Methods of Detecting Alloantibodies Using HLA and Non-HLA Antigens

Abstract

Described herein are materials and methods for detecting alloantibodies using both HLA and non-HLA antigens in a single assay.

Description

[0001] This application claims priority to U.S. Provisional Patent Application No. 62/222,614, filed on Sep. 23, 2015, which is incorporated herein by reference in its entirety.

FIELD OF THE INVENTION

[0002] The present invention is directed to materials and methods for detecting alloantibodies using both HLA and non-HLA antigens.

BACKGROUND

[0003] Transplant rejection occurs when the immune system of the recipient of a transplant, particularly antibodies produced by the recipient, attacks the transplanted organ or tissue. The recipient's immune system recognizes the transplanted organ as foreign tissue and attempts to destroy it. Rejection also occurs when the transplanted organ comprises the donor's lymphocytes or progenitor stem cells, which may generate an immune response to the recipient tissues such as graft vs. host disease. Chronic rejection is a term used to describe all long term loss of function in organ transplants associated with chronic alloreactive immune response. Long term chronic rejection usually leads to a need for a new transplanted organ about a decade after the initial transplant. Human leukocyte antigens (HLA) are one type of molecules within a transplanted organ in which the recipient's immune system attacks that causes a transplant rejection.

[0004] It is a standard practice in the transplant field to test all potential recipients against a panel of HLA antigens selected to represent a human population and the percentage of HLA alleles against which the serum is reactive is determined. In this panel reactive antibody (PRA) testing reaction of a patient's serum against a high percentage of HLA alleles present in a normal human population is predictive of a high risk of graft rejection.

[0005] Alloantibodies, particularly when donor specific, are one of the most important factors that cause both early and late graft rejection. Despite improvements in the transplantation outcomes, antibody-mediated rejection (AMR) remains substantial and it is associated with increased morbidity, mortality and costs (Colvin, ASN 18(4):1046-1056, 2007).

[0006] The presence of HLA antibodies is widely believed to be the major elements contributing to humoral graft rejections. Transplant recipients with high panel reaction antigens (PRA) are associated with early graft rejection. Elevated donor specific HLA antibodies in the organ recipients either before and/or after allograft transplantation has been associated with acute and chronic AMR and decreased long term graft survival. Despite advanced HLA typing matching programs, there has not been a major improvement in the incidence of Graft-versus-host disease (GVHD). Several studies indicate that in addition to HLA alloantibodies, transplant recipients also develope antibodies against antigens other than HLA molecules. The role of alloantibodies against non-HLA antigens is a critical element in the pathogenesis of acute and chronic allograft outcomes (Tinckam and Chandraker, CJASN 1(3):404-414, 2006).

[0007] Currently, there are no defined non-HLA alloantibody antigens. MHC class I-related chain A (MicA), a group of polymorphic non-HLA antigens expressed on endothelial cells, have been implicated in the pathogenesis of hyperacute, acute and chronic organ allograft rejections (Sumitran-Holgers son, Current Opinion Immunology. 20(5):607-13, 2008). In addition, Vimentin, Angiotensin II Type I receptor (AT1R), LG3 peptide of Perlecan and Collagen V are also considered to be non-HLA antigens (Sigdel and Sarwal, Human Immunology, 74:1486-1490, 2013). Targets for anti-endothelial cell antibody (AECA), islet cell antibodies (ICAs), anti-Liver sinusoidal endothelial cells (anti-LSECs) and Antineutrophil cytoplasmic autoantibodies (ANCA) are also considered as non-HLA antigens. The AECA, ICA, anti-LSECs and ANCA target antigens are not well defined (Hepatology, 40(5):1211-1221, 2004).

[0008] Accordingly, there remains a need in the art for improved methods of HLA typing including methods for determination of percentage of PRA which is rapid, convenient and accurate.

SUMMARY

[0009] In one aspect, described herein is a composition comprising a first collection of solid-phase substrates each coated with different purified human leukocyte antigens (HLAs) to represent the HLA antigen population of a single cell line and a second collection of solid-phase substrates coated with a different non-HLA antigen listed in Table 1 or Table 1A. In some embodiments, the different purified HLA antigens are Class I HLA antigens. In some embodiments, the different purified HLA antigens are Class II HLA antigens.

[0010] In some embodiments, the first collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54 55, 56, 57, 58, 59, 60 or more different Class I HLA antigens. In some embodiments, the first collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more different Class II HLA antigens. In some embodiments, the first collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54 55, 56, 57, 58, 59, 60 or more different Class I HLA antigens and or Class II HLA antigens.

[0011] In some embodiments, the second collection comprises the non-HLA antigen set forth in Table 1 or 1A. In some embodiments, the second collection comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-HLA antigens set forth in Table 1 and/or Table 1A.

[0012] In another aspect, described herein is a kit for determining the percentage of panel reactive antibodies in serum of a subject against HLA antigens comprising a first collection of solid-phase substrates wherein each solid-phase substrate is coated with different purified HLA antigens to represent the HLA antigen population of a single cell line such that said collection simulates the distribution of HLA antigens in a normal human population and a second collection of solid phase substrates wherein each substrate is coated with different purified non-HLA antigens listed in Table 1 or Table 1A.

[0013] In another aspect, described herein is a method for determining the percentage of panel reactive antibodies in serum of a subject against human leukocyte antigens (HLA) antigens, said method comprising: contacting a first collection of solid-phase substrates subtypes and a second collection of solid-phase substrate subtypes with serum from said subject for a sufficient time for anti-HLA antibodies in said serum to bind to said HLA-antigens to form a complex, wherein each substrate subtype in the first collection is coated with different purified HLA antigens to present HLA antigens derived from a cell population of a single cell, wherein each substrate subtype of the second collection is coated with different purified non-HLA antigens listed in Table 1 or Table 1A, detecting the presence of the complex to determine the presence or absence of panel reactive antibodies, and determining the percentage of panel reactive antibodies in the serum. In some embodiments, the subject is a transplant or transfusion recipient. In some embodiments, the serum sample is collected before the subject has received a transplant or transfusion. In other embodiments, the serum sample is collected after the subject has received a transplant or transfusion. In further embodiments, the serum sample is collected both before and after the transplant or transfusion.

[0014] The method of determining the percentage of panel reactive antibodies may be carried out to monitor the risk that the recipient will reject the transplant or transfusion or develop graft versus host disease (GVHD). Thus, in one embodiment the method may further comprise the step of obtaining a base line percentage of panel reactive antibodies before the subject receives the transplant or transfusion. The methods may also comprise a step of comparing the percent of panel reactive antibodies before and after receipt of the transplant and transfusion. The monitoring may be carried out at various time points, after transplant or transfusion to determine if the subject is developing GVHD. For example, in some embodiments, the baseline percentage of panel reactive antibodies is determined between a time period ranging from 1 hour to about 1 year or longer before the subject receives the transplant or transfusion. In some embodiments, the baseline percentage of panel reactive antibodies is determined about 1 hour, about 6 hours, about 12 hours, about 1 day, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 1 months, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months about 1 year or longer before the subject received the transplant or transfusion. In some embodiments, the percent of panel reactive antibodies is determined between a time period ranging from 1 hours to about 1 year or longer after the subject has received the transplant or transfusion. For example, in some embodiments, the percent of panel reactive antibodies is determined about 1 hour, about 6 hours, about 12 hours, about 1 day, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 1 months, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months about 1 year or longer after the subject has received the transplant or transfusion.

[0015] In some embodiments, the detecting step comprises detecting labeled ligand bound to the complex to determine the presence or absence of panel reactive antibodies. In some embodiments, detecting of the labeled ligand is carried out by flow cytometry. In some embodiments, the detecting step comprises detecting the presence of the complex using a solid phase immunoassay or a multiplexed bead immunoassay.

[0016] The solid-phase substrate can be any solid substrate known in the art. In some embodiments, the solid-phase substrate is selected from the group consisting of microparticle, microbead, magnetic bead, ion torrent bead, flow cytometer bead and an affinity purification column. In some embodiments, the solid-phase substrate is a microbead. In some embodiments, the microbead is a laytex microbead. The microbead, in some embodiments, has a diameter ranging from about 2 .mu.m to about 15 .mu.m, inclusive. Microbeads having a diameter of about 2 .mu.m, 3 .mu.m, 4 .mu.m, 5 .mu.m, 6 .mu.m, 7 .mu.m, 8 .mu.m, 9 .mu.m, 10 .mu.m, 11 .mu.m, 12 .mu.m, 13 .mu.m, 14 .mu.m or 15 .mu.m are also contemplated. In some embodiments, at least one microbead presenting Class I HLA antigens is 3 .mu.m is diameter. In some embodiments, at least one microbead presented Class II HLA antigens is 5 .mu.m in diameter. In some embodiments, the microbeads comprise a mixture of 3 .mu.m microbeads presenting Class I HLA antigens and 5 .mu.m microbeads presented Class II HLA antigens.

[0017] In some embodiments, each solid phase substrate is detectably distinguishable from other solid phase substrates within the composition. In some embodiments, the detectably distinguishable solid phase substrates are distinguishable by fluorescent labels.

[0018] In some embodiments, the different purified HLA antigens are Class I HLA antigens. In some embodiments, the HLA antigens are selected such that the HLA antigens presented on the solid phase substrate comprise Class I HLA antigens so as to simulate the distribution of Class I HLA antigens in a normal human population. In some embodiments, the first collection comprises 54 different Class I HLA antigens. In some embodiments, the 54 different Class I HLA antigens are purified from 30 different cell lines. In some embodiments, the first collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54 55, 56, 57, 58, 59, 60 or more different Class I HLA antigens.

[0019] In some embodiments, the different purified HLA antigens are Class II HLA antigens. In some embodiments, the first collection comprises 22 different Class II HLA antigens. In some embodiments, the first collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more different Class II HLA antigens.

[0020] In some embodiments, the second collection comprises different non-HLA antigens set forth in Table 1 or 1A. In some embodiments, the second collection comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more non-HLA antigens set forth in Table 1 and/or Table 1A. The non-HLA antigen, in some embodiments, is a fusion protein comprising at least one domain, wherein the domain is a signal peptide, a modified cytoplasmic domain, purification tag or detection tag. In some embodiments, the domain is the B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag.

BRIEF DESCRIPTION OF THE FIGURES

[0021] FIG. 1 describes the output data from the non-HLA multiplex assay. Four subjects (S10823K, S11114A, S11143B and FL71681) show distinct cross relativities against a panel of non-HLA antigens.

[0022] FIG. 2 describes the trend line of increase of anti-non-HLA antibodies in samples obtained from a patient undergoing 2nd lung graft in a multiplex platform.

[0023] FIG. 3 describes (a) the fusion DPD tag that enhances the multiplex reactivity and (b) the structure of DPD indicates it is an alpha helix loop.

[0024] FIG. 4 describes the Box and whiskers' plot of non-HLA antigens from two patient population using a panel of 21 non-HLA antigens in one test.

[0025] FIG. 5 describe the reactivity of non-HLA fusion proteins detected by an anti- fusion antibody on a multiplex platform.

[0026] FIG. 6 depicts the correlation between the results of the method of the invention in determining the percentage PRA versus a standard cytotoxity test for sample sera.

[0027] FIGS. 7A-7D depict the reaction of the mixture of Class I and Class II beads and their reaction to anti-HLA Class I antibodies (FIGS. 7A and 7B) or anti-HLA Class II antibodies (FIGS. 7C and 7D).

DETAILED DESCRIPTION

[0028] Graft rejection is when transplanted tissue is rejected by the recipient's immune system, which destroys the transplanted tissue. The rejection is an adaptive immune response via cellular immunity and humoral immunity. Chronic rejection induced by humoral response is a major cause of graft dysfunction and re-transplantation. It is well recognized that pre-existing antibodies to HLA antigens expressed by the allograft is detrimental to survival of allografts. The presence of panel-reactive antibodies (PRA) against HLA antigens before transplantation can lead to early rejection. Despite intensive HLA typing screening for HLA matching and progressive monitoring the development of anti-HLA alloantibodies, declining graft function remains a paramount clinical concern.

[0029] With the focus on the graft rejection among HLA-identical-sibling recipients, the slow decline in survival curves of HLA-identical-sibling transplants suggests that antigens other than HLA antigens may contribute to allograft rejection. Transplant recipients have also developed antibodies against targets other than HLA molecules (non-HLA antigens), such as autoimmune antigens.

[0030] The development of a solid phase platform as described in the Examples provided herein allows for large-scale antibody screening for both HLA and non-HLA antigens. As described in Example 6, antibodies to kidney-expressed non-HLA antigens have been identified in kidney allografts patients, resulting in acute kidney rejection and allograft loss. Autoantibodies are also found in patients with chronic humoral rejection.

[0031] The present inventors have discovered that the currently available methods useful for detecting HLA antibodies are not reliable and reproducible for the detection of non-HLA antibodies. For example, ELISA is the most common detection method. However, it is more suitable for a single target. Flow cytometry against panels of endothelial cells is another method, but the use of a cell based assay may result in high background and reliability reduced. As non-HLA antibodies become more relevant to antibody-mediated processes, development of reproducible assays on the multiplex global scales optimized for transplantation for these antibodies becomes important. The multi-plex assays described herein provide a reliable and reproducible method for determining the presence of both HLA and non-HLA antibodies in a single assay.

HLA Antigens

[0032] The HLA locus is highly polymorphic in nature. As disclosed in the Nomenclature for Factors of the HLA System 2000 (Hum. Immunol.; 62(4):419-68, 2001) there are 124 HLA-A alleles, 258 HLA-B alleles, 74 HLA-C alleles, 221 HLA-DRB 1 alleles, 19 DRB3 alleles, 89 DRB4 alleles, 14 DRB5 alleles, 19 DQA1 alleles and 39 DQB1 alleles, with new alleles being discovered continuously. As testament to this rapid progress, a April 2007 update by the WHO nomenclature Committee for Factors of the HLA System (www.anthonynolan.com/HIG/) showed there are 545 HLA-A alleles, 895 HLA-B alleles, 307 HLA-C alleles, 8 HLA-E alleles, 12 HLA-H alleles, 9 HLA-J alleles, 6 HLA-K alleles, 4 HLA-L alleles, 4 HLA-P alleles, 3 HLA-V alleles, 3 DRA alleles, 494 DRB 1 alleles, 1 DRB2 alleles, 44 DRB3 alleles, 13 DRB4 alleles, 18 DRB5 alleles, 3 DRB6 alleles, 2 DRB7 alleles, 10 DRB8 alleles, 1 DRB9 alleles, 34 DQA1 alleles, 83 DQB1 alleles, 23 DPA1, 126 DPB1 alleles, 4 DMA alleles, 7 DMB alleles, 12 DOA alleles and 9 DOB alleles.

[0033] Solid phase immunoassays for the detection and characterization of HLA-specific antibodies provide increased sensitivity and specificity, while being more efficient for time and, compared to the traditionally used cell-based methods. Multiplexed bead immunoassay (MBIA) has emerged as a powerful tool to simultaneously detect several antibodies targets in limited sample volumes. The limited sample volume and time-saving gains of the MBIA have made it an election technique for studies involving multiple factors. The invention provided herein allows for the multiplexed bead immunoassays detecting both HLA reactive antibodies and non-HLA reactive antibodies in a single assay.

Non-HLA Antigens

[0034] This invention describes the development of a multiplex solid phase platform allowing for global-scale antibody screening for both HLA and non-HLA antigens in a biological sample. For example, using such methods, in some embodiments, antibodies to kidney-expressed non-HLA antigens in the kidney allografts patients can be monitored. Some transplant recipients develop autoantibodies with acute kidney rejection and allograft loss. Autoantibodies are also found in patients with chronic humoral rejection.

[0035] The targets of humoral responses against non-HLA antigens are primarily antigens expressed on endothelial cells and epithelial cells and categorized as non-HLA alloantigens or tissue-specific autoantigens. Most of them are either patient- or graft-specific. Whether antibodies to non-HLA antigens are pathogenic and/or whether they can be used as biomarkers for transplant outcome remains unclear (J Am Soc Nephrol 22: 1168-1178, 2011). In addition, targets for anti-endothelial cell antibody (AECA), islet cell antibodies (ICAs), anti-Liver sinusoidal endothelial cells (anti-LSECs) and antineutrophil cytoplasmic autoantibodies (ANCA) are considered as non-HLA antigens. The AECA, ICA, anti-LSECs and ANCA target antigens are not defined and are subject to every research lab's definition (Hepatology, 40(5):1211-1221, 2004).

[0036] Agrin is the most abundantly expressed glycoprotein in the glomerular basement membrane (GBM). The GBM is a basement membrane specialized in ultrafiltration and consists of various matrix molecules, including fibronectin, and collagens. The 22 kDa C-terminus Agrin fagment (CAF) is recently discovered as the biomarkers for kidney function and physical health activities (American journal of nephrology, 38(6):501-508). The presence of anti-Argrin antibodies was associated with the number of rejection episodes prior to diagnosis of transplant glomerulopathy (TGP), a symptom of kidney failure after kidney transplant (American Journal of Transplantation 2005; 5: 383-393).

[0037] Angiotensinogen (AGT) is a component of the renin-angiotensin system (RAS), a hormone system that regulates blood pressure and fluid balance. It is also known as the renin substrate, and is a non-inhibitory member of the serpin family of proteinase inhibitors. It causes vasoconstriction and a subsequent increase in blood pressure. AGT has shown very strong correlation in renal graft rejection and has been validated by customized ELISA assays in independent patient sera and their localization confirmed by immunohistochemistry (J. Proteome Res., 2010, 9 (12), pp 6715-6721).

[0038] Angiotensin II type 1 receptor (AT1R, or ATGR1) is a G protein-coupled receptor that mediates angiotensin effects and causes vasoconstriction in vascular smooth muscle. It mediates most physiologic and pathophysiologic actions of its endogenous ligand, angiotensin II, with overactivity leading to vascular remodeling and hypertension. Antibodies to AT1R are implicated in several vascular pathologies. Several studies have shown that AT1R is associated with antibody-mediated organ rejection.

[0039] Rho GDP-dissociation inhibitor 2 is a protein that, in humans, is encoded by the ARHGDIB gene. It regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. By using two-dimensional Western blotting experiments, Rho GDP-dissociation inhibitor has been identified as the non-HLA antigens target in patients undergoing chronic hemodialysis.

[0040] Aurora kinase A-interacting protein (AURKA) is a cell cycle-regulated kinase that appears to be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. AURKA protein is found at the centrosome in interphase cells and at the spindle poles in mitosis. This gene may play a role in tumor development and progression. By comparing antibody repertoires in pre- and post-transplant sera from several cohorts of patients with and without transplant glomerulopathy, de novo increase of anti-AURKA has been identified as non-HLA antigen.

[0041] Complement C4-B is a part of the classical activation pathway. It provides a surface for interaction between the antigen-antibody complex and other complement components. It can be cleaved to release C4 anaphylatoxin, a mediator of local inflammation. Deficiency of this protein is associated with systemic lupus erythematosus. C4B has been involved with graft injuries by combined with C2a and starts cascades reactions in the antibody mediated damages.

[0042] Chromatin assembly factor 1 subunit B (CHAF1b, CAF-1, or p60) is required for the assembly of histone octamers onto newly-replicated DNA. CAF-I is composed of three protein subunits, p50, p60, and p150. The protein encoded by this gene corresponds to the p60 subunit and is required for chromatin assembly after replication. The encoded protein is differentially phosphorylated in a cell cycle-dependent manner. In addition, it is normally found in the nucleus except during mitosis, when it is released into the cytoplasm. CHAF1b-specific antibodies were predominantly detected in patients with acute myeloid leukemia (AML) one year after allogeneic bone marrow transplantation.

[0043] CXCL11 is a small cytokine belonging to the CC chemokine family. Gene expression of CXCL11 is strongly induced by IFN-.gamma. and IFN-.beta., and weakly induced by IFN-.alpha.CXCL11 has been identified independently as I-TAC. CXCL11 is thought to play a critical role in allograft rejection. It is a dominant chemokine in controlling skin intragraft inflammation. By using high-density protein arrays to identify non-HLA antibodies in chronic allograft injury (CAI) and subsequently validated a subset in a cohort of 172 serum samples collected serially post-transplantation, the authors have identified CXCL11 as the non-HLA antigens (Sigdel et al. Non-HLA antibodies to immunogenic epitopes predict the evolution of chronic renal allograft injury. JASN Apr. 1, 2012 vol. 23 no. 4 750-763).

[0044] CXCL9, also known as MIG, is a CXC inflammatory chemokine. CXCL9 plays a key role in leukocyte trafficking and induces angiostatic effects in human microvacular endothelial cells. CXCL9 enhances T lymphocyte function in alloimmune response. CXCL9 is induced by cytokines, particularly IFN.gamma. during infection, injury, or immunoinflammatory responses. Similar to CXCL11, CLCX9 was identified as non-HLA in the bone marrow transplant patients by microarray.

[0045] Cyclophilin A or peptidylprolyl isomerase A (PPIA) is a ubiquitously distributed protein belonging to the immunophilin family. PPIA was initially believed to function primarily as an intracellular protein. Recent studies have revealed that it can be secreted by cells in response to inflammatory stimuli. It has shown that extracellular PPIA stimulates pro-inflammatory signals in endothelial cells (EC) and vascular smooth muscle cells (VSMC). Similar to AURKA, by compare antibody repertoires in pre- and post-transplant sera from several cohorts of patients with and without transplant glomerulopathy, de novo increase of anti-PPIA has been identified as non-HLA antigen (Dinavah et al., Antibodies Reactive to Non-HLA Antigens in Transplant Glomerulopathy, J Am Soc Nephrol 22: 1168-1178, 2011).

[0046] Eukaryotic translation initiation factor 2A (eIF2A) is a eukaryotic initiation factor. It is required in the initiation of translation. It is an essential factor for protein synthesis. Since eIF2 is essential for translation initiation and therefore protein synthesis, defects in eIF2 are lethal. Its activity is regulated by a mechanism involving both guanine nucleotide exchange and phosphorylation. By using IgG isolated from patients with allograft rejection and look the reactivity against endothelial cell surface, eIF2A has been identified an antigen of interests for liver transplant allograft rejection.

[0047] Alpha-enolase (EOS-1), also known as phosphopyruvate hydratase, is responsible for the catalysis of the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. Higher concentrations of ENO-1 in cerebrospinal fluid more strongly correlated to low-grade astrocytoma. Increased levels of alpha enolase have also been identified in patients who have suffered a recent myocardial infarction or cerebrovascular accident. By looking for the Anti Endothelial Cells antibody targets in the anti-neutrophil cytoplasmic antigens (ANA) associated vasculitides, ENO-1 has been identified as one of the targets.

[0048] Glutamate decarboxylase 2 or glutamic acid decarboxylase 2 (GAD2, GAD65) is an enzyme that catalyzes the decarboxylation of glutamate. It is the targets of autoantibodies in people who later develop type 1 diabetes mellitus or latent autoimmune diabetes. Autoimmunity is the term to describe an attack against native cells and tissues by the immune system. An autoimmune response against glutamic acid decarboxylase in neurons has been implicated in a rare neurological condition known as Stiff-Man syndrome. It has been proposed that a similar autoimmune response against GAD in pancreatic cells may be associated with type 1 diabetes. Circulating GAD65 can be used as a biomarker of islet damage or transplant rejection and it will facilitate in vivo studies of the pathogenesis of anti-GAD65 autoreactivity. By checking simultaneous pancreas-kidney transplant (SPKT) recipients on type 1 diabetic patients, the incidence of rejection episodes was significantly higher in pretransplantation GAD autoantibody-positive daclizumab-treated recipients compared with GAD autoantibody-negative or ATG-treated recipients (Janet al., Pretransplantation GAD-Autoantibody Status to Guide Prophylactic Antibody Induction Therapy in Simultaneous Pancreas and Kidney Transplantation. Transplantation 96(8):745-752, 2013).

[0049] Glial cell-derived neurotrophic factor, also known as GDNF is a small protein that potently promotes the survival of many types of neurons. GDNF has regenerative properties for brain cells and showed potential as treatment for Parkinson's disease--monkeys with an induced form of Parkinson's disease showed less trembling when treated with the drug, and neuronal fibres grew in part of the human brain exposed to the drug. Similar to CXCL11, GDNF is identified as non-HLA in the bone marrow transplant patients by microarray in the chronical renal graft rejection.

[0050] Heterogeneous nuclear ribonucleoprotein K (hnRNPK) is involved in several steps of gene expression regulation. It integrates cellular signaling cascades with multiple processes of gene expression mechanisms. This protein has a role during cell cycle progession of gene expression. It is one of the major pre-mRNA-binding proteins. HNRNPK has been reported to be involved in the life cycle of different viruses by either direct interaction with viral proteins. hnRPNK has been identified by screen a coronary artery cells cDNA library against cardiac allograft vasculopathy patient serum sample as the new antigenic targets (Acevedo et al., Antibodies against heterogeneous nuclear ribonucleoprotein K in patients with cardiac allograft vasculopathy. Journal of Heart and Lung Transplantation, 30(9):1051-1059, 2011).

[0051] Intercellular adhesion molecule 1, ICAM-1, also known as CD54, binds to CD11a/CD18 (HNA5), or CD11b/CD18 (HNA4), and is known for its importance in stabilizing cell-cell interactions and facilitating leukocyte endothelial transmigration. More recently, ICAM-1 has been characterized as a site for the cellular entry of human rhinovirus. Signal-transducing functions of ICAM-1 seem to be associated primarily with proinflammatory pathways. In particular, ICAM-1 signaling seems to produce a recruitment of inflammatory immune cells such as macrophages and granulocytes. ICAM-1 is considered one of AECA. 60% of cardiac recipients have developed anti ICAM-1 IgM (Lawson et al., Anti-intercellular adhesion molecule-1 antibodies in sera of heart transplant recipients: a role in endothelial cell activation. Transplantation 2005; 80: 264-271).

[0052] Gamma-interferon inducible protein 16 (IFI16) also known as interferon-inducible myeloid differentiation transcriptional activator. IFI16 has been shown to play a role in the sensing of intracellular DNA--and has also been linked to HIV-infected helper T-cell pyroptosis. IF116 binds nuclear viral DNA, triggering expression of antiviral cytokines in response to infection with herpesviruses. Similar to eIF2A, IgG isolated from patients with allograft rejection reacts against endothelial cell surface. IF116 has been identified as an antigen of interest for liver transplant allograft rejection.

[0053] Interferon-gamma (IFN-gamma) is crucial for immunity against intracellular pathogens and for tumor control. However, aberrant IFN-gamma expression has been associated with a number of autoinflammatory and autoimmune diseases. It is a potent activator of macrophages, which has antiproliferative effects on transformed cells and can potentiate the antiviral and antitumor effects of the type I interferons. IFN-gamma is produced mainly by T-cells and natural killer cells activated by antigens, mitogens, or alloantigens. Similar to CXCL11, IFN-gamma is identified as non-HLA in the bone marrow transplant patients by high density microarray in the chronical renal graft rejection.

[0054] The interleukin-2 receptor (IL-2R) is a heterotrimeric protein expressed on the surface of certain immune cells, such as lymphocytes, that binds and responds to a cytokine called IL-2. It has three subunits, generated by different combinations of three different proteins, often referred to as "chains": .alpha. (alpha) (also called IL-2R.alpha., CD25, or Tac antigen), .beta. (beta) (also called IL-2R.beta., or CD122), and .gamma. (gamma) (also called IL-2R.gamma., .gamma.c, common gamma chain, or CD132); these subunits are also parts of receptors for other cytokines. The .beta. and .gamma. chains of the IL-2R is membranes of the type I cytokine receptor family. IL-2 and its receptor have key roles in key functions of the immune system, tolerance and immunity, primarily via their direct effects on T cells. The polymorphism of alpha chain has been reported linked to multiple sclerosis, an autoimmune disease.

[0055] Interleukin-7 receptor subunit alpha (IL7R-a), also known as CD127, is the alpha-subunit of IL7 Receptor for interleukin-7 and acts as a receptor for thymic stromal lymphopoietin (TSLP). The interleukin-7 receptor a chain transmits distinct signals for proliferation and differentiation during B lymphopoiesis and is essential for the development of T Cells. There are reports indicating IL7R polymorphisms is associated with inflammatory demyelinating diseases.

[0056] Insulin (INS) is a peptide hormone produced by beta cells in the pancreas and it regulates the metabolism of carbohydrates and fats by promoting the absorption of glucose from the blood to skeletal muscles and fat tissue. Insulin also inhibits the production of glucose by the liver. Type 1 diabetes is a chronic illness characterized by the body's inability to produce insulin due to the autoimmune destruction of the beta cells in the pancreas. Anti-insulin antibodies are a cause of hypoglycemia following pancreas transplantation. In Islet cell transplantation for the treatment of Type 1 diabetes, insulin autoantibodies can be detected in Type 1 diabetes.

[0057] Far upstream element-binding protein 2 (FUBP2) binds to the dendritic targeting element and may play a role in mRNA trafficking. It may activate gene expression. FUBP2 represents a novel and frequent pro-tumorigenic mechanism promoting proliferation (tumor growth) and motility (dissemination) of human liver cancer cells. Similar to ENO-1, by looking for the Anti Endothelial Cells antibody targets in the anti-neutrophil cytoplasmic antigens (ANA) associated vasculitides, FUBP2 has been identified as one of the AECA targets.

[0058] Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Lamin-A plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Whereas Lamin-B 1 (LMNB 1) (.about.585 aa) is in the protein matrix over inner nuclear membrane and has been associated with aging. LMNB 1 forms homodimer. There is a common polymorphism A510V (2%) in Lamin-B1, which is not that significant. The only commercial source for LMNB1 protein is from wheat germ in vitro translation system. There are some LMNB 1 Elisa kits available but it aims for the antigen detection rather than for autoimmune rejection. Lamin A has been identified as one of target antigens of anti-endothelial cell and anti-vascular smooth muscle cell antibodies in patients with giant cell arteritis. Similar to Rho GDP-dissociation inhibitor, by using two-dimensional Western blotting experiments, Lamin B has been identified as the non-HLA antigens target in patients undergoing chronic hemodialysis.

[0059] Myosin comprise a family of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other eukaryotic motility processes. Cardiac myosin (CM) is a heart specific antigen implicated in allograft rejection. Pretransplant myosin autoantibodies correlated with acute cardiac transplant rejection. The expansion of alloreactive T cells was followed by an increase of cardiac myosin reactive T cells and development of anti-myosin IgG1 autoantibodies in a mouse heart transplant model mismatched for minor histocompatibility alloantigens. This supports the idea that CM released during alloimmune injury of the allograft is recognized by CD4+ T helper autoreactive cells through indirect recognition pathway and triggers the generation of autoreactive CM antibodies. Notably, mature CM is not expressed in the thymus during development which may result in incomplete negative selection (Zhang and Reed, Non-MHC antigenic targets of the humoral immune response in transplantation. Curr Opin Immunol. 2010 October; 22(5): 682-688.). Since CM consists of myosin heavy chain and light chains, they may also responsible for the graft rejections.

[0060] Neuropilin-1 (NRP-1) bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. It is a membrane-bound coreceptor to a tyrosine kinase receptor. Neuropilin expression is up-regulated in multiple tumor types, and correlates with tumor progression and prognosis in specific tumors. Neuropilins may indirectly mediate effects on tumor progression by affecting angiogenesis or directly through effects on tumor cells. (Bates et al., High diversity of non-human leukocyte antigens in transplant-associated coronary artery disease. Transplantation. 2003; 75:1347-1350.)

[0061] Nuclear and spindle-associated protein 1 (NuSap1) has been reported to function in mitotic spindle assembly, chromosome segregation, and regulation of cytokinesis. Depletion of NUSAP1 from cells led to the suppression of double strand DNA break repair via the homologous recombination and single-strand annealing pathways. NUSAP1 has recently been identified as a biomarker for aggressive prostate cancer. By testing the sera on protein array, Nusap1 is identified as one of the targets of de novo antibody after allogeneic allogeneic hematopoietic cell transplantation (HCT), Wadia et al., Antibodies specifically target AML antigen NuSAP1 after allogeneic bone marrow transplantation. Blood. 115(10): 2077-2087 2010.)

[0062] Collagen V (Col V) acts as a major risk factor after human lung transplantation. Col V is not normally expressed in healthy tissue. However, Col V is unveiled during graft injuries in lung transplants. Col V-specific T cells appear in lung transplant recipients before the clinical onset of rejection. It has been implicated in a number of autoimmune or inflammatory conditions and allograft rejection. Collagen V are associated with chronic rejection after lung transplantation (American Journal of Transplantation 2014; 14: 685-693).

[0063] The ErbB3 binding protein-1 (EBP1) or Proliferation-associated protein 2G4 (PA2G4) belongs to a family of DNA/RNA binding proteins implicated in cell growth, apoptosis and differentiation. Ebp1 is a well-conserved DNA/RNA binding protein that is implicated in cell growth, apoptosis and differentiation in many cell types. Similar to eIF2A, IgG isolated from patients with allograft rejection reacts against endothelial cell surface. EBP1 has been Identified an antigen of interests for liver transplant allograft rejection.

[0064] Peroxiredoxin 2 (PRDX2) might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. It is the third most abundant protein in erythrocytes. PRDX2 is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells. Proteins extracted from human umbilical vein endothelial cells (HUVEC) were separated by two-dimensional electrophoresis, and Western blotting was subsequently conducted using sera from patients with systemic vasculitis.PRDX2 has been identified as one of the anti-endothelial cell antibodies (AECA) targets in systemic vasculitis (Karasawa et al., Peroxiredoxin 2 is a novel autoantigen for anti-endothelial cell antibodies in systemic vasculitis. Clin Exp Immunol. 161(3):459-70), 2010.

[0065] Protein Kinase C-zeta plays an important role in insulin-stimulated glucose transport. It has at least two alternative transcripts, the full-length PKC.zeta. (this protein) and an N-terminal truncated form PKM.zeta.. PKC.zeta. is about 67 kDa (592 aa) and located in the cytoplasmic region.

[0066] BPI fold-containing family A member 1 (BPIFA1), or palate, lung and nasal epithelium clone (PLUNC) plays a role in the innate immune responses of the upper airways. It reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria. BPIFA1 binds bacterial lipopolysaccharide (LPS) and negatively regulates airway surface liquid homeostasis and proper clearance of mucus. It plays a role in the airway inflammatory response after exposure to irritants.

[0067] 26S protease regulatory subunit 6B (PSMC4) is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. It is a part of the immunoproteasome whose function is to process class I HLA peptides. PSMC4 has been shown to interact with an orphan member of the nuclear hormone receptor superfamily highly expressed in liver, and with gankyrin, a liver oncoprotein. Similar to PLUNC, PSMC4 is discovered as the one of the non-HLA antibodies targets from the lung transplants.

[0068] Islet cell antigen 512 also termed IA-2 is a novel autoantigen of type 1 diabetes, which has a tyrosine phosphatase-like domain. IA-2 is a major target of islet cell autoantibodies. The frequencies of autoantibodies against glutamic acid decarboxylase 65 (GAD65) and islet cell antigen (ICA) 512/IA-2 (512/IA-2) are common on the specific human leukocyte antigen (HLA) in type 1 diabetes mellitus (T1D). In pancreas transplantations, anti-GAD (Glutamic Acid Decarboxylase) and anti-IA2 (protein tyrosine phosphatase, IA-2) autoantibodies is related to the onset of rejection or graft loss. In islet transplantation, the presence of autoantibodies also correlates with a worse evolution and could be a key factor in the chronic failure of the graft (Diabetol Metab Syndr. 2009; 1: 9).

[0069] Tyrosine-protein phosphatase non-receptor type 22 (PTPN22) affects the responsiveness of T and B cell receptors, and mutations are associated with increases or decreases in risks of autoimmune diseases. PTPN22 gene has been associated with autoimmune disorders, including an increased risk of Type 1 Diabetes, rheumatoid arthritis, Systemic Lupus Erythematosus (SLE), Vitiligo and Graves' disease, but a decreased risk of Crohn's disease. PTPN22 acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Protein tyrosine phosphatase non-receptor 22 (PTPN22) plays a central role in T cell, B cell and innate immune cell signaling. The allelic polymorphism, TPN22 R620W-variant allele, could be involved in the susceptibility to acute allograft rejection in kidney transplant patients (Transplant Proc. 2009 March; 41(2):657-9). By using PTPN22 knockout mouse, the lack of the protein tyrosine phosphatase PTPN22 improves transplant tolerance to pancreatic islets in mice (Diabetologia. 2015 Mar. 7).

[0070] Ribosomal Protein L7 (RPL7) plays a regulatory role in the translation apparatus. It is located in the cytoplasm. RPL7 has been shown to be an autoantigen in patients with systemic autoimmune diseases, such as systemic lupus erythematosus. By screening of a HUVEC cDNA library with transplant-associated coronary artery disease sera, RPL7is identified as a candidate autoantigen associated with transplant rejection. (Clin Exp Immunol. 2001; 126:173-179).

[0071] Speedy Homologue A (SPDYA) as a member of the Speedy/RINGO family and a novel activator of cyclin-dependent kinases, was shown to promote cell cycle progression and cell survival in response to DNA damage. SPDYA is a cell cycle protein that promotes cell proliferation by activating cyclin-dependent kinase-2 (CDK2; 116953) at the G1/S phase transition. Overexpression of SPDYA in several human and mouse cell lines increased DNA replication and the rate of cell proliferation. Similar to AGT, SPYDA has shown very strong correlation in renal graft rejection and has been validated by customized ELISA assays in independent patient sera and their localization confirmed by immunohistochemistry.

[0072] Tumor necrosis factor alpha (TNF, tumor necrosis factor, TNF.alpha., cachexin, or cachectin) is a cell signaling protein (cytokine) involved in systemic inflammation. The primary role of TNF is in the regulation of immune cells. TNF, being an endogenous pyrogen, is able to induce fever, apoptotic cell death, cachexia, inflammation and to inhibit tumorigenesis and viral replication. TNF.alpha. stimulates IL1 and GM-CSF, increases tissue damage by IL1 and induces the onset of collagenases by fibroblasts and chondrocytes. It has a role in modulating HLA class 2 expression, as well as the adhesion molecule. TNF .alpha. level more than 45 pg/mL can be taken as an immunological marker of renal transplant rejection (Saudi J Kidney Dis Transpl 2009; 20(6):1000-1004).

[0073] Regenerating Islet-derived protein 3-alpha (Reg3A) or pancreatitis-associated protein 1 (PAP1) is a pancreatic secretory protein that may be involved in cell proliferation or differentiation. PAP is activated in primary liver cancers. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells. Elevated anti Reg3A s has been reported on simultaneous kidney-pancreas transplantation (SKP Tx) patients (2015 American Transplant Congress Abstract #446).

[0074] Receptor tyrosine-protein kinase ERBB-3, also known as HERS (human epidermal growth factor receptor 3), is a member of the epidermal growth factor receptor (EGFR/ERBB) family of receptor tyrosine kinases. The kinase-impaired ERBB3 is known to form active heterodimers with other members of the ErbB family, most notably the ligand binding-impaired ERBB2. ERBB3 binds to the ligands heregulin and NRG-2 and causes a change in conformation that allows for dimerization, phosphorylation, and activation of signal transduction. Similar to eIF2A, IgG isolated from patients with allograft rejection reacts against endothelial cell surface. ERBB3 has been Identified an antigen of interests for liver transplant allograft rejection.

[0075] Platelet glycoprotein 4, or CD36, also known as FAT (fatty acid translocase), FAT/CD36, (FAT)/CD36, SCARB3, GP88, glycoprotein IV (gpIV), and glycoprotein Mb (gpIIIb), is an integral membrane protein found on the surface. CD36 interacts with a number of ligands, including collagen types I and IV, thrombospondin, erythrocytes, platelet-agglutinating protein p37, and long-chain fatty acids. CD36 function in long-chain fatty acid uptake. CD36 is recognized as Naka antigen. The abnormality of anti CD36 antibody has been linked to heart failure in transplant coronary artery disease (Int J Mol Med. 1998 June; 1(6):1007-10).

[0076] Nucleolin (NCL) is a multifunctional phosphoprotein ubiquitously distributed in the nucleolus, nucleus and cytoplasm of the cell. NCL is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. NCL may play a role in the process of transcriptional elongation. It regulates various aspects of DNA and RNA metabolism, chromatin structure, rDNA transcription, rRNA maturation, cytokinesis, nucleogenesis, cell proliferation and growth, the folding, maturation and ribosome assembly and nucleocytoplasmic transport of newly synthesized pre-RNA. Antibodies against NCL are found in many transplant patients and they seemed to be associated with kidney allografts rejection and with coronary artery disease in heart transplant recipients (Transplantation 2011;92: 829-835).

[0077] Peroxisomal trans-2-enoyl-CoA reductase, PECR, is an enzyme responsible for the reduction of phytenoyl-CoA to phytanoyl-CoA in peroxisomes. PECR is strongly expressed in the kidney. Recently, it has been shown that anti-PECR antibodies could be associated with transplant glomerulopathy. Similar to AURKA, by compare antibody repertoires in pre- and post-transplant sera from several cohorts of patients with and without transplant glomerulopathy, de novo increase of anti-PECR has been identified as a non-HLA antigen.

[0078] E3 ubiquitin-protein ligase TRIM21, also known as Tripartite motif-containing protein 21 (TRIM21) is an intracellular antibody effector in the intracellular antibody-mediated proteolysis pathway. TRIM21, also known as Ro52 is often the target of circulating autoantibodies in autoimmune diseases. Studies showed that anti-Ro52 antibodies are associated with different clinical outcomesTRIM21 is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. It interacts with autoantigens in patients with Sjogren's syndrome and systemic lupus erythematosus. TRIM21 is considered as one of AECA target protein. High anti-TRIM21 was correlated to renal rejection.

[0079] Proteasome subunit alpha type-4, PSMA4, is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. Proteasome dysfunction leads to many diseases including cancer, and drugs that inhibit proteasome activity directly affect lung cancer susceptibility through its modulation of cell proliferation and apoptosis. It has been reported that proteasome subunit alpha type-4 (PSMA4) mRNA levels are increased in lung tumors, and down-regulation of PSMA4 expression decreased proteasome activity. PSMA4 has been identified on renal rejection patient as one of the non-HLA candidates (American Journal of Transplantation 2009; 9:2126-2135).

[0080] Tissue factor (F3) also called platelet tissue factor, factor III, thromboplastin, or CD142 is a protein present in subendothelial tissue and leukocytes necessary for the initiation of thrombin formation from the zymogen prothrombin. The best known function of tissue factor is its role in blood coagulation. The signaling function of F3 plays a role in angiogenesis and apoptosis. Similar to PLUNC, F3 is discovered as the one of the non-HLA antibodies targets from the lung transplants.

[0081] 60 kDa SS-A/Ro ribonucleoprotein is also known as TROVE domain family, member 2 (TROVE2) functions as a RNA chaperone that binds to misfolded pre-5S ribosomal RNA and may hasten the degradation of the defective molecule. Autoantibodies directed against Ro/SSA and La/SSB autoantigens were originally identified in patients with Sjogren's syndrome and systemic lupus erythematosus (SLE). Subsequent studies showed that anti-Ro/SSA antibodies may be present in patients with other autoimmune diseases, including systemic sclerosis, idiopathic inflammatory myopathies (IIM), primary biliary cirrhosis (PBC), and rheumatoid arthritis (RA). Additionally, anti-Ro/SSA antibodies (with or without anti-La/SSB antibodies) identify pregnant women who are at increased risk of having a child with neonatal lupus syndrome. Polymorphism of TROVE2 (L10P) has linked to lung transplant by TGF-beta (Clin Rev Allergy Immunol. 2011 February; 40(1): 27-41).

[0082] Interferon-induced helicase C domain-containing protein 1 (IFIH1) plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. IFIH1 polymorphisms have been associated with type 1 diabetes. Autoimmune disease risk variant of IFIH1 is associated with increased sensitivity to IFN-.alpha. and serologic autoimmunity in lupus patients (J Immunol. 2011 Aug. 1; 187(3):1298-303).

[0083] Tubulin is the major building block of microtubules. The tubulin family consist of alpha- and beta-tubulin. To form microtubules, the dimers of .alpha.- and .beta.-tubulin bind to GTP and assemble onto the (+) ends of microtubules while in the GTP-bound state. Antibodies to KA1 tubulin (TUBA1B) is associated with chronic rejection after lung transplantation (J Immunol. 2008 Apr. 1; 180(7):4487-94). Similar to Rho GDP-dissociation inhibitor, by using two-dimensional Western blotting experiments, beta tubulin has been identified as the non-HLA antigens target in patients undergoing chronic hemodialysis.

[0084] Perlecan (PLC) also known as basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) or heparan sulfate proteoglycan 2 (HSPG2). Perlican LG3 peptide lies inside the Endorepellin subunit which is the domain V of Perlecan. LG3 is a biomarker for breast cancer, IgA induced nephropathy, physical status, and acute allograft vascular rejection. Patients with increased anti-LG3 antibodies have correlated with accelerated organ rejection. In addition, anti-LG3 antibodies also increase deposit buildups and induce clogged arteries (American Journal of Transplantation 2013; 13: 861-874).

[0085] PRKR-interacting protein 1 protein (PRKRIP1) binds double-stranded RNA. PRKRIP1 interacts with PKR (protein kinase RNA-activated) and functions to inhibit or negatively regulate PKR activity and is associated with adipogenesis. Similar to AGT, PRKRIP1 has shown very strong correlation in renal graft rejection and has been validated by customized ELISA assays in independent patient sera and their localization confirmed by immunohistochemistry.

[0086] Endothelin receptor type A, also known as ETAR or EDNRA, is a human G protein-coupled receptor for the endothelin-1. Endothelin-1 promotes myofibroblast induction through the ETA receptor via a rac/phosphoinositide 3-kinase/Akt-dependent pathway and it is essential for the enhanced contractile phenotype of fibrotic fibroblasts. ENDRA polymorphism 1136L has been linked to breast cancer. EDNRA expresses only in platelets. The presence of anti-ETAR antibodies is associated with a decrease renal transplant function during the first 12months after transplantation (Transpl Immunol. 2014 Jan.; 30(1):24-9).

[0087] Fibronectin (FN) is a high-molecular weight (.about.440 kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. FN plays a major role in cell adhesion, growth, migration, and differentiation, and it is important for processes such as wound healing and embryonic development. Similar to Collagen V, elevated anti FN antibodies has linked to transplant Glomerulopathy in renal graft recipients (American Journal of Transplantation 2014; 14: 685-693).

[0088] Fibronectin Leucine-rich Repeat transmembrane protein 2 (FLRT2) functions in cell adhesion and receptor signaling. FLRT2 is required in the epicardium to promote heart morphogenesis. FLRT2 is involved in mediating cell-matrix interactions. Anti-FLRT2 antibody has the potential to induce direct endothelial cell cytotoxicity. By using the human umbilical vein endothelial cells retroviral expression system, FLRT2 has been identified as one of the AECA targets on for systemic lupus erythematosus patient (Arthritis Res Ther. 2012; 14(4): R157).

[0089] Vimentin (VIM) is a non-polymorphic intermediate filament expressed in cytosol of endothelial, vascular smooth muscle cells, activated platelets and macrophages, renal tubular cells, mesangial cells and renal stromal cells. VIM expressed in the intima and media of coronary arteries where vascular smooth muscle cells and fibroblasts locate. Autoimmune responses to VIM are associated with both acute and chronic rejection of heart and renal allografts. Anti-vimentin antibodies are an independent predictor of transplant-associated coronary artery disease and can be used to identify some of the patients who are at high risk of developing this complication (Transplatation Vol. 71, 886-892, No. 7, Apr. 15, 200).

[0090] Glutathione S-transferase theta-1 (GSTT1) conjugate reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Individuals with a homozygous deletion of the glutathione S-transferase theta 1 (GSTT1) gene lack GSTT1 enzymatic detoxification and have high risk of acute myeloid leukemia. In liver transplant,antibodies against glutathione-S-transferaseT1 (GSTT1) expressed on the graft may induce an antibody response leading to a severe graft dysfunction. In addition, donor- specific antibodies against MICA and GSTT1 antigens could be responsible for the occurrence of antibody-mediated kidney graft rejection (Transplantation 2009; 87: 94-99).

[0091] Endoplasmic reticulum lipid raft-associated protein 2 (ERLIN2) plays a critical role in inositol 1,4,5-trisphosphate (IP3) signaling by mediating ER-associated degradation of activated IP3 receptors. Mutations in this gene are a cause of spastic paraplegia-18 (SPG18). ERLIN2 is in the prohibitin family of proteins that define lipid-raft-like domains of the ER. ERLIN2 may confer a selective growth advantage for breast cancer cells by facilitating a cytoprotective response to various cellular stresses. Similar to eIF2A, IgG isolated from patients with allograft rejection reacts against endothelial cell surface. ERLIN2 has been Identified an antigen of interests for liver transplant allograft rejection.

[0092] Complement Factor H (CFH) is a member of the regulators of complement activation family. Factor H has been shown to interact with Complement component 3. A shortage (deficiency) of complement factor H can cause uncontrolled activation of the complement system. Complement factor H deficiency, a known hereditary risk factor for post-transplant thrombotic microangiopathy (TMA), may also favor development of acute allograft glomerulopathy AAG. Unopposed complement activation is a risk factor for both immune and nonimmune forms of microvascular injuries in renal allografts (Fortin et al. Am J Transplant. 2004 Feb.; 4(2):270-3.) Atypical Hemolytic Uremic Syndrom (HUS) associated with anti-CFH autoantibodies is an uncommon illness associated with high risk of progression to end-stage renal disease (Khandelwal et al. Pediatr Transplant. 2014 August; 18(5):E134-9)

[0093] Complement C3 produced within the kidney is an important mediator of inflammatory and immunological injury. Synthesis of complement component C3 regulates acute renal transplant rejection. Patients with SLE had increased titers of anti-C3 antibodies, compared with healthy controls. C3 nephritic factors (increased C3 autoantibodies) prolong the half-life or prevent regulation of the alternative pathway C3 convertase; result in uncontrolled complement activation. They are strongly associated with renal disease with symptoms like acquired partial lipodystrophy (APLD) or C3 glomerulopathy (C3GP) (Dragon-Durey 2013, Molecular Immunology 56 (2013) 213-221)

[0094] Phospholipase A2 Receptor , a 185 kDa type I transmembrane glycoprotein expressed on glomerular podocytes, is identified as a major target antigen of the autoantibodies involved in membranous nephropathy (MN), a common cause of adult nephrotic syndrome, one of the most common glomerulonephritides involving the renal transplant. (Dai et al. 2015, Nature). Idiopathic membranous nephropathy, a common form of the nephrotic syndrome, is an antibody-mediated autoimmune glomerular disease. A majority of patients with idiopathic membranous nephropathy have antibodies against a conformation-dependent epitope in PLA2R. PLA2R is present in normal podocytes and in immune deposits in patients with idiopathic membranous nephropathy, indicating that PLA2R is a major antigen in this disease. In addition, Anti-PLA(2)R autoantibodies in serum samples from patients with membranous nephropathy were mainly IgG4.

[0095] In some embodiments, the non-HLA antigen is selected from the set of non-HLA antigens set forth in Table 1.

TABLE-US-00001 TABLE 1 Uniprot SEQ Non-HLA Antigen Description Alias Access No. ID NO Agrin (CAF) AGRN O00468 1 Angiotensinogen AGT P01019 2 Rho GDP-dissociation inhibitor 2 ARGHDIB P52566 3 Aurora kinase A-interacting protein AURKA Q9NWT8 4 Complement C4-B C4B, C4D P0C0L5 5 Chromatin assembly factor 1 subunit B CHAF1b, CAF-1, p60 Q13112 6 C--X--C motif chemokine 11 ITAC, CXCL11 O14625 7 C--X--C motif chemokine 9 MIG, CXCL9 Q07325 8 Cyclophilin A PPIA P62937 9 Eukaryotic translation initiation factor 2A EIF2A Q9BY44 10 Alpha-enolase ENO1 P06733 11 Glutamate decarboxylase 2 GAD2, GAD65 Q05329 12 Glial cell line-derived neurotrophic factor GDNF P39905 13 Heterogeneous nuclear ribonucleoprotein K HNRNPK P61978 14 Intercellular adhesion molecule 1 ICAM-1, CD54 P05362 15 gamma-interferon inducible protein 16 IFI16 Q16666 16 gamma-interferon IFN-.gamma. P17803 17 Interleukin-2 receptor subunit alpha IL2RA, CD25 P01589 18 Interleukin-7 receptor subunit alpha IL7R, CD127 P16871 19 Insulin INS P01308 20 Far upstream element-binding protein 2 FUBP2, KHSRP Q92945 21 Lamin A/C LMNA P02545 22 Lamin B1 LMNB1 P20700 23 NEUROPHILIN-1 NRP1, CD304 O14786 24 Nucleolar and spindle-associated protein 1 NUSAP1 Q9BXS6 25 ERBB3 Binding protein 1 PA2G4, EBP1 Q9UQ80 26 PEROXIREDOXIN 2 PRDX2 P32119 27 Protein Kinase C-zeta PKC-Z Q05513 28 BPI fold-containing family A member 1 PLUNC, BPIFA1 Q9NP55 29 26S protease regulatory subunit 6B PSMC4 P43686 30 Islet cell antigen 512 PTPRN, PTPIA2, ICA512 Q16849 31 Tyrosine-protein phosphatase non-receptor type 22 PTPN22 Q9Y2R2 32 Ribosomal Protein L7 RPL7 P18124 33 Speedy Homologue A SPDYA Q5MJ70 34 Tumour necrosis factor alpha TNF-.alpha. P01375 35 Regenerating Islet-derived protein 3-alpha PAP-1, REG3A Q06141 36 Receptor tyrosine-protein kinase erbB-3 ERBB3 P21860 37 Platelet glycoprotein 4 CD36 P16671 38 Nucleolin NCL P19338 39 Peroxisomal trans-2-enoyl-CoA reductase PECR Q9BY49 40 E3 ubiquitin-protein ligase TRIM21 TRIM21, RO52 P19474 41 Proteasome subunit alpha type-4 PSMA4 P25789 42 Tissue factor F3, TFA, CD142 P13726 43 60 kDa SS-A/Ro ribonucleoprotein TROVE2, RO60 P10155 44 Interferon-induced helicase C domain-containing IFIH1 Q9BYX4 45 protein 1 alpha Tubulin-1A TUBA1A Q71U36 46 alpha Tubulin 1B TUBA1B P68363 47 alpha Tubulin 1C TUBA1C Q9BQE3 48 beta Tubulin TUBB P07437 49 Perlecan LG3 HSPG2 P98160 50 PRKR-interacting protein 1 PRKRIP1 Q9H875 51 Endothelin Receptor type A EDNRA, ETAR P25101 52 Fibronectin Leucine-rich Repeat Transmembrane FLRT2 O43155 53 protein Vimentin Vim P08670 54 Angiotensin II Type I receptor AT1R, AGTR1 P30556 55 C-type lectin domain family 16, member A CLEC16A Q2KHT3 56 Collagen I COL1A1, COL1A2 P02452 57 Collagen II COL2A1, COL2A2 P02458 58 Collagen III COL3A1, COL3A2 P02461 59 Collagen IV COL4A1, COL4A2 P02462 60 Collagen V COL5A1, COL5A2 P20908 61 Cytotoxic T-lymphocyte protein 4 CTLA4, CD152 P16410 62 Endoplasmic reticulum lipid raft-associated protein 2 ERLIN2 O94905 63 Fibronectin FN1 P02751 64 Glutathione S-transferase theta-1 GSTT1 P30711 65 Keratin, type II cytoskeletal 1 KRT1 P04264 66 Myosin Heavy Chain alpha MYH6 MYH6 P13533 67 Myosin Heavy Chain beta MYH7 MYH7 P12883 68 Myosin Light Chain MYL4 MYL4 P12829 69 Zinc finger protein 33A ZNF33A Q06730 70 Zinc transporter 8 ZnT8, SLC30A8 Q8IWU4 71 Complement Factor H CHF P08603 72 Complement C3 C3 P01024 73 Phospholipase A2 Receptor PLA2R1 Q13018 74

[0096] In some embodiments, the non-HLA antigen is selected from the set of non-HLA antigens set forth in Table 1A.

TABLE-US-00002 TABLE 1A Uniprot Non-HLA Antigen Description Alias Access No. Publication No. Protein Kinase C-zeta PKC-Z Q05513 US 20120077689 Ribosomal Protein L7 RPL7 P18124 U.S. Pat. No. 7,132,245 Perlecan LG3 HSPG2 P98160 US20130004978 Endothelin Receptor type A EDNRA, ETAR P25101 U.S. Pat. No. 8,592,164 Vimentin Vim P08670 U.S. Pat. No. 7,132,245 Angiotensin II Type I receptor AT1R, AGTR1 P30556 U.S. Pat. No. 8,425,877 Collagen II COL2A1, COL2A2 P02458 WO2000037940 Collagen V COL5A1, COL5A2 P20908 U.S. Pat. No. 8,039,225 Glutathione S-transferase theta-1 GSTT1 P30711 US 20110039281 Myosin Light Chain MYL4 MYL4 P12829 US 20120077689 Zinc transporter 8 ZnT8, SLC30A8 Q8IWU4 US20100143374 Complement Factor H CFH P08603 U.S. Pat. No. 8,501,427 Anti-Phospholipase-A2-Receptor PLA2R1 Q13018 US 20110177534

Preparation of HLA and Non-HLA-Antigens

[0097] In some embodiments, the HLA antigen and/or the non-HLA antigen is a fusion protein. For example, the invention provides for transforming or transfecting host cells with a nucleic acid encoding the amino acid sequence of an HLA antigen polypeptide or a non-HLA antigen polypeptide fused with a heterologous domain selected from the group consisting of B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag. A nucleic acid molecule encoding the amino acid sequence of an HLA antigen polypeptide or a non-HLA antigen polypeptide may be fused with the domain and inserted into an appropriate expression vector using standard ligation techniques. Exemplary vectors include, but are not limited to, bacterial vectors, eukaryotic vectors, plasmids, cosmids, viral vectors, adenovirus vectors and adenovirus associated vectors.

[0098] The HLA antigen polypeptide and/or the non-HLA antigen polypeptide may contain a sequence encoding a "tag" or exogenous amino acid sequence, such as an oligonucleotide molecule located at the 5' or 3' end of the non-HLA polypeptide coding sequence; an oligonucleotide sequence encoding polyHis (such as hexaHis), FLAG, hemaglutinin influenza virus (HA), V5 or myc or other tags, for which commercially available antibodies exist. This tag may be fused to the non-HLA polypeptide upon expression. The term "exogenous" as used herein refers to a substance or molecule originating or produced outside of an organism. The term "exogenous gene" or "exogenous nucleic acid molecule," as used herein, refers to a nucleic acid that codes for the expression of an RNA and/or protein that has been introduced ("transformed") into a cell or a progenitor of the cell. An exogenous gene may be from a different species (and so a "heterologous" gene) or from the same species (and so a "homologous" gene), relative to the cell being transformed.

[0099] In some embodiments, the expression vectors contain sequences for cloning and expression of exogenous nucleotide sequences. Such sequences may include one or more of the following nucleotide sequences: a promoter, one or more enhancer sequences, an origin of replication, a transcriptional termination sequence, a complete intron sequence containing a donor and acceptor splice site, a sequence encoding a leader sequence for polypeptide secretion, a ribosome binding site, a polyadenylation sequence, a polylinker region for inserting the nucleic acid encoding the polypeptide to be expressed, and a selectable marker element.

[0100] In some embodiments, the vector comprises a selectable marker gene element. A selectable marker gene element encoding a protein necessary for the survival and growth of a host cell grown in a selective culture medium may also be a component of the expression vector. Exemplary selection marker genes include those that encode proteins that complement auxotrophic deficiencies of the cell; or supply critical nutrients not available from complex media. The invention also contemplates that the HLA antigen polypeptides and/or non-HLA antigen polypeptides described herein comprise one or more of these exogenous amino acid sequences.

[0101] In some embodiments, a leader, or signal, sequence is used to direct the non-HLA antigen polypeptide (or HLA antigen polypeptide) out of the stem cell after administration. For example, a nucleotide sequence encoding the signal sequence is positioned in the coding region of the non-HLA antigen encoding nucleic acid (or HLA antigen encoding nucleic acid), or directly at the 5' end of the non-HLA antigen coding region (or HLA antigen coding region). The signal sequence may be homologous or heterologous to the non-HLA antigen polypeptide (or HLA antigen polypeptide) gene or cDNA, or chemically synthesized. The secretion of the non-HLA antigen polypeptide (or HLA antigen polypeptide) from the stem cell via the presence of a signal peptide may result in the removal of the signal peptide from the secreted non-HLA antigen polypeptide (or HLA antigen polypeptide). The signal sequence may be a component of the vector, or it may be a part of the nucleic acid molecule encoding the non-HLA antigen polypeptide (or HLA antigen polypeptide) that is inserted into the vector.

[0102] In some embodiments, the domain is a cytoplasmic domain, or traffic signal, sequence. Cytoplasmic domain sequences may be used to direct the non-HLA antigen polypeptides (or HLA antigen polypeptides) out of the cells after administration or to modify its characteristics to avoid cell signaling pathway that leads to cell death.

[0103] The vectors described herein optionally comprise a promoter operably linked to the nucleic acid encoding the non-HLA antigen polypeptide (or HLA antigen polypeptide). Promoters are untranscribed sequences located upstream to the start codon of a structural gene that control the transcription of the structural gene. Inducible promoters initiate increased levels of transcription from DNA under their control in response to some change in culture conditions, such as the presence or absence of a nutrient or a change in temperature. Alternatively, constitutive promoters initiate continual gene product production with little or no control over gene expression. A large number of promoters, recognized by a variety of potential host cells, are well known. The native non-HLA (or HLA) gene promoter sequence may be used to direct amplification and/or expression of the non-HLA (or HLA) polypeptide nucleic acid molecule. A heterologous promoter also may be used to induce greater transcription and higher yields of the non-HLA (or HLA) polypeptide expression as compared to the non-HLA (or HLA) polypeptide expression induced by the native promoter.

[0104] In addition, an enhancer sequence may be inserted into the vector to increase the transcription of a DNA encoding the non-HLA antigen polypeptide (or HLA antigen polypeptide). Enhancers are cis-acting elements of DNA, usually about 10-300 by in length, that act on the promoter to increase transcription. Enhancer sequences available from mammalian genes include globin, elastase, albumin, alpha-feto-protein and insulin. Exemplary viral enhancers that activate eukaryotic promoters include the SV40 enhancer, the cytomegalovirus early promoter enhancer, the polyoma enhancer, and adenovirus enhancers. While an enhancer may be spliced into the vector at a position 5' or 3' to a nucleic acid molecule encoding the non-HLA antigen polypeptide (or HLA antigen polypeptide), it is typically located at a site 5' from the promoter. The enhancer may be native to the non-HLA antigen polynucleotide sequence or may be heterologous to the non-HLA antigen polynucleotide sequence.

[0105] The transformation of an expression vector encoding a non-HLA antigen polypeptide (or HLA antigen polypeptide) into a host cell may be accomplished by well-known methods such as transfection, infection, calcium chloride, electroporation, microinjection, lipofection or the DEAE-dextran method or any other technique known in the art. These methods and other suitable methods are well known in the art, for example, in Sambrook, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press; 3rd ed., 2001, the disclosure of which is incorporated herein by reference in its entirety.

[0106] Expression vectors of the invention may be constructed from a starting vector such as a commercially available vector. Such vectors may or may not contain all of the desired flanking sequences. Where one or more of the desired flanking sequences are not already present in the vector, they may be individually obtained and ligated into the vector. Methods used for obtaining each of the flanking sequences are well known to one skilled in the art.

[0107] Preferred vectors for practicing this invention are those which are compatible with bacterial, insect, and mammalian host cells. Such vectors include, inter alia, pCRII, pCR3, and pcDNA3.1 (Invitrogen Company, Carlsbad, Calif.), pBSII (Stratagene Company, La Jolla, Calif.), pET15? (Novagen, Madison, Wis.), pGEX (Pharmacia Biotech, Piscataway, N.J.), pEGFP-N2 (Clontech, Palo Alto, Calif.), pETL (BlueBacIl; Invitrogen), pDSR-alpha (PCT Publication No. WO90/14363) and pFastBacDual (Gibco/BRL, Grand Island, N.Y.).

[0108] Additional suitable vectors include, but are not limited to, cosmids, plasmids or modified viruses, but it will be appreciated that the vector system must be compatible with the selected host cell. Such vectors include, but are not limited to plasmids such as Bluescript.RTM. plasmid derivatives (a high copy number ColE1-based phagemid, Stratagene Cloning Systems Inc., La Jolla Calif.), PCR cloning plasmids designed for cloning Taq-amplified PCR products (e.g., TOPO.TM. TA Cloning.RTM. Kit, PCR2.1.RTM. plasmid derivatives, Invitrogen, Carlsbad, Calif.), and mammalian, yeast, or virus vectors such as a baculovirus expression system (pBacPAK plasmid derivatives, Clontech, Palo Alto, Calif.). The recombinant molecules can be introduced into host cells via transformation, transfection, infection, or other known techniques.

[0109] Host cells may be prokaryotic host cells (such as E. coli) or eukaryotic host cells (such as a yeast cell, an insect cell or a vertebrate cell). The host cell, when cultured under appropriate conditions, synthesizes a non-HLA antigen polypeptide (or HLA antigen polypeptide) described herein which can subsequently be collected from the culture medium (if the host cell secretes it into the medium) or directly from the host cell producing it (if it is not secreted). The selection of an appropriate host cell will depend upon various factors, such as desired expression levels, polypeptide modifications that are desirable or necessary for activity, such as glycosylation or phosphorylation, and ease of folding into a biologically active molecule.

[0110] A number of suitable host cells are known in the art and many are available from the American Type Culture Collection (ATCC), 10801 University Boulevard, Manassas, Va. 20110-2209. Examples include, but are not limited to, mammalian cells, such as Chinese hamster ovary cells (CHO) (ATCC No. CCL61) CHO DHFR-cells (Urlaub et al., Proc. Natl. Acad. Sci. USA, 97:4216-4220 (1980)), human embryonic kidney (HEK) 293 or 293T cells (ATCC No. CRL1573), Hmy2.ClR cells (ATCC No. CRL1992) or K562 cells (ATCC No. CCL243). The selection of suitable mammalian host cells and methods for transformation, culture, amplification, screening and product production and purification are known in the art. Other suitable mammalian cell lines, are the monkey COS-1 (ATCC No. CRL1650) and COS-7 cell lines (ATCC No. CRL1651), and the CV-1 cell line (ATCC No. CCL70). Further exemplary mammalian host cells include primate cell lines and rodent cell lines, including transformed cell lines. Normal diploid cells, cell strains derived from in vitro culture of primary tissue, as well as primary explants, are also suitable. Candidate cells may be genotypically deficient in the selection gene, or may contain a dominantly acting selection gene. Other suitable mammalian cell lines include but are not limited to, mouse neuroblastoma N2A cells, HeLa, mouse L-929 cells, 3T3 lines derived from Swiss, Balb-c or NIH mice, BHK or HaK hamster cell lines, which are available from the ATCC. Each of these cell lines is known by and available to those skilled in the art of protein expression.

