaaaaca    900 

tggaagcctt ataagtactt tgcgactaac tgctccgcta catttggcct ggaagatgat    960 

gttgtcaaga agggcgctat ttgtacttct aaatactcca gtccttttcc atgcactgga   1020 

ggagaggtta ttttcaaagc tttgtcacca ccatacgata cagagaaccc ttacagtgcc   1080 

aaagttcagg agcagctgaa gatcaccaac cttcgcgtgc agctgctgaa acgacagtct   1140 

tgtccctgtc agagaaatga cctgaacgaa gagcctcaac attttacaca ctatgcaatc   1200 

tatgatttca ttgtcaaggg cagctgcttc tgcaatggcc acgctgatca atgcatacct   1260 

gttcatggct tcagacctgt caaggcccca ggaacattcc acatggtcca tgggaagtgt   1320 

atgtgtaagc acaacacagc aggcagccac tgccagcact gtgccccgtt atacaatgac   1380 

cggccatggg aggcagctga tggcaaaacg ggggctccca acgagtgcag aacctgcaag   1440 

tgtaatgggc atgctgatac ctgtcacttc gacgttaatg tgtgggaggc atcagggaat   1500 

cgtagtggtg gtgtctgtga tgactgtcag cacaacacag aaggacagta ttgccagagg   1560 

tgcaagccag gcttctatcg tgacctgcgg agacccttct cagctccaga tgcttgcaaa   1620 

ccgtgttcct gccatccagt aggatcagct gtccttcctg ccaactcagt gaccttctgc   1680 

gaccccagca atggtgactg cccttgcaag cctggggtgg cagggcgacg ttgtgacagg   1740 

tgcatggtgg gatactgggg cttcggagac tatggctgtc gaccatgtga ctgtgcaggg   1800 

agctgtgacc ctatcaccgg agactgcatc agcagccaca cagacataga ctggtatcat   1860 

gaagttcctg acttccgtcc cgtgcacaat aagagcgaac cagcctggga gtgggaggat   1920 

gcgcaggggt tttctgcact tctacactca ggtaaatgcg aatgtaagga acagacatta   1980 

ggaaatgcca aggcattctg tggaatgaaa tattcatatg tgctaaaaat aaagatttta   2040 

tcagctcatg ataaaggtac tcatgttgag gtcaatgtga agattaaaaa ggtcttaaaa   2100 

tctaccaaac tgaagatttt ccgaggaaag cgaacattat atccagaatc atggacggac   2160 

agaggatgca cttgtccaat cctcaatcct ggtttggaat accttgtagc aggacatgag   2220 

gatataagaa caggcaaact aattgtgaat atgaaaagct ttgtccagca ctggaaacct   2280 

tctcttggaa gaaaagtcat ggatatttta aaaagagagt gcaagtagca ttaagatgga   2340 

tagcacataa tggcacttgt ctatgtacaa aacacaaact ttagagcaag aagacctcag   2400 

acaggaaact ggaatttttt aaagtgccaa aacatataga aatgtttgaa tgcatgggtc   2460 

ttatctaatt tatctcttct ggacccatgt ttaaatacag ttttatttca tgaagagaaa   2520 

tgaaaacccc tacactgata tctgttttct atgggactga ttctgaaatt cttaactatt   2580 

aagaatattt taatagcagc atgacattta gcagtaatcc attaagggca gtacctctaa   2640 

caaggacgcc ttccagcttc agctatgtta cttacgtttg atgctactta aagtaatgaa   2700 

tgacgtttta aggaatccct aaccctacta tcagaaaagg tgtttgttaa agagccttct   2760 

cttgtgtgtt acgcatgaac tttggtctgt aggtgttaaa tggaacctct ccatgtgtat   2820 

atagtatttc cttgtataaa gcactttact acctaccact tgtgttgtga acgtttggtg   2880 

actgctgttg aaagaaggaa aagggtgtgt gagaaagcct actgaagcag cagcactgcc   2940 

actacatgtg gacaaaagtg aacatataaa agaagttgtg ctatttaact ctgaatactt   3000 

ggagaaacta ggtgaagatg caaccagaaa ggagaatatg tatgcgtgaa gtctcagctt   3060 

tgagctggag gctagattcc aagatgacag ccatgatgaa actttttaaa aaactaaacc   3120 

agaagagact ttaaaataag agaaagaaat cataaatgta gacatatgct tggctaaagg   3180 

ggaaatggac tttaaatttt aaagagctca tttgcaatgc acttgtatac acttcaaaaa   3240 

ttattgtaga cacagcattt gtta                                          3264 

 
           
             42  
             3383  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1386915CB1  
             
           
            42 

tgcgatctag aacgtccgac ctctcctctc ccagccagtc gtggctggcc tttcaaagtg     60 

tgcagttgtc tcctccctgt ccagccccat cgtcgcccag gaccagctgg gccgcggtct    120 

gacctgaggc tgctgctcag cgccggggcg ctggcgctct ccattcgagc accttccagc    180 

ataccgctcg gctccgggag ccgctctgca aagttgagca gctcagagcg caagctttgc    240 

ctctcgactt ctccctcctt gggtccccgg cgcccccgcc tcccacgatc cctttcacta    300 

ggagcagcca gtcccagcgg gctggcaact tgcacccctt cctagtcatc ctccctgaaa    360 

cgcgaccatg ctgttaaggg gcgtcctcct ggcgttgcaa gccctgcagc tcgccggtgc    420 

cctcgacctg cccgctgggt cctgtgcctt tgaagagagc acttgcggct ttgactccgt    480 

gttggcctct ctgccgtgga ttttaaatga ggaaggccat tacatttatg tggatacctc    540 

ctttggcaag cagggggaga aagctgtgct gctaagtcct gacttacagg ctgaggaatg    600 

gagctgcctc cgtttggtct accagataac cacatcttcg gagtctctgt cagatcccag    660 

ccagctgaac ctctacatga gatttgaaga tgaaagcttt gatcgcttgc tttggtcagc    720 

taaggaacct tcagacagct ggctcatagc cagcttggat ttgcaaaaca gttccaagaa    780 

attcaagatt ttaatagaag gtgtactagg acagggaaac acagccagca tcgcactatt    840 

tgaaatcaag atgacaaccg gctactgtat tgaatgtgac tttgaagaaa atcatctctg    900 

tggctttgtg aaccgctgga atcccaatgt gaactggttt gttggaggag gaagtattcg    960 

gaatgtccac tccattctcc cacaggatca caccttcaag agtgaactgg gccactacat   1020 

gtacgtggac tcagtttatg tgaagcactt ccaggaggtg gcacagctca tctccccgtt   1080 

gaccacggcc cccatggctg gctgcctgtc attttattac cagatccagc aggggaatga   1140 

caatgtcttt tccctttaca ctcgggatgt ggctggcctt tacgaggaaa tctggaaagc   1200 

agacaggcca gggaatgctg cctggaacct tgcggaggtc gagttcaatg ctccttaccc   1260 

catggaggtt atttttgaag ttgctttcaa tggtcccaag ggaggttatg ttgccctgga   1320 

tgatatttca ttctctcctg ttcactgcca gaatcagaca gaacttctgt tcagtgccgt   1380 

ggaagccagc tgcaattttg agcaagatct ctgcaacttt taccaagata aagaaggtcc   1440 

aggttggacc cgagtgaaag taaaaccaaa catgtatcgg gctggagacc acactacagg   1500 

cttagggtat tacctgctag ccaacacaaa gttcacatct cagcctggct acattggaag   1560 

gctctatggg ccctccctac caggaaactt gcagtattgt ctgcgttttc attatgccat   1620 

ctatggattt ttaaaaatga gtgacaccct agcagtttac atctttgaag agaaccatgt   1680 

ggttcaagag aagatctggt ctgtgttgga gtccccaagg ggtgtttgga tgcaagctga   1740 

aatcaccttt aagaagccca tgcctaccaa ggtggttttc atgagcctat gcaaaagttt   1800 

ctgggactgt gggcttgtag ccctggatga cattacaata caattgggaa gctgctcatc   1860 

ttcagagaaa cttccacctc cacctggaga gtgtactttc gagcaagatg aatgtacatt   1920 

tactcaggag aaaagaaacc ggagcagctg gcacaggagg aggggagaaa ctcccacttc   1980 

ctacacagga ccaaagggag atcacactac tggggtaggc tactacatgt acattgaggc   2040 

ctcccatatg gtgtatggac aaaaagcacg cctcttgtcc aggcctctgc gaggagtctc   2100 

tggaaaacac tgcttgacct ttttctacca catgtatgga gggggcactg gcctgctgag   2160 

tgtttatctg aaaaaggaag aagacagtga agagtccctc ttatggagga gaagaggtga   2220 

acagagcatt tcctggctac gagcactgat tgaatacagc tgtgagaggc aacaccagat   2280 

aatttttgaa gccattcgag gagtatcaat aagaagtgat attgccattg atgatgttaa   2340 

atttcaggca ggaccctgtg gagaaatgga agatacaact caacaatcat caggatattc   2400 

tgaggactta aatgaaattg agtattaaga aatgatctgc attggattta ctagacgaaa   2460 

accatacctc tcttcaatca aaatgaaaac aaagcaaatg aatactggac agtcttaaca   2520 

attttataag ttataaaatg actttagagc accctccttc attacttttg caaaaacata   2580 

ctgactcagg gctctttttt tctttttgca tatgacaact gttactagaa atacaggcta   2640 

ctggttttgc atagatcatt catcttaatt ttggtaccag ttaaaaatac aaatgtacta   2700 

tattgtagtc attttaaagt acacaaaggg cacaatcaaa atgagatgca ctcatttaaa   2760 

tctgcattca gtgaatgtat tgggagaaaa ataggtcttg caggtttcct tttgaatttt   2820 

aagtatcata aatatttttt aagtaaataa tacggggtgt cagtaatatc tgcagaatga   2880 

atgcagtctt tcatgctaat gagttagtct ggaaaaataa agtcttattt tctatgtttt   2940 

attcatagaa atggagtatt aatttttaat attttcacca tatgtgataa caaaggatct   3000 

ttcatgaatg tccaagggta agtcagtatt aattaatgct gtattacaag gcaatgctac   3060 

cttctttatt ccccctttga actacctttg aagtcactat gagcacatgg atagaaattt   3120 

aacttttttt tgtaaagcaa gcttaaaatg tttatgtata catacccagc aacttttata   3180 

aatgtgttaa acaattttac tgatttttat aataaatatt ttggtaagat tttgaataat   3240 

atgaattcag gcagatatac taaactgctt ttatttactt gtttagaaaa ttgtatatat   3300 

atgtttgtgt atcctaacag ctgctatgaa attataaaat tacctaataa aaataatttg   3360 

aaaatcttaa aaaaaaaaaa aaa                                           3383 

 
           
             43  
             2741  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1344495CB1  
             
           
            43 

ggcagctgcg ggtcgcgggt cgcgggtcgc gagtcgccgg tcgccggtcg cggcggagcc     60 

tgggcgctga gtgaagaaaa tgaggcacga ggaattgtta accaagacct tccaaggccc    120 

agctgttgtg tgtgggactc cgaccagcca cgtatacatg tttaagaatg gcagtgggga    180 

ctcgggggac tcttctgaag aagagtctca ccgtgtggtt ttgcggcccc ggggcaagga    240 

gcgccacaag agcggtgtcc accagcctcc ccaggcggga gcaggtgacg tggtgctgct    300 

gcagcgggag ctggcccagg aggacagcct caacaagctg gcgctgcagt atggctgcaa    360 

agttgcagat atcaagaaag tcaacaactt catcagagaa caagacttat atgctttgaa    420 

atctgttaag attccagtga gaaaccatgg gatcctgatg gagacccaca aagaactgaa    480 

accccttctg agcccgtctt ccgagaccac agtgaccgtg gaactgccag aggcagacag    540 

agcaggcgcg ggcaccggtg cccaggccgg ccaactgatg ggcttcttta aggggattga    600 

ccaggatatt gagcgtgcag tgcagtcaga aatctttcta catgaaagtt actgcatgga    660 

cacctcccat cagccactgc tcccggcacc tccgaagacg cctatggatg gtgcagattg    720 

tggcattcag tggtggaatg ctgttttcat catgctgctg attggtattg tcttgcctgt    780 

cttttatttg gtctacttta aaatacaagc tagtggtgag acccctaata gcttgaacac    840 

aactgtcatc cccaatggct cgatggcaat gggtacagtt ccagggcaag cccccagact    900 

agcagttgca gtgccagccg tcacttctgc agacagccag ttcagtcaga ccacccaagc    960 

ggggagctaa gctttgtttt taaagactcg gcccagcttt agcaattggc tgttgatgtg   1020 

cctcagctgt cactggcgat gtcctagggg tgctgcattt tgcttccggg gaaggatgga   1080 

cacttttcag aagtcactgc agtattccca attgcactgg ccctgggcat ggccttaccc   1140 

agtctaagct ggcaggatct aaaacagcag cgacctcggc ccctatccag agaggtgcag   1200 

caagagagcc atttccctgt gacatttagt ggactggcca gttcatagca gcactgtgag   1260 

gacccccaag ttggacgtgc tcggagggaa agatttatgg cctctgtcga gggacctgca   1320 

gcgtgagagc cagtggcatc tgcgcggctt gcctggctct tgctgtatcc tcacttcctg   1380 

tggagcgggg attggctctg agaaggagtg ttctctgtct gcctggcaaa ggtgctgtgg   1440 

aataggcttg gcatgccacc ctgttttaga gagtgacagt tacagttgta acaagcctac   1500 

ttcatattgg ccccctcagt tagccttttt gaggcaatgc catttctaga gttgaaaaag   1560 

ccctggaccc aaactgcggc actgttgaat aaagggcagt cctactcctg tccttttaga   1620 

gtggcttagt gtgacacaca ggcatctccc aggccaagca cacacaggct gcgcccagtt   1680 

ccgcaggagc cgtcccacag cgtggctctc tggattctcc cacttgtcct ccttggaagg   1740 

agctcttgct ggccagtgtt tggaggggag gatgagtgcc tgtcactgag gcctcactat   1800 

ggttggcgtc tgaagctggg cggtcgtcag gcctgtgctg agagccgcag cccctgtgca   1860 

cacctaacac agggcgctcc ccctgctgct tccctggctc agttcttcgg agctccagag   1920 

tgagaaggcc gcttcgtcct ttttctctgg gtgatgccct tagaataaca ctatatgcaa   1980 

tgtaactcac aatgttccag gaccaaagac ttgatggagg ggctagaggc gacccttgtt   2040 

gtaaaaggcg atcagaacac ctgagggagg aaggggcttg cagttttccc agcccttctc   2100 

gctgccaagg cagcagtggt gctgtggatg ggctggggac tgcgggacag agcctgctac   2160 

tacttgggag ttggtgctgc cctgtggcat ggaggggtgg gaggggctga gatggctgct   2220 

ggcccggcct ccaagagttc tggacaggag gcagacactg cccagatgct cggtggaggg   2280 

acagtgatgg cctttgactc atgaggcctg gagaaaagta tcaaaggtct caccatgtaa   2340 

gagtgatttc cgatttctct cctttcagtt gtgtgaaaaa acagctggcc tgggttccat   2400 

tagcaaatta aatcatcttc aatcttaaat tagagaccag aatgatcttc aggataaaaa   2460 

gaacttctga atctctgcaa taggaaatgt ttcgatcatg caagtgcttt cccagccaaa   2520 

tgtctgtgct ctctgtgtca ctgagggcca caggttcctc taacatctgt cactgtcact   2580 

tcaccaggca ggccttggag ttccatgaca aaatcacttt tgtcagacaa agaatgtatc   2640 

ctttactttt ctcaaatgga ataaaattat ttcttctgtg gaggaaaatt gattccccct   2700 

ttttatttaa tttttttttg gagacagtct cactccttcc c                       2741 

 
           
             44  
             2076  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1485774CB1  
             
           
            44 

cggggctcca gccaggagcc ctgctgccca gggcatggcc aaacctttct tccgactcca     60 

gaagtttctc cgccgaacac agttcctgct gttcttcctc acggctgcct acctgatgac    120 

cggcagcctg ctgctgctgc agcgggtccg cgtggctctc ccacagggcc cccgggcacc    180 

cggccccctg cagaccttgc cagtggccgc cgtggcgctg ggcgtgggct tgctggacag    240 

cagagccctg cacgaccctc gagtcagccc agagctgctg ctgggtgtgg acatgctgca    300 

gagccccctg acccggcccc ggcccggccc ccgctggctc cggagccgca actcggagct    360 

gcgtcagttg cgtcgccgct ggttccacca cttcatgagt gactcccagg gaccgcccgc    420 

cctgggcccc gaggctgcca ggcccgccat ccacagccga ggcacctaca ttggatgctt    480 

cagtgacgat ggccatgaga ggactctgaa aggagctgtg ttttatgact tgagaaagat    540 

gactgtctcc cactgccagg atgcgtgtgc tgagcggtcc tatgtctacg ccggcttgga    600 

ggccggggcg gagtgttact gcgggaaccg gctgccagcg gtgagcgtgg ggctggaaga    660 

gtgtaaccat gagtgcaaag gcgagaaggg ctctgtgtgc ggggctgtgg accggctctc    720 

cgtgtaccgt gtggacgagc tgcagccggg ctccaggaag cggcggaccg ccacctaccg    780 

cggatgcttc cgactgccag agaacatcac acatgccttc cccagctccc tgatacaggc    840 

caatgtgacc gtggggactt gctcgggctt ttgttcccag aaagagttcc ccttggccat    900 

tctcaggggc tgggaatgct actgtgctta ccctaccccc cggttcaacc tgcgggatgc    960 

catggacagc tcagtatgtg gccaggaccc tgaggcacag aggctggcag aatactgtga   1020 

ggtctaccag acacctgtgc aagacactcg ttgtacagac aggaggttcc tgcctaacaa   1080 

atccaaagtg tttgtggctt tgtcaagctt cccaggagcc gggaacacgt gggcacggca   1140 

cctcattgag catgccactg gcttctatac agggagctac tactttgatg gaaccctcta   1200 

caacaaaggg ttcaagggcg aaaaggacca ctggcggagc cgacgcacca tctgtgtcaa   1260 

aacccacgag agtggcagga gggagattga gatgtctgat tcagccatcc tgctaatccg   1320 

gaacccatac aggtccctgg tggcagaatt caacagaaaa tgtgccgggc acctgggata   1380 

tgcagctgac cgcaactgga agagcaaaga gtggccggac tttgtcaaca gctacgcctc   1440 

gtggtggtcc tcgcacgtcc tggactggct caagtacggg aagcggctgc tggtggtgca   1500 

ctacgaggag ctgcggcgca gcctggtgcc cacgttacgg gagatggtgg ccttcctcaa   1560 

cgtgtctgtg agcgaggagc ggctgctctg cgtggagaac aacaaggagg gcagcttccg   1620 

gcggcgcggc cggcgctccc acgaccctga gcccttcacc ccggagatga aagacttgat   1680 

caatggctac atccggacgg tggaccaagc cctgcgtgac cacaactgga cggggctgcc   1740 

cagggagtat gtgcccagat gataggcctg gcccacgccg ccgcccccgc tgagtgacgc   1800 

aatcgcacca cggggctgcg ctccccactc tgatgctcag gcccgtggcc tcactgggac   1860 

gaacggtggg tggggggctc accctggtgc tgcctcccgc acaaggagac ctggacacaa   1920 

cagacacaca tcacaaggcg aacacaaatg gacacacata cctggccatg aacccacacc   1980 

tcctcagaca ctcagacacc actccaggct catagcccgt cttgatgcag agaagccccc   2040 

acgtgggtgt gccaggcacc ccagatacaa atgttt                             2076 

 
           
             45  
             2957  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7289372CB1  
             
           
            45 

cataagattg ctttacacca gggttcctga aatcaaggaa aatactggcc aaaatcaccg     60 

accccattct accttcaatt acctagattc tgcgtccccg gcgctaggta cccaatcctg    120 

gctgtccgac cacaggatcc ccggcaggga cgggtcacag tgctctcacc cctcgaccat    180 

tttcgaaaaa accttcctct gcaaacgcat tgcgccctcc ccatgggtcc gcgggcgggg    240 

actccaggcc cgagcagtcg gtgtgaagtt ctgtgttctg aactggggct gagcaagatg    300 

cgatggtctc ntaccgctgg gccgcccgta gcgacggcag gagtaggggt attgatctcc    360 

acggaagccc caaaccctcg ccatcgagag acccccatgg cccggggtga tggctgtggg    420 

gcttggtgct cccagagagc tcagtggcta cagaatgggt ggggattctg cgtgtctccc    480 

ggagcctgaa cccctttcct ggttatggcc ggtagctgtc tccagggact aacgtgggca    540 

gcgcaggggg gcggaaaccg ggttttagcc aaatgcctcg acatcgccgc gcctccgcct    600 

cctcgtcgct gaaagaaatg tcggggtttc atcagagcta gggagcgaca gtcgggaaca    660 

gcgagtctgc cgaagccggc tgttgtgtga gggtgtgaga cggcggggcg gtgaggggcc    720 

accgcggctt gggggatagt gcgtgtgggg ttgaccgtgt gtctgcttga gaggctgtga    780 

agatatgggg ggcagatatg ggagaaatgc tcgggcctga agtccccagc ccaccgtgct    840 

caagagtagc ggacgttttg ccaccatcct tgtctgtgct actgtctgct gcagcttccg    900 

tgccccgttc tcctggagca gggcgtaaaa gcggcttgca ttcaattagc agcgaagctc    960 

gcgggcgctg gcgggacagg cgcgtgaggc cacaacacat gcgtgtatct tgcttgggct   1020 

atcttccctg ctctgccacg ccgggtctgg agaaggggtt tcagccccag gacatttact   1080 

gagagtcggc gaatattggg agccgcgatg ttcccccttc gggccctgtg gttggtctgg   1140 

gcgcttctag gagtggccgg atcatgcccg gagccgtgcg cctgcgtgga caagtacgct   1200 

caccagttcg cggactgcgc ttacaaagag ttgcgtgagg tgccggaagg actgcctgcc   1260 

aacgtgacga cgcttagtct gtccgcgaac aagatcactg tgctgcggcg cggggccttc   1320 

gccgacgtca cacaggtcac gtcgctgtgg ctggcgcaca atgaggtgcg caccgtggag   1380 

ccaggcgcac tggccgtgct gagtcagctc aagaacctcg atctgagcca caacttcata   1440 

tccagctttc cgtggagcga cctgcgcaac ctgagcgcgc tgcagctgct caaaatgaac   1500 

cacaaccgcc tgggctctct gccccgggac gcactcggtg cgctacccga cctgcgttcc   1560 

ctgcgcatca acaacaaccg gctgcgtacg ctggcgcctg gcaccttcga cgcgcttagc   1620 

gcgctgtcac acttgcaact ctatcacaat cccttccact gcggctgcgg ccttgtgtgg   1680 

ctgcaggcct gggccgcgag cacccgggtg tccttacccg agcccgactc cattgcttgt   1740 

gcctcgcctc ccgcgctgca gggggtgccg gtgtaccgcc tgcccgccct gccctgtgca   1800 

ccgcccagcg tgcatctgag tgccgagcca ccgcttgaag cacccggcac cccactgcgc   1860 

gcaggactgg cgttcgtgtt acactgcatc gccgacggcc accctacgcc tcgcctgcaa   1920 

tggcaacttc agatccccgg tggcaccgta gtcttagagc caccggttct gagcggggag   1980 

gacgacgggg ttggggcgga ggaaggagag ggagaaggag atggggattt gctgacgcag   2040 

acccaagccc aaacgccgac tccagcaccc gcttggccgg cgcccccagc cacaccgcgc   2100 

ttcctggccc tcgcaaatgg ctccctgttg gtgcccctcc tgagtgccaa ggaggcgggc   2160 

gtctacactt gccgtgcaca caatgagctg ggcgccaact ctacgtcaat acgcgtggcg   2220 

gtggcagcaa ccgggccccc aaaacacgcg cctggcgccg ggggagaacc cgacggacag   2280 

gccccgacct ctgagcgcaa gtccacagcc aagggccggg gcaacagcgt cctgccttcc   2340 

aaacccgagg gcaaaatcaa aggccaaggc ctggccaagg tcagcattct cggggagacc   2400 

gagacggagc cggaggagga cacaagtgag ggagaggagg ccgaagacca gatcctcgcg   2460 

gacccggcgg aggagcagcg ctgtggcaac ggggacccct ctcggtacgt ttctaaccac   2520 

gcgttcaacc agagcgcaga gctcaagccg cacgtcttcg agctgggcgt catcgcgctg   2580 

gatgtggcgg agcgcgaggc gcgggtgcag ctgactccgc tggctgcgcg ctggggccct   2640 

gggcccggcg gggctggcgg agccccgcga cccgggcggc gacccctgcg cctactctat   2700 

ctgtgtccag cggggggcgg cgcggcagtg cagtggtccc gcgtagagga aggcgtcaac   2760 

gcctactggt tccgcggcct gcggccgggt accaactact ccgtgtgcct ggcgctggcg   2820 

ggcgaagcct gccacgtgca agtggtgttt ccaccaagaa ggagctccca tcgctgctgg   2880 

tcatagtggc agtgagcgta tccctcctgg tgctggccac agtgcccctt ctgggcgccg   2940 

cctgttgcca tctgctg                                                  2957 

 
           
             46  
             1223  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1672338CB1  
             