Methods of Detecting HLA- and Non-HLA-Specific Antibodies

[0111] The invention provides for methods for determining the percentage of panel reactive antibodies in a biological sample from a subject against human leukocyte antigens. In some embodiments, the method comprises contacting a first collection of solid-phase substrates subtypes and a second collection of solid-phase substrate subtypes with serum from said subject for a sufficient time for anti-HLA antibodies in said serum to bind to said HLA-antigens to form a complex, wherein each substrate subtype in the first collection is coated with different purified HLA antigens to present HLA antigens derived from a cell population of a single cell, wherein each substrate subtype of the second collection is coated with different purified non-HLA antigens listed in Table 1 or Table 1A, detecting the presence of the complex to determine the presence or absence of panel reactive antibodies, and determining the percentage of panel reactive antibodies in the serum.

[0112] The term "panel reactive antibody" as used herein refers to an antibody in the biological sample from a subject that specifically binds to an HLA antigen present on the solid-phase substrate or specifically binds to a non-HLA antigen.

[0113] The methods are carried out with solid-phase panels wherein the panel comprises substrates that present (or have immobilized) at least one or more selected HLA antigens. The invention also may be carried out with liquid-phase assays such as assays using column chromatography, affinity chromatography, thin layer chromatography, liquid-phase immunodiagnostic (LIPA) assays, liquid-phase chemiluminescent ELISA and liquid-phase immunoradiometric (IRMA) to name a few.

[0114] HLA- and non-HLA antigens described herein may be a whole protein, a truncated protein, a fragment of a protein or a peptide. Antigens may be naturally occurring, genetically engineered variants of the protein, or may be codon optimized for expression in a particular mammalian subject or host. Generally, a B-cell epitope will include at least about 5 amino acids but can be as small as 3-4 amino acids. The antigens may be recombinantly expressed and purified from cells that either endogenously express the HLA antigens at a low level or do those that do not endogenously express the HLA antigens. Furthermore, the HLA antigens may be recombinantly expressed and presented on the cell surface, and the cells would be used in the methods of the invention.

[0115] Normally, an epitope will include between about 7 and 15 amino acids, such as, 9, 10, 12 or 15 amino acids. The term "antigen" denotes both subunit antigens, (i.e., antigens which are separate and discrete from a whole organism with which the antigen is associated in nature). Antibodies such as anti-idiotype antibodies, or fragments thereof, and synthetic peptide mimotopes, that is synthetic peptides which can mimic an antigen or antigenic determinant, are also captured under the definition of antigen as used herein.

[0116] Furthermore, for purposes of the present invention, an "antigen" refers to a protein, which includes modifications, such as deletions, additions and substitutions, generally conservative in nature, to the naturally occurring sequence, so long as the protein maintains the ability to elicit an immunological response, as defined herein. These modifications may be deliberate, as through site-directed mutagenesis, or may be accidental, such as through mutations of hosts which produce the antigens. Antigens of the present invention may also be codon optimized by methods known in the art to improve their expression or immunogenicity in the host.

[0117] Exemplary solid-phase assays such as assays of the invention may use solid substrates such as microparticles, microbeads, magnetic particles such as ferromagnetic beads and paramagnetic beads, microtiter plates, membranes, filters, glass, metal, metal-alloy, anopol, polymers, nylon, plastic or microarrays such as protein chips. Microarrays may be of any material such as glass or silica. Binding on a microtiter plate may be detected using ELISA assays, RIA assays or other immunosorbent sandwich assays. Binding on a filter may be detected using immunoblotting techniques.

[0118] Methods known in the art for HLA testing include the complement-dependent lymphocytotoxicity (CDC) test in which serum from a recipient is incubated with donor or panel lymphocytes followed by incubation with complement. The level of cytotoxicity is estimated by discriminating between dead and viable cells using a dye. This method is labor intensive, requires viable cells, may be nonspecific and requires a subjective evaluation.

[0119] Pouletty et al. U.S. Pat. No. 5,223,397 discloses methods for testing HLA compatibility between a donor and a recipient comprising the steps of adding blood from the donor to a substrate having anti-HLA antibodies bound thereto and incubating for sufficient time for soluble HLA antigens present in the blood to bind to the antibodies or ligand. Blood from the recipient is then added to the solid substrate whereby any antibody specific for any HLA antigens bound to the solid substrate may become bound. The detection of an absence of antibodies from the recipient's blood to the HLA antigen is indicative of a cross-match.

[0120] Zaer et al., Transplantion 63: 48-51 (1997) discloses use of an ELISA using HLA class I molecules purified from pooled platelets to detect anti-HLA antibodies. The reference reports that in patients found to be unsensitized, the incidence of false-positive results was less for ELISA testing than for panel studies. In patients who were highly sensitized, both tests performed equally well, whereas discordant results were registered mainly in cases of mild sensitization. In such cases, the incidence of false-negative results was higher for ELISA testing than for panel studies.

[0121] Of interest to the present invention are assay methods making use of flow cytometry. Wilson et al., J. Immunol. Methods 107: 231-237 (1988) disclose the use of polyacrylamide microspheres coupled with cell membrane proteins in immunofluorescence assays for antibodies to membrane-associated antigens. The method is said to make possible the rapid flow cytometric analysis of plasma membrane antigens from cell populations that would otherwise be unsuitable for use in flow cytometry. Scillian et al., Blood 73: 2041-2048 (1989) disclose the use of immunoreactive beads in flow cytometric assays for detection of antibodies to HIV. Frengen et al., Clin. Chem. 40/3: 420-425 (1994) disclose the use of flow cytometry for particle-based immunoassays of ce-fetoprotein (AFP). This reference further reports the ability of serum factors to cross-link labeled mouse monoclonal antibodies of irrelevant specificity to different particle types coated with various immunoglobulins.

[0122] Flow cytometry methods using lymphocytes are also known but suffer with difficulties because of the activity of auto-antibodies. See Shroyer et al., Transplantation 59:626-630 Moreover, when using flow cytometry with lymphocytes, use of ten or more different lymphocytes tends to result in confusing signals. As a consequence, studies using lymphocytes have been limited by presenting a small panel of HLA antigens that do not effectively simulate the distribution of HLA antigens in a normal human population.

[0123] Sumitran-Karuppan et al., Transplantation 61: 1539-1545 (1996) discloses the use of magnetic beads which use an anti-HLA capture antibody to immobilize a variety of soluble HLA antigens pooled from 80 to 100 individuals on each bead. The beads can then be directly added to patient serum for efficient absorption of HLA antibodies. The reference discloses visualization of antibody binding to the antigen-coated beads using flow cytometry. The reference suggests that this development will allow testing for antibody specificity for crossmatching purposes and for the screening of panel-reactive antibodies. The methods of Sumitran-Karuppan are limited, however, because the pooling of antigens causes sensitivity to certain rare HLA antigens. Moreover, the method is not capable of detecting the percentage of PRA.

Solid-Phase Substrates

[0124] The solid-phase substrates described herein include, but are not limited to, microparticles, microbeads, magnetic beads, ion torrent beads, flow cytometry beads, beads or microspheres of any material, e.g. silica, gold, latex, polymers such as polystyrene, polysulfone and polyethyl, or hydrogel. The solid-phase substrate may also be an affinity purification column. Additional exemplary microparticles are encoded with the dyes and the antigens are immobilized to the encoded microparticles. The microparticles used in the methods of the invention are commercially available from sources such from Luminex Inc., Invitrogen (Carlsbad, Calif.), Polysciences Inc. (Warrington, Pa.) and Bangs Laboratories (Fishers, Ind.) to name a few.

[0125] In some embodiments, the solid-phase substrate is a microbead. The microbead, in some embodiments, has a diameter ranging from about 2 .mu.m to about 15 .mu.m, inclusive of each endpoint of the range. Microbeads having a diameter of about 2 .mu.m, 3 .mu.m, 4 .mu.m, 5 .mu.m, 6 .mu.m, 7 .mu.m, 8 .mu.m, 9 .mu.m, 10 .mu.m, 11 .mu.m, 12 .mu.m, 13 .mu.m, 14 .mu.m or 15 .mu.m are also contemplated.

[0126] The solid-phase substrates described herein may comprise a detectable label or another identifying characteristic. The solid-phase substrates may comprise a single fluorescent dye or multiple fluorescent dyes. In one embodiment, the microparticles are internally labeled with fluorescent dyes and contain surface carboxyl groups for covalent attachment of biomolecules. In another embodiment, the solid-phase substrates are internally labeled with fluorescent dyes and contain a surface layer of Avidin for near covalent binding of biotin and biotinylated ligands. In another embodiment, the solid-phase substrates may comprise a combination of different dyes, such as a fluorescent and a non-fluorescent dye. For example, the microparticles may be labeled with E)-5-[2-(methoxycarbonyl)ethenyl]cytidine, which is a nonfluorescent molecule, that when subjected to ultraviolet (UV) irradiation yields a single product, 3-?-D-ribofuranosyl-2,7-dioxopyrido[2,3-d]pyrimidine, which displays a strong fluorescence signal. In another embodiment, the solid-phase substrates may comprise bar codes as an identifiable characteristic as described in U.S. Patent Publication No. US 20070037195.

[0127] In another embodiment, the solid-phase substrate may be nanocrystals or quantum dots. These nanocrystals are substances that absorb photons of light, then re-emit photons at a different wavelength (fluorophores). In addition, additional florescent labels, or secondary antibodies may be conjugated to the nanocrystals. These nanocrystals are commercially available form sources such as Invitrogen and Evident Technologies (Troy, N.Y.),

[0128] The invention can be carried out with any system that detects the identifiable characteristic or label, such as FLOW cytometry. Detection of fluorescent labels may also be carried out using a microscope or camera that will read the image on the microparticles, such as the Bioarray BeadChip (Bioarray Solutions, Ltd., Warren, N.J.). The BeadChip format combines microparticle ("bead") chemistry with semiconductor wafer processing in which binding to the microparticle is recorded using an optical microscope and camera.

[0129] Biological samples for use in the methods described herein include, but are not limited to, whole blood, blood derivatives, red blood cell concentrates, plasma, serum, fresh frozen plasma, whole blood derived platelet concentrates, apheresis platelets, pooled platelets, intravenous gamma-globulin, cryoprecipitate, cerebrospinal fluid, tissues and cells such as epithelial cells, such as those collected from the buccal cavity, stem cells, leukocytes, neutrophils and granulocytes. The biological samples may be obtained from a human donor of tissue or cells intended for transplantation or a human donor of blood or blood derivatives intended for transfusion. The biological sample may be obtained from a healthy bone marrow donor or a subject of a paternity test. The biological sample may also be obtained from a human subject that is an intended recipient of a transplant or transfusion, or the human subject that is donating the tissue or organ intended for transplantation or transfusion. Alternatively, the biological sample may be obtained directly from tissues or cells that are intended for transplantation in a human recipient. In addition, the biological sample may be obtained from blood or blood derivatives that are intended for transfusion in a human recipient. In some embodiments, the sample is obtained before the subject has received the transplant or transfusion. In some embodiments, the sample is obtained after the subject has received the transplant or transfusion. In still further embodiments, the sample is obtained both before and after the subject has received the transplant or transfusion in order to monitor success of the transplant or transfusion.

[0130] Antibodies useful for detecting the antigens described herein may be polyclonal antibodies, monoclonal antibodies, antibody fragments which retain their ability to bind their unique epitope (e.g., Fv, Fab and F(ab).sub.2 fragments), single chain antibodies and human or humanized antibodies. Antibodies may be generated by techniques standard in the art using an antigenic HLA epitope. See, e.g. Kohler et al., Nature, 256:495-497 (1975), Brodeur et al., Monoclonal Antibody Production Techniques and Applications, pp. 51-63 (Marcel Dekker, Inc., New York, 1987). Antibody molecules of the present invention include the classes of IgG (as well as subtypes IgG 1, IgG 2a, and IgG2b), IgM, IgA, IgD, and IgE.

[0131] The antibodies of the invention may be labeled for detection of binding within the biological sample. The antibodies may comprise a radioactive label such as 3H, 14C, 32P, 35S, or 125I. In addition, the labels may be a fluorescent or chemiluminescent compound, such as fluorescein isothiocyanate, phycoerythrin, rhodamine, or luciferin. The labels may be enzymes such as alkaline phosphatase, .beta.-galactosidase, biotin and avidin or horseradish peroxidase (Bayer et al., Meth. Enz., 184:138-163 (1990)).

[0132] Specific binding of an antibody to an antigen described herein within a biological sample may be carried out using Western blot analysis with immunoblotting, immunocytochemistry, immunohistochemistry, dot blot analysis, flow cytometry, ELISA assays or RIA assays. These techniques and other approaches are conventional in the art (See Sambrook et al., Molecular Cloning: A Laboratory Manual, cold Springs Harbor Laboratories (New York, 1989).

Kits

[0133] The invention also provides for kits to carry out the methods of the invention. In particular, the invention provides for kit for determining the percentage of panel reactive antibodies in serum of a subject against HLA antigens comprising a first collection of solid-phase substrates wherein each solid-phase substrate is coated with different purified HLA antigens to represent the HLA antigen population of a single cell line such that said collection simulates the distribution of HLA antigens in a normal human population and a second collection of solid phase substrates wherein each substrate is coated with different purified non-HLA antigens listed in Table 1. The antigens provided in the kit may be conjugated to solid substrates in the kit. Alternatively, the kit comprises solid substrates and antigens and the skilled artisan can conjugate the antigens to the solid substrates allowing for optimization of the antigens used in the assay. The kits may also comprise the reagents necessary to detect and measure antibodies, such as HLA antibodies for use as a positive control.

[0134] In some embodiments, the HLA antigens comprise Class I HLA antigens (e.g., wherein the HLA antigens are selected such that the HLA antigens presented on the solid phase substrate comprise Class I HLA antigens so as to simulate the distribution of Class I HLA antigens in a normal human population). In some embodiments, the HLA antigens comprise Class II HLA antigens.

[0135] In some embodiments, the first collection comprises 54 different Class I HLA antigens, optionally purified from 30 different cell lines. In other embodiments, the first collection comprises 22 different Class II HLA antigens.

[0136] In some embodiments, the non-HLA antigens in the second collection are optionally a fusion protein comprising at least one domain, wherein the domain is a signal peptide, a modified cytoplasmic domain, purification tag or detection tag. In some embodiments, domain is the B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag.

[0137] The kits described herein may further comprise any components necessary to carry out the detection assays that are conventional in the art. For example, the kits may comprise buffers, loading dyes, gels such as polyacrylamide gels and molecular weight markers for preparing SDS-PAGE gels to carry out Western blots. The kits may also comprise filters, membranes blocking buffers, control buffers, isotype control antibodies, wash buffers or buffers and reagents for detection to carry out immunoblotting or dot blotting analysis such as labeled secondary antibodies. The kit may also comprise fixing reagents, blocking buffers, control buffers, wash buffers, staining dyes and detection reagents including anti-idiospecific antibodies. Furthermore, the kits may comprise the necessary reagents and tools to carryout flow cytometry, ELISA assays, RIA assays or microtoxicity assays.

[0138] Other aspects and advantages of the present invention will be understood upon consideration of the following illustrative examples.

EXAMPLES

Example 1

A Multiplex Assay on a Panel Consisting of 10 Non-HLA Antigens in One Single Test

[0139] Panel consists of 10 non-HLA were incubated with 4 different patient serum. Sera are used neat. The microbeads are subsequently washed with wash buffer comprising PBS with 0.1% polysorbate 20 (TWEEN) and incubated with goat anti-human IgG antibodies conjugated with phycocrythrin (PE) for 30 minutes. The microbeads were washed two times with wash buffer and analyzed on a Luminex analyzer according to the manufacturer's instructions.

[0140] Reaction pattern is compared. Four individuals (S 10823K, S11114A, S11143B and FL71681) showed distinct reaction patterns on 10 non-HLA antigens tested (FIG. 1).

Example 2

Trend Increase in Anti-non-HLA Allosera in a Lung Transplant Recipient During 1.sup.st Graft Rejection on a Panel Consisting of 58 Non-HLA Antigens in One Single Test

[0141] Panel consists of 58 non-HLA were incubated with 4 serum samples collected from different stage of graft rejection. Sera are used neat. The microbeads are subsequently washed with wash buffer comprising PBS with 0.1% polysorbate 20 (TWEEN) and incubated with goat anti-human IgG antibodies conjugated with phycocrythrin (PE) for 30 minutes. The microbeads were washed two times with wash buffer and analyzed on a Luminex analyzer according to the manufacturer's instructions.

[0142] Reaction pattern is compared on each individual non-HLA and analyzed against in a time course plot. Trend line is determined. Six non-HLA antigens show a correlation over the increasing anti-allosera activities with the graft rejection progression (FIG. 2).

Example 3

Increase of Anti-non-HLA Allosera in Transplant Recipients During Graft Rejection on a Panel Consisting of 21 Non-HLA Antigens in One Single Test

[0143] Panel consists of 21 non-HLA were incubated with serum samples collected from 13 graft recipients for graft post-transplant monitoring. Sera are collected on time course. Sera are used neat. The microbeads are subsequently washed with wash buffer comprising PBS with 0.1% polysorbate 20 (TWEEN) and incubated with goat anti-human IgG antibodies conjugated with phycocrythrin (PE) for 30 minutes. The microbeads were washed two times with wash buffer and analyzed on a Luminex analyzer according to the manufacturer's instructions.

[0144] Reaction pattern is compared on each individual non-HLA antigens and each individual graft recipient is analyzed against on a time course plot. Trend line on each non-HLA antigen over individual patient is determined. Six non-HLA antigens show a correlation over the increasing anti-allosera activities with the graft rejection progression among graft recipient monitored. See Table 2.

TABLE-US-00003 TABLE 2 % Patient shows positive increase of non-HLA allosera during post-translation non-HLA Antigen monitoring TubA1B 0.23 Perlican 0.69 PRKRIP1 0.31 EDNRA 0.23 FLRT2 0.38 Vimentin 0.15

Example 4

Increase Detection Sensitization by Fusion Tag in One Single Test

[0145] Enhancing antigenic polypeptide NusA-V5 binding on Luminex beads by a synthetic domain, DPD. The antigenic polypeptides NusA-V5 were fused to DPD. Mouse anti V5 antibody (1 .mu.g) are incubated with NusA polypeptides containing microbeads. The NusA polypeptides containing microbeads are subsequently washed with wash buffer comprising PBS with 0.1% polysorbate 20 (TWEEN) and incubated with goat anti-mouse IgG antibodies conjugated with phycocrythrin (PE) for 30 minutes. The microbeads were washed two times with wash buffer and analyzed on a Luminex analyzer according to the manufacturer's instruction.

[0146] The NusA-V5 fused with DPD tag shows higher sensitivity compared with no fusion (FIG. 3).

Example 5

Box and Whiskers' Plot of Non-HLA Antigens from Two Patient Population Using a Panel of 21 Non-HLA Antigens in One Test

[0147] Panel consists of 21 non-HLA were incubated with serum samples collected from graft recipients before and after transplant for graft post-transplant monitoring. Sera are collect and used neat. The microbeads are subsequently washed with wash buffer comprising PBS with 0.1% polysorbate 20 (TWEEN) and incubated with goat anti-human IgG antibodies conjugated with phycocrythrin (PE) for 30 minutes. The microbeads were washed two times with wash buffer and analyzed on a Luminex analyzer according to the manufacturer's instructions.

[0148] Serum anti non-HLA alloantibodies activities are determined for 45 post-transplant allograft patients and 33 pre-transplant allograft patients. The median (line) and IQR (box top and bottom) values are shown with a Mann-Whitney Rank Sum test providing a p-value listed in the box. Three non-HLA antigens show a significance increase of de novo alloantibodies (FIG. 4).

Example 6

Antibodies to Non-HLA Antigens have been Identified in Kidney Allograft Patients

[0149] Anti-vimentin IgG and IgM which target at the non-HLA antigen vimentin has been identified in a chronic kidney transplant patient under post-transplant monitoring. In addition, high titer of HLA IgM antibodies was observed (Table 3)

TABLE-US-00004 TABLE 3 Large scale monitoring of both nHLA and non-HLA antigens Signals Monitoring Vimentin HLA time IgG IgM IgG IgM beginning 708 2910 175 340 1 month 699 3579 172 204 1 year 1281 4537 141 367 1.5 year 1080 7256 139 1025

Example 7

[0150] According to this example, Class I HLA antigen preparations were purified from Epstein Barr virus transformed lymphocyte cell lines according to the methods of Henderson et al., Virology 76: 152-163 (1977). Thirty of the Class I HLA antigen preparations were then selected to simulate the distribution of HLA in a normal population as set out in Table 4 and were coated by passive absorption onto 3 .mu.m latex beads obtained from Spherotech according to the method of Cantarero et al., Anal. Biochem., 105: 373-382 (1980).

TABLE-US-00005 TABLE 4 Bead No. HLA CLASS I Antigen Typing 1 A11 B27, 48 2 A2, 29 B39, 56 3 A1, 29 B8, 45 4 A2, 24 B7, 55 5 A2, 25 B18, 64 6 A26, 24 B52, 62 7 A31, 68 B53 8 A2, 11 B13, 62 9 A23, 33 B45, 63 10 A23, 34 B44 11 A11, 23 B49, 52 12 A11, 24 B59, 60 13 A24, 33 B44, 51 14 A23, 26 B41, 72 15 A3, 32 B50, 56 16 A2, 24 B54, 67 17 A2 B52, 73 18 A26, 66 B38, 75 19 A11, 33 B51, 54 20 A30 B13, 72 21 A30, 36 B35, 71 22 A69 B35, 61 23 A1, 32 B60, 64 24 A2 B7, 46 25 A30 B42 26 A2 B8, 58 27 A2, 3 B58, 65 28 A1, 36 B37, 57 29 A3, 68 B7, 65 30 A33, 36 B53, 61

[0151] The reactivity of the HLA antigen on each bead was confirmed by a panel of serologically defined HLA monoclonal antibodies or by human allosera using a flow cytometry test. Each bead reacted specifically to the HLA monoclonal antibodies or allosera with the same HLA specificity.

[0152] The sensitivity of the beads was tested by mixing two beads with different typing at different percentages. A minimum of 2 to 3% of one kind of bead was found to be sufficient to detect the antigen.

Example 8

[0153] According to this example, the sensitivity of the microbeads useful with the invention was tested by carrying out a serial dilution of selected PRA sera. The results presented in Table 5 below show that most PRA sera decrease the percentage of reactivity at a 1:10 dilution measured by a cytotoxicity test while they did not decrease the percentage of reactivity at a 1:40 dilution by use of the microbeads in a flow cytometry device according to the invention.

TABLE-US-00006 TABLE 5 Percentage Flow Sera ID Dilution Cytotoxicity Cytometry N21 1 40 -- 1:10 10 41 1:20 0 30 1:40 0 41 1:50 0 18 1:160 0 16 A2 1 30 1:20 0 25 1:40 0 26 1:80 0 8 S193 1 25 1:10 31 28 1:20 17 100 1:40 10 100 1:80 0 100 S176 1 54 1:10 24 40 1:20 28 41 1:40 10 40 1:50 0 40 S199 1 100 1:10 10 97 1:20 3 97 1:40 10 97 1:50 3 99 B73 1 65 1:10 27 54 1:20 3 40 1:40 3 43 1:50 0 25

Example 9

[0154] According to this example, an assay to detect panel reactive antibodies was carried out by mixing 10 .mu.l of a mixture of the 30 different types of beads produced according to Example 7 with 100 .mu.l (1:10 diluted) serum to be tested and incubating for 30 minutes at 20-25.degree. C. with gentle rotating. The beads were then washed three times with 1 mL of wash buffer. The beads were then incubated with 100 .mu.l of 1:100 diluted Goat anti-human IgG-PE obtained from Jackson InnumoResearch for 30 minutes. The beads were then washed twice and 1 mL of wash buffer and read on a flow cytometer (B.D. FacStar Plus). The percentage of PRA is represented by the percentage of microbeads which are positively labeled.

[0155] According to this example, 61 sera samples including 22 negative and 39 PRA patients who had panel reactive antibody activities developed by earlier transplantation or transfusion were tested with the results shown in FIG. 6 which shows the correlation of the flow cytometry results with those where the same samples were tested by complement-dependent lymphocytotoxicity. The correlation coefficient R is 0.94 for the 61 data points indicating a high degree of correlation between results obtained by flow cytometry and those obtained by a cytotoxicity test.

Example 10

[0156] According to this example, 30 Class II HLA antigen preparations as set out in Table 5 were purified from Epstein Barr virus transformed lymphocyte cell lines according to the methods of Henderson et al., Virology 76: 152-163 (1977). The antigen preparations may then be coated by passive absorption onto 5 .mu.m latex beads obtained from Spherotech according to the method of Cantarero et al., Anal. Biochem., 105: 373-382 (1980). From this collection of Class II HLA preparations, from 15 to 30 beads may selected to simulate the distribution of the 22 Class II HLA antigens in a normal population.

TABLE-US-00007 TABLE 5 Bead No. HLA CLASS II Antigen Typing Typing 1 DR15, 9 53, 51 DQ5, 9 2 DR4, 15 53, 51 DQ6, 7 3 DR16, 4 53, 51 DQ4, 5 4 DR8, 14 52 DQ4, 5 5 DR4, 7 53 DQ2, 8 6 DR15, 18 51, 52 DQ6, 4 7 DR11, 12 52 DQ5, 7 8 DR103, 17 52 DQ5, 2 9 DR1, 13 52 DQ5, 6 10 DR9, 10 53 DQ5, 9 11 DR15, 12 51, 52 DQ5, 7 12 DR16, 14 51, 52 DQ5 13 DR13, 8 52 DQ5, 6 14 DR11, 13 52 DQ5, 6 15 DR17, 7 52, 53 DQ2, 9 16 DR15, 8 51 DQ6, 8 17 DR15, 4 51, 53 DQ2, 6 18 DR15, 17 51, 52 DQ6, 2 19 DR15, 7 51, 53 DQ6, 2 20 DR1, 7 53 DQ2, 5 21 DR15, 11 52 DQ5, 6 22 DR7, 13 52, 53 DQ6, 9 23 DR15, 13 51, 52 DQ6, 2 24 DR9, 14 52, 53 DQ5, 9 25 DR8, 9 53 DQ2, 7 26 DR17, 14 52 DQ2, 5 27 DR1, 11 52 DQ5, 6 28 DR17, 4 52, 53 DQ2 29 DR11, 4 52, 53 DQ7, 8 30 DR1, 14 52 DQ5

Example 11

[0157] According to this example, 3 .mu.m latex beads presenting HLA Class I antigens produced according to the methods of Example 7 and 5 .mu..m latex beads presenting HLA Class II antigens produced according to the methods of Example 9 were mixed to perform an assay to detect the presence of antibodies specific to HLA Class I and Class II antigens. Because the beads presenting HLA Class II antigens are different in size from the HLA Class I beads, the two different sized beads can be electronically distinguished according to their sizes when analyzed on a flow cytometer as illustrated in FIGS. 7A-7D. FIGS. 7A-7D depict the reaction of the mixture of Class I and Class II beads and their reaction to anti-HLA Class I antibodies (FIGS. 7A and 7B) or anti-HLA Class II antibodies (FIGS. 7C and 7D). When the Class I beads are selected by gating around the 3 .mu.m size, the beads react to the anti-Class I antibody as illustrated in FIG. 7A. When the Class II beads are selected by gating around the 5 .mu.m size, there is no reaction to the anti-Class I antibody as illustrated in FIG. 7B. The reaction pattern of the mixed beads to the anti-class II antibody is the reverse. When Class I beads are selected by gating around 3 .mu.m in size, the beads do not react to the anti-Class II antibody as illustrated in FIG. 7C. When Class II antibodies are selected by gating around 5 .mu.m in size, the Class II antigen beads react to the anti-Class II antibody as illustrated in FIG. 7D.

[0158] Numerous modifications and variations in the practice of the invention are expected to occur to those skilled in the art upon consideration of the foregoing description on the presently preferred embodiments thereof. Consequently, the only limitations which should be placed upon the scope of the present invention are those that appear in the appended claims.