           
            46 

ggcacctgga gggccgcact cccgttccag ccaggctgag ccttctgtcc cctgcctctg     60 

gggcctggga accccccttc ttctttctcc tgaatggcac ccccgcccta gaatccagac    120 

accgagtttc ccactgtggc tggttcaagg gtatgtgaga gctccctggt gacagtctgt    180 

ggctgagcat ggccctccca gccctgggcc tggacccctg gagcctcctg ggccttttcc    240 

tcttccaact gcttcagctg ctgctgccga cgacgaccgc ggggggaggc gggcaggggc    300 

ccatgcccag ggtcagatac tatgcagggg atgaacgtag ggcacttagc ttcttccacc    360 

agaagggcct ccaggatttt gacactctgc tcctgagtgg tgatggaaat actctctacg    420 

tgggggctcg agaagccatt ctggccttgg atatccagga tccaggggtc cccaggctaa    480 

agaacatgat accgtggcca gccagtgaca gaaaaaagag tgaatgtgcc tttaagaaga    540 

agagcaatga gacacagtgt ttcaacttca tccgtgtcct ggtttcttac aatgtcaccc    600 

atctctacac ctgcggcacc ttcgccttca gccctgcttg taccttcatt gtgagttctc    660 

tggtgcccag cgctcaggcc cccaagcatc ccttctcaca tctacccacg actttcctct    720 

gtagctctgg aaaactctgg ccttccagat gcaggaccct catgaacttc ctggccccag    780 

accaatttcc ctctatgtcc ctttcccttc cttcctcaag cccctcattt cccagatgtg    840 

agaccttggc gttctggccc cccagcctct ctccccattt aggaacttca agattcctac    900 

ctgttgccca tctcggagga caaggtcatg gagggaaaag gccaaagccc ctttgacccc    960 

gctcacaagc atacggctgt cttggtgggt gagtatcagg tttcccactt catcccaaca   1020 

tctactttct ccagtcacgc tgtgaaatat ggaatattac agagttttcc aaaaggcagg   1080 

ggaaactggg tgtggtgatg cgtgcatatg gtcccagtta tttggaagct gaagttgaag   1140 

gatgcttgag tttaggggtt tgagtctagc ctgggcaaca cagcgagatc gtctcaaaaa   1200 

aaaaaaaaaa aaaaaaaaaa aaa                                           1223 

 
           
             47  
             2888  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 184661CB1  
             
           
            47 

cgcacgacgt aaatcctgcg gctacatgag cggctcggaa ttcggctcga gcccggcccg     60 

ggcagctgcg gctcgggatc cgtcgagggg aggccgagct tgccaagctg gcgcccagcg    120 

gggtcatggt gcccggcgcc cgcggcggcg gcgcactggc gcgggctgcc gggcggggcc    180 

tcctggcttt gctgctcgcg gtctccgccc cgctccggct gcaggcggag gagctgggtg    240 

atggctgtgg acacctagtg acttatcagg atagtggcac aatgacatct aagaattatc    300 

ccgggaccta ccccaatcac actgtttgcg aaaagacaat tacagtacca aaggggaaaa    360 

gactgattct gaggttggga gatttggata tcgaatccca gacctgtgct tctgactatc    420 

ttctcttcac cagctcttca gatcaatatg gtccatactg tggaagtatg actgttccca    480 

aagaactctt gttgaacaca agtgaagtaa ccgtccgctt tgagagtgga tcccacattt    540 

ctggccgggg ttttttgctg acctatgcga gcagcgacca tccagattta ataacatgtt    600 

tggaacgagc tagccattat ttgaagacag aatacagcaa attctgccca gctggttgta    660 

gagacgtagc aggagacatt tctgggaata tggtagatgg atatagagat acctctttat    720 

tgtgcaaagc tgccatccat gcaggaataa ttgctgatga actaggtggc cagatcagtg    780 

tgcttcagcg caaagggatc agtcgatatg aagggattct ggccaatggt gttctttcga    840 

gggatggttc cctgtcagac aagcgatttc tgtttacctc caatggttgc agcagatcct    900 

tgagttttga acctgacggg caaatcagag cttcttcctc atggcagtcg gtcaatgaga    960 

gtggagacca agttcactgg tctcctggcc aagcccgact tcaggaccaa ggcccatcat   1020 

gggcttcggg cgacagtagc aacaaccaca aaccacgaga gtggctggag atcgatttgg   1080 

gggagaaaaa gaaaataaca ggaattagga ccacaggatc tacacagtcg aacttcaact   1140 

tttatgttaa gagttttgtg atgaacttca aaaacaataa ttctaagtgg aagacctata   1200 

aaggaattgt gaataatgaa gaaaaggtgt ttcagggtaa ctctaacttt cgggacccag   1260 

tgcaaaacaa tttcatccct cccatcgtgg ccagatatgt gcgggttgtc ccccagacat   1320 

ggcaccagag gatagccttg aaggtggagc tcattggttg ccagattaca caaggtaatg   1380 

attcattggt gtggcgcaag acaagtcaaa gcaccagtgt ttcaactaag aaagaagatg   1440 

agacaatcac aaggcccatc ccctcggaag aaacatccac aggaataaac attacaacgg   1500 

tggctattcc attggtgctc cttgttgtcc tggtgtttgc tggaatgggg atctttgcag   1560 

cctttagaaa gaagaagaag aaaggaagtc cgtatggatc agcagaggct cagaaaacag   1620 

actgttggaa gcagattaaa tatccctttg ccagacatca gtcagctgag tttaccatca   1680 

gctatgataa tgagaaggag atgacacaaa agttagatct catcacaagt gatatggcag   1740 

attaccagca gcccctcatg attggcaccg ggacagtcac gaggaagggc tccaccttcc   1800 

ggcccatgga cacggatgcc gaggaggcag gggtgagcac cgatgccggc ggccactatg   1860 

actgcccgca gcgggccggc cgccacgagt acgcgctgcc ctggcgcccc cggagcccga   1920 

gtacgccacg cccatcgtgg agcggcacgt gctgcgcgcc cacacgttct ctgcgcagag   1980 

cggctaccgc gtcccagggc cccagcccgg ccacaaacac tccctctcct cgggcggctt   2040 

ctcccccgta gcgggtgtgg gcgcccagga cggagactat caaaggccac acagcgcaca   2100 

gcctgcgggc aggggctacg accggcccaa agctgtcagc gccctcgcca ccgaaagcgg   2160 

acaccctgac tctcagaagc ccccaacgca tcccgggacg agtgacagct attctgcccc   2220 

cagagactgc ctcacacccc tcaaccagac ggccatgact gcccttttgt gaacacaatg   2280 

tgaaagaagc ctgctgtggt actgagcgtc gggctgtcac aaggcactgg aagaagggag   2340 

cctgctggtc cagagtgtgc gtgtgtatcg gtgtgtgtgt acacttgcat gtgtgtgtgt   2400 

gatccagtag gatcctagag acaacctgtc atactgttta caaaattgtg cagctggttt   2460 

cgtgctgacc cttagggtgc gtctgttggg ttttgttggg ctagaaaaat gaaaattttt   2520 

agatggcgtt ttcattcctc tgactgatat tgagctgctt tggtgttaaa ggtgtaatgt   2580 

gtacagagtt gtatttaaca ataataaaag taacttaagt ttgctctatc agattttagt   2640 

tctgcacaga ggttaagtgg gaaaatgcag ctgttgcaaa atgtatataa atagtatgtt   2700 

catttttttc agtatattat ctgatactgt gttagcagca ggtctgtctt aaacctagtc   2760 

ttgttgttat ttgagtcatt tcctctcctt tgataactag aactgaaagc atttttaaca   2820 

ttcttctcct ggaagaaatg aattacttga agcatgaaaa gcacaccagg gtggttgttt   2880 

atttagca                                                            2888 

 
           
             48  
             3142  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3719737CB1  
             
           
            48 

tgcgcgcagg ctcacaggcc ctgggagtga gctggtgccc ggcgacctgg cacccgcgcc     60 

tggatatggg gcgtctacat cgtcccagga gcagcaccag ctacaggaac ctgccgcatc    120 

tgtttctgtt tttcctcttc gtgggaccct tcagctgcct cgggagttac agccgggcca    180 

ccgagcttct gtacagccta aacgagggac tacccgcggg ggtgctcatc ggcagcctgg    240 

ccgaggacct gcggctgctg cccaggtctg cagggaggcc ggacccgcag tcgcagctgc    300 

cagagcgcac cggtgctgag tggaaccccc ctctctcctt cagcctggcc tcccggggac    360 

tgagtggcca gtacgtgacc ctagacaacc gctctgggga gctgcacact tcagctcagg    420 

agatcgacag ggaggccctg tgtgttgaag ggggtggagg gactgcgtgg agcggcagcg    480 

tttccatctc ctcctctcct tctgactctt gtcttttgct gctggatgtg cttgtcctgc    540 

ctcaggaata cttcaggttt gtgaaggtga agatcgccat cagagacatc aatgacaacg    600 

ccccgcagtt ccctgtttcc cagatctcgg tgtgggtccc ggaaaatgca cctgtaaaca    660 

cccgactggc catagagcat cctgctgtgg acccagatgt aggcattaat ggggtacaga    720 

cctatcgctt actggactac catggtatgt tcaccctgga cgtggaggag aatgagaatg    780 

gggagcgcac cccctaccta attgtcatgg gtgctttgga cagggaaacc caggaccagt    840 

atgtgagcat catcatagct gaggatggtg ggtctccacc acttttgggc agtgccactc    900 

tcaccattgg catcagtgac attaatgaca attgccctct cttcacagac tcacaaatca    960 

atgtcactgt gtatgggaat gctacagtgg gcaccccaat tgcagctgtc caggctgtgg   1020 

ataaagactt ggggaccaat gctcaaatta cttattctta cagtcagaaa gttccacaag   1080 

catctaagga tttatttcac ctggatgaaa acactggagt cattaaactt ttcagtaaga   1140 

ttggaggaag tgttctggag tcccacaagc tcaccatcct tgctaatgga ccaggctgca   1200 

tccctgctgt aatcactgct cttgtgtcca ttattaaagt tattttcaga ccccctgaaa   1260 

ttgtccctcg ttacatagca aacgagatag atggtgttgt ttatctgaaa gaactggaac   1320 

ccgttaacac tcccattgcg tttttcacca taagagatcc agaaggtaaa tacaaggtta   1380 

actgctacct ggatggtgaa gggccgttta ggttatcacc ttacaaacca tacaataatg   1440 

aatatttact agagaccaca aaacctatgg actatgagct acagcagttc tatgaagtag   1500 

ctgtggtggc ttggaactct gagggatttc atgtcaaaag ggtcattaaa gtgcaacttt   1560 

tagatgacaa tgataatgct ccaattttcc ttcaaccctt aatagaacta accatcgaag   1620 

agaacaactc acccaatgcc tttttgacta agctgtatgc tacagatgcc gacagcgagg   1680 

agagaggcca agtttcatat tttctgggac ctgatgctcc atcatatttt tccttagaca   1740 

gtgtcacagg aattctgaca gtttctactc agctggaccg agaagagaaa gaaaagtaca   1800 

gatacactgt cagagctgtt gactgtggga agccacccag agaatcagta gccactgtgg   1860 

ccctcacagt gttggataaa aatgacaaca gtcctcggtt tatcaacaag gacttcagct   1920 

tttttgtgcc tgaaaacttt ccaggctatg gtgagattgg agtaattagt gtaacagatg   1980 

ctgacgctgg acgaaatgga tgggtcgccc tctctgtggt gaaccagagt gatatttttg   2040 

tcatagatac aggaaagggt atgctgaggg ctaaagtctc tttggacaga gagcagcaaa   2100 

gctcctatac tttgtgggtt gaagctgttg atgggggtga gcctgccctc tcctctacag   2160 

caaaaatcac aattctcctt ctagatatca atgacaaccc tcctcttgtt ttgtttcctc   2220 

agtctaatat gtcttatctg ttagtactgc cttctactct gccaggctcc ccggttacag   2280 

aagtctatgc tgtcgacaaa gacacaggca tgaatgctgt catagcttac agcatcatag   2340 

ggagaagagg tcctaggcct gagtccttca ggattgaccc taaaactggc aacattactt   2400 

tggaagaggc attgctgcag acagattatg ggctccatcg cttactggtg aaagtgagtg   2460 

atcatggtta tcccgagcct ctccactcca cagtcatggt gaacctattt gtcaatgaca   2520 

ctgtcagtaa tgagagttac attgagagtc ttttaagaaa agaaccagag attaatatag   2580 

aggagaaaga accacaaatc tcaatagaac cgactcatag gaaggtagaa tctgtgtctt   2640 

gtatgcccac cttagtagct ctgtctgtaa taagcttggg ttccatcaca ctggtcacag   2700 

ggatgggcat atacatctgt ttaaggaaag gggaaaagca tcccagggaa gatgaaaatt   2760 

tggaagtaca gattccactg aaaggaaaaa ttgacttgca tatgcgagag agaaagccaa   2820 

tggatatttc taatatttga tatttcatgg tggaataaca cagagaaatg ttttaactga   2880 

ctttggatct tcatcaccta aaaaagagtg tgttgatggc agttccaatg aaggacaact   2940 

aatttataac ttgttctata ttgtaaatag ctgtttacag gtttttaaat ttaaattcag   3000 

aggttataaa atgtgtacag catttttaag tgaaaattag tactaacagc tataggactt   3060 

gtatttaaaa aaaaaaaaaa aaagcttgga catggtttgc agctttcata caccaagcag   3120 

atgtttgata aaacctgggg gt                                            3142 

 
           
             49  
             4749  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5773251CB1  
             
           
            49 

gtgcttgcag tggtggaatt cctagagcgt taaatattca gtgataagtg ggcagggttg     60 

aggctgaaaa gatagatagg ggccaggtca aagtgggtta atttatgtgc tgtttgtacc    120 

aacaagcttg gactttggta ttgtgacagg cagttaggag gcattcaaga cttaagcaga    180 

gtgacatggt aaaattactc cagaaaacgt tcaaattata tttgatgatc cactaccaat    240 

ttcatacagt cagccagaga aggtgaatgg agagtccaag agcagcagta ccagcgagag    300 

tggggacagt gataacatga ggatttccag ctgcagcgat gaaagtagta acagcaacag    360 

cagtcgtaag agtgacaatc attcaccagc tgtggtcact accactgtga gcagcaaaaa    420 

gcagccatca gttcttgtta catttccaaa ggaagagaga aaatctgttt ctggcaaggc    480 

ttcaataaaa ttgtcagaaa ctatcagtga agggaccagt aattctctat ctacttgtac    540 

aaaatctggt ccatctcccc tttcttctcc aaatgggaag ttaacagtag caagtcctaa    600 

gcgtgggcaa aagagggaag aaggatggaa agaagttgta agaaggtcaa agaaagtcgg    660 

aggctggctt tggctgcgaa aagagaaaaa agaaaagaga agagaaggaa gaaaaaggaa    720 

gaacaaagaa ggaaactaga agaaattgaa gccaaaaata aaagagaact ttgaactcca    780 

agctgctcaa gaaaaagaaa agcttaaagt tgaagatgag cctgaagtct tgacagaacc    840 

tccaagtgcc acaaccacta ctaccatagg tatatctgca acctggacaa ctttggcagg    900 

ttctcatggt aaaagaaata ataccataac tacaaccagt tcaaagagga aaaacaggaa    960 

aaataaaatt actccagaaa acgttcaaat tatatttgat gatccactac caatttcata   1020 

cagtcagcca gagaaggtga atggagagtc caagagcagc agtaccagcg agagtgggga   1080 

cagtgataac atgaggattt ccagctgcag cgatgaaagt agtaacagca acagcagtcg   1140 

taagagtgac aatcattcac cagctgtggt cactaccact gtgagcagca aaaagcagcc   1200 

atcagttctt gttacatttc caaaggaaga gagaaaatct gtttctggca aggcttcaat   1260 

aaaattgtca gaaactatca gtgaagggac cagtaattct ctatctactt gtacaaaatc   1320 

tggtccatct cccctttctt ctccaaatgg gaagttaaca gtagcaagtc ctaagcgtgg   1380 

gcaaaagagg gaagaaggat ggaaagaagt tgtaagaagg tcaaagaaag tatctgttcc   1440 

atcaactgtg atatccagag tgattggaag aggaggctgt aatatcaatg ctattcggga   1500 

gtttactggt gcacacatag atattgataa acagaaagac aagactggag accggataat   1560 

cactataagg ggtggcactg aatcaacaag acaagcaact caattgatta atgctttgat   1620 

caaggatcca gacaaagaaa ttgatgaact tattccaaag aatcgtttga aaagctcctc   1680 

agcaaattcc aaaatagggt catcagcacc taccaccact gctgctaaca cttccttaat   1740 

gggaattaaa atgacaactg tagctctgtc atcaacatct caaactgcca cagcactcac   1800 

tgtgcctgca atttcttctg catccactca caaaaccatt aagaacccag tgaataatgt   1860 

gaggcctggt tttccagttt ctcttccatt agcatatcct cctccacagt ttgcacatgc   1920 

tttgcttgct gctcagactt tccagcagat ccgtccacca aggttgccca tgacccactt   1980 

tggaggtact tttccaccag ctcaatccac ttggggtccg tttcctgtca ggcctttgag   2040 

ccctgccaga gctactaact cgcctaagcc tcacatggtg cctcgccata gcaatcagaa   2100 

tagcagtggt tctcaggtga attcagcagg ttctttaact tcaagcccaa caactacaac   2160 

cagttcatca gcttcaacgg tgcctggtac atctacaaat ggcagtccaa gttcaccttc   2220 

tgtccgaagg cagctttttg tcacagttgt gaagacatcc aatgccacca caacaacagt   2280 

cacaaccacg gcaagcaaca acaacactgc acccacaaat gccacatatc ctatgcctac   2340 

tgccaaagaa cactatccag tatcatcccc atcttcccca tcaccaccag cccagccagg   2400 

aggggtttct agaaacagcc ctttggattg tggatcagca tctccaaata aagtggcatc   2460 

ttcctccgaa caggaagcag gtagtccacc agtagtagaa acaacaaaca ctagacctcc   2520 

aaacagcagc agttcttctg ggagttcatc agctcattct aatcagcaac aacctccggg   2580 

atctgtttct caggaaccaa gaccacctct tcagcagtct caggttcctc ccccggaagt   2640 

tagaatgact gttcctcctt tagcaacaag ttctgctcca gtggcggtgc cttctactgc   2700 

cccagtgact taccctatgc ctcagacacc aatgggatgc ccccagccta ctcctaaaat   2760 

ggaaacccct gctattagac caccccctca tggcacaact gcccctcaca agaattcagc   2820 

ttcagtgcaa aattcatctg ttgcagtcct tagtgtcaat cacattaaaa gacctcacag   2880 

tgttccctct tctgtccagc taccttcgac cttaagtaca caaagtgctt gtcagaattc   2940 

agtacatcca gcaaataagc ctattgctcc caatttcagt gcccccttac catttgggcc   3000 

ctttagcaca ttgtttgaaa acagccctac ttctgctcat gccttctggg gaggatctgt   3060 

tgtttcatct cagtcaacac cagaatctat gctatcagga aaatcctcat atttgccaaa   3120 

ttcagatcct ttacatcagt ctgatacttc caaagctcca ggttttagac caccattaca   3180 

gagacctgct ccaagtccct caggtattgt caatatggac tcgccatatg gttctgtaac   3240 

accttcttca acacatttgg gaaactttgc ttcaaacatt tcaggaggtc agatgtacgg   3300 

acctggggca ccccttggag gagcacccgc agctgctaac tttaacagac aacatttttc   3360 

cccgcttagt ttgttgactc cgtgttcatc agcatcaaat gattcttctg cacagtcagt   3420 

atcctcggga gttcgtgcac catctcctgc cccatcatca gtaccgttag ggtcagaaaa   3480 

gcccagcaat gtgtctcagg acaggaaagt tccagtccct attgggactg aacgttctgc   3540 

acgtatcagg caaactggaa cgtcagctcc atctgttatt gggagcaatt tgtctacatc   3600 

agtaggacat agtggcatct ggtcctttga agggattggt ggcaatcaag acaaagtaga   3660 

ctggtgtaac cctgggatgg gaaatcctat gatccacaga ccgatgtctg acccaggagt   3720 

attttcacaa catcaagcaa tggagcgaga tagtacagga attgtaactc cttctggtac   3780 

attccatcag catgttcctg caggctacat ggactttcct aaagttgggg gtatgccttt   3840 

ttctgtgtat gggaatgcaa tgattcctcc agtagcacct atccctgatg gtgctggagg   3900 

acccatattt aatggccctc atgctgcaga cccttcttgg aactcactga taaagatggt   3960 

ttccagctcc acggaaaata atggccctca aacggtgtgg actggaccct gggcacctca   4020 

catgaacagt gtgcatatga accagcttgg ctgatgagga tcagcttgtt agcctgcaga   4080 

ttccttttca tttggaggaa atcacaagtg gccgaaaaaa aaaattatgc tcccaaatca   4140 

ttctactgat gtgcttgact gaagtgtgta ggctttttgc agaagatctt actaactgac   4200 

ctattttctg tgaacatttg tgactgccca ttccccatca tcatccgttt taccttagtt   4260 

agcatttttc ttatcatttt tctttttttc tttccctctt cccctttgga cataactttc   4320 

tgttgaagct gttctttggc tggttggttt tagtactgta aactgcttct gagcaaacac   4380 

ggaaatttag caaaattatg taaacttgat cctgaagttt tagaatggca aataaatgta   4440 

caattgttta cataacagaa aaggctaagc agaaagtaaa tttcaatatg tcagtataga   4500 

ggctctactt tatgtagact taaattaatg tgagatatgt accttcatat tcagaaatct   4560 

ggatgtttcc ttcatacatt aaactattaa taagcataac ttttctactg gtgtaattta   4620 

agtataaagt aaaataatgg gcattatcat tggatgtttc cccacattgg cttttaaaat   4680 

acccatcttg ctttcttttt ggtttatttg tagcaaggca catatagaag aagaaatttc   4740 

tggcttttc                                                           4749 

 
           
             50  
             4155  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5426470CB1  
             
           
            50 

gccgtcgggg cgggcgtctg gcgagctgca gagaccagat taaaggattt acctgaagag     60 

aaagcattct attcatcaga gactggacaa gagttactct tgcatttggc aattaaagat    120 

gatgtttcca tggaaacagt tgatcctgct ttcattcatt ggctgcttag gaggtgagct    180 

tctcttacaa ggccctgtat ttatcaaaga acccagcaac agcattttcc ctgttggttc    240 

agaagataaa aaaataactt tgcattgtga agcaagaggc aatccatcac ctcattacag    300 

atggcagctg aatggaagtg atattgatat gagtatggaa catcgttata agttgaatgg    360 

aggaaatctt gtggttatta atcccaacag aaattgggat acaggaactt accaatgttt    420 

tgcaacaaat tcacttggaa caattgtcag cagagaagcc aaacttcagt ttgcctatct    480 

tgaaaatttt aaaaccaaaa tgaggagtac agtgtctgtg cgtgaaggcc agggagttgt    540 

gctgctctgc ggccccccac cacactctgg agaactgtca tatgcttgga tcttcaatga    600 

atacccatcg tttgttgaag aagatagtcg gagatttgtc tcccaggaga cagggcacct    660 

ctacatatct aaggtggagc cgtctgatgt gggaaattac acatgtgtgg tgacaagtat    720 

ggtgacaaat gcccgagtgc tgggctctcc aactcctttg gtgctacgtt ctgatggtgt    780 

gatgggtgaa tatgaaccta aaatagaagt tcagtttcca gaaactcttc cagcagctaa    840 

aggttcgact gtgaaattgg aatgttttgc ccttggaaat cccatacctc agattaattg    900 

gagaagaagt gatgggctgc cattttccag caaaattaaa ttaaggaagt tcagtggtgt    960 

gcttgaaatc cccaacttcc aacaggaaga tgcaggttcc tatgaatgca ttgctgagaa   1020 

ttcacgagga aaaaatgttg ccagagggcg tctcacttac tatgcaaagc cccattgggt   1080 

tcaactcata aaggatgtgg aaatagccgt ggaggacagt ctttattggg aatgcagggc   1140 

aagcggcaag cccaagcctt cctaccgatg gctgaaaaat ggagcagccc tggtgctaga   1200 

ggagagaaca cagatagaaa atggtgccct tacaatatca aacctaagtg tgactgattc   1260 

tggcatgttc caatgcatag cagaaaacaa acatggcctt gtttattcca gtgctgagct   1320 

caaagttgtt gcttctgctc cagatttttc aaagaatcca atgaagaagt tggttcaggt   1380 

gcaggtgggc agcctggtca gcttggattg taaacccaga gcctccccaa gggcactctc   1440 

ttcctggaag aagggggatg tgagcgtgca ggagcatgaa agaatttctt tgttaaacga   1500 

tggaggactc aaaatagcca atgtgactaa agctgatgct ggaacttaca cctgcatggc   1560 

agaaaaccag tttgggaaag caaatggcac aacacatttg gttgttacgg aaccaacaag   1620 

aataactttg gcaccatcta acatggatgt ttctgttggt gaaagcgtca tattgccctg   1680 

ccaggtacaa catgacccgc tgttagacat catctttacc tggtatttca atggggccct   1740 

tgcagatttt aagaaagatg gatctcactt tgagaaagtt ggtgggagtt catctggtga   1800 

tttaatgatc agaaacattc agctgaaaca cagtgggaaa tatgtttgta tggtgcaaac   1860 

gggggtggac agtgtttcat ctgctgctga cctcatagta agaggttcac ctggaccacc   1920 

agaaaatgtg aaggtagatg aaattacaga cacaacagcc caactctctt ggaaagaagg   1980 

taaagacaac catagcccag ttatatccta ttctatccag gctcggacac ctttctccgt   2040 

gggttggcaa accgtcacaa cagtgcctga ggtcatcgat gggaagacgc acacagccac   2100 

tgtagttgag ttaaacccat gggtggaata tgaatttcgg gttgtagcca gtaacaaaat   2160 

tggaggtgga gaaccaagtt taccctcaga aaaagtaaga actgaagagg cagttccaga   2220 

agtgcctcct tctgaagtca atggaggagg cggaagccgg tctgaacttg tgataacctg   2280 

ggatccagtc cctgaagaac tacagaatgg tgaaggtttt gggtatgttg ttgctttccg   2340 

ccctcttggg gttaccacct ggatccagac agtggtgaca tcccctgaca ccccaagata   2400 

tgtctttagg aatgaaagca tcgtgccata ttcaccatat gaagttaaag tgggtgttta   2460 

taataacaaa ggtgaaggac catttagccc agtgacaaca gtgttctctg cagaagaaga   2520 

gcctacagtg gccccatctc aagtctctgc aaatagccta tcttcctcag aaattgaggt   2580 

ttcatggaac accattcctt ggaagttgag caatggacat ttactgggct atgaggtgcg   2640 

gtactggaat gggggtggaa aggaggaatc atccagtaag atgaaagtgg caggaaatga   2700 

gacatcagcc agactacggg gcctgaagag caacctggcc tattacacgg ctgtccgggc   2760 

ttacaacagt gccggcgctg ggccttttag cgccacagtt aatgtaacca ccaagaaaac   2820 

gcctcccagt cagccaccag gaaatgttgt ttggaatgcc acagacacta aagtgttact   2880 

taattgggag caagttaaag ccatggagaa tgagtcagaa gtaacaggat ataaagtttt   2940 

ctataggact agcagtcaaa ataacgtaca agtactgaac acaaataaaa cttcagctga   3000 

acttgtgctg cccattaaag aggactacat tattgaagtc aaggccacaa cagatggagg   3060 

ggatgggacc agtagtgaac agatcaggat tccacgaata accagtatgg atgcaagagg   3120 

atccacttca gccatctcga atgtccaccc tatgtcaagt tatatgccta tagtactgtt   3180 

cttaattgta tatgtcctgt ggtgatatta actccttttt attatttatt ggaaagttat   3240 

ttggttacca aaaaaagtgc tttcatgaaa tgcagtgatt atgcatgttt ttttcaactc   3300 

ttatttttaa ctttctactt cattataggt aaatatgaat ataattaaaa aaacagtaaa   3360 

tccttttagg ggaatctgaa atgccttaat attaacttga taaaccaaag gaatttacat   3420 

attacatact tcagactttt gatataaatg ttcttaaact atgagtttaa gcactgccta   3480 

tggataaaga ctcacacact ctcacatgta cacacacacg catgagaatt tctttttaca   3540 

ttgaaaaact ctttcattta attcaaatgc tattttccca ttataatagc attatttgga   3600 

agacttaacc agtatcaatt tgaaatgctg atttaagtcc ccaaggatga aaaatacatt   3660 

ttaaaaatta ttttgttgga gaggagtggc atgtgattca aaagagcatt gttggaaaat   3720 

gctactgtgg ggcttagaag aatgatgttt ggtttggtat gctgctaact agttgtaaga   3780 

ctttacaaat cactttgcca tctgtacctc tcaattattc ctctataaaa tatggagata   3840 

ataataccta tctgatcaga ctttgcccca tgaattagtt tttaaaagat aaagactgaa   3900 

gtatgaaagt gcttttgtca ccccaaatgc aattgaccca tgcaaaatat tagcatgaat   3960 

ttatttaatc acataaaagt catgaagacc agccagattt tcaagcttca ttctgtttca   4020 

ttcagttata ttccaaaatt caaatgatca cattttattc tttctcaaaa aaaaaaaagt   4080 

ttttttaaat taaaaaagga attgtttcct tcacagctat gaataagctt tcaggtttta   4140 

ttaaaaccta gagga                                                    4155 

 
           