Sequence CWU 1 SEQUENCE LISTING <160> NUMBER OF SEQ ID NOS: 74 <210> SEQ ID NO 1 <211> LENGTH: 2067 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O00468 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(2067) <400> SEQUENCE: 1 Met Ala Gly Arg Ser His Pro Gly Pro Leu Arg Pro Leu Leu Pro Leu 1 5 10 15 Leu Val Val Ala Ala Cys Val Leu Pro Gly Ala Gly Gly Thr Cys Pro 20 25 30 Glu Arg Ala Leu Glu Arg Arg Glu Glu Glu Ala Asn Val Val Leu Thr 35 40 45 Gly Thr Val Glu Glu Ile Leu Asn Val Asp Pro Val Gln His Thr Tyr 50 55 60 Ser Cys Lys Val Arg Val Trp Arg Tyr Leu Lys Gly Lys Asp Leu Val 65 70 75 80 Ala Arg Glu Ser Leu Leu Asp Gly Gly Asn Lys Val Val Ile Ser Gly 85 90 95 Phe Gly Asp Pro Leu Ile Cys Asp Asn Gln Val Ser Thr Gly Asp Thr 100 105 110 Arg Ile Phe Phe Val Asn Pro Ala Pro Pro Tyr Leu Trp Pro Ala His 115 120 125 Lys Asn Glu Leu Met Leu Asn Ser Ser Leu Met Arg Ile Thr Leu Arg 130 135 140 Asn Leu Glu Glu Val Glu Phe Cys Val Glu Asp Lys Pro Gly Thr His 145 150 155 160 Phe Thr Pro Val Pro Pro Thr Pro Pro Asp Ala Cys Arg Gly Met Leu 165 170 175 Cys Gly Phe Gly Ala Val Cys Glu Pro Asn Ala Glu Gly Pro Gly Arg 180 185 190 Ala Ser Cys Val Cys Lys Lys Ser Pro Cys Pro Ser Val Val Ala Pro 195 200 205 Val Cys Gly Ser Asp Ala Ser Thr Tyr Ser Asn Glu Cys Glu Leu Gln 210 215 220 Arg Ala Gln Cys Ser Gln Gln Arg Arg Ile Arg Leu Leu Ser Arg Gly 225 230 235 240 Pro Cys Gly Ser Arg Asp Pro Cys Ser Asn Val Thr Cys Ser Phe Gly 245 250 255 Ser Thr Cys Ala Arg Ser Ala Asp Gly Leu Thr Ala Ser Cys Leu Cys 260 265 270 Pro Ala Thr Cys Arg Gly Ala Pro Glu Gly Thr Val Cys Gly Ser Asp 275 280 285 Gly Ala Asp Tyr Pro Gly Glu Cys Gln Leu Leu Arg Arg Ala Cys Ala 290 295 300 Arg Gln Glu Asn Val Phe Lys Lys Phe Asp Gly Pro Cys Asp Pro Cys 305 310 315 320 Gln Gly Ala Leu Pro Asp Pro Ser Arg Ser Cys Arg Val Asn Pro Arg 325 330 335 Thr Arg Arg Pro Glu Met Leu Leu Arg Pro Glu Ser Cys Pro Ala Arg 340 345 350 Gln Ala Pro Val Cys Gly Asp Asp Gly Val Thr Tyr Glu Asn Asp Cys 355 360 365 Val Met Gly Arg Ser Gly Ala Ala Arg Gly Leu Leu Leu Gln Lys Val 370 375 380 Arg Ser Gly Gln Cys Gln Gly Arg Asp Gln Cys Pro Glu Pro Cys Arg 385 390 395 400 Phe Asn Ala Val Cys Leu Ser Arg Arg Gly Arg Pro Arg Cys Ser Cys 405 410 415 Asp Arg Val Thr Cys Asp Gly Ala Tyr Arg Pro Val Cys Ala Gln Asp 420 425 430 Gly Arg Thr Tyr Asp Ser Asp Cys Trp Arg Gln Gln Ala Glu Cys Arg 435 440 445 Gln Gln Arg Ala Ile Pro Ser Lys His Gln Gly Pro Cys Asp Gln Ala 450 455 460 Pro Ser Pro Cys Leu Gly Val Gln Cys Ala Phe Gly Ala Thr Cys Ala 465 470 475 480 Val Lys Asn Gly Gln Ala Ala Cys Glu Cys Leu Gln Ala Cys Ser Ser 485 490 495 Leu Tyr Asp Pro Val Cys Gly Ser Asp Gly Val Thr Tyr Gly Ser Ala 500 505 510 Cys Glu Leu Glu Ala Thr Ala Cys Thr Leu Gly Arg Glu Ile Gln Val 515 520 525 Ala Arg Lys Gly Pro Cys Asp Arg Cys Gly Gln Cys Arg Phe Gly Ala 530 535 540 Leu Cys Glu Ala Glu Thr Gly Arg Cys Val Cys Pro Ser Glu Cys Val 545 550 555 560 Ala Leu Ala Gln Pro Val Cys Gly Ser Asp Gly His Thr Tyr Pro Ser 565 570 575 Glu Cys Met Leu His Val His Ala Cys Thr His Gln Ile Ser Leu His 580 585 590 Val Ala Ser Ala Gly Pro Cys Glu Thr Cys Gly Asp Ala Val Cys Ala 595 600 605 Phe Gly Ala Val Cys Ser Ala Gly Gln Cys Val Cys Pro Arg Cys Glu 610 615 620 His Pro Pro Pro Gly Pro Val Cys Gly Ser Asp Gly Val Thr Tyr Gly 625 630 635 640 Ser Ala Cys Glu Leu Arg Glu Ala Ala Cys Leu Gln Gln Thr Gln Ile 645 650 655 Glu Glu Ala Arg Ala Gly Pro Cys Glu Gln Ala Glu Cys Gly Ser Gly 660 665 670 Gly Ser Gly Ser Gly Glu Asp Gly Asp Cys Glu Gln Glu Leu Cys Arg 675 680 685 Gln Arg Gly Gly Ile Trp Asp Glu Asp Ser Glu Asp Gly Pro Cys Val 690 695 700 Cys Asp Phe Ser Cys Gln Ser Val Pro Gly Ser Pro Val Cys Gly Ser 705 710 715 720 Asp Gly Val Thr Tyr Ser Thr Glu Cys Glu Leu Lys Lys Ala Arg Cys 725 730 735 Glu Ser Gln Arg Gly Leu Tyr Val Ala Ala Gln Gly Ala Cys Arg Gly 740 745 750 Pro Thr Phe Ala Pro Leu Pro Pro Val Ala Pro Leu His Cys Ala Gln 755 760 765 Thr Pro Tyr Gly Cys Cys Gln Asp Asn Ile Thr Ala Ala Arg Gly Val 770 775 780 Gly Leu Ala Gly Cys Pro Ser Ala Cys Gln Cys Asn Pro His Gly Ser 785 790 795 800 Tyr Gly Gly Thr Cys Asp Pro Ala Thr Gly Gln Cys Ser Cys Arg Pro 805 810 815 Gly Val Gly Gly Leu Arg Cys Asp Arg Cys Glu Pro Gly Phe Trp Asn 820 825 830 Phe Arg Gly Ile Val Thr Asp Gly Arg Ser Gly Cys Thr Pro Cys Ser 835 840 845 Cys Asp Pro Gln Gly Ala Val Arg Asp Asp Cys Glu Gln Met Thr Gly 850 855 860 Leu Cys Ser Cys Lys Pro Gly Val Ala Gly Pro Lys Cys Gly Gln Cys 865 870 875 880 Pro Asp Gly Arg Ala Leu Gly Pro Ala Gly Cys Glu Ala Asp Ala Ser 885 890 895 Ala Pro Ala Thr Cys Ala Glu Met Arg Cys Glu Phe Gly Ala Arg Cys 900 905 910 Val Glu Glu Ser Gly Ser Ala His Cys Val Cys Pro Met Leu Thr Cys 915 920 925 Pro Glu Ala Asn Ala Thr Lys Val Cys Gly Ser Asp Gly Val Thr Tyr 930 935 940 Gly Asn Glu Cys Gln Leu Lys Thr Ile Ala Cys Arg Gln Gly Leu Gln 945 950 955 960 Ile Ser Ile Gln Ser Leu Gly Pro Cys Gln Glu Ala Val Ala Pro Ser 965 970 975 Thr His Pro Thr Ser Ala Ser Val Thr Val Thr Thr Pro Gly Leu Leu 980 985 990 Leu Ser Gln Ala Leu Pro Ala Pro Pro Gly Ala Leu Pro Leu Ala Pro 995 1000 1005 Ser Ser Thr Ala His Ser Gln Thr Thr Pro Pro Pro Ser Ser Arg 1010 1015 1020 Pro Arg Thr Thr Ala Ser Val Pro Arg Thr Thr Val Trp Pro Val 1025 1030 1035 Leu Thr Val Pro Pro Thr Ala Pro Ser Pro Ala Pro Ser Leu Val 1040 1045 1050 Ala Ser Ala Phe Gly Glu Ser Gly Ser Thr Asp Gly Ser Ser Asp 1055 1060 1065 Glu Glu Leu Ser Gly Asp Gln Glu Ala Ser Gly Gly Gly Ser Gly 1070 1075 1080 Gly Leu Glu Pro Leu Glu Gly Ser Ser Val Ala Thr Pro Gly Pro 1085 1090 1095 Pro Val Glu Arg Ala Ser Cys Tyr Asn Ser Ala Leu Gly Cys Cys 1100 1105 1110 Ser Asp Gly Lys Thr Pro Ser Leu Asp Ala Glu Gly Ser Asn Cys 1115 1120 1125 Pro Ala Thr Lys Val Phe Gln Gly Val Leu Glu Leu Glu Gly Val 1130 1135 1140 Glu Gly Gln Glu Leu Phe Tyr Thr Pro Glu Met Ala Asp Pro Lys 1145 1150 1155 Ser Glu Leu Phe Gly Glu Thr Ala Arg Ser Ile Glu Ser Thr Leu 1160 1165 1170 Asp Asp Leu Phe Arg Asn Ser Asp Val Lys Lys Asp Phe Arg Ser 1175 1180 1185 Val Arg Leu Arg Asp Leu Gly Pro Gly Lys Ser Val Arg Ala Ile 1190 1195 1200 Val Asp Val His Phe Asp Pro Thr Thr Ala Phe Arg Ala Pro Asp 1205 1210 1215 Val Ala Arg Ala Leu Leu Arg Gln Ile Gln Val Ser Arg Arg Arg 1220 1225 1230 Ser Leu Gly Val Arg Arg Pro Leu Gln Glu His Val Arg Phe Met 1235 1240 1245 Asp Phe Asp Trp Phe Pro Ala Phe Ile Thr Gly Ala Thr Ser Gly 1250 1255 1260 Ala Ile Ala Ala Gly Ala Thr Ala Arg Ala Thr Thr Ala Ser Arg 1265 1270 1275 Leu Pro Ser Ser Ala Val Thr Pro Arg Ala Pro His Pro Ser His 1280 1285 1290 Thr Ser Gln Pro Val Ala Lys Thr Thr Ala Ala Pro Thr Thr Arg 1295 1300 1305 Arg Pro Pro Thr Thr Ala Pro Ser Arg Val Pro Gly Arg Arg Pro 1310 1315 1320 Pro Ala Pro Gln Gln Pro Pro Lys Pro Cys Asp Ser Gln Pro Cys 1325 1330 1335 Phe His Gly Gly Thr Cys Gln Asp Trp Ala Leu Gly Gly Gly Phe 1340 1345 1350 Thr Cys Ser Cys Pro Ala Gly Arg Gly Gly Ala Val Cys Glu Lys 1355 1360 1365 Val Leu Gly Ala Pro Val Pro Ala Phe Glu Gly Arg Ser Phe Leu 1370 1375 1380 Ala Phe Pro Thr Leu Arg Ala Tyr His Thr Leu Arg Leu Ala Leu 1385 1390 1395 Glu Phe Arg Ala Leu Glu Pro Gln Gly Leu Leu Leu Tyr Asn Gly 1400 1405 1410 Asn Ala Arg Gly Lys Asp Phe Leu Ala Leu Ala Leu Leu Asp Gly 1415 1420 1425 Arg Val Gln Leu Arg Phe Asp Thr Gly Ser Gly Pro Ala Val Leu 1430 1435 1440 Thr Ser Ala Val Pro Val Glu Pro Gly Gln Trp His Arg Leu Glu 1445 1450 1455 Leu Ser Arg His Trp Arg Arg Gly Thr Leu Ser Val Asp Gly Glu 1460 1465 1470 Thr Pro Val Leu Gly Glu Ser Pro Ser Gly Thr Asp Gly Leu Asn 1475 1480 1485 Leu Asp Thr Asp Leu Phe Val Gly Gly Val Pro Glu Asp Gln Ala 1490 1495 1500 Ala Val Ala Leu Glu Arg Thr Phe Val Gly Ala Gly Leu Arg Gly 1505 1510 1515 Cys Ile Arg Leu Leu Asp Val Asn Asn Gln Arg Leu Glu Leu Gly 1520 1525 1530 Ile Gly Pro Gly Ala Ala Thr Arg Gly Ser Gly Val Gly Glu Cys 1535 1540 1545 Gly Asp His Pro Cys Leu Pro Asn Pro Cys His Gly Gly Ala Pro 1550 1555 1560 Cys Gln Asn Leu Glu Ala Gly Arg Phe His Cys Gln Cys Pro Pro 1565 1570 1575 Gly Arg Val Gly Pro Thr Cys Ala Asp Glu Lys Ser Pro Cys Gln 1580 1585 1590 Pro Asn Pro Cys His Gly Ala Ala Pro Cys Arg Val Leu Pro Glu 1595 1600 1605 Gly Gly Ala Gln Cys Glu Cys Pro Leu Gly Arg Glu Gly Thr Phe 1610 1615 1620 Cys Gln Thr Ala Ser Gly Gln Asp Gly Ser Gly Pro Phe Leu Ala 1625 1630 1635 Asp Phe Asn Gly Phe Ser His Leu Glu Leu Arg Gly Leu His Thr 1640 1645 1650 Phe Ala Arg Asp Leu Gly Glu Lys Met Ala Leu Glu Val Val Phe 1655 1660 1665 Leu Ala Arg Gly Pro Ser Gly Leu Leu Leu Tyr Asn Gly Gln Lys 1670 1675 1680 Thr Asp Gly Lys Gly Asp Phe Val Ser Leu Ala Leu Arg Asp Arg 1685 1690 1695 Arg Leu Glu Phe Arg Tyr Asp Leu Gly Lys Gly Ala Ala Val Ile 1700 1705 1710 Arg Ser Arg Glu Pro Val Thr Leu Gly Ala Trp Thr Arg Val Ser 1715 1720 1725 Leu Glu Arg Asn Gly Arg Lys Gly Ala Leu Arg Val Gly Asp Gly 1730 1735 1740 Pro Arg Val Leu Gly Glu Ser Pro Lys Ser Arg Lys Val Pro His 1745 1750 1755 Thr Val Leu Asn Leu Lys Glu Pro Leu Tyr Val Gly Gly Ala Pro 1760 1765 1770 Asp Phe Ser Lys Leu Ala Arg Ala Ala Ala Val Ser Ser Gly Phe 1775 1780 1785 Asp Gly Ala Ile Gln Leu Val Ser Leu Gly Gly Arg Gln Leu Leu 1790 1795 1800 Thr Pro Glu His Val Leu Arg Gln Val Asp Val Thr Ser Phe Ala 1805 1810 1815 Gly His Pro Cys Thr Arg Ala Ser Gly His Pro Cys Leu Asn Gly 1820 1825 1830 Ala Ser Cys Val Pro Arg Glu Ala Ala Tyr Val Cys Leu Cys Pro 1835 1840 1845 Gly Gly Phe Ser Gly Pro His Cys Glu Lys Gly Leu Val Glu Lys 1850 1855 1860 Ser Ala Gly Asp Val Asp Thr Leu Ala Phe Asp Gly Arg Thr Phe 1865 1870 1875 Val Glu Tyr Leu Asn Ala Val Thr Glu Ser Glu Leu Ala Asn Glu 1880 1885 1890 Ile Pro Val Pro Glu Thr Leu Asp Ser Gly Ala Leu His Glu Lys 1895 1900 1905 Ala Leu Gln Ser Asn His Phe Glu Leu Ser Leu Arg Thr Glu Ala 1910 1915 1920 Thr Gln Gly Leu Val Leu Trp Ser Gly Lys Ala Thr Glu Arg Ala 1925 1930 1935 Asp Tyr Val Ala Leu Ala Ile Val Asp Gly His Leu Gln Leu Ser 1940 1945 1950 Tyr Asn Leu Gly Ser Gln Pro Val Val Leu Arg Ser Thr Val Pro 1955 1960 1965 Val Asn Thr Asn Arg Trp Leu Arg Val Val Ala His Arg Glu Gln 1970 1975 1980 Arg Glu Gly Ser Leu Gln Val Gly Asn Glu Ala Pro Val Thr Gly 1985 1990 1995 Ser Ser Pro Leu Gly Ala Thr Gln Leu Asp Thr Asp Gly Ala Leu 2000 2005 2010 Trp Leu Gly Gly Leu Pro Glu Leu Pro Val Gly Pro Ala Leu Pro 2015 2020 2025 Lys Ala Tyr Gly Thr Gly Phe Val Gly Cys Leu Arg Asp Val Val 2030 2035 2040 Val Gly Arg His Pro Leu His Leu Leu Glu Asp Ala Val Thr Lys 2045 2050 2055 Pro Glu Leu Arg Pro Cys Pro Thr Pro 2060 2065 <210> SEQ ID NO 2 <211> LENGTH: 485 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01019 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(485) <400> SEQUENCE: 2 Met Arg Lys Arg Ala Pro Gln Ser Glu Met Ala Pro Ala Gly Val Ser 1 5 10 15 Leu Arg Ala Thr Ile Leu Cys Leu Leu Ala Trp Ala Gly Leu Ala Ala 20 25 30 Gly Asp Arg Val Tyr Ile His Pro Phe His Leu Val Ile His Asn Glu 35 40 45 Ser Thr Cys Glu Gln Leu Ala Lys Ala Asn Ala Gly Lys Pro Lys Asp 50 55 60 Pro Thr Phe Ile Pro Ala Pro Ile Gln Ala Lys Thr Ser Pro Val Asp 65 70 75 80 Glu Lys Ala Leu Gln Asp Gln Leu Val Leu Val Ala Ala Lys Leu Asp 85 90 95 Thr Glu Asp Lys Leu Arg Ala Ala Met Val Gly Met Leu Ala Asn Phe 100 105 110 Leu Gly Phe Arg Ile Tyr Gly Met His Ser Glu Leu Trp Gly Val Val 115 120 125 His Gly Ala Thr Val Leu Ser Pro Thr Ala Val Phe Gly Thr Leu Ala 130 135 140 Ser Leu Tyr Leu Gly Ala Leu Asp His Thr Ala Asp Arg Leu Gln Ala 145 150 155 160 Ile Leu Gly Val Pro Trp Lys Asp Lys Asn Cys Thr Ser Arg Leu Asp 165 170 175 Ala His Lys Val Leu Ser Ala Leu Gln Ala Val Gln Gly Leu Leu Val 180 185 190 Ala Gln Gly Arg Ala Asp Ser Gln Ala Gln Leu Leu Leu Ser Thr Val 195 200 205 Val Gly Val Phe Thr Ala Pro Gly Leu His Leu Lys Gln Pro Phe Val 210 215 220 Gln Gly Leu Ala Leu Tyr Thr Pro Val Val Leu Pro Arg Ser Leu Asp 225 230 235 240 Phe Thr Glu Leu Asp Val Ala Ala Glu Lys Ile Asp Arg Phe Met Gln 245 250 255 Ala Val Thr Gly Trp Lys Thr Gly Cys Ser Leu Met Gly Ala Ser Val 260 265 270 Asp Ser Thr Leu Ala Phe Asn Thr Tyr Val His Phe Gln Gly Lys Met 275 280 285 Lys Gly Phe Ser Leu Leu Ala Glu Pro Gln Glu Phe Trp Val Asp Asn 290 295 300 Ser Thr Ser Val Ser Val Pro Met Leu Ser Gly Met Gly Thr Phe Gln 305 310 315 320 His Trp Ser Asp Ile Gln Asp Asn Phe Ser Val Thr Gln Val Pro Phe 325 330 335 Thr Glu Ser Ala Cys Leu Leu Leu Ile Gln Pro His Tyr Ala Ser Asp 340 345 350 Leu Asp Lys Val Glu Gly Leu Thr Phe Gln Gln Asn Ser Leu Asn Trp 355 360 365 Met Lys Lys Leu Ser Pro Arg Thr Ile His Leu Thr Met Pro Gln Leu 370 375 380 Val Leu Gln Gly Ser Tyr Asp Leu Gln Asp Leu Leu Ala Gln Ala Glu 385 390 395 400 Leu Pro Ala Ile Leu His Thr Glu Leu Asn Leu Gln Lys Leu Ser Asn 405 410 415 Asp Arg Ile Arg Val Gly Glu Val Leu Asn Ser Ile Phe Phe Glu Leu 420 425 430 Glu Ala Asp Glu Arg Glu Pro Thr Glu Ser Thr Gln Gln Leu Asn Lys 435 440 445 Pro Glu Val Leu Glu Val Thr Leu Asn Arg Pro Phe Leu Phe Ala Val 450 455 460 Tyr Asp Gln Ser Ala Thr Ala Leu His Phe Leu Gly Arg Val Ala Asn 465 470 475 480 Pro Leu Ser Thr Ala 485 <210> SEQ ID NO 3 <211> LENGTH: 201 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P52566 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(201) <400> SEQUENCE: 3 Met Thr Glu Lys Ala Pro Glu Pro His Val Glu Glu Asp Asp Asp Asp 1 5 10 15 Glu Leu Asp Ser Lys Leu Asn Tyr Lys Pro Pro Pro Gln Lys Ser Leu 20 25 30 Lys Glu Leu Gln Glu Met Asp Lys Asp Asp Glu Ser Leu Ile Lys Tyr 35 40 45 Lys Lys Thr Leu Leu Gly Asp Gly Pro Val Val Thr Asp Pro Lys Ala 50 55 60 Pro Asn Val Val Val Thr Arg Leu Thr Leu Val Cys Glu Ser Ala Pro 65 70 75 80 Gly Pro Ile Thr Met Asp Leu Thr Gly Asp Leu Glu Ala Leu Lys Lys 85 90 95 Glu Thr Ile Val Leu Lys Glu Gly Ser Glu Tyr Arg Val Lys Ile His 100 105 110 Phe Lys Val Asn Arg Asp Ile Val Ser Gly Leu Lys Tyr Val Gln His 115 120 125 Thr Tyr Arg Thr Gly Val Lys Val Asp Lys Ala Thr Phe Met Val Gly 130 135 140 Ser Tyr Gly Pro Arg Pro Glu Glu Tyr Glu Phe Leu Thr Pro Val Glu 145 150 155 160 Glu Ala Pro Lys Gly Met Leu Ala Arg Gly Thr Tyr His Asn Lys Ser 165 170 175 Phe Phe Thr Asp Asp Asp Lys Gln Asp His Leu Ser Trp Glu Trp Asn 180 185 190 Leu Ser Ile Lys Lys Glu Trp Thr Glu 195 200 <210> SEQ ID NO 4 <211> LENGTH: 199 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9NWT8 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(199) <400> SEQUENCE: 4 Met Leu Leu Gly Arg Leu Thr Ser Gln Leu Leu Arg Ala Val Pro Trp 1 5 10 15 Ala Gly Gly Arg Pro Pro Trp Pro Val Ser Gly Val Leu Gly Ser Arg 20 25 30 Val Cys Gly Pro Leu Tyr Ser Thr Ser Pro Ala Gly Pro Gly Arg Ala 35 40 45 Ala Ser Leu Pro Arg Lys Gly Ala Gln Leu Glu Leu Glu Glu Met Leu 50 55 60 Val Pro Arg Lys Met Ser Val Ser Pro Leu Glu Ser Trp Leu Thr Ala 65 70 75 80 Arg Cys Phe Leu Pro Arg Leu Asp Thr Gly Thr Ala Gly Thr Val Ala 85 90 95 Pro Pro Gln Ser Tyr Gln Cys Pro Pro Ser Gln Ile Gly Glu Gly Ala 100 105 110 Glu Gln Gly Asp Glu Gly Val Ala Asp Ala Pro Gln Ile Gln Cys Lys 115 120 125 Asn Val Leu Lys Ile Arg Arg Arg Lys Met Asn His His Lys Tyr Arg 130 135 140 Lys Leu Val Lys Lys Thr Arg Phe Leu Arg Arg Lys Val Gln Glu Gly 145 150 155 160 Arg Leu Arg Arg Lys Gln Ile Lys Phe Glu Lys Asp Leu Arg Arg Ile 165 170 175 Trp Leu Lys Ala Gly Leu Lys Glu Ala Pro Glu Gly Trp Gln Thr Pro 180 185 190 Lys Ile Tyr Leu Arg Gly Lys 195 <210> SEQ ID NO 5 <211> LENGTH: 1744 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P0C0L5 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1744) <400> SEQUENCE: 5 Met Arg Leu Leu Trp Gly Leu Ile Trp Ala Ser Ser Phe Phe Thr Leu 1 5 10 15 Ser Leu Gln Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His 20 25 30 Leu Gly Val Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg 35 40 45 Gly Gln Val Val Lys Gly Ser Val Phe Leu Arg Asn Pro Ser Arg Asn 50 55 60 Asn Val Pro Cys Ser Pro Lys Val Asp Phe Thr Leu Ser Ser Glu Arg 65 70 75 80 Asp Phe Ala Leu Leu Ser Leu Gln Val Pro Leu Lys Asp Ala Lys Ser 85 90 95 Cys Gly Leu His Gln Leu Leu Arg Gly Pro Glu Val Gln Leu Val Ala 100 105 110 His Ser Pro Trp Leu Lys Asp Ser Leu Ser Arg Thr Thr Asn Ile Gln 115 120 125 Gly Ile Asn Leu Leu Phe Ser Ser Arg Arg Gly His Leu Phe Leu Gln 130 135 140 Thr Asp Gln Pro Ile Tyr Asn Pro Gly Gln Arg Val Arg Tyr Arg Val 145 150 155 160 Phe Ala Leu Asp Gln Lys Met Arg Pro Ser Thr Asp Thr Ile Thr Val 165 170 175 Met Val Glu Asn Ser His Gly Leu Arg Val Arg Lys Lys Glu Val Tyr 180 185 190 Met Pro Ser Ser Ile Phe Gln Asp Asp Phe Val Ile Pro Asp Ile Ser 195 200 205 Glu Pro Gly Thr Trp Lys Ile Ser Ala Arg Phe Ser Asp Gly Leu Glu 210 215 220 Ser Asn Ser Ser Thr Gln Phe Glu Val Lys Lys Tyr Val Leu Pro Asn 225 230 235 240 Phe Glu Val Lys Ile Thr Pro Gly Lys Pro Tyr Ile Leu Thr Val Pro 245 250 255 Gly His Leu Asp Glu Met Gln Leu Asp Ile Gln Ala Arg Tyr Ile Tyr 260 265 270 Gly Lys Pro Val Gln Gly Val Ala Tyr Val Arg Phe Gly Leu Leu Asp 275 280 285 Glu Asp Gly Lys Lys Thr Phe Phe Arg Gly Leu Glu Ser Gln Thr Lys 290 295 300 Leu Val Asn Gly Gln Ser His Ile Ser Leu Ser Lys Ala Glu Phe Gln 305 310 315 320 Asp Ala Leu Glu Lys Leu Asn Met Gly Ile Thr Asp Leu Gln Gly Leu 325 330 335 Arg Leu Tyr Val Ala Ala Ala Ile Ile Glu Ser Pro Gly Gly Glu Met 340 345 350 Glu Glu Ala Glu Leu Thr Ser Trp Tyr Phe Val Ser Ser Pro Phe Ser 355 360 365 Leu Asp Leu Ser Lys Thr Lys Arg His Leu Val Pro Gly Ala Pro Phe 370 375 380 Leu Leu Gln Ala Leu Val Arg Glu Met Ser Gly Ser Pro Ala Ser Gly 385 390 395 400 Ile Pro Val Lys Val Ser Ala Thr Val Ser Ser Pro Gly Ser Val Pro 405 410 415 Glu Val Gln Asp Ile Gln Gln Asn Thr Asp Gly Ser Gly Gln Val Ser 420 425 430 Ile Pro Ile Ile Ile Pro Gln Thr Ile Ser Glu Leu Gln Leu Ser Val 435 440 445 Ser Ala Gly Ser Pro His Pro Ala Ile Ala Arg Leu Thr Val Ala Ala 450 455 460 Pro Pro Ser Gly Gly Pro Gly Phe Leu Ser Ile Glu Arg Pro Asp Ser 465 470 475 480 Arg Pro Pro Arg Val Gly Asp Thr Leu Asn Leu Asn Leu Arg Ala Val 485 490 495 Gly Ser Gly Ala Thr Phe Ser His Tyr Tyr Tyr Met Ile Leu Ser Arg 500 505 510 Gly Gln Ile Val Phe Met Asn Arg Glu Pro Lys Arg Thr Leu Thr Ser 515 520 525 Val Ser Val Phe Val Asp His His Leu Ala Pro Ser Phe Tyr Phe Val 530 535 540 Ala Phe Tyr Tyr His Gly Asp His Pro Val Ala Asn Ser Leu Arg Val 545 550 555 560 Asp Val Gln Ala Gly Ala Cys Glu Gly Lys Leu Glu Leu Ser Val Asp 565 570 575 Gly Ala Lys Gln Tyr Arg Asn Gly Glu Ser Val Lys Leu His Leu Glu 580 585 590 Thr Asp Ser Leu Ala Leu Val Ala Leu Gly Ala Leu Asp Thr Ala Leu 595 600 605 Tyr Ala Ala Gly Ser Lys Ser His Lys Pro Leu Asn Met Gly Lys Val 610 615 620 Phe Glu Ala Met Asn Ser Tyr Asp Leu Gly Cys Gly Pro Gly Gly Gly 625 630 635 640 Asp Ser Ala Leu Gln Val Phe Gln Ala Ala Gly Leu Ala Phe Ser Asp 645 650 655 Gly Asp Gln Trp Thr Leu Ser Arg Lys Arg Leu Ser Cys Pro Lys Glu 660 665 670 Lys Thr Thr Arg Lys Lys Arg Asn Val Asn Phe Gln Lys Ala Ile Asn 675 680 685 Glu Lys Leu Gly Gln Tyr Ala Ser Pro Thr Ala Lys Arg Cys Cys Gln 690 695 700 Asp Gly Val Thr Arg Leu Pro Met Met Arg Ser Cys Glu Gln Arg Ala 705 710 715 720 Ala Arg Val Gln Gln Pro Asp Cys Arg Glu Pro Phe Leu Ser Cys Cys 725 730 735 Gln Phe Ala Glu Ser Leu Arg Lys Lys Ser Arg Asp Lys Gly Gln Ala 740 745 750 Gly Leu Gln Arg Ala Leu Glu Ile Leu Gln Glu Glu Asp Leu Ile Asp 755 760 765 Glu Asp Asp Ile Pro Val Arg Ser Phe Phe Pro Glu Asn Trp Leu Trp 770 775 780 Arg Val Glu Thr Val Asp Arg Phe Gln Ile Leu Thr Leu Trp Leu Pro 785 790 795 800 Asp Ser Leu Thr Thr Trp Glu Ile His Gly Leu Ser Leu Ser Lys Thr 805 810 815 Lys Gly Leu Cys Val Ala Thr Pro Val Gln Leu Arg Val Phe Arg Glu 820 825 830 Phe His Leu His Leu Arg Leu Pro Met Ser Val Arg Arg Phe Glu Gln 835 840 845 Leu Glu Leu Arg Pro Val Leu Tyr Asn Tyr Leu Asp Lys Asn Leu Thr 850 855 860 Val Ser Val His Val Ser Pro Val Glu Gly Leu Cys Leu Ala Gly Gly 865 870 875 880 Gly Gly Leu Ala Gln Gln Val Leu Val Pro Ala Gly Ser Ala Arg Pro 885 890 895 Val Ala Phe Ser Val Val Pro Thr Ala Ala Thr Ala Val Ser Leu Lys 900 905 910 Val Val Ala Arg Gly Ser Phe Glu Phe Pro Val Gly Asp Ala Val Ser 915 920 925 Lys Val Leu Gln Ile Glu Lys Glu Gly Ala Ile His Arg Glu Glu Leu 930 935 940 Val Tyr Glu Leu Asn Pro Leu Asp His Arg Gly Arg Thr Leu Glu Ile 945 950 955 960 Pro Gly Asn Ser Asp Pro Asn Met Ile Pro Asp Gly Asp Phe Asn Ser 965 970 975 Tyr Val Arg Val Thr Ala Ser Asp Pro Leu Asp Thr Leu Gly Ser Glu 980 985 990 Gly Ala Leu Ser Pro Gly Gly Val Ala Ser Leu Leu Arg Leu Pro Arg 995 1000 1005 Gly Cys Gly Glu Gln Thr Met Ile Tyr Leu Ala Pro Thr Leu Ala 1010 1015 1020 Ala Ser Arg Tyr Leu Asp Lys Thr Glu Gln Trp Ser Thr Leu Pro 1025 1030 1035 Pro Glu Thr Lys Asp His Ala Val Asp Leu Ile Gln Lys Gly Tyr 1040 1045 1050 Met Arg Ile Gln Gln Phe Arg Lys Ala Asp Gly Ser Tyr Ala Ala 1055 1060 1065 Trp Leu Ser Arg Gly Ser Ser Thr Trp Leu Thr Ala Phe Val Leu 1070 1075 1080 Lys Val Leu Ser Leu Ala Gln Glu Gln Val Gly Gly Ser Pro Glu 1085 1090 1095 Lys Leu Gln Glu Thr Ser Asn Trp Leu Leu Ser Gln Gln Gln Ala 1100 1105 1110 Asp Gly Ser Phe Gln Asp Leu Ser Pro Val Ile His Arg Ser Met 1115 1120 1125 Gln Gly Gly Leu Val Gly Asn Asp Glu Thr Val Ala Leu Thr Ala 1130 1135 1140 Phe Val Thr Ile Ala Leu His His Gly Leu Ala Val Phe Gln Asp 1145 1150 1155 Glu Gly Ala Glu Pro Leu Lys Gln Arg Val Glu Ala Ser Ile Ser 1160 1165 1170 Lys Ala Ser Ser Phe Leu Gly Glu Lys Ala Ser Ala Gly Leu Leu 1175 1180 1185 Gly Ala His Ala Ala Ala Ile Thr Ala Tyr Ala Leu Thr Leu Thr 1190 1195 1200 Lys Ala Pro Ala Asp Leu Arg Gly Val Ala His Asn Asn Leu Met 1205 1210 1215 Ala Met Ala Gln Glu Thr Gly Asp Asn Leu Tyr Trp Gly Ser Val 1220 1225 1230 Thr Gly Ser Gln Ser Asn Ala Val Ser Pro Thr Pro Ala Pro Arg 1235 1240 1245 Asn Pro Ser Asp Pro Met Pro Gln Ala Pro Ala Leu Trp Ile Glu 1250 1255 1260 Thr Thr Ala Tyr Ala Leu Leu His Leu Leu Leu His Glu Gly Lys 1265 1270 1275 Ala Glu Met Ala Asp Gln Ala Ala Ala Trp Leu Thr Arg Gln Gly 1280 1285 1290 Ser Phe Gln Gly Gly Phe Arg Ser Thr Gln Asp Thr Val Ile Ala 1295 1300 1305 Leu Asp Ala Leu Ser Ala Tyr Trp Ile Ala Ser His Thr Thr Glu 1310 1315 1320 Glu Arg Gly Leu Asn Val Thr Leu Ser Ser Thr Gly Arg Asn Gly 1325 1330 1335 Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg Gly 1340 1345 1350 Leu Glu Glu Glu Leu Gln Phe Ser Leu Gly Ser Lys Ile Asn Val 1355 1360 1365 Lys Val Gly Gly Asn Ser Lys Gly Thr Leu Lys Val Leu Arg Thr 1370 1375 1380 Tyr Asn Val Leu Asp Met Lys Asn Thr Thr Cys Gln Asp Leu Gln 1385 1390 1395 Ile Glu Val Thr Val Lys Gly His Val Glu Tyr Thr Met Glu Ala 1400 1405 1410 Asn Glu Asp Tyr Glu Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1415 1420 1425 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu 1430 1435 1440 Phe Glu Gly Arg Arg Asn Arg Arg Arg Arg Glu Ala Pro Lys Val 1445 1450 1455 Val Glu Glu Gln Glu Ser Arg Val His Tyr Thr Val Cys Ile Trp 1460 1465 1470 Arg Asn Gly Lys Val Gly Leu Ser Gly Met Ala Ile Ala Asp Val 1475 1480 1485 Thr Leu Leu Ser Gly Phe His Ala Leu Arg Ala Asp Leu Glu Lys 1490 1495 1500 Leu Thr Ser Leu Ser Asp Arg Tyr Val Ser His Phe Glu Thr Glu 1505 1510 1515 Gly Pro His Val Leu Leu Tyr Phe Asp Ser Val Pro Thr Ser Arg 1520 1525 1530 Glu Cys Val Gly Phe Glu Ala Val Gln Glu Val Pro Val Gly Leu 1535 1540 1545 Val Gln Pro Ala Ser Ala Thr Leu Tyr Asp Tyr Tyr Asn Pro Glu 1550 1555 1560 Arg Arg Cys Ser Val Phe Tyr Gly Ala Pro Ser Lys Ser Arg Leu 1565 1570 1575 Leu Ala Thr Leu Cys Ser Ala Glu Val Cys Gln Cys Ala Glu Gly 1580 1585 1590 Lys Cys Pro Arg Gln Arg Arg Ala Leu Glu Arg Gly Leu Gln Asp 1595 1600 1605 Glu Asp Gly Tyr Arg Met Lys Phe Ala Cys Tyr Tyr Pro Arg Val 1610 1615 1620 Glu Tyr Gly Phe Gln Val Lys Val Leu Arg Glu Asp Ser Arg Ala 1625 1630 1635 Ala Phe Arg Leu Phe Glu Thr Lys Ile Thr Gln Val Leu His Phe 1640 1645 1650 Thr Lys Asp Val Lys Ala Ala Ala Asn Gln Met Arg Asn Phe Leu 1655 1660 1665 Val Arg Ala Ser Cys Arg Leu Arg Leu Glu Pro Gly Lys Glu Tyr 1670 1675 1680 Leu Ile Met Gly Leu Asp Gly Ala Thr Tyr Asp Leu Glu Gly His 1685 1690 1695 Pro Gln Tyr Leu Leu Asp Ser Asn Ser Trp Ile Glu Glu Met Pro 1700 1705 1710 Ser Glu Arg Leu Cys Arg Ser Thr Arg Gln Arg Ala Ala Cys Ala 1715 1720 1725 Gln Leu Asn Asp Phe Leu Gln Glu Tyr Gly Thr Gln Gly Cys Gln 1730 1735 1740 Val <210> SEQ ID NO 6 <211> LENGTH: 559 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q13112 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(559) <400> SEQUENCE: 6 Met Lys Val Ile Thr Cys Glu Ile Ala Trp His Asn Lys Glu Pro Val 1 5 10 15 Tyr Ser Leu Asp Phe Gln His Gly Thr Ala Gly Arg Ile His Arg Leu 20 25 30 Ala Ser Ala Gly Val Asp Thr Asn Val Arg Ile Trp Lys Val Glu Lys 35 40 45 Gly Pro Asp Gly Lys Ala Ile Val Glu Phe Leu Ser Asn Leu Ala Arg 50 55 60 His Thr Lys Ala Val Asn Val Val Arg Phe Ser Pro Thr Gly Glu Ile 65 70 75 80 Leu Ala Ser Gly Gly Asp Asp Ala Val Ile Leu Leu Trp Lys Val Asn 85 90 95 Asp Asn Lys Glu Pro Glu Gln Ile Ala Phe Gln Asp Glu Asp Glu Ala 100 105 110 Gln Leu Asn Lys Glu Asn Trp Thr Val Val Lys Thr Leu Arg Gly His 115 120 125 Leu Glu Asp Val Tyr Asp Ile Cys Trp Ala Thr Asp Gly Asn Leu Met 130 135 140 Ala Ser Ala Ser Val Asp Asn Thr Ala Ile Ile Trp Asp Val Ser Lys 145 150 155 160 Gly Gln Lys Ile Ser Ile Phe Asn Glu His Lys Ser Tyr Val Gln Gly 165 170 175 Val Thr Trp Asp Pro Leu Gly Gln Tyr Val Ala Thr Leu Ser Cys Asp 180 185 190 Arg Val Leu Arg Val Tyr Ser Ile Gln Lys Lys Arg Val Ala Phe Asn 195 200 205 Val Ser Lys Met Leu Ser Gly Ile Gly Ala Glu Gly Glu Ala Arg Ser 210 215 220 Tyr Arg Met Phe His Asp Asp Ser Met Lys Ser Phe Phe Arg Arg Leu 225 230 235 240 Ser Phe Thr Pro Asp Gly Ser Leu Leu Leu Thr Pro Ala Gly Cys Val 245 250 255 Glu Ser Gly Glu Asn Val Met Asn Thr Thr Tyr Val Phe Ser Arg Lys 260 265 270 Asn Leu Lys Arg Pro Ile Ala His Leu Pro Cys Pro Gly Lys Ala Thr 275 280 285 Leu Ala Val Arg Cys Cys Pro Val Tyr Phe Glu Leu Arg Pro Val Val 290 295 300 Glu Thr Gly Val Glu Leu Met Ser Leu Pro Tyr Arg Leu Val Phe Ala 305 310 315 320 Val Ala Ser Glu Asp Ser Val Leu Leu Tyr Asp Thr Gln Gln Ser Phe 325 330 335 Pro Phe Gly Tyr Val Ser Asn Ile His Tyr His Thr Leu Ser Asp Ile 340 345 350 Ser Trp Ser Ser Asp Gly Ala Phe Leu Ala Ile Ser Ser Thr Asp Gly 355 360 365 Tyr Cys Ser Phe Val Thr Phe Glu Lys Asp Glu Leu Gly Ile Pro Leu 370 375 380 Lys Glu Lys Pro Val Leu Asn Met Arg Thr Pro Asp Thr Ala Lys Lys 385 390 395 400 Thr Lys Ser Gln Thr His Arg Gly Ser Ser Pro Gly Pro Arg Pro Val 405 410 415 Glu Gly Thr Pro Ala Ser Arg Thr Gln Asp Pro Ser Ser Pro Gly Thr 420 425 430 Thr Pro Pro Gln Ala Arg Gln Ala Pro Ala Pro Thr Val Ile Arg Asp 435 440 445 Pro Pro Ser Ile Thr Pro Ala Val Lys Ser Pro Leu Pro Gly Pro Ser 450 455 460 Glu Glu Lys Thr Leu Gln Pro Ser Ser Gln Asn Thr Lys Ala His Pro 465 470 475 480 Ser Arg Arg Val Thr Leu Asn Thr Leu Gln Ala Trp Ser Lys Thr Thr 485 490 495 Pro Arg Arg Ile Asn Leu Thr Pro Leu Lys Thr Asp Thr Pro Pro Ser 500 505 510 Ser Val Pro Thr Ser Val Ile Ser Thr Pro Ser Thr Glu Glu Ile Gln 515 520 525 Ser Glu Thr Pro Gly Asp Ala Gln Gly Ser Pro Pro Glu Leu Lys Arg 530 535 540 Pro Arg Leu Asp Glu Asn Lys Gly Gly Thr Glu Ser Leu Asp Pro 545 550 555 <210> SEQ ID NO 7 <211> LENGTH: 94 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O14625 <309> DATABASE ENTRY DATE: 2015-06-24 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(94) <400> SEQUENCE: 7 Met Ser Val Lys Gly Met Ala Ile Ala Leu Ala Val Ile Leu Cys Ala 1 5 10 15 Thr Val Val Gln Gly Phe Pro Met Phe Lys Arg Gly Arg Cys Leu Cys 20 25 30 Ile Gly Pro Gly Val Lys Ala Val Lys Val Ala Asp Ile Glu Lys Ala 35 40 45 Ser Ile Met Tyr Pro Ser Asn Asn Cys Asp Lys Ile Glu Val Ile Ile 50 55 60 Thr Leu Lys Glu Asn Lys Gly Gln Arg Cys Leu Asn Pro Lys Ser Lys 65 70 75 80 Gln Ala Arg Leu Ile Ile Lys Lys Val Glu Arg Lys Asn Phe 85 90 <210> SEQ ID NO 8 <211> LENGTH: 125 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q07325 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(125) <400> SEQUENCE: 8 Met Lys Lys Ser Gly Val Leu Phe Leu Leu Gly Ile Ile Leu Leu Val 1 5 10 15 Leu Ile Gly Val Gln Gly Thr Pro Val Val Arg Lys Gly Arg Cys Ser 20 25 30 Cys Ile Ser Thr Asn Gln Gly Thr Ile His Leu Gln Ser Leu Lys Asp 35 40 45 Leu Lys Gln Phe Ala Pro Ser Pro Ser Cys Glu Lys Ile Glu Ile Ile 50 55 60 Ala Thr Leu Lys Asn Gly Val Gln Thr Cys Leu Asn Pro Asp Ser Ala 65 70 75 80 Asp Val Lys Glu Leu Ile Lys Lys Trp Glu Lys Gln Val Ser Gln Lys 85 90 95 Lys Lys Gln Lys Asn Gly Lys Lys His Gln Lys Lys Lys Val Leu Lys 100 105 110 Val Arg Lys Ser Gln Arg Ser Arg Gln Lys Lys Thr Thr 115 120 125 <210> SEQ ID NO 9 <211> LENGTH: 165 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P62937 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(165) <400> SEQUENCE: 9 Met Val Asn Pro Thr Val Phe Phe Asp Ile Ala Val Asp Gly Glu Pro 1 5 10 15 Leu Gly Arg Val Ser Phe Glu Leu Phe Ala Asp Lys Val Pro Lys Thr 20 25 30 Ala Glu Asn Phe Arg Ala Leu Ser Thr Gly Glu Lys Gly Phe Gly Tyr 35 40 45 Lys Gly Ser Cys Phe His Arg Ile Ile Pro Gly Phe Met Cys Gln Gly 50 55 60 Gly Asp Phe Thr Arg His Asn Gly Thr Gly Gly Lys Ser Ile Tyr Gly 65 70 75 80 Glu Lys Phe Glu Asp Glu Asn Phe Ile Leu Lys His Thr Gly Pro Gly 85 90 95 Ile Leu Ser Met Ala Asn Ala Gly Pro Asn Thr Asn Gly Ser Gln Phe 100 105 110 Phe Ile Cys Thr Ala Lys Thr Glu Trp Leu Asp Gly Lys His Val Val 115 120 125 Phe Gly Lys Val Lys Glu Gly Met Asn Ile Val Glu Ala Met Glu Arg 130 135 140 Phe Gly Ser Arg Asn Gly Lys Thr Ser Lys Lys Ile Thr Ile Ala Asp 145 150 155 160 Cys Gly Gln Leu Glu 165 <210> SEQ ID NO 10 <211> LENGTH: 585 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BY44 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(585) <400> SEQUENCE: 10 Met Ala Pro Ser Thr Pro Leu Leu Thr Val Arg Gly Ser Glu Gly Leu 1 5 10 15 Tyr Met Val Asn Gly Pro Pro His Phe Thr Glu Ser Thr Val Phe Pro 20 25 30 Arg Glu Ser Gly Lys Asn Cys Lys Val Cys Ile Phe Ser Lys Asp Gly 35 40 45 Thr Leu Phe Ala Trp Gly Asn Gly Glu Lys Val Asn Ile Ile Ser Val 50 55 60 Thr Asn Lys Gly Leu Leu His Ser Phe Asp Leu Leu Lys Ala Val Cys 65 70 75 80 Leu Glu Phe Ser Pro Lys Asn Thr Val Leu Ala Thr Trp Gln Pro Tyr 85 90 95 Thr Thr Ser Lys Asp Gly Thr Ala Gly Ile Pro Asn Leu Gln Leu Tyr 100 105 110 Asp Val Lys Thr Gly Thr Cys Leu Lys Ser Phe Ile Gln Lys Lys Met 115 120 125 Gln Asn Trp Cys Pro Ser Trp Ser Glu Asp Glu Thr Leu Cys Ala Arg 130 135 140 Asn Val Asn Asn Glu Val His Phe Phe Glu Asn Asn Asn Phe Asn Thr 145 150 155 160 Ile Ala Asn Lys Leu His Leu Gln Lys Ile Asn Asp Phe Val Leu Ser 165 170 175 Pro Gly Pro Gln Pro Tyr Lys Val Ala Val Tyr Val Pro Gly Ser Lys 180 185 190 Gly Ala Pro Ser Phe Val Arg Leu Tyr Gln Tyr Pro Asn Phe Ala Gly 195 200 205 Pro His Ala Ala Leu Ala Asn Lys Ser Phe Phe Lys Ala Asp Lys Val 210 215 220 Thr Met Leu Trp Asn Lys Lys Ala Thr Ala Val Leu Val Ile Ala Ser 225 230 235 240 Thr Asp Val Asp Lys Thr Gly Ala Ser Tyr Tyr Gly Glu Gln Thr Leu 245 250 255 His Tyr Ile Ala Thr Asn Gly Glu Ser Ala Val Val Gln Leu Pro Lys 260 265 270 Asn Gly Pro Ile Tyr Asp Val Val Trp Asn Ser Ser Ser Thr Glu Phe 275 280 285 Cys Ala Val Tyr Gly Phe Met Pro Ala Lys Ala Thr Ile Phe Asn Leu 290 295 300 Lys Cys Asp Pro Val Phe Asp Phe Gly Thr Gly Pro Arg Asn Ala Ala 305 310 315 320 Tyr Tyr Ser Pro His Gly His Ile Leu Val Leu Ala Gly Phe Gly Asn 325 330 335 Leu Arg Gly Gln Met Glu Val Trp Asp Val Lys Asn Tyr Lys Leu Ile 340 345 350 Ser Lys Pro Val Ala Ser Asp Ser Thr Tyr Phe Ala Trp Cys Pro Asp 355 360 365 Gly Glu His Ile Leu Thr Ala Thr Cys Ala Pro Arg Leu Arg Val Asn 370 375 380 Asn Gly Tyr Lys Ile Trp His Tyr Thr Gly Ser Ile Leu His Lys Tyr 385 390 395 400 Asp Val Pro Ser Asn Ala Glu Leu Trp Gln Val Ser Trp Gln Pro Phe 405 410 415 Leu Asp Gly Ile Phe Pro Ala Lys Thr Ile Thr Tyr Gln Ala Val Pro 420 425 430 Ser Glu Val Pro Asn Glu Glu Pro Lys Val Ala Thr Ala Tyr Arg Pro 435 440 445 Pro Ala Leu Arg Asn Lys Pro Ile Thr Asn Ser Lys Leu His Glu Glu 450 455 460 Glu Pro Pro Gln Asn Met Lys Pro Gln Ser Gly Asn Asp Lys Pro Leu 465 470 475 480 Ser Lys Thr Ala Leu Lys Asn Gln Arg Lys His Glu Ala Lys Lys Ala 485 490 495 Ala Lys Gln Glu Ala Arg Ser Asp Lys Ser Pro Asp Leu Ala Pro Thr 500 505 510 Pro Ala Pro Gln Ser Thr Pro Arg Asn Thr Val Ser Gln Ser Ile Ser 515 520 525 Gly Asp Pro Glu Ile Asp Lys Lys Ile Lys Asn Leu Lys Lys Lys Leu 530 535 540 Lys Ala Ile Glu Gln Leu Lys Glu Gln Ala Ala Thr Gly Lys Gln Leu 545 550 555 560 Glu Lys Asn Gln Leu Glu Lys Ile Gln Lys Glu Thr Ala Leu Leu Gln 565 570 575 Glu Leu Glu Asp Leu Glu Leu Gly Ile 580 585 <210> SEQ ID NO 11 <211> LENGTH: 434 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P06733 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(434) <400> SEQUENCE: 11 Met Ser Ile Leu Lys Ile His Ala Arg Glu Ile Phe Asp Ser Arg Gly 1 5 10 15 Asn Pro Thr Val Glu Val Asp Leu Phe Thr Ser Lys Gly Leu Phe Arg 20 25 30 Ala Ala Val Pro Ser Gly Ala Ser Thr Gly Ile Tyr Glu Ala Leu Glu 35 40 45 Leu Arg Asp Asn Asp Lys Thr Arg Tyr Met Gly Lys Gly Val Ser Lys 50 55 60 Ala Val Glu His Ile Asn Lys Thr Ile Ala Pro Ala Leu Val Ser Lys 65 70 75 80 Lys Leu Asn Val Thr Glu Gln Glu Lys Ile Asp Lys Leu Met Ile Glu 85 90 95 Met Asp Gly Thr Glu Asn Lys Ser Lys Phe Gly Ala Asn Ala Ile Leu 100 105 110 Gly Val Ser Leu Ala Val Cys Lys Ala Gly Ala Val Glu Lys Gly Val 115 120 125 Pro Leu Tyr Arg His Ile Ala Asp Leu Ala Gly Asn Ser Glu Val Ile 130 135 140 Leu Pro Val Pro Ala Phe Asn Val Ile Asn Gly Gly Ser His Ala Gly 145 150 155 160 Asn Lys Leu Ala Met Gln Glu Phe Met Ile Leu Pro Val Gly Ala Ala 165 170 175 Asn Phe Arg Glu Ala Met Arg Ile Gly Ala Glu Val Tyr His Asn Leu 180 185 190 Lys Asn Val Ile Lys Glu Lys Tyr Gly Lys Asp Ala Thr Asn Val Gly 195 200 205 Asp Glu Gly Gly Phe Ala Pro Asn Ile Leu Glu Asn Lys Glu Gly Leu 210 215 220 Glu Leu Leu Lys Thr Ala Ile Gly Lys Ala Gly Tyr Thr Asp Lys Val 225 230 235 240 Val Ile Gly Met Asp Val Ala Ala Ser Glu Phe Phe Arg Ser Gly Lys 245 250 255 Tyr Asp Leu Asp Phe Lys Ser Pro Asp Asp Pro Ser Arg Tyr Ile Ser 260 265 270 Pro Asp Gln Leu Ala Asp Leu Tyr Lys Ser Phe Ile Lys Asp Tyr Pro 275 280 285 Val Val Ser Ile Glu Asp Pro Phe Asp Gln Asp Asp Trp Gly Ala Trp 290 295 300 Gln Lys Phe Thr Ala Ser Ala Gly Ile Gln Val Val Gly Asp Asp Leu 305 310 315 320 Thr Val Thr Asn Pro Lys Arg Ile Ala Lys Ala Val Asn Glu Lys Ser 325 330 335 Cys Asn Cys Leu Leu Leu Lys Val Asn Gln Ile Gly Ser Val Thr Glu 340 345 350 Ser Leu Gln Ala Cys Lys Leu Ala Gln Ala Asn Gly Trp Gly Val Met 355 360 365 Val Ser His Arg Ser Gly Glu Thr Glu Asp Thr Phe Ile Ala Asp Leu 370 375 380 Val Val Gly Leu Cys Thr Gly Gln Ile Lys Thr Gly Ala Pro Cys Arg 385 390 395 400 Ser Glu Arg Leu Ala Lys Tyr Asn Gln Leu Leu Arg Ile Glu Glu Glu 405 410 415 Leu Gly Ser Lys Ala Lys Phe Ala Gly Arg Asn Phe Arg Asn Pro Leu 420 425 430 Ala Lys <210> SEQ ID NO 12 <211> LENGTH: 585 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q05329 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(585) <400> SEQUENCE: 12 Met Ala Ser Pro Gly Ser Gly Phe Trp Ser Phe Gly Ser Glu Asp Gly 1 5 10 15 Ser Gly Asp Ser Glu Asn Pro Gly Thr Ala Arg Ala Trp Cys Gln Val 20 25 30 Ala Gln Lys Phe Thr Gly Gly Ile Gly Asn Lys Leu Cys Ala Leu Leu 35 40 45 Tyr Gly Asp Ala Glu Lys Pro Ala Glu Ser Gly Gly Ser Gln Pro Pro 50 55 60 Arg Ala Ala Ala Arg Lys Ala Ala Cys Ala Cys Asp Gln Lys Pro Cys 65 70 75 80 Ser Cys Ser Lys Val Asp Val Asn Tyr Ala Phe Leu His Ala Thr Asp 85 90 95 Leu Leu Pro Ala Cys Asp Gly Glu Arg Pro Thr Leu Ala Phe Leu Gln 100 105 110 Asp Val Met Asn Ile Leu Leu Gln Tyr Val Val Lys Ser Phe Asp Arg 115 120 125 Ser Thr Lys Val Ile Asp Phe His Tyr Pro Asn Glu Leu Leu Gln Glu 130 135 140 Tyr Asn Trp Glu Leu Ala Asp Gln Pro Gln Asn Leu Glu Glu Ile Leu 145 150 155 160 Met His Cys Gln Thr Thr Leu Lys Tyr Ala Ile Lys Thr Gly His Pro 165 170 175 Arg Tyr Phe Asn Gln Leu Ser Thr Gly Leu Asp Met Val Gly Leu Ala 180 185 190 Ala Asp Trp Leu Thr Ser Thr Ala Asn Thr Asn Met Phe Thr Tyr Glu 195 200 205 Ile Ala Pro Val Phe Val Leu Leu Glu Tyr Val Thr Leu Lys Lys Met 210 215 220 Arg Glu Ile Ile Gly Trp Pro Gly Gly Ser Gly Asp Gly Ile Phe Ser 225 230 235 240 Pro Gly Gly Ala Ile Ser Asn Met Tyr Ala Met Met Ile Ala Arg Phe 245 250 255 Lys Met Phe Pro Glu Val Lys Glu Lys Gly Met Ala Ala Leu Pro Arg 260 265 270 Leu Ile Ala Phe Thr Ser Glu His Ser His Phe Ser Leu Lys Lys Gly 275 280 285 Ala Ala Ala Leu Gly Ile Gly Thr Asp Ser Val Ile Leu Ile Lys Cys 290 295 300 Asp Glu Arg Gly Lys Met Ile Pro Ser Asp Leu Glu Arg Arg Ile Leu 305 310 315 320 Glu Ala Lys Gln Lys Gly Phe Val Pro Phe Leu Val Ser Ala Thr Ala 325 330 335 Gly Thr Thr Val Tyr Gly Ala Phe Asp Pro Leu Leu Ala Val Ala Asp 340 345 350 Ile Cys Lys Lys Tyr Lys Ile Trp Met His Val Asp Ala Ala Trp Gly 355 360 365 Gly Gly Leu Leu Met Ser Arg Lys His Lys Trp Lys Leu Ser Gly Val 370 375 380 Glu Arg Ala Asn Ser Val Thr Trp Asn Pro His Lys Met Met Gly Val 385 390 395 400 Pro Leu Gln Cys Ser Ala Leu Leu Val Arg Glu Glu Gly Leu Met Gln 405 410 415 Asn Cys Asn Gln Met His Ala Ser Tyr Leu Phe Gln Gln Asp Lys His 420 425 430 Tyr Asp Leu Ser Tyr Asp Thr Gly Asp Lys Ala Leu Gln Cys Gly Arg 435 440 445 His Val Asp Val Phe Lys Leu Trp Leu Met Trp Arg Ala Lys Gly Thr 450 455 460 Thr Gly Phe Glu Ala His Val Asp Lys Cys Leu Glu Leu Ala Glu Tyr 465 470 475 480 Leu Tyr Asn Ile Ile Lys Asn Arg Glu Gly Tyr Glu Met Val Phe Asp 485 490 495 Gly Lys Pro Gln His Thr Asn Val Cys Phe Trp Tyr Ile Pro Pro Ser 500 505 510 Leu Arg Thr Leu Glu Asp Asn Glu Glu Arg Met Ser Arg Leu Ser Lys 515 520 525 Val Ala Pro Val Ile Lys Ala Arg Met Met Glu Tyr Gly Thr Thr Met 530 535 540 Val Ser Tyr Gln Pro Leu Gly Asp Lys Val Asn Phe Phe Arg Met Val 545 550 555 560 Ile Ser Asn Pro Ala Ala Thr His Gln Asp Ile Asp Phe Leu Ile Glu 565 570 575 Glu Ile Glu Arg Leu Gly Gln Asp Leu 580 585 <210> SEQ ID NO 13 <211> LENGTH: 211 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P39905 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(211) <400> SEQUENCE: 13 Met Lys Leu Trp Asp Val Val Ala Val Cys Leu Val Leu Leu His Thr 1 5 10 15 Ala Ser Ala Phe Pro Leu Pro Ala Gly Lys Arg Pro Pro Glu Ala Pro 20 25 30 Ala Glu Asp Arg Ser Leu Gly Arg Arg Arg Ala Pro Phe Ala Leu Ser 35 40 45 Ser Asp Ser Asn Met Pro Glu Asp Tyr Pro Asp Gln Phe Asp Asp Val 50 55 60 Met Asp Phe Ile Gln Ala Thr Ile Lys Arg Leu Lys Arg Ser Pro Asp 65 70 75 80 Lys Gln Met Ala Val Leu Pro Arg Arg Glu Arg Asn Arg Gln Ala Ala 85 90 95 Ala Ala Asn Pro Glu Asn Ser Arg Gly Lys Gly Arg Arg Gly Gln Arg 100 105 110 Gly Lys Asn Arg Gly Cys Val Leu Thr Ala Ile His Leu Asn Val Thr 115 120 125 Asp Leu Gly Leu Gly Tyr Glu Thr Lys Glu Glu Leu Ile Phe Arg Tyr 130 135 140 Cys Ser Gly Ser Cys Asp Ala Ala Glu Thr Thr Tyr Asp Lys Ile Leu 145 150 155 160 Lys Asn Leu Ser Arg Asn Arg Arg Leu Val Ser Asp Lys Val Gly Gln 165 170 175 Ala Cys Cys Arg Pro Ile Ala Phe Asp Asp Asp Leu Ser Phe Leu Asp 180 185 190 Asp Asn Leu Val Tyr His Ile Leu Arg Lys His Ser Ala Lys Arg Cys 195 200 205 Gly Cys Ile 210 <210> SEQ ID NO 14 <211> LENGTH: 463 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P61978 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(463) <400> SEQUENCE: 14 Met Glu Thr Glu Gln Pro Glu Glu Thr Phe Pro Asn Thr Glu Thr Asn 1 5 10 15 Gly Glu Phe Gly Lys Arg Pro Ala Glu Asp Met Glu Glu Glu Gln Ala 20 25 30 Phe Lys Arg Ser Arg Asn Thr Asp Glu Met Val Glu Leu Arg Ile Leu 35 40 45 Leu Gln Ser Lys Asn Ala Gly Ala Val Ile Gly Lys Gly Gly Lys Asn 50 55 60 Ile Lys Ala Leu Arg Thr Asp Tyr Asn Ala Ser Val Ser Val Pro Asp 65 70 75 80 Ser Ser Gly Pro Glu Arg Ile Leu Ser Ile Ser Ala Asp Ile Glu Thr 85 90 95 Ile Gly Glu Ile Leu Lys Lys Ile Ile Pro Thr Leu Glu Glu Gly Leu 100 105 110 Gln Leu Pro Ser Pro Thr Ala Thr Ser Gln Leu Pro Leu Glu Ser Asp 115 120 125 Ala Val Glu Cys Leu Asn Tyr Gln His Tyr Lys Gly Ser Asp Phe Asp 130 135 140 Cys Glu Leu Arg Leu Leu Ile His Gln Ser Leu Ala Gly Gly Ile Ile 145 150 155 160 Gly Val Lys Gly Ala Lys Ile Lys Glu Leu Arg Glu Asn Thr Gln Thr 165 170 175 Thr Ile Lys Leu Phe Gln Glu Cys Cys Pro His Ser Thr Asp Arg Val 180 185 190 Val Leu Ile Gly Gly Lys Pro Asp Arg Val Val Glu Cys Ile Lys Ile 195 200 205 Ile Leu Asp Leu Ile Ser Glu Ser Pro Ile Lys Gly Arg Ala Gln Pro 210 215 220 Tyr Asp Pro Asn Phe Tyr Asp Glu Thr Tyr Asp Tyr Gly Gly Phe Thr 225 230 235 240 Met Met Phe Asp Asp Arg Arg Gly Arg Pro Val Gly Phe Pro Met Arg 245 250 255 Gly Arg Gly Gly Phe Asp Arg Met Pro Pro Gly Arg Gly Gly Arg Pro 260 265 270 Met Pro Pro Ser Arg Arg Asp Tyr Asp Asp Met Ser Pro Arg Arg Gly 275 280 285 Pro Pro Pro Pro Pro Pro Gly Arg Gly Gly Arg Gly Gly Ser Arg Ala 290 295 300 Arg Asn Leu Pro Leu Pro Pro Pro Pro Pro Pro Arg Gly Gly Asp Leu 305 310 315 320 Met Ala Tyr Asp Arg Arg Gly Arg Pro Gly Asp Arg Tyr Asp Gly Met 325 330 335 Val Gly Phe Ser Ala Asp Glu Thr Trp Asp Ser Ala Ile Asp Thr Trp 340 345 350 Ser Pro Ser Glu Trp Gln Met Ala Tyr Glu Pro Gln Gly Gly Ser Gly 355 360 365 Tyr Asp Tyr Ser Tyr Ala Gly Gly Arg Gly Ser Tyr Gly Asp Leu Gly 370 375 380 Gly Pro Ile Ile Thr Thr Gln Val Thr Ile Pro Lys Asp Leu Ala Gly 385 390 395 400 Ser Ile Ile Gly Lys Gly Gly Gln Arg Ile Lys Gln Ile Arg His Glu 405 410 415 Ser Gly Ala Ser Ile Lys Ile Asp Glu Pro Leu Glu Gly Ser Glu Asp 420 425 430 Arg Ile Ile Thr Ile Thr Gly Thr Gln Asp Gln Ile Gln Asn Ala Gln 435 440 445 Tyr Leu Leu Gln Asn Ser Val Lys Gln Tyr Ser Gly Lys Phe Phe 450 455 460 <210> SEQ ID NO 15 <211> LENGTH: 532 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P05362 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(532) <400> SEQUENCE: 15 Met Ala Pro Ser Ser Pro Arg Pro Ala Leu Pro Ala Leu Leu Val Leu 1 5 10 15 Leu Gly Ala Leu Phe Pro Gly Pro Gly Asn Ala Gln Thr Ser Val Ser 20 25 30 Pro Ser Lys Val Ile Leu Pro Arg Gly Gly Ser Val Leu Val Thr Cys 35 40 45 Ser Thr Ser Cys Asp Gln Pro Lys Leu Leu Gly Ile Glu Thr Pro Leu 50 55 60 Pro Lys Lys Glu Leu Leu Leu Pro Gly Asn Asn Arg Lys Val Tyr Glu 65 70 75 80 Leu Ser Asn Val Gln Glu Asp Ser Gln Pro Met Cys Tyr Ser Asn Cys 85 90 95 Pro Asp Gly Gln Ser Thr Ala Lys Thr Phe Leu Thr Val Tyr Trp Thr 100 105 110 Pro Glu Arg Val Glu Leu Ala Pro Leu Pro Ser Trp Gln Pro Val Gly 115 120 125 Lys Asn Leu Thr Leu Arg Cys Gln Val Glu Gly Gly Ala Pro Arg Ala 130 135 140 Asn Leu Thr Val Val Leu Leu Arg Gly Glu Lys Glu Leu Lys Arg Glu 145 150 155 160 Pro Ala Val Gly Glu Pro Ala Glu Val Thr Thr Thr Val Leu Val Arg 165 170 175 Arg Asp His His Gly Ala Asn Phe Ser Cys Arg Thr Glu Leu Asp Leu 180 185 190 Arg Pro Gln Gly Leu Glu Leu Phe Glu Asn Thr Ser Ala Pro Tyr Gln 195 200 205 Leu Gln Thr Phe Val Leu Pro Ala Thr Pro Pro Gln Leu Val Ser Pro 210 215 220 Arg Val Leu Glu Val Asp Thr Gln Gly Thr Val Val Cys Ser Leu Asp 225 230 235 240 Gly Leu Phe Pro Val Ser Glu Ala Gln Val His Leu Ala Leu Gly Asp 245 250 255 Gln Arg Leu Asn Pro Thr Val Thr Tyr Gly Asn Asp Ser Phe Ser Ala 260 265 270 Lys Ala Ser Val Ser Val Thr Ala Glu Asp Glu Gly Thr Gln Arg Leu 275 280 285 Thr Cys Ala Val Ile Leu Gly Asn Gln Ser Gln Glu Thr Leu Gln Thr 290 295 300 Val Thr Ile Tyr Ser Phe Pro Ala Pro Asn Val Ile Leu Thr Lys Pro 305 310 315 320 Glu Val Ser Glu Gly Thr Glu Val Thr Val Lys Cys Glu Ala His Pro 325 330 335 Arg Ala Lys Val Thr Leu Asn Gly Val Pro Ala Gln Pro Leu Gly Pro 340 345 350 Arg Ala Gln Leu Leu Leu Lys Ala Thr Pro Glu Asp Asn Gly Arg Ser 355 360 365 Phe Ser Cys Ser Ala Thr Leu Glu Val Ala Gly Gln Leu Ile His Lys 370 375 380 Asn Gln Thr Arg Glu Leu Arg Val Leu Tyr Gly Pro Arg Leu Asp Glu 385 390 395 400 Arg Asp Cys Pro Gly Asn Trp Thr Trp Pro Glu Asn Ser Gln Gln Thr 405 410 415 Pro Met Cys Gln Ala Trp Gly Asn Pro Leu Pro Glu Leu Lys Cys Leu 420 425 430 Lys Asp Gly Thr Phe Pro Leu Pro Ile Gly Glu Ser Val Thr Val Thr 435 440 445 Arg Asp Leu Glu Gly Thr Tyr Leu Cys Arg Ala Arg Ser Thr Gln Gly 450 455 460 Glu Val Thr Arg Lys Val Thr Val Asn Val Leu Ser Pro Arg Tyr Glu 465 470 475 480 Ile Val Ile Ile Thr Val Val Ala Ala Ala Val Ile Met Gly Thr Ala 485 490 495 Gly Leu Ser Thr Tyr Leu Tyr Asn Arg Gln Arg Lys Ile Lys Lys Tyr 500 505 510 Arg Leu Gln Gln Ala Gln Lys Gly Thr Pro Met Lys Pro Asn Thr Gln 515 520 525 Ala Thr Pro Pro 530 <210> SEQ ID NO 16 <211> LENGTH: 785 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q16666 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(785) <400> SEQUENCE: 16 Met Gly Lys Lys Tyr Lys Asn Ile Val Leu Leu Lys Gly Leu Glu Val 1 5 10 15 Ile Asn Asp Tyr His Phe Arg Met Val Lys Ser Leu Leu Ser Asn Asp 20 25 30 Leu Lys Leu Asn Leu Lys Met Arg Glu Glu Tyr Asp Lys Ile Gln Ile 35 40 45 Ala Asp Leu Met Glu Glu Lys Phe Arg Gly Asp Ala Gly Leu Gly Lys 50 55 60 Leu Ile Lys Ile Phe Glu Asp Ile Pro Thr Leu Glu Asp Leu Ala Glu 65 70 75 80 Thr Leu Lys Lys Glu Lys Leu Lys Val Lys Gly Pro Ala Leu Ser Arg 85 90 95 Lys Arg Lys Lys Glu Val Asp Ala Thr Ser Pro Ala Pro Ser Thr Ser 100 105 110 Ser Thr Val Lys Thr Glu Gly Ala Glu Ala Thr Pro Gly Ala Gln Lys 115 120 125 Arg Lys Lys Ser Thr Lys Glu Lys Ala Gly Pro Lys Gly Ser Lys Val 130 135 140 Ser Glu Glu Gln Thr Gln Pro Pro Ser Pro Ala Gly Ala Gly Met Ser 145 150 155 160 Thr Ala Met Gly Arg Ser Pro Ser Pro Lys Thr Ser Leu Ser Ala Pro 165 170 175 Pro Asn Ser Ser Ser Thr Glu Asn Pro Lys Thr Val Ala Lys Cys Gln 180 185 190 Val Thr Pro Arg Arg Asn Val Leu Gln Lys Arg Pro Val Ile Val Lys 195 200 205 Val Leu Ser Thr Thr Lys Pro Phe Glu Tyr Glu Thr Pro Glu Met Glu 210 215 220 Lys Lys Ile Met Phe His Ala Thr Val Ala Thr Gln Thr Gln Phe Phe 225 230 235 240 His Val Lys Val Leu Asn Thr Ser Leu Lys Glu Lys Phe Asn Gly Lys 245 250 255 Lys Ile Ile Ile Ile Ser Asp Tyr Leu Glu Tyr Asp Ser Leu Leu Glu 260 265 270 Val Asn Glu Glu Ser Thr Val Ser Glu Ala Gly Pro Asn Gln Thr Phe 275 280 285 Glu Val Pro Asn Lys Ile Ile Asn Arg Ala Lys Glu Thr Leu Lys Ile 290 295 300 Asp Ile Leu His Lys Gln Ala Ser Gly Asn Ile Val Tyr Gly Val Phe 305 310 315 320 Met Leu His Lys Lys Thr Val Asn Gln Lys Thr Thr Ile Tyr Glu Ile 325 330 335 Gln Asp Asp Arg Gly Lys Met Asp Val Val Gly Thr Gly Gln Cys His 340 345 350 Asn Ile Pro Cys Glu Glu Gly Asp Lys Leu Gln Leu Phe Cys Phe Arg 355 360 365 Leu Arg Lys Lys Asn Gln Met Ser Lys Leu Ile Ser Glu Met His Ser 370 375 380 Phe Ile Gln Ile Lys Lys Lys Thr Asn Pro Arg Asn Asn Asp Pro Lys 385 390 395 400 Ser Met Lys Leu Pro Gln Glu Gln Arg Gln Leu Pro Tyr Pro Ser Glu 405 410 415 Ala Ser Thr Thr Phe Pro Glu Ser His Leu Arg Thr Pro Gln Met Pro 420 425 430 Pro Thr Thr Pro Ser Ser Ser Phe Phe Thr Lys Lys Ser Glu Asp Thr 435 440 445 Ile Ser Lys Met Asn Asp Phe Met Arg Met Gln Ile Leu Lys Glu Gly 450 455 460 Ser His Phe Pro Gly Pro Phe Met Thr Ser Ile Gly Pro Ala Glu Ser 465 470 475 480 His Pro His Thr Pro Gln Met Pro Pro Ser Thr Pro Ser Ser Ser Phe 485 490 495 Leu Thr Thr Lys Ser Glu Asp Thr Ile Ser Lys Met Asn Asp Phe Met 500 505 510 Arg Met Gln Ile Leu Lys Glu Gly Ser His Phe Pro Gly Pro Phe Met 515 520 525 Thr Ser Ile Gly Pro Ala Glu Ser His Pro His Thr Pro Gln Met Pro 530 535 540 Pro Ser Thr Pro Ser Ser Ser Phe Leu Thr Thr Leu Lys Pro Arg Leu 545 550 555 560 Lys Thr Glu Pro Glu Glu Val Ser Ile Glu Asp Ser Ala Gln Ser Asp 565 570 575 Leu Lys Glu Val Met Val Leu Asn Ala Thr Glu Ser Phe Val Tyr Glu 580 585 590 Pro Lys Glu Gln Lys Lys Met Phe His Ala Thr Val Ala Thr Glu Asn 595 600 605 Glu Val Phe Arg Val Lys Val Phe Asn Ile Asp Leu Lys Glu Lys Phe 610 615 620 Thr Pro Lys Lys Ile Ile Ala Ile Ala Asn Tyr Val Cys Arg Asn Gly 625 630 635 640 Phe Leu Glu Val Tyr Pro Phe Thr Leu Val Ala Asp Val Asn Ala Asp 645 650 655 Arg Asn Met Glu Ile Pro Lys Gly Leu Ile Arg Ser Ala Ser Val Thr 660 665 670 Pro Lys Ile Asn Gln Leu Cys Ser Gln Thr Lys Gly Ser Phe Val Asn 675 680 685 Gly Val Phe Glu Val His Lys Lys Asn Val Arg Gly Glu Phe Thr Tyr 690 695 700 Tyr Glu Ile Gln Asp Asn Thr Gly Lys Met Glu Val Val Val His Gly 705 710 715 720 Arg Leu Thr Thr Ile Asn Cys Glu Glu Gly Asp Lys Leu Lys Leu Thr 725 730 735 Cys Phe Glu Leu Ala Pro Lys Ser Gly Asn Thr Gly Glu Leu Arg Ser 740 745 750 Val Ile His Ser His Ile Lys Val Ile Lys Thr Arg Lys Asn Lys Lys 755 760 765 Asp Ile Leu Asn Pro Asp Ser Ser Met Glu Thr Ser Pro Asp Phe Phe 770 775 780 Phe 785 <210> SEQ ID NO 17 <211> LENGTH: 166 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P17803 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(166) <400> SEQUENCE: 17 Met Ser Tyr Thr Thr Tyr Phe Leu Ala Phe Gln Leu Cys Val Thr Leu 1 5 10 15 Cys Phe Ser Gly Ser Tyr Cys Gln Ala Pro Phe Phe Lys Glu Ile Thr 20 25 30 Ile Leu Lys Asp Tyr Phe Asn Ala Ser Thr Ser Asp Val Pro Asn Gly 35 40 45 Gly Pro Leu Phe Leu Glu Ile Leu Lys Asn Trp Lys Glu Glu Ser Asp 50 55 60 Lys Lys Ile Ile Gln Ser Gln Ile Val Ser Phe Tyr Phe Lys Phe Phe 65 70 75 80 Glu Ile Phe Lys Asp Asn Gln Ala Ile Gln Arg Ser Met Asp Val Ile 85 90 95 Lys Gln Asp Met Phe Gln Arg Phe Leu Asn Gly Ser Ser Gly Lys Leu 100 105 110 Asn Asp Phe Glu Lys Leu Ile Lys Ile Pro Val Asp Asn Leu Gln Ile 115 120 125 Gln Arg Lys Ala Ile Ser Glu Leu Ile Lys Val Met Asn Asp Leu Ser 130 135 140 Pro Arg Ser Asn Leu Arg Lys Arg Lys Arg Ser Gln Thr Met Phe Gln 145 150 155 160 Gly Gln Arg Ala Ser Lys 165 <210> SEQ ID NO 18 <211> LENGTH: 272 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01589 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(272) <400> SEQUENCE: 18 Met Asp Ser Tyr Leu Leu Met Trp Gly Leu Leu Thr Phe Ile Met Val 1 5 10 15 Pro Gly Cys Gln Ala Glu Leu Cys Asp Asp Asp Pro Pro Glu Ile Pro 20 25 30 His Ala Thr Phe Lys Ala Met Ala Tyr Lys Glu Gly Thr Met Leu Asn 35 40 45 Cys Glu Cys Lys Arg Gly Phe Arg Arg Ile Lys Ser Gly Ser Leu Tyr 50 55 60 Met Leu Cys Thr Gly Asn Ser Ser His Ser Ser Trp Asp Asn Gln Cys 65 70 75 80 Gln Cys Thr Ser Ser Ala Thr Arg Asn Thr Thr Lys Gln Val Thr Pro 85 90 95 Gln Pro Glu Glu Gln Lys Glu Arg Lys Thr Thr Glu Met Gln Ser Pro 100 105 110 Met Gln Pro Val Asp Gln Ala Ser Leu Pro Gly His Cys Arg Glu Pro 115 120 125 Pro Pro Trp Glu Asn Glu Ala Thr Glu Arg Ile Tyr His Phe Val Val 130 135 140 Gly Gln Met Val Tyr Tyr Gln Cys Val Gln Gly Tyr Arg Ala Leu His 145 150 155 160 Arg Gly Pro Ala Glu Ser Val Cys Lys Met Thr His Gly Lys Thr Arg 165 170 175 Trp Thr Gln Pro Gln Leu Ile Cys Thr Gly Glu Met Glu Thr Ser Gln 180 185 190 Phe Pro Gly Glu Glu Lys Pro Gln Ala Ser Pro Glu Gly Arg Pro Glu 195 200 205 Ser Glu Thr Ser Cys Leu Val Thr Thr Thr Asp Phe Gln Ile Gln Thr 210 215 220 Glu Met Ala Ala Thr Met Glu Thr Ser Ile Phe Thr Thr Glu Tyr Gln 225 230 235 240 Val Ala Val Ala Gly Cys Val Phe Leu Leu Ile Ser Val Leu Leu Leu 245 250 255 Ser Gly Leu Thr Trp Gln Arg Arg Gln Arg Lys Ser Arg Arg Thr Ile 260 265 270 <210> SEQ ID NO 19 <211> LENGTH: 459 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16871 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(459) <400> SEQUENCE: 19 Met Thr Ile Leu Gly Thr Thr Phe Gly Met Val Phe Ser Leu Leu Gln 1 5 10 15 Val Val Ser Gly Glu Ser Gly Tyr Ala Gln Asn Gly Asp Leu Glu Asp 20 25 30 Ala Glu Leu Asp Asp Tyr Ser Phe Ser Cys Tyr Ser Gln Leu Glu Val 35 40 45 Asn Gly Ser Gln His Ser Leu Thr Cys Ala Phe Glu Asp Pro Asp Val 50 55 60 Asn Thr Thr Asn Leu Glu Phe Glu Ile Cys Gly Ala Leu Val Glu Val 65 70 75 80 Lys Cys Leu Asn Phe Arg Lys Leu Gln Glu Ile Tyr Phe Ile Glu Thr 85 90 95 Lys Lys Phe Leu Leu Ile Gly Lys Ser Asn Ile Cys Val Lys Val Gly 100 105 110 Glu Lys Ser Leu Thr Cys Lys Lys Ile Asp Leu Thr Thr Ile Val Lys 115 120 125 Pro Glu Ala Pro Phe Asp Leu Ser Val Ile Tyr Arg Glu Gly Ala Asn 130 135 140 Asp Phe Val Val Thr Phe Asn Thr Ser His Leu Gln Lys Lys Tyr Val 145 150 155 160 Lys Val Leu Met His Asp Val Ala Tyr Arg Gln Glu Lys Asp Glu Asn 165 170 175 Lys Trp Thr His Val Asn Leu Ser Ser Thr Lys Leu Thr Leu Leu Gln 180 185 190 Arg Lys Leu Gln Pro Ala Ala Met Tyr Glu Ile Lys Val Arg Ser Ile 195 200 205 Pro Asp His Tyr Phe Lys Gly Phe Trp Ser Glu Trp Ser Pro Ser Tyr 210 215 220 Tyr Phe Arg Thr Pro Glu Ile Asn Asn Ser Ser Gly Glu Met Asp Pro 225 230 235 240 Ile Leu Leu Thr Ile Ser Ile Leu Ser Phe Phe Ser Val Ala Leu Leu 245 250 255 Val Ile Leu Ala Cys Val Leu Trp Lys Lys Arg Ile Lys Pro Ile Val 260 265 270 Trp Pro Ser Leu Pro Asp His Lys Lys Thr Leu Glu His Leu Cys Lys 275 280 285 Lys Pro Arg Lys Asn Leu Asn Val Ser Phe Asn Pro Glu Ser Phe Leu 290 295 300 Asp Cys Gln Ile His Arg Val Asp Asp Ile Gln Ala Arg Asp Glu Val 305 310 315 320 Glu Gly Phe Leu Gln Asp Thr Phe Pro Gln Gln Leu Glu Glu Ser Glu 325 330 335 Lys Gln Arg Leu Gly Gly Asp Val Gln Ser Pro Asn Cys Pro Ser Glu 340 345 350 Asp Val Val Ile Thr Pro Glu Ser Phe Gly Arg Asp Ser Ser Leu Thr 355 360 365 Cys Leu Ala Gly Asn Val Ser Ala Cys Asp Ala Pro Ile Leu Ser Ser 370 375 380 Ser Arg Ser Leu Asp Cys Arg Glu Ser Gly Lys Asn Gly Pro His Val 385 390 395 400 Tyr Gln Asp Leu Leu Leu Ser Leu Gly Thr Thr Asn Ser Thr Leu Pro 405 410 415 Pro Pro Phe Ser Leu Gln Ser Gly Ile Leu Thr Leu Asn Pro Val Ala 420 425 430 Gln Gly Gln Pro Ile Leu Thr Ser Leu Gly Ser Asn Gln Glu Glu Ala 435 440 445 Tyr Val Thr Met Ser Ser Phe Tyr Gln Asn Gln 450 455 <210> SEQ ID NO 20 <211> LENGTH: 110 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01308 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(110) <400> SEQUENCE: 20 Met Ala Leu Trp Met Arg Leu Leu Pro Leu Leu Ala Leu Leu Ala Leu 1 5 10 15 Trp Gly Pro Asp Pro Ala Ala Ala Phe Val Asn Gln His Leu Cys Gly 20 25 30 Ser His Leu Val Glu Ala Leu Tyr Leu Val Cys Gly Glu Arg Gly Phe 35 40 45 Phe Tyr Thr Pro Lys Thr Arg Arg Glu Ala Glu Asp Leu Gln Val Gly 50 55 60 Gln Val Glu Leu Gly Gly Gly Pro Gly Ala Gly Ser Leu Gln Pro Leu 65 70 75 80 Ala Leu Glu Gly Ser Leu Gln Lys Arg Gly Ile Val Glu Gln Cys Cys 85 90 95 Thr Ser Ile Cys Ser Leu Tyr Gln Leu Glu Asn Tyr Cys Asn 100 105 110 <210> SEQ ID NO 21 <211> LENGTH: 711 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q92945 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(459) <400> SEQUENCE: 21 Met Ser Asp Tyr Ser Thr Gly Gly Pro Pro Pro Gly Pro Pro Pro Pro 1 5 10 15 Ala Gly Gly Gly Gly Gly Ala Gly Gly Ala Gly Gly Gly Pro Pro Pro 20 25 30 Gly Pro Pro Gly Ala Gly Asp Arg Gly Gly Gly Gly Pro Gly Gly Gly 35 40 45 Gly Pro Gly Gly Gly Ser Ala Gly Gly Pro Ser Gln Pro Pro Gly Gly 50 55 60 Gly Gly Pro Gly Ile Arg Lys Asp Ala Phe Ala Asp Ala Val Gln Arg 65 70 75 80 Ala Arg Gln Ile Ala Ala Lys Ile Gly Gly Asp Ala Ala Thr Thr Val 85 90 95 Asn Asn Ser Thr Pro Asp Phe Gly Phe Gly Gly Gln Lys Arg Gln Leu 100 105 110 Glu Asp Gly Asp Gln Pro Glu Ser Lys Lys Leu Ala Ser Gln Gly Asp 115 120 125 Ser Ile Ser Ser Gln Leu Gly Pro Ile His Pro Pro Pro Arg Thr Ser 130 135 140 Met Thr Glu Glu Tyr Arg Val Pro Asp Gly Met Val Gly Leu Ile Ile 145 150 155 160 Gly Arg Gly Gly Glu Gln Ile Asn Lys Ile Gln Gln Asp Ser Gly Cys 165 170 175 Lys Val Gln Ile Ser Pro Asp Ser Gly Gly Leu Pro Glu Arg Ser Val 180 185 190 Ser Leu Thr Gly Ala Pro Glu Ser Val Gln Lys Ala Lys Met Met Leu 195 200 205 Asp Asp Ile Val Ser Arg Gly Arg Gly