             51  
             1327  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7087904CB1  
             
           
            51 

gcgagctgaa agctgctgga gagtgagcag ccctagcagg gatggacatg atgctgttgg     60 

tgcagggtgc ttgttgctcg aaccagtggc tggcggcggt gctcctcagc ctgtgctgcc    120 

tgctaccctc ctgcctcccg gctggacaga gtgtggactt cccctgggcg gccgtggaca    180 

acatgatggt cagaaaaggg gacacggcgg tgcttaggtg ttatttggaa gatggagctt    240 

caaagggtgc ctggctgaac cggtcaagta ttatttttgc gggaggtgat aagtggtcag    300 

tggatcctcg agtttcaatt tcaacattga ataaaaggga ctacagcctc cagatacaga    360 

atgtagatgt gacagatgat ggcccataca cgtgttctgt tcagactcaa catacaccca    420 

gaacaatgca ggtgcatcta actgtgcaag ttcctcctaa gatatatgac atctcaaatg    480 

atatgaccgt caatgaagga accaacgtca ctcttacttg tttggccact gggaaaccag    540 

agccttccat ttcttggcga cacatctccc catcagcaaa accatttgaa aatggacaat    600 

atttggacat ttatggaatt acaagggacc aggctgggga atatgaatgc agtgcggaaa    660 

atgatgtgtc attcccagat gtgaggaaag taaaagttgt tgtcaacttt gctcctacta    720 

ttcaggaaat taaatctggc accgtgaccc ccggacgcag tggcctgata agatgtgaag    780 

gtgcaggtgt gccgcctcca gcctttgaat ggtacaaagg agagaagaag ctcttcaatg    840 

gccaacaagg aattattatt caaaatttta gcacaagatc cattctcact gttaccaacg    900 

tgacacagga gcacttcggc aattatactt gtgtggctgc caacaagcta ggcacaacca    960 

atgcgagcct gcctcttaac cctccaagta cagcccagta tggaattacc gggagcgctg   1020 

atgttctttt ctcctgctgg taccttgtgt tgacactgtc ctctttcacc agcatattct   1080 

acctgaagaa tgccattcta caataaattc aaagacccat aaaaggcttt taaggattct   1140 

ctgaaagtgc tgatggctgg atccaatctg gtacagttgt taaaagcgcg tgggatttat   1200 

cagcagtgct acctgggatg accgctttgg aaaatgccct tatttatcct tatccaccct   1260 

tttgaaagaa ctccttgagg cgacattgcc tttaaacgac gcgaatctaa gatacggccg   1320 

ttgcacc                                                             1327 

 
           
             52  
             5529  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477312CB1  
             
           
            52 

atgcagctga gccgcgccgc cgccgccgcc gccgccgccc ctgcggagcc cccggagccg     60 

ctgtcccccg cgccggcccc ggccccggcc ccccccggcc ccctcccgcg cagcgcggcc    120 

gacggggctc cggcgggggg gaaggggggg ccggggcgcc gcgcgcggag tccccgggcg    180 

ctccgttccc cggcgcgagc ggccccggcc cgggccccgg cgcggggatg gacggccccg    240 

gggccagggg ccagcgccgt ggtcgtgcgc gtcggcatcc cggacctgca gcagacgaag    300 

tgcctgcgcc tggacccggc cgcgcccgtg tgggccgcca agcagcgcgt gctctgcgcc    360 

ctcaaccaca gcctccagga cgcgctcaac tatgggcttt tccagccgcc ctcccggggc    420 

cgcgccggca agttcctgga tgaggagcgg ctcctgcagg agtacccgcc caacctggac    480 

acgcccctgc cctacctgga gtttcgatac aagcggcgag tttatgccca gaacctcatc    540 

gatgataagc agtttgcaaa gcttcacaca aaggcgaacc tgaagaagtt catggactac    600 

gtccagctgc atagcacgga caaggtggca cgcctgttgg acaaggggct ggaccccaac    660 

ttccatgacc ctgactcagg agagtgcccc ctgagcctcg cagcccagct ggacaacgcc    720 

acggacctgc taaaggtgct gaagaatggt ggtgcccacc tggacttccg cactcgcgat    780 

gggctcactg ccgtgcactg tgccacacgc cagcggaatg cggcagcact gacgaccctg    840 

ctggacctgg gggcttcacc tgactacaag gacagccgcg gcttgacacc cctctaccac    900 

agcgccctgg ggggtgggga tgccctctgc tgtgagctgc ttctccacga ccacgctcag    960 

ctggggacca ccgacgagaa tggctggcag gagatccacc aggcctgccg ctttgggcac   1020 

gtgcagcatc tggagcacct gctgttctat ggggcagaca tgggggccca gaacgcctcg   1080 

gggaacacag ccctgcacat ctgtgccctc tacaaccagg agagctgtgc tcgtgtcctg   1140 

ctcttccgtg gagctaacag ggatgtccgc aactacaaca gccagacagc cttccaggtg   1200 

gccatcatcg cagggaactt tgagcttgca gaggttatca agacccacaa agactcggat   1260 

gttggacagg acagtcatga cttgctacat cctatgccca ctggggtccc agagtggggc   1320 

ctgtacacag aagaggaact ggaaggaggt gccgccttct ctgtaccatt cagggaaacc   1380 

cccagctatg cgaagcggcg gcgactggct ggccccagtg gcttggcatc ccctcggcct   1440 

ctgcagcgct cagccagcga tatcaacctg aagggggagg cacagccagc agcttctcct   1500 

ggaccctcgc tgagaagcct cccccaccag ctgctgctcc agcggctgca agaggagaaa   1560 

gatcgtgacc gggatgccga ccaggagagc aacatcagtg gccctttagc aggcagggcc   1620 

ggccaaagca agatcaggag ctgtattcga attcgagctc ggttccccgc gccccctgcg   1680 

ccccccgcac cgccgccccg gggcccgaag cggaaacttt acagcgccgt ccccggccgc   1740 

aagttcatcg ccgtgaaggc gcacagcccg cagggtgaag gcgagatccc gctgcaccgc   1800 

ggcgaggccg tgaaggtgct cagcattggg gagggcggtt tctgggaggg aaccgtgaaa   1860 

ggccgcacgg gctggttccc ggccgactgc gtggaggaag tgcagatgag gcagcatgac   1920 

acacggcctg aaacgcggga ggaccggacg aagcggctct ttcggcacta cacagtgggc   1980 

tcctacgaca gcctcacctc acacagcgat tatgtcattg atgacaaagt ggctgtcctg   2040 

cagaaacggg accacgaggg ctttggtttt gtgctccggg gagccaaagc agagaccccc   2100 

atcgaggagt tcacgcccac gccagccttc ccggcgctgc agtatctcga gtcggtggac   2160 

gtggagggtg tggcctggag ggccgggctg cgcacgggag acttcctcat cgaggtgaac   2220 

ggggtgaacg tggtgaaggt cggacacaag caggtggtgg ctctgattcg ccagggtggc   2280 

aaccgcctcg tcatgaaggt tgtgtctgtg acaaggaagc cagaagagga cggggctcgg   2340 

cgcagagccc caccgccccc caagagggcc cccagcacca cactgaccct gcgctccaag   2400 

tccatgacag ctgagctcga ggaacttgag aagctggacg agatgctggc agccgccgca   2460 

gagccaacgc tgcggccaga catcgcagac gcagactcca gagccgccac cgtcaaacag   2520 

aggcccacca gtcggaggat cacacccgcc gagattagct cattgtttga acgccagggc   2580 

ctcccaggcc cagagaagct gccgggctcc ttgcggaagg ggattccacg gaccaagtct   2640 

gtaggggagg acgagaagct ggcgtccctg ctggaagggc gcttcccgcg gagcacctcg   2700 

atgcaagacc cggtgcgcga gggtcgcggc atcccgcccc cgccgcagac cgcgccgcct   2760 

cccccgcccg cgccctacta cttcgactcg gggccgcccc cggccttctc gccgccgccc   2820 

ccgccgggcc gcgcctacga cacggtgcgc tccagcttca agcccggcct ggaggcgcgc   2880 

ctgggcgcgg gcgctgccgg cctgtacgag ccgggcgcgg ccctcggccc gctgccgtat   2940 

cccgagcggc agaagcgcgc gcgctccatg atcatcctgc aggactcggc gcccgagtcg   3000 

ggcgacgccc ctcgaccccc gcccgcggcc accccgcccg agcgacccaa gcgccggccg   3060 

cggccgcccg gccccgacag cccctacgcc aacctgggcg ccttcagcgc cagcctcttc   3120 

gctccgtcca agccgcagcg ccgcaagagc cccctggtga agcagctgca ggtggaggac   3180 

gcgcaggagc gcgcggccct ggccgtgggc agccccggtc ccggcggcgg cagcttcgcc   3240 

cgcgagccct ccccgaccca ccgcggtccg cgcccgggtg gcctcgacta cggcgcgggc   3300 

gatggcccgg ggctcgcgtt cggcggcccg ggcccggcca aggaccggcg gctggaggag   3360 

cggcgccgct ccactgtgtt cctgtccgtg ggggccatcg agggcagcgc ccccggcgcg   3420 

gatctgccat ccctacagcc ctcccgctcc atcgacgagc gcctcctggg gaccggcccc   3480 

accgccggcc gcgacctgct gctgccctcc ccggtgtctg ccctgaagcc gttggtcagc   3540 

ggcccgagcc tggggccctc gggttccacc ttcatccacc cactcaccgg caaacccctg   3600 

gaccccagct cacccctggc ccttgccctg gctgcccgag agcgagctct ggcctcccag   3660 

gcgccctccc ggtcccccac acccgtgcac agtcccgacg ccgaccgccc cggacccctg   3720 

tttgtggatg tacaggcccg ggacccagag cgagggtccc tggcttcccc ggctttctcc   3780 

ccacggagcc cagcctggat tcctgtgcct gctcgcaggg aggcagagaa ggtcccccgg   3840 

gaggagcgga agtcacccga ggacaagaag tccatgatcc tcagcgtcct ggacacatcc   3900 

ctgcagcggc cagctggcct catcgttgtg cacgccacca gcaacgggca ggagcccagc   3960 

aggctggggg gggccgaaga ggagcgcccg ggcaccccgg agttggcccc ggcccccatg   4020 

cagtcagcgg ctgtggcaga gcccctgccc agcccccggg cccagccccc tggtggcacc   4080 

ccggcagacg ccgggccagg ccagggcagc tcagaggaag agccagagct ggtgtttgct   4140 

gtgaacctgc cacctgccca gctgtcgtcc agcgatgagg agaccaggga ggagctggcc   4200 

cgaattgggt tggtgccacc ccctgaagag tttgccaacg gggtcctgct ggccacccca   4260 

ctcgctggcc cgggcccctc gcccaccacg gtgcccagcc cggcctcagg gaagcccagc   4320 

agtgagccac cccctgcccc tgagtctgca gccgactctg gggtggagga ggctgacaca   4380 

cgcagctcca gcgaccccca cctggagacc acaagcacca tctccacggt gtccagcatg   4440 

tccaccttga gctcggagag cggggaactc actgacaccc acacctcctt cgctgacgga   4500 

cacacttttc tactcgagaa gccaccagtg cctcccaagc ccaagctcaa gtccccgctg   4560 

gggaaggggc cggtgacctt cagggacccg ctgctgaagc agtcctcgga cagcgagctc   4620 

atggcccagc agcaccacgc cgcctctgcc gggctggcct ctgccgccgg gcctgcccgc   4680 

cctcgctacc tcttccagag aaggtccaag ctatgggggg accccgtgga gagccggggg   4740 

ctccctgggc ctgaagacga caaaccaact gtgatcagtg agctcagctc ccgcctgcag   4800 

cagctgaaca aggacacgcg ttccctgggg gaggaaccag ttggtggcct gggcagcctg   4860 

ctggaccctg ccaagaagtc gcccatcgca gcagctcggc tcttcagcag cctcggtgag   4920 

ctgagctcca tttcagcgca gcgcagcccc gggggcccgg gcggcggggc ctcgtactcg   4980 

gtgaggccca gtggccgcta ccccgtggcg agacgcgccc cgagcccggt gaagcccgcg   5040 

tcgctggagc gggtggaggg gctgggggcg ggcgcggggg gcgcagggcg gcccttcggc   5100 

ctcacgcccc ccaccatcct caagtcgtcc agcctctcca tcccgcacga gcccaaggag   5160 

gtgcgcttcg tggtgcgcag cgtgagcgcg cgcagtcgct ccccctcgcc gtcgccgctg   5220 

ccctcgcccg cgtccggccc cggccccggc gcccccggcc cacgccgacc cttccagcag   5280 

aagccgctgc agctctggag caagttcgac gtgggcgact ggctggagag catccaccta   5340 

ggcgagcacc gcgaccgctt cgaggaccat gagatagaag gcgcgcacct acccgcgctt   5400 

accaaggacg acttcgtgga gctgggcgtc acgcgcgtgg gccaccgcat gaacatcgag   5460 

cgcgcgctca ggcagctgga cggcagctga cgccccaccc ccactcccgc cccaggccga   5520 

gcccgcggc                                                           5529 

 
           
             53  
             1623  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2739431CB1  
             
           
            53 

tgatatttga agaagtgttt tcatctatcc aagaaaaata tgatgtctcc atcccaagcc     60 

tcactcttat tcttaaatgt atgtattttt atttgtggag aagctgtaca aggtaactgt    120 

gtacatcatt ctacggactc ttcagtagtt aacattgtag aagatggatc taatgcaaaa    180 

gatgaaagta aaagtaatga tactgtttgt aaggaagact gtgaggaatc atgtgatgtt    240 

aaaactaaaa ttacacgaga agaaaaacat ttcatgtgta gaaatttgca aaattctatt    300 

gtttcctaca caagaagtac caaaaaacta ctaaggaata tgatggatga gcaacaagct    360 

tccttggatt atttatctaa tcaggtaatg tgtgacatgg attacagagg aggtggatgg    420 

actgtgatac agaaaagaat tgatgggata attgatttcc agaggttgtg gtgtgattat    480 

ctggatggat ttggagatct tctaggagaa ttttggctag gactgaaaaa gattttttat    540 

atagtaaatc agaaaaatac cagttttatg ctgtatgtgg ctttggaatc tgaagatgac    600 

actcttgctt atgcatcata tgataatttt tggctagagg atgaaacgag attttttaaa    660 

atgcacttag gacggtattc aggaaatgct ggtgatgcat tccggggtct caaaaaagaa    720 

gataatcaaa atgcaatgcc ttttagcaca tcagatgttg ataatgatgg gtgtcgccct    780 

gcatgcctgg tcaatggtca gtctgtgaag agctgcagtc acctccataa caagaccggc    840 

tggtggttta acgagtgtgg tctagcaaat ctaaatggca ttcatcactt ctctggaaaa    900 

ttgcttgcaa ctggaattca atggggcacg tggaccaaaa acaactcacc tgtcaagatt    960 

aaatctgttt caatgaaaat tagaagaatg tacaatccat attttaaata atctcattta   1020 

acattgtaat gcaagttcta caatgataat atattaaaga tttttaaaag tttatctttt   1080 

cacttagtgt ttcaaacata ttaggcaaaa tttaactgta gatggcattt agatgttatg   1140 

agtttaatta gaaaacttca attttgtagt attctataaa agaaaacatg gcttattgta   1200 

tgtttttact tctgactata ttaacaatat acaatgaaat ttgtttcaag tgaactacaa   1260 

cttgtcttcc taaaatttat agtgatttta aaggattttg ccttttcttt gaagcatttt   1320 

taaaccataa tatgttgtaa ggaaaattga agggaatatt ttacttattt ttatacttta   1380 

tatgattata taatctacag ataatttcta ctgaagacag ttacaataaa taactttatg   1440 

cagattaata tataagctac acatgatgta aaaaccttac tatttctagg tgatgccata   1500 

ccattttaaa agtagtaaga gtttgctgcc caaatagttt ttcttgtttt catatctaat   1560 

catggttaac tattttgtta ttgtttgtaa taaatatatg tacttttata tcctgaaaaa   1620 

aaa                                                                 1623 

 
           
             54  
             2242  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473606CB1  
             
           
            54 

ccacaagggc ctgactgagc gagcgagcat ggacggccgc ggggctttct ggacagtggc     60 

cattcccaga gccaggcagg aaggcctcgg gaggctgggg ctcccgttcc cggtgaagcg    120 

gacgccgcca gcgccccaga acccaggagg aagcacacag gccccacaga gagtggttgg    180 

caagagtcac tcggggatta ggatgccggc caaatcgcgg aatttgaggc tggaatccaa    240 

gctcaacagg aaagtagtga aatacaaatg gggaaaacag ggctctggag cggggaggga    300 

gctggtgccg gcatttccca ccaacgccgg tttaggaaga cgggaccgat gccggccgcc    360 

ccctgctgga ggggatgtgg catctcacgg gctgccaggg agcggggttg gctactcctg    420 

caaccagcgt gaagagggtc tcaggggagg ctgtggtggg atcccccacg tgcccttgtt    480 

cctctcaccg ttacctctgg atgcctcggg gcaaaggcct tcttccacct atagacagag    540 

tctacgcagg ggtcttggaa cccgggcaca ccagtcccca gctaacgaaa tccccgagtt    600 

gggggatttg agagggtcac gtttggccca agaacccgca gtcctctttg gtcttcggcc    660 

ctctatttct aagcgtgggc ttctggcacg gcggctctgg gcacagccca tgctgctttc    720 

gggctgggtg gtttcaacga cgacaacaat tatcacagtg acggtgacct tcaccccaac    780 

aggactgctg tgtgtgaagc actcaagagg gcccctacaa ccaacctgcc aggagtcggc    840 

tcctgaaaac agggtcggaa aagcgctaat tactttttcc aaaggctgga gggcttcact    900 

ccggctggcg ccgccgccta gcgcgctcct gcttcgccgc cacggtccgg gggggctgcc    960 

ggtcccgggt accatgtgtg acggcgccct gctgcctccg ctcgtcctgc ccgtgctgct   1020 

gctgctggtt tggggactgg acccgggcac aggtagcgcc ccctcccaca gccctcttca   1080 

ccccgcgtcc tgcggctacc ttccctctgc gttctcgcgg cgtcctggcg gcccgggggc   1140 

ggcggcggga ccgctgacgg cgcccgagcg gaggaggcgc gggccgcggc cggagtacgg   1200 

gaatcgggtg gctccgtggc aggcgcgccg ccgccgggtc tccgctcgcc gatgcgcggc   1260 

gccgttccgg gaggtgctcg cgcggctgcg ccggagaccc tccccgggtg gcgcgggcca   1320 

gcgtggagct gtcggcgacg cggcggccga cgtggaggtg gtgctcccgt ggcgggtgcg   1380 

ccccgacgac gtgcacctgc cgccgctgcc cgcagccccc gggccccgac ggcggcgacg   1440 

cccccgcacg cccccagccg ccccgcgcgc ccggcccgga gagcgcgccc tgctgctgca   1500 

cctgccggcc ttcgggcgcg acctgtacct tcagctgcgc cgcgacctgc gcttcctgtc   1560 

ccgaggcttc gaggtggagg aggcgggcgc ggcccggcgc cgcggccgcc ccgccgagct   1620 

gtgcttctac tcgggccgtg tgctcggcca ccccggctcc ctcgtctcgc tcagcgcctg   1680 

cggcgccgcc ggcggcctgg ttggcctcat tcagcttggg caggagcagg tgctaatcca   1740 

gcccctcaac aactcccagg gcccattcag tggacgagaa catctgatca ggcgcaaatg   1800 

gtccttgacc cccagccctt ctgctgaggc ccagagacct gagcagctct gcaaggttct   1860 

aacagttcca cagtgtctgg gcctcacctg ggaggacttg aaatctggag gctggagtga   1920 

tctggaggtg cctcattcat gtgtctggcc tggaggtgga tgacttgaag acaaggacaa   1980 

caacgtggag cgtctacctg tggcctctgc agcttggcgt ccataccttg gtggcagaca   2040 

tacttcttct atggccacca gggctcccaa tgcaagagtt cccgcaagcc cagcaggagc   2100 

tgtgctgcct ttgaggatca gcctcagaaa tcctagagca tcactctgaa ggtactctgt   2160 

tggctgaagc ggttagaaac ctacccaggt tcaagggcag agagatagac cccaccgctc   2220 

aatgtcaaag aatttggggg gc                                            2242 

 
           
             55  
             3751  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3534918CB1  
             