Gly Pro Pro Gly Gln Phe His 210 215 220 Asp Asn Ala Asn Gly Gly Gln Asn Gly Thr Val Gln Glu Ile Met Ile 225 230 235 240 Pro Ala Gly Lys Ala Gly Leu Val Ile Gly Lys Gly Gly Glu Thr Ile 245 250 255 Lys Gln Leu Gln Glu Arg Ala Gly Val Lys Met Ile Leu Ile Gln Asp 260 265 270 Gly Ser Gln Asn Thr Asn Val Asp Lys Pro Leu Arg Ile Ile Gly Asp 275 280 285 Pro Tyr Lys Val Gln Gln Ala Cys Glu Met Val Met Asp Ile Leu Arg 290 295 300 Glu Arg Asp Gln Gly Gly Phe Gly Asp Arg Asn Glu Tyr Gly Ser Arg 305 310 315 320 Ile Gly Gly Gly Ile Asp Val Pro Val Pro Arg His Ser Val Gly Val 325 330 335 Val Ile Gly Arg Ser Gly Glu Met Ile Lys Lys Ile Gln Asn Asp Ala 340 345 350 Gly Val Arg Ile Gln Phe Lys Gln Asp Asp Gly Thr Gly Pro Glu Lys 355 360 365 Ile Ala His Ile Met Gly Pro Pro Asp Arg Cys Glu His Ala Ala Arg 370 375 380 Ile Ile Asn Asp Leu Leu Gln Ser Leu Arg Ser Gly Pro Pro Gly Pro 385 390 395 400 Pro Gly Gly Pro Gly Met Pro Pro Gly Gly Arg Gly Arg Gly Arg Gly 405 410 415 Gln Gly Asn Trp Gly Pro Pro Gly Gly Glu Met Thr Phe Ser Ile Pro 420 425 430 Thr His Lys Cys Gly Leu Val Ile Gly Arg Gly Gly Glu Asn Val Lys 435 440 445 Ala Ile Asn Gln Gln Thr Gly Ala Phe Val Glu Ile Ser Arg Gln Leu 450 455 460 Pro Pro Asn Gly Asp Pro Asn Phe Lys Leu Phe Ile Ile Arg Gly Ser 465 470 475 480 Pro Gln Gln Ile Asp His Ala Lys Gln Leu Ile Glu Glu Lys Ile Glu 485 490 495 Gly Pro Leu Cys Pro Val Gly Pro Gly Pro Gly Gly Pro Gly Pro Ala 500 505 510 Gly Pro Met Gly Pro Phe Asn Pro Gly Pro Phe Asn Gln Gly Pro Pro 515 520 525 Gly Ala Pro Pro His Ala Gly Gly Pro Pro Pro His Gln Tyr Pro Pro 530 535 540 Gln Gly Trp Gly Asn Thr Tyr Pro Gln Trp Gln Pro Pro Ala Pro His 545 550 555 560 Asp Pro Ser Lys Ala Ala Ala Ala Ala Ala Asp Pro Asn Ala Ala Trp 565 570 575 Ala Ala Tyr Tyr Ser His Tyr Tyr Gln Gln Pro Pro Gly Pro Val Pro 580 585 590 Gly Pro Ala Pro Ala Pro Ala Ala Pro Pro Ala Gln Gly Glu Pro Pro 595 600 605 Gln Pro Pro Pro Thr Gly Gln Ser Asp Tyr Thr Lys Ala Trp Glu Glu 610 615 620 Tyr Tyr Lys Lys Ile Gly Gln Gln Pro Gln Gln Pro Gly Ala Pro Pro 625 630 635 640 Gln Gln Asp Tyr Thr Lys Ala Trp Glu Glu Tyr Tyr Lys Lys Gln Ala 645 650 655 Gln Val Ala Thr Gly Gly Gly Pro Gly Ala Pro Pro Gly Ser Gln Pro 660 665 670 Asp Tyr Ser Ala Ala Trp Ala Glu Tyr Tyr Arg Gln Gln Ala Ala Tyr 675 680 685 Tyr Gly Gln Thr Pro Gly Pro Gly Gly Pro Gln Pro Pro Pro Thr Gln 690 695 700 Gln Gly Gln Gln Gln Ala Gln 705 710 <210> SEQ ID NO 22 <211> LENGTH: 664 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02545 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(664) <400> SEQUENCE: 22 Met Glu Thr Pro Ser Gln Arg Arg Ala Thr Arg Ser Gly Ala Gln Ala 1 5 10 15 Ser Ser Thr Pro Leu Ser Pro Thr Arg Ile Thr Arg Leu Gln Glu Lys 20 25 30 Glu Asp Leu Gln Glu Leu Asn Asp Arg Leu Ala Val Tyr Ile Asp Arg 35 40 45 Val Arg Ser Leu Glu Thr Glu Asn Ala Gly Leu Arg Leu Arg Ile Thr 50 55 60 Glu Ser Glu Glu Val Val Ser Arg Glu Val Ser Gly Ile Lys Ala Ala 65 70 75 80 Tyr Glu Ala Glu Leu Gly Asp Ala Arg Lys Thr Leu Asp Ser Val Ala 85 90 95 Lys Glu Arg Ala Arg Leu Gln Leu Glu Leu Ser Lys Val Arg Glu Glu 100 105 110 Phe Lys Glu Leu Lys Ala Arg Asn Thr Lys Lys Glu Gly Asp Leu Ile 115 120 125 Ala Ala Gln Ala Arg Leu Lys Asp Leu Glu Ala Leu Leu Asn Ser Lys 130 135 140 Glu Ala Ala Leu Ser Thr Ala Leu Ser Glu Lys Arg Thr Leu Glu Gly 145 150 155 160 Glu Leu His Asp Leu Arg Gly Gln Val Ala Lys Leu Glu Ala Ala Leu 165 170 175 Gly Glu Ala Lys Lys Gln Leu Gln Asp Glu Met Leu Arg Arg Val Asp 180 185 190 Ala Glu Asn Arg Leu Gln Thr Met Lys Glu Glu Leu Asp Phe Gln Lys 195 200 205 Asn Ile Tyr Ser Glu Glu Leu Arg Glu Thr Lys Arg Arg His Glu Thr 210 215 220 Arg Leu Val Glu Ile Asp Asn Gly Lys Gln Arg Glu Phe Glu Ser Arg 225 230 235 240 Leu Ala Asp Ala Leu Gln Glu Leu Arg Ala Gln His Glu Asp Gln Val 245 250 255 Glu Gln Tyr Lys Lys Glu Leu Glu Lys Thr Tyr Ser Ala Lys Leu Asp 260 265 270 Asn Ala Arg Gln Ser Ala Glu Arg Asn Ser Asn Leu Val Gly Ala Ala 275 280 285 His Glu Glu Leu Gln Gln Ser Arg Ile Arg Ile Asp Ser Leu Ser Ala 290 295 300 Gln Leu Ser Gln Leu Gln Lys Gln Leu Ala Ala Lys Glu Ala Lys Leu 305 310 315 320 Arg Asp Leu Glu Asp Ser Leu Ala Arg Glu Arg Asp Thr Ser Arg Arg 325 330 335 Leu Leu Ala Glu Lys Glu Arg Glu Met Ala Glu Met Arg Ala Arg Met 340 345 350 Gln Gln Gln Leu Asp Glu Tyr Gln Glu Leu Leu Asp Ile Lys Leu Ala 355 360 365 Leu Asp Met Glu Ile His Ala Tyr Arg Lys Leu Leu Glu Gly Glu Glu 370 375 380 Glu Arg Leu Arg Leu Ser Pro Ser Pro Thr Ser Gln Arg Ser Arg Gly 385 390 395 400 Arg Ala Ser Ser His Ser Ser Gln Thr Gln Gly Gly Gly Ser Val Thr 405 410 415 Lys Lys Arg Lys Leu Glu Ser Thr Glu Ser Arg Ser Ser Phe Ser Gln 420 425 430 His Ala Arg Thr Ser Gly Arg Val Ala Val Glu Glu Val Asp Glu Glu 435 440 445 Gly Lys Phe Val Arg Leu Arg Asn Lys Ser Asn Glu Asp Gln Ser Met 450 455 460 Gly Asn Trp Gln Ile Lys Arg Gln Asn Gly Asp Asp Pro Leu Leu Thr 465 470 475 480 Tyr Arg Phe Pro Pro Lys Phe Thr Leu Lys Ala Gly Gln Val Val Thr 485 490 495 Ile Trp Ala Ala Gly Ala Gly Ala Thr His Ser Pro Pro Thr Asp Leu 500 505 510 Val Trp Lys Ala Gln Asn Thr Trp Gly Cys Gly Asn Ser Leu Arg Thr 515 520 525 Ala Leu Ile Asn Ser Thr Gly Glu Glu Val Ala Met Arg Lys Leu Val 530 535 540 Arg Ser Val Thr Val Val Glu Asp Asp Glu Asp Glu Asp Gly Asp Asp 545 550 555 560 Leu Leu His His His His Gly Ser His Cys Ser Ser Ser Gly Asp Pro 565 570 575 Ala Glu Tyr Asn Leu Arg Ser Arg Thr Val Leu Cys Gly Thr Cys Gly 580 585 590 Gln Pro Ala Asp Lys Ala Ser Ala Ser Gly Ser Gly Ala Gln Val Gly 595 600 605 Gly Pro Ile Ser Ser Gly Ser Ser Ala Ser Ser Val Thr Val Thr Arg 610 615 620 Ser Tyr Arg Ser Val Gly Gly Ser Gly Gly Gly Ser Phe Gly Asp Asn 625 630 635 640 Leu Val Thr Arg Ser Tyr Leu Leu Gly Asn Ser Ser Pro Arg Thr Gln 645 650 655 Ser Pro Gln Asn Cys Ser Ile Met 660 <210> SEQ ID NO 23 <211> LENGTH: 586 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P20700 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(586) <400> SEQUENCE: 23 Met Ala Thr Ala Thr Pro Val Pro Pro Arg Met Gly Ser Arg Ala Gly 1 5 10 15 Gly Pro Thr Thr Pro Leu Ser Pro Thr Arg Leu Ser Arg Leu Gln Glu 20 25 30 Lys Glu Glu Leu Arg Glu Leu Asn Asp Arg Leu Ala Val Tyr Ile Asp 35 40 45 Lys Val Arg Ser Leu Glu Thr Glu Asn Ser Ala Leu Gln Leu Gln Val 50 55 60 Thr Glu Arg Glu Glu Val Arg Gly Arg Glu Leu Thr Gly Leu Lys Ala 65 70 75 80 Leu Tyr Glu Thr Glu Leu Ala Asp Ala Arg Arg Ala Leu Asp Asp Thr 85 90 95 Ala Arg Glu Arg Ala Lys Leu Gln Ile Glu Leu Gly Lys Cys Lys Ala 100 105 110 Glu His Asp Gln Leu Leu Leu Asn Tyr Ala Lys Lys Glu Ser Asp Leu 115 120 125 Asn Gly Ala Gln Ile Lys Leu Arg Glu Tyr Glu Ala Ala Leu Asn Ser 130 135 140 Lys Asp Ala Ala Leu Ala Thr Ala Leu Gly Asp Lys Lys Ser Leu Glu 145 150 155 160 Gly Asp Leu Glu Asp Leu Lys Asp Gln Ile Ala Gln Leu Glu Ala Ser 165 170 175 Leu Ala Ala Ala Lys Lys Gln Leu Ala Asp Glu Thr Leu Leu Lys Val 180 185 190 Asp Leu Glu Asn Arg Cys Gln Ser Leu Thr Glu Asp Leu Glu Phe Arg 195 200 205 Lys Ser Met Tyr Glu Glu Glu Ile Asn Glu Thr Arg Arg Lys His Glu 210 215 220 Thr Arg Leu Val Glu Val Asp Ser Gly Arg Gln Ile Glu Tyr Glu Tyr 225 230 235 240 Lys Leu Ala Gln Ala Leu His Glu Met Arg Glu Gln His Asp Ala Gln 245 250 255 Val Arg Leu Tyr Lys Glu Glu Leu Glu Gln Thr Tyr His Ala Lys Leu 260 265 270 Glu Asn Ala Arg Leu Ser Ser Glu Met Asn Thr Ser Thr Val Asn Ser 275 280 285 Ala Arg Glu Glu Leu Met Glu Ser Arg Met Arg Ile Glu Ser Leu Ser 290 295 300 Ser Gln Leu Ser Asn Leu Gln Lys Glu Ser Arg Ala Cys Leu Glu Arg 305 310 315 320 Ile Gln Glu Leu Glu Asp Leu Leu Ala Lys Glu Lys Asp Asn Ser Arg 325 330 335 Arg Met Leu Thr Asp Lys Glu Arg Glu Met Ala Glu Ile Arg Asp Gln 340 345 350 Met Gln Gln Gln Leu Asn Asp Tyr Glu Gln Leu Leu Asp Val Lys Leu 355 360 365 Ala Leu Asp Met Glu Ile Ser Ala Tyr Arg Lys Leu Leu Glu Gly Glu 370 375 380 Glu Glu Arg Leu Lys Leu Ser Pro Ser Pro Ser Ser Arg Val Thr Val 385 390 395 400 Ser Arg Ala Ser Ser Ser Arg Ser Val Arg Thr Thr Arg Gly Lys Arg 405 410 415 Lys Arg Val Asp Val Glu Glu Ser Glu Ala Ser Ser Ser Val Ser Ile 420 425 430 Ser His Ser Ala Ser Ala Thr Gly Asn Val Cys Ile Glu Glu Ile Asp 435 440 445 Val Asp Gly Lys Phe Ile Arg Leu Lys Asn Thr Ser Glu Gln Asp Gln 450 455 460 Pro Met Gly Gly Trp Glu Met Ile Arg Lys Ile Gly Asp Thr Ser Val 465 470 475 480 Ser Tyr Lys Tyr Thr Ser Arg Tyr Val Leu Lys Ala Gly Gln Thr Val 485 490 495 Thr Ile Trp Ala Ala Asn Ala Gly Val Thr Ala Ser Pro Pro Thr Asp 500 505 510 Leu Ile Trp Lys Asn Gln Asn Ser Trp Gly Thr Gly Glu Asp Val Lys 515 520 525 Val Ile Leu Lys Asn Ser Gln Gly Glu Glu Val Ala Gln Arg Ser Thr 530 535 540 Val Phe Lys Thr Thr Ile Pro Glu Glu Glu Glu Glu Glu Glu Glu Ala 545 550 555 560 Ala Gly Val Val Val Glu Glu Glu Leu Phe His Gln Gln Gly Thr Pro 565 570 575 Arg Ala Ser Asn Arg Ser Cys Ala Ile Met 580 585 <210> SEQ ID NO 24 <211> LENGTH: 923 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O14786 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(923) <400> SEQUENCE: 24 Met Glu Arg Gly Leu Pro Leu Leu Cys Ala Val Leu Ala Leu Val Leu 1 5 10 15 Ala Pro Ala Gly Ala Phe Arg Asn Asp Lys Cys Gly Asp Thr Ile Lys 20 25 30 Ile Glu Ser Pro Gly Tyr Leu Thr Ser Pro Gly Tyr Pro His Ser Tyr 35 40 45 His Pro Ser Glu Lys Cys Glu Trp Leu Ile Gln Ala Pro Asp Pro Tyr 50 55 60 Gln Arg Ile Met Ile Asn Phe Asn Pro His Phe Asp Leu Glu Asp Arg 65 70 75 80 Asp Cys Lys Tyr Asp Tyr Val Glu Val Phe Asp Gly Glu Asn Glu Asn 85 90 95 Gly His Phe Arg Gly Lys Phe Cys Gly Lys Ile Ala Pro Pro Pro Val 100 105 110 Val Ser Ser Gly Pro Phe Leu Phe Ile Lys Phe Val Ser Asp Tyr Glu 115 120 125 Thr His Gly Ala Gly Phe Ser Ile Arg Tyr Glu Ile Phe Lys Arg Gly 130 135 140 Pro Glu Cys Ser Gln Asn Tyr Thr Thr Pro Ser Gly Val Ile Lys Ser 145 150 155 160 Pro Gly Phe Pro Glu Lys Tyr Pro Asn Ser Leu Glu Cys Thr Tyr Ile 165 170 175 Val Phe Val Pro Lys Met Ser Glu Ile Ile Leu Glu Phe Glu Ser Phe 180 185 190 Asp Leu Glu Pro Asp Ser Asn Pro Pro Gly Gly Met Phe Cys Arg Tyr 195 200 205 Asp Arg Leu Glu Ile Trp Asp Gly Phe Pro Asp Val Gly Pro His Ile 210 215 220 Gly Arg Tyr Cys Gly Gln Lys Thr Pro Gly Arg Ile Arg Ser Ser Ser 225 230 235 240 Gly Ile Leu Ser Met Val Phe Tyr Thr Asp Ser Ala Ile Ala Lys Glu 245 250 255 Gly Phe Ser Ala Asn Tyr Ser Val Leu Gln Ser Ser Val Ser Glu Asp 260 265 270 Phe Lys Cys Met Glu Ala Leu Gly Met Glu Ser Gly Glu Ile His Ser 275 280 285 Asp Gln Ile Thr Ala Ser Ser Gln Tyr Ser Thr Asn Trp Ser Ala Glu 290 295 300 Arg Ser Arg Leu Asn Tyr Pro Glu Asn Gly Trp Thr Pro Gly Glu Asp 305 310 315 320 Ser Tyr Arg Glu Trp Ile Gln Val Asp Leu Gly Leu Leu Arg Phe Val 325 330 335 Thr Ala Val Gly Thr Gln Gly Ala Ile Ser Lys Glu Thr Lys Lys Lys 340 345 350 Tyr Tyr Val Lys Thr Tyr Lys Ile Asp Val Ser Ser Asn Gly Glu Asp 355 360 365 Trp Ile Thr Ile Lys Glu Gly Asn Lys Pro Val Leu Phe Gln Gly Asn 370 375 380 Thr Asn Pro Thr Asp Val Val Val Ala Val Phe Pro Lys Pro Leu Ile 385 390 395 400 Thr Arg Phe Val Arg Ile Lys Pro Ala Thr Trp Glu Thr Gly Ile Ser 405 410 415 Met Arg Phe Glu Val Tyr Gly Cys Lys Ile Thr Asp Tyr Pro Cys Ser 420 425 430 Gly Met Leu Gly Met Val Ser Gly Leu Ile Ser Asp Ser Gln Ile Thr 435 440 445 Ser Ser Asn Gln Gly Asp Arg Asn Trp Met Pro Glu Asn Ile Arg Leu 450 455 460 Val Thr Ser Arg Ser Gly Trp Ala Leu Pro Pro Ala Pro His Ser Tyr 465 470 475 480 Ile Asn Glu Trp Leu Gln Ile Asp Leu Gly Glu Glu Lys Ile Val Arg 485 490 495 Gly Ile Ile Ile Gln Gly Gly Lys His Arg Glu Asn Lys Val Phe Met 500 505 510 Arg Lys Phe Lys Ile Gly Tyr Ser Asn Asn Gly Ser Asp Trp Lys Met 515 520 525 Ile Met Asp Asp Ser Lys Arg Lys Ala Lys Ser Phe Glu Gly Asn Asn 530 535 540 Asn Tyr Asp Thr Pro Glu Leu Arg Thr Phe Pro Ala Leu Ser Thr Arg 545 550 555 560 Phe Ile Arg Ile Tyr Pro Glu Arg Ala Thr His Gly Gly Leu Gly Leu 565 570 575 Arg Met Glu Leu Leu Gly Cys Glu Val Glu Ala Pro Thr Ala Gly Pro 580 585 590 Thr Thr Pro Asn Gly Asn Leu Val Asp Glu Cys Asp Asp Asp Gln Ala 595 600 605 Asn Cys His Ser Gly Thr Gly Asp Asp Phe Gln Leu Thr Gly Gly Thr 610 615 620 Thr Val Leu Ala Thr Glu Lys Pro Thr Val Ile Asp Ser Thr Ile Gln 625 630 635 640 Ser Glu Phe Pro Thr Tyr Gly Phe Asn Cys Glu Phe Gly Trp Gly Ser 645 650 655 His Lys Thr Phe Cys His Trp Glu His Asp Asn His Val Gln Leu Lys 660 665 670 Trp Ser Val Leu Thr Ser Lys Thr Gly Pro Ile Gln Asp His Thr Gly 675 680 685 Asp Gly Asn Phe Ile Tyr Ser Gln Ala Asp Glu Asn Gln Lys Gly Lys 690 695 700 Val Ala Arg Leu Val Ser Pro Val Val Tyr Ser Gln Asn Ser Ala His 705 710 715 720 Cys Met Thr Phe Trp Tyr His Met Ser Gly Ser His Val Gly Thr Leu 725 730 735 Arg Val Lys Leu Arg Tyr Gln Lys Pro Glu Glu Tyr Asp Gln Leu Val 740 745 750 Trp Met Ala Ile Gly His Gln Gly Asp His Trp Lys Glu Gly Arg Val 755 760 765 Leu Leu His Lys Ser Leu Lys Leu Tyr Gln Val Ile Phe Glu Gly Glu 770 775 780 Ile Gly Lys Gly Asn Leu Gly Gly Ile Ala Val Asp Asp Ile Ser Ile 785 790 795 800 Asn Asn His Ile Ser Gln Glu Asp Cys Ala Lys Pro Ala Asp Leu Asp 805 810 815 Lys Lys Asn Pro Glu Ile Lys Ile Asp Glu Thr Gly Ser Thr Pro Gly 820 825 830 Tyr Glu Gly Glu Gly Glu Gly Asp Lys Asn Ile Ser Arg Lys Pro Gly 835 840 845 Asn Val Leu Lys Thr Leu Asp Pro Ile Leu Ile Thr Ile Ile Ala Met 850 855 860 Ser Ala Leu Gly Val Leu Leu Gly Ala Val Cys Gly Val Val Leu Tyr 865 870 875 880 Cys Ala Cys Trp His Asn Gly Met Ser Glu Arg Asn Leu Ser Ala Leu 885 890 895 Glu Asn Tyr Asn Phe Glu Leu Val Asp Gly Val Lys Leu Lys Lys Asp 900 905 910 Lys Leu Asn Thr Gln Ser Thr Tyr Ser Glu Ala 915 920 <210> SEQ ID NO 25 <211> LENGTH: 441 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BXS6 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(441) <400> SEQUENCE: 25 Met Ile Ile Pro Ser Leu Glu Glu Leu Asp Ser Leu Lys Tyr Ser Asp 1 5 10 15 Leu Gln Asn Leu Ala Lys Ser Leu Gly Leu Arg Ala Asn Leu Arg Ala 20 25 30 Thr Lys Leu Leu Lys Ala Leu Lys Gly Tyr Ile Lys His Glu Ala Arg 35 40 45 Lys Gly Asn Glu Asn Gln Asp Glu Ser Gln Thr Ser Ala Ser Ser Cys 50 55 60 Asp Glu Thr Glu Ile Gln Ile Ser Asn Gln Glu Glu Ala Glu Arg Gln 65 70 75 80 Pro Leu Gly His Val Thr Lys Thr Arg Arg Arg Cys Lys Thr Val Arg 85 90 95 Val Asp Pro Asp Ser Gln Gln Asn His Ser Glu Ile Lys Ile Ser Asn 100 105 110 Pro Thr Glu Phe Gln Asn His Glu Lys Gln Glu Ser Gln Asp Leu Arg 115 120 125 Ala Thr Ala Lys Val Pro Ser Pro Pro Asp Glu His Gln Glu Ala Glu 130 135 140 Asn Ala Val Ser Ser Gly Asn Arg Asp Ser Lys Val Pro Ser Glu Gly 145 150 155 160 Lys Lys Ser Leu Tyr Thr Asp Glu Ser Ser Lys Pro Gly Lys Asn Lys 165 170 175 Arg Thr Ala Ile Thr Thr Pro Asn Phe Lys Lys Leu His Glu Ala His 180 185 190 Phe Lys Glu Met Glu Ser Ile Asp Gln Tyr Ile Glu Arg Lys Lys Lys 195 200 205 His Phe Glu Glu His Asn Ser Met Asn Glu Leu Lys Gln Gln Pro Ile 210 215 220 Asn Lys Gly Gly Val Arg Thr Pro Val Pro Pro Arg Gly Arg Leu Ser 225 230 235 240 Val Ala Ser Thr Pro Ile Ser Gln Arg Arg Ser Gln Gly Arg Ser Cys 245 250 255 Gly Pro Ala Ser Gln Ser Thr Leu Gly Leu Lys Gly Ser Leu Lys Arg 260 265 270 Ser Ala Ile Ser Ala Ala Lys Thr Gly Val Arg Phe Ser Ala Ala Thr 275 280 285 Lys Asp Asn Glu His Lys Arg Ser Leu Thr Lys Thr Pro Ala Arg Lys 290 295 300 Ser Ala His Val Thr Val Ser Gly Gly Thr Pro Lys Gly Glu Ala Val 305 310 315 320 Leu Gly Thr His Lys Leu Lys Thr Ile Thr Gly Asn Ser Ala Ala Val 325 330 335 Ile Thr Pro Phe Lys Leu Thr Thr Glu Ala Thr Gln Thr Pro Val Ser 340 345 350 Asn Lys Lys Pro Val Phe Asp Leu Lys Ala Ser Leu Ser Arg Pro Leu 355 360 365 Asn Tyr Glu Pro His Lys Gly Lys Leu Lys Pro Trp Gly Gln Ser Lys 370 375 380 Glu Asn Asn Tyr Leu Asn Gln His Val Asn Arg Ile Asn Phe Tyr Lys 385 390 395 400 Lys Thr Tyr Lys Gln Pro His Leu Gln Thr Lys Glu Glu Gln Arg Lys 405 410 415 Lys Arg Glu Gln Glu Arg Lys Glu Lys Lys Ala Lys Val Leu Gly Met 420 425 430 Arg Arg Gly Leu Ile Leu Ala Glu Asp 435 440 <210> SEQ ID NO 26 <211> LENGTH: 394 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9UQ80 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(394) <400> SEQUENCE: 26 Met Ser Gly Glu Asp Glu Gln Gln Glu Gln Thr Ile Ala Glu Asp Leu 1 5 10 15 Val Val Thr Lys Tyr Lys Met Gly Gly Asp Ile Ala Asn Arg Val Leu 20 25 30 Arg Ser Leu Val Glu Ala Ser Ser Ser Gly Val Ser Val Leu Ser Leu 35 40 45 Cys Glu Lys Gly Asp Ala Met Ile Met Glu Glu Thr Gly Lys Ile Phe 50 55 60 Lys Lys Glu Lys Glu Met Lys Lys Gly Ile Ala Phe Pro Thr Ser Ile 65 70 75 80 Ser Val Asn Asn Cys Val Cys His Phe Ser Pro Leu Lys Ser Asp Gln 85 90 95 Asp Tyr Ile Leu Lys Glu Gly Asp Leu Val Lys Ile Asp Leu Gly Val 100 105 110 His Val Asp Gly Phe Ile Ala Asn Val Ala His Thr Phe Val Val Asp 115 120 125 Val Ala Gln Gly Thr Gln Val Thr Gly Arg Lys Ala Asp Val Ile Lys 130 135 140 Ala Ala His Leu Cys Ala Glu Ala Ala Leu Arg Leu Val Lys Pro Gly 145 150 155 160 Asn Gln Asn Thr Gln Val Thr Glu Ala Trp Asn Lys Val Ala His Ser 165 170 175 Phe Asn Cys Thr Pro Ile Glu Gly Met Leu Ser His Gln Leu Lys Gln 180 185 190 His Val Ile Asp Gly Glu Lys Thr Ile Ile Gln Asn Pro Thr Asp Gln 195 200 205 Gln Lys Lys Asp His Glu Lys Ala Glu Phe Glu Val His Glu Val Tyr 210 215 220 Ala Val Asp Val Leu Val Ser Ser Gly Glu Gly Lys Ala Lys Asp Ala 225 230 235 240 Gly Gln Arg Thr Thr Ile Tyr Lys Arg Asp Pro Ser Lys Gln Tyr Gly 245 250 255 Leu Lys Met Lys Thr Ser Arg Ala Phe Phe Ser Glu Val Glu Arg Arg 260 265 270 Phe Asp Ala Met Pro Phe Thr Leu Arg Ala Phe Glu Asp Glu Lys Lys 275 280 285 Ala Arg Met Gly Val Val Glu Cys Ala Lys His Glu Leu Leu Gln Pro 290 295 300 Phe Asn Val Leu Tyr Glu Lys Glu Gly Glu Phe Val Ala Gln Phe Lys 305 310 315 320 Phe Thr Val Leu Leu Met Pro Asn Gly Pro Met Arg Ile Thr Ser Gly 325 330 335 Pro Phe Glu Pro Asp Leu Tyr Lys Ser Glu Met Glu Val Gln Asp Ala 340 345 350 Glu Leu Lys Ala Leu Leu Gln Ser Ser Ala Ser Arg Lys Thr Gln Lys 355 360 365 Lys Lys Lys Lys Lys Ala Ser Lys Thr Ala Glu Asn Ala Thr Ser Gly 370 375 380 Glu Thr Leu Glu Glu Asn Glu Ala Gly Asp 385 390 <210> SEQ ID NO 27 <211> LENGTH: 198 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P32119 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(198) <400> SEQUENCE: 27 Met Ala Ser Gly Asn Ala Arg Ile Gly Lys Pro Ala Pro Asp Phe Lys 1 5 10 15 Ala Thr Ala Val Val Asp Gly Ala Phe Lys Glu Val Lys Leu Ser Asp 20 25 30 Tyr Lys Gly Lys Tyr Val Val Leu Phe Phe Tyr Pro Leu Asp Phe Thr 35 40 45 Phe Val Cys Pro Thr Glu Ile Ile Ala Phe Ser Asn Arg Ala Glu Asp 50 55 60 Phe Arg Lys Leu Gly Cys Glu Val Leu Gly Val Ser Val Asp Ser Gln 65 70 75 80 Phe Thr His Leu Ala Trp Ile Asn Thr Pro Arg Lys Glu Gly Gly Leu 85 90 95 Gly Pro Leu Asn Ile Pro Leu Leu Ala Asp Val Thr Arg Arg Leu Ser 100 105 110 Glu Asp Tyr Gly Val Leu Lys Thr Asp Glu Gly Ile Ala Tyr Arg Gly 115 120 125 Leu Phe Ile Ile Asp Gly Lys Gly Val Leu Arg Gln Ile Thr Val Asn 130 135 140 Asp Leu Pro Val Gly Arg Ser Val Asp Glu Ala Leu Arg Leu Val Gln 145 150 155 160 Ala Phe Gln Tyr Thr Asp Glu His Gly Glu Val Cys Pro Ala Gly Trp 165 170 175 Lys Pro Gly Ser Asp Thr Ile Lys Pro Asn Val Asp Asp Ser Lys Glu 180 185 190 Tyr Phe Ser Lys His Asn 195 <210> SEQ ID NO 28 <211> LENGTH: 592 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q05513 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(592) <400> SEQUENCE: 28 Met Pro Ser Arg Thr Gly Pro Lys Met Glu Gly Ser Gly Gly Arg Val 1 5 10 15 Arg Leu Lys Ala His Tyr Gly Gly Asp Ile Phe Ile Thr Ser Val Asp 20 25 30 Ala Ala Thr Thr Phe Glu Glu Leu Cys Glu Glu Val Arg Asp Met Cys 35 40 45 Arg Leu His Gln Gln His Pro Leu Thr Leu Lys Trp Val Asp Ser Glu 50 55 60 Gly Asp Pro Cys Thr Val Ser Ser Gln Met Glu Leu Glu Glu Ala Phe 65 70 75 80 Arg Leu Ala Arg Gln Cys Arg Asp Glu Gly Leu Ile Ile His Val Phe 85 90 95 Pro Ser Thr Pro Glu Gln Pro Gly Leu Pro Cys Pro Gly Glu Asp Lys 100 105 110 Ser Ile Tyr Arg Arg Gly Ala Arg Arg Trp Arg Lys Leu Tyr Arg Ala 115 120 125 Asn Gly His Leu Phe Gln Ala Lys Arg Phe Asn Arg Arg Ala Tyr Cys 130 135 140 Gly Gln Cys Ser Glu Arg Ile Trp Gly Leu Ala Arg Gln Gly Tyr Arg 145 150 155 160 Cys Ile Asn Cys Lys Leu Leu Val His Lys Arg Cys His Gly Leu Val 165 170 175 Pro Leu Thr Cys Arg Lys His Met Asp Ser Val Met Pro Ser Gln Glu 180 185 190 Pro Pro Val Asp Asp Lys Asn Glu Asp Ala Asp Leu Pro Ser Glu Glu 195 200 205 Thr Asp Gly Ile Ala Tyr Ile Ser Ser Ser Arg Lys His Asp Ser Ile 210 215 220 Lys Asp Asp Ser Glu Asp Leu Lys Pro Val Ile Asp Gly Met Asp Gly 225 230 235 240 Ile Lys Ile Ser Gln Gly Leu Gly Leu Gln Asp Phe Asp Leu Ile Arg 245 250 255 Val Ile Gly Arg Gly Ser Tyr Ala Lys Val Leu Leu Val Arg Leu Lys 260 265 270 Lys Asn Asp Gln Ile Tyr Ala Met Lys Val Val Lys Lys Glu Leu Val 275 280 285 His Asp Asp Glu Asp Ile Asp Trp Val Gln Thr Glu Lys His Val Phe 290 295 300 Glu Gln Ala Ser Ser Asn Pro Phe Leu Val Gly Leu His Ser Cys Phe 305 310 315 320 Gln Thr Thr Ser Arg Leu Phe Leu Val Ile Glu Tyr Val Asn Gly Gly 325 330 335 Asp Leu Met Phe His Met Gln Arg Gln Arg Lys Leu Pro Glu Glu His 340 345 350 Ala Arg Phe Tyr Ala Ala Glu Ile Cys Ile Ala Leu Asn Phe Leu His 355 360 365 Glu Arg Gly Ile Ile Tyr Arg Asp Leu Lys Leu Asp Asn Val Leu Leu 370 375 380 Asp Ala Asp Gly His Ile Lys Leu Thr Asp Tyr Gly Met Cys Lys Glu 385 390 395 400 Gly Leu Gly Pro Gly Asp Thr Thr Ser Thr Phe Cys Gly Thr Pro Asn 405 410 415 Tyr Ile Ala Pro Glu Ile Leu Arg Gly Glu Glu Tyr Gly Phe Ser Val 420 425 430 Asp Trp Trp Ala Leu Gly Val Leu Met Phe Glu Met Met Ala Gly Arg 435 440 445 Ser Pro Phe Asp Ile Ile Thr Asp Asn Pro Asp Met Asn Thr Glu Asp 450 455 460 Tyr Leu Phe Gln Val Ile Leu Glu Lys Pro Ile Arg Ile Pro Arg Phe 465 470 475 480 Leu Ser Val Lys Ala Ser His Val Leu Lys Gly Phe Leu Asn Lys Asp 485 490 495 Pro Lys Glu Arg Leu Gly Cys Arg Pro Gln Thr Gly Phe Ser Asp Ile 500 505 510 Lys Ser His Ala Phe Phe Arg Ser Ile Asp Trp Asp Leu Leu Glu Lys 515 520 525 Lys Gln Ala Leu Pro Pro Phe Gln Pro Gln Ile Thr Asp Asp Tyr Gly 530 535 540 Leu Asp Asn Phe Asp Thr Gln Phe Thr Ser Glu Pro Val Gln Leu Thr 545 550 555 560 Pro Asp Asp Glu Asp Ala Ile Lys Arg Ile Asp Gln Ser Glu Phe Glu 565 570 575 Gly Phe Glu Tyr Ile Asn Pro Leu Leu Leu Ser Thr Glu Glu Ser Val 580 585 590 <210> SEQ ID NO 29 <211> LENGTH: 256 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9NP55 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(256) <400> SEQUENCE: 29 Met Phe Gln Thr Gly Gly Leu Ile Val Phe Tyr Gly Leu Leu Ala Gln 1 5 10 15 Thr Met Ala Gln Phe Gly Gly Leu Pro Val Pro Leu Asp Gln Thr Leu 20 25 30 Pro Leu Asn Val Asn Pro Ala Leu Pro Leu Ser Pro Thr Gly Leu Ala 35 40 45 Gly Ser Leu Thr Asn Ala Leu Ser Asn Gly Leu Leu Ser Gly Gly Leu 50 55 60 Leu Gly Ile Leu Glu Asn Leu Pro Leu Leu Asp Ile Leu Lys Pro Gly 65 70 75 80 Gly Gly Thr Ser Gly Gly Leu Leu Gly Gly Leu Leu Gly Lys Val Thr 85 90 95 Ser Val Ile Pro Gly Leu Asn Asn Ile Ile Asp Ile Lys Val Thr Asp 100 105 110 Pro Gln Leu Leu Glu Leu Gly Leu Val Gln Ser Pro Asp Gly His Arg 115 120 125 Leu Tyr Val Thr Ile Pro Leu Gly Ile Lys Leu Gln Val Asn Thr Pro 130 135 140 Leu Val Gly Ala Ser Leu Leu Arg Leu Ala Val Lys Leu Asp Ile Thr 145 150 155 160 Ala Glu Ile Leu Ala Val Arg Asp Lys Gln Glu Arg Ile His Leu Val 165 170 175 Leu Gly Asp Cys Thr His Ser Pro Gly Ser Leu Gln Ile Ser Leu Leu 180 185 190 Asp Gly Leu Gly Pro Leu Pro Ile Gln Gly Leu Leu Asp Ser Leu Thr 195 200 205 Gly Ile Leu Asn Lys Val Leu Pro Glu Leu Val Gln Gly Asn Val Cys 210 215 220 Pro Leu Val Asn Glu Val Leu Arg Gly Leu Asp Ile Thr Leu Val His 225 230 235 240 Asp Ile Val Asn Met Leu Ile His Gly Leu Gln Phe Val Ile Lys Val 245 250 255 <210> SEQ ID NO 30 <211> LENGTH: 418 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P43686 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(418) <400> SEQUENCE: 30 Met Glu Glu Ile Gly Ile Leu Val Glu Lys Ala Gln Asp Glu Ile Pro 1 5 10 15 Ala Leu Ser Val Ser Arg Pro Gln Thr Gly Leu Ser Phe Leu Gly Pro 20 25 30 Glu Pro Glu Asp Leu Glu Asp Leu Tyr Ser Arg Tyr Lys Lys Leu Gln 35 40 45 Gln Glu Leu Glu Phe Leu Glu Val Gln Glu Glu Tyr Ile Lys Asp Glu 50 55 60 Gln Lys Asn Leu Lys Lys Glu Phe Leu His Ala Gln Glu Glu Val Lys 65 70 75 80 Arg Ile Gln Ser Ile Pro Leu Val Ile Gly Gln Phe Leu Glu Ala Val 85 90 95 Asp Gln Asn Thr Ala Ile Val Gly Ser Thr Thr Gly Ser Asn Tyr Tyr 100 105 110 Val Arg Ile Leu Ser Thr Ile Asp Arg Glu Leu Leu Lys Pro Asn Ala 115 120 125 Ser Val Ala Leu His Lys His Ser Asn Ala Leu Val Asp Val Leu Pro 130 135 140 Pro Glu Ala Asp Ser Ser Ile Met Met Leu Thr Ser Asp Gln Lys Pro 145 150 155 160 Asp Val Met Tyr Ala Asp Ile Gly Gly Met Asp Ile Gln Lys Gln Glu 165 170 175 Val Arg Glu Ala Val Glu Leu Pro Leu Thr His Phe Glu Leu Tyr Lys 180 185 190 Gln Ile Gly Ile Asp Pro Pro Arg Gly Val Leu Met Tyr Gly Pro Pro 195 200 205 Gly Cys Gly Lys Thr Met Leu Ala Lys Ala Val Ala His His Thr Thr 210 215 220 Ala Ala Phe Ile Arg Val Val Gly Ser Glu Phe Val Gln Lys Tyr Leu 225 230 235 240 Gly Glu Gly Pro Arg Met Val Arg Asp Val Phe Arg Leu Ala Lys Glu 245 250 255 Asn Ala Pro Ala Ile Ile Phe Ile Asp Glu Ile Asp Ala Ile Ala Thr 260 265 270 Lys Arg Phe Asp Ala Gln Thr Gly Ala Asp Arg Glu Val Gln Arg Ile 275 280 285 Leu Leu Glu Leu Leu Asn Gln Met Asp Gly Phe Asp Gln Asn Val Asn 290 295 300 Val Lys Val Ile Met Ala Thr Asn Arg Ala Asp Thr Leu Asp Pro Ala 305 310 315 320 Leu Leu Arg Pro Gly Arg Leu Asp Arg Lys Ile Glu Phe Pro Leu Pro 325 330 335 Asp Arg Arg Gln Lys Arg Leu Ile Phe Ser Thr Ile Thr Ser Lys Met 340 345 350 Asn Leu Ser Glu Glu Val Asp Leu Glu Asp Tyr Val Ala Arg Pro Asp 355 360 365 Lys Ile Ser Gly Ala Asp Ile Asn Ser Ile Cys Gln Glu Ser Gly Met 370 375 380 Leu Ala Val Arg Glu Asn Arg Tyr Ile Val Leu Ala Lys Asp Phe Glu 385 390 395 400 Lys Ala Tyr Lys Thr Val Ile Lys Lys Asp Glu Gln Glu His Glu Phe 405 410 415 Tyr Lys <210> SEQ ID NO 31 <211> LENGTH: 979 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q16849 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(979) <400> SEQUENCE: 31 Met Arg Arg Pro Arg Arg Pro Gly Gly Leu Gly Gly Ser Gly Gly Leu 1 5 10 15 Arg Leu Leu Leu Cys Leu Leu Leu Leu Ser Ser Arg Pro Gly Gly Cys 20 25 30 Ser Ala Val Ser Ala His Gly Cys Leu Phe Asp Arg Arg Leu Cys Ser 35 40 45 His Leu Glu Val Cys Ile Gln Asp Gly Leu Phe Gly Gln Cys Gln Val 50 55 60 Gly Val Gly Gln Ala Arg Pro Leu Leu Gln Val Thr Ser Pro Val Leu 65 70 75 80 Gln Arg Leu Gln Gly Val Leu Arg Gln Leu Met Ser Gln Gly Leu Ser 85 90 95 Trp His Asp Asp Leu Thr Gln Tyr Val Ile Ser Gln Glu Met Glu Arg 100 105 110 Ile Pro Arg Leu Arg Pro Pro Glu Pro Arg Pro Arg Asp Arg Ser Gly 115 120 125 Leu Ala Pro Lys Arg Pro Gly Pro Ala Gly Glu Leu Leu Leu Gln Asp 130 135 140 Ile Pro Thr Gly Ser Ala Pro Ala Ala Gln His Arg Leu Pro Gln Pro 145 150 155 160 Pro Val Gly Lys Gly Gly Ala Gly Ala Ser Ser Ser Leu Ser Pro Leu 165 170 175 Gln Ala Glu Leu Leu Pro Pro Leu Leu Glu His Leu Leu Leu Pro Pro 180 185 190 Gln Pro Pro His Pro Ser Leu Ser Tyr Glu Pro Ala Leu Leu Gln Pro 195 200 205 Tyr Leu Phe His Gln Phe Gly Ser Arg Asp Gly Ser Arg Val Ser Glu 210 215 220 Gly Ser Pro Gly Met Val Ser Val Gly Pro Leu Pro Lys Ala Glu Ala 225 230 235 240 Pro Ala Leu Phe Ser Arg Thr Ala Ser Lys Gly Ile Phe Gly Asp His 245 250 255 Pro Gly His Ser Tyr Gly Asp Leu Pro Gly Pro Ser Pro Ala Gln Leu 260 265 270 Phe Gln Asp Ser Gly Leu Leu Tyr Leu Ala Gln Glu Leu Pro Ala Pro 275 280 285 Ser Arg Ala Arg Val Pro Arg Leu Pro Glu Gln Gly Ser Ser Ser Arg 290 295 300 Ala Glu Asp Ser Pro Glu Gly Tyr Glu Lys Glu Gly Leu Gly Asp Arg 305 310 315 320 Gly Glu Lys Pro Ala Ser Pro Ala Val Gln Pro Asp Ala Ala Leu Gln 325 330 335 Arg Leu Ala Ala Val Leu Ala Gly Tyr Gly Val Glu Leu Arg Gln Leu 340 345 350 Thr Pro Glu Gln Leu Ser Thr Leu Leu Thr Leu Leu Gln Leu Leu Pro 355 360 365 Lys Gly Ala Gly Arg Asn Pro Gly Gly Val Val Asn Val Gly Ala Asp 370 375 380 Ile Lys Lys Thr Met Glu Gly Pro Val Glu Gly Arg Asp Thr Ala Glu 385 390 395 400 Leu Pro Ala Arg Thr Ser Pro Met Pro Gly His Pro Thr Ala Ser Pro 405 410 415 Thr Ser Ser Glu Val Gln Gln Val Pro Ser Pro Val Ser Ser Glu Pro 420 425 430 Pro Lys Ala Ala Arg Pro Pro Val Thr Pro Val Leu Leu Glu Lys Lys 435 440 445 Ser Pro Leu Gly Gln Ser Gln Pro Thr Val Ala Gly Gln Pro Ser Ala 450 455 460 Arg Pro Ala Ala Glu Glu Tyr Gly Tyr Ile Val Thr Asp Gln Lys Pro 465 470 475 480 Leu Ser Leu Ala Ala Gly Val Lys Leu Leu Glu Ile Leu Ala Glu His 485 490 495 Val His Met Ser Ser Gly Ser Phe Ile Asn Ile Ser Val Val Gly Pro 500 505 510 Ala Leu Thr Phe Arg Ile Arg His Asn Glu Gln Asn Leu Ser Leu Ala 515 520 525 Asp Val Thr Gln Gln Ala Gly Leu Val Lys Ser Glu Leu Glu Ala Gln 530 535 540 Thr Gly Leu Gln Ile Leu Gln Thr Gly Val Gly Gln Arg Glu Glu Ala 545 550 555 560 Ala Ala Val Leu Pro Gln Thr Ala His Ser Thr Ser Pro Met Arg Ser 565 570 575 Val Leu Leu Thr Leu Val Ala Leu Ala Gly Val Ala Gly Leu Leu Val 580 585 590 Ala Leu Ala Val Ala Leu Cys Val Arg Gln His Ala Arg Gln Gln Asp 595 600 605 Lys Glu Arg Leu Ala Ala Leu Gly Pro Glu Gly Ala His Gly Asp Thr 610 615 620 Thr Phe Glu Tyr Gln Asp Leu Cys Arg Gln His Met Ala Thr Lys Ser 625 630 635 640 Leu Phe Asn Arg Ala Glu Gly Pro Pro Glu Pro Ser Arg Val Ser Ser 645 650 655 Val Ser Ser Gln Phe Ser Asp Ala Ala Gln Ala Ser Pro Ser Ser His 660 665 670 Ser Ser Thr Pro Ser Trp Cys Glu Glu Pro Ala Gln Ala Asn Met Asp 675 680 685 Ile Ser Thr Gly His Met Ile Leu Ala Tyr Met Glu Asp His Leu Arg 690 695 700 Asn Arg Asp Arg Leu Ala Lys Glu Trp Gln Ala Leu Cys Ala Tyr Gln 705 710 715 720 Ala Glu Pro Asn Thr Cys Ala Thr Ala Gln Gly Glu Gly Asn Ile Lys 725 730 735 Lys Asn Arg His Pro Asp Phe Leu Pro Tyr Asp His Ala Arg Ile Lys 740 745 750 Leu Lys Val Glu Ser Ser Pro Ser Arg Ser Asp Tyr Ile Asn Ala Ser 755 760 765 Pro Ile Ile Glu His Asp Pro Arg Met Pro Ala Tyr Ile Ala Thr Gln 770 775 780 Gly Pro Leu Ser His Thr Ile Ala Asp Phe Trp Gln Met Val Trp Glu 785 790 795 800 Ser Gly Cys Thr Val Ile Val Met Leu Thr Pro Leu Val Glu Asp Gly 805 810 815 Val Lys Gln Cys Asp Arg Tyr Trp Pro Asp Glu Gly Ala Ser Leu Tyr 820 825 830 His Val Tyr Glu Val Asn Leu Val Ser Glu His Ile Trp Cys Glu Asp 835 840 845 Phe Leu Val Arg Ser Phe Tyr Leu Lys Asn Val Gln Thr Gln Glu Thr 850 855 860 Arg Thr Leu Thr Gln Phe His Phe Leu Ser Trp Pro Ala Glu Gly Thr 865 870 875 880 Pro Ala Ser Thr Arg Pro Leu Leu Asp Phe Arg Arg Lys Val Asn Lys 885 890 895 Cys Tyr Arg Gly Arg Ser Cys Pro Ile Ile Val His Cys Ser Asp Gly 900 905 910 Ala Gly Arg Thr Gly Thr Tyr Ile Leu Ile Asp Met Val Leu Asn Arg 915 920 925 Met Ala Lys Gly Val Lys Glu Ile Asp Ile Ala Ala Thr Leu Glu His 930 935 940 Val Arg Asp Gln Arg Pro Gly Leu Val Arg Ser Lys Asp Gln Phe Glu 945 950 955 960 Phe Ala Leu Thr Ala Val Ala Glu Glu Val Asn Ala Ile Leu Lys Ala 965 970 975 Leu Pro Gln <210> SEQ ID NO 32 <211> LENGTH: 807 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9Y2R2 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(807) <400> SEQUENCE: 32 Met Asp Gln Arg Glu Ile Leu Gln Lys Phe Leu Asp Glu Ala Gln Ser 1 5 10 15 Lys Lys Ile Thr Lys Glu Glu Phe Ala Asn Glu Phe Leu Lys Leu Lys 20 25 30 Arg Gln Ser Thr Lys Tyr Lys Ala Asp Lys Thr Tyr Pro Thr Thr Val 35 40 45 Ala Glu Lys Pro Lys Asn Ile Lys Lys Asn Arg Tyr Lys Asp Ile Leu 50 55 60 Pro Tyr Asp Tyr Ser Arg Val Glu Leu Ser Leu Ile Thr Ser Asp Glu 65 70 75 80 Asp Ser Ser Tyr Ile Asn Ala Asn Phe Ile Lys Gly Val Tyr Gly Pro 85 90 95 Lys Ala Tyr Ile Ala Thr Gln Gly Pro Leu Ser Thr Thr Leu Leu Asp 100 105 110 Phe Trp Arg Met Ile Trp Glu Tyr Ser Val Leu Ile Ile Val Met Ala 115 120 125 Cys Met Glu Tyr Glu Met Gly Lys Lys Lys Cys Glu Arg Tyr Trp Ala 130 135 140 Glu Pro Gly Glu Met Gln Leu Glu Phe Gly Pro Phe Ser Val Ser Cys 145 150 155 160 Glu Ala Glu Lys Arg Lys Ser Asp Tyr Ile Ile Arg Thr Leu Lys Val 165 170 175 Lys Phe Asn Ser Glu Thr Arg Thr Ile Tyr Gln Phe His Tyr Lys Asn 180 185 190 Trp Pro Asp His Asp Val Pro Ser Ser Ile Asp Pro Ile Leu Glu Leu 195 200 205 Ile Trp Asp Val Arg Cys Tyr Gln Glu Asp Asp Ser Val Pro Ile Cys 210 215 220 Ile His Cys Ser Ala Gly Cys Gly Arg Thr Gly Val Ile Cys Ala Ile 225 230 235 240 Asp Tyr Thr Trp Met Leu Leu Lys Asp Gly Ile Ile Pro Glu Asn Phe 245 250 255 Ser Val Phe Ser Leu Ile Arg Glu Met Arg Thr Gln Arg Pro Ser Leu 260 265 270 Val Gln Thr Gln Glu Gln Tyr Glu Leu Val Tyr Asn Ala Val Leu Glu 275 280 285 Leu Phe Lys Arg Gln Met Asp Val Ile Arg Asp Lys His Ser Gly Thr 290 295 300 Glu Ser Gln Ala Lys His Cys Ile Pro Glu Lys Asn His Thr Leu Gln 305 310 315 320 Ala Asp Ser Tyr Ser Pro Asn Leu Pro Lys Ser Thr Thr Lys Ala Ala 325 330 335 Lys Met Met Asn Gln Gln Arg Thr Lys Met Glu Ile Lys Glu Ser Ser 340 345 350 Ser Phe Asp Phe Arg Thr Ser Glu Ile Ser Ala Lys Glu Glu Leu Val 355 360 365 Leu His Pro Ala Lys Ser Ser Thr Ser Phe Asp Phe Leu Glu Leu Asn 370 375 380 Tyr Ser Phe Asp Lys Asn Ala Asp Thr Thr Met Lys Trp Gln Thr Lys 385 390 395 400 Ala Phe Pro Ile Val Gly Glu Pro Leu Gln Lys His Gln Ser Leu Asp 405 410 415 Leu Gly Ser Leu Leu Phe Glu Gly Cys Ser Asn Ser Lys Pro Val Asn 420 425 430 Ala Ala Gly Arg Tyr Phe Asn Ser Lys Val Pro Ile Thr Arg Thr Lys 435 440 445 Ser Thr Pro Phe Glu Leu Ile Gln Gln Arg Glu Thr Lys Glu Val Asp 450 455 460 Ser Lys Glu Asn Phe Ser Tyr Leu Glu Ser Gln Pro His Asp Ser Cys 465 470 475 480 Phe Val Glu Met Gln Ala Gln Lys Val Met His Val Ser Ser Ala Glu 485 490 495 Leu Asn Tyr Ser Leu Pro Tyr Asp Ser Lys His Gln Ile Arg Asn Ala 500 505 510 Ser Asn Val Lys His His Asp Ser Ser Ala Leu Gly Val Tyr Ser Tyr 515 520 525 Ile Pro Leu Val Glu Asn Pro Tyr Phe Ser Ser Trp Pro Pro Ser Gly 530 535 540 Thr Ser Ser Lys Met Ser Leu Asp Leu Pro Glu Lys Gln Asp Gly Thr 545 550 555 560 Val Phe Pro Ser Ser Leu Leu Pro Thr Ser Ser Thr Ser Leu Phe Ser 565 570 575 Tyr Tyr Asn Ser His Asp Ser Leu Ser Leu Asn Ser Pro Thr Asn Ile 580 585 590 Ser Ser Leu Leu Asn Gln Glu Ser Ala Val Leu Ala Thr Ala Pro Arg 595 600 605 Ile Asp Asp Glu Ile Pro Pro Pro Leu Pro Val Arg Thr Pro Glu Ser 610 615 620 Phe Ile Val Val Glu Glu Ala Gly Glu Phe Ser Pro Asn Val Pro Lys 625 630 635 640 Ser Leu Ser Ser Ala Val Lys Val Lys Ile Gly Thr Ser Leu Glu Trp 645 650 655 Gly Gly Thr Ser Glu Pro Lys Lys Phe Asp Asp Ser Val Ile Leu Arg 660 665 670 Pro Ser Lys Ser Val Lys Leu Arg Ser Pro Lys Ser Glu Leu His Gln 675 680 685 Asp Arg Ser Ser Pro Pro Pro Pro Leu Pro Glu Arg Thr Leu Glu Ser 690 695 700 Phe Phe Leu Ala Asp Glu Asp Cys Met Gln Ala Gln Ser Ile Glu Thr 705 710 715 720 Tyr Ser Thr Ser Tyr Pro Asp Thr Met Glu Asn Ser Thr Ser Ser Lys 725 730 735 Gln Thr Leu Lys Thr Pro Gly Lys Ser Phe Thr Arg Ser Lys Ser Leu 740 745 750 Lys Ile Leu Arg Asn Met Lys Lys Ser Ile Cys Asn Ser Cys Pro Pro 755 760 765 Asn Lys Pro Ala Glu Ser Val Gln Ser Asn Asn Ser Ser Ser Phe Leu 770 775 780 Asn Phe Gly Phe Ala Asn Arg Phe Ser Lys Pro Lys Gly Pro Arg Asn 785 790 795 800 Pro Pro Pro Thr Trp Asn Ile 805 <210> SEQ ID NO 33 <211> LENGTH: 248 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P18124 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(248) <400> SEQUENCE: 33 Met Glu Gly Val Glu Glu Lys Lys Lys Glu Val Pro Ala Val Pro Glu 1 5 10 15 Thr Leu Lys Lys Lys Arg Arg Asn Phe Ala Glu Leu Lys Ile Lys Arg 20 25 30 Leu Arg Lys Lys Phe Ala Gln Lys Met Leu Arg Lys Ala Arg Arg Lys 35 40 45 Leu Ile Tyr Glu Lys Ala Lys His Tyr His Lys Glu Tyr Arg Gln Met 50 55 60 Tyr Arg Thr Glu Ile Arg Met Ala Arg Met Ala Arg Lys Ala Gly Asn 65 70 75 80 Phe Tyr Val Pro Ala Glu Pro Lys Leu Ala Phe Val Ile Arg Ile Arg 85 90 95 Gly Ile Asn Gly Val Ser Pro Lys Val Arg Lys Val Leu Gln Leu Leu 100 105 110 Arg Leu Arg Gln Ile Phe Asn Gly Thr Phe Val Lys Leu Asn Lys Ala 115 120 125 Ser Ile Asn Met Leu Arg Ile Val Glu Pro Tyr Ile Ala Trp Gly Tyr 130 135 140 Pro Asn Leu Lys Ser Val Asn Glu Leu Ile Tyr Lys Arg Gly Tyr Gly 145 150 155 160 Lys Ile Asn Lys Lys Arg Ile Ala Leu Thr Asp Asn Ala Leu Ile Ala 165 170 175 Arg Ser Leu Gly Lys Tyr Gly Ile Ile Cys Met Glu Asp Leu Ile His 180 185 190 Glu Ile Tyr Thr Val Gly Lys Arg Phe Lys Glu Ala Asn Asn Phe Leu 195 200 205 Trp Pro Phe Lys Leu Ser Ser Pro Arg Gly Gly Met Lys Lys Lys Thr 210 215 220 Thr His Phe Val Glu Gly Gly Asp Ala Gly Asn Arg Glu Asp Gln Ile 225 230 235 240 Asn Arg Leu Ile Arg Arg Met Asn 245 <210> SEQ ID NO 34 <211> LENGTH: 313 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q5MJ70 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(313) <400> SEQUENCE: 34 Met Arg His Asn Gln Met Cys Cys Glu Thr Pro Pro Thr Val Thr Val 1 5 10 15 Tyr Val Lys Ser Gly Ser Asn Arg Ser His Gln Pro Lys Lys Pro Ile 20 25 30 Thr Leu Lys Arg Pro Ile Cys Lys Asp Asn Trp Gln Ala Phe Glu Lys 35 40 45 Asn Thr His Asn Asn Asn Lys Ser Lys Arg Pro Lys Gly Pro Cys Leu 50 55 60 Val Ile Gln Arg Gln Asp Met Thr Ala Phe Phe Lys Leu Phe Asp Asp 65 70 75 80 Asp Leu Ile Gln Asp Phe Leu Trp Met Asp Cys Cys Cys Lys Ile Ala 85 90 95 Asp Lys Tyr Leu Leu Ala Met Thr Phe Val Tyr Phe Lys Arg Ala Lys 100 105 110 Phe Thr Ile Ser Glu His Thr Arg Ile Asn Phe Phe Ile Ala Leu Tyr 115 120 125 Leu Ala Asn Thr Val Glu Glu Asp Glu Glu Glu Thr Lys Tyr Glu Ile 130 135 140 Phe Pro Trp Ala Leu Gly Lys Asn Trp Arg Lys Leu Phe Pro Asn Phe 145 150 155 160 Leu Lys Leu Arg Asp Gln Leu Trp Asp Arg Ile Asp Tyr Arg Ala Ile 165 170 175 Val Ser Arg Arg Cys Cys Glu Glu Val Met Ala Ile Ala Pro Thr His 180 185 190 Tyr Ile Trp Gln Arg Glu Arg Ser Val His His Ser Gly Ala Val Arg 195 200 205 Asn Tyr Asn Arg Asp Glu Val Gln Leu Pro Arg Gly Pro Ser Ala Thr 210 215 220 Pro Val Asp Cys Ser Leu Cys Gly Lys Lys Arg Arg Tyr Val Arg Leu 225 230 235 240 Gly Leu Ser Ser Ser Ser Ser Leu Ser Ser His Thr Ala Gly Val Thr 245 250 255 Glu Lys His Ser Gln Asp Ser Tyr Asn Ser Leu Ser Met Asp Ile Ile 260 265 270 Gly Asp Pro Ser Gln Ala Tyr Thr Gly Ser Glu Val Val Asn Asp His 275 280 285 Gln Ser Asn Lys Gly Lys Lys Thr Asn Phe Leu Lys Lys Asp Lys Ser 290 295 300 Met Glu Trp Phe Thr Gly Ser Glu Glu 305 310 <210> SEQ ID NO 35 <211> LENGTH: 233 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01375 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(233) <400> SEQUENCE: 35 Met Ser Thr Glu Ser Met Ile Arg Asp Val Glu Leu Ala Glu Glu Ala 1 5 10 15 Leu Pro Lys Lys Thr Gly Gly Pro Gln Gly Ser Arg Arg Cys Leu Phe 20 25 30 Leu Ser Leu Phe Ser Phe Leu Ile Val Ala Gly Ala Thr Thr Leu Phe 35 40 45 Cys Leu Leu His Phe Gly Val Ile Gly Pro Gln Arg Glu Glu Phe Pro 50 55 60 Arg Asp Leu Ser Leu Ile Ser Pro Leu Ala Gln Ala Val Arg Ser Ser 65 70 75 80 Ser Arg Thr Pro Ser Asp Lys Pro Val Ala His Val Val Ala Asn Pro 85 90 95 Gln Ala Glu Gly Gln Leu Gln Trp Leu Asn Arg Arg Ala Asn Ala Leu 100 105 110 Leu Ala Asn Gly Val Glu Leu Arg Asp Asn Gln Leu Val Val Pro Ser 115 120 125 Glu Gly Leu Tyr Leu Ile Tyr Ser Gln Val Leu Phe Lys Gly Gln Gly 130 135 140 Cys Pro Ser Thr His Val Leu Leu Thr His Thr Ile Ser Arg Ile Ala 145 150 155 160 Val Ser Tyr Gln Thr Lys Val Asn Leu Leu Ser Ala Ile Lys Ser Pro 165 170 175 Cys Gln Arg Glu Thr Pro Glu Gly Ala Glu Ala Lys Pro Trp Tyr Glu 180 185 190 Pro Ile Tyr Leu Gly Gly Val Phe Gln Leu Glu Lys Gly Asp Arg Leu 195 200 205 Ser Ala Glu Ile Asn Arg Pro Asp Tyr Leu Asp Phe Ala Glu Ser Gly 210 215 220 Gln Val Tyr Phe Gly Ile Ile Ala Leu 225 230 <210> SEQ ID NO 36 <211> LENGTH: 175 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q06141 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(175) <400> SEQUENCE: 36 Met Leu Pro Pro Met Ala Leu Pro Ser Val Ser Trp Met Leu Leu Ser 1 5 10 15 Cys Leu Met Leu Leu Ser Gln Val Gln Gly Glu Glu Pro Gln Arg Glu 20 25 30 Leu Pro Ser Ala Arg Ile Arg Cys Pro Lys Gly Ser Lys Ala Tyr Gly 35 40 45 Ser His Cys Tyr Ala Leu Phe Leu Ser Pro Lys Ser Trp Thr Asp Ala 50 55 60 Asp Leu Ala Cys Gln Lys Arg Pro Ser Gly Asn Leu Val Ser Val Leu 65 70 75 80 Ser Gly Ala Glu Gly Ser Phe Val Ser Ser Leu Val Lys Ser Ile Gly 85 90 95 Asn Ser Tyr Ser Tyr Val Trp Ile Gly Leu His Asp Pro Thr Gln Gly 100 105 110 Thr Glu Pro Asn Gly Glu Gly Trp Glu Trp Ser Ser Ser Asp Val Met 115 120 125 Asn Tyr Phe Ala Trp Glu Arg Asn Pro Ser Thr Ile Ser Ser Pro Gly 130 135 140 His Cys Ala Ser Leu Ser Arg Ser Thr Ala Phe Leu Arg Trp Lys Asp 145 150 155 160 Tyr Asn Cys Asn Val Arg Leu Pro Tyr Val Cys Lys Phe Thr Asp 165 170 175 <210> SEQ ID NO 37 <211> LENGTH: 1342 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P21860 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1342) <400> SEQUENCE: 37 Met Arg Ala Asn Asp Ala Leu Gln Val Leu Gly Leu Leu Phe Ser Leu 1 5 10 15 Ala Arg Gly Ser Glu Val Gly Asn Ser Gln Ala Val Cys Pro Gly Thr 20 25 30 Leu Asn Gly Leu Ser Val Thr Gly Asp Ala Glu Asn Gln Tyr Gln Thr 35 40 45 Leu Tyr Lys Leu Tyr Glu Arg Cys Glu Val Val Met Gly Asn Leu Glu 50 55 60 Ile Val Leu Thr Gly His Asn Ala Asp Leu Ser Phe Leu Gln Trp Ile 65 70 75 80 Arg Glu Val Thr Gly Tyr Val Leu Val Ala Met Asn Glu Phe Ser Thr 85 90 95 Leu Pro Leu Pro Asn Leu Arg Val Val Arg Gly Thr Gln Val Tyr Asp 100 105 110 Gly Lys Phe Ala Ile Phe Val Met Leu Asn Tyr Asn Thr Asn Ser Ser 115 120 125 His Ala Leu Arg Gln Leu Arg Leu Thr Gln Leu Thr Glu Ile Leu Ser 130 135 140 Gly Gly Val Tyr Ile Glu Lys Asn Asp Lys Leu Cys His Met Asp Thr 145 150 155 160 Ile Asp Trp Arg Asp Ile Val Arg Asp Arg Asp Ala Glu Ile Val Val 165 170 175 Lys Asp Asn Gly Arg Ser Cys Pro Pro Cys His Glu Val Cys Lys Gly 180 185 190 Arg Cys Trp Gly Pro Gly Ser Glu Asp Cys Gln Thr Leu Thr Lys Thr 195 200 205 Ile Cys Ala Pro Gln Cys Asn Gly His Cys Phe Gly Pro Asn Pro Asn 210 215 220 Gln Cys Cys His Asp Glu Cys Ala Gly Gly Cys Ser Gly Pro Gln Asp 225 230 235 240 Thr Asp Cys Phe Ala Cys Arg His Phe Asn Asp Ser Gly Ala Cys Val 245 250 255 Pro Arg Cys Pro Gln Pro Leu Val Tyr Asn Lys Leu Thr Phe Gln Leu 260 265 270 Glu Pro Asn Pro His Thr Lys Tyr Gln Tyr Gly Gly Val Cys Val Ala 275 280 285 Ser Cys Pro His Asn Phe Val Val Asp Gln Thr Ser Cys Val Arg Ala 290 295 300 Cys Pro Pro Asp Lys Met Glu Val Asp Lys Asn Gly Leu Lys Met Cys 305 310 315 320 Glu Pro Cys Gly Gly Leu Cys Pro Lys Ala Cys Glu Gly Thr Gly Ser 325 330 335 Gly Ser Arg Phe Gln Thr Val Asp Ser Ser Asn Ile Asp Gly Phe Val 340 345 350 Asn Cys Thr Lys Ile Leu Gly Asn Leu Asp Phe Leu Ile Thr Gly Leu 355 360 365 Asn Gly Asp Pro Trp His Lys Ile Pro Ala Leu Asp Pro Glu Lys Leu 370 375 380 Asn Val Phe Arg Thr Val Arg Glu Ile Thr Gly Tyr Leu Asn Ile Gln 385 390 395 400 Ser Trp Pro Pro His Met His Asn Phe Ser Val Phe Ser Asn Leu Thr 405 410 415 Thr Ile Gly Gly Arg Ser Leu Tyr Asn Arg Gly Phe Ser Leu Leu Ile 420 425 430 Met Lys Asn Leu Asn Val Thr Ser Leu Gly Phe Arg Ser Leu Lys Glu 435 440 445 Ile Ser Ala Gly Arg Ile Tyr Ile Ser Ala Asn Arg Gln Leu Cys Tyr 450 455 460 His His Ser Leu Asn Trp Thr Lys Val Leu Arg Gly Pro Thr Glu Glu 465 470 475 480 Arg Leu Asp Ile Lys His Asn Arg Pro Arg Arg Asp Cys Val Ala Glu 485 490 495 Gly Lys Val Cys Asp Pro Leu Cys Ser Ser Gly Gly Cys Trp Gly Pro 500 505 510 Gly Pro Gly Gln Cys Leu Ser Cys Arg Asn Tyr Ser Arg Gly Gly Val 515 520 525 Cys Val Thr His Cys Asn Phe Leu Asn Gly Glu Pro Arg Glu Phe Ala 530 535 540 His Glu Ala Glu Cys Phe Ser Cys His Pro Glu Cys Gln Pro Met Glu 545 550 555 560 Gly Thr Ala Thr Cys Asn Gly Ser Gly Ser Asp Thr Cys Ala Gln Cys 565 570 575 Ala His Phe Arg Asp Gly Pro His Cys Val Ser Ser Cys Pro His Gly 580 585 590 Val Leu Gly Ala Lys Gly Pro Ile Tyr Lys Tyr Pro Asp Val Gln Asn 595 600 605 Glu Cys Arg Pro Cys His Glu Asn Cys Thr Gln Gly Cys Lys Gly Pro 610 615 620 Glu Leu Gln Asp Cys Leu Gly Gln Thr Leu Val Leu Ile Gly Lys Thr 625 630 635 640 His Leu Thr Met Ala Leu Thr Val Ile Ala Gly Leu Val Val Ile Phe 645 650 655 Met Met Leu Gly Gly Thr Phe Leu Tyr Trp Arg Gly Arg Arg Ile Gln 660 665 670 Asn Lys Arg Ala Met Arg Arg Tyr Leu Glu Arg Gly Glu Ser Ile Glu 675 680 685 Pro Leu Asp Pro Ser Glu Lys Ala Asn Lys Val Leu Ala Arg Ile Phe 690 695 700 Lys Glu Thr Glu Leu Arg Lys Leu Lys Val Leu Gly Ser Gly Val Phe 705 710 715 720 Gly Thr Val His Lys Gly Val Trp Ile Pro Glu Gly Glu Ser Ile Lys 725 730 735 Ile Pro Val Cys Ile Lys Val Ile Glu Asp Lys Ser Gly Arg Gln Ser 740 745 750 Phe Gln Ala Val Thr Asp His Met Leu Ala Ile Gly Ser Leu Asp His 755 760 765 Ala His Ile Val Arg Leu Leu Gly Leu Cys Pro Gly Ser Ser Leu Gln 770 775 780 Leu Val Thr Gln Tyr Leu Pro Leu Gly Ser Leu Leu Asp His Val Arg 785 790 795 800 Gln His Arg Gly Ala Leu Gly Pro Gln Leu Leu Leu Asn Trp Gly Val 805 810 815 Gln Ile Ala Lys Gly Met Tyr Tyr Leu Glu Glu His Gly Met Val His 820 825 830 Arg Asn Leu Ala Ala Arg Asn Val Leu Leu Lys Ser Pro Ser Gln Val 835 840 845 Gln Val Ala Asp Phe Gly Val Ala Asp Leu Leu Pro Pro Asp Asp Lys 850 855 860 Gln Leu Leu Tyr Ser Glu Ala Lys Thr Pro Ile Lys Trp Met Ala Leu 865 870 875 880 Glu Ser Ile His Phe Gly Lys Tyr Thr His Gln Ser Asp Val Trp Ser 885 890 895 Tyr Gly Val Thr Val Trp Glu Leu Met Thr Phe Gly Ala Glu Pro Tyr 900 905 910 Ala Gly Leu Arg Leu Ala Glu Val Pro Asp Leu Leu Glu Lys Gly Glu 915 920 925 Arg Leu Ala Gln Pro Gln Ile Cys Thr Ile Asp Val Tyr Met Val Met 930 935 940 Val Lys Cys Trp Met Ile Asp Glu Asn Ile Arg Pro Thr Phe Lys Glu 945 950 955 960 Leu Ala Asn Glu Phe Thr Arg Met Ala Arg Asp Pro Pro Arg Tyr Leu 965 970 975 Val Ile Lys Arg Glu Ser Gly Pro Gly Ile Ala Pro Gly Pro Glu Pro 980 985 990 His Gly Leu Thr Asn Lys Lys Leu Glu Glu Val Glu Leu Glu Pro Glu 995 1000 1005 Leu Asp Leu Asp Leu Asp Leu Glu Ala Glu Glu Asp Asn Leu Ala 1010 1015 1020 Thr Thr Thr Leu Gly Ser Ala Leu Ser Leu Pro Val Gly Thr Leu 1025 1030 1035 Asn Arg Pro Arg Gly Ser Gln Ser Leu Leu Ser Pro Ser Ser Gly 1040 1045 1050 Tyr Met Pro Met Asn Gln Gly Asn Leu Gly Glu Ser Cys Gln Glu 1055 1060 1065 Ser Ala Val Ser Gly Ser Ser Glu Arg Cys Pro Arg Pro Val Ser 1070 1075 1080 Leu His Pro Met Pro Arg Gly Cys Leu Ala Ser Glu Ser Ser Glu 1085 1090 1095 Gly His Val Thr Gly Ser Glu Ala Glu Leu Gln Glu Lys Val Ser 1100 1105 1110 Met Cys Arg Ser Arg Ser Arg Ser Arg Ser Pro Arg Pro Arg Gly 1115 1120 1125 Asp Ser Ala Tyr His Ser Gln Arg His Ser Leu Leu Thr Pro Val 1130 1135 1140 Thr Pro Leu Ser Pro Pro Gly Leu Glu Glu Glu Asp Val Asn Gly 1145 1150 1155 Tyr Val Met Pro Asp Thr His Leu Lys Gly Thr Pro Ser Ser Arg 1160 1165 1170 Glu Gly Thr Leu Ser Ser Val Gly Leu Ser Ser Val Leu Gly Thr 1175 1180 1185 Glu Glu Glu Asp Glu Asp Glu Glu Tyr Glu Tyr Met Asn Arg Arg 1190 1195 1200 Arg Arg His Ser Pro Pro His Pro Pro Arg Pro Ser Ser Leu Glu 1205 1210 1215 Glu Leu Gly Tyr Glu Tyr Met Asp Val Gly Ser Asp Leu Ser Ala 1220 1225 1230 Ser Leu Gly Ser Thr Gln Ser Cys Pro Leu His Pro Val Pro Ile 1235 1240 1245 Met Pro Thr Ala Gly Thr Thr Pro Asp Glu Asp Tyr Glu Tyr Met 1250 1255 1260 Asn Arg Gln Arg Asp Gly Gly Gly Pro Gly Gly Asp Tyr Ala Ala 1265 1270 1275 Met Gly Ala Cys Pro Ala Ser Glu Gln Gly Tyr Glu Glu Met Arg 1280 1285 1290 Ala Phe Gln Gly Pro Gly His Gln Ala Pro His Val His Tyr Ala 1295 1300 1305 Arg Leu Lys Thr Leu Arg Ser Leu Glu Ala Thr Asp Ser Ala Phe 1310 1315 1320 Asp Asn Pro Asp Tyr Trp His Ser Arg Leu Phe Pro Lys Ala Asn 1325 1330 1335 Ala Gln Arg Thr 1340 <210> SEQ ID NO 38 <211> LENGTH: 472 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16671 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(472) <400> SEQUENCE: 38 Met Gly Cys Asp Arg Asn Cys Gly Leu Ile Ala Gly Ala Val Ile Gly 1 5 10 15 Ala Val Leu Ala Val Phe Gly Gly Ile Leu Met Pro Val Gly Asp Leu 20 25 30 Leu Ile Gln Lys Thr Ile Lys Lys Gln Val Val Leu Glu Glu Gly Thr 35 40 45 Ile Ala Phe Lys Asn Trp Val Lys Thr Gly Thr Glu Val Tyr Arg Gln 50 55 60 Phe Trp Ile Phe Asp Val Gln Asn Pro Gln Glu Val Met Met Asn Ser 65 70 75 80 Ser Asn Ile Gln Val Lys Gln Arg Gly Pro Tyr Thr Tyr Arg Val Arg 85 90 95 Phe Leu Ala Lys Glu Asn Val Thr Gln Asp Ala Glu Asp Asn Thr Val 100 105 110 Ser Phe Leu Gln Pro Asn Gly Ala Ile Phe Glu Pro Ser Leu Ser Val 115 120 125 Gly Thr Glu Ala Asp Asn Phe Thr Val Leu Asn Leu Ala Val Ala Ala 130 135 140 Ala Ser His Ile Tyr Gln Asn Gln Phe Val Gln Met Ile Leu Asn Ser 145 150 155 160 Leu Ile Asn Lys Ser Lys Ser Ser Met Phe Gln Val Arg Thr Leu Arg 165 170 175 Glu Leu Leu Trp Gly Tyr Arg Asp Pro Phe Leu Ser Leu Val Pro Tyr 180 185 190 Pro Val Thr Thr Thr Val Gly Leu Phe Tyr Pro Tyr Asn Asn Thr Ala 195 200 205 Asp Gly Val Tyr Lys Val Phe Asn Gly Lys Asp Asn Ile Ser Lys Val 210 215 220 Ala Ile Ile Asp Thr Tyr Lys Gly Lys Arg Asn Leu Ser Tyr Trp Glu 225 230 235 240 Ser His Cys Asp Met Ile Asn Gly Thr Asp Ala Ala Ser Phe Pro Pro 245 250 255 Phe Val Glu Lys Ser Gln Val Leu Gln Phe Phe Ser Ser Asp Ile Cys 260 265 270 Arg Ser Ile Tyr Ala Val Phe Glu Ser Asp Val Asn Leu Lys Gly Ile 275 280 285 Pro Val Tyr Arg Phe Val Leu Pro Ser Lys Ala Phe Ala Ser Pro Val 290 295 300 Glu Asn Pro Asp Asn Tyr Cys Phe Cys Thr Glu Lys Ile Ile Ser Lys 305 310 315 320 Asn Cys Thr Ser Tyr Gly Val Leu Asp Ile Ser Lys Cys Lys Glu Gly 325 330 335 Arg Pro Val Tyr Ile Ser Leu Pro His Phe Leu Tyr Ala Ser Pro Asp 340 345 350 Val Ser Glu Pro Ile Asp Gly Leu Asn Pro Asn Glu Glu Glu His Arg 355 360 365 Thr Tyr Leu Asp Ile Glu Pro Ile Thr Gly Phe Thr Leu Gln Phe Ala 370 375 380 Lys Arg Leu Gln Val Asn Leu Leu Val Lys Pro Ser Glu Lys Ile Gln 385 390 395 400 Val Leu Lys Asn Leu Lys Arg Asn Tyr Ile Val Pro Ile Leu Trp Leu 405 410 415 Asn Glu Thr Gly Thr Ile Gly Asp Glu Lys Ala Asn Met Phe Arg Ser 420 425 430 Gln Val Thr Gly Lys Ile Asn Leu Leu Gly Leu Ile Glu Met Ile Leu 435 440 445 Leu Ser Val Gly Val Val Met Phe Val Ala Phe Met Ile Ser Tyr Cys 450 455 460 Ala Cys Arg Ser Lys Thr Ile Lys 465 470 <210> SEQ ID NO 39 <211> LENGTH: 710 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P19338 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(710) <400> SEQUENCE: 39 Met Val Lys Leu Ala Lys Ala Gly Lys Asn Gln Gly Asp Pro Lys Lys 1 5 10 15 Met Ala Pro Pro Pro Lys Glu Val Glu Glu Asp Ser Glu Asp Glu Glu 20 25 30 Met Ser Glu Asp Glu Glu Asp Asp Ser Ser Gly Glu Glu Val Val Ile 35 40 45 Pro Gln Lys Lys Gly Lys Lys Ala Ala Ala Thr Ser Ala Lys Lys Val 50 55 60 Val Val Ser Pro Thr Lys Lys Val Ala Val Ala Thr Pro Ala Lys Lys 65 70 75 80 Ala Ala Val Thr Pro Gly Lys Lys Ala Ala Ala Thr Pro Ala Lys Lys 85 90 95 Thr Val Thr Pro Ala Lys Ala Val Thr Thr Pro Gly Lys Lys Gly Ala 100 105 110 Thr Pro Gly Lys Ala Leu Val Ala Thr Pro Gly Lys Lys Gly Ala Ala 115 120 125 Ile Pro Ala Lys Gly Ala Lys Asn Gly Lys Asn Ala Lys Lys Glu Asp 130 135 140 Ser Asp Glu Glu Glu Asp Asp Asp Ser Glu Glu Asp Glu Glu Asp Asp 145 150 155 160 Glu Asp Glu Asp Glu Asp Glu Asp Glu Ile Glu Pro Ala Ala Met Lys 165 170 175 Ala Ala Ala Ala Ala Pro Ala Ser Glu Asp Glu Asp Asp Glu Asp Asp 180 185 190 Glu Asp Asp Glu Asp Asp Asp Asp Asp Glu Glu Asp Asp Ser Glu Glu 195 200 205 Glu Ala Met Glu Thr Thr Pro Ala Lys Gly Lys Lys Ala Ala Lys Val 210 215 220 Val Pro Val Lys Ala Lys Asn Val Ala Glu Asp Glu Asp Glu Glu Glu 225 230 235 240 Asp Asp Glu Asp Glu Asp Asp Asp Asp Asp Glu Asp Asp Glu Asp Asp 245 250 255 Asp Asp Glu Asp Asp Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Pro 260 265 270 Val Lys Glu Ala Pro Gly Lys Arg Lys Lys Glu Met Ala Lys Gln Lys 275 280 285 Ala Ala Pro Glu Ala Lys Lys Gln Lys Val Glu Gly Thr Glu Pro Thr 290 295 300 Thr Ala Phe Asn Leu Phe Val Gly Asn Leu Asn Phe Asn Lys Ser Ala 305 310 315 320 Pro Glu Leu Lys Thr Gly Ile Ser Asp Val Phe Ala Lys Asn Asp Leu 325 330 335 Ala Val Val Asp Val Arg Ile Gly Met Thr Arg Lys Phe Gly Tyr Val 340 345 350 Asp Phe Glu Ser Ala Glu Asp Leu Glu Lys Ala Leu Glu Leu Thr Gly 355 360 365 Leu Lys Val Phe Gly Asn Glu Ile Lys Leu Glu Lys Pro Lys Gly Lys 370 375 380 Asp Ser Lys Lys Glu Arg Asp Ala Arg Thr Leu Leu Ala Lys Asn Leu 385 390 395 400 Pro Tyr Lys Val Thr Gln Asp Glu Leu Lys Glu Val Phe Glu Asp Ala 405 410 415 Ala Glu Ile Arg Leu Val Ser Lys Asp Gly Lys Ser Lys Gly Ile Ala 420 425 430 Tyr Ile Glu Phe Lys Thr Glu Ala Asp Ala Glu Lys Thr Phe Glu Glu 435 440 445 Lys Gln Gly Thr Glu Ile Asp Gly Arg Ser Ile Ser Leu Tyr Tyr Thr 450 455 460 Gly Glu Lys Gly Gln Asn Gln Asp Tyr Arg Gly Gly Lys Asn Ser Thr 465 470 475 480 Trp Ser Gly Glu Ser Lys Thr Leu Val Leu Ser Asn Leu Ser Tyr Ser 485 490 495 Ala Thr Glu Glu Thr Leu Gln Glu Val Phe Glu Lys Ala Thr Phe Ile 500 505 510 Lys Val Pro Gln Asn Gln Asn Gly Lys Ser Lys Gly Tyr Ala Phe Ile 515 520 525 Glu Phe Ala Ser Phe Glu Asp Ala Lys Glu Ala Leu Asn Ser Cys Asn 530 535 540 Lys Arg Glu Ile Glu Gly Arg Ala Ile Arg Leu Glu Leu Gln Gly Pro 545 550 555 560 Arg Gly Ser Pro Asn Ala Arg Ser Gln Pro Ser Lys Thr Leu Phe Val 565 570 575 Lys Gly Leu Ser Glu Asp Thr Thr Glu Glu Thr Leu Lys Glu Ser Phe 580 585 590 Asp Gly Ser Val Arg Ala Arg Ile Val Thr Asp Arg Glu Thr Gly Ser 595 600 605 Ser Lys Gly Phe Gly Phe Val Asp Phe Asn Ser Glu Glu Asp Ala Lys 610 615 620 Ala Ala Lys Glu Ala Met Glu Asp Gly Glu Ile Asp Gly Asn Lys Val 625 630 635 640 Thr Leu Asp Trp Ala Lys Pro Lys Gly Glu Gly Gly Phe Gly Gly Arg 645 650 655 Gly Gly Gly Arg Gly Gly Phe Gly Gly Arg Gly Gly Gly Arg Gly Gly 660 665 670 Arg Gly Gly Phe Gly Gly Arg Gly Arg Gly Gly Phe Gly Gly Arg Gly 675 680 685 Gly Phe Arg Gly Gly Arg Gly Gly Gly Gly Asp His Lys Pro Gln Gly 690 695 700 Lys Lys Thr Lys Phe Glu 705 710 <210> SEQ ID NO 40 <211> LENGTH: 303 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BY49 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(303) <400> SEQUENCE: 40 Met Ala Ser Trp Ala Lys Gly Arg Ser Tyr Leu Ala Pro Gly Leu Leu 1 5 10 15 Gln Gly Gln Val Ala Ile Val Thr Gly Gly Ala Thr Gly Ile Gly Lys 20 25 30 Ala Ile Val Lys Glu Leu Leu Glu Leu Gly Ser Asn Val Val Ile Ala 35 40 45 Ser Arg Lys Leu Glu Arg Leu Lys Ser Ala Ala Asp Glu Leu Gln Ala 50 55 60 Asn Leu Pro Pro Thr Lys Gln Ala Arg Val Ile Pro Ile Gln Cys Asn 65 70 75 80 Ile Arg Asn Glu Glu Glu Val Asn Asn Leu Val Lys Ser Thr Leu Asp 85 90 95 Thr Phe Gly Lys Ile Asn Phe Leu Val Asn Asn Gly Gly Gly Gln Phe 100 105 110 Leu Ser Pro Ala Glu His Ile Ser Ser Lys Gly Trp His Ala Val Leu 115 120 125 Glu Thr Asn Leu Thr Gly Thr Phe Tyr Met Cys Lys Ala Val Tyr Ser 130 135 140 Ser Trp Met Lys Glu His Gly Gly Ser Ile Val Asn Ile Ile Val Pro 145 150 155 160 Thr Lys Ala Gly Phe Pro Leu Ala Val His Ser Gly Ala Ala Arg Ala 165 170 175 Gly Val Tyr Asn Leu Thr Lys Ser Leu Ala Leu Glu Trp Ala Cys Ser 180 185 190 Gly Ile Arg Ile Asn Cys Val Ala Pro Gly Val Ile Tyr Ser Gln Thr 195 200 205 Ala Val Glu Asn Tyr Gly Ser Trp Gly Gln Ser Phe Phe Glu Gly Ser 210 215 220 Phe Gln Lys Ile Pro Ala Lys Arg Ile Gly Val Pro Glu Glu Val Ser 225 230 235 240 Ser Val Val Cys Phe Leu Leu Ser Pro Ala Ala Ser Phe Ile Thr Gly 245 250 255 Gln Ser Val Asp Val Asp Gly Gly Arg Ser Leu Tyr Thr His Ser Tyr 260 265 270 Glu Val Pro Asp His Asp Asn Trp Pro Lys Gly Ala Gly Asp Leu Ser 275 280 285 Val Val Lys Lys Met Lys Glu Thr Phe Lys Glu Lys Ala Lys Leu 290 295 300 <210> SEQ ID NO 41 <211> LENGTH: 475 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P19474 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(475) <400> SEQUENCE: 41 Met Ala Ser Ala Ala Arg Leu Thr Met Met Trp Glu Glu Val Thr Cys 1 5 10 15 Pro Ile Cys Leu Asp Pro Phe Val Glu Pro Val Ser Ile Glu Cys Gly 20 25 30 His Ser Phe Cys Gln Glu Cys Ile Ser Gln Val Gly Lys Gly Gly Gly 35 40 45 Ser Val Cys Pro Val Cys Arg Gln Arg Phe Leu Leu Lys Asn Leu Arg 50 55 60 Pro Asn Arg Gln Leu Ala Asn Met Val Asn Asn Leu Lys Glu Ile Ser 65 70 75 80 Gln Glu Ala Arg Glu Gly Thr Gln Gly Glu Arg Cys Ala Val His Gly 85 90 95 Glu Arg Leu His Leu Phe Cys Glu Lys Asp Gly Lys Ala Leu Cys Trp 100 105 110 Val Cys Ala Gln Ser Arg Lys His Arg Asp His Ala Met Val Pro Leu 115 120 125 Glu Glu Ala Ala Gln Glu Tyr Gln Glu Lys Leu Gln Val Ala Leu Gly 130 135 140 Glu Leu Arg Arg Lys Gln Glu Leu Ala Glu Lys Leu Glu Val Glu Ile 145 150 155 160 Ala Ile Lys Arg Ala Asp Trp Lys Lys Thr Val Glu Thr Gln Lys Ser 165 170 175 Arg Ile His Ala Glu Phe Val Gln Gln Lys Asn Phe Leu Val Glu Glu 180 185 190 Glu Gln Arg Gln Leu Gln Glu Leu Glu Lys Asp Glu Arg Glu Gln Leu 195 200 205 Arg Ile Leu Gly Glu Lys Glu Ala Lys Leu Ala Gln Gln Ser Gln Ala 210 215 220 Leu Gln Glu Leu Ile Ser Glu Leu Asp Arg Arg Cys His Ser Ser Ala 225 230 235 240 Leu Glu Leu Leu Gln Glu Val Ile Ile Val Leu Glu Arg Ser Glu Ser 245 250 255 Trp Asn Leu Lys Asp Leu Asp Ile Thr Ser Pro Glu Leu Arg Ser Val 260 265 270 Cys His Val Pro Gly Leu Lys Lys Met Leu Arg Thr Cys Ala Val His 275 280 285 Ile Thr Leu Asp Pro Asp Thr Ala Asn Pro Trp Leu Ile Leu Ser Glu 290 295 300 Asp Arg Arg Gln Val Arg Leu Gly Asp Thr Gln Gln Ser Ile Pro Gly 305 310 315 320 Asn Glu Glu Arg Phe Asp Ser Tyr Pro Met Val Leu Gly Ala Gln His 325 330 335 Phe His Ser Gly Lys His Tyr Trp Glu Val Asp Val Thr Gly Lys Glu 340 345 350 Ala Trp Asp Leu Gly Val Cys Arg Asp Ser Val Arg Arg Lys Gly His 355 360 365 Phe Leu Leu Ser Ser Lys Ser Gly Phe Trp Thr Ile Trp Leu Trp Asn 370 375 380 Lys Gln Lys Tyr Glu Ala Gly Thr Tyr Pro Gln Thr Pro Leu His Leu 385 390 395 400 Gln Val Pro Pro Cys Gln Val Gly Ile Phe Leu Asp Tyr Glu Ala Gly 405 410 415 Met Val Ser Phe Tyr Asn Ile Thr Asp His Gly Ser Leu Ile Tyr Ser 420 425 430 Phe Ser Glu Cys Ala Phe Thr Gly Pro Leu Arg Pro Phe Phe Ser Pro 435 440 445 Gly Phe Asn Asp Gly Gly Lys Asn Thr Ala Pro Leu Thr Leu Cys Pro 450 455 460 Leu Asn Ile Gly Ser Gln Gly Ser Thr Asp Tyr 465 470 475 <210> SEQ ID NO 42 <211> LENGTH: 261 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P25789 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(261) <400> SEQUENCE: 42 Met Ser Arg Arg Tyr Asp Ser Arg Thr Thr Ile Phe Ser Pro Glu Gly 1 5 10 15 Arg Leu Tyr Gln Val Glu Tyr Ala Met Glu Ala Ile Gly His Ala Gly 20 25 30 Thr Cys Leu Gly Ile Leu Ala Asn Asp Gly Val Leu Leu Ala Ala Glu 35 40 45 Arg Arg Asn Ile His Lys Leu Leu Asp Glu Val Phe Phe Ser Glu Lys 50 55 60 Ile Tyr Lys Leu Asn Glu Asp Met Ala Cys Ser Val Ala Gly Ile Thr 65 70 75 80 Ser Asp Ala Asn Val Leu Thr Asn Glu Leu Arg Leu Ile Ala Gln Arg 85 90 95 Tyr Leu Leu Gln Tyr Gln Glu Pro Ile Pro Cys Glu Gln Leu Val Thr 100 105 110 Ala Leu Cys Asp Ile Lys Gln Ala Tyr Thr Gln Phe Gly Gly Lys Arg 115 120 125 Pro Phe Gly Val Ser Leu Leu Tyr Ile Gly Trp Asp Lys His Tyr Gly 130 135 140 Phe Gln Leu Tyr Gln Ser Asp Pro Ser Gly Asn Tyr Gly Gly Trp Lys 145 150 155 160 Ala Thr Cys Ile Gly Asn Asn Ser Ala Ala Ala Val Ser Met Leu Lys 165 170 175 Gln Asp Tyr Lys Glu Gly Glu Met Thr Leu Lys Ser Ala Leu Ala Leu 180 185 190 Ala Ile Lys Val Leu Asn Lys Thr Met Asp Val Ser Lys Leu Ser Ala 195 200 205 Glu Lys Val Glu Ile Ala Thr Leu Thr Arg Glu Asn Gly Lys Thr Val 210 215 220 Ile Arg Val Leu Lys Gln Lys Glu Val Glu Gln Leu Ile Lys Lys His 225 230 235 240 Glu Glu Glu Glu Ala Lys Ala Glu Arg Glu Lys Lys Glu Lys Glu Gln 245 250 255 Lys Glu Lys Asp Lys 260 <210> SEQ ID NO 43 <211> LENGTH: 295 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P13726 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(295) <400> SEQUENCE: 43 Met Glu Thr Pro Ala Trp Pro Arg Val Pro Arg Pro Glu Thr Ala Val 1 5 10 15 Ala Arg Thr Leu Leu Leu Gly Trp Val Phe Ala Gln Val Ala Gly Ala 20 25 30 Ser Gly Thr Thr Asn Thr Val Ala Ala Tyr Asn Leu Thr Trp Lys Ser 35 40 45 Thr Asn Phe Lys Thr Ile Leu Glu Trp Glu Pro Lys Pro Val Asn Gln 50 55 60 Val Tyr Thr Val Gln Ile Ser Thr Lys Ser Gly Asp Trp Lys Ser Lys 65 70 75 80 Cys Phe Tyr Thr Thr Asp Thr Glu Cys Asp Leu Thr Asp Glu Ile Val 85 90 95 Lys Asp Val Lys Gln Thr Tyr Leu Ala Arg Val Phe Ser Tyr Pro Ala 100 105 110 Gly Asn Val Glu Ser Thr Gly Ser Ala Gly Glu Pro Leu Tyr Glu Asn 115 120 125 Ser Pro Glu Phe Thr Pro Tyr Leu Glu Thr Asn Leu Gly Gln Pro Thr 130 135 140 Ile Gln Ser Phe Glu Gln Val Gly Thr Lys Val Asn Val Thr Val Glu 145 150 155 160 Asp Glu Arg Thr Leu Val Arg Arg Asn Asn Thr Phe Leu Ser Leu Arg 165 170 175 Asp Val Phe Gly Lys Asp Leu Ile Tyr Thr Leu Tyr Tyr Trp Lys Ser 180 185 190 Ser Ser Ser Gly Lys Lys Thr Ala Lys Thr Asn Thr Asn Glu Phe Leu 195 200 205 Ile Asp Val Asp Lys Gly Glu Asn Tyr Cys Phe Ser Val Gln Ala Val 210 215 220 Ile Pro Ser Arg Thr Val Asn Arg Lys Ser Thr Asp Ser Pro Val Glu 225 230 235 240 Cys Met Gly Gln Glu Lys Gly Glu Phe Arg Glu Ile Phe Tyr Ile Ile 245 250 255 Gly Ala Val Val Phe Val Val Ile Ile Leu Val Ile Ile Leu Ala Ile 260 265 270 Ser Leu His Lys Cys Arg Lys Ala Gly Val Gly Gln Ser Trp Lys Glu 275 280 285 Asn Ser Pro Leu Asn Val Ser 290 295 <210> SEQ ID NO 44 <211> LENGTH: 538 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P10155 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(538) <400> SEQUENCE: 44 Met Glu Glu Ser Val Asn Gln Met Gln Pro Leu Asn Glu Lys Gln Ile 1 5 10 15 Ala Asn Ser Gln Asp Gly Tyr Val Trp Gln Val Thr Asp Met Asn Arg 20 25 30 Leu His Arg Phe Leu Cys Phe Gly Ser Glu Gly Gly Thr Tyr Tyr Ile 35 40 45 Lys Glu Gln Lys Leu Gly Leu Glu Asn Ala Glu Ala Leu Ile Arg Leu 50 55 60 Ile Glu Asp Gly Arg Gly Cys Glu Val Ile Gln Glu Ile Lys Ser Phe 65 70 75 80 Ser Gln Glu Gly Arg Thr Thr Lys Gln Glu Pro Met Leu Phe Ala Leu 85 90 95 Ala Ile Cys Ser Gln Cys Ser Asp Ile Ser Thr Lys Gln Ala Ala Phe 100 105 110 Lys Ala Val Ser Glu Val Cys Arg Ile Pro Thr His Leu Phe Thr Phe 115 120 125 Ile Gln Phe Lys Lys Asp Leu Lys Glu Ser Met Lys Cys Gly Met Trp 130 135 140 Gly Arg Ala Leu Arg Lys Ala Ile Ala Asp Trp Tyr Asn Glu Lys Gly 145 150 155 160 Gly Met Ala Leu Ala Leu Ala Val Thr Lys Tyr Lys Gln Arg Asn Gly 165 170 175 Trp Ser His Lys Asp Leu Leu Arg Leu Ser His Leu Lys Pro Ser Ser 180 185 190 Glu Gly Leu Ala Ile Val Thr Lys Tyr Ile Thr Lys Gly Trp Lys Glu 195 200 205 Val His Glu Leu Tyr Lys Glu Lys Ala Leu Ser Val Glu Thr Glu Lys 210 215 220 Leu Leu Lys Tyr Leu Glu Ala Val Glu Lys Val Lys Arg Thr Arg Asp 225 230 235 240 Glu Leu Glu Val Ile His Leu Ile Glu Glu His Arg Leu Val Arg Glu 245 250 255 His Leu Leu Thr Asn His Leu Lys Ser Lys Glu Val Trp Lys Ala Leu 260 265 270 Leu Gln Glu Met Pro Leu Thr Ala Leu Leu Arg Asn Leu Gly Lys Met 275 280 285 Thr Ala Asn Ser Val Leu Glu Pro Gly Asn Ser Glu Val Ser Leu Val 290 295 300 Cys Glu Lys Leu Cys Asn Glu Lys Leu Leu Lys Lys Ala Arg Ile His 305 310 315 320 Pro Phe His Ile Leu Ile Ala Leu Glu Thr Tyr Lys Thr Gly His Gly 325 330 335 Leu Arg Gly Lys Leu Lys Trp Arg Pro Asp Glu Glu Ile Leu Lys Ala 340 345 350 Leu Asp Ala Ala Phe Tyr Lys Thr Phe Lys Thr Val Glu Pro Thr Gly 355 360 365 Lys Arg Phe Leu Leu Ala Val Asp Val Ser Ala Ser Met Asn Gln Arg 370 375 380 Val Leu Gly Ser Ile Leu Asn Ala Ser Thr Val Ala Ala Ala Met Cys 385 390 395 400 Met Val Val Thr Arg Thr Glu Lys Asp Ser Tyr Val Val Ala Phe Ser 405 410 415 Asp Glu Met Val Pro Cys Pro Val Thr Thr Asp Met Thr Leu Gln Gln 420 425 430 Val Leu Met Ala Met Ser Gln Ile Pro Ala Gly Gly Thr Asp Cys Ser 435 440 445 Leu Pro Met Ile Trp Ala Gln Lys Thr Asn Thr Pro Ala Asp Val Phe 450 455 460 Ile Val Phe Thr Asp Asn Glu Thr Phe Ala Gly Gly Val His Pro Ala 465 470 475 480 Ile Ala Leu Arg Glu Tyr Arg Lys Lys Met Asp Ile Pro Ala Lys Leu 485 490 495 Ile Val Cys Gly Met Thr Ser Asn Gly Phe Thr Ile Ala Asp Pro Asp 500 505 510 Asp Arg Gly Met Leu Asp Met Cys Gly Phe Asp Thr Gly Ala Leu Asp 515 520 525 Val Ile Arg Asn Phe Thr Leu Asp Met Ile 530 535 <210> SEQ ID NO 45 <211> LENGTH: 1025 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BYX4 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1025) <400> SEQUENCE: 45 Met Ser Asn Gly Tyr Ser Thr Asp Glu Asn Phe Arg Tyr Leu Ile Ser 1 5 10 15 Cys Phe Arg Ala Arg Val Lys Met Tyr Ile Gln Val Glu Pro Val Leu 20 25 30 Asp Tyr Leu Thr Phe Leu Pro Ala Glu Val Lys Glu Gln Ile Gln Arg 35 40 45 Thr Val Ala Thr Ser Gly Asn Met Gln Ala Val Glu Leu Leu Leu Ser 50 55 60 Thr Leu Glu Lys Gly Val Trp His Leu Gly Trp Thr Arg Glu Phe Val 65 70 75 80 Glu Ala Leu Arg Arg Thr Gly Ser Pro Leu Ala Ala Arg Tyr Met Asn 85 90 95 Pro Glu Leu Thr Asp Leu Pro Ser Pro Ser Phe Glu Asn Ala His Asp 100 105 110 Glu Tyr Leu Gln Leu Leu Asn Leu Leu Gln Pro Thr Leu Val Asp Lys 115 120 125 Leu Leu Val Arg Asp Val Leu Asp Lys Cys Met Glu Glu Glu Leu Leu 130 135 140 Thr Ile Glu Asp Arg Asn Arg Ile Ala Ala Ala Glu Asn Asn Gly Asn 145 150 155 160 Glu Ser Gly Val Arg Glu Leu Leu Lys Arg Ile Val Gln Lys Glu Asn 165 170 175 Trp Phe Ser Ala Phe Leu Asn Val Leu Arg Gln Thr Gly Asn Asn Glu 180 185 190 Leu Val Gln Glu Leu Thr Gly Ser Asp Cys Ser Glu Ser Asn Ala Glu 195 200 205 Ile Glu Asn Leu Ser Gln Val Asp Gly Pro Gln Val Glu Glu Gln Leu 210 215 220 Leu Ser Thr Thr Val Gln Pro Asn Leu Glu Lys Glu Val Trp Gly Met 225 230 235 240 Glu Asn Asn Ser Ser Glu Ser Ser Phe Ala Asp Ser Ser Val Val Ser 245 250 255 Glu Ser Asp Thr Ser Leu Ala Glu Gly Ser Val Ser Cys Leu Asp Glu 260 265 270 Ser Leu Gly His Asn Ser Asn Met Gly Ser Asp Ser Gly Thr Met Gly 275 280 285 Ser Asp Ser Asp Glu Glu Asn Val Ala Ala Arg Ala Ser Pro Glu Pro 290 295 300 Glu Leu Gln Leu Arg Pro Tyr Gln Met Glu Val Ala Gln Pro Ala Leu 305 310 315 320 Glu Gly Lys Asn Ile Ile Ile Cys Leu Pro Thr Gly Ser Gly Lys Thr 325 330 335 Arg Val Ala Val Tyr Ile Ala Lys Asp His Leu Asp Lys Lys Lys Lys 340 345 350 Ala Ser Glu Pro Gly Lys Val Ile Val Leu Val Asn Lys Val Leu Leu 355 360 365 Val Glu Gln Leu Phe Arg Lys Glu Phe Gln Pro Phe Leu Lys Lys Trp 370 375 380 Tyr Arg Val Ile Gly Leu Ser Gly Asp Thr Gln Leu Lys Ile Ser Phe 385 390 395 400 Pro Glu Val Val Lys Ser Cys Asp Ile Ile Ile Ser Thr Ala Gln Ile 405 410 415 Leu Glu Asn Ser Leu Leu Asn Leu Glu Asn Gly Glu Asp Ala Gly Val 420 425 430 Gln Leu Ser Asp Phe Ser Leu Ile Ile Ile Asp Glu Cys His His Thr 435 440 445 Asn Lys Glu Ala Val Tyr Asn Asn Ile Met Arg His Tyr Leu Met Gln 450 455 460 Lys Leu Lys Asn Asn Arg Leu Lys Lys Glu Asn Lys Pro Val Ile Pro 465 470 475 480 Leu Pro Gln Ile Leu Gly Leu Thr Ala Ser Pro Gly Val Gly Gly Ala 485 490 495 Thr Lys Gln Ala Lys Ala Glu Glu His Ile Leu Lys Leu Cys Ala Asn 500 505 510 Leu Asp Ala Phe Thr Ile Lys Thr Val Lys Glu Asn Leu Asp Gln Leu 515 520 525 Lys Asn Gln Ile Gln Glu Pro Cys Lys Lys Phe Ala Ile Ala Asp Ala 530 535 540 Thr Arg Glu Asp Pro Phe Lys Glu Lys Leu Leu Glu Ile Met Thr Arg 545 550 555 560 Ile Gln Thr Tyr Cys Gln Met Ser Pro Met Ser Asp Phe Gly Thr Gln 565 570 575 Pro Tyr Glu Gln Trp Ala Ile Gln Met Glu Lys Lys Ala Ala Lys Glu 580 585 590 Gly Asn Arg Lys Glu Arg Val Cys Ala Glu His Leu Arg Lys Tyr Asn 595 600 605 Glu Ala Leu Gln Ile Asn Asp Thr Ile Arg Met Ile Asp Ala Tyr Thr 610 615 620 His Leu Glu Thr Phe Tyr Asn Glu Glu Lys Asp Lys Lys Phe Ala Val 625 630 635 640 Ile Glu Asp Asp Ser Asp Glu Gly Gly Asp Asp Glu Tyr Cys Asp Gly 645 650 655 Asp Glu Asp Glu Asp Asp Leu Lys Lys Pro Leu Lys Leu Asp Glu Thr 660 665 670 Asp Arg Phe Leu Met Thr Leu Phe Phe Glu Asn Asn Lys Met Leu Lys 675 680 685 Arg Leu Ala Glu Asn Pro Glu Tyr Glu Asn Glu Lys Leu Thr Lys Leu 690 695 700 Arg Asn Thr Ile Met Glu Gln Tyr Thr Arg Thr Glu Glu Ser Ala Arg 705 710 715 720 Gly Ile Ile Phe Thr Lys Thr Arg Gln Ser Ala Tyr Ala Leu Ser Gln 725 730 735 Trp Ile Thr Glu Asn Glu Lys Phe Ala Glu Val Gly Val Lys Ala His 740 745 750 His Leu Ile Gly Ala Gly His Ser Ser Glu Phe Lys Pro Met Thr Gln 755 760 765 Asn Glu Gln Lys Glu Val Ile Ser Lys Phe Arg Thr Gly Lys Ile Asn 770 775 780 Leu Leu Ile Ala Thr Thr Val Ala Glu Glu Gly Leu Asp Ile Lys Glu 785 790 795 800 Cys Asn Ile Val Ile Arg Tyr Gly Leu Val Thr Asn Glu Ile Ala Met 805 810 815 Val Gln Ala Arg Gly Arg Ala Arg Ala Asp Glu Ser Thr Tyr Val Leu 820 825 830 Val Ala His Ser Gly Ser Gly Val Ile Glu His Glu Thr Val Asn Asp 835 840 845 Phe Arg Glu Lys Met Met Tyr Lys Ala Ile His Cys Val Gln Asn Met 850 855 860 Lys Pro Glu Glu Tyr Ala His Lys Ile Leu Glu Leu Gln Met Gln Ser 865 870 875 880 Ile Met Glu Lys Lys Met Lys Thr Lys Arg Asn Ile Ala Lys His Tyr 885 890 895 Lys Asn Asn Pro Ser Leu Ile Thr Phe Leu Cys Lys Asn Cys Ser Val 900 905 910 Leu Ala Cys Ser Gly Glu Asp Ile His Val Ile Glu Lys Met His His 915 920 925 Val Asn Met Thr Pro Glu Phe Lys Glu Leu Tyr Ile Val Arg Glu Asn 930 935 940 Lys Ala Leu Gln Lys Lys Cys Ala Asp Tyr Gln Ile Asn Gly Glu Ile 945 950 955 960 Ile Cys Lys Cys Gly Gln Ala Trp Gly Thr Met Met Val His Lys Gly 965 970 975 Leu Asp Leu Pro Cys Leu Lys Ile Arg Asn Phe Val Val Val Phe Lys 980 985 990 Asn Asn Ser Thr Lys Lys Gln Tyr Lys Lys Trp Val Glu Leu Pro Ile 995 1000 1005 Thr Phe Pro Asn Leu Asp Tyr Ser Glu Cys Cys Leu Phe Ser Asp 1010 1015 1020 Glu Asp 1025 <210> SEQ ID NO 46 <211> LENGTH: 451 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q71U36 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(451) <400> SEQUENCE: 46 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro 20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Gly Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Ser Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Thr Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Ile 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Val Asp Ser Val Glu Gly Glu Gly Glu Glu Glu Gly 435 440 445 Glu Glu Tyr 450 <210> SEQ ID NO 47 <211> LENGTH: 451 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P68363 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(451) <400> SEQUENCE: 47 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro 20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Ser Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Ser Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Ser Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Ile 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Val Asp Ser Val Glu Gly Glu Gly Glu Glu Glu Gly 435 440 445 Glu Glu Tyr 450 <210> SEQ ID NO 48 <211> LENGTH: 449 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BQE3 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(449) <400> SEQUENCE: 48 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro 20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Ser Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Thr Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Thr Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Val 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Ala Asp Ser Ala Asp Gly Glu Asp Glu Gly Glu Glu 435 440 445 Tyr <210> SEQ ID NO 49 <211> LENGTH: 444 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P07437 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(444) <400> SEQUENCE: 49 Met Arg Glu Ile Val His Ile Gln Ala Gly Gln Cys Gly Asn Gln Ile 1 5 10 15 Gly Ala Lys Phe Trp Glu Val Ile Ser Asp Glu His Gly Ile Asp Pro 20 25 30 Thr Gly Thr Tyr His Gly Asp Ser Asp Leu Gln Leu Asp Arg Ile Ser 35 40 45 Val Tyr Tyr Asn Glu Ala Thr Gly Gly Lys Tyr Val Pro Arg Ala Ile 50 55 60 Leu Val Asp Leu Glu Pro Gly Thr Met Asp Ser Val Arg Ser Gly Pro 65 70 75 80 Phe Gly Gln Ile Phe Arg Pro Asp Asn Phe Val Phe Gly Gln Ser Gly 85 90 95 Ala Gly Asn Asn Trp Ala Lys Gly His Tyr Thr Glu Gly Ala Glu Leu 100 105 110 Val Asp Ser Val Leu Asp Val Val Arg Lys Glu Ala Glu Ser Cys Asp 115 120 125 Cys Leu Gln Gly Phe Gln Leu Thr His Ser Leu Gly Gly Gly Thr Gly 130 135 140 Ser Gly Met Gly Thr Leu Leu Ile Ser Lys Ile Arg Glu Glu Tyr Pro 145 150 155 160 Asp Arg Ile Met Asn Thr Phe Ser Val Val Pro Ser Pro Lys Val Ser 165 170 175 Asp Thr Val Val Glu Pro Tyr Asn Ala Thr Leu Ser Val His Gln Leu 180 185 190 Val Glu Asn Thr Asp Glu Thr Tyr Cys Ile Asp Asn Glu Ala Leu Tyr 195 200 205 Asp Ile Cys Phe Arg Thr Leu Lys Leu Thr Thr Pro Thr Tyr Gly Asp 210 215 220 Leu Asn His Leu Val Ser Ala Thr Met Ser Gly Val Thr Thr Cys Leu 225 230 235 240 Arg Phe Pro Gly Gln Leu Asn Ala Asp Leu Arg Lys Leu Ala Val Asn 245 250 255 Met Val Pro Phe Pro Arg Leu His Phe Phe Met Pro Gly Phe Ala Pro 260 265 270 Leu Thr Ser Arg Gly Ser Gln Gln Tyr Arg Ala Leu Thr Val Pro Glu 275 280 285 Leu Thr Gln Gln Val Phe Asp Ala Lys Asn Met Met Ala Ala Cys Asp 290 295 300 Pro Arg His Gly Arg Tyr Leu Thr Val Ala Ala Val Phe Arg Gly Arg 305 310 315 320 Met Ser Met Lys Glu Val Asp Glu Gln Met Leu Asn Val Gln Asn Lys 325 330 335 Asn Ser Ser Tyr Phe Val Glu Trp Ile Pro Asn Asn Val Lys Thr Ala 340 345 350 Val Cys Asp Ile Pro Pro Arg Gly Leu Lys Met Ala Val Thr Phe Ile 355 360 365 Gly Asn Ser Thr Ala Ile Gln Glu Leu Phe Lys Arg Ile Ser Glu Gln 370 375 380 Phe Thr Ala Met Phe Arg Arg Lys Ala Phe Leu His Trp Tyr Thr Gly 385 390 395 400 Glu Gly Met Asp Glu Met Glu Phe Thr Glu Ala Glu Ser Asn Met Asn 405 410 415 Asp Leu Val Ser Glu Tyr Gln Gln Tyr Gln Asp Ala Thr Ala Glu Glu 420 425 430 Glu Glu Asp Phe Gly Glu Glu Ala Glu Glu Glu Ala 435 440 <210> SEQ ID NO 50 <211> LENGTH: 4391 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P98160 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(4391) <400> SEQUENCE: 50 Met Gly Trp Arg Ala Ala Gly Ala Leu Leu Leu Ala Leu Leu Leu His 1 5 10 15 Gly Arg Leu Leu Ala Val Thr His Gly Leu Arg Ala Tyr Asp Gly Leu 20 25 30 Ser Leu Pro Glu Asp Ile Glu Thr Val Thr Ala Ser Gln Met Arg Trp 35 40 45 Thr His Ser Tyr Leu Ser Asp Asp Glu Asp Met Leu Ala Asp Ser Ile 50 55 60 Ser Gly Asp Asp Leu Gly Ser Gly Asp Leu Gly Ser Gly Asp Phe Gln 65 70 75 80 Met Val Tyr Phe Arg Ala Leu Val Asn Phe Thr Arg Ser Ile Glu Tyr 85 90 95 Ser Pro Gln Leu Glu Asp Ala Gly Ser Arg Glu Phe Arg Glu Val Ser 100 105 110 Glu Ala Val Val Asp Thr Leu Glu Ser Glu Tyr Leu Lys Ile Pro Gly 115 120 125 Asp Gln Val Val Ser Val Val Phe Ile Lys Glu Leu Asp Gly Trp Val 130 135 140 Phe Val Glu Leu Asp Val Gly Ser Glu Gly Asn Ala Asp Gly Ala Gln 145 150 155 160 Ile Gln Glu Met Leu Leu Arg Val Ile Ser Ser Gly Ser Val Ala Ser 165 170 175 Tyr Val Thr Ser Pro Gln Gly Phe Gln Phe Arg Arg Leu Gly Thr Val 180 185 190 Pro Gln Phe Pro Arg Ala Cys Thr Glu Ala Glu Phe Ala Cys His Ser 195 200 205 Tyr Asn Glu Cys Val Ala Leu Glu Tyr Arg Cys Asp Arg Arg Pro Asp 210 215 220 Cys Arg Asp Met Ser Asp Glu Leu Asn Cys Glu Glu Pro Val Leu Gly 225 230 235 240 Ile Ser Pro Thr Phe Ser Leu Leu Val Glu Thr Thr Ser Leu Pro Pro 245 250 255 Arg Pro Glu Thr Thr Ile Met Arg Gln Pro Pro Val Thr His Ala Pro 260 265 270 Gln Pro Leu Leu Pro Gly Ser Val Arg Pro Leu Pro Cys Gly Pro Gln 275 280 285 Glu Ala Ala Cys Arg Asn Gly His Cys Ile Pro Arg Asp Tyr Leu Cys 290 295 300 Asp Gly Gln Glu Asp Cys Glu Asp Gly Ser Asp Glu Leu Asp Cys Gly 305 310 315 320 Pro Pro Pro Pro Cys Glu Pro Asn Glu Phe Pro Cys Gly Asn Gly His 325 330 335 Cys Ala Leu Lys Leu Trp Arg Cys Asp Gly Asp Phe Asp Cys Glu Asp 340 345 350 Arg Thr Asp Glu Ala Asn Cys Pro Thr Lys Arg Pro Glu Glu Val Cys 355 360 365 Gly Pro Thr Gln Phe Arg Cys Val Ser Thr Asn Met Cys Ile Pro Ala 370 375 380 Ser Phe His Cys Asp Glu Glu Ser Asp Cys Pro Asp Arg Ser Asp Glu 385 390 395 400 Phe Gly Cys Met Pro Pro Gln Val Val Thr Pro Pro Arg Glu Ser Ile 405 410 415 Gln Ala Ser Arg Gly Gln Thr Val Thr Phe Thr Cys Val Ala Ile Gly 420 425 430 Val Pro Thr Pro Ile Ile Asn Trp Arg Leu Asn Trp Gly His Ile Pro 435 440 445 Ser His Pro Arg Val Thr Val Thr Ser Glu Gly Gly Arg Gly Thr Leu 450 455 460 Ile Ile Arg Asp Val Lys Glu Ser Asp Gln Gly Ala Tyr Thr Cys Glu 465 470 475 480 Ala Met Asn Ala Arg Gly Met Val Phe Gly Ile Pro Asp Gly Val Leu 485 490 495 Glu Leu Val Pro Gln Arg Gly Pro Cys Pro Asp Gly His Phe Tyr Leu 500 505 510 Glu His Ser Ala Ala Cys Leu Pro Cys Phe Cys Phe Gly Ile Thr Ser 515 520 525 Val Cys Gln Ser Thr Arg Arg Phe Arg Asp Gln Ile Arg Leu Arg Phe 530 535 540 Asp Gln Pro Asp Asp Phe Lys Gly Val Asn Val Thr Met Pro Ala Gln 545 550 555 560 Pro Gly Thr Pro Pro Leu Ser Ser Thr Gln Leu Gln Ile Asp Pro Ser 565 570 575 Leu His Glu Phe Gln Leu Val Asp Leu Ser Arg Arg Phe Leu Val His 580 585 590 Asp Ser Phe Trp Ala Leu Pro Glu Gln Phe Leu Gly Asn Lys Val Asp 595 600 605 Ser Tyr Gly Gly Ser Leu Arg Tyr Asn Val Arg Tyr Glu Leu Ala Arg 610 615 620 Gly Met Leu Glu Pro Val Gln Arg Pro Asp Val Val Leu Met Gly Ala 625 630 635 640 Gly Tyr Arg Leu Leu Ser Arg Gly His Thr Pro Thr Gln Pro Gly Ala 645 650 655 Leu Asn Gln Arg Gln Val Gln Phe Ser Glu Glu His Trp Val His Glu 660 665 670 Ser Gly Arg Pro Val Gln Arg Ala Glu Leu Leu Gln Val Leu Gln Ser 675 680 685 Leu Glu Ala Val Leu Ile Gln Thr Val Tyr Asn Thr Lys Met Ala Ser 690 695 700 Val Gly Leu Ser Asp Ile Ala Met Asp Thr Thr Val Thr His Ala Thr 705 710 715 720 Ser His Gly Arg Ala His Ser Val Glu Glu Cys Arg Cys Pro Ile Gly 725 730 735 Tyr Ser Gly Leu Ser Cys Glu Ser Cys Asp Ala His Phe Thr Arg Val 740 745 750 Pro Gly Gly Pro Tyr Leu Gly Thr Cys Ser Gly Cys Asn Cys Asn Gly 755 760 765 His Ala Ser Ser Cys Asp Pro Val Tyr Gly His Cys Leu Asn Cys Gln 770 775 780 His Asn Thr Glu Gly Pro Gln Cys Asn Lys Cys Lys Ala Gly Phe Phe 785 790 795 800 Gly Asp Ala Met Lys Ala Thr Ala Thr Ser Cys Arg Pro Cys Pro Cys 805 810 815 Pro Tyr Ile Asp Ala Ser Arg Arg Phe Ser Asp Thr Cys Phe Leu Asp 820 825 830 Thr Asp Gly Gln Ala Thr Cys Asp Ala Cys Ala Pro Gly Tyr Thr Gly 835 840 845 Arg Arg Cys Glu Ser Cys Ala Pro Gly Tyr Glu Gly Asn Pro Ile Gln 850 855 860 Pro Gly Gly Lys Cys Arg Pro Val Asn Gln Glu Ile Val Arg Cys Asp 865 870 875 880 Glu Arg Gly Ser Met Gly Thr Ser Gly Glu Ala Cys Arg Cys Lys Asn 885 890 895 Asn Val Val Gly Arg Leu Cys Asn Glu Cys Ala Asp Gly Ser Phe His 900 905 910 Leu Ser Thr Arg Asn Pro Asp Gly Cys Leu Lys Cys Phe Cys Met Gly 915 920 925 Val Ser Arg His Cys Thr Ser Ser Ser Trp Ser Arg Ala Gln Leu His 930 935 940 Gly Ala Ser Glu Glu Pro Gly His Phe Ser Leu Thr Asn Ala Ala Ser 945 950 955 960 Thr His Thr Thr Asn Glu Gly Ile Phe Ser Pro Thr Pro Gly Glu Leu 965 970 975 Gly Phe Ser Ser Phe His Arg Leu Leu Ser Gly Pro Tyr Phe Trp Ser 980 985 990 Leu Pro Ser Arg Phe Leu Gly Asp Lys Val Thr Ser Tyr Gly Gly Glu 995 1000 1005 Leu Arg Phe Thr Val Thr Gln Arg Ser Gln Pro Gly Ser Thr Pro 1010 1015 1020 Leu His Gly Gln Pro Leu Val Val Leu Gln Gly Asn Asn Ile Ile 1025 1030 1035 Leu Glu His His Val Ala Gln Glu Pro Ser Pro Gly Gln Pro Ser 1040 1045 1050 Thr Phe Ile Val Pro Phe Arg Glu Gln Ala Trp Gln Arg Pro Asp 1055 1060 1065 Gly Gln Pro Ala Thr Arg Glu His Leu Leu Met Ala Leu Ala Gly 1070 1075 1080 Ile Asp Thr Leu Leu Ile Arg Ala Ser Tyr Ala Gln Gln Pro Ala 1085 1090 1095 Glu Ser Arg Val Ser Gly Ile Ser Met Asp Val Ala Val Pro Glu 1100 1105 1110 Glu Thr Gly Gln Asp Pro Ala Leu Glu Val Glu Gln Cys Ser Cys 1115 1120 1125 Pro Pro Gly Tyr Arg Gly Pro Ser Cys Gln Asp Cys Asp Thr Gly 1130 1135 1140 Tyr Thr Arg Thr Pro Ser Gly Leu Tyr Leu Gly Thr Cys Glu Arg 1145 1150 1155 Cys Ser Cys His Gly His Ser Glu Ala Cys Glu Pro Glu Thr Gly 1160 1165 1170 Ala Cys Gln Gly Cys Gln His His Thr Glu Gly Pro Arg Cys Glu 1175 1180 1185 Gln Cys Gln Pro Gly Tyr Tyr Gly Asp Ala Gln Arg Gly Thr Pro 1190 1195 1200 Gln Asp Cys Gln Leu Cys Pro Cys Tyr Gly Asp Pro Ala Ala Gly 1205 1210 1215 Gln Ala Ala His Thr Cys Phe Leu Asp Thr Asp Gly His Pro Thr 1220 1225 1230 Cys Asp Ala Cys Ser Pro Gly His Ser Gly Arg His Cys Glu Arg 1235 1240 1245 Cys Ala Pro Gly Tyr Tyr Gly Asn Pro Ser Gln Gly Gln Pro Cys 1250 1255 1260 Gln Arg Asp Ser Gln Val Pro Gly Pro Ile Gly Cys Asn Cys Asp 1265 1270 1275 Pro Gln Gly Ser Val Ser Ser Gln Cys Asp Ala Ala Gly Gln Cys 1280 1285 1290 Gln Cys Lys Ala Gln Val Glu Gly Leu Thr Cys Ser His Cys Arg 1295 1300 1305 Pro His His Phe His Leu Ser Ala Ser Asn Pro Asp Gly Cys Leu 1310 1315 1320 Pro Cys Phe Cys Met Gly Ile Thr Gln Gln Cys Ala Ser Ser Ala 1325 1330 1335 Tyr Thr Arg His Leu Ile Ser Thr His Phe Ala Pro Gly Asp Phe 1340 1345 1350 Gln Gly Phe Ala Leu Val Asn Pro Gln Arg Asn Ser Arg Leu Thr 1355 1360 1365 Gly Glu Phe Thr Val Glu Pro Val Pro Glu Gly Ala Gln Leu Ser 1370 1375 1380 Phe Gly Asn Phe Ala Gln Leu Gly His Glu Ser Phe Tyr Trp Gln 1385 1390 1395 Leu Pro Glu Thr Tyr Gln Gly Asp Lys Val Ala Ala Tyr Gly Gly 1400 1405 1410 Lys Leu Arg Tyr Thr Leu Ser Tyr Thr Ala Gly Pro Gln Gly Ser 1415 1420 1425 Pro Leu Ser Asp Pro Asp Val Gln Ile Thr Gly Asn Asn Ile Met 1430 1435 1440 Leu Val Ala Ser Gln Pro Ala Leu Gln Gly Pro Glu Arg Arg Ser 1445 1450 1455 Tyr Glu Ile Met Phe Arg Glu Glu Phe Trp Arg Arg Pro Asp Gly 1460 1465 1470 Gln Pro Ala Thr Arg Glu His Leu Leu Met Ala Leu Ala Asp Leu 1475 1480 1485 Asp Glu Leu Leu Ile Arg Ala Thr Phe Ser Ser Val Pro Leu Ala 1490 1495 1500 Ala Ser Ile Ser Ala Val Ser Leu Glu Val Ala Gln Pro Gly Pro 1505 1510 1515 Ser Asn Arg Pro Arg Ala Leu Glu Val Glu Glu Cys Arg Cys Pro 1520 1525 1530 Pro Gly Tyr Ile Gly Leu Ser Cys Gln Asp Cys Ala Pro Gly Tyr 1535 1540 1545 Thr Arg Thr Gly Ser Gly Leu Tyr Leu Gly His Cys Glu Leu Cys 1550 1555 1560 Glu Cys Asn Gly His Ser Asp Leu Cys His Pro Glu Thr Gly Ala 1565 1570 1575 Cys Ser Gln Cys Gln His Asn Ala Ala Gly Glu Phe Cys Glu Leu 1580 1585 1590 Cys Ala Pro Gly Tyr Tyr Gly Asp Ala Thr Ala Gly Thr Pro Glu 1595 1600 1605 Asp Cys Gln Pro Cys Ala Cys Pro Leu Thr Asn Pro Glu Asn Met 1610 1615 1620 Phe Ser Arg Thr Cys Glu Ser Leu Gly Ala Gly Gly Tyr Arg Cys 1625 1630 1635 Thr Ala Cys Glu Pro Gly Tyr Thr Gly Gln Tyr Cys Glu Gln Cys 1640 1645 1650 Gly Pro Gly Tyr Val Gly Asn Pro Ser Val Gln Gly Gly Gln Cys 1655 1660 1665 Leu Pro Glu Thr Asn Gln Ala Pro Leu Val Val Glu Val His Pro 1670 1675 1680 Ala Arg Ser Ile Val Pro Gln Gly Gly Ser His Ser Leu Arg Cys 1685 1690 1695 Gln Val Ser Gly Ser Pro Pro His Tyr Phe Tyr Trp Ser Arg Glu 1700 1705 1710 Asp Gly Arg Pro Val Pro Ser Gly Thr Gln Gln Arg His Gln Gly 1715 1720 1725 Ser Glu Leu His Phe Pro Ser Val Gln Pro Ser Asp Ala Gly Val 1730 1735 1740 Tyr Ile Cys Thr Cys Arg Asn Leu His Gln Ser Asn Thr Ser Arg 1745 1750 1755 Ala Glu Leu Leu Val Thr Glu Ala Pro Ser Lys Pro Ile Thr Val 1760 1765 1770 Thr Val Glu Glu Gln Arg Ser Gln Ser Val Arg Pro Gly Ala Asp 1775 1780 1785 Val Thr Phe Ile Cys Thr Ala Lys Ser Lys Ser Pro Ala Tyr Thr 1790 1795 1800 Leu Val Trp Thr Arg Leu His Asn Gly Lys Leu Pro Thr Arg Ala 1805 1810 1815 Met Asp Phe Asn Gly Ile Leu Thr Ile Arg Asn Val Gln Leu Ser 1820 1825 1830 Asp Ala Gly Thr Tyr Val Cys Thr Gly Ser Asn Met Phe Ala Met 1835 1840 1845 Asp Gln Gly Thr Ala Thr Leu His Val Gln Ala Ser Gly Thr Leu 1850 1855 1860 Ser Ala Pro Val Val Ser Ile His Pro Pro Gln Leu Thr Val Gln 1865 1870 1875 Pro Gly Gln Leu Ala Glu Phe Arg Cys Ser Ala Thr Gly Ser Pro 1880 1885 1890 Thr Pro Thr Leu Glu Trp Thr Gly Gly Pro Gly Gly Gln Leu Pro 1895 1900 1905 Ala Lys Ala Gln Ile His Gly Gly Ile Leu Arg Leu Pro Ala Val 1910 1915 1920 Glu Pro Thr Asp Gln Ala Gln Tyr Leu Cys Arg Ala His Ser Ser 1925 1930 1935 Ala Gly Gln Gln Val Ala Arg Ala Val Leu His Val His Gly Gly 1940 1945 1950 Gly Gly Pro Arg Val Gln Val Ser Pro Glu Arg Thr Gln Val His 1955 1960 1965 Ala Gly Arg Thr Val Arg Leu Tyr Cys Arg Ala Ala Gly Val Pro 1970 1975 1980 Ser Ala Thr Ile Thr Trp Arg Lys Glu Gly Gly Ser Leu Pro Pro 1985 1990 1995 Gln Ala Arg Ser Glu Arg Thr Asp Ile Ala Thr Leu Leu Ile Pro 2000 2005 2010 Ala Ile Thr Thr Ala Asp Ala Gly Phe Tyr Leu Cys Val Ala Thr 2015 2020 2025 Ser Pro Ala Gly Thr Ala Gln Ala Arg Ile Gln Val Val Val Leu 2030 2035 2040 Ser Ala Ser Asp Ala Ser Pro Pro Pro Val Lys Ile Glu Ser Ser 2045 2050 2055 Ser Pro Ser Val Thr Glu Gly Gln Thr Leu Asp Leu Asn Cys Val 2060 2065 2070 Val Ala Gly Ser Ala His Ala Gln Val Thr Trp Tyr Arg Arg Gly 2075 2080 2085 Gly Ser Leu Pro Pro His Thr Gln Val His Gly Ser Arg Leu Arg 2090 2095 2100 Leu Pro Gln Val Ser Pro Ala Asp Ser Gly Glu Tyr Val Cys Arg 2105 2110 2115 Val Glu Asn Gly Ser Gly Pro Lys Glu Ala Ser Ile Thr Val Ser 2120 2125 2130 Val Leu His Gly Thr His Ser Gly Pro Ser Tyr Thr Pro Val Pro 2135 2140 2145 Gly Ser Thr Arg Pro Ile Arg Ile Glu Pro Ser Ser Ser His Val 2150 2155 2160 Ala Glu Gly Gln Thr Leu Asp Leu Asn Cys Val Val Pro Gly Gln 2165 2170 2175 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Ser Leu Pro 2180 2185 2190 Ala Arg His Gln Thr His Gly Ser Leu Leu Arg Leu His Gln Val 2195 2200 2205 Thr Pro Ala Asp Ser Gly Glu Tyr Val Cys His Val Val Gly Thr 2210 2215 2220 Ser Gly Pro Leu Glu Ala Ser Val Leu Val Thr Ile Glu Ala Ser 2225 2230 2235 Val Ile Pro Gly Pro Ile Pro Pro Val Arg Ile Glu Ser Ser Ser 2240 2245 2250 Ser Thr Val Ala Glu Gly Gln Thr Leu Asp Leu Ser Cys Val Val 2255 2260 2265 Ala Gly Gln Ala His Ala Gln Val Thr Trp Tyr Lys Arg Gly Gly 2270 2275 2280 Ser Leu Pro Ala Arg His Gln Val Arg Gly Ser Arg Leu Tyr Ile 2285 2290 2295 Phe Gln Ala Ser Pro Ala Asp Ala Gly Gln Tyr Val Cys Arg Ala 2300 2305 2310 Ser Asn Gly Met Glu Ala Ser Ile Thr Val Thr Val Thr Gly Thr 2315 2320 2325 Gln Gly Ala Asn Leu Ala Tyr Pro Ala Gly Ser Thr Gln Pro Ile 2330 2335 2340 Arg Ile Glu Pro Ser Ser Ser Gln Val Ala Glu Gly Gln Thr Leu 2345 2350 2355 Asp Leu Asn Cys Val Val Pro Gly Gln Ser His Ala Gln Val Thr 2360 2365 2370 Trp His Lys Arg Gly Gly Ser Leu Pro Val Arg His Gln Thr His 2375 2380 2385 Gly Ser Leu Leu Arg Leu Tyr Gln Ala Ser Pro Ala Asp Ser Gly 2390 2395 2400 Glu Tyr Val Cys Arg Val Leu Gly Ser Ser Val Pro Leu Glu Ala 2405 2410 2415 Ser Val Leu Val Thr Ile Glu Pro Ala Gly Ser Val Pro Ala Leu 2420 2425 2430 Gly Val Thr Pro Thr Val Arg Ile Glu Ser Ser Ser Ser Gln Val 2435 2440 2445 Ala Glu Gly Gln Thr Leu Asp Leu Asn Cys Leu Val Ala Gly Gln 2450 2455 2460 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Ser Leu Pro 2465 2470 2475 Ala Arg His Gln Val His Gly Ser Arg Leu Arg Leu Leu Gln Val 2480 2485 2490 Thr Pro Ala Asp Ser Gly Glu Tyr Val Cys Arg Val Val Gly Ser 2495 2500 2505 Ser Gly Thr Gln Glu Ala Ser Val Leu Val Thr Ile Gln Gln Arg 2510 2515 2520 Leu Ser Gly Ser His Ser Gln Gly Val Ala Tyr Pro Val Arg Ile 2525 2530 2535 Glu Ser Ser Ser Ala Ser Leu Ala Asn Gly His Thr Leu Asp Leu 2540 2545 2550 Asn Cys Leu Val Ala Ser Gln Ala Pro His Thr Ile Thr Trp Tyr 2555 2560 2565 Lys Arg Gly Gly Ser Leu Pro Ser Arg His Gln Ile Val Gly Ser 2570 2575 2580 Arg Leu Arg Ile Pro Gln Val Thr Pro Ala Asp Ser Gly Glu Tyr 2585 2590 2595 Val Cys His Val Ser Asn Gly Ala Gly Ser Arg Glu Thr Ser Leu 2600 2605 2610 Ile Val Thr Ile Gln Gly Ser Gly Ser Ser His Val Pro Ser Val 2615 2620 2625 Ser Pro Pro Ile Arg Ile Glu Ser Ser Ser Pro Thr Val Val Glu 2630 2635 2640 Gly Gln Thr Leu Asp Leu Asn Cys Val Val Ala Arg Gln Pro Gln 2645 2650 2655 Ala Ile Ile Thr Trp Tyr Lys Arg Gly Gly Ser Leu Pro Ser Arg 2660 2665 2670 His Gln Thr His Gly Ser His Leu Arg Leu His Gln Met Ser Val 2675 2680 2685 Ala Asp Ser Gly Glu Tyr Val Cys Arg Ala Asn Asn Asn Ile Asp 2690 2695 2700 Ala Leu Glu Ala Ser Ile Val Ile Ser Val Ser Pro Ser Ala Gly 2705 2710 2715 Ser Pro Ser Ala Pro Gly Ser Ser Met Pro Ile Arg Ile Glu Ser 2720 2725 2730 Ser Ser Ser His Val Ala Glu Gly Glu Thr Leu Asp Leu Asn Cys 2735 2740 2745 Val Val Pro Gly Gln Ala His Ala Gln Val Thr Trp His Lys Arg 2750 2755 2760 Gly Gly Ser Leu Pro Ser His His Gln Thr Arg Gly Ser Arg Leu 2765 2770 2775 Arg Leu His His Val Ser Pro Ala Asp Ser Gly Glu Tyr Val Cys 2780 2785 2790 Arg Val Met Gly Ser Ser Gly Pro Leu Glu Ala Ser Val Leu Val 2795 2800 2805 Thr Ile Glu Ala Ser Gly Ser Ser Ala Val His Val Pro Ala Pro 2810 2815 2820 Gly Gly Ala Pro Pro Ile Arg Ile Glu Pro Ser Ser Ser Arg Val 2825 2830 2835 Ala Glu Gly Gln Thr Leu Asp Leu Lys Cys Val Val Pro Gly Gln 2840 2845 2850 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Asn Leu Pro 2855 2860 2865 Ala Arg His Gln Val His Gly Pro Leu Leu Arg Leu Asn Gln Val 2870 2875 2880 Ser Pro Ala Asp Ser Gly Glu Tyr Ser Cys Gln Val Thr Gly Ser 2885 2890 2895 Ser Gly Thr Leu Glu Ala Ser Val Leu Val Thr Ile Glu Pro Ser 2900 2905 2910 Ser Pro Gly Pro Ile Pro Ala Pro Gly Leu Ala Gln Pro Ile Tyr 2915 2920 2925 Ile Glu Ala Ser Ser Ser His Val Thr Glu Gly Gln Thr Leu Asp 2930 2935 2940 Leu Asn Cys Val Val Pro Gly Gln Ala His Ala Gln Val Thr Trp 2945 2950 2955 Tyr Lys Arg Gly Gly Ser Leu Pro Ala Arg His Gln Thr His Gly 2960 2965 2970 Ser Gln Leu Arg Leu His Leu Val Ser Pro Ala Asp Ser Gly Glu 2975 2980 2985 Tyr Val Cys Arg Ala Ala Ser Gly Pro Gly Pro Glu Gln Glu Ala 2990 2995 3000 Ser Phe Thr Val Thr Val Pro Pro Ser Glu Gly Ser Ser Tyr Arg 3005 3010 3015 Leu Arg Ser Pro Val Ile Ser Ile Asp Pro Pro Ser Ser Thr Val 3020 3025 3030 Gln Gln Gly Gln Asp Ala Ser Phe Lys Cys Leu Ile His Asp Gly 3035 3040 3045 Ala Ala Pro Ile Ser Leu Glu Trp Lys Thr Arg Asn Gln Glu Leu 3050 3055 3060 Glu Asp Asn Val His Ile Ser Pro Asn Gly Ser Ile Ile Thr Ile 3065 3070 3075 Val Gly Thr Arg Pro Ser Asn His Gly Thr Tyr Arg Cys Val Ala 3080 3085 3090 Ser Asn Ala Tyr Gly Val Ala Gln Ser Val Val Asn Leu Ser Val 3095 3100 3105 His Gly Pro Pro Thr Val Ser Val Leu Pro Glu Gly Pro Val Trp 3110 3115 3120 Val Lys Val Gly Lys Ala Val Thr Leu Glu Cys Val Ser Ala Gly 3125 3130 3135 Glu Pro Arg Ser Ser Ala Arg Trp Thr Arg Ile Ser Ser Thr Pro 3140 3145 3150 Ala Lys Leu Glu Gln Arg Thr Tyr Gly Leu Met Asp Ser His Ala 3155 3160 3165 Val Leu Gln Ile Ser Ser Ala Lys Pro Ser Asp Ala Gly Thr Tyr 3170 3175 3180 Val Cys Leu Ala Gln Asn Ala Leu Gly Thr Ala Gln Lys Gln Val 3185 3190 3195 Glu Val Ile Val Asp Thr Gly Ala Met Ala Pro Gly Ala Pro Gln 3200 3205 3210 Val Gln Ala Glu Glu Ala Glu Leu Thr Val Glu Ala Gly His Thr 3215 3220 3225 Ala Thr Leu Arg Cys Ser Ala Thr Gly Ser Pro Ala Pro Thr Ile 3230 3235 3240 His Trp Ser Lys Leu Arg Ser Pro Leu Pro Trp Gln His Arg Leu 3245 3250 3255 Glu Gly Asp Thr Leu Ile Ile Pro Arg Val Ala Gln Gln Asp Ser 3260 3265 3270 Gly Gln Tyr Ile Cys Asn Ala Thr Ser Pro Ala Gly His Ala Glu 3275 3280 3285 Ala Thr Ile Ile Leu His Val Glu Ser Pro Pro Tyr Ala Thr Thr 3290 3295 3300 Val Pro Glu His Ala Ser Val Gln Ala Gly Glu Thr Val Gln Leu 3305 3310 3315 Gln Cys Leu Ala His Gly Thr Pro Pro Leu Thr Phe Gln Trp Ser 3320 3325 3330 Arg Val Gly Ser Ser Leu Pro Gly Arg Ala Thr Ala Arg Asn Glu 3335 3340 3345 Leu Leu His Phe Glu Arg Ala Ala Pro Glu Asp Ser Gly Arg Tyr 3350 3355 3360 Arg Cys Arg Val Thr Asn Lys Val Gly Ser Ala Glu Ala Phe Ala 3365 3370 3375 Gln Leu Leu Val Gln Gly Pro Pro Gly Ser Leu Pro Ala Thr Ser 3380 3385 3390 Ile Pro Ala Gly Ser Thr Pro Thr Val Gln Val Thr Pro Gln Leu 3395 3400 3405 Glu Thr Lys Ser Ile Gly Ala Ser Val Glu Phe His Cys Ala Val 3410 3415 3420 Pro Ser Asp Arg Gly Thr Gln Leu Arg Trp Phe Lys Glu Gly Gly 3425 3430 3435 Gln Leu Pro Pro Gly His Ser Val Gln Asp Gly Val Leu Arg Ile 3440 3445 3450 Gln Asn Leu Asp Gln Ser Cys Gln Gly Thr Tyr Ile Cys Gln Ala 3455 3460 3465 His Gly Pro Trp Gly Lys Ala Gln Ala Ser Ala Gln Leu Val Ile 3470 3475 3480 Gln Ala Leu Pro Ser Val Leu Ile Asn Ile Arg Thr Ser Val Gln 3485 3490 3495 Thr Val Val Val Gly His Ala Val Glu Phe Glu Cys Leu Ala Leu 3500 3505 3510 Gly Asp Pro Lys Pro Gln Val Thr Trp Ser Lys Val Gly Gly His 3515 3520 3525 Leu Arg Pro Gly Ile Val Gln Ser Gly Gly Val Val Arg Ile Ala 3530 3535 3540 His Val Glu Leu Ala Asp Ala Gly Gln Tyr Arg Cys Thr Ala Thr 3545 3550 3555 Asn Ala Ala Gly Thr Thr Gln Ser His Val Leu Leu Leu Val Gln 3560 3565 3570 Ala Leu Pro Gln Ile Ser Met Pro Gln Glu Val Arg Val Pro Ala 3575 3580 3585 Gly Ser Ala Ala Val Phe Pro Cys Ile Ala Ser Gly Tyr Pro Thr 3590 3595 3600 Pro Asp Ile Ser Trp Ser Lys Leu Asp Gly Ser Leu Pro Pro Asp 3605 3610 3615 Ser Arg Leu Glu Asn Asn Met Leu Met Leu Pro Ser Val Arg Pro 3620 3625 3630 Gln Asp Ala Gly Thr Tyr Val Cys Thr Ala Thr Asn Arg Gln Gly 3635 3640 3645 Lys Val Lys Ala Phe Ala His Leu Gln Val Pro Glu Arg Val Val 3650 3655 3660 Pro Tyr Phe Thr Gln Thr Pro Tyr Ser Phe Leu Pro Leu Pro Thr 3665 3670 3675 Ile Lys Asp Ala Tyr Arg Lys Phe Glu Ile Lys Ile Thr Phe Arg 3680 3685 3690 Pro Asp Ser Ala Asp Gly Met Leu Leu Tyr Asn Gly Gln Lys Arg 3695 3700 3705 Val Pro Gly Ser Pro Thr Asn Leu Ala Asn Arg Gln Pro Asp Phe 3710 3715 3720 Ile Ser Phe Gly Leu Val Gly Gly Arg Pro Glu Phe Arg Phe Asp 3725 3730 3735 Ala Gly Ser Gly Met Ala Thr Ile Arg His Pro Thr Pro Leu Ala 3740 3745 3750 Leu Gly His Phe His Thr Val Thr Leu Leu Arg Ser Leu Thr Gln 3755 3760 3765 Gly Ser Leu Ile Val Gly Asp Leu Ala Pro Val Asn Gly Thr Ser 3770 3775 3780 Gln Gly Lys Phe Gln Gly Leu Asp Leu Asn Glu Glu Leu Tyr Leu 3785 3790 3795 Gly Gly Tyr Pro Asp Tyr Gly Ala Ile Pro Lys Ala Gly Leu Ser 3800 3805 3810 Ser Gly Phe Ile Gly Cys Val Arg Glu Leu Arg Ile Gln Gly Glu 3815 3820 3825 Glu Ile Val Phe His Asp Leu Asn Leu Thr Ala His Gly Ile Ser 3830 3835 3840 His Cys Pro Thr Cys Arg Asp Arg Pro Cys Gln Asn Gly Gly Gln 3845 3850 3855 Cys His Asp Ser Glu Ser Ser Ser Tyr Val Cys Val Cys Pro Ala 3860 3865 3870 Gly Phe Thr Gly Ser Arg Cys Glu His Ser Gln Ala Leu His Cys 3875 3880 3885 His Pro Glu Ala Cys Gly Pro Asp Ala Thr Cys Val Asn Arg Pro 3890 3895 3900 Asp Gly Arg Gly Tyr Thr Cys Arg Cys His Leu Gly Arg Ser Gly 3905 3910 3915 Leu Arg Cys Glu Glu Gly Val Thr Val Thr Thr Pro Ser Leu Ser 3920 3925 3930 Gly Ala Gly Ser Tyr Leu Ala Leu Pro Ala Leu Thr Asn Thr His 3935 3940 3945 His Glu Leu Arg Leu Asp Val Glu Phe Lys Pro Leu Ala Pro Asp 3950 3955 3960 Gly Val Leu Leu Phe Ser Gly Gly Lys Ser Gly Pro Val Glu Asp 3965 3970 3975 Phe Val Ser Leu Ala Met Val Gly Gly His Leu Glu Phe Arg Tyr 3980 3985 3990 Glu Leu Gly Ser Gly Leu Ala Val Leu Arg Ser Ala Glu Pro Leu 3995 4000 4005 Ala Leu Gly Arg Trp His Arg Val Ser Ala Glu Arg Leu Asn Lys 4010 4015 4020 Asp Gly Ser Leu Arg Val Asn Gly Gly Arg Pro Val Leu Arg Ser 4025 4030 4035 Ser Pro Gly Lys Ser Gln Gly Leu Asn Leu His Thr Leu Leu Tyr 4040 4045 4050 Leu Gly Gly Val Glu Pro Ser Val Pro Leu Ser Pro Ala Thr Asn 4055 4060 4065 Met Ser Ala His Phe Arg Gly Cys Val Gly Glu Val Ser Val Asn 4070 4075 4080 Gly Lys Arg Leu Asp Leu Thr Tyr Ser Phe Leu Gly Ser Gln Gly 4085 4090 4095 Ile Gly Gln Cys Tyr Asp Ser Ser Pro Cys Glu Arg Gln Pro Cys 4100 4105 4110 Gln His Gly Ala Thr Cys Met Pro Ala Gly Glu Tyr Glu Phe Gln 4115 4120 4125 Cys Leu Cys Arg Asp Gly Phe Lys Gly Asp Leu Cys Glu His Glu 4130 4135 4140 Glu Asn Pro Cys Gln Leu Arg Glu Pro Cys Leu His Gly Gly Thr 4145 4150 4155 Cys Gln Gly Thr Arg Cys Leu Cys Leu Pro Gly Phe Ser Gly Pro 4160 4165 4170 Arg Cys Gln Gln Gly Ser Gly His Gly Ile Ala Glu Ser Asp Trp 4175 4180 4185 His Leu Glu Gly Ser Gly Gly Asn Asp Ala Pro Gly Gln Tyr Gly 4190 4195 4200 Ala Tyr Phe His Asp Asp Gly Phe Leu Ala Phe Pro Gly His Val 4205 4210 4215 Phe Ser Arg Ser Leu Pro Glu Val Pro Glu Thr Ile Glu Leu Glu 4220 4225 4230 Val Arg Thr Ser Thr Ala Ser Gly Leu Leu Leu Trp Gln Gly Val 4235 4240 4245 Glu Val Gly Glu Ala Gly Gln Gly Lys Asp Phe Ile Ser Leu Gly 4250 4255 4260 Leu Gln Asp Gly His Leu Val Phe Arg Tyr Gln Leu Gly Ser Gly 4265 4270 4275 Glu Ala Arg Leu Val Ser Glu Asp Pro Ile Asn Asp Gly Glu Trp 4280 4285 4290 His Arg Val Thr Ala Leu Arg Glu Gly Arg Arg Gly Ser Ile Gln 4295 4300 4305 Val Asp Gly Glu Glu Leu Val Ser Gly Arg Ser Pro Gly Pro Asn 4310 4315 4320 Val Ala Val Asn Ala Lys Gly Ser Val Tyr Ile Gly Gly Ala Pro 4325 4330 4335 Asp Val Ala Thr Leu Thr Gly Gly Arg Phe Ser Ser Gly Ile Thr 4340 4345 4350 Gly Cys Val Lys Asn Leu Val Leu His Ser Ala Arg Pro Gly Ala 4355 4360 4365 Pro Pro Pro Gln Pro Leu Asp Leu Gln His Arg Ala Gln Ala Gly 4370 4375 4380 Ala Asn Thr Arg Pro Cys Pro Ser 4385 4390 <210> SEQ ID NO 51 <211> LENGTH: 184 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9H875 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(184) <400> SEQUENCE: 51 Met Ala Ser Pro Ala Ala Ser Ser Val Arg Pro Pro Arg Pro Lys Lys 1 5 10 15 Glu Pro Gln Thr Leu Val Ile Pro Lys Asn Ala Ala Glu Glu Gln Lys 20 25 30 Leu Lys Leu Glu Arg Leu Met Lys Asn Pro Asp Lys Ala Val Pro Ile 35 40 45 Pro Glu Lys Met Ser Glu Trp Ala Pro Arg Pro Pro Pro Glu Phe Val 50 55 60 Arg Asp Val Met Gly Ser Ser Ala Gly Ala Gly Ser Gly Glu Phe His 65 70 75 80 Val Tyr Arg His Leu Arg Arg Arg Glu Tyr Gln Arg Gln Asp Tyr Met 85 90 95 Asp Ala Met Ala Glu Lys Gln Lys Leu Asp Ala Glu Phe Gln Lys Arg 100 105 110 Leu Glu Lys Asn Lys Ile Ala Ala Glu Glu Gln Thr Ala Lys Arg Arg 115 120 125 Lys Lys Arg Gln Lys Leu Lys Glu Lys Lys Leu Leu Ala Lys Lys Met 130 135 140 Lys Leu Glu Gln Lys Lys Gln Glu Gly Pro Gly Gln Pro Lys Glu Gln 145 150 155 160 Gly Ser Ser Ser Ser Ala Glu Ala Ser Gly Thr Glu Glu Glu Glu Glu 165 170 175 Val Pro Ser Phe Thr Met Gly Arg 180 <210> SEQ ID NO 52 <211> LENGTH: 427 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P25101 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(427) <400> SEQUENCE: 52 Met Glu Thr Leu Cys Leu Arg Ala Ser Phe Trp Leu Ala Leu Val Gly 1 5 10 15 Cys Val Ile Ser Asp Asn Pro Glu Arg Tyr Ser Thr Asn Leu Ser Asn 20 25 30 His Val Asp Asp Phe Thr Thr Phe Arg Gly Thr Glu Leu Ser Phe Leu 35 40 45 Val Thr Thr His Gln Pro Thr Asn Leu Val Leu Pro Ser Asn Gly Ser 50 55 60 Met His Asn Tyr Cys Pro Gln Gln Thr Lys Ile Thr Ser Ala Phe Lys 65 70 75 80 Tyr Ile Asn Thr Val Ile Ser Cys Thr Ile Phe Ile Val Gly Met Val 85 90 95 Gly Asn Ala Thr Leu Leu Arg Ile Ile Tyr Gln Asn Lys Cys Met Arg 100 105 110 Asn Gly Pro Asn Ala Leu Ile Ala Ser Leu Ala Leu Gly Asp Leu Ile 115 120 125 Tyr Val Val Ile Asp Leu Pro Ile Asn Val Phe Lys Leu Leu Ala Gly 130 135 140 Arg Trp Pro Phe Asp His Asn Asp Phe Gly Val Phe Leu Cys Lys Leu 145 150 155 160 Phe Pro Phe Leu Gln Lys Ser Ser Val Gly Ile Thr Val Leu Asn Leu 165 170 175 Cys Ala Leu Ser Val Asp Arg Tyr Arg Ala Val Ala Ser Trp Ser Arg 180 185 190 Val Gln Gly Ile Gly Ile Pro Leu Val Thr Ala Ile Glu Ile Val Ser 195 200 205 Ile Trp Ile Leu Ser Phe Ile Leu Ala Ile Pro Glu Ala Ile Gly Phe 210 215 220 Val Met Val Pro Phe Glu Tyr Arg Gly Glu Gln His Lys Thr Cys Met 225 230 235 240 Leu Asn Ala Thr Ser Lys Phe Met Glu Phe Tyr Gln Asp Val Lys Asp 245 250 255 Trp Trp Leu Phe Gly Phe Tyr Phe Cys Met Pro Leu Val Cys Thr Ala 260 265 270 Ile Phe Tyr Thr Leu Met Thr Cys Glu Met Leu Asn Arg Arg Asn Gly 275 280 285 Ser Leu Arg Ile Ala Leu Ser Glu His Leu Lys Gln Arg Arg Glu Val 290 295 300 Ala Lys Thr Val Phe Cys Leu Val Val Ile Phe Ala Leu Cys Trp Phe 305 310 315 320 Pro Leu His Leu Ser Arg Ile Leu Lys Lys Thr Val Tyr Asn Glu Met 325 330 335 Asp Lys Asn Arg Cys Glu Leu Leu Ser Phe Leu Leu Leu Met Asp Tyr 340 345 350 Ile Gly Ile Asn Leu Ala Thr Met Asn Ser Cys Ile Asn Pro Ile Ala 355 360 365 Leu Tyr Phe Val Ser Lys Lys Phe Lys Asn Cys Phe Gln Ser Cys Leu 370 375 380 Cys Cys Cys Cys Tyr Gln Ser Lys Ser Leu Met Thr Ser Val Pro Met 385 390 395 400 Asn Gly Thr Ser Ile Gln Trp Lys Asn His Asp Gln Asn Asn His Asn 405 410 415 Thr Asp Arg Ser Ser His Lys Asp Ser Met Asn 420 425 <210> SEQ ID NO 53 <211> LENGTH: 660 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O43155 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(660) <400> SEQUENCE: 53 Met Gly Leu Gln Thr Thr Lys Trp Pro Ser His Gly Ala Phe Phe Leu 1 5 10 15 Lys Ser Trp Leu Ile Ile Ser Leu Gly Leu Tyr Ser Gln Val Ser Lys 20 25 30 Leu Leu Ala Cys Pro Ser Val Cys Arg Cys Asp Arg Asn Phe Val Tyr 35 40 45 Cys Asn Glu Arg Ser Leu Thr Ser Val Pro Leu Gly Ile Pro Glu Gly 50 55 60 Val Thr Val Leu Tyr Leu His Asn Asn Gln Ile Asn Asn Ala Gly Phe 65 70 75 80 Pro Ala Glu Leu His Asn Val Gln Ser Val His Thr Val Tyr Leu Tyr 85 90 95 Gly Asn Gln Leu Asp Glu Phe Pro Met Asn Leu Pro Lys Asn Val Arg 100 105 110 Val Leu His Leu Gln Glu Asn Asn Ile Gln Thr Ile Ser Arg Ala Ala 115 120 125 Leu Ala Gln Leu Leu Lys Leu Glu Glu Leu His Leu Asp Asp Asn Ser 130 135 140 Ile Ser Thr Val Gly Val Glu Asp Gly Ala Phe Arg Glu Ala Ile Ser 145 150 155 160 Leu Lys Leu Leu Phe Leu Ser Lys Asn His Leu Ser Ser Val Pro Val 165 170 175 Gly Leu Pro Val Asp Leu Gln Glu Leu Arg Val Asp Glu Asn Arg Ile 180 185 190 Ala Val Ile Ser Asp Met Ala Phe Gln Asn Leu Thr Ser Leu Glu Arg 195 200 205 Leu Ile Val Asp Gly Asn Leu Leu Thr Asn Lys Gly Ile Ala Glu Gly 210 215 220 Thr Phe Ser His Leu Thr Lys Leu Lys Glu Phe Ser Ile Val Arg Asn 225 230 235 240 Ser Leu Ser His Pro Pro Pro Asp Leu Pro Gly Thr His Leu Ile Arg 245 250 255 Leu Tyr Leu Gln Asp Asn Gln Ile Asn His Ile Pro Leu Thr Ala Phe 260 265 270 Ser Asn Leu Arg Lys Leu Glu Arg Leu Asp Ile Ser Asn Asn Gln Leu 275 280 285 Arg Met Leu Thr Gln Gly Val Phe Asp Asn Leu Ser Asn Leu Lys Gln 290 295 300 Leu Thr Ala Arg Asn Asn Pro Trp Phe Cys Asp Cys Ser Ile Lys Trp 305 310 315 320 Val Thr Glu Trp Leu Lys Tyr Ile Pro Ser Ser Leu Asn Val Arg Gly 325 330 335 Phe Met Cys Gln Gly Pro Glu Gln Val Arg Gly Met Ala Val Arg Glu 340 345 350 Leu Asn Met Asn Leu Leu Ser Cys Pro Thr Thr Thr Pro Gly Leu Pro 355 360 365 Leu Phe Thr Pro Ala Pro Ser Thr Ala Ser Pro Thr Thr Gln Pro Pro 370 375 380 Thr Leu Ser Ile Pro Asn Pro Ser Arg Ser Tyr Thr Pro Pro Thr Pro 385 390 395 400 Thr Thr Ser Lys Leu Pro Thr Ile Pro Asp Trp Asp Gly Arg Glu Arg 405 410 415 Val Thr Pro Pro Ile Ser Glu Arg Ile Gln Leu Ser Ile His Phe Val 420 425 430 Asn Asp Thr Ser Ile Gln Val Ser Trp Leu Ser Leu Phe Thr Val Met 435 440 445 Ala Tyr Lys Leu Thr Trp Val Lys Met Gly His Ser Leu Val Gly Gly 450 455 460 Ile Val Gln Glu Arg Ile Val Ser Gly Glu Lys Gln His Leu Ser Leu 465 470 475 480 Val Asn Leu Glu Pro Arg Ser Thr Tyr Arg Ile Cys Leu Val Pro Leu 485 490 495 Asp Ala Phe Asn Tyr Arg Ala Val Glu Asp Thr Ile Cys Ser Glu Ala 500 505 510 Thr Thr His Ala Ser Tyr Leu Asn Asn Gly Ser Asn Thr Ala Ser Ser 515 520 525 His Glu Gln Thr Thr Ser His Ser Met Gly Ser Pro Phe Leu Leu Ala 530 535 540 Gly Leu Ile Gly Gly Ala Val Ile Phe Val Leu Val Val Leu Leu Ser 545 550 555 560 Val Phe Cys Trp His Met His Lys Lys Gly Arg Tyr Thr Ser Gln Lys 565 570 575 Trp Lys Tyr Asn Arg Gly Arg Arg Lys Asp Asp Tyr Cys Glu Ala Gly 580 585 590 Thr Lys Lys Asp Asn Ser Ile Leu Glu Met Thr Glu Thr Ser Phe Gln 595 600 605 Ile Val Ser Leu Asn Asn Asp Gln Leu Leu Lys Gly Asp Phe Arg Leu 610 615 620 Gln Pro Ile Tyr Thr Pro Asn Gly Gly Ile Asn Tyr Thr Asp Cys His 625 630 635 640 Ile Pro Asn Asn Met Arg Tyr Cys Asn Ser Ser Val Pro Asp Leu Glu 645 650 655 His Cys His Thr 660 <210> SEQ ID NO 54 <211> LENGTH: 466 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P08670 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(466) <400> SEQUENCE: 54 Met Ser Thr Arg Ser Val Ser Ser Ser Ser Tyr Arg Arg Met Phe Gly 1 5 10 15 Gly Pro Gly Thr Ala Ser Arg Pro Ser Ser Ser Arg Ser Tyr Val Thr 20 25 30 Thr Ser Thr Arg Thr Tyr Ser Leu Gly Ser Ala Leu Arg Pro Ser Thr 35 40 45 Ser Arg Ser Leu Tyr Ala Ser Ser Pro Gly Gly Val Tyr Ala Thr Arg 50 55 60 Ser Ser Ala Val Arg Leu Arg Ser Ser Val Pro Gly Val Arg Leu Leu 65 70 75 80 Gln Asp Ser Val Asp Phe Ser Leu Ala Asp Ala Ile Asn Thr Glu Phe 85 90 95 Lys Asn Thr Arg Thr Asn Glu Lys Val Glu Leu Gln Glu Leu Asn Asp 100 105 110 Arg Phe Ala Asn Tyr Ile Asp Lys Val Arg Phe Leu Glu Gln Gln Asn 115 120 125 Lys Ile Leu Leu Ala Glu Leu Glu Gln Leu Lys Gly Gln Gly Lys Ser 130 135 140 Arg Leu Gly Asp Leu Tyr Glu Glu Glu Met Arg Glu Leu Arg Arg Gln 145 150 155 160 Val Asp Gln Leu Thr Asn Asp Lys Ala Arg Val Glu Val Glu Arg Asp 165 170 175 Asn Leu Ala Glu Asp Ile Met Arg Leu Arg Glu Lys Leu Gln Glu Glu 180 185 190 Met Leu Gln Arg Glu Glu Ala Glu Asn Thr Leu Gln Ser Phe Arg Gln 195 200 205 Asp Val Asp Asn Ala Ser Leu Ala Arg Leu Asp Leu Glu Arg Lys Val 210 215 220 Glu Ser Leu Gln Glu Glu Ile Ala Phe Leu Lys Lys Leu His Glu Glu 225 230 235 240 Glu Ile Gln Glu Leu Gln Ala Gln Ile Gln Glu Gln His Val Gln Ile 245 250 255 Asp Val Asp Val Ser Lys Pro Asp Leu Thr Ala Ala Leu Arg Asp Val 260 265 270 Arg Gln Gln Tyr Glu Ser Val Ala Ala Lys Asn Leu Gln Glu Ala Glu 275 280 285 Glu Trp Tyr Lys Ser Lys Phe Ala Asp Leu Ser Glu Ala Ala Asn Arg 290 295 300 Asn Asn Asp Ala Leu Arg Gln Ala Lys Gln Glu Ser Thr Glu Tyr Arg 305 310 315 320 Arg Gln Val Gln Ser Leu Thr Cys Glu Val Asp Ala Leu Lys Gly Thr 325 330 335 Asn Glu Ser Leu Glu Arg Gln Met Arg Glu Met Glu Glu Asn Phe Ala 340 345 350 Val Glu Ala Ala Asn Tyr Gln Asp Thr Ile Gly Arg Leu Gln Asp Glu 355 360 365 Ile Gln Asn Met Lys Glu Glu Met Ala Arg His Leu Arg Glu Tyr Gln 370 375 380 Asp Leu Leu Asn Val Lys Met Ala Leu Asp Ile Glu Ile Ala Thr Tyr 385 390 395 400 Arg Lys Leu Leu Glu Gly Glu Glu Ser Arg Ile Ser Leu Pro Leu Pro 405 410 415 Asn Phe Ser Ser Leu Asn Leu Arg Glu Thr Asn Leu Asp Ser Leu Pro 420 425 430 Leu Val Asp Thr His Ser Lys Arg Thr Leu Leu Ile Lys Thr Val Glu 435 440 445 Thr Arg Asp Gly Gln Val Ile Asn Glu Thr Ser Gln His His Asp Asp 450 455 460 Leu Glu 465 <210> SEQ ID NO 55 <211> LENGTH: 359 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P30556 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(359) <400> SEQUENCE: 55 Met Ile Leu Asn Ser Ser Thr Glu Asp Gly Ile Lys Arg Ile Gln Asp 1 5 10 15 Asp Cys Pro Lys Ala Gly Arg His Asn Tyr Ile Phe Val Met Ile Pro 20 25 30 Thr Leu Tyr Ser Ile Ile Phe Val Val Gly Ile Phe Gly Asn Ser Leu 35 40 45 Val Val Ile Val Ile Tyr Phe Tyr Met Lys Leu Lys Thr Val Ala Ser 50 55 60 Val Phe Leu Leu Asn Leu Ala Leu Ala Asp Leu Cys Phe Leu Leu Thr 65 70 75 80 Leu Pro Leu Trp Ala Val Tyr Thr Ala Met Glu Tyr Arg Trp Pro Phe 85 90 95 Gly Asn Tyr Leu Cys Lys Ile Ala Ser Ala Ser Val Ser Phe Asn Leu 100 105 110 Tyr Ala Ser Val Phe Leu Leu Thr Cys Leu Ser Ile Asp Arg Tyr Leu 115 120 125 Ala Ile Val His Pro Met Lys Ser Arg Leu Arg Arg Thr Met Leu Val 130 135 140 Ala Lys Val Thr Cys Ile Ile Ile Trp Leu Leu Ala Gly Leu Ala Ser 145 150 155 160 Leu Pro Ala Ile Ile His Arg Asn Val Phe Phe Ile Glu Asn Thr Asn 165 170 175 Ile Thr Val Cys Ala Phe His Tyr Glu Ser Gln Asn Ser Thr Leu Pro 180 185 190 Ile Gly Leu Gly Leu Thr Lys Asn Ile Leu Gly Phe Leu Phe Pro Phe 195 200 205 Leu Ile Ile Leu Thr Ser Tyr Thr Leu Ile Trp Lys Ala Leu Lys Lys 210 215 220 Ala Tyr Glu Ile Gln Lys Asn Lys Pro Arg Asn Asp Asp Ile Phe Lys 225 230 235 240 Ile Ile Met Ala Ile Val Leu Phe Phe Phe Phe Ser Trp Ile Pro His 245 250 255 Gln Ile Phe Thr Phe Leu Asp Val Leu Ile Gln Leu Gly Ile Ile Arg 260 265 270 Asp Cys Arg Ile Ala Asp Ile Val Asp Thr Ala Met Pro Ile Thr Ile 275 280 285 Cys Ile Ala Tyr Phe Asn Asn Cys Leu Asn Pro Leu Phe Tyr Gly Phe 290 295 300 Leu Gly Lys Lys Phe Lys Arg Tyr Phe Leu Gln Leu Leu Lys Tyr Ile 305 310 315 320 Pro Pro Lys Ala Lys Ser His Ser Asn Leu Ser Thr Lys Met Ser Thr 325 330 335 Leu Ser Tyr Arg Pro Ser Asp Asn Val Ser Ser Ser Thr Lys Lys Pro 340 345 350 Ala Pro Cys Phe Glu Val Glu 355 <210> SEQ ID NO 56 <211> LENGTH: 1053 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q2KHT3 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1053) <400> SEQUENCE: 56 Met Phe Gly Arg Ser Arg Ser Trp Val Gly Gly Gly His Gly Lys Thr 1 5 10 15 Ser Arg Asn Ile His Ser Leu Asp His Leu Lys Tyr Leu Tyr His Val 20 25 30 Leu Thr Lys Asn Thr Thr Val Thr Glu Gln Asn Arg Asn Leu Leu Val 35 40 45 Glu Thr Ile Arg Ser Ile Thr Glu Ile Leu Ile Trp Gly Asp Gln Asn 50 55 60 Asp Ser Ser Val Phe Asp Phe Phe Leu Glu Lys Asn Met Phe Val Phe 65 70 75 80 Phe Leu Asn Ile Leu Arg Gln Lys Ser Gly Arg Tyr Val Cys Val Gln 85 90 95 Leu Leu Gln Thr Leu Asn Ile Leu Phe Glu Asn Ile Ser His Glu Thr 100 105 110 Ser Leu Tyr Tyr Leu Leu Ser Asn Asn Tyr Val Asn Ser Ile Ile Val 115 120 125 His Lys Phe Asp Phe Ser Asp Glu Glu Ile Met Ala Tyr Tyr Ile Ser 130 135 140 Phe Leu Lys Thr Leu Ser Leu Lys Leu Asn Asn His Thr Val His Phe 145 150 155 160 Phe Tyr Asn Glu His Thr Asn Asp Phe Ala Leu Tyr Thr Glu Ala Ile 165 170 175 Lys Phe Phe Asn His Pro Glu Ser Met Val Arg Ile Ala Val Arg Thr 180 185 190 Ile Thr Leu Asn Val Tyr Lys Val Ser Leu Asp Asn Gln Ala Met Leu 195 200 205 His Tyr Ile Arg Asp Lys Thr Ala Val Pro Tyr Phe Ser Asn Leu Val 210 215 220 Trp Phe Ile Gly Ser His Val Ile Glu Leu Asp Asp Cys Val Gln Thr 225 230 235 240 Asp Glu Glu His Arg Asn Arg Gly Lys Leu Ser Asp Leu Val Ala Glu 245 250 255 His Leu Asp His Leu His Tyr Leu Asn Asp Ile Leu Ile Ile Asn Cys 260 265 270 Glu Phe Leu Asn Asp Val Leu Thr Asp His Leu Leu Asn Arg Leu Phe 275 280 285 Leu Pro Leu Tyr Val Tyr Ser Leu Glu Asn Gln Asp Lys Gly Gly Glu 290 295 300 Arg Pro Lys Ile Ser Leu Pro Val Ser Leu Tyr Leu Leu Ser Gln Val 305 310 315 320 Phe Leu Ile Ile His His Ala Pro Leu Val Asn Ser Leu Ala Glu Val 325 330 335 Ile Leu Asn Gly Asp Leu Ser Glu Met Tyr Ala Lys Thr Glu Gln Asp 340 345 350 Ile Gln Arg Ser Ser Ala Lys Pro Ser Ile Arg Cys Phe Ile Lys Pro 355 360 365 Thr Glu Thr Leu Glu Arg Ser Leu Glu Met Asn Lys His Lys Gly Lys 370 375 380 Arg Arg Val Gln Lys Arg Pro Asn Tyr Lys Asn Val Gly Glu Glu Glu 385 390 395 400 Asp Glu Glu Lys Gly Pro Thr Glu Asp Ala Gln Glu Asp Ala Glu Lys 405 410 415 Ala Lys Gly Thr Glu Gly Gly Ser Lys Gly Ile Lys Thr Ser Gly Glu 420 425 430 Ser Glu Glu Ile Glu Met Val Ile Met Glu Arg Ser Lys Leu Ser Glu 435 440 445 Leu Ala Ala Ser Thr Ser Val Gln Glu Gln Asn Thr Thr Asp Glu Glu 450 455 460 Lys Ser Ala Ala Ala Thr Cys Ser Glu Ser Thr Gln Trp Ser Arg Pro 465 470 475 480 Phe Leu Asp Met Val Tyr His Ala Leu Asp Ser Pro Asp Asp Asp Tyr 485 490 495 His Ala Leu Phe Val Leu Cys Leu Leu Tyr Ala Met Ser His Asn Lys 500 505 510 Gly Met Asp Pro Glu Lys Leu Glu Arg Ile Gln Leu Pro Val Pro Asn 515 520 525 Ala Ala Glu Lys Thr Thr Tyr Asn His Pro Leu Ala Glu Arg Leu Ile 530 535 540 Arg Ile Met Asn Asn Ala Ala Gln Pro Asp Gly Lys Ile Arg Leu Ala 545 550 555 560 Thr Leu Glu Leu Ser Cys Leu Leu Leu Lys Gln Gln Val Leu Met Ser 565 570 575 Ala Gly Cys Ile Met Lys Asp Val His Leu Ala Cys Leu Glu Gly Ala 580 585 590 Arg Glu Glu Ser Val His Leu Val Arg His Phe Tyr Lys Gly Glu Asp 595 600 605 Ile Phe Leu Asp Met Phe Glu Asp Glu Tyr Arg Ser Met Thr Met Lys 610 615 620 Pro Met Asn Val Glu Tyr Leu Met Met Asp Ala Ser Ile Leu Leu Pro 625 630 635 640 Pro Thr Gly Thr Pro Leu Thr Gly Ile Asp Phe Val Lys Arg Leu Pro 645 650 655 Cys Gly Asp Val Glu Lys Thr Arg Arg Ala Ile Arg Val Phe Phe Met 660 665 670 Leu Arg Ser Leu Ser Leu Gln Leu Arg Gly Glu Pro Glu Thr Gln Leu 675 680 685 Pro Leu Thr Arg Glu Glu Asp Leu Ile Lys Thr Asp Asp Val Leu Asp 690 695 700 Leu Asn Asn Ser Asp Leu Ile Ala Cys Thr Val Ile Thr Lys Asp Gly 705 710 715 720 Gly Met Val Gln Arg Phe Leu Ala Val Asp Ile Tyr Gln Met Ser Leu 725 730 735 Val Glu Pro Asp Val Ser Arg Leu Gly Trp Gly Val Val Lys Phe Ala 740 745 750 Gly Leu Leu Gln Asp Met Gln Val Thr Gly Val Glu Asp Asp Ser Arg 755 760 765 Ala Leu Asn Ile Thr Ile His Lys Pro Ala Ser Ser Pro His Ser Lys 770 775 780 Pro Phe Pro Ile Leu Gln Ala Thr Phe Ile Phe Ser Asp His Ile Arg 785 790 795 800 Cys Ile Ile Ala Lys Gln Arg Leu Ala Lys Gly Arg Ile Gln Ala Arg 805 810 815 Arg Met Lys Met Gln Arg Ile Ala Ala Leu Leu Asp Leu Pro