           
            55 

ttcatggagc atggagcgct tggcagcctt ggggaacatg cagcgaaagt tgtgggaaag     60 

gtactcagac aagagcaaga ctttgtaata acccaccacc agcgtttggt gggtcctact    120 

gtgatggagc agaaacacag atgcaagttt gcaatgaaag aaattgtcca attcatggca    180 

agtgggcgac ttgggccagt tggagtgcct gttctgtgtc atgtggagga ggtgccagac    240 

agagaacaag gggctgctcc gaccctgtgc cccagtatgg aggaaggaaa tgcgaaggga    300 

gtgatgtcca gagtgatttt tgcaacagtg acccttgccc aagtgagtgt tggaaatacc    360 

catggtaact ggagtccttg gagtggctgg ggaacatgca gccggacgtg taacggaggg    420 

cagatgcggc ggtaccgcac atgtgataac cctcctccct ccaatggggg aagagcttgt    480 

gggggaccag actcccagat ccagaggtgc aacactgaca tgtgtcctgt ggatggaagt    540 

tggggaagct ggcatagttg gagccagtgc tctgcctcct gtggaggagg tgaaaagact    600 

cggaagcggc tgtgcgacca tcctgtgcca gttaaaggtg gccgtccctg tcccggagac    660 

actactcagg tgaccaggtg caatgtacaa gcatgtccag gtgggcccca gcgagccaga    720 

ggaagtgtta ttggaaatat taatgatgtt gaatttggaa ttgctttcct taatgccaca    780 

ataactgata gccctaactc tgatactaga ataatacgtg ccaaaattac caatgtacct    840 

cgtagtcttg gttcagcaat gagaaagata gtttctattc taaatcccat ttattggaca    900 

acagcaaagg aaataggaga agcagtcaat ggctttaccc tcaccaatgc agtcttcaaa    960 

agagaaactc aagtggaatt tgcaactgga gaaatcttgc agatgagtca tattgcccgg   1020 

ggcttggatt ccgatggttc tttgctgcta gatatcgttg tgagtggcta tgtcctacag   1080 

cttcagtcac ctgctgaagt cactgtaaag gattacacag aggactacat tcaaacaggt   1140 

cctgggcagc tgtacgccta ctcaacccgg ctgttcacca ttgatggcat cagcatccca   1200 

tacacatgga accacaccgt tttctatgat caggcacagg gaagaatgcc tttcttggtt   1260 

gaaacacttc atgcatcctc tgtggaatct gactataacc agatagaaga gacactgggt   1320 

tttaaaattc atgcttcaat atccaaagga gatcgcagta atcagtgccc ctccgggttt   1380 

accttagact cagttggacc tttttgtgct gatgaggatg aatgtgcagc agggaatccc   1440 

tgctcccata gctgccacaa tgccatgggg acttactact gctcctgccc taaaggcctc   1500 

accatagctg cagatggaag aacttgtcaa gatattgatg agtgtgcttt gggtaggcat   1560 

acctgccacg ctggtcagga ctgtgacaat acgattggat cttatcgctg tgtggtccgt   1620 

tgtggaagtg gctttcgaag aacctctgat gggctgagtt gtcaagatat taatgaatgt   1680 

caagaatcca gcccctgtca ccagcgctgt ttcaatgcca taggaagttt ccattgtgga   1740 

tgtgaacctg ggtatcagct caaaggcaga aaatgcatgg atgtgaacga gtgtagacaa   1800 

aatgtatgca gaccagatca gcactgtaag aacacccgtg gtggctataa gtgcattgat   1860 

ctttgtccaa atggaatgac caaggcagaa aatggaacct gtattgatat tgatgaatgt   1920 

aaagatggga cccatcagtg cagatataac cagatatgtg agaatacaag aggcagctat   1980 

cgttgtgtat gcccaagagg ttatcggtct caaggagttg gaagaccctg catggatatt   2040 

gatgaatgtg aaaatacaga tgcctgccag catgagtgta agaatacctt tggaagttat   2100 

cagtgcatct gcccacctgg ctatcaactc acacacaatg gaaagacatg ccaagatatc   2160 

gatgaatgtc tggagcagaa tgtgcactgt ggacccaatc gcatgtgctt caacatgaga   2220 

ggaagctacc agtgcatcga tacaccctgt ccacccaact accaacggga tcctgtttca   2280 

gggttctgcc tcaagaactg tccacccaat gatttggaat gtgccttgag cccatatgcc   2340 

ttggaataca aactcgtctc cctcccattt ggaatagcca ccaatcaaga tttaatccgg   2400 

ctggttgcat acacacagga tggagtgatg catcccagga caactttcct catggtagat   2460 

gaggaacaga ctgttccttt tgccttgagg gatgaaaacc tgaaaggagt ggtgtataca   2520 

acacgaccac tacgagaagc agagacctac cgcatgaggg tccgagcctc atcctacagt   2580 

gccaatggga ccattgaata tcagaccaca ttcatagttt atatagctgt gtccgcctat   2640 

ccatactaag gaactctcca aagcctattc cacatattta aaccgcatta atcatggcaa   2700 

tcaagccccc ttccagatta ctgtctcttg aacagttgca atcttggcag cttgaaaatg   2760 

gtgctacact ctgttttgtg tgccttcctt ggtacttctg aggtattttc atgatcccac   2820 

catggtcata tcttgaagta tggtctagaa aagtccctta ttattttatt tattacactg   2880 

gagcagttac ttcccaaaga ttattctgaa catctaacag gacatatcag tgatggttta   2940 

cagtagtgta gtacctaaga tcattttcct gaaagccaaa ccaaacaacg aaaaacaaga   3000 

acaactaatt cagaatcaaa tagagttttt gagcatttga ctatttttag aatcataaaa   3060 

ttagttacta agtattttga tcaaagctta taaaataact tacggagatt tttgtaagta   3120 

ttgatacatt ataataggac ttgcctattt tcatttttaa gaagaaaaac accactcatt   3180 

ttataaaata tagtacagct actataaggc ttgtttgatc ccaaatggtg cttatcttga   3240 

ttgaacattc agaacaagga tattattttc agtgattttg tgagatcagc tgaaccactt   3300 

atgataataa taataaaaaa gactgctttg ccctcacgtc agttgtacat ggcatggaac   3360 

tttaaaaatt ttaatataaa ctttcatcca gttagcttca taacttttac gttccagaat   3420 

tttgtttatt ttcctgtcaa tgaaagcaat ttttaaagat accagtggga caggtttggt   3480 

tttttaaaaa tctcatgtgt tcaaattaac ataaatatta cacgtcaata cactgtacat   3540 

ggtggtaata gactctaagc aattgccaag atgtattcta tttttatgaa gtgtatatat   3600 

attaccttag tgtgcatttt ctatataata tcttgatgga ctcttttata aaattatttt   3660 

ataaaaaaca atgttacact aaaatcagcc taaataaatt ttcacaactt tttttcataa   3720 

ccaaaaacaa caaacaacaa aaccggggcc g                                  3751 

 
           
             56  
             3579  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2428715CB1  
             
           
            56 

gggtcgacca cgcgtcgggg caggtggcga gcagcgagca gcgcctgcgg gagcggccgg     60 

tcggtcgggt ccccgcgccc cgcacgcccg cacgcccagc ggggcccgca ttgagcatgg    120 

gcgcggcggc cgtgcgctgg cacttgtgcg tgctgctggc cctgggcaca cgcgggcggc    180 

tggccggggg cagcgggctc ccagggtcag tcgacgtgga tgagtgctca gagggcacag    240 

atgactgcca catcgatgcc atctgtcaga acacgcccaa gtcctacaaa tgcctctgca    300 

agccaggcta caagggggaa ggcaagcagt gtgaagacat tgacgagtgt gagaatgact    360 

actacaatgg gggctgtgtc cacgagtgca tcaacatccc ggggaactac aggtgtacct    420 

gctttgatgg cttcatgctg gcacacgatg gacacaactg cctggatgtg gacgagtgtc    480 

aggacaataa tggtggctgc cagcagatct gcgtcaatgc catgggcagc tacgagtgtc    540 

agtgccacag tggcttcttc cttagtgaca accagcatac ctgcatccac cgctccaatg    600 

agggtatgaa ctgcatgaac aaagaccatg gctgtgccca catctgccgg gagacgccca    660 

aaggtggggt ggcctgcgac tgcaggcccg gctttgacct tgcccaaaac cagaaggact    720 

gcacactaac ctgtaattat ggaaacggag gctgccagca cagctgtgag gacacagaca    780 

caggccccac gtgtggttgc caccagaagt acgccctcca ctcagacggt cgcacgtgca    840 

tcgagaagga tgaggctgca attgagcgct ctcagttcaa tgccacgtca gtagctgatg    900 

tggacaagcg ggtgaaacgg cggctactca tggagacgtg cgcagtcaat aacggaggct    960 

gcgaccggac atgcaaggac acagccactg gcgtgcgatg cagctgcccc gttggattca   1020 

cactgcagcc ggacgggaag acatgcaaag acatcaacga gtgcctggtc aacaacggag   1080 

gctgcgacca cttctgccgc aacaccgtgg gcagcttcga gtgcggctgc cggaagggct   1140 

acaagctgct caccgacgag cgcacctgcc aggacatcga cgagtgctcc ttcgagcgga   1200 

cctgtgacca catctgcatc aactccccgg gcagcttcca gtgcctgtgt caccgcggct   1260 

acatcctcta cgggacaacc cactgcggag atgtggacga gtgcagcatg agcaacggga   1320 

gctgtgacca gggctgcgtc aacaccaagg gcagctacga gtgcgtctgt cccccgggga   1380 

ggcggctcca ctggaaccgg aaggattgcg tggagacagg caagtgtctt tctcgtgcca   1440 

agacctcccc ccgggcccag ctgtcctgca gcaaggcagg cggtgtggag agctgcttcc   1500 

tttcctgccc ggctcacaca ctcttcgtgc cagatgcccc caccaccccc atcaaacaga   1560 

aggcccgctt caagatccga gatgccaagt gccacctccg gccccacagc caggcacgag   1620 

caaaggagac cgccaggcag ccgctgctgg accactgcca tgtgactttc gtgaccctca   1680 

agtgtgactc ctccaagaag aggcgccgtg gccgcaagtc cccatccaag gaggtgtccc   1740 

acatcacagc agagtttgag atcgagacaa agatggaaga ggcctcagac acatgcgaag   1800 

cggactgctt gcggaagcga gcagaacaga gcctgcaggc cgccatcaag accctgcgca   1860 

agtccatcgg ccggcagcag ttctatgtcc aggtctcagg cactgagtac gaggtagccc   1920 

agaggccagc caaggcgctg gaggggcagg gggcatgtgg cgcaggccag gtgctacagg   1980 

acagcaaatg cgttgcctgt gggcctggca cccacttcgg tggtgagctc ggccagtgtg   2040 

tgccatgtat gccaggaaca taccaggaca tggaaggcca gctcagttgc acaccgtgcc   2100 

ccagcagcga cgggcttggt ctgcctggtg cccgcaacgt gtcggaatgt ggaggccagt   2160 

gttctccagg cttcttctcg gccgatggct tcaagccctg ccaggcctgc cccgtgggca   2220 

cgtaccagcc tgagcccggg cgcaccggct gcttcccctg tggagggggt ttgctcacca   2280 

aacacgaagg caccacctcc ttccaggact gcgaggctaa agtgcactgc tcccccggcc   2340 

accactacaa caccaccacc caccgctgca tccgctgccc cgtcggcacc taccagcccg   2400 

agtttggcca gaaccactgc atcacctgtc cgggcaacac cagcacagac ttcgatggct   2460 

ccaccaacgt cacacactgc aaaaaccagc actgcggcgg cgagcttggt gactacaccg   2520 

gctacatcga gtcccccaac taccctggcg actacccagc caacgctgaa tgcgtctggc   2580 

acatcgcacc tcccccaaag cgcaggatcc tcatcgtggt ccctgagatc ttcctgccca   2640 

tcgaggatga gtgcggcgat gttctggtca tgaggaagag tgcctctccc acgtccatca   2700 

ccacctatga gacctgccag acctacgaga ggcccatcgc cttcacctcc cgctcccgca   2760 

agctctggat ccagttcaaa tccaatgaag gcaacagcgg caaaggcttc caagtgccct   2820 

atgtcaccta cgatgaggac taccagcaac tcatagagga catcgtgcgc gatgggcgcc   2880 

tgtacgcctc ggagaaccac caggaaattt tgaaagacaa gaagctgatc aaggccctct   2940 

tcgacgtgct ggcgcatccc cagaaccgcg gcttagtttc ctcatgttaa aagaaaatac   3000 

ttatcctccc tgtggcacag ggttttgttt aaaagattag acaagatgat acaaccattt   3060 

tggaaataat ttggcagctt cttataaaca tatactttac aggtaagcca gcaattgcac   3120 

tcctagctgc acccacgaga aatgaaaata tgtccataca aagatttata cacaaatgtt   3180 

tatagcagct ttattcataa taatcaaaaa ctgaaaacaa ctcaaacatc catcaacagg   3240 

cagatggata aacaaattat ggtatgtcca tgcaacggaa tacaactcac tgatgaaaag   3300 

gaataaacca caaatgcctg caacgccatg atgaatctca aaacatgctg agtgtagaga   3360 

agccagacac aagagtagat actcctatac aattccactt acatggaaat ctagaaaaga   3420 

caattcgaat atatagtggc aaaaagcaga agagtggttg cctggaacca gggtgggaat   3480 

gaagattaac tgcccagagg cataaaaaat ggggtggtgg gggcggtgat ggaaaagtgc   3540 

tatgccttca ctgtaccttt gtcaaaactt gttgaactg                          3579 

 
           
             57  
             5178  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3351332CB1  
             
           
            57 

gggaacccag aaccagcccg agccgcctgc cccgtcgccc ggccgccggc ttagggcgca     60 

gcgcggttgg tcctcgcccc ctcccgcccg ccggcctacc aggccatggg ggcgtcccgg    120 

gaccgcgggc tggccgcgct ctggtgcctt gggctcctgg ggggcctggc gcgcgtcgcg    180 

ggcacgcact accgctacct ctggaggggc tgctacccat gtcacctggg ccaggccggc    240 

taccccgtga gcgccggtga ccagaggcca gatgtggacg aatgccgaac ccacaacggt    300 

ggctgccagc accggtgcgt gaacacccca ggctcctacc tctgtgagtg caagcccggc    360 

ttccggctcc acactgacag caggacctgc ctggccatta actcctgcgc cctgggcaat    420 

ggcggctgcc agcaccactg tgtccagctc acaatcactc ggcatcgctg ccagtgccgg    480 

cccgggttcc agctccagga ggacggcagg cattgtgtcc gtagaagccc gtgtgccaac    540 

aggaacggca gctgcatgca caggtgccag gtggtccggg gcctcgcccg ctgtgagtgc    600 

cacgtgggct atcagctagc agcggacggc aaggcctgtc cagatgtgga cgaatgtgcc    660 

gcagggctgg cccagtgtgc ccatggctgc ctcaacaccc aggggtcctt caagtgcgtg    720 

tgtcacgcgg gctatgagct gggcgccgat ggccggcagt gctaccggat tgagatggaa    780 

atcgtgaaca gctgtgaggc caacaacggc ggctgctccc atggctgcag ccacaccagt    840 

gctgggcccc tgtgcacatg tccccgcggc tacgagctgg acacagatca gaggacctgc    900 

atcgatgtcg acgactgtgc agacagcccg tgctgccagc aggtgtgcac caacaaccct    960 

ggcgggtacg agtgcggctg ctacgccggc taccggctca gtgccgatgg ctgcggctgt   1020 

gaggatgtgg atgagtgcgc ctccagccgt ggcggctgcg agcaccactg caccaacctg   1080 

gccggctcct tccagtgctc ctgcgaggcc ggctaccggc tgcacgagga ccgtaggggc   1140 

tgcagccccc tggaggagcc gatggtggac ctggacggcg agctgccttt cgtgcggccc   1200 

ctgccccaca ttgccgtgct ccaggacgag ctgccgcaac tcttccagga tgacgacgtc   1260 

ggggccgatg aggaagaggc agagttgcgg ggcgaacaca cgctcacaga gaagtttgtc   1320 

tgcctggatg actcctttgg ccatgactgc agcttgacct gtgatgactg caggaacgga   1380 

gggacctgcc tcctgggcct ggatggctgt gattgccccg agggctggac tgggctcatc   1440 

tgcaatgaga cttgtcctcc ggacaccttt gggaagaact gcagcttctc ctgcagctgt   1500 

cagaatggtg ggacctgcga ctctgtcacg ggggcctgcc gctgcccccc gggtgtcagt   1560 

ggaactaact gtgaggatgg ctgccccaag ggctactatg gcaagcactg tcgcaagaaa   1620 

tgcaactgtg ccaaccgggg ccggtgccac cgcctctacg gggcctgcct ctgcgaccca   1680 

gggctctacg gccgcttctg ccacctcacc tgcccgccgt gggcctttgg gccgggctgc   1740 

tcggaggagt gccagtgtgt gcagccccac acgcagtcct gtgacaagag ggatggcagc   1800 

tgctcctgca aggctggctt ccggggcgag cgctgtcagg cagagtgtga gctgggctac   1860 

tttgggccgg ggtgctggca ggcatgcacc tgcccagtgg gcgtggcctg tgactccgtg   1920 

agcggcgagt gtgggaagcg gtgtcctgct ggcttccagg gagaggactg tggccaagag   1980 

tgcccggtgg ggacgtttgg cgtgaactgc tcgagctcct gctcctgtgg gggggccccc   2040 

tgccacgggg tcacggggca gtgccggtgt ccgccgggga ggactgggga agactgtgag   2100 

gcagattgtc ccgagggccg ctgggggctg ggctgccagg agatctgccc agcatgccag   2160 

cacgctgccc gctgcgaccc tgagaccgga gcctgcctgt gcctccctgg cttcgtcggc   2220 

agccgctgcc aggacgtgtg cccagcaggc tggtatggtc ccagctgcca gacaaggtgc   2280 

tcttgtgcca atgatgggca ctgccaccca gccaccggac actgcagctg tgcccccggg   2340 

tggaccggct ttagctgcca gagagcctgt gatactgggc actggggacc tgactgcagc   2400 

cacccctgca actgcagcgc tggccacggg agctgtgatg ccatcagcgg cctgtgtctg   2460 

tgtgaggctg gctacgtggg cccgcggtgc gagcagcagt gtccccaggg ccactttggg   2520 

cccggctgtg agcagctgtg ccagtgtcag catggagcag cctgtgacca cgtcagcggg   2580 

gcctgcacct gcccggccgg ctggaggggc accttctgcg agcatgcctg cccggccggc   2640 

ttctttggat tggactgtcg cagtgcctgc aactgcaccg ccggagctgc ctgtgatgcc   2700 

gtgaatggct cctgcctctg ccccgctggc cgccggggcc cccgctgtgc cgagacctgc   2760 

ccagcccaca cctacgggca caattgcagc caggcctgtg cctgctttaa cggggcctcc   2820 

tgtgaccctg tccacgggca gtgccactgt gcccctggct ggatggggcc ctcctgcctg   2880 

caggagtgcc tcccccggga cgtcagagct ggctgccggc acagcggcgg ttgcctcaac   2940 

gggggcctgt gtgacccgca cacgggccgc tgcctctgcc cagccggctg gactggggac   3000 

aagtgtcaga gcccctgcct gcggggctgg tttggagagg cctgtgccca gcgctgcagc   3060 

tgcccgcctg gcgctgcctg ccaccacgtc actggggcct gccgctgtcc ccctggcttc   3120 

actggctccg gctgcgagca ggcctgccca cccggcagct ttggggagga ctgtgcgcag   3180 

atgtgccagt gtcccggtga gaacccggcc tgccaccctg ccaccgggac ctgctcatgt   3240 

gctgctggct accacggccc cagctgccag caacgatgtc cgcccgggcg gtatgggcca   3300 

ggctgtgaac agctgtgtgg gtgtctcaac gggggctcct gtgatgcggc cacgggggcc   3360 

tgccgctgcc ccactgggtt cctcgggacg gactgcaacc tcacctgtcc gcagggccgc   3420 

ttcggcccca actgcaccca cgtgtgtggg tgtgggcagg gggcggcctg cgaccctgtg   3480 

accggcacct gcctctgccc cccggggaga gccggcgtcc gctgtgagcg aggctgcccc   3540 

cagaaccggt ttggcgtggg ctgcgagcac acctgctcct gcagaaatgg gggcctgtgc   3600 

cacgccagca acggcagctg ctcctgtggc ctgggctgga cggggcggca ctgcgagctg   3660 

gcctgtcccc ctgggcgcta cggagccgcc tgccatctgg agtgctcctg ccacaacaac   3720 

agcacgtgtg agcctgccac gggcacctgc cgctgcggcc ccggcttcta tggccaggcc   3780 

tgcgagcacc cctgtccccc tggcttccac ggggctggct gccaggggtt gtgctggtgt   3840 

caacatggag ccccctgcga ccccatcagt ggccgatgcc tctgccctgc cggcttccac   3900 

ggccacttct gtgagagggg gtgtgagcca ggttcatttg gagagggctg ccaccagcgc   3960 

tgtgactgtg acgggggggc accctgtgac cctgtcaccg gtctctgcct ttgcccacca   4020 

gggcgctcag gagccacctg taacctggat tgcagaaggg gccagtttgg gcccagctgc   4080 

accctgcact gtgactgcgg gggtggggct gactgcgacc ctgtcagtgg gcagtgtcac   4140 

tgtgtggatg gctacatggg gcccacgtgc cgggaaggtg ggcccctccg gctccccgag   4200 

aacccgtcct tagcccaggg ctcagcgggc acactgcccg cctccagcag acccacatcc   4260 

cggagcggtg gaccagcgag gcactagtag aggcagtccc gtggagcccg cctctccagt   4320 

cccagccaga ggggaccctg gcctttggtg accactgaga aggacacttc acgggcccag   4380 

agctcctggt actgcccttc ctttgagggc cgtggagggc tgtggacagc ccagcaacct   4440 

gtcgctcttg gaggctggtg tggccttgag gagggaagcc tcgcatggcc gctggaagag   4500 

aggcgcctcc tggcctggct ctgcagaacc caggggcacg ctctgggcct gggctgagga   4560 

agtcccgctc tccccgcggc tctgagttgg actgaggaca ggtgtgggcg ccagtgtggg   4620 

tgcaggcgca ggtgcaggca cagggccact gtcctccagg caggcttttt ggtgctaggc   4680 

cctgggactg gaagtcgccc agcccgtatt tatgtaaagg tatttatggg ccactgcaca   4740 

tgcccgctgc agccctggga tcagctggaa gctgcctgtc atctcctgcc caatccccag   4800 

aaaccctgat tcaggtctgc aggctcctgc gggctcacca ggctgctggc tccggtacca   4860 

tgtaaaccta ggaaggtaaa ggagcaggca acctcctcgt ggcctgtgtg tttgctgtgt   4920 

tacgtggact ctgtgtgggc tcctccctgg ggcccggcca gcataacggt gcacccaggg   4980 

acctcccagt gcacccgggg ccctttgcag gggtgggggt gccacacaag tgaagaagtt   5040 

gggactcatc tcagttccca gtgctattga ggagaacgct ggggctgcat tcattaccgc   5100 

tgagacccag agactggctg ttcccagaga atggcccagg gggaggaggg ctggtgtgga   5160 

agggcaactt ggactgag                                                 5178 

 
           
             58  
             11367  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6382722CB1  
             
           
            58 

atggcgaagc ggctctgcgc ggggagcgca ctgtgtgttc gcggcccccg gggccccgcg     60 

ccgctgctgc tggtcgggct ggcgctgctg ggcgcggcgc gggcgcggga ggaggcgggc    120 

ggcggcttca gcctgcaccc gccctacttc aacctggccg agggcgcccg catcgccgcc    180 

tccgcgacct gcggagagga ggccccggcg cgcggctccc cgcgccccac cgaggacctt    240 

tactgcaagc tggtaggggg ccccgtggcc ggcggcgacc ccaaccagac catccggggc    300 

cagtactgcg acatctgcac ggctgccaac agcaacaagg cacaccccgc gagcaatgcc    360 

atcgatggca cggagcgctg gtggcagagt ccaccgctgt cccgcggcct ggagtacaac    420 

gaggtcaacg tcaccctgga cctgggccag gtcttccacg tggcctacgt cctcatcaag    480 

tttgccaact caccccggcc ggacctctgg gtgctggagc ggtccatgga cttcggccgc    540 

acctaccagc cctggcagtt ctttgcctcc tctaagaggg actgtctgga gcggttcggg    600 

ccacagacgc tggagcgcat cacacgggac gacgcggcca tctgcaccac cgagtactca    660 

cgcatcgtgc ccctggagaa cggagagatc gtggtgtccc tggtgaacgg acgtccgggc    720 

gccatgaatt tctcctactc gccgctgcta cgtgagttca ccaaggccac caacgtccgc    780 

ctgcgcttcc tgcgtaccaa cacgctgctg ggccatctca tggggaaggc gctgcgggac    840 

cccacggtca cccgccggta ttattacagc atcaaggata tcagcatcgg aggccgctgt    900 

gtctgccacg gccacgcgga tgcctgcgat gccaaagacc ccacggaccc gttcaggctg    960 

cagtgcacct gccagcacaa cacctgcggg ggcacctgcg accgctgctg ccccggcttc   1020 

aatcagcagc cgtggaagcc tgcgactgcc aacagtgcca acgagtgcca gtcctgtaac   1080 

tgctacggcc atgccaccga ctgttactac gaccctgagg tggaccggcg ccgcgccagc   1140 

cagagcctgg atggcaccta tcagggtggg ggtgtctgta tcgactgcca gcaccacacc   1200 

gccggcgtca actgtgagcg ctgcctgccc ggcttctacc gctctcccaa ccaccctctc   1260 

gactcgcccc acgtctgccg ccgctgcaac tgcgagtccg acttcacgga tggcacctgc   1320 

gaggacctga cgggtcgatg ctactgccgg cccaacttct ctggggagcg gtgtgacgtg   1380 

tgtgccgagg gcttcacggg cttcccaagc tgctacccga cgccctcgtc ctccaatgac   1440 

accagggagc aggtgctgcc agctggccag attgtgaatt gtgactgcag cgcggcaggg   1500 

acccagggca acgcctgccg gaaggaccca agggtgggac gctgtctgtg caaacccaac   1560 

ttccaaggca cccattgtga gctctgcgcg ccagggttct acggccccgg ctgccagccc   1620 

tgccagtgtt ccagccctgg agtggccgat gaccgctgtg accctgacac aggccagtgc   1680 

aggtgccgag tgggcttcga gggggccaca tgtgatcgct gtgcccccgg ctactttcac   1740 

ttccctctct gccagttgtg tggctgcagc cctgcaggaa ccttgcccga gggctgcgat   1800 

gaggccggcc gctgcctatg ccagcctgag tttgctggac ctcattgtga ccggtgccgc   1860 

cctggctacc atggtttccc caactgccaa gcatgcacct gcgaccctcg gggagccctg   1920 

gaccagctct gtggggcggg aggtttgtgc cgctgccgcc ccggctacac aggcactgcc   1980 

tgccaggaat gcagccccgg ctttcacggc ttccccagct gtgtcccctg ccactgctct   2040 

gctgaaggct ccctgcacgc agcctgtgac ccccggagtg ggcagtgcag ctgccggccc   2100 

cgtgtgacgg ggctgcggtg tgacacgtgt gtgcccggtg cctacaactt cccctactgc   2160 

gaagctggct cttgccaccc tgccggtctg gccccagtgg atcctgccct tcctgaggca   2220 

caggttccct gtatgtgccg ggctcacgtg gaggggccga gctgtgaccg ctgcaaacct   2280 

gggttctggg gactgagccc cagcaacccc gagggctgta cccgctgcag ctgcgacctc   2340 

aggggcacac tgggtggagt tgctgagtgc cagccgggca ccggccagtg cttctgcaag   2400 

ccccacgtgt gcggccaggc ctgcgcgtcc tgcaaggatg gcttctttgg actggatcag   2460 

gctgactatt ttggctgccg cagctgccgg tgtgacattg gcggtgcact gggccagagc   2520 

tgtgaaccga ggacgggcgt ctgccggtgc cgccccaaca cccagggccc cacctgcagc   2580 

gagcctgcga gggaccacta cctcccggac ctgcaccacc tgcgcctgga gctggaggag   2640 

gctgccacac ctgagggtca cgccgtgcgc tttggcttca accccctcga gttcgagaac   2700 

ttcagctgga ggggctacgc gcagatggca cctgtccagc ccaggatcgt ggccaggctg   2760 

aacctgacct cccccgacct tttctggctc gtcttccgat acgtcaaccg gggggccatg   2820 

agtgtgagcg ggcgggtctc tgtgcgagag gagggcaggt cggccgcctg tgccaactgc   2880 

acagcacaga gtcagcccgt ggccttccca cccagcacgg agcctgcctt catcaccgtg   2940 

ccccagaggg gcttcggaga gccctttgtg ctgaaccctg gcacctgggc cctgcgtgtg   3000 

gaggccgaag gggtgctcct ggactacgtg gttctgctgc ctagcgcata ctacgaggcg   3060 

gcgctcctgc agctgcgggt gactgaggcc tgcacatacc gtccctctgc ccagcagtct   3120 

ggcgacaact gcctcctcta cacacacctc cccctggatg gcttcccctc ggccgccggg   3180 

ctggaggccc tgtgtcgcca ggacaacagc ctgccccggc cctgccccac ggagcagctc   3240 

agcccgtcgc acccgccact gatcacctgc acgggcagtg atgtggacgt ccagcttcaa   3300 

gtggcagtgc cacagccagg ccgctatgcc ctagtggtgg agtacgccaa tgaggatgcc   3360 

cgccaggagg tgggcgtggc tgtgcacacc ccacagcggg ccccccagca ggggctgctc   3420 

tccctgcacc cctgcctgta cagcaccctg tgccggggca ctgcccggga tacccaggac   3480 

cacctggctg tcttccacct ggactcggag gccagcgtga ggctcacagc cgagcaggca   3540 

cgcttcttcc tgcacggggt cactctggtg cccattgagg agttcagccc ggagttcgtg   3600 

gagccccggg tcagctgcat cagcagccac ggcgcctttg gccccaacag tgccgcctgt   3660 

ctgccctcgc gcttcccaaa gccgccccag cccatcatcc tcagggactg ccaggtgatc   3720 

ccgctgccgc ccggcctccc gctgacccac gcgcaggatc tcactccagc cacgtcccca   3780 

gctggacccc gacctcggcc ccccaccgct gtggaccctg atgcagagcc caccctgctg   3840 

cgtgagcccc aggccaccgt ggtcttcacc acccatgtgc ccacgctggg ccgctatgcc   3900 

ttcctgctgc acggctacca gccagcccac cccaccttcc ccgtggaagt cctcatcaac   3960 

gccggccgcg tgtggcaggg ccacgccaac gccagcttct gtccacatgg ctacggctgc   4020 

cgcaccctgg tggtgtgtga gggccaggcc ctgctggacg tgacccacag cgagctcact   4080 

gtgaccgtgc gtgtgcccga gggccggtgg ctctggctgg attatgtact cgtggtccct   4140 

gagaacgtct acagctttgg ctacctccgg gaggagcccc tggataaatc ctatgacttc   4200 

atcagccact gcgcagccca gggctaccac atcagcccca gcagctcatc cctgttctgc   4260 

cgaaacgctg ctgcttccct ctccctcttc tataacaacg gagcccgtcc atgtggctgc   4320 

cacgaagtag gtgctacagg ccccacgtgt gagcccttcg ggggccagtg tccctgccat   4380 

gcccatgtca ttggccgtga ctgctcccgc tgtgccaccg gatactgggg cttccccaac   4440 

tgcaggccct gtgactgcgg tgcccgcctc tgtgacgagc tcacgggcca gtgcatctgc   4500 

ccgccacgca ccatcccgcc cgactgcctg ctgtgccagc cccagacctt tggctgccac   4560 

cccctggtcg gctgtgagga gtgtaactgc tcagggcccg gcatccagga gctcacagac   4620 

cctacctgtg acacagacag cggccagtgc aagtgcagac ccaacgtgac tgggcgccgc   4680 

tgtgatacct gctctccggg cttccatggc tacccccgct gccgcccctg tgactgtcac   4740 

gaggcgggca ctgcgcctgg cgtgtgtgac cccctcacag ggcagtgcta ctgtaaggag   4800 

aacgtgcagg gccccaaatg tgaccagtgc agccttggga ccttctcact ggatgctgcc   4860 

aaccccaaag gttgcacccg ctgcttctgc tttggggcca cggagcgctg ccggagctcg   4920 

tcctacaccc gccaggagtt cgtggatatg gagggatggg tgctgctgag cactgaccgg   4980 

caggtggtgc cccacgagcg gcagccaggg acggagatgc tccgtgcaga cctgcggcac   5040 

gtgcctgagg ctgtgcccga ggctttcccc gagctgtact ggcaggcccc accctcctac   5100 

ctgggggacc gggtgtcatc ctacggtggg accctccgtt atgaactgca ctcagagacc   5160 

cagcggggag atgtctttgt ccccatggag agcaggccgg atgtggtgct gcagggcaac   5220 

cagatgagca tcacattcct ggagccggca taccccacgc ctggccacgt tcaccgtggg   5280 

cagctgcagc tggtggaggg gaacttccgg catacggaga ctcgcaacac tgtgtcccgc   5340 

gaggagctca tgatggtgct ggccagcctg gagcagctgc agatccgtgc cctcttctca   5400 

cagatctcct cggctgtctc cctgcgcagg gtggcactgg aggtggccag cccagcaggc   5460 

cagggggccc tggccagcaa tgtggagctg tgcctgtgcc ccgccagcta ccggggggac   5520 

tcatgccagg aatgtgcccc cggcttctat cgggacgtca aaggtctctt cctgggccga   5580 

tgtgtccctt gtcagtgcca tggacactca gaccgctgcc tccctggctc tggcgtctgt   5640 

gtggactgcc agcacaacac cgaaggggcc cactgtgagc gctgccaggc tggcttcatg   5700 

agcagcaggg acgaccccag cgccccctgt gtcagctgcc cctgccccct ctcagtgcct   5760 

tccaacaact tcgccgaggg ctgtgtcctg cgaggcggcc gcacccagtg cctctgcaaa   5820 

cctggttatg caggtgcctc ctgcgagcgg tgtgcgcccg gattctttgg gaacccactg   5880 

gtgctgggca gctcctgcca gccatgcgac tgcagcggca acggtgaccc caacttgctc   5940 

ttcagcgact gcgaccccct gacgggcgcc tgccgtggct gcctgcgcca caccactggg   6000 

ccccgctgcg agatctgtgc ccccggcttc tacggcaacg ccctgctgcc cggcaactgc   6060 

acccggtgcg actgtacccc atgtgggaca gaggcctgcg acccccacag cgggcactgc   6120 

ctgtgcaagg cgggcgtgac tgggcggcgc tgtgaccgct gccaggaggg acattttggt   6180 

ttcaatggct gcgggggctg ccgcccgtgt gcttgtggac cggccgccga gggctccgag   6240 

tgccaccccc agagcggaca gtgccactgc cgaccaggga ccatgggacc ccagtgccgc   6300 

gagtgtgccc ctggctactg ggggctccct gagcagggct gcaggcgctg ccagtgccct   6360 

gggggccgct gtgaccctca cacgggccgc tgcaactgcc ccccggggct cagcggggag   6420 

cgctgcgaca cctgcagcca gcagcatcag gtgcctgttc caggcgggcc tgtgggccac   6480 

agcatccact gtgaagtgtg tgaccactgt gtggtcctgc tcctggatga cctggaacgg   6540 

gccggcgccc tcctccccgc cattcacgag caactgcgtg gcatcaatgc cagctccatg   6600 

gcctgggccc gtctgcacag gctgaacgcc tccatcgctg acctgcagag ccagctccgg   6660 

agccccctgg gcccccgcca tgagacggca cagcagctgg aggtgctgga gcagcagagc   6720 

acaagcctcg ggcaggacgc acggcggcta ggcggccagg ccgtggggac ccgagaccag   6780 

gcgagccaat tgctggccgg caccgaggcc acactgggcc atgcgaagac gctgttggcg   6840 

gccatccggg ctgtggaccg caccctgagc gagctcatgt cccagacggg ccacctgggg   6900 

ctggccaatg cctcggctcc atcaggtgag cagctgctcc ggacactggc cgaggtggag   6960 

cggctgctct gggagatgcg ggcccgggac ctgggggccc cgcaggcagc agctgaggct   7020 

gagttggctg cagcacagag attgctggcc cgggtgcagg agcagctgag cagcctctgg   7080 

gaggagaacc aggcactggc cacacaaacg cgcgaccggc tggcccagca cgaggccggc   7140 

ctcatggacc tgcgagaggc tttgaaccgg gcagtggacg ccacacggga ggcccaggag   7200 

ctcaacagcc gcaaccagga gcgcctggag gaagccctgc aaaggaagca ggagctgtcc   7260 

cgggacaatg ccaccctgca ggccactctg catgcggcta gggacaccct ggccagcgtc   7320 

ttcagattgc tgcacagcct ggaccaggct aaggaggagc tggagcgcct cgccgccagc   7380 

ctggacgggg ctcggacccc actgctgcag aggatgcaga ccttctcccc ggcgggcagc   7440 

aagctgcgtc tagtggaggc cgccgaggcc cacgcacagc agctgggcca gctggcactc   7500 

aatctgtcca gcatcatcct ggacgtcaac caggaccgcc tcacccagag ggccatcgag   7560 

gcctccaacg cctacagccg catcctgcag gccgtgcagg ctgccgagga tgctgctggc   7620 

caggccctgc agcaggcgga ccacacgtgg gcgacggtgg tgcggcaggg cctggtggac   7680 

cgagcccagc agctcctggc caacagcact gcactagaag aggccatgct ccaggaacag   7740 

cagaggctgg gccttgtgtg ggctgccctc cagggtgcca ggacccagct ccgagatgtc   7800 

cgggccaaga aggaccagct ggaggcgcac atccaggcgg cgcaggccat gcttgccatg   7860 

gacacagacg agacaagcaa gaagatcgca catgccaagg ctgtggctgc tgaagcccag   7920 

gacaccgcca cccgtgtgca gtcccagctg caggccatgc aggagaatgt ggagcggtgg   7980 

cagggccagt acgagggcct gcggggccag gacctgggcc aggcagtgct tgacgcaggc   8040 

cactcagtgt ccaccctgga gaagacgctg ccccagctgc tggccaagct gagcatcctg   8100 

gagaaccgtg gggtgcacaa cgccagcctg gccctgtccg ccagcattgg ccgcgtgcga   8160 

gagctcattg cccaggcccg gggggctgcc agtaaggtca aggtgcccat gaagttcaac   8220 

gggcgctcag gggtgcagct gcgcacccca cgggatcttg ccgaccttgc tgcctacact   8280 

gccctcaagt tctacctgca gggcccagag cctgagcctg ggcagggtac cgaggatcgc   8340 

tttgtgatgt acatgggcag ccgccaggcc actggggact acatgggtgt gtctctgcgt   8400 

gacaagaagg tgcactgggt gtatcagctg ggtgaggcgg gccctgcagt cctaagcatc   8460 

gatgaggaca ttggggagca gttcgcagct gtcagcctgg acaggactct ccagtttggc   8520 

cacatgtccg tcacagtgga gagacagatg atccaggaaa ccaagggtga cacggtggcc   8580 

cctggggcag aggggctgct caacctgcgg ccagacgact tcgtcttcta cgtcgggggg   8640 

taccccagta ccttcacgcc ccctcccctg cttcgcttcc ccggctaccg gggctgcatc   8700 

gagatggaca cgctgaatga ggaggtggtc agcctctaca acttcgagag gaccttccag   8760 

ctggacacgg ctgtggacag gccttgtgcc cgctccaagt cgaccgggga cccgtggctc   8820 

acggacggct cctacctgga cggcaccggc ttcgcccgca tcagcttcga cagtcagatc   8880 

agcaccacca agcgcttcga gcaggagctg cggctcgtgt cctacagcgg ggtgctcttc   8940 

ttcctgaagc agcagagcca gttcctgtgc ttggccgtgc aagaaggcag cctcgtgctg   9000 

ttgtatgact ttggggctgg cctgaaaaag gccgtcccac tgcagccccc accgcccctg   9060 

acctcggcca gcaaggcgat ccaggtgttc ctgctggggg gcagccgcaa gcgtgtgctg   9120 

gtgcgtgtgg agcgggccac ggtgtacagc gtggagcagg acaatgatct ggagctggcc   9180 

gacgcctact acctgggggg cgtgccgccc gaccagctgc ccccgagcct gcgacggctc   9240 

ttccccaccg gaggctcagt ccgtggctgc gtcaaaggca tcaaggccct gggcaagtat   9300 

gtggacctca agcggctgaa cacgacaggc gtgagcgccg gctgcaccgc cgacctgctg   9360 

gtggggcgcg ccatgacttt ccatggccac ggcttccttc gcctggcgct ctcgaacgtg   9420 

gcaccgctca ctggcaacgt ctactccggc ttcggcttcc acagcgccca ggacagtgcc   9480 

ctgctctact accgggcgtc cccggatggg ctatgccagg tgtccctgca gcagggccgt   9540 

gtgagcctac agctcctgag gactgaagtg aaaactcaag cgggcttcgc cgatggtgcc   9600 

ccccattacg tcgccttcta cagcaatgcc acgggagtct ggctgtatgt cgatgaccag   9660 

ctccagcaga tgaagcccca ccggggacca ccccccgagc tccagccgca gcctgagggg   9720 

cccccgaggc tcctcctggg aggcctgcct gagtctggca ccatttacaa cttcagtggc   9780 

tgcatcagca acgtcttcgt gcagcggctc ctgggcccac agcgcgtatt tgatctgcag   9840 

cagaacctgg gcagcgtcaa tgtgagcacg ggctgtgcac ccgccctgca agcccagacc   9900 

ccgggcctgg ggcctagagg actgcaggcc accgcccgga aggcctcccg ccgcagccgt   9960 

cagcccgccc ggcatcctgc ctgcatgctg cccccacacc tcaggaccac ccgagactcc  10020 

taccagtttg ggggttccct gtccagtcac ctggagtttg tgggcatcct ggcccgacat  10080 

aggaactggc ccagtctctc catgcacgtc ctcccgcgaa gctcccgagg cctcctcctc  10140 

ttcactgccc gtctgaggcc cggcagcccc tccctggcgc tcttcctgag caatggccac  10200 

ttcgttgcac agatggaagg cctcgggact cggctccgcg cccagagccg ccagcgctcc  10260 

cggcctggcc gctggcacaa ggtctccgtg cgctgggaga agaaccggat cctgctggtg  10320 

acggacgggg cccgggcctg gagccaggag gggccgcacc ggcagcacca gggggcagag  10380 

cacccccagc cccacaccct ctttgtgggc ggcctcccgg ccagcagcca cagctccaaa  10440 

cttccggtga ccgtcgggtt cagcggctgt gtgaagagac tgaggctgca cgggaggccc  10500 

ctgggggccc ccacacggat ggcaggggtc acaccctgca tcttgggccc cctggaggcg  10560 

ggcctgttct tcccaggcag cgggggagtt atcactttag acctcccagg agctacactg  10620 

cctgatgtgg gcctggaact ggaggtgcgg cccctggcag tcaccggact gatcttccac  10680 

ttgggccagg cccggacgcc cccctacttg cagttgcagg tgaccgagaa gcaagtcctg  10740 

ctgcgggcgg atgacggagc aggggagttc tccacgtcag tgacccgccc ctcagtgctg  10800 

tgtgatggcc agtggcaccg gctagcggtg atgaaaagcg ggaatgtgct ccggctggag  10860 

gtggacgcgc agagcaacca caccgtgggc cccttgctgg cggctgcagc tggtgcccca  10920 

gcccctctgt acctcggggg cctgcctgag cccatggccg tgcagccctg gccccccgcc  10980 

tactgcggct gcatgaggag gctggcggtg aaccggtccc ccgtcgccat gactcgctct  11040 

gtggaggtcc acggggcagt gggggccagt ggctgcccag ccgcctagga cacagccaac  11100 

cccggcccct ggtcaggccc ctgcagctgc ctcacaccgc cccttgtgct cgcctcatag  11160 

gtgtctattt ggactctaag ctctacgggt gacagatctt gtttctgaag atggtttaag  11220 

ttatagcttc ttaaacgaaa gaataaaata ctgcaaaatg tttttatatt tggcccttcc  11280 

acccattttt aattgtgaga gatttgtcac caatcatcac tggttcctcc ttaaaaatta  11340 

aaaagtaact tctgtgtaaa aaaaaaa                                      11367 

 
           
             59  
             4255  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 55022490CB1  
             
           
            59 

gcggcacaga cccagctctg aattctgggt caaccatgga ccaactgtga cccttcggac     60 

aagtcccttc gcctctctgg agctggccta taagagggaa aaggaacccc tgtggagagg    120 

gtctatttat cctggcgaag atcgcctgaa gtgatcttct aacaggagtg tttccagagg    180 

aggggctggg ccgggagagg tgtggacagc tggggaccgc tctgagcagc gcagccccgg    240 

gcgccccaca ccaccacatg gtccggggag gaaggtggga gcaggcacac aagaaggaac    300 

ctctgggggt ctgggggccc ctgccatgtg tgaggggtgc ccaggggacc cttggggaca    360 

ggaacggggg cacgggtggg tggcggcact ggggagggtg tgagggtatg cccatgccct    420 

cctcctcgca gaatgtctgc acaaactctg gtgcatctgt ggggaccacc tgtcactcca    480 

agctggatgc agctgtggac ggcacccggt gtggggagaa taagtggtgt ctcagtgggg    540 

agtgcgtacc cgtgggcttc cggcccgagg ccgtggatgg tggctggtct ggctggagcg    600 

cctggtccat ctgctcacgg agctgtggca tgggcgtaca gagcgccgag cggcagtgca    660 

cgcagcctac gcccaaatac aaaggcagat actgtgtggg tgagcgcaag cgcttccgcc    720 

tctgcaacct gcaggcctgc cctgctggcc acccctcctt ccgccacgtc cagtgcagcc    780 

actttgacgc tatgctctac aagggccagc tgcacacatg ggtgcccgtg gtcaatgacg    840 

tgaacccctg cgagctgcac tgccggcccg cgaatgagta ctttgccgag aagctgcggg    900 

acgccgtggt cgatggcacc ccctgctacc aggtccgagc cagccgggac ctctgcatca    960 

acggcatctg taagaacgtg ggctgtgact tcgagattga ctccggtgct atggaggacc   1020 

gctgtggtgt gtgccacggc aacggctcca cctgccacac cgtgagcggg accttcgagg   1080 

aggccgaggg cctggggtat gtggatgtgg ggctgatccc agccggcgca cgcgagatcc   1140 

gcatccaaga ggttgccgag gctgccaact tcctggcact gcggagtgag gacccggaga   1200 

agtacttcct caatggtggc tggaccatcc agtggaacgg ggactaccag gtggcaggga   1260 

ccaccttcac atacgcacgc aggggcaact gggagaacct cacgtccccg ggtcccacca   1320 

aggagcctgt ctggatccag ctgctgttcc aggagagcaa ccctggggtg cactacgagt   1380 

acaccatcca cagggaggca ggtggccacg acgaggtccc gccgcccgtg ttctcctggc   1440 

attatgggcc ctggaccaag tgcacagtca cctgcggcag aggtgtgcag aggcagaatg   1500 

tgtactgctt ggagcggcag gcagggcccg tggacgagga gcactgtgac cccctgggcc   1560 

ggcctgatga ccaacagagg aagtgcagcg agcagccctg ccctgccagg tggtgggcag   1620 

gtgagtggca gctgtgctcc agctcctgcg ggcctggggg cctctcccgc cgggccgtgc   1680 

tctgcatccg cagcgtgggg ctggatgagc agagcgccct ggagccaccc gcctgtgaac   1740 

accttccccg gccccctact gaaacccctt gcaaccgcca tgtaccctgt ccggccacct   1800 

gggctgtggg gaactggtct cagtgctcag tgacatgtgg ggagggcact cagcgccgaa   1860 

atgtcctctg caccaatgac accggtgtcc cctgtgacga ggcccagcag ccagccagcg   1920 

aagtcacctg ctctctgcca ctctgtcggt ggcccctggg cacactgggc cctgaaggct   1980 

caggcagcgg ctcctccagc cacgagctct tcaacgaggc tgacttcatc ccgcaccacc   2040 

tggccccacg cccttcaccc gcctcatcac ccaagccagg caccatgggc aacgccattg   2100 

aggaggaggc tccagagctg gacctgccgg ggcccgtgtt tgtggacgac ttctactacg   2160 

actacaattt catcaatttc cacgaggatc tgtcctacgg gccctctgag gagcccgatc   2220 

tagacctggc ggggacaggg gaccggacac ccccaccaca cagccgtcct gctgcgccct   2280 

ccacgggtag ccctgtgcct gccacagagc ctcctgcagc caaggaggag ggggtactgg   2340 

gaccttggtc cccgagccct tggcctagcc aggccggccg ctccccaccc ccaccctcag   2400 

agcagacccc tgggaaccct ttgatcaatt tcctgcctga ggaagacacc cccatagggg   2460 

ccccagatct tgggctcccc agcctgtcct ggcccagggt ttccactgat ggcctgcaga   2520 

cacctgccac ccctgagagc caaaatgatt tcccagttgg caaggacagc cagagccagc   2580 

tgccccctcc atggcgggac aggaccaatg aggttttcaa ggatgatgag gaacccaagg   2640 

gccgcggagc accccacctg cccccgagac ccagctccac gctgccccct ttgtcccctg   2700 

ttggcagcac ccactcctct cctagtcctg acgtggcgga gctgtggaca ggaggcacag   2760 

tggcctggga gccagctctg gagggtggcc tggggcctgt ggacagtgaa ctgtggccca   2820 

ctgttggggt ggcttctctc cttcctcctc ccatagcccc tctgccagag atgaaggtca   2880 

gggacagttc cctggagccg gggactccct ccttcccaac cccaggacca ggctcatggg   2940 

acctgcagac tgtggcagtg tgggggacct tcctccccac aaccctgact ggcctcgggc   3000 

acatgcctga gcctgccctg aacccaggac ccaagggtca gcctgagtcc ctcagccctg   3060 

aggtgcccct gagctctagg ctgctgtcca caccagcttg ggacagcccc gccaacagcc   3120 

acagagtccc tgagacccag ccgctggctc ccagcctggc tgaagcgggg ccccccgcgg   3180 

acccgttggt tgtcaggaac gccagctggc aagcgggaaa ctggagcgag tgctctacca   3240 

cctgtggcct gggtgcggtc tggaggccgg tgcgctgtag ctccggccgg gatgaggact   3300 

gcgcccccgc tggccggccc cagcctgccc gccgctgcca cctgcggccc tgtgccacct   3360 

ggcactcagg caactggagt aagtgctccc gcagctgcgg cggaggttcc tcagtgcggg   3420 

acgtgcagtg tgtggacaca cgggacctcc ggccactgcg gcccttccat tgtcagcccg   3480 

ggcctgccaa gccgcctgcg caccggccct gcggggccca gccctgcctc agctggtaca   3540 

catcttcctg gagggagtgc tccgaggcct gtggcggtgg tgagcagcag cgtctagtga   3600 

cctgcccgga gccaggcctc tgcgaggagg cgctgagacc caacaccacc cggccctgca   3660 

acacccaccc ctgcacgcag tgggtggtgg ggccctgggg ccagtgctca gccccctgtg   3720 

gtggtggtgt ccagcggcgc ctggtcaagt gtgtcaacac ccagacaggg ctgcccgagg   3780 

aagacagtga ccagtgtggc cacgaggcct ggcctgagag ctcccggccg tgtggcaccg   3840 

aggattgtga gcccgtcgag cctccccgct gtgagcggga ccgcctgtcc ttcgggttct   3900 

gcgagacgct gcgcctactg ggccgctgcc agctgcccac catccgcacc cagtgctgcc   3960 

gctcgtgctc tccgcccagc cacggcgccc cctcccgagg ccatcagcgg gttgcccgcc   4020 

gctgactgtg ccaggatgca cagaccgacc gacagacctc agtgcccacc acgggctgtg   4080 

gcggagctcc cgccccctgc gccctaatgg tgctaacccc ctctcactac ccagcagcag   4140 

gctggggacc tcctccccct caaaaaaggt atttttttat tctaacagtt tgtgtaacat   4200 

ttattatgat tttacataaa tgagcatcta ccattccaaa aaaaaaaaaa aaaaa        4255 

 
           
             60  
             3438  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6755002CB1  
             