Ile Gln 820 825 830 Pro Thr Thr Glu Val Leu Gly Phe Gly Leu Gly Ser Ser Thr Ser Thr 835 840 845 Gln His Leu Pro Phe Arg Phe Tyr Asp Gln Gly Arg Arg Gly Ser Ser 850 855 860 Asp Pro Thr Val Gln Arg Ser Val Phe Ala Ser Val Asp Lys Val Pro 865 870 875 880 Gly Phe Ala Val Ala Gln Cys Ile Asn Gln His Ser Ser Pro Ser Leu 885 890 895 Ser Ser Gln Ser Pro Pro Ser Ala Ser Gly Ser Pro Ser Gly Ser Gly 900 905 910 Ser Thr Ser His Cys Asp Ser Gly Gly Thr Ser Ser Ser Ser Thr Pro 915 920 925 Ser Thr Ala Gln Ser Pro Ala Asp Ala Pro Met Ser Pro Glu Leu Pro 930 935 940 Lys Pro His Leu Pro Asp Gln Leu Val Ile Val Asn Glu Thr Glu Ala 945 950 955 960 Asp Ser Lys Pro Ser Lys Asn Val Ala Arg Ser Ala Ala Val Glu Thr 965 970 975 Ala Ser Leu Ser Pro Ser Leu Val Pro Ala Arg Gln Pro Thr Ile Ser 980 985 990 Leu Leu Cys Glu Asp Thr Ala Asp Thr Leu Ser Val Glu Ser Leu Thr 995 1000 1005 Leu Val Pro Pro Val Asp Pro His Ser Leu Arg Ser Leu Thr Gly 1010 1015 1020 Met Pro Pro Leu Ser Thr Pro Ala Ala Ala Cys Thr Glu Pro Val 1025 1030 1035 Gly Glu Glu Ala Ala Cys Ala Glu Pro Val Gly Thr Ala Glu Asp 1040 1045 1050 <210> SEQ ID NO 57 <211> LENGTH: 1464 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02452 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1464) <400> SEQUENCE: 57 Met Phe Ser Phe Val Asp Leu Arg Leu Leu Leu Leu Leu Ala Ala Thr 1 5 10 15 Ala Leu Leu Thr His Gly Gln Glu Glu Gly Gln Val Glu Gly Gln Asp 20 25 30 Glu Asp Ile Pro Pro Ile Thr Cys Val Gln Asn Gly Leu Arg Tyr His 35 40 45 Asp Arg Asp Val Trp Lys Pro Glu Pro Cys Arg Ile Cys Val Cys Asp 50 55 60 Asn Gly Lys Val Leu Cys Asp Asp Val Ile Cys Asp Glu Thr Lys Asn 65 70 75 80 Cys Pro Gly Ala Glu Val Pro Glu Gly Glu Cys Cys Pro Val Cys Pro 85 90 95 Asp Gly Ser Glu Ser Pro Thr Asp Gln Glu Thr Thr Gly Val Glu Gly 100 105 110 Pro Lys Gly Asp Thr Gly Pro Arg Gly Pro Arg Gly Pro Ala Gly Pro 115 120 125 Pro Gly Arg Asp Gly Ile Pro Gly Gln Pro Gly Leu Pro Gly Pro Pro 130 135 140 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly Gly Asn Phe Ala 145 150 155 160 Pro Gln Leu Ser Tyr Gly Tyr Asp Glu Lys Ser Thr Gly Gly Ile Ser 165 170 175 Val Pro Gly Pro Met Gly Pro Ser Gly Pro Arg Gly Leu Pro Gly Pro 180 185 190 Pro Gly Ala Pro Gly Pro Gln Gly Phe Gln Gly Pro Pro Gly Glu Pro 195 200 205 Gly Glu Pro Gly Ala Ser Gly Pro Met Gly Pro Arg Gly Pro Pro Gly 210 215 220 Pro Pro Gly Lys Asn Gly Asp Asp Gly Glu Ala Gly Lys Pro Gly Arg 225 230 235 240 Pro Gly Glu Arg Gly Pro Pro Gly Pro Gln Gly Ala Arg Gly Leu Pro 245 250 255 Gly Thr Ala Gly Leu Pro Gly Met Lys Gly His Arg Gly Phe Ser Gly 260 265 270 Leu Asp Gly Ala Lys Gly Asp Ala Gly Pro Ala Gly Pro Lys Gly Glu 275 280 285 Pro Gly Ser Pro Gly Glu Asn Gly Ala Pro Gly Gln Met Gly Pro Arg 290 295 300 Gly Leu Pro Gly Glu Arg Gly Arg Pro Gly Ala Pro Gly Pro Ala Gly 305 310 315 320 Ala Arg Gly Asn Asp Gly Ala Thr Gly Ala Ala Gly Pro Pro Gly Pro 325 330 335 Thr Gly Pro Ala Gly Pro Pro Gly Phe Pro Gly Ala Val Gly Ala Lys 340 345 350 Gly Glu Ala Gly Pro Gln Gly Pro Arg Gly Ser Glu Gly Pro Gln Gly 355 360 365 Val Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Ala Ala Gly Pro 370 375 380 Ala Gly Asn Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Ala Asn 385 390 395 400 Gly Ala Pro Gly Ile Ala Gly Ala Pro Gly Phe Pro Gly Ala Arg Gly 405 410 415 Pro Ser Gly Pro Gln Gly Pro Gly Gly Pro Pro Gly Pro Lys Gly Asn 420 425 430 Ser Gly Glu Pro Gly Ala Pro Gly Ser Lys Gly Asp Thr Gly Ala Lys 435 440 445 Gly Glu Pro Gly Pro Val Gly Val Gln Gly Pro Pro Gly Pro Ala Gly 450 455 460 Glu Glu Gly Lys Arg Gly Ala Arg Gly Glu Pro Gly Pro Thr Gly Leu 465 470 475 480 Pro Gly Pro Pro Gly Glu Arg Gly Gly Pro Gly Ser Arg Gly Phe Pro 485 490 495 Gly Ala Asp Gly Val Ala Gly Pro Lys Gly Pro Ala Gly Glu Arg Gly 500 505 510 Ser Pro Gly Pro Ala Gly Pro Lys Gly Ser Pro Gly Glu Ala Gly Arg 515 520 525 Pro Gly Glu Ala Gly Leu Pro Gly Ala Lys Gly Leu Thr Gly Ser Pro 530 535 540 Gly Ser Pro Gly Pro Asp Gly Lys Thr Gly Pro Pro Gly Pro Ala Gly 545 550 555 560 Gln Asp Gly Arg Pro Gly Pro Pro Gly Pro Pro Gly Ala Arg Gly Gln 565 570 575 Ala Gly Val Met Gly Phe Pro Gly Pro Lys Gly Ala Ala Gly Glu Pro 580 585 590 Gly Lys Ala Gly Glu Arg Gly Val Pro Gly Pro Pro Gly Ala Val Gly 595 600 605 Pro Ala Gly Lys Asp Gly Glu Ala Gly Ala Gln Gly Pro Pro Gly Pro 610 615 620 Ala Gly Pro Ala Gly Glu Arg Gly Glu Gln Gly Pro Ala Gly Ser Pro 625 630 635 640 Gly Phe Gln Gly Leu Pro Gly Pro Ala Gly Pro Pro Gly Glu Ala Gly 645 650 655 Lys Pro Gly Glu Gln Gly Val Pro Gly Asp Leu Gly Ala Pro Gly Pro 660 665 670 Ser Gly Ala Arg Gly Glu Arg Gly Phe Pro Gly Glu Arg Gly Val Gln 675 680 685 Gly Pro Pro Gly Pro Ala Gly Pro Arg Gly Ala Asn Gly Ala Pro Gly 690 695 700 Asn Asp Gly Ala Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly Ser 705 710 715 720 Gln Gly Ala Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Ala Ala 725 730 735 Gly Leu Pro Gly Pro Lys Gly Asp Arg Gly Asp Ala Gly Pro Lys Gly 740 745 750 Ala Asp Gly Ser Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro 755 760 765 Ile Gly Pro Pro Gly Pro Ala Gly Ala Pro Gly Asp Lys Gly Glu Ser 770 775 780 Gly Pro Ser Gly Pro Ala Gly Pro Thr Gly Ala Arg Gly Ala Pro Gly 785 790 795 800 Asp Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Phe Ala Gly Pro 805 810 815 Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Glu Pro Gly Asp Ala 820 825 830 Gly Ala Lys Gly Asp Ala Gly Pro Pro Gly Pro Ala Gly Pro Ala Gly 835 840 845 Pro Pro Gly Pro Ile Gly Asn Val Gly Ala Pro Gly Ala Lys Gly Ala 850 855 860 Arg Gly Ser Ala Gly Pro Pro Gly Ala Thr Gly Phe Pro Gly Ala Ala 865 870 875 880 Gly Arg Val Gly Pro Pro Gly Pro Ser Gly Asn Ala Gly Pro Pro Gly 885 890 895 Pro Pro Gly Pro Ala Gly Lys Glu Gly Gly Lys Gly Pro Arg Gly Glu 900 905 910 Thr Gly Pro Ala Gly Arg Pro Gly Glu Val Gly Pro Pro Gly Pro Pro 915 920 925 Gly Pro Ala Gly Glu Lys Gly Ser Pro Gly Ala Asp Gly Pro Ala Gly 930 935 940 Ala Pro Gly Thr Pro Gly Pro Gln Gly Ile Ala Gly Gln Arg Gly Val 945 950 955 960 Val Gly Leu Pro Gly Gln Arg Gly Glu Arg Gly Phe Pro Gly Leu Pro 965 970 975 Gly Pro Ser Gly Glu Pro Gly Lys Gln Gly Pro Ser Gly Ala Ser Gly 980 985 990 Glu Arg Gly Pro Pro Gly Pro Met Gly Pro Pro Gly Leu Ala Gly Pro 995 1000 1005 Pro Gly Glu Ser Gly Arg Glu Gly Ala Pro Gly Ala Glu Gly Ser 1010 1015 1020 Pro Gly Arg Asp Gly Ser Pro Gly Ala Lys Gly Asp Arg Gly Glu 1025 1030 1035 Thr Gly Pro Ala Gly Pro Pro Gly Ala Pro Gly Ala Pro Gly Ala 1040 1045 1050 Pro Gly Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu 1055 1060 1065 Thr Gly Pro Ala Gly Pro Thr Gly Pro Val Gly Pro Val Gly Ala 1070 1075 1080 Arg Gly Pro Ala Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu 1085 1090 1095 Thr Gly Glu Gln Gly Asp Arg Gly Ile Lys Gly His Arg Gly Phe 1100 1105 1110 Ser Gly Leu Gln Gly Pro Pro Gly Pro Pro Gly Ser Pro Gly Glu 1115 1120 1125 Gln Gly Pro Ser Gly Ala Ser Gly Pro Ala Gly Pro Arg Gly Pro 1130 1135 1140 Pro Gly Ser Ala Gly Ala Pro Gly Lys Asp Gly Leu Asn Gly Leu 1145 1150 1155 Pro Gly Pro Ile Gly Pro Pro Gly Pro Arg Gly Arg Thr Gly Asp 1160 1165 1170 Ala Gly Pro Val Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro 1175 1180 1185 Pro Gly Pro Pro Ser Ala Gly Phe Asp Phe Ser Phe Leu Pro Gln 1190 1195 1200 Pro Pro Gln Glu Lys Ala His Asp Gly Gly Arg Tyr Tyr Arg Ala 1205 1210 1215 Asp Asp Ala Asn Val Val Arg Asp Arg Asp Leu Glu Val Asp Thr 1220 1225 1230 Thr Leu Lys Ser Leu Ser Gln Gln Ile Glu Asn Ile Arg Ser Pro 1235 1240 1245 Glu Gly Ser Arg Lys Asn Pro Ala Arg Thr Cys Arg Asp Leu Lys 1250 1255 1260 Met Cys His Ser Asp Trp Lys Ser Gly Glu Tyr Trp Ile Asp Pro 1265 1270 1275 Asn Gln Gly Cys Asn Leu Asp Ala Ile Lys Val Phe Cys Asn Met 1280 1285 1290 Glu Thr Gly Glu Thr Cys Val Tyr Pro Thr Gln Pro Ser Val Ala 1295 1300 1305 Gln Lys Asn Trp Tyr Ile Ser Lys Asn Pro Lys Asp Lys Arg His 1310 1315 1320 Val Trp Phe Gly Glu Ser Met Thr Asp Gly Phe Gln Phe Glu Tyr 1325 1330 1335 Gly Gly Gln Gly Ser Asp Pro Ala Asp Val Ala Ile Gln Leu Thr 1340 1345 1350 Phe Leu Arg Leu Met Ser Thr Glu Ala Ser Gln Asn Ile Thr Tyr 1355 1360 1365 His Cys Lys Asn Ser Val Ala Tyr Met Asp Gln Gln Thr Gly Asn 1370 1375 1380 Leu Lys Lys Ala Leu Leu Leu Gln Gly Ser Asn Glu Ile Glu Ile 1385 1390 1395 Arg Ala Glu Gly Asn Ser Arg Phe Thr Tyr Ser Val Thr Val Asp 1400 1405 1410 Gly Cys Thr Ser His Thr Gly Ala Trp Gly Lys Thr Val Ile Glu 1415 1420 1425 Tyr Lys Thr Thr Lys Thr Ser Arg Leu Pro Ile Ile Asp Val Ala 1430 1435 1440 Pro Leu Asp Val Gly Ala Pro Asp Gln Glu Phe Gly Phe Asp Val 1445 1450 1455 Gly Pro Val Cys Phe Leu 1460 <210> SEQ ID NO 58 <211> LENGTH: 1487 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02458 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1487) <400> SEQUENCE: 58 Met Ile Arg Leu Gly Ala Pro Gln Thr Leu Val Leu Leu Thr Leu Leu 1 5 10 15 Val Ala Ala Val Leu Arg Cys Gln Gly Gln Asp Val Gln Glu Ala Gly 20 25 30 Ser Cys Val Gln Asp Gly Gln Arg Tyr Asn Asp Lys Asp Val Trp Lys 35 40 45 Pro Glu Pro Cys Arg Ile Cys Val Cys Asp Thr Gly Thr Val Leu Cys 50 55 60 Asp Asp Ile Ile Cys Glu Asp Val Lys Asp Cys Leu Ser Pro Glu Ile 65 70 75 80 Pro Phe Gly Glu Cys Cys Pro Ile Cys Pro Thr Asp Leu Ala Thr Ala 85 90 95 Ser Gly Gln Pro Gly Pro Lys Gly Gln Lys Gly Glu Pro Gly Asp Ile 100 105 110 Lys Asp Ile Val Gly Pro Lys Gly Pro Pro Gly Pro Gln Gly Pro Ala 115 120 125 Gly Glu Gln Gly Pro Arg Gly Asp Arg Gly Asp Lys Gly Glu Lys Gly 130 135 140 Ala Pro Gly Pro Arg Gly Arg Asp Gly Glu Pro Gly Thr Pro Gly Asn 145 150 155 160 Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly 165 170 175 Gly Asn Phe Ala Ala Gln Met Ala Gly Gly Phe Asp Glu Lys Ala Gly 180 185 190 Gly Ala Gln Leu Gly Val Met Gln Gly Pro Met Gly Pro Met Gly Pro 195 200 205 Arg Gly Pro Pro Gly Pro Ala Gly Ala Pro Gly Pro Gln Gly Phe Gln 210 215 220 Gly Asn Pro Gly Glu Pro Gly Glu Pro Gly Val Ser Gly Pro Met Gly 225 230 235 240 Pro Arg Gly Pro Pro Gly Pro Pro Gly Lys Pro Gly Asp Asp Gly Glu 245 250 255 Ala Gly Lys Pro Gly Lys Ala Gly Glu Arg Gly Pro Pro Gly Pro Gln 260 265 270 Gly Ala Arg Gly Phe Pro Gly Thr Pro Gly Leu Pro Gly Val Lys Gly 275 280 285 His Arg Gly Tyr Pro Gly Leu Asp Gly Ala Lys Gly Glu Ala Gly Ala 290 295 300 Pro Gly Val Lys Gly Glu Ser Gly Ser Pro Gly Glu Asn Gly Ser Pro 305 310 315 320 Gly Pro Met Gly Pro Arg Gly Leu Pro Gly Glu Arg Gly Arg Thr Gly 325 330 335 Pro Ala Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Gln Pro Gly Pro 340 345 350 Ala Gly Pro Pro Gly Pro Val Gly Pro Ala Gly Gly Pro Gly Phe Pro 355 360 365 Gly Ala Pro Gly Ala Lys Gly Glu Ala Gly Pro Thr Gly Ala Arg Gly 370 375 380 Pro Glu Gly Ala Gln Gly Pro Arg Gly Glu Pro Gly Thr Pro Gly Ser 385 390 395 400 Pro Gly Pro Ala Gly Ala Ser Gly Asn Pro Gly Thr Asp Gly Ile Pro 405 410 415 Gly Ala Lys Gly Ser Ala Gly Ala Pro Gly Ile Ala Gly Ala Pro Gly 420 425 430 Phe Pro Gly Pro Arg Gly Pro Pro Gly Pro Gln Gly Ala Thr Gly Pro 435 440 445 Leu Gly Pro Lys Gly Gln Thr Gly Glu Pro Gly Ile Ala Gly Phe Lys 450 455 460 Gly Glu Gln Gly Pro Lys Gly Glu Pro Gly Pro Ala Gly Pro Gln Gly 465 470 475 480 Ala Pro Gly Pro Ala Gly Glu Glu Gly Lys Arg Gly Ala Arg Gly Glu 485 490 495 Pro Gly Gly Val Gly Pro Ile Gly Pro Pro Gly Glu Arg Gly Ala Pro 500 505 510 Gly Asn Arg Gly Phe Pro Gly Gln Asp Gly Leu Ala Gly Pro Lys Gly 515 520 525 Ala Pro Gly Glu Arg Gly Pro Ser Gly Leu Ala Gly Pro Lys Gly Ala 530 535 540 Asn Gly Asp Pro Gly Arg Pro Gly Glu Pro Gly Leu Pro Gly Ala Arg 545 550 555 560 Gly Leu Thr Gly Arg Pro Gly Asp Ala Gly Pro Gln Gly Lys Val Gly 565 570 575 Pro Ser Gly Ala Pro Gly Glu Asp Gly Arg Pro Gly Pro Pro Gly Pro 580 585 590 Gln Gly Ala Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys 595 600 605 Gly Ala Asn Gly Glu Pro Gly Lys Ala Gly Glu Lys Gly Leu Pro Gly 610 615 620 Ala Pro Gly Leu Arg Gly Leu Pro Gly Lys Asp Gly Glu Thr Gly Ala 625 630 635 640 Ala Gly Pro Pro Gly Pro Ala Gly Pro Ala Gly Glu Arg Gly Glu Gln 645 650 655 Gly Ala Pro Gly Pro Ser Gly Phe Gln Gly Leu Pro Gly Pro Pro Gly 660 665 670 Pro Pro Gly Glu Gly Gly Lys Pro Gly Asp Gln Gly Val Pro Gly Glu 675 680 685 Ala Gly Ala Pro Gly Leu Val Gly Pro Arg Gly Glu Arg Gly Phe Pro 690 695 700 Gly Glu Arg Gly Ser Pro Gly Ala Gln Gly Leu Gln Gly Pro Arg Gly 705 710 715 720 Leu Pro Gly Thr Pro Gly Thr Asp Gly Pro Lys Gly Ala Ser Gly Pro 725 730 735 Ala Gly Pro Pro Gly Ala Gln Gly Pro Pro Gly Leu Gln Gly Met Pro 740 745 750 Gly Glu Arg Gly Ala Ala Gly Ile Ala Gly Pro Lys Gly Asp Arg Gly 755 760 765 Asp Val Gly Glu Lys Gly Pro Glu Gly Ala Pro Gly Lys Asp Gly Gly 770 775 780 Arg Gly Leu Thr Gly Pro Ile Gly Pro Pro Gly Pro Ala Gly Ala Asn 785 790 795 800 Gly Glu Lys Gly Glu Val Gly Pro Pro Gly Pro Ala Gly Ser Ala Gly 805 810 815 Ala Arg Gly Ala Pro Gly Glu Arg Gly Glu Thr Gly Pro Pro Gly Pro 820 825 830 Ala Gly Phe Ala Gly Pro Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys 835 840 845 Gly Glu Gln Gly Glu Ala Gly Gln Lys Gly Asp Ala Gly Ala Pro Gly 850 855 860 Pro Gln Gly Pro Ser Gly Ala Pro Gly Pro Gln Gly Pro Thr Gly Val 865 870 875 880 Thr Gly Pro Lys Gly Ala Arg Gly Ala Gln Gly Pro Pro Gly Ala Thr 885 890 895 Gly Phe Pro Gly Ala Ala Gly Arg Val Gly Pro Pro Gly Ser Asn Gly 900 905 910 Asn Pro Gly Pro Pro Gly Pro Pro Gly Pro Ser Gly Lys Asp Gly Pro 915 920 925 Lys Gly Ala Arg Gly Asp Ser Gly Pro Pro Gly Arg Ala Gly Glu Pro 930 935 940 Gly Leu Gln Gly Pro Ala Gly Pro Pro Gly Glu Lys Gly Glu Pro Gly 945 950 955 960 Asp Asp Gly Pro Ser Gly Ala Glu Gly Pro Pro Gly Pro Gln Gly Leu 965 970 975 Ala Gly Gln Arg Gly Ile Val Gly Leu Pro Gly Gln Arg Gly Glu Arg 980 985 990 Gly Phe Pro Gly Leu Pro Gly Pro Ser Gly Glu Pro Gly Lys Gln Gly 995 1000 1005 Ala Pro Gly Ala Ser Gly Asp Arg Gly Pro Pro Gly Pro Val Gly 1010 1015 1020 Pro Pro Gly Leu Thr Gly Pro Ala Gly Glu Pro Gly Arg Glu Gly 1025 1030 1035 Ser Pro Gly Ala Asp Gly Pro Pro Gly Arg Asp Gly Ala Ala Gly 1040 1045 1050 Val Lys Gly Asp Arg Gly Glu Thr Gly Ala Val Gly Ala Pro Gly 1055 1060 1065 Ala Pro Gly Pro Pro Gly Ser Pro Gly Pro Ala Gly Pro Thr Gly 1070 1075 1080 Lys Gln Gly Asp Arg Gly Glu Ala Gly Ala Gln Gly Pro Met Gly 1085 1090 1095 Pro Ser Gly Pro Ala Gly Ala Arg Gly Ile Gln Gly Pro Gln Gly 1100 1105 1110 Pro Arg Gly Asp Lys Gly Glu Ala Gly Glu Pro Gly Glu Arg Gly 1115 1120 1125 Leu Lys Gly His Arg Gly Phe Thr Gly Leu Gln Gly Leu Pro Gly 1130 1135 1140 Pro Pro Gly Pro Ser Gly Asp Gln Gly Ala Ser Gly Pro Ala Gly 1145 1150 1155 Pro Ser Gly Pro Arg Gly Pro Pro Gly Pro Val Gly Pro Ser Gly 1160 1165 1170 Lys Asp Gly Ala Asn Gly Ile Pro Gly Pro Ile Gly Pro Pro Gly 1175 1180 1185 Pro Arg Gly Arg Ser Gly Glu Thr Gly Pro Ala Gly Pro Pro Gly 1190 1195 1200 Asn Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro Gly Ile 1205 1210 1215 Asp Met Ser Ala Phe Ala Gly Leu Gly Pro Arg Glu Lys Gly Pro 1220 1225 1230 Asp Pro Leu Gln Tyr Met Arg Ala Asp Gln Ala Ala Gly Gly Leu 1235 1240 1245 Arg Gln His Asp Ala Glu Val Asp Ala Thr Leu Lys Ser Leu Asn 1250 1255 1260 Asn Gln Ile Glu Ser Ile Arg Ser Pro Glu Gly Ser Arg Lys Asn 1265 1270 1275 Pro Ala Arg Thr Cys Arg Asp Leu Lys Leu Cys His Pro Glu Trp 1280 1285 1290 Lys Ser Gly Asp Tyr Trp Ile Asp Pro Asn Gln Gly Cys Thr Leu 1295 1300 1305 Asp Ala Met Lys Val Phe Cys Asn Met Glu Thr Gly Glu Thr Cys 1310 1315 1320 Val Tyr Pro Asn Pro Ala Asn Val Pro Lys Lys Asn Trp Trp Ser 1325 1330 1335 Ser Lys Ser Lys Glu Lys Lys His Ile Trp Phe Gly Glu Thr Ile 1340 1345 1350 Asn Gly Gly Phe His Phe Ser Tyr Gly Asp Asp Asn Leu Ala Pro 1355 1360 1365 Asn Thr Ala Asn Val Gln Met Thr Phe Leu Arg Leu Leu Ser Thr 1370 1375 1380 Glu Gly Ser Gln Asn Ile Thr Tyr His Cys Lys Asn Ser Ile Ala 1385 1390 1395 Tyr Leu Asp Glu Ala Ala Gly Asn Leu Lys Lys Ala Leu Leu Ile 1400 1405 1410 Gln Gly Ser Asn Asp Val Glu Ile Arg Ala Glu Gly Asn Ser Arg 1415 1420 1425 Phe Thr Tyr Thr Ala Leu Lys Asp Gly Cys Thr Lys His Thr Gly 1430 1435 1440 Lys Trp Gly Lys Thr Val Ile Glu Tyr Arg Ser Gln Lys Thr Ser 1445 1450 1455 Arg Leu Pro Ile Ile Asp Ile Ala Pro Met Asp Ile Gly Gly Pro 1460 1465 1470 Glu Gln Glu Phe Gly Val Asp Ile Gly Pro Val Cys Phe Leu 1475 1480 1485 <210> SEQ ID NO 59 <211> LENGTH: 1466 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02461 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1466) <400> SEQUENCE: 59 Met Met Ser Phe Val Gln Lys Gly Ser Trp Leu Leu Leu Ala Leu Leu 1 5 10 15 His Pro Thr Ile Ile Leu Ala Gln Gln Glu Ala Val Glu Gly Gly Cys 20 25 30 Ser His Leu Gly Gln Ser Tyr Ala Asp Arg Asp Val Trp Lys Pro Glu 35 40 45 Pro Cys Gln Ile Cys Val Cys Asp Ser Gly Ser Val Leu Cys Asp Asp 50 55 60 Ile Ile Cys Asp Asp Gln Glu Leu Asp Cys Pro Asn Pro Glu Ile Pro 65 70 75 80 Phe Gly Glu Cys Cys Ala Val Cys Pro Gln Pro Pro Thr Ala Pro Thr 85 90 95 Arg Pro Pro Asn Gly Gln Gly Pro Gln Gly Pro Lys Gly Asp Pro Gly 100 105 110 Pro Pro Gly Ile Pro Gly Arg Asn Gly Asp Pro Gly Ile Pro Gly Gln 115 120 125 Pro Gly Ser Pro Gly Ser Pro Gly Pro Pro Gly Ile Cys Glu Ser Cys 130 135 140 Pro Thr Gly Pro Gln Asn Tyr Ser Pro Gln Tyr Asp Ser Tyr Asp Val 145 150 155 160 Lys Ser Gly Val Ala Val Gly Gly Leu Ala Gly Tyr Pro Gly Pro Ala 165 170 175 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 180 185 190 Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 195 200 205 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 210 215 220 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 225 230 235 240 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile 245 250 255 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn 260 265 270 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 275 280 285 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 290 295 300 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 305 310 315 320 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 325 330 335 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 340 345 350 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 355 360 365 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly 370 375 380 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 385 390 395 400 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro 405 410 415 Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly 420 425 430 Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu 435 440 445 Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp 450 455 460 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 465 470 475 480 Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro 485 490 495 Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro 500 505 510 Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly 515 520 525 Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly 530 535 540 Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser 545 550 555 560 Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 565 570 575 Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys 580 585 590 Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro 595 600 605 Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 610 615 620 Pro Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu 625 630 635 640 Gln Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn Gly Lys Pro 645 650 655 Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly 660 665 670 Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro Pro Gly Leu 675 680 685 Ala Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Pro Pro Gly Pro Glu 690 695 700 Gly Gly Lys Gly Ala Ala Gly Pro Pro Gly Pro Pro Gly Ala Ala Gly 705 710 715 720 Thr Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Gly Leu Gly Ser 725 730 735 Pro Gly Pro Lys Gly Asp Lys Gly Glu Pro Gly Gly Pro Gly Ala Asp 740 745 750 Gly Val Pro Gly Lys Asp Gly Pro Arg Gly Pro Thr Gly Pro Ile Gly 755 760 765 Pro Pro Gly Pro Ala Gly Gln Pro Gly Asp Lys Gly Glu Gly Gly Ala 770 775 780 Pro Gly Leu Pro Gly Ile Ala Gly Pro Arg Gly Ser Pro Gly Glu Arg 785 790 795 800 Gly Glu Thr Gly Pro Pro Gly Pro Ala Gly Phe Pro Gly Ala Pro Gly 805 810 815 Gln Asn Gly Glu Pro Gly Gly Lys Gly Glu Arg Gly Ala Pro Gly Glu 820 825 830 Lys Gly Glu Gly Gly Pro Pro Gly Val Ala Gly Pro Pro Gly Gly Ser 835 840 845 Gly Pro Ala Gly Pro Pro Gly Pro Gln Gly Val Lys Gly Glu Arg Gly 850 855 860 Ser Pro Gly Gly Pro Gly Ala Ala Gly Phe Pro Gly Ala Arg Gly Leu 865 870 875 880 Pro Gly Pro Pro Gly Ser Asn Gly Asn Pro Gly Pro Pro Gly Pro Ser 885 890 895 Gly Ser Pro Gly Lys Asp Gly Pro Pro Gly Pro Ala Gly Asn Thr Gly 900 905 910 Ala Pro Gly Ser Pro Gly Val Ser Gly Pro Lys Gly Asp Ala Gly Gln 915 920 925 Pro Gly Glu Lys Gly Ser Pro Gly Ala Gln Gly Pro Pro Gly Ala Pro 930 935 940 Gly Pro Leu Gly Ile Ala Gly Ile Thr Gly Ala Arg Gly Leu Ala Gly 945 950 955 960 Pro Pro Gly Met Pro Gly Pro Arg Gly Ser Pro Gly Pro Gln Gly Val 965 970 975 Lys Gly Glu Ser Gly Lys Pro Gly Ala Asn Gly Leu Ser Gly Glu Arg 980 985 990 Gly Pro Pro Gly Pro Gln Gly Leu Pro Gly Leu Ala Gly Thr Ala Gly 995 1000 1005 Glu Pro Gly Arg Asp Gly Asn Pro Gly Ser Asp Gly Leu Pro Gly 1010 1015 1020 Arg Asp Gly Ser Pro Gly Gly Lys Gly Asp Arg Gly Glu Asn Gly 1025 1030 1035 Ser Pro Gly Ala Pro Gly Ala Pro Gly His Pro Gly Pro Pro Gly 1040 1045 1050 Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu Ser Gly 1055 1060 1065 Pro Ala Gly Pro Ala Gly Ala Pro Gly Pro Ala Gly Ser Arg Gly 1070 1075 1080 Ala Pro Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu Thr Gly 1085 1090 1095 Glu Arg Gly Ala Ala Gly Ile Lys Gly His Arg Gly Phe Pro Gly 1100 1105 1110 Asn Pro Gly Ala Pro Gly Ser Pro Gly Pro Ala Gly Gln Gln Gly 1115 1120 1125 Ala Ile Gly Ser Pro Gly Pro Ala Gly Pro Arg Gly Pro Val Gly 1130 1135 1140 Pro Ser Gly Pro Pro Gly Lys Asp Gly Thr Ser Gly His Pro Gly 1145 1150 1155 Pro Ile Gly Pro Pro Gly Pro Arg Gly Asn Arg Gly Glu Arg Gly 1160 1165 1170 Ser Glu Gly Ser Pro Gly His Pro Gly Gln Pro Gly Pro Pro Gly 1175 1180 1185 Pro Pro Gly Ala Pro Gly Pro Cys Cys Gly Gly Val Gly Ala Ala 1190 1195 1200 Ala Ile Ala Gly Ile Gly Gly Glu Lys Ala Gly Gly Phe Ala Pro 1205 1210 1215 Tyr Tyr Gly Asp Glu Pro Met Asp Phe Lys Ile Asn Thr Asp Glu 1220 1225 1230 Ile Met Thr Ser Leu Lys Ser Val Asn Gly Gln Ile Glu Ser Leu 1235 1240 1245 Ile Ser Pro Asp Gly Ser Arg Lys Asn Pro Ala Arg Asn Cys Arg 1250 1255 1260 Asp Leu Lys Phe Cys His Pro Glu Leu Lys Ser Gly Glu Tyr Trp 1265 1270 1275 Val Asp Pro Asn Gln Gly Cys Lys Leu Asp Ala Ile Lys Val Phe 1280 1285 1290 Cys Asn Met Glu Thr Gly Glu Thr Cys Ile Ser Ala Asn Pro Leu 1295 1300 1305 Asn Val Pro Arg Lys His Trp Trp Thr Asp Ser Ser Ala Glu Lys 1310 1315 1320 Lys His Val Trp Phe Gly Glu Ser Met Asp Gly Gly Phe Gln Phe 1325 1330 1335 Ser Tyr Gly Asn Pro Glu Leu Pro Glu Asp Val Leu Asp Val His 1340 1345 1350 Leu Ala Phe Leu Arg Leu Leu Ser Ser Arg Ala Ser Gln Asn Ile 1355 1360 1365 Thr Tyr His Cys Lys Asn Ser Ile Ala Tyr Met Asp Gln Ala Ser 1370 1375 1380 Gly Asn Val Lys Lys Ala Leu Lys Leu Met Gly Ser Asn Glu Gly 1385 1390 1395 Glu Phe Lys Ala Glu Gly Asn Ser Lys Phe Thr Tyr Thr Val Leu 1400 1405 1410 Glu Asp Gly Cys Thr Lys His Thr Gly Glu Trp Ser Lys Thr Val 1415 1420 1425 Phe Glu Tyr Arg Thr Arg Lys Ala Val Arg Leu Pro Ile Val Asp 1430 1435 1440 Ile Ala Pro Tyr Asp Ile Gly Gly Pro Asp Gln Glu Phe Gly Val 1445 1450 1455 Asp Val Gly Pro Val Cys Phe Leu 1460 1465 <210> SEQ ID NO 60 <211> LENGTH: 1669 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02462 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1669) <400> SEQUENCE: 60 Met Gly Pro Arg Leu Ser Val Trp Leu Leu Leu Leu Pro Ala Ala Leu 1 5 10 15 Leu Leu His Glu Glu His Ser Arg Ala Ala Ala Lys Gly Gly Cys Ala 20 25 30 Gly Ser Gly Cys Gly Lys Cys Asp Cys His Gly Val Lys Gly Gln Lys 35 40 45 Gly Glu Arg Gly Leu Pro Gly Leu Gln Gly Val Ile Gly Phe Pro Gly 50 55 60 Met Gln Gly Pro Glu Gly Pro Gln Gly Pro Pro Gly Gln Lys Gly Asp 65 70 75 80 Thr Gly Glu Pro Gly Leu Pro Gly Thr Lys Gly Thr Arg Gly Pro Pro 85 90 95 Gly Ala Ser Gly Tyr Pro Gly Asn Pro Gly Leu Pro Gly Ile Pro Gly 100 105 110 Gln Asp Gly Pro Pro Gly Pro Pro Gly Ile Pro Gly Cys Asn Gly Thr 115 120 125 Lys Gly Glu Arg Gly Pro Leu Gly Pro Pro Gly Leu Pro Gly Phe Ala 130 135 140 Gly Asn Pro Gly Pro Pro Gly Leu Pro Gly Met Lys Gly Asp Pro Gly 145 150 155 160 Glu Ile Leu Gly His Val Pro Gly Met Leu Leu Lys Gly Glu Arg Gly 165 170 175 Phe Pro Gly Ile Pro Gly Thr Pro Gly Pro Pro Gly Leu Pro Gly Leu 180 185 190 Gln Gly Pro Val Gly Pro Pro Gly Phe Thr Gly Pro Pro Gly Pro Pro 195 200 205 Gly Pro Pro Gly Pro Pro Gly Glu Lys Gly Gln Met Gly Leu Ser Phe 210 215 220 Gln Gly Pro Lys Gly Asp Lys Gly Asp Gln Gly Val Ser Gly Pro Pro 225 230 235 240 Gly Val Pro Gly Gln Ala Gln Val Gln Glu Lys Gly Asp Phe Ala Thr 245 250 255 Lys Gly Glu Lys Gly Gln Lys Gly Glu Pro Gly Phe Gln Gly Met Pro 260 265 270 Gly Val Gly Glu Lys Gly Glu Pro Gly Lys Pro Gly Pro Arg Gly Lys 275 280 285 Pro Gly Lys Asp Gly Asp Lys Gly Glu Lys Gly Ser Pro Gly Phe Pro 290 295 300 Gly Glu Pro Gly Tyr Pro Gly Leu Ile Gly Arg Gln Gly Pro Gln Gly 305 310 315 320 Glu Lys Gly Glu Ala Gly Pro Pro Gly Pro Pro Gly Ile Val Ile Gly 325 330 335 Thr Gly Pro Leu Gly Glu Lys Gly Glu Arg Gly Tyr Pro Gly Thr Pro 340 345 350 Gly Pro Arg Gly Glu Pro Gly Pro Lys Gly Phe Pro Gly Leu Pro Gly 355 360 365 Gln Pro Gly Pro Pro Gly Leu Pro Val Pro Gly Gln Ala Gly Ala Pro 370 375 380 Gly Phe Pro Gly Glu Arg Gly Glu Lys Gly Asp Arg Gly Phe Pro Gly 385 390 395 400 Thr Ser Leu Pro Gly Pro Ser Gly Arg Asp Gly Leu Pro Gly Pro Pro 405 410 415 Gly Ser Pro Gly Pro Pro Gly Gln Pro Gly Tyr Thr Asn Gly Ile Val 420 425 430 Glu Cys Gln Pro Gly Pro Pro Gly Asp Gln Gly Pro Pro Gly Ile Pro 435 440 445 Gly Gln Pro Gly Phe Ile Gly Glu Ile Gly Glu Lys Gly Gln Lys Gly 450 455 460 Glu Ser Cys Leu Ile Cys Asp Ile Asp Gly Tyr Arg Gly Pro Pro Gly 465 470 475 480 Pro Gln Gly Pro Pro Gly Glu Ile Gly Phe Pro Gly Gln Pro Gly Ala 485 490 495 Lys Gly Asp Arg Gly Leu Pro Gly Arg Asp Gly Val Ala Gly Val Pro 500 505 510 Gly Pro Gln Gly Thr Pro Gly Leu Ile Gly Gln Pro Gly Ala Lys Gly 515 520 525 Glu Pro Gly Glu Phe Tyr Phe Asp Leu Arg Leu Lys Gly Asp Lys Gly 530 535 540 Asp Pro Gly Phe Pro Gly Gln Pro Gly Met Thr Gly Arg Ala Gly Ser 545 550 555 560 Pro Gly Arg Asp Gly His Pro Gly Leu Pro Gly Pro Lys Gly Ser Pro 565 570 575 Gly Ser Val Gly Leu Lys Gly Glu Arg Gly Pro Pro Gly Gly Val Gly 580 585 590 Phe Pro Gly Ser Arg Gly Asp Thr Gly Pro Pro Gly Pro Pro Gly Tyr 595 600 605 Gly Pro Ala Gly Pro Ile Gly Asp Lys Gly Gln Ala Gly Phe Pro Gly 610 615 620 Gly Pro Gly Ser Pro Gly Leu Pro Gly Pro Lys Gly Glu Pro Gly Lys 625 630 635 640 Ile Val Pro Leu Pro Gly Pro Pro Gly Ala Glu Gly Leu Pro Gly Ser 645 650 655 Pro Gly Phe Pro Gly Pro Gln Gly Asp Arg Gly Phe Pro Gly Thr Pro 660 665 670 Gly Arg Pro Gly Leu Pro Gly Glu Lys Gly Ala Val Gly Gln Pro Gly 675 680 685 Ile Gly Phe Pro Gly Pro Pro Gly Pro Lys Gly Val Asp Gly Leu Pro 690 695 700 Gly Asp Met Gly Pro Pro Gly Thr Pro Gly Arg Pro Gly Phe Asn Gly 705 710 715 720 Leu Pro Gly Asn Pro Gly Val Gln Gly Gln Lys Gly Glu Pro Gly Val 725 730 735 Gly Leu Pro Gly Leu Lys Gly Leu Pro Gly Leu Pro Gly Ile Pro Gly 740 745 750 Thr Pro Gly Glu Lys Gly Ser Ile Gly Val Pro Gly Val Pro Gly Glu 755 760 765 His Gly Ala Ile Gly Pro Pro Gly Leu Gln Gly Ile Arg Gly Glu Pro 770 775 780 Gly Pro Pro Gly Leu Pro Gly Ser Val Gly Ser Pro Gly Val Pro Gly 785 790 795 800 Ile Gly Pro Pro Gly Ala Arg Gly Pro Pro Gly Gly Gln Gly Pro Pro 805 810 815 Gly Leu Ser Gly Pro Pro Gly Ile Lys Gly Glu Lys Gly Phe Pro Gly 820 825 830 Phe Pro Gly Leu Asp Met Pro Gly Pro Lys Gly Asp Lys Gly Ala Gln 835 840 845 Gly Leu Pro Gly Ile Thr Gly Gln Ser Gly Leu Pro Gly Leu Pro Gly 850 855 860 Gln Gln Gly Ala Pro Gly Ile Pro Gly Phe Pro Gly Ser Lys Gly Glu 865 870 875 880 Met Gly Val Met Gly Thr Pro Gly Gln Pro Gly Ser Pro Gly Pro Val 885 890 895 Gly Ala Pro Gly Leu Pro Gly Glu Lys Gly Asp His Gly Phe Pro Gly 900 905 910 Ser Ser Gly Pro Arg Gly Asp Pro Gly Leu Lys Gly Asp Lys Gly Asp 915 920 925 Val Gly Leu Pro Gly Lys Pro Gly Ser Met Asp Lys Val Asp Met Gly 930 935 940 Ser Met Lys Gly Gln Lys Gly Asp Gln Gly Glu Lys Gly Gln Ile Gly 945 950 955 960 Pro Ile Gly Glu Lys Gly Ser Arg Gly Asp Pro Gly Thr Pro Gly Val 965 970 975 Pro Gly Lys Asp Gly Gln Ala Gly Gln Pro Gly Gln Pro Gly Pro Lys 980 985 990 Gly Asp Pro Gly Ile Ser Gly Thr Pro Gly Ala Pro Gly Leu Pro Gly 995 1000 1005 Pro Lys Gly Ser Val Gly Gly Met Gly Leu Pro Gly Thr Pro Gly 1010 1015 1020 Glu Lys Gly Val Pro Gly Ile Pro Gly Pro Gln Gly Ser Pro Gly 1025 1030 1035 Leu Pro Gly Asp Lys Gly Ala Lys Gly Glu Lys Gly Gln Ala Gly 1040 1045 1050 Pro Pro Gly Ile Gly Ile Pro Gly Leu Arg Gly Glu Lys Gly Asp 1055 1060 1065 Gln Gly Ile Ala Gly Phe Pro Gly Ser Pro Gly Glu Lys Gly Glu 1070 1075 1080 Lys Gly Ser Ile Gly Ile Pro Gly Met Pro Gly Ser Pro Gly Leu 1085 1090 1095 Lys Gly Ser Pro Gly Ser Val Gly Tyr Pro Gly Ser Pro Gly Leu 1100 1105 1110 Pro Gly Glu Lys Gly Asp Lys Gly Leu Pro Gly Leu Asp Gly Ile 1115 1120 1125 Pro Gly Val Lys Gly Glu Ala Gly Leu Pro Gly Thr Pro Gly Pro 1130 1135 1140 Thr Gly Pro Ala Gly Gln Lys Gly Glu Pro Gly Ser Asp Gly Ile 1145 1150 1155 Pro Gly Ser Ala Gly Glu Lys Gly Glu Pro Gly Leu Pro Gly Arg 1160 1165 1170 Gly Phe Pro Gly Phe Pro Gly Ala Lys Gly Asp Lys Gly Ser Lys 1175 1180 1185 Gly Glu Val Gly Phe Pro Gly Leu Ala Gly Ser Pro Gly Ile Pro 1190 1195 1200 Gly Ser Lys Gly Glu Gln Gly Phe Met Gly Pro Pro Gly Pro Gln 1205 1210 1215 Gly Gln Pro Gly Leu Pro Gly Ser Pro Gly His Ala Thr Glu Gly 1220 1225 1230 Pro Lys Gly Asp Arg Gly Pro Gln Gly Gln Pro Gly Leu Pro Gly 1235 1240 1245 Leu Pro Gly Pro Met Gly Pro Pro Gly Leu Pro Gly Ile Asp Gly 1250 1255 1260 Val Lys Gly Asp Lys Gly Asn Pro Gly Trp Pro Gly Ala Pro Gly 1265 1270 1275 Val Pro Gly Pro Lys Gly Asp Pro Gly Phe Gln Gly Met Pro Gly 1280 1285 1290 Ile Gly Gly Ser Pro Gly Ile Thr Gly Ser Lys Gly Asp Met Gly 1295 1300 1305 Pro Pro Gly Val Pro Gly Phe Gln Gly Pro Lys Gly Leu Pro Gly 1310 1315 1320 Leu Gln Gly Ile Lys Gly Asp Gln Gly Asp Gln Gly Val Pro Gly 1325 1330 1335 Ala Lys Gly Leu Pro Gly Pro Pro Gly Pro Pro Gly Pro Tyr Asp 1340 1345 1350 Ile Ile Lys Gly Glu Pro Gly Leu Pro Gly Pro Glu Gly Pro Pro 1355 1360 1365 Gly Leu Lys Gly Leu Gln Gly Leu Pro Gly Pro Lys Gly Gln Gln 1370 1375 1380 Gly Val Thr Gly Leu Val Gly Ile Pro Gly Pro Pro Gly Ile Pro 1385 1390 1395 Gly Phe Asp Gly Ala Pro Gly Gln Lys Gly Glu Met Gly Pro Ala 1400 1405 1410 Gly Pro Thr Gly Pro Arg Gly Phe Pro Gly Pro Pro Gly Pro Asp 1415 1420 1425 Gly Leu Pro Gly Ser Met Gly Pro Pro Gly Thr Pro Ser Val Asp 1430 1435 1440 His Gly Phe Leu Val Thr Arg His Ser Gln Thr Ile Asp Asp Pro 1445 1450 1455 Gln Cys Pro Ser Gly Thr Lys Ile Leu Tyr His Gly Tyr Ser Leu 1460 1465 1470 Leu Tyr Val Gln Gly Asn Glu Arg Ala His Gly Gln Asp Leu Gly 1475 1480 1485 Thr Ala Gly Ser Cys Leu Arg Lys Phe Ser Thr Met Pro Phe Leu 1490 1495 1500 Phe Cys Asn Ile Asn Asn Val Cys Asn Phe Ala Ser Arg Asn Asp 1505 1510 1515 Tyr Ser Tyr Trp Leu Ser Thr Pro Glu Pro Met Pro Met Ser Met 1520 1525 1530 Ala Pro Ile Thr Gly Glu Asn Ile Arg Pro Phe Ile Ser Arg Cys 1535 1540 1545 Ala Val Cys Glu Ala Pro Ala Met Val Met Ala Val His Ser Gln 1550 1555 1560 Thr Ile Gln Ile Pro Pro Cys Pro Ser Gly Trp Ser Ser Leu Trp 1565 1570 1575 Ile Gly Tyr Ser Phe Val Met His Thr Ser Ala Gly Ala Glu Gly 1580 1585 1590 Ser Gly Gln Ala Leu Ala Ser Pro Gly Ser Cys Leu Glu Glu Phe 1595 1600 1605 Arg Ser Ala Pro Phe Ile Glu Cys His Gly Arg Gly Thr Cys Asn 1610 1615 1620 Tyr Tyr Ala Asn Ala Tyr Ser Phe Trp Leu Ala Thr Ile Glu Arg 1625 1630 1635 Ser Glu Met Phe Lys Lys Pro Thr Pro Ser Thr Leu Lys Ala Gly 1640 1645 1650 Glu Leu Arg Thr His Val Ser Arg Cys Gln Val Cys Met Arg Arg 1655 1660 1665 Thr <210> SEQ ID NO 61 <211> LENGTH: 1838 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P20908 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1838) <400> SEQUENCE: 61 Met Asp Val His Thr Arg Trp Lys Ala Arg Ser Ala Leu Arg Pro Gly 1 5 10 15 Ala Pro Leu Leu Pro Pro Leu Leu Leu Leu Leu Leu Trp Ala Pro Pro 20 25 30 Pro Ser Arg Ala Ala Gln Pro Ala Asp Leu Leu Lys Val Leu Asp Phe 35 40 45 His Asn Leu Pro Asp Gly Ile Thr Lys Thr Thr Gly Phe Cys Ala Thr 50 55 60 Arg Arg Ser Ser Lys Gly Pro Asp Val Ala Tyr Arg Val Thr Lys Asp 65 70 75 80 Ala Gln Leu Ser Ala Pro Thr Lys Gln Leu Tyr Pro Ala Ser Ala Phe 85 90 95 Pro Glu Asp Phe Ser Ile Leu Thr Thr Val Lys Ala Lys Lys Gly Ser 100 105 110 Gln Ala Phe Leu Val Ser Ile Tyr Asn Glu Gln Gly Ile Gln Gln Ile 115 120 125 Gly Leu Glu Leu Gly Arg Ser Pro Val Phe Leu Tyr Glu Asp His Thr 130 135 140 Gly Lys Pro Gly Pro Glu Asp Tyr Pro Leu Phe Arg Gly Ile Asn Leu 145 150 155 160 Ser Asp Gly Lys Trp His Arg Ile Ala Leu Ser Val His Lys Lys Asn 165 170 175 Val Thr Leu Ile Leu Asp Cys Lys Lys Lys Thr Thr Lys Phe Leu Asp 180 185 190 Arg Ser Asp His Pro Met Ile Asp Ile Asn Gly Ile Ile Val Phe Gly 195 200 205 Thr Arg Ile Leu Asp Glu Glu Val Phe Glu Gly Asp Ile Gln Gln Leu 210 215 220 Leu Phe Val Ser Asp His Arg Ala Ala Tyr Asp Tyr Cys Glu His Tyr 225 230 235 240 Ser Pro Asp Cys Asp Thr Ala Val Pro Asp Thr Pro Gln Ser Gln Asp 245 250 255 Pro Asn Pro Asp Glu Tyr Tyr Thr Glu Gly Asp Gly Glu Gly Glu Thr 260 265 270 Tyr Tyr Tyr Glu Tyr Pro Tyr Tyr Glu Asp Pro Glu Asp Leu Gly Lys 275 280 285 Glu Pro Thr Pro Ser Lys Lys Pro Val Glu Ala Ala Lys Glu Thr Thr 290 295 300 Glu Val Pro Glu Glu Leu Thr Pro Thr Pro Thr Glu Ala Ala Pro Met 305 310 315 320 Pro Glu Thr Ser Glu Gly Ala Gly Lys Glu Glu Asp Val Gly Ile Gly 325 330 335 Asp Tyr Asp Tyr Val Pro Ser Glu Asp Tyr Tyr Thr Pro Ser Pro Tyr 340 345 350 Asp Asp Leu Thr Tyr Gly Glu Gly Glu Glu Asn Pro Asp Gln Pro Thr 355 360 365 Asp Pro Gly Ala Gly Ala Glu Ile Pro Thr Ser Thr Ala Asp Thr Ser 370 375 380 Asn Ser Ser Asn Pro Ala Pro Pro Pro Gly Glu Gly Ala Asp Asp Leu 385 390 395 400 Glu Gly Glu Phe Thr Glu Glu Thr Ile Arg Asn Leu Asp Glu Asn Tyr 405 410 415 Tyr Asp Pro Tyr Tyr Asp Pro Thr Ser Ser Pro Ser Glu Ile Gly Pro 420 425 430 Gly Met Pro Ala Asn Gln Asp Thr Ile Tyr Glu Gly Ile Gly Gly Pro 435 440 445 Arg Gly Glu Lys Gly Gln Lys Gly Glu Pro Ala Ile Ile Glu Pro Gly 450 455 460 Met Leu Ile Glu Gly Pro Pro Gly Pro Glu Gly Pro Ala Gly Leu Pro 465 470 475 480 Gly Pro Pro Gly Thr Met Gly Pro Thr Gly Gln Val Gly Asp Pro Gly 485 490 495 Glu Arg Gly Pro Pro Gly Arg Pro Gly Leu Pro Gly Ala Asp Gly Leu 500 505 510 Pro Gly Pro Pro Gly Thr Met Leu Met Leu Pro Phe Arg Phe Gly Gly 515 520 525 Gly Gly Asp Ala Gly Ser Lys Gly Pro Met Val Ser Ala Gln Glu Ser 530 535 540 Gln Ala Gln Ala Ile Leu Gln Gln Ala Arg Leu Ala Leu Arg Gly Pro 545 550 555 560 Ala Gly Pro Met Gly Leu Thr Gly Arg Pro Gly Pro Val Gly Pro Pro 565 570 575 Gly Ser Gly Gly Leu Lys Gly Glu Pro Gly Asp Val Gly Pro Gln Gly 580 585 590 Pro Arg Gly Val Gln Gly Pro Pro Gly Pro Ala Gly Lys Pro Gly Arg 595 600 605 Arg Gly Arg Ala Gly Ser Asp Gly Ala Arg Gly Met Pro Gly Gln Thr 610 615 620 Gly Pro Lys Gly Asp Arg Gly Phe Asp Gly Leu Ala Gly Leu Pro Gly 625 630 635 640 Glu Lys Gly His Arg Gly Asp Pro Gly Pro Ser Gly Pro Pro Gly Pro 645 650 655 Pro Gly Asp Asp Gly Glu Arg Gly Asp Asp Gly Glu Val Gly Pro Arg 660 665 670 Gly Leu Pro Gly Glu Pro Gly Pro Arg Gly Leu Leu Gly Pro Lys Gly 675 680 685 Pro Pro Gly Pro Pro Gly Pro Pro Gly Val Thr Gly Met Asp Gly Gln 690 695 700 Pro Gly Pro Lys Gly Asn Val Gly Pro Gln Gly Glu Pro Gly Pro Pro 705 710 715 720 Gly Gln Gln Gly Asn Pro Gly Ala Gln Gly Leu Pro Gly Pro Gln Gly 725 730 735 Ala Ile Gly Pro Pro Gly Glu Lys Gly Pro Leu Gly Lys Pro Gly Leu 740 745 750 Pro Gly Met Pro Gly Ala Asp Gly Pro Pro Gly His Pro Gly Lys Glu 755 760 765 Gly Pro Pro Gly Glu Lys Gly Gly Gln Gly Pro Pro Gly Pro Gln Gly 770 775 780 Pro Ile Gly Tyr Pro Gly Pro Arg Gly Val Lys Gly Ala Asp Gly Ile 785 790 795 800 Arg Gly Leu Lys Gly Thr Lys Gly Glu Lys Gly Glu Asp Gly Phe Pro 805 810 815 Gly Phe Lys Gly Asp Met Gly Ile Lys Gly Asp Arg Gly Glu Ile Gly 820 825 830 Pro Pro Gly Pro Arg Gly Glu Asp Gly Pro Glu Gly Pro Lys Gly Arg 835 840 845 Gly Gly Pro Asn Gly Asp Pro Gly Pro Leu Gly Pro Pro Gly Glu Lys 850 855 860 Gly Lys Leu Gly Val Pro Gly Leu Pro Gly Tyr Pro Gly Arg Gln Gly 865 870 875 880 Pro Lys Gly Ser Ile Gly Phe Pro Gly Phe Pro Gly Ala Asn Gly Glu 885 890 895 Lys Gly Gly Arg Gly Thr Pro Gly Lys Pro Gly Pro Arg Gly Gln Arg 900 905 910 Gly Pro Thr Gly Pro Arg Gly Glu Arg Gly Pro Arg Gly Ile Thr Gly 915 920 925 Lys Pro Gly Pro Lys Gly Asn Ser Gly Gly Asp Gly Pro Ala Gly Pro 930 935 940 Pro Gly Glu Arg Gly Pro Asn Gly Pro Gln Gly Pro Thr Gly Phe Pro 945 950 955 960 Gly Pro Lys Gly Pro Pro Gly Pro Pro Gly Lys Asp Gly Leu Pro Gly 965 970 975 His Pro Gly Gln Arg Gly Glu Thr Gly Phe Gln Gly Lys Thr Gly Pro 980 985 990 Pro Gly Pro Pro Gly Val Val Gly Pro Gln Gly Pro Thr Gly Glu Thr 995 1000 1005 Gly Pro Met Gly Glu Arg Gly His Pro Gly Pro Pro Gly Pro Pro 1010 1015 1020 Gly Glu Gln Gly Leu Pro Gly Leu Ala Gly Lys Glu Gly Thr Lys 1025 1030 1035 Gly Asp Pro Gly Pro Ala Gly Leu Pro Gly Lys Asp Gly Pro Pro 1040 1045 1050 Gly Leu Arg Gly Phe Pro Gly Asp Arg Gly Leu Pro Gly Pro Val 1055 1060 1065 Gly Ala Leu Gly Leu Lys Gly Asn Glu Gly Pro Pro Gly Pro Pro 1070 1075 1080 Gly Pro Ala Gly Ser Pro Gly Glu Arg Gly Pro Ala Gly Ala Ala 1085 1090 1095 Gly Pro Ile Gly Ile Pro Gly Arg Pro Gly Pro Gln Gly Pro Pro 1100 1105 1110 Gly Pro Ala Gly Glu Lys Gly Ala Pro Gly Glu Lys Gly Pro Gln 1115 1120 1125 Gly Pro Ala Gly Arg Asp Gly Leu Gln Gly Pro Val Gly Leu Pro 1130 1135 1140 Gly Pro Ala Gly Pro Val Gly Pro Pro Gly Glu Asp Gly Asp Lys 1145 1150 1155 Gly Glu Ile Gly Glu Pro Gly Gln Lys Gly Ser Lys Gly Asp Lys 1160 1165 1170 Gly Glu Gln Gly Pro Pro Gly Pro Thr Gly Pro Gln Gly Pro Ile 1175 1180 1185 Gly Gln Pro Gly Pro Ser Gly Ala Asp Gly Glu Pro Gly Pro Arg 1190 1195 1200 Gly Gln Gln Gly Leu Phe Gly Gln Lys Gly Asp Glu Gly Pro Arg 1205 1210 1215 Gly Phe Pro Gly Pro Pro Gly Pro Val Gly Leu Gln Gly Leu Pro 1220 1225 1230 Gly Pro Pro Gly Glu Lys Gly Glu Thr Gly Asp Val Gly Gln Met 1235 1240 1245 Gly Pro Pro Gly Pro Pro Gly Pro Arg Gly Pro Ser Gly Ala Pro 1250 1255 1260 Gly Ala Asp Gly Pro Gln Gly Pro Pro Gly Gly Ile Gly Asn Pro 1265 1270 1275 Gly Ala Val Gly Glu Lys Gly Glu Pro Gly Glu Ala Gly Glu Pro 1280 1285 1290 Gly Leu Pro Gly Glu Gly Gly Pro Pro Gly Pro Lys Gly Glu Arg 1295 1300 1305 Gly Glu Lys Gly Glu Ser Gly Pro Ser Gly Ala Ala Gly Pro Pro 1310 1315 1320 Gly Pro Lys Gly Pro Pro Gly Asp Asp Gly Pro Lys Gly Ser Pro 1325 1330 1335 Gly Pro Val Gly Phe Pro Gly Asp Pro Gly Pro Pro Gly Glu Pro 1340 1345 1350 Gly Pro Ala Gly Gln Asp Gly Pro Pro Gly Asp Lys Gly Asp Asp 1355 1360 1365 Gly Glu Pro Gly Gln Thr Gly Ser Pro Gly Pro Thr Gly Glu Pro 1370 1375 1380 Gly Pro Ser Gly Pro Pro Gly Lys Arg Gly Pro Pro Gly Pro Ala 1385 1390 1395 Gly Pro Glu Gly Arg Gln Gly Glu Lys Gly Ala Lys Gly Glu Ala 1400 1405 1410 Gly Leu Glu Gly Pro Pro Gly Lys Thr Gly Pro Ile Gly Pro Gln 1415 1420 1425 Gly Ala Pro Gly Lys Pro Gly Pro Asp Gly Leu Arg Gly Ile Pro 1430 1435 1440 Gly Pro Val Gly Glu Gln Gly Leu Pro Gly Ser Pro Gly Pro Asp 1445 1450 1455 Gly Pro Pro Gly Pro Met Gly Pro Pro Gly Leu Pro Gly Leu Lys 1460 1465 1470 Gly Asp Ser Gly Pro Lys Gly Glu Lys Gly His Pro Gly Leu Ile 1475 1480 1485 Gly Leu Ile Gly Pro Pro Gly Glu Gln Gly Glu Lys Gly Asp Arg 1490 1495 1500 Gly Leu Pro Gly Pro Gln Gly Ser Ser Gly Pro Lys Gly Glu Gln 1505 1510 1515 Gly Ile Thr Gly Pro Ser Gly Pro Ile Gly Pro Pro Gly Pro Pro 1520 1525 1530 Gly Leu Pro Gly Pro Pro Gly Pro Lys Gly Ala Lys Gly Ser Ser 1535 1540 1545 Gly Pro Thr Gly Pro Lys Gly Glu Ala Gly His Pro Gly Pro Pro 1550 1555 1560 Gly Pro Pro Gly Pro Pro Gly Glu Val Ile Gln Pro Leu Pro Ile 1565 1570 1575 Gln Ala Ser Arg Thr Arg Arg Asn Ile Asp Ala Ser Gln Leu Leu 1580 1585 1590 Asp Asp Gly Asn Gly Glu Asn Tyr Val Asp Tyr Ala Asp Gly Met 1595 1600 1605 Glu Glu Ile Phe Gly Ser Leu Asn Ser Leu Lys Leu Glu Ile Glu 1610 1615 1620 Gln Met Lys Arg Pro Leu Gly Thr Gln Gln Asn Pro Ala Arg Thr 1625 1630 1635 Cys Lys Asp Leu Gln Leu Cys His Pro Asp Phe Pro Asp Gly Glu 1640 1645 1650 Tyr Trp Val Asp Pro Asn Gln Gly Cys Ser Arg Asp Ser Phe Lys 1655 1660 1665 Val Tyr Cys Asn Phe Thr Ala Gly Gly Ser Thr Cys Val Phe Pro 1670 1675 1680 Asp Lys Lys Ser Glu Gly Ala Arg Ile Thr Ser Trp Pro Lys Glu 1685 1690 1695 Asn Pro Gly Ser Trp Phe Ser Glu Phe Lys Arg Gly Lys Leu Leu 1700 1705 1710 Ser Tyr Val Asp Ala Glu Gly Asn Pro Val Gly Val Val Gln Met 1715 1720 1725 Thr Phe Leu Arg Leu Leu Ser Ala Ser Ala His Gln Asn Val Thr 1730 1735 1740 Tyr His Cys Tyr Gln Ser Val Ala Trp Gln Asp Ala Ala Thr Gly 1745 1750 1755 Ser Tyr Asp Lys Ala Leu Arg Phe Leu Gly Ser Asn Asp Glu Glu 1760 1765 1770 Met Ser Tyr Asp Asn Asn Pro Tyr Ile Arg Ala Leu Val Asp Gly 1775 1780 1785 Cys Ala Thr Lys Lys Gly Tyr Gln Lys Thr Val Leu Glu Ile Asp 1790 1795 1800 Thr Pro Lys Val Glu Gln Val Pro Ile Val Asp Ile Met Phe Asn 1805 1810 1815 Asp Phe Gly Glu Ala Ser Gln Lys Phe Gly Phe Glu Val Gly Pro 1820 1825 1830 Ala Cys Phe Met Gly 1835 <210> SEQ ID NO 62 <211> LENGTH: 223 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16410 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(223) <400> SEQUENCE: 62 Met Ala Cys Leu Gly Phe Gln Arg His Lys Ala Gln Leu Asn Leu Ala 1 5 10 15 Thr Arg Thr Trp Pro Cys Thr Leu Leu Phe Phe Leu Leu Phe Ile Pro 20 25 30 Val Phe Cys Lys Ala Met His Val Ala Gln Pro Ala Val Val Leu Ala 35 40 45 Ser Ser Arg Gly Ile Ala Ser Phe Val Cys Glu Tyr Ala Ser Pro Gly 50 55 60 Lys Ala Thr Glu Val Arg Val Thr Val Leu Arg Gln Ala Asp Ser Gln 65 70 75 80 Val Thr Glu Val Cys Ala Ala Thr Tyr Met Met Gly Asn Glu Leu Thr 85 90 95 Phe Leu Asp Asp Ser Ile Cys Thr Gly Thr Ser Ser Gly Asn Gln Val 100 105 110 Asn Leu Thr Ile Gln Gly Leu Arg Ala Met Asp Thr Gly Leu Tyr Ile 115 120 125 Cys Lys Val Glu Leu Met Tyr Pro Pro Pro Tyr Tyr Leu Gly Ile Gly 130 135 140 Asn Gly Thr Gln Ile Tyr Val Ile Asp Pro Glu Pro Cys Pro Asp Ser 145 150 155 160 Asp Phe Leu Leu Trp Ile Leu Ala Ala Val Ser Ser Gly Leu Phe Phe 165 170 175 Tyr Ser Phe Leu Leu Thr Ala Val Ser Leu Ser Lys Met Leu Lys Lys 180 185 190 Arg Ser Pro Leu Thr Thr Gly Val Tyr Val Lys Met Pro Pro Thr Glu 195 200 205 Pro Glu Cys Glu Lys Gln Phe Gln Pro Tyr Phe Ile Pro Ile Asn 210 215 220 <210> SEQ ID NO 63 <211> LENGTH: 339 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O94905 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(339) <400> SEQUENCE: 63 Met Ala Gln Leu Gly Ala Val Val Ala Val Ala Ser Ser Phe Phe Cys 1 5 10 15 Ala Ser Leu Phe Ser Ala Val His Lys Ile Glu Glu Gly His Ile Gly 20 25 30 Val Tyr Tyr Arg Gly Gly Ala Leu Leu Thr Ser Thr Ser Gly Pro Gly 35 40 45 Phe His Leu Met Leu Pro Phe Ile Thr Ser Tyr Lys Ser Val Gln Thr 50 55 60 Thr Leu Gln Thr Asp Glu Val Lys Asn Val Pro Cys Gly Thr Ser Gly 65 70 75 80 Gly Val Met Ile Tyr Phe Asp Arg Ile Glu Val Val Asn Phe Leu Val 85 90 95 Pro Asn Ala Val Tyr Asp Ile Val Lys Asn Tyr Thr Ala Asp Tyr Asp 100 105 110 Lys Ala Leu Ile Phe Asn Lys Ile His His Glu Leu Asn Gln Phe Cys 115 120 125 Ser Val His Thr Leu Gln Glu Val Tyr Ile Glu Leu Phe Asp Gln Ile 130 135 140 Asp Glu Asn Leu Lys Leu Ala Leu Gln Gln Asp Leu Thr Ser Met Ala 145 150 155 160 Pro Gly Leu Val Ile Gln Ala Val Arg Val Thr Lys Pro Asn Ile Pro 165 170 175 Glu Ala Ile Arg Arg Asn Tyr Glu Leu Met Glu Ser Glu Lys Thr Lys 180 185 190 Leu Leu Ile Ala Ala Gln Lys Gln Lys Val Val Glu Lys Glu Ala Glu 195 200 205 Thr Glu Arg Lys Lys Ala Leu Ile Glu Ala Glu Lys Val Ala Gln Val 210 215 220 Ala Glu Ile Thr Tyr Gly Gln Lys Val Met Glu Lys Glu Thr Glu Lys 225 230 235 240 Lys Ile Ser Glu Ile Glu Asp Ala Ala Phe Leu Ala Arg Glu Lys Ala 245 250 255 Lys Ala Asp Ala Glu Cys Tyr Thr Ala Met Lys Ile Ala Glu Ala Asn 260 265 270 Lys Leu Lys Leu Thr Pro Glu Tyr Leu Gln Leu Met Lys Tyr Lys Ala 275 280 285 Ile Ala Ser Asn Ser Lys Ile Tyr Phe Gly Lys Asp Ile Pro Asn Met 290 295 300 Phe Met Asp Ser Ala Gly Ser Val Ser Lys Gln Phe Glu Gly Leu Ala 305 310 315 320 Asp Lys Leu Ser Phe Gly Leu Glu Asp Glu Pro Leu Glu Thr Ala Thr 325 330 335 Lys Glu Asn <210> SEQ ID NO 64 <211> LENGTH: 2386 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02751 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(2386) <400> SEQUENCE: 64 Met Leu Arg Gly Pro Gly Pro Gly Leu Leu Leu Leu Ala Val Gln Cys 1 5 10 15 Leu Gly Thr Ala Val Pro Ser Thr Gly Ala Ser Lys Ser Lys Arg Gln 20 25 30 Ala Gln Gln Met Val Gln Pro Gln Ser Pro Val Ala Val Ser Gln Ser 35 40 45 Lys Pro Gly Cys Tyr Asp Asn Gly Lys His Tyr Gln Ile Asn Gln Gln 50 55 60 Trp Glu Arg Thr Tyr Leu Gly Asn Ala Leu Val Cys Thr Cys Tyr Gly 65 70 75 80 Gly Ser Arg Gly Phe Asn Cys Glu Ser Lys Pro Glu Ala Glu Glu Thr 85 90 95 Cys Phe Asp Lys Tyr Thr Gly Asn Thr Tyr Arg Val Gly Asp Thr Tyr 100 105 110 Glu Arg Pro Lys Asp Ser Met Ile Trp Asp Cys Thr Cys Ile Gly Ala 115 120 125 Gly Arg Gly Arg Ile Ser Cys Thr Ile Ala Asn Arg Cys His Glu Gly 130 135 140 Gly Gln Ser Tyr Lys Ile Gly Asp Thr Trp Arg Arg Pro His Glu Thr 145 150 155 160 Gly Gly Tyr Met Leu Glu Cys Val Cys Leu Gly Asn Gly Lys Gly Glu 165 170 175 Trp Thr Cys Lys Pro Ile Ala Glu Lys Cys Phe Asp His Ala Ala Gly 180 185 190 Thr Ser Tyr Val Val Gly Glu Thr Trp Glu Lys Pro Tyr Gln Gly Trp 195 200 205 Met Met Val Asp Cys Thr Cys Leu Gly Glu Gly Ser Gly Arg Ile Thr 210 215 220 Cys Thr Ser Arg Asn Arg Cys Asn Asp Gln Asp Thr Arg Thr Ser Tyr 225 230 235 240 Arg Ile Gly Asp Thr Trp Ser Lys Lys Asp Asn Arg Gly Asn Leu Leu 245 250 255 Gln Cys Ile Cys Thr Gly Asn Gly Arg Gly Glu Trp Lys Cys Glu Arg 260 265 270 His Thr Ser Val Gln Thr Thr Ser Ser Gly Ser Gly Pro Phe Thr Asp 275 280 285 Val Arg Ala Ala Val Tyr Gln Pro Gln Pro His Pro Gln Pro Pro Pro 290 295 300 Tyr Gly His Cys Val Thr Asp Ser Gly Val Val Tyr Ser Val Gly Met 305 310 315 320 Gln Trp Leu Lys Thr Gln Gly Asn Lys Gln Met Leu Cys Thr Cys Leu 325 330 335 Gly Asn Gly Val Ser Cys Gln Glu Thr Ala Val Thr Gln Thr Tyr Gly 340 345 350 Gly Asn Ser Asn Gly Glu Pro Cys Val Leu Pro Phe Thr Tyr Asn Gly 355 360 365 Arg Thr Phe Tyr Ser Cys Thr Thr Glu Gly Arg Gln Asp Gly His Leu 370 375 380 Trp Cys Ser Thr Thr Ser Asn Tyr Glu Gln Asp Gln Lys Tyr Ser Phe 385 390 395 400 Cys Thr Asp His Thr Val Leu Val Gln Thr Arg Gly Gly Asn Ser Asn 405 410 415 Gly Ala Leu Cys His Phe Pro Phe Leu Tyr Asn Asn His Asn Tyr Thr 420 425 430 Asp Cys Thr Ser Glu Gly Arg Arg Asp Asn Met Lys Trp Cys Gly Thr 435 440 445 Thr Gln Asn Tyr Asp Ala Asp Gln Lys Phe Gly Phe Cys Pro Met Ala 450 455 460 Ala His Glu Glu Ile Cys Thr Thr Asn Glu Gly Val Met Tyr Arg Ile 465 470 475 480 Gly Asp Gln Trp Asp Lys Gln His Asp Met Gly His Met Met Arg Cys 485 490 495 Thr Cys Val Gly Asn Gly Arg Gly Glu Trp Thr Cys Ile Ala Tyr Ser 500 505 510 Gln Leu Arg Asp Gln Cys Ile Val Asp Asp Ile Thr Tyr Asn Val Asn 515 520 525 Asp Thr Phe His Lys Arg His Glu Glu Gly His Met Leu Asn Cys Thr 530 535 540 Cys Phe Gly Gln Gly Arg Gly Arg Trp Lys Cys Asp Pro Val Asp Gln 545 550 555 560 Cys Gln Asp Ser Glu Thr Gly Thr Phe Tyr Gln Ile Gly Asp Ser Trp 565 570 575 Glu Lys Tyr Val His Gly Val Arg Tyr Gln Cys Tyr Cys Tyr Gly Arg 580 585 590 Gly Ile Gly Glu Trp His Cys Gln Pro Leu Gln Thr Tyr Pro Ser Ser 595 600 605 Ser Gly Pro Val Glu Val Phe Ile Thr Glu Thr Pro Ser Gln Pro Asn 610 615 620 Ser His Pro Ile Gln Trp Asn Ala Pro Gln Pro Ser His Ile Ser Lys 625 630 635 640 Tyr Ile Leu Arg Trp Arg Pro Lys Asn Ser Val Gly Arg Trp Lys Glu 645 650 655 Ala Thr Ile Pro Gly His Leu Asn Ser Tyr Thr Ile Lys Gly Leu Lys 660 665 670 Pro Gly Val Val Tyr Glu Gly Gln Leu Ile Ser Ile Gln Gln Tyr Gly 675 680 685 His Gln Glu Val Thr Arg Phe Asp Phe Thr Thr Thr Ser Thr Ser Thr 690 695 700 Pro Val Thr Ser Asn Thr Val Thr Gly Glu Thr Thr Pro Phe Ser Pro 705 710 715 720 Leu Val Ala Thr Ser Glu Ser Val Thr Glu Ile Thr Ala Ser Ser Phe 725 730 735 Val Val Ser Trp Val Ser Ala Ser Asp Thr Val Ser Gly Phe Arg Val 740 745 750 Glu Tyr Glu Leu Ser Glu Glu Gly Asp Glu Pro Gln Tyr Leu Asp Leu 755 760 765 Pro Ser Thr Ala Thr Ser Val Asn Ile Pro Asp Leu Leu Pro Gly Arg 770 775 780 Lys Tyr Ile Val Asn Val Tyr Gln Ile Ser Glu Asp Gly Glu Gln Ser 785 790 795 800 Leu Ile Leu Ser Thr Ser Gln Thr Thr Ala Pro Asp Ala Pro Pro Asp 805 810 815 Thr Thr Val Asp Gln Val Asp Asp Thr Ser Ile Val Val Arg Trp Ser 820 825 830 Arg Pro Gln Ala Pro Ile Thr Gly Tyr Arg Ile Val Tyr Ser Pro Ser 835 840 845 Val Glu Gly Ser Ser Thr Glu Leu Asn Leu Pro Glu Thr Ala Asn Ser 850 855 860 Val Thr Leu Ser Asp Leu Gln Pro Gly Val Gln Tyr Asn Ile Thr Ile 865 870 875 880 Tyr Ala Val Glu Glu Asn Gln Glu Ser Thr Pro Val Val Ile Gln Gln 885 890 895 Glu Thr Thr Gly Thr Pro Arg Ser Asp Thr Val Pro Ser Pro Arg Asp 900 905 910 Leu Gln Phe Val Glu Val Thr Asp Val Lys Val Thr Ile Met Trp Thr 915 920 925 Pro Pro Glu Ser Ala Val Thr Gly Tyr Arg Val Asp Val Ile Pro Val 930 935 940 Asn Leu Pro Gly Glu His Gly Gln Arg Leu Pro Ile Ser Arg Asn Thr 945 950 955 960 Phe Ala Glu Val Thr Gly Leu Ser Pro Gly Val Thr Tyr Tyr Phe Lys 965 970 975 Val Phe Ala Val Ser His Gly Arg Glu Ser Lys Pro Leu Thr Ala Gln 980 985 990 Gln Thr Thr Lys Leu Asp Ala Pro Thr Asn Leu Gln Phe Val Asn Glu 995 1000 1005 Thr Asp Ser Thr Val Leu Val Arg Trp Thr Pro Pro Arg Ala Gln 1010 1015 1020 Ile Thr Gly Tyr Arg Leu Thr Val Gly Leu Thr Arg Arg Gly Gln 1025 1030 1035 Pro Arg Gln Tyr Asn Val Gly Pro Ser Val Ser Lys Tyr Pro Leu 1040 1045 1050 Arg Asn Leu Gln Pro Ala Ser Glu Tyr Thr Val Ser Leu Val Ala 1055 1060 1065 Ile Lys Gly Asn Gln Glu Ser Pro Lys Ala Thr Gly Val Phe Thr 1070 1075 1080 Thr Leu Gln Pro Gly Ser Ser Ile Pro Pro Tyr Asn Thr Glu Val 1085 1090 1095 Thr Glu Thr Thr Ile Val Ile Thr Trp Thr Pro Ala Pro Arg Ile 1100 1105 1110 Gly Phe Lys Leu Gly Val Arg Pro Ser Gln Gly Gly Glu Ala Pro 1115 1120 1125 Arg Glu Val Thr Ser Asp Ser Gly Ser Ile Val Val Ser Gly Leu 1130 1135 1140 Thr Pro Gly Val Glu Tyr Val Tyr Thr Ile Gln Val Leu Arg Asp 1145 1150 1155 Gly Gln Glu Arg Asp Ala Pro Ile Val Asn Lys Val Val Thr Pro 1160 1165 1170 Leu Ser Pro Pro Thr Asn Leu His Leu Glu Ala Asn Pro Asp Thr 1175 1180 1185 Gly Val Leu Thr Val Ser Trp Glu Arg Ser Thr Thr Pro Asp Ile 1190 1195 1200 Thr Gly Tyr Arg Ile Thr Thr Thr Pro Thr Asn Gly Gln Gln Gly 1205 1210 1215 Asn Ser Leu Glu Glu Val Val His Ala Asp Gln Ser Ser Cys Thr 1220 1225 1230 Phe Asp Asn Leu Ser Pro Gly Leu Glu Tyr Asn Val Ser Val Tyr 1235 1240 1245 Thr Val Lys Asp Asp Lys Glu Ser Val Pro Ile Ser Asp Thr Ile 1250 1255 1260 Ile Pro Ala Val Pro Pro Pro Thr Asp Leu Arg Phe Thr Asn Ile 1265 1270 1275 Gly Pro Asp Thr Met Arg Val Thr Trp Ala Pro Pro Pro Ser Ile 1280 1285 1290 Asp Leu Thr Asn Phe Leu Val Arg Tyr Ser Pro Val Lys Asn Glu 1295 1300 1305 Glu Asp Val Ala Glu Leu Ser Ile Ser Pro Ser Asp Asn Ala Val 1310 1315 1320 Val Leu Thr Asn Leu Leu Pro Gly Thr Glu Tyr Val Val Ser Val 1325 1330 1335 Ser Ser Val Tyr Glu Gln His Glu Ser Thr Pro Leu Arg Gly Arg 1340 1345 1350 Gln Lys Thr Gly Leu Asp Ser Pro Thr Gly Ile Asp Phe Ser Asp 1355 1360 1365 Ile Thr Ala Asn Ser Phe Thr Val His Trp Ile Ala Pro Arg Ala 1370 1375 1380 Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro Glu His Phe Ser 1385 1390 1395 Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg Asn Ser Ile 1400 1405 1410 Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val Ser Ile 1415 1420 1425 Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Leu Leu Ile Gly Gln 1430 1435 1440 Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 1445 1450 1455 Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val 1460 1465 1470 Thr Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn 1475 1480 1485 Ser Pro Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala 1490 1495 1500 Thr Ile Ser Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val 1505 1510 1515 Tyr Ala Val Thr Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro 1520 1525 1530 Ile Ser Ile Asn Tyr Arg Thr Glu Ile Asp Lys Pro Ser Gln Met 1535 1540 1545 Gln Val Thr Asp Val Gln Asp Asn Ser Ile Ser Val Lys Trp Leu 1550 1555 1560 Pro Ser Ser Ser Pro Val Thr Gly Tyr Arg Val Thr Thr Thr Pro 1565 1570 1575 Lys Asn Gly Pro Gly Pro Thr Lys Thr Lys Thr Ala Gly Pro Asp 1580 1585 1590 Gln Thr Glu Met Thr Ile Glu Gly Leu Gln Pro Thr Val Glu Tyr 1595 1600 1605 Val Val Ser Val Tyr Ala Gln Asn Pro Ser Gly Glu Ser Gln Pro 1610 1615 1620 Leu Val Gln Thr Ala Val Thr Asn Ile Asp Arg Pro Lys Gly Leu 1625 1630 1635 Ala Phe Thr Asp Val Asp Val Asp Ser Ile Lys Ile Ala Trp Glu 1640 1645 1650 Ser Pro Gln Gly Gln Val Ser Arg Tyr Arg Val Thr Tyr Ser Ser 1655 1660 1665 Pro Glu Asp Gly Ile His Glu Leu Phe Pro Ala Pro Asp Gly Glu 1670 1675 1680 Glu Asp Thr Ala Glu Leu Gln Gly Leu Arg Pro Gly Ser Glu Tyr 1685 1690 1695 Thr Val Ser Val Val Ala Leu His Asp Asp Met Glu Ser Gln Pro 1700 1705 1710 Leu Ile Gly Thr Gln Ser Thr Ala Ile Pro Ala Pro Thr Asp Leu 1715 1720 1725 Lys Phe Thr Gln Val Thr Pro Thr Ser Leu Ser Ala Gln Trp Thr 1730 1735 1740 Pro Pro Asn Val Gln Leu Thr Gly Tyr Arg Val Arg Val Thr Pro 1745 1750 1755 Lys Glu Lys Thr Gly Pro Met Lys Glu Ile Asn Leu Ala Pro Asp 1760 1765 1770 Ser Ser Ser Val Val Val Ser Gly Leu Met Val Ala Thr Lys Tyr 1775 1780 1785 Glu Val Ser Val Tyr Ala Leu Lys Asp Thr Leu Thr Ser Arg Pro 1790 1795 1800 Ala Gln Gly Val Val Thr Thr Leu Glu Asn Val Ser Pro Pro Arg 1805 1810 1815 Arg Ala Arg Val Thr Asp Ala Thr Glu Thr Thr Ile Thr Ile Ser 1820 1825 1830 Trp Arg Thr Lys Thr Glu Thr Ile Thr Gly Phe Gln Val Asp Ala 1835 1840 1845 Val Pro Ala Asn Gly Gln Thr Pro Ile Gln Arg Thr Ile Lys Pro 1850 1855 1860 Asp Val Arg Ser Tyr Thr Ile Thr Gly Leu Gln Pro Gly Thr Asp 1865 1870 1875 Tyr Lys Ile Tyr Leu Tyr Thr Leu Asn Asp Asn Ala Arg Ser Ser 1880 1885 1890 Pro Val Val Ile Asp Ala Ser Thr Ala Ile Asp Ala Pro Ser Asn 1895 1900 1905 Leu Arg Phe Leu Ala Thr Thr Pro Asn Ser Leu Leu Val Ser Trp 1910 1915 1920 Gln Pro Pro Arg Ala Arg Ile Thr Gly Tyr Ile Ile Lys Tyr Glu 1925 1930 1935 Lys Pro Gly Ser Pro Pro Arg Glu Val Val Pro Arg Pro Arg Pro 1940 1945 1950 Gly Val Thr Glu Ala Thr Ile Thr Gly Leu Glu Pro Gly Thr Glu 1955 1960 1965 Tyr Thr Ile Tyr Val Ile Ala Leu Lys Asn Asn Gln Lys Ser Glu 1970 1975 1980 Pro Leu Ile Gly Arg Lys Lys Thr Asp Glu Leu Pro Gln Leu Val 1985 1990 1995 Thr Leu Pro His Pro Asn Leu His Gly Pro Glu Ile Leu Asp Val 2000 2005 2010 Pro Ser Thr Val Gln Lys Thr Pro Phe Val Thr His Pro Gly Tyr 2015 2020 2025 Asp Thr Gly Asn Gly Ile Gln Leu Pro Gly Thr Ser Gly Gln Gln 2030 2035 2040 Pro Ser Val Gly Gln Gln Met Ile Phe Glu Glu His Gly Phe Arg 2045 2050 2055 Arg Thr Thr Pro Pro Thr Thr Ala Thr Pro Ile Arg His Arg Pro 2060 2065 2070 Arg Pro Tyr Pro Pro Asn Val Gly Glu Glu Ile Gln Ile Gly His 2075 2080 2085 Ile Pro Arg Glu Asp Val Asp Tyr His Leu Tyr Pro His Gly Pro 2090 2095 2100 Gly