           
            60 

tgtgcgccgg gagggccggc gccctcttcc gaatgtcctg cggccccagc ctctcctcac     60 

gctcgcgcag tctccgccgc agtctcagct gcagctgcag gactgagccg tgcacccgga    120 

ggagaccccc ggaggaggcg acaaacttcg cagtgccgcg acccaacccc agccctgggt    180 

agcctgcagc atggcccagc tgttcctgcc cctgctggca gccctggtcc tggcccaggc    240 

tcctgcagct ttagcagatg ttctggaagg agacagctca gaggaccgcg cttttcgcgt    300 

gcgcatcgcg ggcgacgcgc cactgcaggg cgtgctcggc ggcgccctca ccatcccttg    360 

ccacgtccac tacctgcggc caccgccgag ccgccgggct gtgctgggct ctccgcgggt    420 

caagtggact ttcctgtccc ggggccggga ggcagaggtg ctggtggcgc ggggagtgcg    480 

cgtcaaggtg aacgaggcct accggttccg cgtggcactg cctgcgtacc cagcgtcgct    540 

caccgacgtc tccctggcgc tgagcgagct gcgccccaac gactcaggta tctatcgctg    600 

tgaggtccag cacggcatcg atgacagcag cgacgctgtg gaggtcaagg tcaaaggggt    660 

cgtctttctc taccgagagg gctctgcccg ctatgctttc tccttttctg gggcccagga    720 

ggcctgtgcc cgcattggag cccacatcgc caccccggag cagctctatg ccgcctacct    780 

tgggggctat gagcaatgtg atgctggctg gctgtcggat cagaccgtga ggtatcccat    840 

ccagacccca cgagaggcct gttacggaga catggatggc ttccccgggg tccggaacta    900 

tggtgtggtg gacccggatg acctctatga tgtgtactgt tatgctgaag acctaaatgg    960 

agaactgttc ctgggtgacc ctccagagaa gctgacattg gaggaagcac gggcgtactg   1020 

ccaggagcgg ggtgcagaga ttgccaccac gggccaactg tatgcagcct gggatggtgg   1080 

cctggaccac tgcagcccag ggtggctagc tgatggcagt gtgcgctacc ccatcgtcac   1140 

acccagccag cgctgtggtg ggggcttgcc tggtgtcaag actctcttcc tcttccccaa   1200 

ccagactggc ttccccaata agcacagccg cttcaacgtc tactgcttcc gagactcggc   1260 

ccagccttct gccatccctg aggcctccaa cccagcctcc aacccagcct ctgatggact   1320 

agaggctatc gtcacagtga cagagaccct ggaggaactg cagctgcctc aggaagccac   1380 

agagagtgaa tcccgtgggg ccatctactc catccccatc atggaggacg gaggaggtgg   1440 

aagctccact ccagaagacc cagcagaggc ccctaggacg ctcctagaat ttgaaacaca   1500 

atccatggta ccgcccacgg ggttctcaga agaggaaggt aaggcattgg aggaagaaga   1560 

gaaatatgaa gatgaagaag agaaagagga ggaagaagaa gaggaggagg tggaggatga   1620 

ggctctgtgg gcatggccca gcgagctcag cagcccgggc cctgaggcct ctctccccac   1680 

tgagccagca gcccaggaga agtcactctc ccaggcgcca gcaagggcag tcctgcagcc   1740 

tggtgcatca ccacttcctg atggagagtc agaagcttcc aggcctccaa gggtccatgg   1800 

accacctact gagactctgc ccactcccag ggagaggaac ctagcatccc catcaccttc   1860 

cactctggtt gaggcaagag aggtggggga ggcaactggt ggtcctgagc tatctggggt   1920 

ccctcgagga gagagcgagg agacaggaag ctccgagggt gccccttccc tgcttccagc   1980 

cacacgggcc cctgagggta ccagggagct ggaggccccc tctgaagata attctggaag   2040 

aactgcccca gcagggacct cagtgcaggc ccagccagtg ctgcccactg acagcgccag   2100 

ccgaggtgga gtggccgtgg tccccgcatc aggtgactgt gtccccagcc cctgccacaa   2160 

tggtgggaca tgcttggagg aggaggaagg ggtccgctgc ctatgtctgc ctggctatgg   2220 

gggggacctg tgcgatgttg gcctccgctt ctgcaacccc ggctgggacg ccttccaggg   2280 

cgcctgctac aagcactttt ccacacgaag gagctgggag gaggcagaga cccagtgccg   2340 

gatgtacggc gcgcatctgg ccagcatcag cacacccgag gaacaggact tcatcaacaa   2400 

ccggtaccgg gagtaccagt ggatcggact caacgacagg accatcgaag gcgacttctt   2460 

gtggtcggat ggcgtccccc tgctctatga gaactggaac cctgggcagc ctgacagcta   2520 

cttcctgtct ggagagaact gcgtggtcat ggtgtggcat gatcagggac aatggagtga   2580 

cgtgccctgc aactaccacc tgtcctacac ctgcaagatg gggctggtgt cctgtgggcc   2640 

gccaccggag ctgcccctgg ctcaagtgtt cggccgccca cggctgcgct atgaggtgga   2700 

cactgtgctt cgctaccggt gccgggaagg actggcccag cgcaatctgc cgctgatccg   2760 

atgccaagag aacggtcgtt gggaggcccc ccagatctcc tgtgtgccca gaagacctgc   2820 

ccgagctctg cacccagagg aggacccaga aggacgtcag gggaggctac tgggacgctg   2880 

gaaggcgctg ttgatccccc cttccagccc catgccaggt ccctaggggg caaggccttg   2940 

aacactgccg gccacagcac tgccctgtca cccaaatttt ccctcacacc ctgcgctccc   3000 

gccaccacag gaagtgacaa catgacgagg ggtggtgctg gagtccaggt gacagttcct   3060 

gaaggggctt ctgggaaata cctaggaggc tccagcccag cccaggccct ctccccctac   3120 

cctgggcacc agatcttcca tcagggccgg agtaaatccc taagtgcctc aactgccctc   3180 

tccctggcag ccatcttgtc ccctctattc ctctagggag cactgtgccc actctttctg   3240 

ggttttccaa gggaatgggc ttgcaggatg gagtgtctgt aaaatcaaca ggaaataaaa   3300 

ctgtgtatga gcccagggta gggggagagg gcctgggctg ggctggagcc tcctaggtat   3360 

ttcccagaag ccccttcagg aactgtcacc tggactccag caccacccct cgtcatgttg   3420 

tcacttcctg tggtggcg                                                 3438 

 
           
             61  
             1683  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7350907CB1  
             
           
            61 

ggcgtgggga cacgagccag gcgccgccgc cggagccagc ggagccgggg ccagagccgg     60 

agcgcgtccg cgtccacgca gccgccggcc ggccagcacc cagggccctg catgccaggt    120 

cgttggaggt ggcagcgaga catgcacccg gcccggaagc tcctcagcct cctcttcctc    180 

atcctgatgg gcactgaact cactcaagtg ctgcccacca accctgagga gagctggcag    240 

gtgtacagct ctgcccagga cagcgagggc aggtgtatct gcacagtggt cgccccacag    300 

cagaccatgt gttcacggga tgcccgcaca aaacagctga ggcagctact ggagaaggtg    360 

cagaacatgt ctcaatccat agaggtcttg gacaggcgga cccagagaga cttgcagtac    420 

gtggagaaga tggagaacca aatgaaagga ctggagtcca agttcaaaca ggtggaggag    480 

agtcataagc aacacctggc caggcagttt aaggcgataa aagcgaaaat ggatgaactt    540 

aggcctttga tacctgtgtt ggaagagtac aaggccgatg ccaaattggt attgcagttt    600 

aaagaggagg tccagaatct gacgtcagtg cttaacgagc tgcaagagga aattggcgcc    660 

tatgactacg atgaacttca gagcagagtg tccaatcttg aagaaaggct ccgtgcatgc    720 

atgcaaaaac tagcttgcgg gaagttgacg ggcatcagtg accccgtgac tgtcaagacc    780 

tccggctcga ggttcggatc ctggatgaca gaccctctcg cccctgaagg cgataaccgg    840 

gtgtggtaca tggacggcta tcacaacaac cgcttcgtac gtgagtacaa gtccatggtt    900 

gacttcatga acacggacaa tttcacctcc caccgtctcc cccacccctg gtcgggcacg    960 

gggcaggtgg tctacaacgg ttctatctac ttcaacaagt tccagagcca catcatcatc   1020 

aggtttgacc tgaagacaga gaccatcctc aagacccgca gcctggacta tgccggttac   1080 

aacaacatgt accactacgc ctggggtggc cactcggaca tcgacctcat ggtggacgag   1140 

agcgggctgt gggccgtgta cgccaccaac cagaacgctg gcaacatcgt ggtcagtagg   1200 

ctggaccccg tgtccctgca gaccctgcag acctggaaca cgagctaccc caagcgcagc   1260 

gccggggagg ccttcatcat ctgcggcacg ctgtacgtca ccaacggcta ctcagggggt   1320 

accaaggtcc actatgcata ccagaccaat gcctccacct atgaatacat cgacatccca   1380 

ttccagaaca aatactccca catctccatg ctggactaca accccaagga ccgggccctg   1440 

tatgcctgga acaacggcca ccagatcctc tacaacgtga ccctcttcca cgtcatccgc   1500 

tccgacgagt tgtagctccc tcctcctgga agccaagggc ccacgtcctc accacaaagg   1560 

gactcctgtg aaactgctgc caaaaagata ccaataacac taacaatacc gatcttgaaa   1620 

aatcatcagc agtgcggatt ctgacatcga gggatggcat tacctccgtg tttctccctt   1680 

tcg                                                                 1683 

 
           
             62  
             6886  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474411CB1  
             
           
            62 

cggggcacag cgggagcccg tgcaggcggg cgcggggcgg ctgggcggcg gtggcggccg     60 

tccatgcggc ggcgctcggg gctgcccggc gccgggaacc acgcgggggc gaggcgaggc    120 

gaggcggccg ccggtcgctc cgggacgcgg accgccagga cttgaacgca actcccaatt    180 

gcagaaaatt ggcaacgtct ctgaagagcc cttgcttttg cctggacccc cagcatcatg    240 

gtttcccatt tcatggggtc tctcagtgtc ctgtgtttcc ttctgctgct tggattccag    300 

ttcgtctgcc cacagccctc cactcaacac aggaaggtcc cgcagcggat ggcggcggag    360 

ggcgcccccg aggacgacgg cggcggcggc gccccgggag tgtggggcgc ctggggcccc    420 

tggtcggcct gctcgcgtag ctgcagcggc ggcgtgatgg agcagacgcg gccctgcctg    480 

ccccgctcct accgcctgcg cggcggccag cggcctggcg cccctgcgcg cgccttcgcg    540 

gaccacgtgg tgtcggcggt gcgcacgtcg gtgccactgc accggagccg cgacgagacg    600 

ccagcgctgg ccggtacgga cgccagccgc cagggcccca cggtgctgcg aggcagccgg    660 

cacccacagc cccagggcct cgaagtcact ggggacagaa ggagcaggac ccgtggtacc    720 

attggccctg gcaagtatgg ctatggtaag gccccatata tcttaccact gcagacagac    780 

actgcacaca cgccacagag gctccggaga cagaagctct catcccgcca ttccaggtcc    840 

cagggagcat cttctgctag gcatggctac agttcaccag cccaccaggt cccccaacat    900 

gggcctttgt accaaagtga cagtggccct cgctctggac tgcaggctgc ggaggccccc    960 

atctaccagc tacctttgac ccatgatcaa ggctaccctg cagcttcaag tctctttcac   1020 

agcccagaaa caagcaacaa ccacggtgtg gggacccatg gggcaactca gagcttctct   1080 

cagcctgccc gatctacagc aatctcatgc atcggggcct atcggcagta caagctgtgc   1140 

aacaccaacg tatgtccaga aagcagtaga agtatccggg aggtacagtg tgcatcctac   1200 

aacaacaagc cattcatggg ccggttttat gagtgggaac catttgcaga agtaaaaggc   1260 

aatcgcaaat gtgagttgaa ctgccaggca atgggctacc gcttctatgt acggcaagct   1320 

gagaaagtca tcgatggcac cccctgtgac cagaacggca cggccatctg tgtgtctggg   1380 

cagtgcaaga gcattggctg tgatgactac ttaggctccg acaaagtcgt ggacaaatgt   1440 

ggggtgtgtg gaggagacaa cacgggctgt caggttgtgt cgggcgtgtt taagcatgcc   1500 

ctcaccagcc tgggctacca ccgcgtcgtg gagattcccg agggagccac gaaaatcaac   1560 

atcacggaga tgtacaagag caacaactat ttggccctga gaagtcgttc tggacgctcc   1620 

atcatcaatg ggaactgggc aattgatcga ccaggaaaat acgagggcgg agggaccatg   1680 

ttcacctaca agcgtccaaa tgagatttcg agcactgccg gagagtcctt tttggcggaa   1740 

ggtcccacca acgagatctt ggatgtctac atgatacacc agcagccaaa cccaggcgtg   1800 

cactacgagt acgtgatcat ggggaccaac gccatcagcc cccaggtgcc accccacagg   1860 

agaccagggg aacccttcaa tggccagatg gtgacagaag gcaggagcca ggaggaggga   1920 

gaacagaaag ggaggaacga ggagaaggaa gacttgcgtg gggaggcccc tgagatgttc   1980 

acctcagaat cggcacagac cttcccagtc aggcatccag acagattttc tccccatcga   2040 

ccggacaact tggtgccacc agcaccgcag cccccacggc gcagccggga tcacaactgg   2100 

aagcagcttg ggacaacaga atgttccacg acctgtggga aaggatcgca gtaccctatt   2160 

ttccgctgtg tgcacagaag cactcatgaa gaggctcctg agagttactg tgactccagc   2220 

atgaagccga cccccgagga ggagccctgc aacatcttcc cttgcccagc cttctgggac   2280 

atcggggagt ggtctgagtg cagcaagacc tgtggcctgg gcatgcagca ccgccaggtt   2340 

ctgtgccgcc aggtgtacgc caaccgcagc ctgacggtgc agccctaccg ctgccagcac   2400 

ctggagaaac ctgagaccac cagcacctgc caactcaaga tctgcagcga gtggcagatc   2460 

cggaccgact ggacctcgtg ctcggtgccc tgtggcgtgg gacagaggac ccgtgatgtg   2520 

aagtgtgtga gcaacattgg ggatgtggtt gacgatgagg aatgcaacat gaagctccgg   2580 

ccgaatgaca ttgagaactg cgacatggga ccctgtgcca agagctggtt cctcaccgag   2640 

tggagcgaaa ggtgctcagc ggagtgtggg gccggagtgc ggacacgctc ggtggtgtgc   2700 

atgaccaacc atgtcagcag cctgcccctg gagggctgtg ggaacaaccg gccggcagag   2760 

gccaccccat gtgacaacgg accctgcacg ggcaaggtgg agtggtttgc cgggagctgg   2820 

agtcagtgtt ccatcgagtg tgggagcggg acgcaacaga gggaggtgat ttgtgttaga   2880 

aagaatgcag acacctttga agtgttggac ccctctgaat gttctttcct ggagaaaccc   2940 

cccagccagc aatcctgcca cctcaagcct tgcggagcca aatggtttag caccgaatgg   3000 

agcatgtgtt ccaagagctg ccagggtggc tttcgggtcc gggaagtgcg gtgtctgtct   3060 

gatgacatga ctctaagtaa cctctgtgac cctcagttga aaccagaaga gagagaatct   3120 

tgtaaccctc aggactgtgt ccctgaagtt gatgaaaact gcaaggacaa gtactacaac   3180 

tgcaacgtgg tggtccaggc aagactctgt gtctacaact actacaagac cgcctgctgt   3240 

gcctcctgca cccgtgtggc caacaggcag acgggcttcc tggggagcag ataacactcc   3300 

tgcaccccca tcagtagggc agcatcactg ccttcccggg ggcttcagca gtgcgcctgg   3360 

ctggctgctg ctccaccacg ggccccctgg cccaggcgct gccaaccaac ttagtcacca   3420 

cccctgcctc cggtgaatgc accccgtggt acccaggggc tttttacaca agatgtttga   3480 

aagccacagt cagtccttta agcatcacca tgtactgatg atcccctcct tggacctggc   3540 

atctgctaat ggtgcccttt gaaagtcaag cagtgggaag tacatggagc tctcagccct   3600 

gctcccatct ggcaccttca agtcagcaga tgggccactg actgagcact gccccgtccc   3660 

tggtgctact ggtctttcta aacttagcac cctggagagt ccaaggaggc agcgccccca   3720 

acccagcgcc ccactaagcc ttgctgacac gcgtgcatcc ctctgtgacc tcagcccaga   3780 

tgtgcctgtt ttcattctca aagacattag actgttttcc tgccctatga cacagatagc   3840 

tcacatgaat attgtgcttt atttagcagg tgtactcaca gatactagct ccttagcagc   3900 

tcacaacatc ccagaatggg aggcaggggg tgactcatta tccccatttt actgacaggg   3960 

aaactgaggc tcaacttaag taattgacct gccaggtata ttcacccatc cagtggaaga   4020 

gctgagtccc cgccccagtc atctaccagt atccagcctg gggcctgtac ttagatgtga   4080 

aaggtgctgc ttcatttctg accaagagac tgagaagttt cccagaatgc aaacaaagcc   4140 

caggcccctg aaatctttcc ggtcaagcct ttatcccagc actcagttgt tttggatgtc   4200 

tgttcctact tgcccttacc cccaaagtta cagatcctag ttacaggact ctgccagctt   4260 

tgttaaactg tccgtgagac aagaaagcca ttggggaaac caggtgattg cctgaaattc   4320 

ttactccgtt ccaagtgctg ttcctcccag gaaatcaaag gccagggtcc ttatggccgt   4380 

ggagccttcc cgaccacaga gccaacttgt gaagcacaca gctctgcagc ctgggctctg   4440 

ccctgcctca gccgcctccc ccacgctctt caccacgttc ctggagagtc cggccaacct   4500 

gtcccagcca aaacactgct gtattagaaa aagtctcttt ctggtctttc tggttttgtt   4560 

tatgaatttc cctctgtggc cacaaattcc tcccctcccc catgactcac agtccatatg   4620 

gcccaccccc agacttgagc accaagctct gcattaatgc agttggcctg cgacaaggag   4680 

ctgtggaccc ttccccatct cttccaattc actttcccca actatccagt tccagaggcc   4740 

gcaggcctgg aaggatgcag tgcatattga aaggtggacc ctctgaaaac agttaagagg   4800 

aatatatgta tgttttgccc attaagaaaa aatggcaagc taaacaaatg ttaaacttac   4860 

agaaaatttg tcttatggtc ctgagcatat ttccctttta gagcaagcct ggattcttag   4920 

caaagtgttt cccccatttg ctcttttagc tgacaaatct gccactgtga tgatggtttg   4980 

cagcttttgg aagcagtatg gcaacctggc ctgacatgct ctttaggctt ccactaacct   5040 

ggggctttca gaaattctat ttggcctttc tgtgggtagc tttccagctt ctcttctagg   5100 

gagccccagg catcatttcc caaaagcatc cccatctcct gattctcttg gaactcctac   5160 

agataagcat cctggcagag gcccaggctc ccaaaccgac aaagtgaaaa gagaccagag   5220 

aggccaagca tattgactgg tgctgttcag ggcctgctct tttccactca ccacttgttt   5280 

tgctgcttgt cacgaggaga gttgttcctg tatgtggctg ctctcagatc tttccaagca   5340 

agccagtcat ttgaagaggt tttcttttca tgctggaggg caggctaaga tcaatgagtg   5400 

gaagagagaa aggctgtttt agctcaagtt aaaggaacac cttctagcca tcaaagccgc   5460 

ccaacagagg caagggccac cacacatgag agagcgctct gtccttaaag ggaattctct   5520 

gttgagtggg aggtgaacac cctggttctt ccaactcagg aattctcgtg gctgggctgg   5580 

gtcagtgatg gctttgtctc tttatgtcta aagtgcccta tggctgctga aggttaccta   5640 

accattcttt aaaaggagaa tgaccctcca tgggaatggc cagcctgcca actgtgcaat   5700 

tgaagaagac ccgatggatc aaccccatgt ctcccttggg gagaaagtgc ataaaccagg   5760 

ggtctctttt tttttttttt caacaaacca ttgagctgtt cttggagttc atctctggag   5820 

aggttataca ttattagaag tttgattatt attatagttt gatcaattta tttgtcttag   5880 

agatccaatt tttactaatt ccctagtttt ttatttcagc atctgaatgt ctttctccct   5940 

agcacagtgc atacaatcag ggccttgggt atttccagtg ataactttcc ttggagagga   6000 

tctaagaaaa gcccagattt cggtagccat ctccctccaa atatgtctct ttctgctttc   6060 

ttagtgccca ttatttcccc ttctcctttc ttctgtcact gccatctcct tcttggtctt   6120 

cccattgttc tttaactggc tgtaatgtgg aattgatatt tacattttga tacggttttt   6180 

ttcttggcct gtgtacggga ttgcctcatt tcctgctctg aattttaaaa ttagatatta   6240 

aagctgtcat atggtttcct cacaaaagtc aacaaagtcc aaacaaaaat agtttgccgt   6300 

tttactttca tccattgaaa aaggaaattg tgcctcttgc agcctaggca aaggacattt   6360 

agtactatcg attctttcca ccctcacgat gacttgcggt tctctctgta gaaaagggat   6420 

ggcctaagaa atacaactaa aaaaacaaac aaaaacacca aaagaaaaaa aaaagccatt   6480 

taaagccagc cactagaggg agtcagttca gttccgtaaa ggtatgctca gtgcccgctg   6540 

cctgcaagct gttggggacc ccagggaggg caaggcagcc tgtccccgcc cccagggaac   6600 

tagaacatga caagaattct ccgcactgtg cctacctgtc cctttaactt acctctctgg   6660 

cccagagttc ttggagggta aaccttctat ttctcttatg tactcatcta cttattctca   6720 

aagtatttag cattcaacac tcttttggct ttaaaaagaa tgggccttac aaagggacag   6780 

aacacgagaa gacacgagct aggtgtattt catcaagtat gtggcacgag aaatccagat   6840 

attaccagga cctgtctaac caatgtgggg ttactttcat cggatg                  6886 

 
           
             63  
             4457  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4755911CB1  
             
           
            63 

atggggaagg agcaggagct ggtgcaggcg gtgaaggcgg aggacgtagg gaccgcgcag     60 

aggctgctgc agaggccgcg gcccgggaag gccacgcgta gcctccctgg gggccgccgg    120 

agatggatgg atgggcgtgt ggaccagccg cgtgtgcggc tgcgcacgta tagccgtgtc    180 

agtgtgtcag ggcacctgtg cgggcacgga cagggctctg cagagctcct gggttccacc    240 

aagaagatca atgtcaactt ccaggacccg gatggggttg ggtttggggt caagggtcag    300 

ctcccagcat cccctcgccc cccaggcatg cggccgctgc actatgcggc ctggcagggc    360 

cggaaggagc ccatgaagct ggtgctgaag gcgggctcgg ccgtgaacat cccgtctgat    420 

gagggccaca tccccctgca cctggcggcc cagcatggtc actatgatgt gtctgagatg    480 

ctgctacagc accagtctaa cccgtgcatg gtggacaact cggggaagac gcccctggac    540 

ctggcctgcg agttcggccg cgttggggtg gtccagctgc tcctcagcag caatatgtgt    600 

gcggcgctgc tggagccccg gccgggagac gccaccgacc ccaacggcac cagccctttg    660 

cacctcgcag ctaaaaacgg ccacatcgac atcatcaggc tcctcctcca agccggcatc    720 

gacattaacc gccagaccaa gtccggcacg gccctgcacg aggctgcgct ctgcggaaag    780 

acagaggtgg tgcggctgct gctggatagc gggatcaatg cccacgtgag gaacacctac    840 

agccagacag ccctggacat cgtgcaccag ttcaccacgt cccaggccag cagggagatc    900 

aagcagctgt tgcgagaggc ctcagcggcc ctgcaggtcc gggcgaccaa ggattattgc    960 

aacaattacg acctgaccag cctcaacgtg aaggcagggg acatcatcac agtcctcgag   1020 

cagcatccgg atggccggtg gaagggctgc atccatgaca accggacggg caatgaccgg   1080 

gtgggctact tcccgtcctc cctgggcgag gccattgtca agcgagcagg ttcccgagca   1140 

ggcactgaac caagcctgcc ccagggaagc agctcatcgg gaccctctgc acccccagag   1200 

gagatctggg tgctgaggaa gccttttgca ggtggggacc gaagcggcag cattagcggc   1260 

atggctggcg gccggggcag cgggggtcac gccctacacg cgggctctga aggcgtcaag   1320 

ctcctggcaa cggtgctttc ccagaagtcc gtctctgagt ccggcccggg ggacagcccc   1380 

gccaagcctc cggaaggctc tgcaggtgtg gcccggtccc agcctccagt ggcccacgcc   1440 

gggcaggtct atggggagca gccgcccaag aagctggagc cagcatcgga gggcaagagc   1500 

tctgaggccg tgagccagtg gctcaccgcg ttccagctgc agctctacgc ccccaacttc   1560 

atcagcgccg gctacgacct gcccaccatc agccgcatga ctcccgagga cctcacggcc   1620 

attggtgtca ccaagccggg ccaccggaag aagatcgcgg cagagatcag cggcctaagc   1680 

atccctgact ggctgcctga gcacaaaccc gctaacctgg ccgtgtggct gtccatgatc   1740 

ggcctggccc agtactacaa ggtgttggtg gacaatggct acgagaacat tgatttcatc   1800 

accgacatca cctgggagga cctgcaggag atcggcatca ccaagctggg gcaccagaag   1860 

aagctgatgc tcgctgtgag gaagctggca gagctgcaga aggctgaata cgccaagtat   1920 

gaggggggcc ccctgcgccg gaaggcgccc cagtctcttg aagtgatggc catcgagtcg   1980 

ccgcccccgc ctgagcccac accggccgac tgccagtccc ctaaaatgac caccttccag   2040 

gacagcgagc tcagtgacga gctgcaggct gccatgactg gcccggctga ggtggggccc   2100 

accactgaga agccctccag ccacctgcca cccaccccga gggccaccac gcggcaggac   2160 

tccagcctgg gtggtcgggc acggcacatg agcagctcgc aggagctgct gggagatggg   2220 

ccccctgggc ccagcagccc catgtctcga agccaggagt acctcctgga tgagggcccc   2280 

gcccccggca ccccgcccag ggaggcccgg cccggccgcc acggccacag catcaagagg   2340 

gccagcgtgc cccccgtgcc tggcaagcca cggcaggtcc tcccaccagg cactagccac   2400 

ttcacgcccc cccagacgcc caccaaaacc cgaccaggct ctccccaggc ccttggggga   2460 

cctcatggtc cagccccagc tacggccaag gtgaagccca ccccgcagct gctgccgccg   2520 

acagagcgcc ccatgtcacc ccgctccctg cctcagtcac cgacgcaccg cggctttgcc   2580 

tacgtgctgc cccagcccgt ggagggcgag gtggggccgg ctgccccggg gcctgcgccc   2640 

ccacccgtgc cgacggctgt gcccacactg tgcctgcccc ctgaggccga cgcggagccg   2700 

gggcggccca agaagcgggc ccacagcctg aatcgctatg cggcgtccga cagcgagccg   2760 

gagcgggacg agctgctggt gcctgcggct gccggcccct atgccacggt ccagcggcgc   2820 

gtgggccgca gccactcagt gagggcgccc gcaggtgccg acaagaacgt caaccgcagc   2880 

cagtcctttg ccgtgcggcc ccgaaagaag gggcccccgc cgcccccacc caagcgctcc   2940 

agctcggccc tggctagtgc caacctggcg gatgagccgg tgcctgacgc cgagcctgag   3000 

gatggcctgc tgggggtccg ggcacagtgc cggcgggcca gtgacctggc cggcagcgtg   3060 

gacacgggta gtgccggcag tgtgaagagc atcgcggcca tgctggagct gtcctccatt   3120 

gggggtgggg gccgggctgc ccgcaggcct cctgagggcc accccactcc ccgccctgcc   3180 

agcccagagc cgggccgggt ggccaccgtg ctggcctcag tgaaacacaa agaggccatc   3240 

gggcctggcg gggaggtggt gaaccggcgc cgcacgctca gcgggccagt caccggactt   3300 

ctggccactg cccgccgggg gcctggggag tcggcagacc caggcccctt tgtggaggat   3360 

ggcactggcc ggcagcggcc tcggggtccc tccaagggcg aggcgggtgt cgaaggcccg   3420 

cccttggcca aggtggaagc cagcgccaca ctcaagaggc gcatccgggc caagcagaac   3480 

cagcaggaga acgtcaagtt catcctgacc gagtctgaca cggtcaagcg caggcccaag   3540 

gccaaggagc gggaggccgg gcctgagcca ccaccgccac tgtccgtgta ccataatggc   3600 

actggcaccg tgcgccgccg accggcctcg gagcaggctg ggcctccgga gctgcctcca   3660 

ccgcccccgc ctgccgaacc cccgcccacc gacctggcgc acctaccccc attgcccccg   3720 

cccgagggcg aagcccggaa gccggccaag ccgcctgtct ctcccaagcc cgtcctgacg   3780 

cagcctgtgc ccaagctcca gggctcgccc acacccacct ccaagaaggt gccgctgcca   3840 

ggccctggca gcccagaggt gaagcgcgcc cacggcacgc caccgcccgt gtctcccaag   3900 

ccgccgccgc cgcccacagc gcccaagccc gtcaaggcgg tcgcggggct gccttcgggc   3960 

agcgccggcc cttcacccgc accctcgccc gcgcgacagc cgcccgccgc cctcgccaag   4020 

ccgcccggta cgccgccctc gctgggcgcc agccccgcca agcccccgtc ccccggcgcg   4080 

cccgcgctgc acgtgcccgc caagcccccg cgagccgccg ccgccgccgc cgccgccgcc   4140 

gccgcgcccc ccgccccgcc cgaaggcgcc tcgccagggg acagcgcccg gcagaaactg   4200 

gaggagacaa gcgcgtgcct ggccgcggcg ctgcaggcgg tggaggagaa gatccggcag   4260 

gaggacgcgc agggcccgcg cgactcggcg gcggaaaaga gcactggcag catcctggac   4320 

gacatcggca gcatgttcga cgacctggcc gaccagctgg atgccatgct ggagtgaacg   4380 

ccgcctggcc gggccctccc gcgccgcccg ggccctcccc gcacactgac ctatacctca   4440 

ggatgggcgc gtctggg                                                  4457 

 
           
             64  
             1943  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 379766CB1  
             
           
            64 

ggcggcggcg actgcggcgc cgcgggctgg aggccggcgt cggggaaggt cctggtgccg     60 

gattccgcac gaggtgttga cgggcggctt ctgccaactt ctccccagcg cgcgccgagc    120 

ccgcgcggcc ccggggctgc acgtcccaga tacttctgcg gcgcaaggct acaactgaga    180 

cccggaggag actagacccc atggcttcct ggacgagccc ctggtgggtg ctgataggga    240 

tggtcttcat gcactctccc ctcccgcaga ccacagctga gaaatctcct ggagcctatt    300 

tccttcccga gtttgcactt tctcctcagg gaagttttct ggaagacaca acaggggagc    360 

agttcctcac ttatcgctat gatgaccaga cctcaagaaa cactcgttca gatgaagaca    420 

aagatggcaa ctgggatgct tggggcgact ggagtgactg ctcccggacc tgtgggggag    480 

gagcatcata ttctctgcgg agatgtttga ctggaaggaa ttgtgaaggg cagaacattc    540 

ggtacaagac atgcagcaat catgactgcc ctccagatgc agaagatttc agagcccagc    600 

agtgctcagc ctacaatgat gtccagtatc aggggcgtta ctatgaatgg cttccacgat    660 

ataatgatcc tgctgccccg tgtgcactca agtgtcatgc acaaggacaa aacttggtgg    720 

tggagctggc acctaaggta ctggatggaa ctcgttgcaa cacggactcc ttggacatgt    780 

gtatcagtgg catctgtcag gcagtgggct gcgatcggca actgggaagc aatgccaagg    840 

aggacaactg tggagtctgt gccggcgatg gctccacctg caggcttgta cggggacaat    900 

caaagtcaca cgtttctcct gaaaaaagag aagaaaatgt aattgctgtt cctttgggaa    960 

gtcgaagtgt gagaattaca gtgaaaggac ctgcttatcc tgtggcctgg gctttagcca   1020 

tctcttccaa taccaattgc ctagtgttat tatgtaaagc taatttggcc agctctggtc   1080 

cttattttgc actcattcca gtaaacccaa ccactatggc acttaatact gccattgtca   1140 

gtcagtctgc agtattgatt gactgccttt agagctctct tttgtgtgcc ttgtccactc   1200 

ttcagtcact gagagagaga ccaaagaaca gagaccaaca ccctgtactt ggcatggcca   1260 

ttagtcactg gagttagatg aatcacactg tatctaagag agaagactca gggagaaggg   1320 

cttagcacaa cacagaaaag ctttaaacac tcttaccttt gactggaatt acacacacac   1380 

acacacacac acacacatac acacacacac atacacacac acacactaag gctttcccac   1440 

aaagccatga tgcatcctta aaaataacac acagctctga aaagtgaatg tcgggggtga   1500 

agagagccct cctacactcc ttttcctagt gatgacaagg ttgtgggggc atggctgact   1560 

gtgaggagca gaagatgaga gggagatatc attttacttc tttgtactgc aataataaaa   1620 

agaacagata gaatggaagg aagaggccag gggcagtggc tcatacctgt aatcccagca   1680 

ctttgggagg ctgaggcagg tggatcacct gaggtcagga gttcgagacc agcctggcca   1740 

acatggagaa actccgtctc tattaagaat acaaaaatta gccaggcgtg gtggtgggca   1800 

cctataatca cagctacccg ggaggttgag gcaggagaat cacttgaact tgtggggcgg   1860 

aggtcgcagt gagccaagat tgcaccactt cactccagcc tgggcgagaa agtgaactct   1920 

gtctcaaaaa aaaaaaaaaa aaa                                           1943 

 
           
             65  
             4111  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 553744CB1  
             
           
            65 

gcgatctagg gcggggcaac tgtacagatg aacaatctgg aatattaaat tcaactcaca     60 

gagtggcaac aaacaatact ggagagctgg gcatgaatcc tggaaagcct tgtatggccc    120 

tgcaagggaa gccatgttct gaaagctcct atgaggggga ctgactgact ctagataagt    180 

agattgaaag aattagaggt aaagtcagtg cagcagcact aatcacaatt aaaataaatg    240 

ctttaatttt taaaaagcgg aaaaacatga aaggacactt cgcaagcttc tcaaaacttc    300 

ctgtgatttg gagggctatt ttgagcagag tctagacgaa aactggatct gactggctcc    360 

agagtaaaga tctgagaaat ggaacccagc aatttagata ttacaagagc ctgttatact    420 

tgtcattttt tatttggtat ttgttaaata ttacaaaaat ggttatgctt tttaattcaa    480 

aatttgacgt ttcagcatga tgatacattc ttgccttttt tcccccttcc atatagcatt    540 

ttccacccca gcaagtcaac tcttttctcc tcatggttct aatccttcaa cacctgctgc    600 

aactcctgtt cctactgcat ccccagtcaa ggcaattaat catccatcag catcagcagc    660 

tgccaccgtt tctggaatga acctgctgaa tactgtcctt cctgtgttcc cagggcaggt    720 

ctcctcagcc gttcacacac ctcagccatc aataccaaac ccaacagtta tcagaacccc    780 

ttcattgccc actgcacctg ttacatccat ccacagtaca accaccactc ctgttccttc    840 

cattttttct ggcctagtgt cactgccagg tccttctgcc actcctaccg cagccactcc    900 

taccccagga cctacaccac ggtccactct tggttccagt gaagcatttg cttctacttc    960 

tgcacctttc actagcctcc ccttttccac cagctcttct gctgcttcta ccagcaaccc   1020 

aaattctgct tcattgtcat cagtttttgc agggctccct ttgcccttac caccaacatc   1080 

ccaaggccta tccaacccga ctcctgtaat tgctggtggc tctactccca gcgttgccgg   1140 

tccacttggt gtgaacagtc catcttttgt ctgcgttaaa aggttttctg acatccaatg   1200 

acaccaattt aatcaactcc tctgctttat cctctgctgt cacaagtggg ctggcttcac   1260 

tatcttctct tactcttcag aactctgact cttctgcttc agcccctaac aagtgctatg   1320 

ccccatcagc catccctacc ccacagagga cttccactcc agggttggcc ctgttcccag   1380 

gcctgccgtc tcccgtggct aactcaactt ccactcccct gacattgcct gtacagtctc   1440 

ctttagccac tgctgcatca gcttccacgt cagtgccagt tagctgtggc tcctcagcct   1500 

cccttttgcg tggcccccac ccaggtacct cagatctgca tatttcatct acccctgctg   1560 

caacaactct tcctgttatg atcaaaactg agcccacaag tcctactccc tcggccttca   1620 

aaggtccatc tcattctggg aatccctctc atggcacttt aggtttgtca gggacattgg   1680 

gccgtgcata tacttcaaca tccgtgccca tcagtttatc tgcttgcctt aatcctgcat   1740 

tgtcaggtct ctccagcttg agtactcctt taaatggttc aaatcctctt tcctctattt   1800 

cccttccacc acatggttcc tccactccca ttgcaccagt attcactgct cttccttctt   1860 

ttacttcttt gaccaacaat tttcctttaa ctggcaaccc atctcttaat ccgtcagtat   1920 

ctctcccagg gtcattaata gccacctcat ctaccgctgc cacctccaca tctctccctc   1980 

atcctagctc aacggcagct gttctctcag ggctttctgc ttcagcacca gtctcagcag   2040 

cacctttccc cctcaacctg tccactgctg ttccctcact tttctctgtt actcaaggac   2100 

ctctgtcatc ttcaaatccc tcctatccag gcttttctgt ctctaatacc ccaagcgtta   2160 

cccctgctct tccctcattc ccggggctgc aggcgccctc tacagtcgca gctgtcacac   2220 

cactacctgt ggctgccaca gccccatccc cagctccagt cctcccagga ttcgcctcag   2280 

cattcagttc caatttcaac tccgctcttg ttgcacaagc cggtttatca tctggacttc   2340 

aagctgcagg cagttctgtt tttccaggcc ttttgtccct cccgggtatc cctgggtttc   2400 

ctcagaatcc ttcacaatca tccttgcaag aattacagca taatgcggct gcgcagtcag   2460 

cattgttaca gcaggtccat tcagcttcgg ctctggaaag ctatccagct cagcctgatg   2520 

ggtttcctag ttatccttca gcgccaggaa caccattttc tttgcaacca agcctgtccc   2580 

agagtgggtg gcagtgaata cttttaactt ttattctcct tcagagcaac atcagaattg   2640 

cctgagaact gcaatgaaca atctgacaaa tgtgaagctg gccaaaagtc ggaaaatgag   2700 

aatgagggta atcctggaga aattgtgaca acaatttgaa aattgtggtt gcattttaaa   2760 

gtgtgaacac tcccctatgt aaatatgctg acaataaatt gtatggagaa tggtatttaa   2820 

aaagtgtttg gagacttttc acctgtccta taaaattttg aattgtgtat gtgatctaca   2880 

tagaaagaat attaaagagt aggttgaact ctttatagcc gaatacagcc ttaaatatgc   2940 

ttgtatagca tccactggca gaagtaatag ttgtgcctca gacttggggg ttgcatgtgg   3000 

ccctggggga gttactaccc ttggtatgca tgagcggttc ctattagcat cagtgggaac   3060 

tcagtactct gtatgtatcc acaaaaggga acttgagacc cacagttatt cttaatttct   3120 

gatattaaca accgtacata ctgctgaatt taactcaaaa tatttcaggt aagtgaaagt   3180 

ggtgcttaat gtagactata gaatgacttt caggtgtttt caactgaaag tatatatcca   3240 

gaactgcatc cttatagaaa tacaagtaag acttaggata atttgccttc aaaacagttt   3300 

tcctaatctc agcagtatcc agtgagtgaa gaacacttga ctgactcttg ggccacctct   3360 

gttacttact gtactatgga agctcctggt gaatgtttac aattatggga tgtagtattt   3420 

ctatttgtac tttaagtcaa atgcttatat gaaatatgtg acaacaaata gagaagactg   3480 

gctctgttag taattatgca gtatgtactc tatttaagga tctgtggtag tataacatga   3540 

gtgaatgtca ttaattttga agtaataact gccacatgtg ggaagtaggg gagtaaggag   3600 

aatgaattcc aatctgtgat taaaagtgta aactatagac tctactgtag tacatttcag   3660 

gatctagaag ttttactttt ataaagatgg tgtccggaag atgttgctaa tgtattttac   3720 

ttcaacatag ggaacaaact ttttaagtat attaataaac ctgtatggtt agtttttaac   3780 

agttttttaa aataaactat ggatatgaca aatattctgt gttttactaa gtgcttggat   3840 

aggctttcta attttgtata cgtgctagag ttaattattg aacattttta tccaaattta   3900 

gttgtaactc tgtttatact actgattgct cattcgttta aatgatattt taatgtaaaa   3960 

gtcataacca acatatgaac agacagattt atgtctttaa acacagaatg taagctatag   4020 

tttaatctga taccagttgc tggaagttgc catttgtttt tcttaaatct atacccataa   4080 

aacttctttt aagattaaaa aaaaaaaaaa a                                  4111 

 
           
             66  
             1604  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1825473CB1  
             
           
            66 

gatcttaaat ctaatagatt tcctatttcc aaaaagctcg actggagtgt tataaaacct     60 

gaaaattctc ttgtgctttc tcttcttttg cttctagtta ccatcctcaa aggattggct    120 

aaaagcaagc aactggattg aacaccctaa gaagaaagat tcacactgca ccaggagaca    180 

tcagaaagaa tgaaaactct gccgctgttt gtgtgcatct gtgcactgag tgcttgcttc    240 

tcgttcagtg aaggtcgaga aagggatcat gaactacgtc acagaaggca tcatcaccaa    300 

tcacccaaat ctcactttga attaccacat tatcctggac tgctagctca ccagaagccg    360 

ttcattagaa agtcctataa atgtctgcac aaacgctgta ggcctaagct tccaccttca    420 

cctaataacc cccccaaatt cccaaatcct caccagccac ctaaacatcc agataaaaat    480 

agcagtgtgg tcaaccctac cttagtggct acaacccaaa ttccatctgt gactttccca    540 

tcagcttcca ccaaaattac tacccttcca aatgtgactt ttcttcccca gaatgccacc    600 

accatatctt caagagaaaa tgttaacaca agctcttctg tagctacatt agcaccagtg    660 

aattccccag ctccacaaga caccacagct gccccaccca caccttctgc aactacacca    720 

gctccaccat cttcctcagc tccaccagag accacagctg ccccacccac accttctgca    780 

actacacaag ctccaccatc ttcctcagct ccaccagaga ccacagctgc cccacccaca    840 

cctcctgcaa ctacaccagc tccaccatct tcctcagctc caccagagac cacagctgcc    900 

ccacccacac cttctgcaac tacaccagct ccactatctt cctcagctcc accagagacc    960 

acagctgtcc cacccacacc ttctgcaact accctagacc catcatccgc ctcagctcca   1020 

ccagagacca cagctgcccc acccacacct tctgcaacta caccagctcc accgtcttcc   1080 

ccagctccac aagagaccac agctgcccca attaccacac ctaattcttc cccaactact   1140 

cttgcacctg acacttctga aacttcagct gcacccacac accagactac tacttcggtc   1200 

actactcaaa ctactactac taaacaacca acttcagctc ctggccaaaa taaaatttct   1260 

cgatttcttt tatatatgaa gaatctacta aacagaatta ttgacgacat ggtggagcaa   1320 

tagtatattg tatgttgtaa agtgttctgt catttacaag atgtgattca tgagtgcaga   1380 

actaccacct ttcttttagc accaatccca acatgaaatt atattactca gatttaaagc   1440 

actatcatta atctttcaat ctaattattc accaccacaa gacctattaa caagacaaaa   1500 

tgcctctatc ccacaagcca gatgcaggtc tggggttcaa aataactctt tggatcctac   1560 

agagatagcc tactgagggc agagaaagtc cttagataaa gaga                    1604 

 
           
             67  
             2646  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7950094CB1  
             
           
            67 

gcgagcgcgg gcaggcggcg acgcgggggc aggggtggac ggcggtcaga gccgaacgcg     60 

agggcggcgc ccggggactg gagctgcgcg caataggaca gctggcctga agctcagagc    120 

cggggcgtgc gccatggccc cacactgggc tgtctggctg ctggcagcaa ggctgtgggg    180 

cctgggcatt ggggctgagg tgtggtggaa ccttgtgccg cgtaagacag tgtcttctgg    240 

ggagctggcc acggtagtac ggcggttctc ccagaccggc atccaggact tcctgacact    300 

gacgctgacg gagcccactg ggcttctgta cgtgggcgcc cgagaggccc tgtttgcctt    360 

cagcatggag gccctggagc tgcaaggagc gatctcctgg gaggcccccg tggagaagaa    420 

gactgagtgt atccagaaag ggaagaacaa ccagaccgag tgcttcaact tcatccgctt    480 

cctgcagccc tacaatgcct cccacctgta cgtctgtggc acctacgcct tccagcccaa    540 

gtgcacctac gtcaacatgc tcaccttcac tttggagcat ggagagtttg aagatgggaa    600 

gggcaagtgt ccctatgacc cagctaaggg ccatgctggc cttcttgtgg atggtgagct    660 

gtactcggcc acactcaaca acttcctggg cacggaaccc attatcctgc gtaacatggg    720 

gccccaccac tccatgaaga cagagtacct ggccttttgg ctcaacgaac ctcactttgt    780 

aggctctgcc tatgtacctg agagtgtggg cagcttcacg ggggacgacg acaaggtcta    840 

cttcttcttc agggagcggg cagtggagtc cgactgctat gccgagcagg tggtggctcg    900 

tgtggcccgt gtctgcaagg gcgatatggg gggcgcacgg accctgcaga ggaagtggac    960 

cacgttcctg aaggcgcggc tggcatgctc tgccccgaac tggcagctct acttcaacca   1020 

gctgcaggcg atgcacaccc tgcaggacac ctcctggcac aacaccacct tctttggggt   1080 

ttttcaagca cagtggggtg acatgtacct gtcggccatc tgtgagtacc agttggaaga   1140 

gatccagcgg gtgtttgagg gcccctataa ggagtaccat gaggaagccc agaagtggga   1200 

ccgctacact gaccctgtac ccagccctcg gcctggctcg tgcattaaca actggcatcg   1260 

gcgccacggc tacaccagct ccctggagct acccgacaac atcctcaact tcgtcaagaa   1320 

gcacccgctg atggaggagc aggtggggcc tcggtggagc cgccccctgc tcgtgaagaa   1380 

gggcaccaac ttcacccacc tggtggccga ccgggttaca ggacttgatg gagccaccta   1440 

tacagtgctg ttcattggca caggagacgg ctggctgctc aaggctgtga gcctggggcc   1500 

ctgggttcac ctgattgagg agctgcagct gtttgaccag gagcccatga gaagcctggt   1560 

gctatctcag agcaagaagc tgctctttgc cggctcccgc tctcagctgg tgcagctgcc   1620 

cgtggccgac tgcatgaagt atcgctcctg tgcagactgt gtcctcgccc gggaccccta   1680 

ttgcgcctgg agcgtcaaca ccagccgctg tgtggccgtg ggtggccact ctggatctct   1740 

actgatccag catgtgatga cctcggacac ttcaggcatc tgcaacctcc gtggcagtaa   1800 

gaaagtcagg cccactccca aaaacatcac ggtggtggcg ggcacagacc tggtgctgcc   1860 

ctgccacctc tcctccaact tggcccatgc ccgctggacc tttgggggcc gggacctgcc   1920 

tgcggaacag cccgggtcct tcctctacga tgcccggctc caggccctgg ttgtgatggc   1980 

tgcccagccc cgccatgccg gggcctacca ctgcttttca gaggagcagg gggcgcggct   2040 

ggctgctgaa ggctaccttg tggctgtcgt ggcaggcccg tcggtgacct tggaggcccg   2100 

ggcccccctg gaaaacctgg ggctggtgtg gctggcggtg gtggccctgg gggctgtgtg   2160 

cctggtgctg ctgctgctgg tgctgtcatt gcgccggcgg ctgcgggaag agctggagaa   2220 

aggggccaag gctactgaga ggaccttggt gtaccccctg gagctgccca aggagcccac   2280 

cagtcccccc ttccggccct gtcctgaacc agatgagaaa ctttgggatc ctgtcggtta   2340 

ctactattca gatggctccc ttaagatagt acctgggcat gcccggtgcc agcccggtgg   2400 

ggggccccct tcgccacctc caggcatccc aggccagcct ctgccttctc caactcggct   2460 

tcacctgggg ggtgggcgga actcaaatgc caatggttac gtgcgcttac aactaggagg   2520 

ggaggaccgg ggagggctcg ggcaccccct gcctgagctc gcggatgaac tgagacgcaa   2580 

actgcagcaa cgccagccac tgcccgactc caaccccgag gagtcatcag tatgagggga   2640 

accccc                                                              2646 

 
           
             68  
             3876  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7479484CB1  
             
           
            68 

atgttccgac caaccacggt ggctgtagac gaggatggtg gagaagagga taaagatgag     60 

tcatcaacca acagtggtgc aagtgctgtt tcttcttgtg gctttggagc cgacttctcc    120 

acagataaag ggggctcctt cacgtcagta cagatcacta ataccactgg actgtcacag    180 

gctcctggct tagcctccca aggtattagc tttggcatta agaataatct gggaccccca    240 

ctgcagaaat tgggagtatc attttccttt gccaagaaag ctcccgtcaa acttgaatca    300 

atagcatccg ttttcaagga ccatgcagag gaagggagct cagaagatgg aacgaaggct    360 

gatgagaaga gctctgacca aggggtgcag aaggtgggag atactgatgg cactggtaat    420 

cttgatggaa agaaagaaga tgaagaccct caggatggag ggtcccttgc ctcaacactg    480 

tccaagttga aaaggatgaa acgggaagaa ggaacagggg ctacagagcc agaatattac    540 

cactacatcc ccccagcaca ctgcaaggtc aaacctaatt tccccttctt actctttatg    600 

agagccagtg aacagatgga aggggatcat agtgcacact caaagagtgc ccccgagaac    660 

agaaaaagca gctctcccaa gccgcaaggc tgtagtaaga cagcagcaag cccaggggca    720 

gaaagaacag tgagtgaagc ttctgagctg caaaaggaag ccgctgtggc tgggccttca    780 

gagcctggag gtaaaactga aacaaagaaa ggctccggag gaggggaaga tgagcagagt    840 

gtagagagta gggagacgtc agagagcccg atgtgtgagt ccaatcctaa agacatttct    900 

caggccaccc cagcaacaaa agcaggccag ggacccaagc atcctactgg tccattcttt    960 

ccagttttaa gcaaggatga aagcactgcc ctccagtggc catcagaact actcattttc   1020 

accaaagcag agccttccat ctcctacagt tgtaatcctt tatactttga ctttaaactt   1080 

tcaagaaaca aagatgctaa agctaaaggg acagaaaagc caaaagatgt cgcaggctcc   1140 

tcaaaggatc atctccagag ccttgatcct agagaaccga ataaaagcca ggaagaggag   1200 

caggatgtag tgctctcttc agaaggcaga gtggatgaac ctgcatcagg ggctgcctgt   1260 

agcagcctga acaagcagga gcctgggggt agccatatgt cagaaactga agacactggg   1320 

agaagccatc ctagcaagaa agaaccatca ggcaagtctc acagacacaa gaagaaaaag   1380 

aaacacaaaa aatccagcaa gcacaaacgt aaacacaagg ctgacacgga agagaagagt   1440 

tctaaggcag agtctgggga gaaatctaag aagcgcaaga aacgaaaacg gaagaagaac   1500 

aaatcatcag ccgcagctga ttctgaacgc ggacccaaat cagaacctcc tggaagcggc   1560 

agcccggcac caccgagaag gcggcgccga gctcaagatg attcccagcg gagatccctt   1620 

cctgctgaag aaggaaacag tggcaagaag gatgatggtg ggggtggtag cagttgccaa   1680 

gatcacagtg ggaggaaaca caaaggtgaa ccaccaactt cctcctgcca gcggagagct   1740 

aacaccaaac atagcagccg gtccagccat cggagccaac ccagtagtgg tgatgaggat   1800 

agtgatgatg cttcctcaca ccgactgcac cagaagtctc catcccagta cagtgaggag   1860 

gaggaagagg aggaggagga agaagaggag gaagatgaag actccggtag tgagcattct   1920 

cgtagccgct ctcggtctgg ccatcgccat tcctcacatc gttcctcccg gcgctcttat   1980 

tctagcagct ctgatgcctc ttcagaccag agctgctata gtagacagca cagttactct   2040 

gatgatagct atagtgacta tagcgaccga tcacgaaggc actctaagcg ctctcacgat   2100 

tcagatgatt cagactatac cagctccaaa cacaggtcta aacgacacaa atactcatca   2160 

tctgatgatg actatagcct cagttgcagc cagtcccgaa gccgatctcg gagtcataca   2220 

agggagcgat caagatcccg gggtcgaagc cgcagtagca gctgtagtcg cagtcgaagc   2280 

aagaggagaa gtcgcagcac cacagcccac agctggcagc gaagccgaag ctatagccgg   2340 

gaccggagcc gcagcaccag gagcccttct cagagatcag gctccagaaa gggctcatgg   2400 

ggtcatgaga gcccagagga aaggcgctct ggccgccggg atttcattcg ttcaaagatc   2460 

taccgctctc aatcccccca ctatttccaa tcaggtcggg gagaaggtcc tggaaagaaa   2520 

gaagatggca gaggagatga cagtaaagga gcaggcctgc cctcccagaa tagcaatact   2580 

ggcacaggaa gggggtcaga aagtgactgc agtcctgaag ataagaattc tgttactgcc   2640 

agactgctgc tagagaagat ccagtccagg aaagtggaga ggaaacccaa tgtgtgcgag   2700 

gaggtgctgg ccacccctaa taaggctggg ctcaagtaca agaacccccc acaaggttac   2760 

tttgggccta agctcccccc gtctcttggt aataagcctg ttcttccaat gatagggaag   2820 

cttccagcta cccggaagtc caataagaaa tgtgaagagt ctggcttaga aaggggagaa   2880 

gagcaggaac attcagagcc agaagaaggg tccccaagga gtagtgatgc tccatttggg   2940 

catcagttct cagaggaagc agctggtccc ttatcagacc ctcccccaga agagccaaag   3000 

tctgaagaag ctactgctga tcactctgtg gctccgctag gcaccccagc ccacactgac   3060 

tgctaccctg gggatccagc catctcccat aactacctcc cggaccccag tgatggggat   3120 

actctggagt ctctggatag tggcagtcaa ccaggccctg tggaatccag cttgctgcct   3180 

atagccccag accttgagca cttccccaat tatgcacctc ccagtgggga acctagtatt   3240 

gaatcaacag atgggactga ggatgcctcc ttggctcctc tcgagagcca gcccatcacc   3300 

ttcacccctg aggagatgga gaagtacagc aagctccagc aggctgcaca gcagcacatc   3360 

cagcagcagc ttctggccaa acaagtgaag gcctttccag cctccaccgc cctagctcca   3420 

gccacaccag ccctgcagcc catccacatt cagcagccag ccacagcctc tgccacctcc   3480 

atcaccactg ttcagcatgc catcctacag catcatgctg cagccgctgc tgccgccatt   3540 

ggcattcacc ctcaccccca ccctcagccg cttgctcaag tacatcatat tccccagccc   3600 

catctaaccc ctatttcttt gtcccatctc actcactcaa ttatccctgg ccaccctgcc   3660 

acctttcttg ctagccaccc tatccatata attcctgcct cagccatcca tcctgggccc   3720 

ttcacctttc atcccgtccc acacgctgcc ctctacccca ccctgcttgc cccacggcct   3780 

gctgcagcag ctgccacagc cctccatctt cacccactgc ttcaccccat cttctcaggt   3840 

caggacctgc agcaccctcc cagccatggg acttga                             3876 

 
           