Leu Asn Pro Asn Ala Ser Thr Gly Gln Glu Ala Leu Ser Gln 2105 2110 2115 Thr Thr Ile Ser Trp Ala Pro Phe Gln Asp Thr Ser Glu Tyr Ile 2120 2125 2130 Ile Ser Cys His Pro Val Gly Thr Asp Glu Glu Pro Leu Gln Phe 2135 2140 2145 Arg Val Pro Gly Thr Ser Thr Ser Ala Thr Leu Thr Gly Leu Thr 2150 2155 2160 Arg Gly Ala Thr Tyr Asn Val Ile Val Glu Ala Leu Lys Asp Gln 2165 2170 2175 Gln Arg His Lys Val Arg Glu Glu Val Val Thr Val Gly Asn Ser 2180 2185 2190 Val Asn Glu Gly Leu Asn Gln Pro Thr Asp Asp Ser Cys Phe Asp 2195 2200 2205 Pro Tyr Thr Val Ser His Tyr Ala Val Gly Asp Glu Trp Glu Arg 2210 2215 2220 Met Ser Glu Ser Gly Phe Lys Leu Leu Cys Gln Cys Leu Gly Phe 2225 2230 2235 Gly Ser Gly His Phe Arg Cys Asp Ser Ser Arg Trp Cys His Asp 2240 2245 2250 Asn Gly Val Asn Tyr Lys Ile Gly Glu Lys Trp Asp Arg Gln Gly 2255 2260 2265 Glu Asn Gly Gln Met Met Ser Cys Thr Cys Leu Gly Asn Gly Lys 2270 2275 2280 Gly Glu Phe Lys Cys Asp Pro His Glu Ala Thr Cys Tyr Asp Asp 2285 2290 2295 Gly Lys Thr Tyr His Val Gly Glu Gln Trp Gln Lys Glu Tyr Leu 2300 2305 2310 Gly Ala Ile Cys Ser Cys Thr Cys Phe Gly Gly Gln Arg Gly Trp 2315 2320 2325 Arg Cys Asp Asn Cys Arg Arg Pro Gly Gly Glu Pro Ser Pro Glu 2330 2335 2340 Gly Thr Thr Gly Gln Ser Tyr Asn Gln Tyr Ser Gln Arg Tyr His 2345 2350 2355 Gln Arg Thr Asn Thr Asn Val Asn Cys Pro Ile Glu Cys Phe Met 2360 2365 2370 Pro Leu Asp Val Gln Ala Asp Arg Glu Asp Ser Arg Glu 2375 2380 2385 <210> SEQ ID NO 65 <211> LENGTH: 240 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P30711 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(240) <400> SEQUENCE: 65 Met Gly Leu Glu Leu Tyr Leu Asp Leu Leu Ser Gln Pro Cys Arg Ala 1 5 10 15 Val Tyr Ile Phe Ala Lys Lys Asn Asp Ile Pro Phe Glu Leu Arg Ile 20 25 30 Val Asp Leu Ile Lys Gly Gln His Leu Ser Asp Ala Phe Ala Gln Val 35 40 45 Asn Pro Leu Lys Lys Val Pro Ala Leu Lys Asp Gly Asp Phe Thr Leu 50 55 60 Thr Glu Ser Val Ala Ile Leu Leu Tyr Leu Thr Arg Lys Tyr Lys Val 65 70 75 80 Pro Asp Tyr Trp Tyr Pro Gln Asp Leu Gln Ala Arg Ala Arg Val Asp 85 90 95 Glu Tyr Leu Ala Trp Gln His Thr Thr Leu Arg Arg Ser Cys Leu Arg 100 105 110 Ala Leu Trp His Lys Val Met Phe Pro Val Phe Leu Gly Glu Pro Val 115 120 125 Ser Pro Gln Thr Leu Ala Ala Thr Leu Ala Glu Leu Asp Val Thr Leu 130 135 140 Gln Leu Leu Glu Asp Lys Phe Leu Gln Asn Lys Ala Phe Leu Thr Gly 145 150 155 160 Pro His Ile Ser Leu Ala Asp Leu Val Ala Ile Thr Glu Leu Met His 165 170 175 Pro Val Gly Ala Gly Cys Gln Val Phe Glu Gly Arg Pro Lys Leu Ala 180 185 190 Thr Trp Arg Gln Arg Val Glu Ala Ala Val Gly Glu Asp Leu Phe Gln 195 200 205 Glu Ala His Glu Val Ile Leu Lys Ala Lys Asp Phe Pro Pro Ala Asp 210 215 220 Pro Thr Ile Lys Gln Lys Leu Met Pro Trp Val Leu Ala Met Ile Arg 225 230 235 240 <210> SEQ ID NO 66 <211> LENGTH: 644 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P04264 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(644) <400> SEQUENCE: 66 Met Ser Arg Gln Phe Ser Ser Arg Ser Gly Tyr Arg Ser Gly Gly Gly 1 5 10 15 Phe Ser Ser Gly Ser Ala Gly Ile Ile Asn Tyr Gln Arg Arg Thr Thr 20 25 30 Ser Ser Ser Thr Arg Arg Ser Gly Gly Gly Gly Gly Arg Phe Ser Ser 35 40 45 Cys Gly Gly Gly Gly Gly Ser Phe Gly Ala Gly Gly Gly Phe Gly Ser 50 55 60 Arg Ser Leu Val Asn Leu Gly Gly Ser Lys Ser Ile Ser Ile Ser Val 65 70 75 80 Ala Arg Gly Gly Gly Arg Gly Ser Gly Phe Gly Gly Gly Tyr Gly Gly 85 90 95 Gly Gly Phe Gly Gly Gly Gly Phe Gly Gly Gly Gly Phe Gly Gly Gly 100 105 110 Gly Ile Gly Gly Gly Gly Phe Gly Gly Phe Gly Ser Gly Gly Gly Gly 115 120 125 Phe Gly Gly Gly Gly Phe Gly Gly Gly Gly Tyr Gly Gly Gly Tyr Gly 130 135 140 Pro Val Cys Pro Pro Gly Gly Ile Gln Glu Val Thr Ile Asn Gln Ser 145 150 155 160 Leu Leu Gln Pro Leu Asn Val Glu Ile Asp Pro Glu Ile Gln Lys Val 165 170 175 Lys Ser Arg Glu Arg Glu Gln Ile Lys Ser Leu Asn Asn Gln Phe Ala 180 185 190 Ser Phe Ile Asp Lys Val Arg Phe Leu Glu Gln Gln Asn Gln Val Leu 195 200 205 Gln Thr Lys Trp Glu Leu Leu Gln Gln Val Asp Thr Ser Thr Arg Thr 210 215 220 His Asn Leu Glu Pro Tyr Phe Glu Ser Phe Ile Asn Asn Leu Arg Arg 225 230 235 240 Arg Val Asp Gln Leu Lys Ser Asp Gln Ser Arg Leu Asp Ser Glu Leu 245 250 255 Lys Asn Met Gln Asp Met Val Glu Asp Tyr Arg Asn Lys Tyr Glu Asp 260 265 270 Glu Ile Asn Lys Arg Thr Asn Ala Glu Asn Glu Phe Val Thr Ile Lys 275 280 285 Lys Asp Val Asp Gly Ala Tyr Met Thr Lys Val Asp Leu Gln Ala Lys 290 295 300 Leu Asp Asn Leu Gln Gln Glu Ile Asp Phe Leu Thr Ala Leu Tyr Gln 305 310 315 320 Ala Glu Leu Ser Gln Met Gln Thr Gln Ile Ser Glu Thr Asn Val Ile 325 330 335 Leu Ser Met Asp Asn Asn Arg Ser Leu Asp Leu Asp Ser Ile Ile Ala 340 345 350 Glu Val Lys Ala Gln Tyr Glu Asp Ile Ala Gln Lys Ser Lys Ala Glu 355 360 365 Ala Glu Ser Leu Tyr Gln Ser Lys Tyr Glu Glu Leu Gln Ile Thr Ala 370 375 380 Gly Arg His Gly Asp Ser Val Arg Asn Ser Lys Ile Glu Ile Ser Glu 385 390 395 400 Leu Asn Arg Val Ile Gln Arg Leu Arg Ser Glu Ile Asp Asn Val Lys 405 410 415 Lys Gln Ile Ser Asn Leu Gln Gln Ser Ile Ser Asp Ala Glu Gln Arg 420 425 430 Gly Glu Asn Ala Leu Lys Asp Ala Lys Asn Lys Leu Asn Asp Leu Glu 435 440 445 Asp Ala Leu Gln Gln Ala Lys Glu Asp Leu Ala Arg Leu Leu Arg Asp 450 455 460 Tyr Gln Glu Leu Met Asn Thr Lys Leu Ala Leu Asp Leu Glu Ile Ala 465 470 475 480 Thr Tyr Arg Thr Leu Leu Glu Gly Glu Glu Ser Arg Met Ser Gly Glu 485 490 495 Cys Ala Pro Asn Val Ser Val Ser Val Ser Thr Ser His Thr Thr Ile 500 505 510 Ser Gly Gly Gly Ser Arg Gly Gly Gly Gly Gly Gly Tyr Gly Ser Gly 515 520 525 Gly Ser Ser Tyr Gly Ser Gly Gly Gly Ser Tyr Gly Ser Gly Gly Gly 530 535 540 Gly Gly Gly Gly Arg Gly Ser Tyr Gly Ser Gly Gly Ser Ser Tyr Gly 545 550 555 560 Ser Gly Gly Gly Ser Tyr Gly Ser Gly Gly Gly Gly Gly Gly His Gly 565 570 575 Ser Tyr Gly Ser Gly Ser Ser Ser Gly Gly Tyr Arg Gly Gly Ser Gly 580 585 590 Gly Gly Gly Gly Gly Ser Ser Gly Gly Arg Gly Ser Gly Gly Gly Ser 595 600 605 Ser Gly Gly Ser Ile Gly Gly Arg Gly Ser Ser Ser Gly Gly Val Lys 610 615 620 Ser Ser Gly Gly Ser Ser Ser Val Lys Phe Val Ser Thr Thr Tyr Ser 625 630 635 640 Gly Val Thr Arg <210> SEQ ID NO 67 <211> LENGTH: 1939 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P13533 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1939) <400> SEQUENCE: 67 Met Thr Asp Ala Gln Met Ala Asp Phe Gly Ala Ala Ala Gln Tyr Leu 1 5 10 15 Arg Lys Ser Glu Lys Glu Arg Leu Glu Ala Gln Thr Arg Pro Phe Asp 20 25 30 Ile Arg Thr Glu Cys Phe Val Pro Asp Asp Lys Glu Glu Phe Val Lys 35 40 45 Ala Lys Ile Leu Ser Arg Glu Gly Gly Lys Val Ile Ala Glu Thr Glu 50 55 60 Asn Gly Lys Thr Val Thr Val Lys Glu Asp Gln Val Leu Gln Gln Asn 65 70 75 80 Pro Pro Lys Phe Asp Lys Ile Glu Asp Met Ala Met Leu Thr Phe Leu 85 90 95 His Glu Pro Ala Val Leu Phe Asn Leu Lys Glu Arg Tyr Ala Ala Trp 100 105 110 Met Ile Tyr Thr Tyr Ser Gly Leu Phe Cys Val Thr Val Asn Pro Tyr 115 120 125 Lys Trp Leu Pro Val Tyr Asn Ala Glu Val Val Ala Ala Tyr Arg Gly 130 135 140 Lys Lys Arg Ser Glu Ala Pro Pro His Ile Phe Ser Ile Ser Asp Asn 145 150 155 160 Ala Tyr Gln Tyr Met Leu Thr Asp Arg Glu Asn Gln Ser Ile Leu Ile 165 170 175 Thr Gly Glu Ser Gly Ala Gly Lys Thr Val Asn Thr Lys Arg Val Ile 180 185 190 Gln Tyr Phe Ala Ser Ile Ala Ala Ile Gly Asp Arg Gly Lys Lys Asp 195 200 205 Asn Ala Asn Ala Asn Lys Gly Thr Leu Glu Asp Gln Ile Ile Gln Ala 210 215 220 Asn Pro Ala Leu Glu Ala Phe Gly Asn Ala Lys Thr Val Arg Asn Asp 225 230 235 240 Asn Ser Ser Arg Phe Gly Lys Phe Ile Arg Ile His Phe Gly Ala Thr 245 250 255 Gly Lys Leu Ala Ser Ala Asp Ile Glu Thr Tyr Leu Leu Glu Lys Ser 260 265 270 Arg Val Ile Phe Gln Leu Lys Ala Glu Arg Asn Tyr His Ile Phe Tyr 275 280 285 Gln Ile Leu Ser Asn Lys Lys Pro Glu Leu Leu Asp Met Leu Leu Val 290 295 300 Thr Asn Asn Pro Tyr Asp Tyr Ala Phe Val Ser Gln Gly Glu Val Ser 305 310 315 320 Val Ala Ser Ile Asp Asp Ser Glu Glu Leu Met Ala Thr Asp Ser Ala 325 330 335 Phe Asp Val Leu Gly Phe Thr Ser Glu Glu Lys Ala Gly Val Tyr Lys 340 345 350 Leu Thr Gly Ala Ile Met His Tyr Gly Asn Met Lys Phe Lys Gln Lys 355 360 365 Gln Arg Glu Glu Gln Ala Glu Pro Asp Gly Thr Glu Asp Ala Asp Lys 370 375 380 Ser Ala Tyr Leu Met Gly Leu Asn Ser Ala Asp Leu Leu Lys Gly Leu 385 390 395 400 Cys His Pro Arg Val Lys Val Gly Asn Glu Tyr Val Thr Lys Gly Gln 405 410 415 Ser Val Gln Gln Val Tyr Tyr Ser Ile Gly Ala Leu Ala Lys Ala Val 420 425 430 Tyr Glu Lys Met Phe Asn Trp Met Val Thr Arg Ile Asn Ala Thr Leu 435 440 445 Glu Thr Lys Gln Pro Arg Gln Tyr Phe Ile Gly Val Leu Asp Ile Ala 450 455 460 Gly Phe Glu Ile Phe Asp Phe Asn Ser Phe Glu Gln Leu Cys Ile Asn 465 470 475 480 Phe Thr Asn Glu Lys Leu Gln Gln Phe Phe Asn His His Met Phe Val 485 490 495 Leu Glu Gln Glu Glu Tyr Lys Lys Glu Gly Ile Glu Trp Thr Phe Ile 500 505 510 Asp Phe Gly Met Asp Leu Gln Ala Cys Ile Asp Leu Ile Glu Lys Pro 515 520 525 Met Gly Ile Met Ser Ile Leu Glu Glu Glu Cys Met Phe Pro Lys Ala 530 535 540 Thr Asp Met Thr Phe Lys Ala Lys Leu Tyr Asp Asn His Leu Gly Lys 545 550 555 560 Ser Asn Asn Phe Gln Lys Pro Arg Asn Ile Lys Gly Lys Gln Glu Ala 565 570 575 His Phe Ser Leu Ile His Tyr Ala Gly Thr Val Asp Tyr Asn Ile Leu 580 585 590 Gly Trp Leu Glu Lys Asn Lys Asp Pro Leu Asn Glu Thr Val Val Ala 595 600 605 Leu Tyr Gln Lys Ser Ser Leu Lys Leu Met Ala Thr Leu Phe Ser Ser 610 615 620 Tyr Ala Thr Ala Asp Thr Gly Asp Ser Gly Lys Ser Lys Gly Gly Lys 625 630 635 640 Lys Lys Gly Ser Ser Phe Gln Thr Val Ser Ala Leu His Arg Glu Asn 645 650 655 Leu Asn Lys Leu Met Thr Asn Leu Arg Thr Thr His Pro His Phe Val 660 665 670 Arg Cys Ile Ile Pro Asn Glu Arg Lys Ala Pro Gly Val Met Asp Asn 675 680 685 Pro Leu Val Met His Gln Leu Arg Cys Asn Gly Val Leu Glu Gly Ile 690 695 700 Arg Ile Cys Arg Lys Gly Phe Pro Asn Arg Ile Leu Tyr Gly Asp Phe 705 710 715 720 Arg Gln Arg Tyr Arg Ile Leu Asn Pro Val Ala Ile Pro Glu Gly Gln 725 730 735 Phe Ile Asp Ser Arg Lys Gly Thr Glu Lys Leu Leu Ser Ser Leu Asp 740 745 750 Ile Asp His Asn Gln Tyr Lys Phe Gly His Thr Lys Val Phe Phe Lys 755 760 765 Ala Gly Leu Leu Gly Leu Leu Glu Glu Met Arg Asp Glu Arg Leu Ser 770 775 780 Arg Ile Ile Thr Arg Met Gln Ala Gln Ala Arg Gly Gln Leu Met Arg 785 790 795 800 Ile Glu Phe Lys Lys Ile Val Glu Arg Arg Asp Ala Leu Leu Val Ile 805 810 815 Gln Trp Asn Ile Arg Ala Phe Met Gly Val Lys Asn Trp Pro Trp Met 820 825 830 Lys Leu Tyr Phe Lys Ile Lys Pro Leu Leu Lys Ser Ala Glu Thr Glu 835 840 845 Lys Glu Met Ala Thr Met Lys Glu Glu Phe Gly Arg Ile Lys Glu Thr 850 855 860 Leu Glu Lys Ser Glu Ala Arg Arg Lys Glu Leu Glu Glu Lys Met Val 865 870 875 880 Ser Leu Leu Gln Glu Lys Asn Asp Leu Gln Leu Gln Val Gln Ala Glu 885 890 895 Gln Asp Asn Leu Asn Asp Ala Glu Glu Arg Cys Asp Gln Leu Ile Lys 900 905 910 Asn Lys Ile Gln Leu Glu Ala Lys Val Lys Glu Met Asn Glu Arg Leu 915 920 925 Glu Asp Glu Glu Glu Met Asn Ala Glu Leu Thr Ala Lys Lys Arg Lys 930 935 940 Leu Glu Asp Glu Cys Ser Glu Leu Lys Lys Asp Ile Asp Asp Leu Glu 945 950 955 960 Leu Thr Leu Ala Lys Val Glu Lys Glu Lys His Ala Thr Glu Asn Lys 965 970 975 Val Lys Asn Leu Thr Glu Glu Met Ala Gly Leu Asp Glu Ile Ile Ala 980 985 990 Lys Leu Thr Lys Glu Lys Lys Ala Leu Gln Glu Ala His Gln Gln Ala 995 1000 1005 Leu Asp Asp Leu Gln Val Glu Glu Asp Lys Val Asn Ser Leu Ser 1010 1015 1020 Lys Ser Lys Val Lys Leu Glu Gln Gln Val Asp Asp Leu Glu Gly 1025 1030 1035 Ser Leu Glu Gln Glu Lys Lys Val Arg Met Asp Leu Glu Arg Ala 1040 1045 1050 Lys Arg Lys Leu Glu Gly Asp Leu Lys Leu Thr Gln Glu Ser Ile 1055 1060 1065 Met Asp Leu Glu Asn Asp Lys Leu Gln Leu Glu Glu Lys Leu Lys 1070 1075 1080 Lys Lys Glu Phe Asp Ile Asn Gln Gln Asn Ser Lys Ile Glu Asp 1085 1090 1095 Glu Gln Val Leu Ala Leu Gln Leu Gln Lys Lys Leu Lys Glu Asn 1100 1105 1110 Gln Ala Arg Ile Glu Glu Leu Glu Glu Glu Leu Glu Ala Glu Arg 1115 1120 1125 Thr Ala Arg Ala Lys Val Glu Lys Leu Arg Ser Asp Leu Ser Arg 1130 1135 1140 Glu Leu Glu Glu Ile Ser Glu Arg Leu Glu Glu Ala Gly Gly Ala 1145 1150 1155 Thr Ser Val Gln Ile Glu Met Asn Lys Lys Arg Glu Ala Glu Phe 1160 1165 1170 Gln Lys Met Arg Arg Asp Leu Glu Glu Ala Thr Leu Gln His Glu 1175 1180 1185 Ala Thr Ala Ala Ala Leu Arg Lys Lys His Ala Asp Ser Val Ala 1190 1195 1200 Glu Leu Gly Glu Gln Ile Asp Asn Leu Gln Arg Val Lys Gln Lys 1205 1210 1215 Leu Glu Lys Glu Lys Ser Glu Phe Lys Leu Glu Leu Asp Asp Val 1220 1225 1230 Thr Ser Asn Met Glu Gln Ile Ile Lys Ala Lys Ala Asn Leu Glu 1235 1240 1245 Lys Val Ser Arg Thr Leu Glu Asp Gln Ala Asn Glu Tyr Arg Val 1250 1255 1260 Lys Leu Glu Glu Ala Gln Arg Ser Leu Asn Asp Phe Thr Thr Gln 1265 1270 1275 Arg Ala Lys Leu Gln Thr Glu Asn Gly Glu Leu Ala Arg Gln Leu 1280 1285 1290 Glu Glu Lys Glu Ala Leu Ile Ser Gln Leu Thr Arg Gly Lys Leu 1295 1300 1305 Ser Tyr Thr Gln Gln Met Glu Asp Leu Lys Arg Gln Leu Glu Glu 1310 1315 1320 Glu Gly Lys Ala Lys Asn Ala Leu Ala His Ala Leu Gln Ser Ala 1325 1330 1335 Arg His Asp Cys Asp Leu Leu Arg Glu Gln Tyr Glu Glu Glu Thr 1340 1345 1350 Glu Ala Lys Ala Glu Leu Gln Arg Val Leu Ser Lys Ala Asn Ser 1355 1360 1365 Glu Val Ala Gln Trp Arg Thr Lys Tyr Glu Thr Asp Ala Ile Gln 1370 1375 1380 Arg Thr Glu Glu Leu Glu Glu Ala Lys Lys Lys Leu Ala Gln Arg 1385 1390 1395 Leu Gln Asp Ala Glu Glu Ala Val Glu Ala Val Asn Ala Lys Cys 1400 1405 1410 Ser Ser Leu Glu Lys Thr Lys His Arg Leu Gln Asn Glu Ile Glu 1415 1420 1425 Asp Leu Met Val Asp Val Glu Arg Ser Asn Ala Ala Ala Ala Ala 1430 1435 1440 Leu Asp Lys Lys Gln Arg Asn Phe Asp Lys Ile Leu Ala Glu Trp 1445 1450 1455 Lys Gln Lys Tyr Glu Glu Ser Gln Ser Glu Leu Glu Ser Ser Gln 1460 1465 1470 Lys Glu Ala Arg Ser Leu Ser Thr Glu Leu Phe Lys Leu Lys Asn 1475 1480 1485 Ala Tyr Glu Glu Ser Leu Glu His Leu Glu Thr Phe Lys Arg Glu 1490 1495 1500 Asn Lys Asn Leu Gln Glu Glu Ile Ser Asp Leu Thr Glu Gln Leu 1505 1510 1515 Gly Glu Gly Gly Lys Asn Val His Glu Leu Glu Lys Val Arg Lys 1520 1525 1530 Gln Leu Glu Val Glu Lys Leu Glu Leu Gln Ser Ala Leu Glu Glu 1535 1540 1545 Ala Glu Ala Ser Leu Glu His Glu Glu Gly Lys Ile Leu Arg Ala 1550 1555 1560 Gln Leu Glu Phe Asn Gln Ile Lys Ala Glu Ile Glu Arg Lys Leu 1565 1570 1575 Ala Glu Lys Asp Glu Glu Met Glu Gln Ala Lys Arg Asn His Gln 1580 1585 1590 Arg Val Val Asp Ser Leu Gln Thr Ser Leu Asp Ala Glu Thr Arg 1595 1600 1605 Ser Arg Asn Glu Val Leu Arg Val Lys Lys Lys Met Glu Gly Asp 1610 1615 1620 Leu Asn Glu Met Glu Ile Gln Leu Ser His Ala Asn Arg Met Ala 1625 1630 1635 Ala Glu Ala Gln Lys Gln Val Lys Ser Leu Gln Ser Leu Leu Lys 1640 1645 1650 Asp Thr Gln Ile Gln Leu Asp Asp Ala Val Arg Ala Asn Asp Asp 1655 1660 1665 Leu Lys Glu Asn Ile Ala Ile Val Glu Arg Arg Asn Asn Leu Leu 1670 1675 1680 Gln Ala Glu Leu Glu Glu Leu Arg Ala Val Val Glu Gln Thr Glu 1685 1690 1695 Arg Ser Arg Lys Leu Ala Glu Gln Glu Leu Ile Glu Thr Ser Glu 1700 1705 1710 Arg Val Gln Leu Leu His Ser Gln Asn Thr Ser Leu Ile Asn Gln 1715 1720 1725 Lys Lys Lys Met Glu Ser Asp Leu Thr Gln Leu Gln Ser Glu Val 1730 1735 1740 Glu Glu Ala Val Gln Glu Cys Arg Asn Ala Glu Glu Lys Ala Lys 1745 1750 1755 Lys Ala Ile Thr Asp Ala Ala Met Met Ala Glu Glu Leu Lys Lys 1760 1765 1770 Glu Gln Asp Thr Ser Ala His Leu Glu Arg Met Lys Lys Asn Met 1775 1780 1785 Glu Gln Thr Ile Lys Asp Leu Gln His Arg Leu Asp Glu Ala Glu 1790 1795 1800 Gln Ile Ala Leu Lys Gly Gly Lys Lys Gln Leu Gln Lys Leu Glu 1805 1810 1815 Ala Arg Val Arg Glu Leu Glu Gly Glu Leu Glu Ala Glu Gln Lys 1820 1825 1830 Arg Asn Ala Glu Ser Val Lys Gly Met Arg Lys Ser Glu Arg Arg 1835 1840 1845 Ile Lys Glu Leu Thr Tyr Gln Thr Glu Glu Asp Lys Lys Asn Leu 1850 1855 1860 Leu Arg Leu Gln Asp Leu Val Asp Lys Leu Gln Leu Lys Val Lys 1865 1870 1875 Ala Tyr Lys Arg Gln Ala Glu Glu Ala Glu Glu Gln Ala Asn Thr 1880 1885 1890 Asn Leu Ser Lys Phe Arg Lys Val Gln His Glu Leu Asp Glu Ala 1895 1900 1905 Glu Glu Arg Ala Asp Ile Ala Glu Ser Gln Val Asn Lys Leu Arg 1910 1915 1920 Ala Lys Ser Arg Asp Ile Gly Ala Lys Gln Lys Met His Asp Glu 1925 1930 1935 Glu <210> SEQ ID NO 68 <211> LENGTH: 1935 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P12883 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1935) <400> SEQUENCE: 68 Met Gly Asp Ser Glu Met Ala Val Phe Gly Ala Ala Ala Pro Tyr Leu 1 5 10 15 Arg Lys Ser Glu Lys Glu Arg Leu Glu Ala Gln Thr Arg Pro Phe Asp 20 25 30 Leu Lys Lys Asp Val Phe Val Pro Asp Asp Lys Gln Glu Phe Val Lys 35 40 45 Ala Lys Ile Val Ser Arg Glu Gly Gly Lys Val Thr Ala Glu Thr Glu 50 55 60 Tyr Gly Lys Thr Val Thr Val Lys Glu Asp Gln Val Met Gln Gln Asn 65 70 75 80 Pro Pro Lys Phe Asp Lys Ile Glu Asp Met Ala Met Leu Thr Phe Leu 85 90 95 His Glu Pro Ala Val Leu Tyr Asn Leu Lys Asp Arg Tyr Gly Ser Trp 100 105 110 Met Ile Tyr Thr Tyr Ser Gly Leu Phe Cys Val Thr Val Asn Pro Tyr 115 120 125 Lys Trp Leu Pro Val Tyr Thr Pro Glu Val Val Ala Ala Tyr Arg Gly 130 135 140 Lys Lys Arg Ser Glu Ala Pro Pro His Ile Phe Ser Ile Ser Asp Asn 145 150 155 160 Ala Tyr Gln Tyr Met Leu Thr Asp Arg Glu Asn Gln Ser Ile Leu Ile 165 170 175 Thr Gly Glu Ser Gly Ala Gly Lys Thr Val Asn Thr Lys Arg Val Ile 180 185 190 Gln Tyr Phe Ala Val Ile Ala Ala Ile Gly Asp Arg Ser Lys Lys Asp 195 200 205 Gln Ser Pro Gly Lys Gly Thr Leu Glu Asp Gln Ile Ile Gln Ala Asn 210 215 220 Pro Ala Leu Glu Ala Phe Gly Asn Ala Lys Thr Val Arg Asn Asp Asn 225 230 235 240 Ser Ser Arg Phe Gly Lys Phe Ile Arg Ile His Phe Gly Ala Thr Gly 245 250 255 Lys Leu Ala Ser Ala Asp Ile Glu Thr Tyr Leu Leu Glu Lys Ser Arg 260 265 270 Val Ile Phe Gln Leu Lys Ala Glu Arg Asp Tyr His Ile Phe Tyr Gln 275 280 285 Ile Leu Ser Asn Lys Lys Pro Glu Leu Leu Asp Met Leu Leu Ile Thr 290 295 300 Asn Asn Pro Tyr Asp Tyr Ala Phe Ile Ser Gln Gly Glu Thr Thr Val 305 310 315 320 Ala Ser Ile Asp Asp Ala Glu Glu Leu Met Ala Thr Asp Asn Ala Phe 325 330 335 Asp Val Leu Gly Phe Thr Ser Glu Glu Lys Asn Ser Met Tyr Lys Leu 340 345 350 Thr Gly Ala Ile Met His Phe Gly Asn Met Lys Phe Lys Leu Lys Gln 355 360 365 Arg Glu Glu Gln Ala Glu Pro Asp Gly Thr Glu Glu Ala Asp Lys Ser 370 375 380 Ala Tyr Leu Met Gly Leu Asn Ser Ala Asp Leu Leu Lys Gly Leu Cys 385 390 395 400 His Pro Arg Val Lys Val Gly Asn Glu Tyr Val Thr Lys Gly Gln Asn 405 410 415 Val Gln Gln Val Ile Tyr Ala Thr Gly Ala Leu Ala Lys Ala Val Tyr 420 425 430 Glu Arg Met Phe Asn Trp Met Val Thr Arg Ile Asn Ala Thr Leu Glu 435 440 445 Thr Lys Gln Pro Arg Gln Tyr Phe Ile Gly Val Leu Asp Ile Ala Gly 450 455 460 Phe Glu Ile Phe Asp Phe Asn Ser Phe Glu Gln Leu Cys Ile Asn Phe 465 470 475 480 Thr Asn Glu Lys Leu Gln Gln Phe Phe Asn His His Met Phe Val Leu 485 490 495 Glu Gln Glu Glu Tyr Lys Lys Glu Gly Ile Glu Trp Thr Phe Ile Asp 500 505 510 Phe Gly Met Asp Leu Gln Ala Cys Ile Asp Leu Ile Glu Lys Pro Met 515 520 525 Gly Ile Met Ser Ile Leu Glu Glu Glu Cys Met Phe Pro Lys Ala Thr 530 535 540 Asp Met Thr Phe Lys Ala Lys Leu Phe Asp Asn His Leu Gly Lys Ser 545 550 555 560 Ala Asn Phe Gln Lys Pro Arg Asn Ile Lys Gly Lys Pro Glu Ala His 565 570 575 Phe Ser Leu Ile His Tyr Ala Gly Ile Val Asp Tyr Asn Ile Ile Gly 580 585 590 Trp Leu Gln Lys Asn Lys Asp Pro Leu Asn Glu Thr Val Val Gly Leu 595 600 605 Tyr Gln Lys Ser Ser Leu Lys Leu Leu Ser Thr Leu Phe Ala Asn Tyr 610 615 620 Ala Gly Ala Asp Ala Pro Ile Glu Lys Gly Lys Gly Lys Ala Lys Lys 625 630 635 640 Gly Ser Ser Phe Gln Thr Val Ser Ala Leu His Arg Glu Asn Leu Asn 645 650 655 Lys Leu Met Thr Asn Leu Arg Ser Thr His Pro His Phe Val Arg Cys 660 665 670 Ile Ile Pro Asn Glu Thr Lys Ser Pro Gly Val Met Asp Asn Pro Leu 675 680 685 Val Met His Gln Leu Arg Cys Asn Gly Val Leu Glu Gly Ile Arg Ile 690 695 700 Cys Arg Lys Gly Phe Pro Asn Arg Ile Leu Tyr Gly Asp Phe Arg Gln 705 710 715 720 Arg Tyr Arg Ile Leu Asn Pro Ala Ala Ile Pro Glu Gly Gln Phe Ile 725 730 735 Asp Ser Arg Lys Gly Ala Glu Lys Leu Leu Ser Ser Leu Asp Ile Asp 740 745 750 His Asn Gln Tyr Lys Phe Gly His Thr Lys Val Phe Phe Lys Ala Gly 755 760 765 Leu Leu Gly Leu Leu Glu Glu Met Arg Asp Glu Arg Leu Ser Arg Ile 770 775 780 Ile Thr Arg Ile Gln Ala Gln Ser Arg Gly Val Leu Ala Arg Met Glu 785 790 795 800 Tyr Lys Lys Leu Leu Glu Arg Arg Asp Ser Leu Leu Val Ile Gln Trp 805 810 815 Asn Ile Arg Ala Phe Met Gly Val Lys Asn Trp Pro Trp Met Lys Leu 820 825 830 Tyr Phe Lys Ile Lys Pro Leu Leu Lys Ser Ala Glu Arg Glu Lys Glu 835 840 845 Met Ala Ser Met Lys Glu Glu Phe Thr Arg Leu Lys Glu Ala Leu Glu 850 855 860 Lys Ser Glu Ala Arg Arg Lys Glu Leu Glu Glu Lys Met Val Ser Leu 865 870 875 880 Leu Gln Glu Lys Asn Asp Leu Gln Leu Gln Val Gln Ala Glu Gln Asp 885 890 895 Asn Leu Ala Asp Ala Glu Glu Arg Cys Asp Gln Leu Ile Lys Asn Lys 900 905 910 Ile Gln Leu Glu Ala Lys Val Lys Glu Met Asn Glu Arg Leu Glu Asp 915 920 925 Glu Glu Glu Met Asn Ala Glu Leu Thr Ala Lys Lys Arg Lys Leu Glu 930 935 940 Asp Glu Cys Ser Glu Leu Lys Arg Asp Ile Asp Asp Leu Glu Leu Thr 945 950 955 960 Leu Ala Lys Val Glu Lys Glu Lys His Ala Thr Glu Asn Lys Val Lys 965 970 975 Asn Leu Thr Glu Glu Met Ala Gly Leu Asp Glu Ile Ile Ala Lys Leu 980 985 990 Thr Lys Glu Lys Lys Ala Leu Gln Glu Ala His Gln Gln Ala Leu Asp 995 1000 1005 Asp Leu Gln Ala Glu Glu Asp Lys Val Asn Thr Leu Thr Lys Ala 1010 1015 1020 Lys Val Lys Leu Glu Gln Gln Val Asp Asp Leu Glu Gly Ser Leu 1025 1030 1035 Glu Gln Glu Lys Lys Val Arg Met Asp Leu Glu Arg Ala Lys Arg 1040 1045 1050 Lys Leu Glu Gly Asp Leu Lys Leu Thr Gln Glu Ser Ile Met Asp 1055 1060 1065 Leu Glu Asn Asp Lys Gln Gln Leu Asp Glu Arg Leu Lys Lys Lys 1070 1075 1080 Asp Phe Glu Leu Asn Ala Leu Asn Ala Arg Ile Glu Asp Glu Gln 1085 1090 1095 Ala Leu Gly Ser Gln Leu Gln Lys Lys Leu Lys Glu Leu Gln Ala 1100 1105 1110 Arg Ile Glu Glu Leu Glu Glu Glu Leu Glu Ala Glu Arg Thr Ala 1115 1120 1125 Arg Ala Lys Val Glu Lys Leu Arg Ser Asp Leu Ser Arg Glu Leu 1130 1135 1140 Glu Glu Ile Ser Glu Arg Leu Glu Glu Ala Gly Gly Ala Thr Ser 1145 1150 1155 Val Gln Ile Glu Met Asn Lys Lys Arg Glu Ala Glu Phe Gln Lys 1160 1165 1170 Met Arg Arg Asp Leu Glu Glu Ala Thr Leu Gln His Glu Ala Thr 1175 1180 1185 Ala Ala Ala Leu Arg Lys Lys His Ala Asp Ser Val Ala Glu Leu 1190 1195 1200 Gly Glu Gln Ile Asp Asn Leu Gln Arg Val Lys Gln Lys Leu Glu 1205 1210 1215 Lys Glu Lys Ser Glu Phe Lys Leu Glu Leu Asp Asp Val Thr Ser 1220 1225 1230 Asn Met Glu Gln Ile Ile Lys Ala Lys Ala Asn Leu Glu Lys Met 1235 1240 1245 Cys Arg Thr Leu Glu Asp Gln Met Asn Glu His Arg Ser Lys Ala 1250 1255 1260 Glu Glu Thr Gln Arg Ser Val Asn Asp Leu Thr Ser Gln Arg Ala 1265 1270 1275 Lys Leu Gln Thr Glu Asn Gly Glu Leu Ser Arg Gln Leu Asp Glu 1280 1285 1290 Lys Glu Ala Leu Ile Ser Gln Leu Thr Arg Gly Lys Leu Thr Tyr 1295 1300 1305 Thr Gln Gln Leu Glu Asp Leu Lys Arg Gln Leu Glu Glu Glu Val 1310 1315 1320 Lys Ala Lys Asn Ala Leu Ala His Ala Leu Gln Ser Ala Arg His 1325 1330 1335 Asp Cys Asp Leu Leu Arg Glu Gln Tyr Glu Glu Glu Thr Glu Ala 1340 1345 1350 Lys Ala Glu Leu Gln Arg Val Leu Ser Lys Ala Asn Ser Glu Val 1355 1360 1365 Ala Gln Trp Arg Thr Lys Tyr Glu Thr Asp Ala Ile Gln Arg Thr 1370 1375 1380 Glu Glu Leu Glu Glu Ala Lys Lys Lys Leu Ala Gln Arg Leu Gln 1385 1390 1395 Glu Ala Glu Glu Ala Val Glu Ala Val Asn Ala Lys Cys Ser Ser 1400 1405 1410 Leu Glu Lys Thr Lys His Arg Leu Gln Asn Glu Ile Glu Asp Leu 1415 1420 1425 Met Val Asp Val Glu Arg Ser Asn Ala Ala Ala Ala Ala Leu Asp 1430 1435 1440 Lys Lys Gln Arg Asn Phe Asp Lys Ile Leu Ala Glu Trp Lys Gln 1445 1450 1455 Lys Tyr Glu Glu Ser Gln Ser Glu Leu Glu Ser Ser Gln Lys Glu 1460 1465 1470 Ala Arg Ser Leu Ser Thr Glu Leu Phe Lys Leu Lys Asn Ala Tyr 1475 1480 1485 Glu Glu Ser Leu Glu His Leu Glu Thr Phe Lys Arg Glu Asn Lys 1490 1495 1500 Asn Leu Gln Glu Glu Ile Ser Asp Leu Thr Glu Gln Leu Gly Ser 1505 1510 1515 Ser Gly Lys Thr Ile His Glu Leu Glu Lys Val Arg Lys Gln Leu 1520 1525 1530 Glu Ala Glu Lys Met Glu Leu Gln Ser Ala Leu Glu Glu Ala Glu 1535 1540 1545 Ala Ser Leu Glu His Glu Glu Gly Lys Ile Leu Arg Ala Gln Leu 1550 1555 1560 Glu Phe Asn Gln Ile Lys Ala Glu Ile Glu Arg Lys Leu Ala Glu 1565 1570 1575 Lys Asp Glu Glu Met Glu Gln Ala Lys Arg Asn His Leu Arg Val 1580 1585 1590 Val Asp Ser Leu Gln Thr Ser Leu Asp Ala Glu Thr Arg Ser Arg 1595 1600 1605 Asn Glu Ala Leu Arg Val Lys Lys Lys Met Glu Gly Asp Leu Asn 1610 1615 1620 Glu Met Glu Ile Gln Leu Ser His Ala Asn Arg Met Ala Ala Glu 1625 1630 1635 Ala Gln Lys Gln Val Lys Ser Leu Gln Ser Leu Leu Lys Asp Thr 1640 1645 1650 Gln Ile Gln Leu Asp Asp Ala Val Arg Ala Asn Asp Asp Leu Lys 1655 1660 1665 Glu Asn Ile Ala Ile Val Glu Arg Arg Asn Asn Leu Leu Gln Ala 1670 1675 1680 Glu Leu Glu Glu Leu Arg Ala Val Val Glu Gln Thr Glu Arg Ser 1685 1690 1695 Arg Lys Leu Ala Glu Gln Glu Leu Ile Glu Thr Ser Glu Arg Val 1700 1705 1710 Gln Leu Leu His Ser Gln Asn Thr Ser Leu Ile Asn Gln Lys Lys 1715 1720 1725 Lys Met Asp Ala Asp Leu Ser Gln Leu Gln Thr Glu Val Glu Glu 1730 1735 1740 Ala Val Gln Glu Cys Arg Asn Ala Glu Glu Lys Ala Lys Lys Ala 1745 1750 1755 Ile Thr Asp Ala Ala Met Met Ala Glu Glu Leu Lys Lys Glu Gln 1760 1765 1770 Asp Thr Ser Ala His Leu Glu Arg Met Lys Lys Asn Met Glu Gln 1775 1780 1785 Thr Ile Lys Asp Leu Gln His Arg Leu Asp Glu Ala Glu Gln Ile 1790 1795 1800 Ala Leu Lys Gly Gly Lys Lys Gln Leu Gln Lys Leu Glu Ala Arg 1805 1810 1815 Val Arg Glu Leu Glu Asn Glu Leu Glu Ala Glu Gln Lys Arg Asn 1820 1825 1830 Ala Glu Ser Val Lys Gly Met Arg Lys Ser Glu Arg Arg Ile Lys 1835 1840 1845 Glu Leu Thr Tyr Gln Thr Glu Glu Asp Arg Lys Asn Leu Leu Arg 1850 1855 1860 Leu Gln Asp Leu Val Asp Lys Leu Gln Leu Lys Val Lys Ala Tyr 1865 1870 1875 Lys Arg Gln Ala Glu Glu Ala Glu Glu Gln Ala Asn Thr Asn Leu 1880 1885 1890 Ser Lys Phe Arg Lys Val Gln His Glu Leu Asp Glu Ala Glu Glu 1895 1900 1905 Arg Ala Asp Ile Ala Glu Ser Gln Val Asn Lys Leu Arg Ala Lys 1910 1915 1920 Ser Arg Asp Ile Gly Thr Lys Gly Leu Asn Glu Glu 1925 1930 1935 <210> SEQ ID NO 69 <211> LENGTH: 197 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P12829 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(197) <400> SEQUENCE: 69 Met Ala Pro Lys Lys Pro Glu Pro Lys Lys Glu Ala Ala Lys Pro Ala 1 5 10 15 Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Glu 20 25 30 Ala Pro Lys Glu Pro Ala Phe Asp Pro Lys Ser Val Lys Ile Asp Phe 35 40 45 Thr Ala Asp Gln Ile Glu Glu Phe Lys Glu Ala Phe Ser Leu Phe Asp 50 55 60 Arg Thr Pro Thr Gly Glu Met Lys Ile Thr Tyr Gly Gln Cys Gly Asp 65 70 75 80 Val Leu Arg Ala Leu Gly Gln Asn Pro Thr Asn Ala Glu Val Leu Arg 85 90 95 Val Leu Gly Lys Pro Lys Pro Glu Glu Met Asn Val Lys Met Leu Asp 100 105 110 Phe Glu Thr Phe Leu Pro Ile Leu Gln His Ile Ser Arg Asn Lys Glu 115 120 125 Gln Gly Thr Tyr Glu Asp Phe Val Glu Gly Leu Arg Val Phe Asp Lys 130 135 140 Glu Ser Asn Gly Thr Val Met Gly Ala Glu Leu Arg His Val Leu Ala 145 150 155 160 Thr Leu Gly Glu Lys Met Thr Glu Ala Glu Val Glu Gln Leu Leu Ala 165 170 175 Gly Gln Glu Asp Ala Asn Gly Cys Ile Asn Tyr Glu Ala Phe Val Lys 180 185 190 His Ile Met Ser Gly 195 <210> SEQ ID NO 70 <211> LENGTH: 810 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q06730 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(810) <400> SEQUENCE: 70 Met Asn Lys Val Glu Gln Lys Ser Gln Glu Ser Val Ser Phe Lys Asp 1 5 10 15 Val Thr Val Gly Phe Thr Gln Glu Glu Trp Gln His Leu Asp Pro Ser 20 25 30 Gln Arg Ala Leu Tyr Arg Asp Val Met Leu Glu Asn Tyr Ser Asn Leu 35 40 45 Val Ser Val Gly Tyr Cys Val His Lys Pro Glu Val Ile Phe Arg Leu 50 55 60 Gln Gln Gly Glu Glu Pro Trp Lys Gln Glu Glu Glu Phe Pro Ser Gln 65 70 75 80 Ser Phe Pro Val Trp Thr Ala Asp His Leu Lys Glu Arg Ser Gln Glu 85 90 95 Asn Gln Ser Lys His Leu Trp Glu Val Val Phe Ile Asn Asn Glu Met 100 105 110 Leu Thr Lys Glu Gln Gly Asp Val Ile Gly Ile Pro Phe Asn Val Asp 115 120 125 Val Ser Ser Phe Pro Ser Arg Lys Met Phe Cys Gln Cys Asp Ser Cys 130 135 140 Gly Met Ser Phe Asn Thr Val Ser Glu Leu Val Ile Ser Lys Ile Asn 145 150 155 160 Tyr Leu Gly Lys Lys Ser Asp Glu Phe Asn Ala Cys Gly Lys Leu Leu 165 170 175 Leu Asn Ile Lys His Asp Glu Thr His Thr Gln Glu Lys Asn Glu Val 180 185 190 Leu Lys Asn Arg Asn Thr Leu Ser His His Glu Glu Thr Leu Gln His 195 200 205 Glu Lys Ile Gln Thr Leu Glu His Asn Phe Glu Tyr Ser Ile Cys Gln 210 215 220 Glu Thr Leu Leu Glu Lys Ala Val Phe Asn Thr Gln Lys Arg Glu Asn 225 230 235 240 Ala Glu Glu Asn Asn Cys Asp Tyr Asn Glu Phe Gly Arg Thr Leu Cys 245 250 255 Asp Ser Ser Ser Leu Leu Phe His Gln Ile Ser Pro Ser Arg Asp Asn 260 265 270 His Tyr Glu Phe Ser Asp Cys Glu Lys Phe Leu Cys Val Lys Ser Thr 275 280 285 Leu Ser Lys Pro His Gly Val Ser Met Lys His Tyr Asp Cys Gly Glu 290 295 300 Ser Gly Asn Asn Phe Arg Arg Lys Leu Cys Leu Ser His Leu Gln Lys 305 310 315 320 Gly Asp Lys Gly Glu Lys His Phe Glu Cys Asn Glu Cys Gly Lys Ala 325 330 335 Phe Trp Glu Lys Ser His Leu Thr Arg His Gln Arg Val His Thr Gly 340 345 350 Gln Lys Pro Phe Gln Cys Asn Glu Cys Glu Lys Ala Phe Trp Asp Lys 355 360 365 Ser Asn Leu Thr Lys His Gln Arg Ser His Thr Gly Glu Lys Pro Phe 370 375 380 Glu Cys Asn Glu Cys Gly Lys Ala Phe Ser His Lys Ser Ala Leu Thr 385 390 395 400 Leu His Gln Arg Thr His Thr Gly Glu Lys Pro Tyr Gln Cys Asn Ala 405 410 415 Cys Gly Lys Thr Phe Cys Gln Lys Ser Asp Leu Thr Lys His Gln Arg 420 425 430 Thr His Thr Gly Leu Lys Pro Tyr Glu Cys Tyr Glu Cys Gly Lys Ser 435 440 445 Phe Arg Val Thr Ser His Leu Lys Val His Gln Arg Thr His Thr Gly 450 455 460 Glu Lys Pro Phe Glu Cys Leu Glu Cys Gly Lys Ser Phe Ser Glu Lys 465 470 475 480 Ser Asn Leu Thr Gln His Gln Arg Ile His Ile Gly Asp Lys Ser Tyr 485 490 495 Glu Cys Asn Ala Cys Gly Lys Thr Phe Tyr His Lys Ser Leu Leu Thr 500 505 510 Arg His Gln Ile Ile His Thr Gly Trp Lys Pro Tyr Glu Cys Tyr Glu 515 520 525 Cys Gly Lys Thr Phe Cys Leu Lys Ser Asp Leu Thr Val His Gln Arg 530 535 540 Thr His Thr Gly Gln Lys Pro Phe Ala Cys Pro Glu Cys Gly Lys Phe 545 550 555 560 Phe Ser His Lys Ser Thr Leu Ser Gln His Tyr Arg Thr His Thr Gly 565 570 575 Glu Lys Pro Tyr Glu Cys His Glu Cys Gly Lys Ile Phe Tyr Asn Lys 580 585 590 Ser Tyr Leu Thr Lys His Asn Arg Thr His Thr Gly Glu Lys Pro Tyr 595 600 605 Glu Cys Asn Glu Cys Gly Lys Ala Phe Tyr Gln Lys Ser Gln Leu Thr 610 615 620 Gln His Gln Arg Ile His Ile Gly Glu Lys Pro Tyr Lys Cys Asn Glu 625 630 635 640 Cys Gly Lys Ala Phe Cys His Lys Ser Ala Leu Ile Val His Gln Arg 645 650 655 Thr His Thr Gln Glu Lys Pro Tyr Lys Cys Asn Glu Cys Gly Lys Ser 660 665 670 Phe Cys Val Lys Ser Gly Leu Ile Phe His Glu Arg Lys His Thr Gly 675 680 685 Glu Lys Pro Tyr Glu Cys Asn Glu Cys Gly Lys Phe Phe Arg His Lys 690 695 700 Ser Ser Leu Thr Val His His Arg Ala His Thr Gly Glu Lys Ser Cys 705 710 715 720 Gln Cys Asn Glu Cys Gly Lys Ile Phe Tyr Arg Lys Ser Glu Leu Ala 725 730 735 Gln His Gln Arg Ser His Thr Gly Glu Lys Pro Tyr Glu Cys Asn Thr 740 745 750 Cys Arg Lys Thr Phe Ser Gln Lys Ser Asn Leu Ile Val His Gln Arg 755 760 765 Arg His Ile Gly Glu Asn Leu Met Asn Glu Met Asp Ile Arg Asn Phe 770 775 780 Gln Pro Gln Val Ser Leu His Asn Ala Ser Glu Tyr Ser His Cys Gly 785 790 795 800 Glu Ser Pro Asp Asp Ile Leu Asn Val Gln 805 810 <210> SEQ ID NO 71 <211> LENGTH: 369 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q8IWU4 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(369) <400> SEQUENCE: 71 Met Glu Phe Leu Glu Arg Thr Tyr Leu Val Asn Asp Lys Ala Ala Lys 1 5 10 15 Met Tyr Ala Phe Thr Leu Glu Ser Val Glu Leu Gln Gln Lys Pro Val 20 25 30 Asn Lys Asp Gln Cys Pro Arg Glu Arg Pro Glu Glu Leu Glu Ser Gly 35 40 45 Gly Met Tyr His Cys His Ser Gly Ser Lys Pro Thr Glu Lys Gly Ala 50 55 60 Asn Glu Tyr Ala Tyr Ala Lys Trp Lys Leu Cys Ser Ala Ser Ala Ile 65 70 75 80 Cys Phe Ile Phe Met Ile Ala Glu Val Val Gly Gly His Ile Ala Gly 85 90 95 Ser Leu Ala Val Val Thr Asp Ala Ala His Leu Leu Ile Asp Leu Thr 100 105 110 Ser Phe Leu Leu Ser Leu Phe Ser Leu Trp Leu Ser Ser Lys Pro Pro 115 120 125 Ser Lys Arg Leu Thr Phe Gly Trp His Arg Ala Glu Ile Leu Gly Ala 130 135 140 Leu Leu Ser Ile Leu Cys Ile Trp Val Val Thr Gly Val Leu Val Tyr 145 150 155 160 Leu Ala Cys Glu Arg Leu Leu Tyr Pro Asp Tyr Gln Ile Gln Ala Thr 165 170 175 Val Met Ile Ile Val Ser Ser Cys Ala Val Ala Ala Asn Ile Val Leu 180 185 190 Thr Val Val Leu His Gln Arg Cys Leu Gly His Asn His Lys Glu Val 195 200 205 Gln Ala Asn Ala Ser Val Arg Ala Ala Phe Val His Ala Leu Gly Asp 210 215 220 Leu Phe Gln Ser Ile Ser Val Leu Ile Ser Ala Leu Ile Ile Tyr Phe 225 230 235 240 Lys Pro Glu Tyr Lys Ile Ala Asp Pro Ile Cys Thr Phe Ile Phe Ser 245 250 255 Ile Leu Val Leu Ala Ser Thr Ile Thr Ile Leu Lys Asp Phe Ser Ile 260 265 270 Leu Leu Met Glu Gly Val Pro Lys Ser Leu Asn Tyr Ser Gly Val Lys 275 280 285 Glu Leu Ile Leu Ala Val Asp Gly Val Leu Ser Val His Ser Leu His 290 295 300 Ile Trp Ser Leu Thr Met Asn Gln Val Ile Leu Ser Ala His Val Ala 305 310 315 320 Thr Ala Ala Ser Arg Asp Ser Gln Val Val Arg Arg Glu Ile Ala Lys 325 330 335 Ala Leu Ser Lys Ser Phe Thr Met His Ser Leu Thr Ile Gln Met Glu 340 345 350 Ser Pro Val Asp Gln Asp Pro Asp Cys Leu Phe Cys Glu Asp Pro Cys 355 360 365 Asp <210> SEQ ID NO 72 <211> LENGTH: 1231 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P08603 <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1231) <400> SEQUENCE: 72 Met Arg Leu Leu Ala Lys Ile Ile Cys Leu Met Leu Trp Ala Ile Cys 1 5 10 15 Val Ala Glu Asp Cys Asn Glu Leu Pro Pro Arg Arg Asn Thr Glu Ile 20 25 30 Leu Thr Gly Ser Trp Ser Asp Gln Thr Tyr Pro Glu Gly Thr Gln Ala 35 40 45 Ile Tyr Lys Cys Arg Pro Gly Tyr Arg Ser Leu Gly Asn Val Ile Met 50 55 60 Val Cys Arg Lys Gly Glu Trp Val Ala Leu Asn Pro Leu Arg Lys Cys 65 70 75 80 Gln Lys Arg Pro Cys Gly His Pro Gly Asp Thr Pro Phe Gly Thr Phe 85 90 95 Thr Leu Thr Gly Gly Asn Val Phe Glu Tyr Gly Val Lys Ala Val Tyr 100 105 110 Thr Cys Asn Glu Gly Tyr Gln Leu Leu Gly Glu Ile Asn Tyr Arg Glu 115 120 125 Cys Asp Thr Asp Gly Trp Thr Asn Asp Ile Pro Ile Cys Glu Val Val 130 135 140 Lys Cys Leu Pro Val Thr Ala Pro Glu Asn Gly Lys Ile Val Ser Ser 145 150 155 160 Ala Met Glu Pro Asp Arg Glu Tyr His Phe Gly Gln Ala Val Arg Phe 165 170 175 Val Cys Asn Ser Gly Tyr Lys Ile Glu Gly Asp Glu Glu Met His Cys 180 185 190 Ser Asp Asp Gly Phe Trp Ser Lys Glu Lys Pro Lys Cys Val Glu Ile 195 200 205 Ser Cys Lys Ser Pro Asp Val Ile Asn Gly Ser Pro Ile Ser Gln Lys 210 215 220 Ile Ile Tyr Lys Glu Asn Glu Arg Phe Gln Tyr Lys Cys Asn Met Gly 225 230 235 240 Tyr Glu Tyr Ser Glu Arg Gly Asp Ala Val Cys Thr Glu Ser Gly Trp 245 250 255 Arg Pro Leu Pro Ser Cys Glu Glu Lys Ser Cys Asp Asn Pro Tyr Ile 260 265 270 Pro Asn Gly Asp Tyr Ser Pro Leu Arg Ile Lys His Arg Thr Gly Asp 275 280 285 Glu Ile Thr Tyr Gln Cys Arg Asn Gly Phe Tyr Pro Ala Thr Arg Gly 290 295 300 Asn Thr Ala Lys Cys Thr Ser Thr Gly Trp Ile Pro Ala Pro Arg Cys 305 310 315 320 Thr Leu Lys Pro Cys Asp Tyr Pro Asp Ile Lys His Gly Gly Leu Tyr 325 330 335 His Glu Asn Met Arg Arg Pro Tyr Phe Pro Val Ala Val Gly Lys Tyr 340 345 350 Tyr Ser Tyr Tyr Cys Asp Glu His Phe Glu Thr Pro Ser Gly Ser Tyr 355 360 365 Trp Asp His Ile His Cys Thr Gln Asp Gly Trp Ser Pro Ala Val Pro 370 375 380 Cys Leu Arg Lys Cys Tyr Phe Pro Tyr Leu Glu Asn Gly Tyr Asn Gln 385 390 395 400 Asn Tyr Gly Arg Lys Phe Val Gln Gly Lys Ser Ile Asp Val Ala Cys 405 410 415 His Pro Gly Tyr Ala Leu Pro Lys Ala Gln Thr Thr Val Thr Cys Met 420 425 430 Glu Asn Gly Trp Ser Pro Thr Pro Arg Cys Ile Arg Val Lys Thr Cys 435 440 445 Ser Lys Ser Ser Ile Asp Ile Glu Asn Gly Phe Ile Ser Glu Ser Gln 450 455 460 Tyr Thr Tyr Ala Leu Lys Glu Lys Ala Lys Tyr Gln Cys Lys Leu Gly 465 470 475 480 Tyr Val Thr Ala Asp Gly Glu Thr Ser Gly Ser Ile Thr Cys Gly Lys 485 490 495 Asp Gly Trp Ser Ala Gln Pro Thr Cys Ile Lys Ser Cys Asp Ile Pro 500 505 510 Val Phe Met Asn Ala Arg Thr Lys Asn Asp Phe Thr Trp Phe Lys Leu 515 520 525 Asn Asp Thr Leu Asp Tyr Glu Cys His Asp Gly Tyr Glu Ser Asn Thr 530 535 540 Gly Ser Thr Thr Gly Ser Ile Val Cys Gly Tyr Asn Gly Trp Ser Asp 545 550 555 560 Leu Pro Ile Cys Tyr Glu Arg Glu Cys Glu Leu Pro Lys Ile Asp Val 565 570 575 His Leu Val Pro Asp Arg Lys Lys Asp Gln Tyr Lys Val Gly Glu Val 580 585 590 Leu Lys Phe Ser Cys Lys Pro Gly Phe Thr Ile Val Gly Pro Asn Ser 595 600 605 Val Gln Cys Tyr His Phe Gly Leu Ser Pro Asp Leu Pro Ile Cys Lys 610 615 620 Glu Gln Val Gln Ser Cys Gly Pro Pro Pro Glu Leu Leu Asn Gly Asn 625 630 635 640 Val Lys Glu Lys Thr Lys Glu Glu Tyr Gly His Ser Glu Val Val Glu 645 650 655 Tyr Tyr Cys Asn Pro Arg Phe Leu Met Lys Gly Pro Asn Lys Ile Gln 660 665 670 Cys Val Asp Gly Glu Trp Thr Thr Leu Pro Val Cys Ile Val Glu Glu 675 680 685 Ser Thr Cys Gly Asp Ile Pro Glu Leu Glu His Gly Trp Ala Gln Leu 690 695 700 Ser Ser Pro Pro Tyr Tyr Tyr Gly Asp Ser Val Glu Phe Asn Cys Ser 705 710 715 720 Glu Ser Phe Thr Met Ile Gly His Arg Ser Ile Thr Cys Ile His Gly 725 730 735 Val Trp Thr Gln Leu Pro Gln Cys Val Ala Ile Asp Lys Leu Lys Lys 740 745 750 Cys Lys Ser Ser Asn Leu Ile Ile Leu Glu Glu His Leu Lys Asn Lys 755 760 765 Lys Glu Phe Asp His Asn Ser Asn Ile Arg Tyr Arg Cys Arg Gly Lys 770 775 780 Glu Gly Trp Ile His Thr Val Cys Ile Asn Gly Arg Trp Asp Pro Glu 785 790 795 800 Val Asn Cys Ser Met Ala Gln Ile Gln Leu Cys Pro Pro Pro Pro Gln 805 810 815 Ile Pro Asn Ser His Asn Met Thr Thr Thr Leu Asn Tyr Arg Asp Gly 820 825 830 Glu Lys Val Ser Val Leu Cys Gln Glu Asn Tyr Leu Ile Gln Glu Gly 835 840 845 Glu Glu Ile Thr Cys Lys Asp Gly Arg Trp Gln Ser Ile Pro Leu Cys 850 855 860 Val Glu Lys Ile Pro Cys Ser Gln Pro Pro Gln Ile Glu His Gly Thr 865 870 875 880 Ile Asn Ser Ser Arg Ser Ser Gln Glu Ser Tyr Ala His Gly Thr Lys 885 890 895 Leu Ser Tyr Thr Cys Glu Gly Gly Phe Arg Ile Ser Glu Glu Asn Glu 900 905 910 Thr Thr Cys Tyr Met Gly Lys Trp Ser Ser Pro Pro Gln Cys Glu Gly 915 920 925 Leu Pro Cys Lys Ser Pro Pro Glu Ile Ser His Gly Val Val Ala His 930 935 940 Met Ser Asp Ser Tyr Gln Tyr Gly Glu Glu Val Thr Tyr Lys Cys Phe 945 950 955 960 Glu Gly Phe Gly Ile Asp Gly Pro Ala Ile Ala Lys Cys Leu Gly Glu 965 970 975 Lys Trp Ser His Pro Pro Ser Cys Ile Lys Thr Asp Cys Leu Ser Leu 980 985 990 Pro Ser Phe Glu Asn Ala Ile Pro Met Gly Glu Lys Lys Asp Val Tyr 995 1000 1005 Lys Ala Gly Glu Gln Val Thr Tyr Thr Cys Ala Thr Tyr Tyr Lys 1010 1015 1020 Met Asp Gly Ala Ser Asn Val Thr Cys Ile Asn Ser Arg Trp Thr 1025 1030 1035 Gly Arg Pro Thr Cys Arg Asp Thr Ser Cys Val Asn Pro Pro Thr 1040 1045 1050 Val Gln Asn Ala Tyr Ile Val Ser Arg Gln Met Ser Lys Tyr Pro 1055 1060 1065 Ser Gly Glu Arg Val Arg Tyr Gln Cys Arg Ser Pro Tyr Glu Met 1070 1075 1080 Phe Gly Asp Glu Glu Val Met Cys Leu Asn Gly Asn Trp Thr Glu 1085 1090 1095 Pro Pro Gln Cys Lys Asp Ser Thr Gly Lys Cys Gly Pro Pro Pro 1100 1105 1110 Pro Ile Asp Asn Gly Asp Ile Thr Ser Phe Pro Leu Ser Val Tyr 1115 1120 1125 Ala Pro Ala Ser Ser Val Glu Tyr Gln Cys Gln Asn Leu Tyr Gln 1130 1135 1140 Leu Glu Gly Asn Lys Arg Ile Thr Cys Arg Asn Gly Gln Trp Ser 1145 1150 1155 Glu Pro Pro Lys Cys Leu His Pro Cys Val Ile Ser Arg Glu Ile 1160 1165 1170 Met Glu Asn Tyr Asn Ile Ala Leu Arg Trp Thr Ala Lys Gln Lys 1175 1180 1185 Leu Tyr Ser Arg Thr Gly Glu Ser Val Glu Phe Val Cys Lys Arg 1190 1195 1200 Gly Tyr Arg Leu Ser Ser Arg Ser His Thr Leu Arg Thr Thr Cys 1205 1210 1215 Trp Asp Gly Lys Leu Glu Tyr Pro Thr Cys Ala Lys Arg 1220 1225 1230 <210> SEQ ID NO 73 <211> LENGTH: 1663 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01024 <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1663) <400> SEQUENCE: 73 Met Gly Pro Thr Ser Gly Pro Ser Leu Leu Leu Leu Leu Leu Thr His 1 5 10 15 Leu Pro Leu Ala Leu Gly Ser Pro Met Tyr Ser Ile Ile Thr Pro Asn 20 25 30 Ile Leu Arg Leu Glu Ser Glu Glu Thr Met Val Leu Glu Ala His Asp 35 40 45 Ala Gln Gly Asp Val Pro Val Thr Val Thr Val His Asp Phe Pro Gly 50 55 60 Lys Lys Leu Val Leu Ser Ser Glu Lys Thr Val Leu Thr Pro Ala Thr 65 70 75 80 Asn His Met Gly Asn Val Thr Phe Thr Ile Pro Ala Asn Arg Glu Phe 85 90 95 Lys Ser Glu Lys Gly Arg Asn Lys Phe Val Thr Val Gln Ala Thr Phe 100 105 110 Gly Thr Gln Val Val Glu Lys Val Val Leu Val Ser Leu Gln Ser Gly 115 120 125 Tyr Leu Phe Ile Gln Thr Asp Lys Thr Ile Tyr Thr Pro Gly Ser Thr 130 135 140 Val Leu Tyr Arg Ile Phe Thr Val Asn His Lys Leu Leu Pro Val Gly 145 150 155 160 Arg Thr Val Met Val Asn Ile Glu Asn Pro Glu Gly Ile Pro Val Lys 165 170 175 Gln Asp Ser Leu Ser Ser Gln Asn Gln Leu Gly Val Leu Pro Leu Ser 180 185 190 Trp Asp Ile Pro Glu Leu Val Asn Met Gly Gln Trp Lys Ile Arg Ala 195 200 205 Tyr Tyr Glu Asn Ser Pro Gln Gln Val Phe Ser Thr Glu Phe Glu Val 210 215 220 Lys Glu Tyr Val Leu Pro Ser Phe Glu Val Ile Val Glu Pro Thr Glu 225 230 235 240 Lys Phe Tyr Tyr Ile Tyr Asn Glu Lys Gly Leu Glu Val Thr Ile Thr 245 250 255 Ala Arg Phe Leu Tyr Gly Lys Lys Val Glu Gly Thr Ala Phe Val Ile 260 265 270 Phe Gly Ile Gln Asp Gly Glu Gln Arg Ile Ser Leu Pro Glu Ser Leu 275 280 285 Lys Arg Ile Pro Ile Glu Asp Gly Ser Gly Glu Val Val Leu Ser Arg 290 295 300 Lys Val Leu Leu Asp Gly Val Gln Asn Pro Arg Ala Glu Asp Leu Val 305 310 315 320 Gly Lys Ser Leu Tyr Val Ser Ala Thr Val Ile Leu His Ser Gly Ser 325 330 335 Asp Met Val Gln Ala Glu Arg Ser Gly Ile Pro Ile Val Thr Ser Pro 340 345 350 Tyr Gln Ile His Phe Thr Lys Thr Pro Lys Tyr Phe Lys Pro Gly Met 355 360 365 Pro Phe Asp Leu Met Val Phe Val Thr Asn Pro Asp Gly Ser Pro Ala 370 375 380 Tyr Arg Val Pro Val Ala Val Gln Gly Glu Asp Thr Val Gln Ser Leu 385 390 395 400 Thr Gln Gly Asp Gly Val Ala Lys Leu Ser Ile Asn Thr His Pro Ser 405 410 415 Gln Lys Pro Leu Ser Ile Thr Val Arg Thr Lys Lys Gln Glu Leu Ser 420 425 430 Glu Ala Glu Gln Ala Thr Arg Thr Met Gln Ala Leu Pro Tyr Ser Thr 435 440 445 Val Gly Asn Ser Asn Asn Tyr Leu His Leu Ser Val Leu Arg Thr Glu 450 455 460 Leu Arg Pro Gly Glu Thr Leu Asn Val Asn Phe Leu Leu Arg Met Asp 465 470 475 480 Arg Ala His Glu Ala Lys Ile Arg Tyr Tyr Thr Tyr Leu Ile Met Asn 485 490 495 Lys Gly Arg Leu Leu Lys Ala Gly Arg Gln Val Arg Glu Pro Gly Gln 500 505 510 Asp Leu Val Val Leu Pro Leu Ser Ile Thr Thr Asp Phe Ile Pro Ser 515 520 525 Phe Arg Leu Val Ala Tyr Tyr Thr Leu Ile Gly Ala Ser Gly Gln Arg 530 535 540 Glu Val Val Ala Asp Ser Val Trp Val Asp Val Lys Asp Ser Cys Val 545 550 555 560 Gly Ser Leu Val Val Lys Ser Gly Gln Ser Glu Asp Arg Gln Pro Val 565 570 575 Pro Gly Gln Gln Met Thr Leu Lys Ile Glu Gly Asp His Gly Ala Arg 580 585 590 Val Val Leu Val Ala Val Asp Lys Gly Val Phe Val Leu Asn Lys Lys 595 600 605 Asn Lys Leu Thr Gln Ser Lys Ile Trp Asp Val Val Glu Lys Ala Asp 610 615 620 Ile Gly Cys Thr Pro Gly Ser Gly Lys Asp Tyr Ala Gly Val Phe Ser 625 630 635 640 Asp Ala Gly Leu Thr Phe Thr Ser Ser Ser Gly Gln Gln Thr Ala Gln 645 650 655 Arg Ala Glu Leu Gln Cys Pro Gln Pro Ala Ala Arg Arg Arg Arg Ser 660 665 670 Val Gln Leu Thr Glu Lys Arg Met Asp Lys Val Gly Lys Tyr Pro Lys 675 680 685 Glu Leu Arg Lys Cys Cys Glu Asp Gly Met Arg Glu Asn Pro Met Arg 690 695 700 Phe Ser Cys Gln Arg Arg Thr Arg Phe Ile Ser Leu Gly Glu Ala Cys 705 710 715 720 Lys Lys Val Phe Leu Asp Cys Cys Asn Tyr Ile Thr Glu Leu Arg Arg 725 730 735 Gln His Ala Arg Ala Ser His Leu Gly Leu Ala Arg Ser Asn Leu Asp 740 745 750 Glu Asp Ile Ile Ala Glu Glu Asn Ile Val Ser Arg Ser Glu Phe Pro 755 760 765 Glu Ser Trp Leu Trp Asn Val Glu Asp Leu Lys Glu Pro Pro Lys Asn 770 775 780 Gly Ile Ser Thr Lys Leu Met Asn Ile Phe Leu Lys Asp Ser Ile Thr 785 790 795 800 Thr Trp Glu Ile Leu Ala Val Ser Met Ser Asp Lys Lys Gly Ile Cys 805 810 815 Val Ala Asp Pro Phe Glu Val Thr Val Met Gln Asp Phe Phe Ile Asp 820 825 830 Leu Arg Leu Pro Tyr Ser Val Val Arg Asn Glu Gln Val Glu Ile Arg 835 840 845 Ala Val Leu Tyr Asn Tyr Arg Gln Asn Gln Glu Leu Lys Val Arg Val 850 855 860 Glu Leu Leu His Asn Pro Ala Phe Cys Ser Leu Ala Thr Thr Lys Arg 865 870 875 880 Arg His Gln Gln Thr Val Thr Ile Pro Pro Lys Ser Ser Leu Ser Val 885 890 895 Pro Tyr Val Ile Val Pro Leu Lys Thr Gly Leu Gln Glu Val Glu Val 900 905 910 Lys Ala Ala Val Tyr His His Phe Ile Ser Asp Gly Val Arg Lys Ser 915 920 925 Leu Lys Val Val Pro Glu Gly Ile Arg Met Asn Lys Thr Val Ala Val 930 935 940 Arg Thr Leu Asp Pro Glu Arg Leu Gly Arg Glu Gly Val Gln Lys Glu 945 950 955 960 Asp Ile Pro Pro Ala Asp Leu Ser Asp Gln Val Pro Asp Thr Glu Ser 965 970 975 Glu Thr Arg Ile Leu Leu Gln Gly Thr Pro Val Ala Gln Met Thr Glu 980 985 990 Asp Ala Val Asp Ala Glu Arg Leu Lys His Leu Ile Val Thr Pro Ser 995 1000 1005 Gly Cys Gly Glu Gln Asn Met Ile Gly Met Thr Pro Thr Val Ile 1010 1015 1020 Ala Val His Tyr Leu Asp Glu Thr Glu Gln Trp Glu Lys Phe Gly 1025 1030 1035 Leu Glu Lys Arg Gln Gly Ala Leu Glu Leu Ile Lys Lys Gly Tyr 1040 1045 1050 Thr Gln Gln Leu Ala Phe Arg Gln Pro Ser Ser Ala Phe Ala Ala 1055 1060 1065 Phe Val Lys Arg Ala Pro Ser Thr Trp Leu Thr Ala Tyr Val Val 1070 1075 1080 Lys Val Phe Ser Leu Ala Val Asn Leu Ile Ala Ile Asp Ser Gln 1085 1090 1095 Val Leu Cys Gly Ala Val Lys Trp Leu Ile Leu Glu Lys Gln Lys 1100 1105 1110 Pro Asp Gly Val Phe Gln Glu Asp Ala Pro Val Ile His Gln Glu 1115 1120 1125 Met Ile Gly Gly Leu Arg Asn Asn Asn Glu Lys Asp Met Ala Leu 1130 1135 1140 Thr Ala Phe Val Leu Ile Ser Leu Gln Glu Ala Lys Asp Ile Cys 1145 1150 1155 Glu Glu Gln Val Asn Ser Leu Pro Gly Ser Ile Thr Lys Ala Gly 1160 1165 1170 Asp Phe Leu Glu Ala Asn Tyr Met Asn Leu Gln Arg Ser Tyr Thr 1175 1180 1185 Val Ala Ile Ala Gly Tyr Ala Leu Ala Gln Met Gly Arg Leu Lys 1190 1195 1200 Gly Pro Leu Leu Asn Lys Phe Leu Thr Thr Ala Lys Asp Lys Asn 1205 1210 1215 Arg Trp Glu Asp Pro Gly Lys Gln Leu Tyr Asn Val Glu Ala Thr 1220 1225 1230 Ser Tyr Ala Leu Leu Ala Leu Leu Gln Leu Lys Asp Phe Asp Phe 1235 1240 1245 Val Pro Pro Val Val Arg Trp Leu Asn Glu Gln Arg Tyr Tyr Gly 1250 1255 1260 Gly Gly Tyr Gly Ser Thr Gln Ala Thr Phe Met Val Phe Gln Ala 1265 1270 1275 Leu Ala Gln Tyr Gln Lys Asp Ala Pro Asp His Gln Glu Leu Asn 1280 1285 1290 Leu Asp Val Ser Leu Gln Leu Pro Ser Arg Ser Ser Lys Ile Thr 1295 1300 1305 His Arg Ile His Trp Glu Ser Ala Ser Leu Leu Arg Ser Glu Glu 1310 1315 1320 Thr Lys Glu Asn Glu Gly Phe Thr Val Thr Ala Glu Gly Lys Gly 1325 1330 1335 Gln Gly Thr Leu Ser Val Val Thr Met Tyr His Ala Lys Ala Lys 1340 1345 1350 Asp Gln Leu Thr Cys Asn Lys Phe Asp Leu Lys Val Thr Ile Lys 1355 1360 1365 Pro Ala Pro Glu Thr Glu Lys Arg Pro Gln Asp Ala Lys Asn Thr 1370 1375 1380 Met Ile Leu Glu Ile Cys Thr Arg Tyr Arg Gly Asp Gln Asp Ala 1385 1390 1395 Thr Met Ser Ile Leu Asp Ile Ser Met Met Thr Gly Phe Ala Pro 1400 1405 1410 Asp Thr Asp Asp Leu Lys Gln Leu Ala Asn Gly Val Asp Arg Tyr 1415 1420 1425 Ile Ser Lys Tyr Glu Leu Asp Lys Ala Phe Ser Asp Arg Asn Thr 1430 1435 1440 Leu Ile Ile Tyr Leu Asp Lys Val Ser His Ser Glu Asp Asp Cys 1445 1450 1455 Leu Ala Phe Lys Val His Gln Tyr Phe Asn Val Glu Leu Ile Gln 1460 1465 1470 Pro Gly Ala Val Lys Val Tyr Ala Tyr Tyr Asn Leu Glu Glu Ser 1475 1480 1485 Cys Thr Arg Phe Tyr His Pro Glu Lys Glu Asp Gly Lys Leu Asn 1490 1495 1500 Lys Leu Cys Arg Asp Glu Leu Cys Arg Cys Ala Glu Glu Asn Cys 1505 1510 1515 Phe Ile Gln Lys Ser Asp Asp Lys Val Thr Leu Glu Glu Arg Leu 1520 1525 1530 Asp Lys Ala Cys Glu Pro Gly Val Asp Tyr Val Tyr Lys Thr Arg 1535 1540 1545 Leu Val Lys Val Gln Leu Ser Asn Asp Phe Asp Glu Tyr Ile Met 1550 1555 1560 Ala Ile Glu Gln Thr Ile Lys Ser Gly Ser Asp Glu Val Gln Val 1565 1570 1575 Gly Gln Gln Arg Thr Phe Ile Ser Pro Ile Lys Cys Arg Glu Ala 1580 1585 1590 Leu Lys Leu Glu Glu Lys Lys His Tyr Leu Met Trp Gly Leu Ser 1595 1600 1605 Ser Asp Phe Trp Gly Glu Lys Pro Asn Leu Ser Tyr Ile Ile Gly 1610 1615 1620 Lys Asp Thr Trp Val Glu His Trp Pro Glu Glu Asp Glu Cys Gln 1625 1630 1635 Asp Glu Glu Asn Gln Lys Gln Cys Gln Asp Leu Gly Ala Phe Thr 1640 1645 1650 Glu Ser Met Val Val Phe Gly Cys Pro Asn 1655 1660 <210> SEQ ID NO 74 <211> LENGTH: 1463 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1463) <400> SEQUENCE: 74 Met Leu Leu Ser Pro Ser Leu Leu Leu Leu Leu Leu Leu Gly Ala Pro 1 5 10 15 Arg Gly Cys Ala Glu Gly Val Ala Ala Ala Leu Thr Pro Glu Arg Leu 20 25 30 Leu Glu Trp Gln Asp Lys Gly Ile Phe Val Ile Gln Ser Glu Ser Leu 35 40 45 Lys Lys Cys Ile Gln Ala Gly Lys Ser Val Leu Thr Leu Glu Asn Cys 50 55 60 Lys Gln Ala Asn Lys His Met Leu Trp Lys Trp Val Ser Asn His Gly 65 70 75 80 Leu Phe Asn Ile Gly Gly Ser Gly Cys Leu Gly Leu Asn Phe Ser Ala 85 90 95 Pro Glu Gln Pro Leu Ser Leu Tyr Glu Cys Asp Ser Thr Leu Val Ser 100 105 110 Leu Arg Trp Arg Cys Asn Arg Lys Met Ile Thr Gly Pro Leu Gln Tyr 115 120 125 Ser Val Gln Val Ala His Asp Asn Thr Val Val Ala Ser Arg Lys Tyr 130 135 140 Ile His Lys Trp Ile Ser Tyr Gly Ser Gly Gly Gly Asp Ile Cys Glu 145 150 155 160 Tyr Leu His Lys Asp Leu His Thr Ile Lys Gly Asn Thr His Gly Met 165 170 175 Pro Cys Met Phe Pro Phe Gln Tyr Asn His Gln Trp His His Glu Cys 180 185 190 Thr Arg Glu Gly Arg Glu Asp Asp Leu Leu Trp Cys Ala Thr Thr Ser 195 200 205 Arg Tyr Glu Arg Asp Glu Lys Trp Gly Phe Cys Pro Asp Pro Thr Ser 210 215 220 Ala Glu Val Gly Cys Asp Thr Ile Trp Glu Lys Asp Leu Asn Ser His 225 230 235 240 Ile Cys Tyr Gln Phe Asn Leu Leu Ser Ser Leu Ser Trp Ser Glu Ala 245 250 255 His Ser Ser Cys Gln Met Gln Gly Gly Thr Leu Leu Ser Ile Thr Asp 260 265 270 Glu Thr Glu Glu Asn Phe Ile Arg Glu His Met Ser Ser Lys Thr Val 275 280 285 Glu Val Trp Met Gly Leu Asn Gln Leu Asp Glu His Ala Gly Trp Gln 290 295 300 Trp Ser Asp Gly Thr Pro Leu Asn Tyr Leu Asn Trp Ser Pro Glu Val 305 310 315 320 Asn Phe Glu Pro Phe Val Glu Asp His Cys Gly Thr Phe Ser Ser Phe 325 330 335 Met Pro Ser Ala Trp Arg Ser Arg Asp Cys Glu Ser Thr Leu Pro Tyr 340 345 350 Ile Cys Lys Lys Tyr Leu Asn His Ile Asp His Glu Ile Val Glu Lys 355 360 365 Asp Ala Trp Lys Tyr Tyr Ala Thr His Cys Glu Pro Gly Trp Asn Pro 370 375 380 Tyr Asn Arg Asn Cys Tyr Lys Leu Gln Lys Glu Glu Lys Thr Trp His 385 390 395 400 Glu Ala Leu Arg Ser Cys Gln Ala Asp Asn Ser Ala Leu Ile Asp Ile 405 410 415 Thr Ser Leu Ala Glu Val Glu Phe Leu Val Thr Leu Leu Gly Asp Glu 420 425 430 Asn Ala Ser Glu Thr Trp Ile Gly Leu Ser Ser Asn Lys Ile Pro Val 435 440 445 Ser Phe Glu Trp Ser Asn Asp Ser Ser Val Ile Phe Thr Asn Trp His 450 455 460 Thr Leu Glu Pro His Ile Phe Pro Asn Arg Ser Gln Leu Cys Val Ser 465 470 475 480 Ala Glu Gln Ser Glu Gly His Trp Lys Val Lys Asn Cys Glu Glu Arg 485 490 495 Leu Phe Tyr Ile Cys Lys Lys Ala Gly His Val Leu Ser Asp Ala Glu 500 505 510 Ser Gly Cys Gln Glu Gly Trp Glu Arg His Gly Gly Phe Cys Tyr Lys 515 520 525 Ile Asp Thr Val Leu Arg Ser Phe Asp Gln Ala Ser Ser Gly Tyr Tyr 530 535 540 Cys Pro Pro Ala Leu Val Thr Ile Thr Asn Arg Phe Glu Gln Ala Phe 545 550 555 560 Ile Thr Ser Leu Ile Ser Ser Val Val Lys Met Lys Asp Ser Tyr Phe 565 570 575 Trp Ile Ala Leu Gln Asp Gln Asn Asp Thr Gly Glu Tyr Thr Trp Lys 580 585 590 Pro Val Gly Gln Lys Pro Glu Pro Val Gln Tyr Thr His Trp Asn Thr 595 600 605 His Gln Pro Arg Tyr Ser Gly Gly Cys Val Ala Met Arg Gly Arg His 610 615 620 Pro Leu Gly Arg Trp Glu Val Lys His Cys Arg His Phe Lys Ala Met 625 630 635 640 Ser Leu Cys Lys Gln Pro Val Glu Asn Gln Glu Lys Ala Glu Tyr Glu 645 650 655 Glu Arg Trp Pro Phe His Pro Cys Tyr Leu Asp Trp Glu Ser Glu Pro 660 665 670 Gly Leu Ala Ser Cys Phe Lys Val Phe His Ser Glu Lys Val Leu Met 675 680 685 Lys Arg Thr Trp Arg Glu Ala Glu Ala Phe Cys Glu Glu Phe Gly Ala 690 695 700 His Leu Ala Ser Phe Ala His Ile Glu Glu Glu Asn Phe Val Asn Glu 705 710 715 720 Leu Leu His Ser Lys Phe Asn Trp Thr Glu Glu Arg Gln Phe Trp Ile 725 730 735 Gly Phe Asn Lys Arg Asn Pro Leu Asn Ala Gly Ser Trp Glu Trp Ser 740 745 750 Asp Arg Thr Pro Val Val Ser Ser Phe Leu Asp Asn Thr Tyr Phe Gly 755 760 765 Glu Asp Ala Arg Asn Cys Ala Val Tyr Lys Ala Asn Lys Thr Leu Leu 770 775 780 Pro Leu His Cys Gly Ser Lys Arg Glu Trp Ile Cys Lys Ile Pro Arg 785 790 795 800 Asp Val Lys Pro Lys Ile Pro Phe Trp Tyr Gln Tyr Asp Val Pro Trp 805 810 815 Leu Phe Tyr Gln Asp Ala Glu Tyr Leu Phe His Thr Phe Ala Ser Glu 820 825 830 Trp Leu Asn Phe Glu Phe Val Cys Ser Trp Leu His Ser Asp Leu Leu 835 840 845 Thr Ile His Ser Ala His Glu Gln Glu Phe Ile His Ser Lys Ile Lys 850 855 860 Ala Leu Ser Lys Tyr Gly Ala Ser Trp Trp Ile Gly Leu Gln Glu Glu 865 870 875 880 Arg Ala Asn Asp Glu Phe Arg Trp Arg Asp Gly Thr Pro Val Ile Tyr 885 890 895 Gln Asn Trp Asp Thr Gly Arg Glu Arg Thr Val Asn Asn Gln Ser Gln 900 905 910 Arg Cys Gly Phe Ile Ser Ser Ile Thr Gly Leu Trp Gly Ser Glu Glu 915 920 925 Cys Ser Val Ser Met Pro Ser Ile Cys Lys Arg Lys Lys Val Trp Leu 930 935 940 Ile Glu Lys Lys Lys Asp Thr Pro Lys Gln His Gly Thr Cys Pro Lys 945 950 955 960 Gly Trp Leu Tyr Phe Asn Tyr Lys Cys Leu Leu Leu Asn Ile Pro Lys 965 970 975 Asp Pro Ser Ser Trp Lys Asn Trp Thr His Ala Gln His Phe Cys Ala 980 985 990 Glu Glu Gly Gly Thr Leu Val Ala Ile Glu Ser Glu Val Glu Gln Ala 995 1000 1005 Phe Ile Thr Met Asn Leu Phe Gly Gln Thr Thr Ser Val Trp Ile 1010 1015 1020 Gly Leu Gln Asn Asp Asp Tyr Glu Thr Trp Leu Asn Gly Lys Pro 1025 1030 1035 Val Val Tyr Ser Asn Trp Ser Pro Phe Asp Ile Ile Asn Ile Pro 1040 1045 1050 Ser His Asn Thr Thr Glu Val Gln Lys His Ile Pro Leu Cys Ala 1055 1060 1065 Leu Leu Ser Ser Asn Pro Asn Phe His Phe Thr Gly Lys Trp Tyr 1070 1075 1080 Phe Glu Asp Cys Gly Lys Glu Gly Tyr Gly Phe Val Cys Glu Lys 1085 1090 1095 Met Gln Asp Thr Ser Gly His Gly Val Asn Thr Ser Asp Met Tyr 1100 1105 1110 Pro Met Pro Asn Thr Leu Glu Tyr Gly Asn Arg Thr Tyr Lys Ile 1115 1120 1125 Ile Asn Ala Asn Met Thr Trp Tyr Ala Ala Ile Lys Thr Cys Leu 1130 1135 1140 Met His Lys Ala Gln Leu Val Ser Ile Thr Asp Gln Tyr His Gln 1145 1150 1155 Ser Phe Leu Thr Val Val Leu Asn Arg Leu Gly Tyr Ala His Trp 1160 1165 1170 Ile Gly Leu Phe Thr Thr Asp Asn Gly Leu Asn Phe Asp Trp Ser 1175 1180 1185 Asp Gly Thr Lys Ser Ser Phe Thr Phe Trp Lys Asp Glu Glu Ser 1190 1195 1200 Ser Leu Leu Gly Asp Cys Val Phe Ala Asp Ser Asn Gly Arg Trp 1205 1210 1215 His Ser Thr Ala Cys Glu Ser Phe Leu Gln Gly Ala Ile Cys His 1220 1225 1230 Val Pro Pro Glu Thr Arg Gln Ser Glu His Pro Glu Leu Cys Ser 1235 1240 1245 Glu Thr Ser Ile Pro Trp Ile Lys Phe Lys Ser Asn Cys Tyr Ser 1250 1255 1260 Phe Ser Thr Val Leu Asp Ser Met Ser Phe Glu Ala Ala His Glu 1265 1270 1275 Phe Cys Lys Lys Glu Gly Ser Asn Leu Leu Thr Ile Lys Asp Glu 1280 1285 1290 Ala Glu Asn Ala Phe Leu Leu Glu Glu Leu Phe Ala Phe Gly Ser 1295 1300 1305 Ser Val Gln Met Val Trp Leu Asn Ala Gln Phe Asp Gly Asn Asn 1310 1315 1320 Glu Thr Ile Lys Trp Phe Asp Gly Thr Pro Thr Asp Gln Ser Asn 1325 1330 1335 Trp Gly Ile Arg Lys Pro Asp Thr Asp Tyr Phe Lys Pro His His 1340 1345 1350 Cys Val Ala Leu Arg Ile Pro Glu Gly Leu Trp Gln Leu Ser Pro 1355 1360 1365 Cys Gln Glu Lys Lys Gly Phe Ile Cys Lys Met Glu Ala Asp Ile 1370 1375 1380 His Thr Ala Glu Ala Leu Pro Glu Lys Gly Pro Ser His Ser Ile 1385 1390 1395 Ile Pro Leu Ala Val Val Leu Thr Leu Ile Val Ile Val Ala Ile 1400 1405 1410 Cys Thr Leu Ser Phe Cys Ile Tyr Lys His Asn Gly Gly Phe Phe 1415 1420 1425 Arg Arg Leu Ala Gly Phe Arg Asn Pro Tyr Tyr Pro Ala Thr Asn 1430 1435 1440 Phe Ser Thr Val Tyr Leu Glu Glu Asn Ile Leu Ile Ser Asp Leu 1445 1450 1455 Glu Lys Ser Asp Gln 1460