             69  
             2583  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6780147CB1  
             
           
            69 

ggtggcgggt ggctggcggt tccgttaggt ctgagggagc gatggcggta cgcgcgttga     60 

agctgctgac cacactgctg gctgtcgtgg ccgctgcctc ccaagccgag gtcgagtccg    120 

aggcaggatg gggcatggtg acgcctgatc tgctcttcgc cgaggggacc gcagcctacg    180 

cgcgcgggga ctggcccggg gtggtcctga gcatggaacg ggcgctgcgc tcccgggcag    240 

ccctccgcgc ccttcgcctg cgctgccgca cccagtgtgc cgccgacttc ccgtgggagc    300 

tggaccccga ctggtccccc agcccggccc aggcctcggg cgccgccgcc ctgcgcgacc    360 

tgagcttctt cgggggcctt ctgcgtcgcg ctgcctgcct gcgccgctgc ctcgggccgc    420 

cggccgccca ctcgctcagc gaagagatgg agctggagtt ccgcaagcgg agcccctaca    480 

actacctgca ggtcgcctac ttcaagatca acaagttgga gaaagctgtt gctgcagcac    540 

acaccttctt cgtgggcaat cctgagcaca tggaaatgca gcagaaccta gactattacc    600 

aaaccatgtc tggagtgaag gaggccgact tcaaggatct tgagactcaa ccccatatgc    660 

aagaatttcg actgggagtg cgactctact cagaggaaca gccacaggaa gctgtgcccc    720 

acctagaggc ggcgctgcaa gaatactttg tggcctatga ggagtgccgt gccctctgcg    780 

aagggcccta tgactacgat ggctacaact accttgagta caacgctgac ctcttccagg    840 

ccatcacaga tcattacatc caggtcctca actgtaagca gaactgtgtc acggagcttg    900 

cttcccaccc aagtcgagag aagccctttg aagacttcct cccatcgcat tataattatc    960 

tgcagtttgc ctactataac attgggaatt atacacaggc tgttgaatgt gccaagacct   1020 

atcttctctt cttccccaat gacgaggtga tgaaccaaaa tttggcctat tatgcagcta   1080 

tgcttggaga agaacacacc agatccatcg gcccccgtga gagtgccaag gagtaccgac   1140 

agcgaagcct actggaaaaa gaactgcttt tcttcgctta tgatgttttt ggaattccct   1200 

ttgtggatcc ggattcatgg actccagaag aagtgattcc caagagattg caagagaaac   1260 

agaagtcaga acgggaaaca gccgtacgca tctcccagga gattgggaac cttatgaagg   1320 

aaatcgagac ccttgtggaa gagaagacca aggagtcact ggatgtgagc agactgaccc   1380 

gggaaggtgg ccccctgctg tatgaaggca tcagtctcac catgaactcc aaactcctga   1440 

atggttccca gcgggtggtg atggacggcg taatctctga ccacgagtgt caggagctgc   1500 

agagactgac caatgtggca gcaacctcag gagatggcta ccggggtcag acctccccac   1560 

atactcccaa tgaaaagttc tatggtgtca ctgtcttcaa agccctcaag ctggggcaag   1620 

aaggcaaagt tcctctgcag agtgcccacc tgtactacaa cgtgacggag aaggtgcggc   1680 

gcatcatgga gtcctacttc cgcctggata cgcccctcta cttttcctac tctcatctgg   1740 

tgtgccgcac tgccatcgaa gaggtccagg cagagaggaa ggatgatagt catccagtcc   1800 

acgtggacaa ctgcatcctg aatgccgaga ccctcgtgtg tgtcaaagag cccccagcct   1860 

acaccttccg cgactacagc gccatccttt acctaaatgg ggacttcgat ggcggaaact   1920 

tttatttcac tgaactggat gccaagaccg tgacggcaga ggtgcagcct cagtgtggaa   1980 

gagccgtggg attctcttca ggcactgaaa acccacatgg agtgaaggct gtcaccaggg   2040 

ggcagcgctg tgccatcgcc ctgtggttca ccctggaccc tcgacacagc gagcgggaca   2100 

gggtgcaggc agatgacctg gtgaagatgc tcttcagccc agaagagatg gacctctccc   2160 

aggagcagcc cctggatgcc cagcagggcc cccccgaacc tgcacaagag tctctctcag   2220 

gcagtgaatc gaagcccaag gatgagctat gacagcgtcc aggtcagacg gatgggtgac   2280 

tagacccatg gagaggaact cttctgcact ctgagctggc cagcccctcg gggctgcaga   2340 

gcagtgagcc tacatctgcc actcagccga ggggaccctg ctcacagcct tctacatggt   2400 

gctactgctc ttggagtgga catgaccaga caccgcaccc cctggatctg gctgagggct   2460 

caggacacag gcccagccac ccccaggggc ctccacaggc cgctgcataa cagcgataca   2520 

gtacttaagt gtctgtgtag acaaccaaag aataaatgat tcatggtttt ttttaaaaaa   2580 

aaa                                                                 2583 

 
           
             70  
             6147  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7204554CB1  
             
           
            70 

tgatatatag ggccatgctt atctagcatg catgctcgag acgcgcgcat atgtgctgga     60 

aagggcgggg cgcgccccgg ggcggcgggg ctgaagctcc tggcaccatg atgctcaccc    120 

cagcaggacc agagcaccga ggcccaaggc cccagcctgc catgccgctg ccaccgcgga    180 

gcctgcaggt gctcctgctg ctgctgctgt tgctgctgct gctgccgggc atgtgggctg    240 

aggcaggctt gcccagggca ggcgggggtt cacagccccc cttccgcacc ttctcggcca    300 

gcgactgggg cctcacccac ctagtggtgc atgagcagac aggcgaggtg tatgtgggcg    360 

cagtgaaccg catctataag ctgtcgggga acctgacact gctgcgggcc cacgtcacgg    420 

gccctgtgga ggacaacgag aagtgctacc cgccgcccag cgtgcagtcc tgcccccacg    480 

gcctgggcag tactgacaac gtcaacaagc tgctgctgct ggactatgcc gctaaccgcc    540 

tgctggcctg tggcagcgcc tcccagggca tctgccagtt cctgcgtctg gacgatctct    600 

tcaaactggg tgagccacac caccgtaagg agcactacct gtccagcgtg caggaggcag    660 

gcagcatggc gggcgtgctc attgccgggc caccgggcca gggccaggcc aagctcttcg    720 

tgggcacacc catcgatggc aagtccgagt acttccccac actgtccagc cgtcggctca    780 

tggccaacga ggaggatgcc gacatgttcg gcttcgtgta ccaggatgag tttgtgtcat    840 

cacagctcaa gatcccttcg gacacgctgt ccaagttccc ggcctttgac atctactatg    900 

tgtacagctt ccgcagcgag cagtttgtct actacctcac gctgcagcta gacacacagc    960 

tgacctcgcc tgatgccgcc ggcgagcact tcttcacgtc caagatcgtg cggctctgtg   1020 

tggacgaccc caaattctac tcgtacgttg agttccccat tggctgcgag caggcgggtg   1080 

tggagtaccg cctggtgcag gatgcctacc tgagccggcc cggccgtgcc ctggcccacc   1140 

agctgggcct ggctgaggac gaggacgtgc tgttcactgt gttcgcccag ggccagaaga   1200 

accgcgtgaa gccaccaaag gagtcagcac tgtgcctgtt cacgctcagg gccatcaagg   1260 

agaagattaa ggagcgcatc cagtcctgct accgtggtga gggcaagctc tccctgccgt   1320 

ggctgctcaa caaggagctg ggctgcatca actcgcccct gcagatcgat gacgacttct   1380 

gcgggcagga cttcaaccag cccctggggg gcacagtcac cattgagggg acgcccctgt   1440 

tcgtggacaa ggatgatggc ctgaccgccg tggctgccta tgactatcgg ggccgcactg   1500 

tggtattcgc cggcacgcga agtggccgca tccgcaagat cctggtggac ctctcaaacc   1560 

ccggtggccg gcctgccctg gcctacgaga gcgtcgtggc ccaggagggc agccccatcc   1620 

tgcgagacct cgtcctcagc cccaaccacc agtacctcta cgccatgacc gagaagcagg   1680 

tgacgcgggt gcctgtggag agctgtgtgc agtacacgtc ctgtgagctg tgtctggggt   1740 

cacgggaccc ccactgtggc tggtgtgtcc tgcacagcat ctgctcgcgg cgggacgcct   1800 

gtgagcgagc agacgagccc cagcgctttg ctgcggacct gctgcagtgt gtgcagctga   1860 

ctgtgcagcc ccgcaatgtg tctgtcacca tgtcccaggt cccacttgtg ctgcaggcct   1920 

ggaacgtgcc tgacctctca gctggcgtca actgctcctt cgaggacttc acggaatctg   1980 

agagcgtcct ggaggatggc cggatccact gccgctcacc ctccgcccgg gaggtggcgc   2040 

ccatcacgcg gggccaggga gaccagcggg tggtgaaact ctacctaaag tccaaggaga   2100 

cagggaagaa gtttgcgtct gtggacttcg tcttctacaa ctgcagcgtc caccagtcct   2160 

gcctgtcctg tgtcaacggc tcctttccct gccactggtg caaataccgc cacgtgtgca   2220 

cacacaacgt ggctgactgc gccttcctgg agggccgtgt caacgtgtct gaggactgcc   2280 

cacagatcct gccctccacg cagatctacg tgccagtggg agtggtaaaa cccatcaccc   2340 

tggccgcacg gaacctgcca cagccacagt caggccagcg tggatatgag tgcctcttcc   2400 

acatcccggg cagcccggcc cgtgtcaccg ccctgcgctt caacagctcc agcctgcagt   2460 

gccagaattc ctcgtactcc tacgagggga acgatgtcag cgacctgcca gtgaacctgt   2520 

cagtcgtgtg gaacggcaac tttgtcattg acaacccaca gaacatccag gcgcacctct   2580 

acaagtgccc ggccctgcgc gagagctgcg gcctctgcct caaggccgac ccgcgcttcg   2640 

agtgcggatg gtgcgtggcc gagcgccgct gctccctgcg acaccactgc gctgccgaca   2700 

cacctgcatc gtggatgcac gcgcgtcacg gcagcagtcg ctgcaccgac cccaagatcc   2760 

tcaagctgtc ccccgagacg ggcccgaggc agggcggcac gcggctcact atcacaggcg   2820 

agaacctggg cctgcgattc gaagacgtgc gtctgggcgt gcgcgtgggc aaggtgctgt   2880 

gcagccctgt ggagagcgag tacatcagtg cggagcagat cgtctgtgag atcggggacg   2940 

ccagctccgt gcgtgcccat gacgccctgg tggaggtgtg tgtgcgggac tgctcaccac   3000 

actaccgcgc cctgtcaccc aagcgcttca ccttcgtgac accaaccttc taccgtgtga   3060 

gcccctcccg tgggcctctg tcagggggca cctggattgg catcgaggga agccacctga   3120 

acgcaggcag tgatgtggct gtgtcggtcg gtggccggcc ctgctccttc tcctggagga   3180 

actcccgtga gatccggtgc ctgacacccc ccgggcagag ccctggcagc gctcccatca   3240 

tcatcaacat caaccgcgcc cagctcacca accctgaggt gaagtacaac tacaccgagg   3300 

accccaccat cctgaggatc gaccccgagt ggagcatcaa cagcggtggg accctcctga   3360 

cggtcacagg caccaacctg gccactgtcc gtgaaccccg aatccgggcc aagtatggag   3420 

gcattgagag ggagaacggc tgcctggtgt acaatgacac caccatggta tgccgcgccc   3480 

cgtctgtggc caaccctgtg cgcagcccac cagagctggg ggagcggccg gatgagctgg   3540 

gcttcgtcat ggacaacgtg cgctccctgc ttgtgctcaa ctccacctcc ttcctctact   3600 

accctgaccc cgtactggag ccactcagcc ccactggcct gctggagctg aagcccagct   3660 

ccccactcat cctcaagggc cggaacctct tgccacctgc acccggcaac tcccgactca   3720 

actacacggt gctcatcggc tccacaccct gtaccctcac cgtgtcggag acgcaactgc   3780 

tgtgcgaggc gcccaacctc actgggcagc acaaggtcac ggtgcgggca ggtggcttcg   3840 

agttctcgcc agggacactg caggtgtact cggacagcct gctgacgctg cctgccattg   3900 

tgggcattgg cggaggcggg ggtctcctgc tgctggtcat cgtggctgtg ctcatcgcct   3960 

acaagcgcaa gtcacgagat gctgaccgca cactcaagcg gctgcagctc cagatggaca   4020 

acctggagtc ccgcgtggcc ctcgaatgca aggaagcctt tgcagagctg cagacagaca   4080 

tccacgagct gaccaatgac ctggacggtg ccggcatccc cttccttgac taccggacat   4140 

atgccatgcg ggtgctcttt cctgggatcg aggaccaccc tgtgctcaag gagatggagg   4200 

tgcaggccaa tgtggagaag tcgctgacac tgttcgggca gctgctgacc aagaagcact   4260 

tcctgctgac cttcatccgc acgctggagg cacagcgcag cttctccatg cgcgaccgcg   4320 

ggaatgtggc ctcgctcatc atgacggccc tgcagggcga gatggaatac gccacaggcg   4380 

tgctcaagca gctgctttcc gacctcatcg agaagaacct ggagagcaag aaccacccca   4440 

agctgctact gcgccggact gagtcggtgg cagagaagat gctaactaac tggttcacct   4500 

tcctcttgta taagttcctc aaggagtgcg ctggggagcc gctgttcatg ctgtactgcg   4560 

ccatcaagca gcagatggag aagggcccca ttgacgccat cacgggtgag gcacgctact   4620 

ccctgagtga ggacaagctc atccggcagc agattgacta caagacactg accctgaact   4680 

gtgtgaaccc tgagaatgag aatgcacctg aggtgccggt gaaggggctg gactgtgaca   4740 

cggtcaccca ggccaaggag aagctgctgg acgctgccta caagggcgtg ccctactccc   4800 

agcggcccaa ggccgcggac atggacctgg agtggcgcca gggccgcatg gcgcgcatca   4860 

tcctgcagga cgaggacgtc accaccaaga ttgacaacga ttggaagagg ctgaacacac   4920 

tggctcacta ccaggtgaca gacgggtcct cggtggcact ggtgcccaag cagacgtccg   4980 

cctacaacat ctccaactcc tccaccttca ccaagtccct cagcagatac gagagcatgc   5040 

tgcgcacggc cagcagcccc gacagcctgc gctcgcgcac gcccatgatc acgcccgacc   5100 

tggagagcgg caccaagctg tggcacctgg tgaagaacca cgaccacctg gaccagcgtg   5160 

agggtgaccg cggcagcaag atggtctcgg agatctactt gacacggcta ctggccacca   5220 

agggcacact gcagaagttt gtggacgacc tgtttgagac catcttcagc acggcacacc   5280 

ggggctcagc cctgccgctg gccatcaagt acatgttcga cttcctggat gagcaggccg   5340 

acaagcacca gatccacgat gctgacgtgc gccacacctg gaagagcaac tgcctgcccc   5400 

tgcgcttctg ggtgaacgtg atcaagaacc cacagtttgt gttcgacatt cacaagaaca   5460 

gcatcacgga cgcctgcttg tcggtggtgg cccagacctt catggactcc tgctccacct   5520 

ctgagcacaa gctgggcaag gactcaccct ccaacaagct gctctacgcc aaggacatcc   5580 

ccaactacaa gagctgggtg gagaggtact atgcagacat cgccaagatg ccagccatca   5640 

gcgaccagga catgagtgcg tatctggctg agcagtcccg cctgcacctg agccagttca   5700 

acagcatgag cgccttgcac gagatctact cctacatcac caagtacaag gatgagatcc   5760 

tggcagccct ggagaaggat gagcaggcgc ggcggcagcg gctgcggagc aagctggagc   5820 

aggtggtgga cacgatggcc ctgagcagct gagccccagc tgtgatcatc cagcatgatg   5880 

cagcgtgagg acagctgagc agggaccggg acagccctca ccgcatgcgt gtggagtgtc   5940 

cggtggtgct cgggccgccg cagtgcagcg actgcccggc cctccctccc ctgcctcacc   6000 

cggtcgggtc ccggctcttc ctgtgtggag gtgatggtac ctgccacacc acagctgcgc   6060 

acacagctgc ttgctcaggg gccgggacag cactgggtgc tcaggctggc caaggacctt   6120 

cattgcctgg gcaagagctg cccagtg                                       6147 

 
           
             71  
             888  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6833247CB1  
             
           
            71 

cgagcttact tatactggta cctttctaat ctcactacaa tatgtaacat tggtgttcga     60 

tctcaagtat ttctgaatat attcccctat ccacagaaat atactctggg ggaaaaaaaa    120 

tagaacaaat tcttgccgtc ctgaccattg aacaagagac taattagaca atggggctag    180 

aaaaacctca aagtaaactg gaaggaggca tgcatcccca gctgatacct tcggttattg    240 

ctgtagtttt catcttactt ctcagtgtct gttttattgc aagttgtttg gtgactcatc    300 

acaacttttc acgctgtaag agaggcacag gagtgcacaa gttagagcac catgcaaagc    360 

tcaaatgcat caaagagaaa tcagaactga aaagtgctga agggagcacc tggaactgtt    420 

gtcctattga ctggagagcc ttccagtcca actgctattt tcctcttact gacaacaaga    480 

cgtgggctga gagtgaaagg aactgttcag ggatgggggc ccatctgatg accatcagca    540 

cggaagctga gcagaacttt attattcagt ttctggatag acggctttcc tatttccttg    600 

gacttagaga tgagaatgcc aaaggtcagt ggcgttgggt ggaccagacg ccatttaacc    660 

cacgcagagt attctggcat aagaatgaac ccgacaactc tcagggagaa aactgtgttg    720 

ttcttgttta taaccaagat aaatgggcct ggaatgatgt tccttgtaac tttgaagcaa    780 

gtaggatttg taaaatacct ggaacaacat tgaactagaa actcagaaag tggtccttgt    840 

gatggaaaga gaaaagaaaa accaattaga ataaggcaga atgtacgt                 888  
           
             72  
             3582  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4148119CB1  
             
           
            72 

ctggccacac cgaaagagag cccacccaag tctgaggaac cacacccgga gcagttccga     60 

aaagcgaggg agacttcccc tgatctggaa agggtgccag gcacttcagc accatcggca    120 

gccccagccc ctcacccacg gcaagagagg cagagcggct ctcaccgggt ccagaccggc    180 

ccagcccacc ataatggtca aaagaaggcc aagctctgga aggtgggaac aactgaggca    240 

gatggggaca gtaaagccag atggaccgcg cttgagcctt catctccacc agggacccag    300 

gccaccttcc cagttccata cctcttcagc ctcaggtccc tcttgactga gcccagcgtc    360 

accgccccca agaaagttcc ccaatcaccc tgtcccacgc tgggccacct gcttccctcc    420 

ctgaaggctg tccctaagct gtgggtattt atcctactaa ggaggctggg acagagtcct    480 

gacctgcacc catctgttcc caacccacca gccttcaaac aagggggctc ctcctccccg    540 

gggcagctct ggcctctgct gggggccagt cgaggcagat agaagggtga gcctaaccaa    600 

tgacccaacg cccccttccc aattaactac cgccttccaa cggaatccaa gggaatccct    660 

catccccaaa acttcaccgc ggaaggatct gcggggactg acaggcagaa gccaggcaca    720 

gggatatccg aacagcctca gtcttgctac ccaactctgc cttcaagaca ttccaatctg    780 

atgggaagag tcctgtctgg gaagctccct gtctgatggg agacagccct gtccacatgg    840 

aggtctcagt ctgacggagg aaacagcctg gccagccagg cccaggccga caggggagac    900 

acagtccctg cccaaggagc ttccaagcta agggcggaac cacagccaag cccagggagc    960 

tcccaggcta agggcggaga ctgtcccagc ccagggagct cccagtcaaa agggggagac   1020 

acagcactgc ccttacaaag ctaccagcct cacggagaag gcgcagtccc tgtccacaga   1080 

gacacagcct tgccccagtt actgcccacc tgcaagagat ccacatttct gccctccaga   1140 

gctcccaaac tgatggggga gagagacatc atcccccagc tctgggagtt tccagtctga   1200 

tggaggagac agagcctgct tcggtaactc tcactctgcg ggggaagact cagccctatc   1260 

cagggagctc ccacactttc aatggggagg cccacccagt ggccgagcct gctgctgctc   1320 

ctgctgttgc cggggccccc gcccgtcgcc ggcttggaag acgctgcctt cccccacctg   1380 

ggggagagct tgcagcccct gccccgggcc tgtcccctgc gctgctcctg cccccgagtc   1440 

gacactgtgg actgtgatgg cttggacctt cgagtgttcc cggacaacat caccagagcc   1500 

gctcagcacc tctccctgca gaacaaccag ctccaggaac tcccctacaa tgagctgtcc   1560 

cgcctcagtg gcctgcgaac cctcaacctc cacaacaacc tcatctcctc cgaaggcctg   1620 

cctgacgagg ccttcgagtc cctcacccag ctgcagcacc tctgcgtggc tcacaacaag   1680 

ctctcagtgg cccctcagtt tctgccccgg tccctccgtg tcgcggatct ggctgccaac   1740 

caagtgatgg agatcttccc cctcaccttt ggggagaagc cggtactcag gtccgtgtac   1800 

ctccacaaca accagctgag caacgctggc ctgccccccg acgccttccg cggctccgag   1860 

gccatcgcca ccctcagcct ctccaacaac cagctcagct acctgccgcc cagcctgccg   1920 

ccctcactcg agcggctcca cctgcagaac aatctcatct ccaaggtgcc ccgaggagcc   1980 

ctgagccgcc agactcaact ccgtgagctc tacctccagc acaaccagct gacagacagt   2040 

ggcctggatg ccaccacctt cagcaagctg catagccttg aatacctgga tctctcccac   2100 

aaccagctga ccacagtgcc cgccggcctg ccccggaccc tggctatcct gcacctgggc   2160 

cgcaaccgca tccggcaggt ggaggcggct cggctgcacg gggcgcgtgg tctgcgctat   2220 

ttgttgctgc agcacaacca gctggggagc tcagggctgc ccgccggggc tctgcggccg   2280 

ctgcggggcc tgcacacgct gcacctctat ggcaatgggc tggaccgcgt gcctccagcc   2340 

ctgccccgcc gcctgcgtgc cctggtgctg ccccacaacc acgtggccgc gctgggtgcc   2400 

cgtgacctgg tcgccacacc gggcctgacg gagcttaacc tggcctataa ccgcctggcc   2460 

agcgcccgtg tgcaccaccg ggccttccgc cggttgcgtg ccctgcgcag cctcgacctg   2520 

gcagggaatc agctaacccg gctgcccatg ggcctgccca ctggcctgcg caccctgcag   2580 

ctgcaacgca accagctgcg gatgctcgag cccgagcctc tggccggcct ggaccaactg   2640 

cgggagctca gcctggcgca caaccggctc cgggtcggcg acatcgggcc aggcacctgg   2700 

catgagctcc aagccctcca gatgctggac ctcagccaca atgagctgtc ctttgtgccc   2760 

ccggacctgc ctgaggccct agaggagctg cacctcgagg gcaaccgcat cggccacgtg   2820 

ggccccgagg ccttcctcag cacaccccgc ctgcgtgccc tcttcctcag ggccaacagg   2880 

cttcacatga cgagcatcgc ggctgaggcc ttcctggggc tcccaaacct gcgtgtggtg   2940 

gacacggcag ggaatccgga gcaggtcctg atccggctgc ctcccaccac cccacgtggg   3000 

ccacgggcag ggggcccctg atcctagaga ggcccagcag agcagctcag actcctggga   3060 

ctccgctggg ccgtggactg aggagacaac gcccaccagg ggcccttggt ctggctctcc   3120 

tgggcctcca gggctgggcc tgctctgcct gccactggcc gagacacaga ggcacacagc   3180 

tggcatactc caggctcaca gaccacgccg gcctggcggg acacacccta ccccaaactc   3240 

ccaacacaga tggaggcagc aacaataaag ccaaaccctt ccagcactca gcacggacca   3300 

ggcacccttc gggggctctg tccacggact cctccccaca accagtccag ctggggaaac   3360 

tgaggctctg ggatgctaag tgggtcagga ctgaattttg aggtcttgag gcacacactg   3420 

gggtcaccaa acagcaccct gtgcgaccta gccacgtgtg attgcaggga cgcccaaggc   3480 

cacccactga aaaaacactg ggtgacagat atagggaccc tcacatgtat ccccccccac   3540 

agcaagcatg ggaatgaaat gcatccttca aaaaaaaaaa aa                      3582