1 SEQUENCE LISTING <160> NUMBER OF SEQ ID NOS: 74 <210> SEQ ID NO 1 <211> LENGTH: 2067 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O00468 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(2067) <400> SEQUENCE: 1 Met Ala Gly Arg Ser His Pro Gly Pro Leu Arg Pro Leu Leu Pro Leu 1 5 10 15 Leu Val Val Ala Ala Cys Val Leu Pro Gly Ala Gly Gly Thr Cys Pro 20 25 30 Glu Arg Ala Leu Glu Arg Arg Glu Glu Glu Ala Asn Val Val Leu Thr 35 40 45 Gly Thr Val Glu Glu Ile Leu Asn Val Asp Pro Val Gln His Thr Tyr 50 55 60 Ser Cys Lys Val Arg Val Trp Arg Tyr Leu Lys Gly Lys Asp Leu Val 65 70 75 80 Ala Arg Glu Ser Leu Leu Asp Gly Gly Asn Lys Val Val Ile Ser Gly 85 90 95 Phe Gly Asp Pro Leu Ile Cys Asp Asn Gln Val Ser Thr Gly Asp Thr 100 105 110 Arg Ile Phe Phe Val Asn Pro Ala Pro Pro Tyr Leu Trp Pro Ala His 115 120 125 Lys Asn Glu Leu Met Leu Asn Ser Ser Leu Met Arg Ile Thr Leu Arg 130 135 140 Asn Leu Glu Glu Val Glu Phe Cys Val Glu Asp Lys Pro Gly Thr His 145 150 155 160 Phe Thr Pro Val Pro Pro Thr Pro Pro Asp Ala Cys Arg Gly Met Leu 165 170 175 Cys Gly Phe Gly Ala Val Cys Glu Pro Asn Ala Glu Gly Pro Gly Arg 180 185 190 Ala Ser Cys Val Cys Lys Lys Ser Pro Cys Pro Ser Val Val Ala Pro 195 200 205 Val Cys Gly Ser Asp Ala Ser Thr Tyr Ser Asn Glu Cys Glu Leu Gln 210 215 220 Arg Ala Gln Cys Ser Gln Gln Arg Arg Ile Arg Leu Leu Ser Arg Gly 225 230 235 240 Pro Cys Gly Ser Arg Asp Pro Cys Ser Asn Val Thr Cys Ser Phe Gly 245 250 255 Ser Thr Cys Ala Arg Ser Ala Asp Gly Leu Thr Ala Ser Cys Leu Cys 260 265 270 Pro Ala Thr Cys Arg Gly Ala Pro Glu Gly Thr Val Cys Gly Ser Asp 275 280 285 Gly Ala Asp Tyr Pro Gly Glu Cys Gln Leu Leu Arg Arg Ala Cys Ala 290 295 300 Arg Gln Glu Asn Val Phe Lys Lys Phe Asp Gly Pro Cys Asp Pro Cys 305 310 315 320 Gln Gly Ala Leu Pro Asp Pro Ser Arg Ser Cys Arg Val Asn Pro Arg 325 330 335 Thr Arg Arg Pro Glu Met Leu Leu Arg Pro Glu Ser Cys Pro Ala Arg 340 345 350 Gln Ala Pro Val Cys Gly Asp Asp Gly Val Thr Tyr Glu Asn Asp Cys 355 360 365 Val Met Gly Arg Ser Gly Ala Ala Arg Gly Leu Leu Leu Gln Lys Val 370 375 380 Arg Ser Gly Gln Cys Gln Gly Arg Asp Gln Cys Pro Glu Pro Cys Arg 385 390 395 400 Phe Asn Ala Val Cys Leu Ser Arg Arg Gly Arg Pro Arg Cys Ser Cys 405 410 415 Asp Arg Val Thr Cys Asp Gly Ala Tyr Arg Pro Val Cys Ala Gln Asp 420 425 430 Gly Arg Thr Tyr Asp Ser Asp Cys Trp Arg Gln Gln Ala Glu Cys Arg 435 440 445 Gln Gln Arg Ala Ile Pro Ser Lys His Gln Gly Pro Cys Asp Gln Ala 450 455 460 Pro Ser Pro Cys Leu Gly Val Gln Cys Ala Phe Gly Ala Thr Cys Ala 465 470 475 480 Val Lys Asn Gly Gln Ala Ala Cys Glu Cys Leu Gln Ala Cys Ser Ser 485 490 495 Leu Tyr Asp Pro Val Cys Gly Ser Asp Gly Val Thr Tyr Gly Ser Ala 500 505 510 Cys Glu Leu Glu Ala Thr Ala Cys Thr Leu Gly Arg Glu Ile Gln Val 515 520 525 Ala Arg Lys Gly Pro Cys Asp Arg Cys Gly Gln Cys Arg Phe Gly Ala 530 535 540 Leu Cys Glu Ala Glu Thr Gly Arg Cys Val Cys Pro Ser Glu Cys Val 545 550 555 560 Ala Leu Ala Gln Pro Val Cys Gly Ser Asp Gly His Thr Tyr Pro Ser 565 570 575 Glu Cys Met Leu His Val His Ala Cys Thr His Gln Ile Ser Leu His 580 585 590 Val Ala Ser Ala Gly Pro Cys Glu Thr Cys Gly Asp Ala Val Cys Ala 595 600 605 Phe Gly Ala Val Cys Ser Ala Gly Gln Cys Val Cys Pro Arg Cys Glu 610 615 620 His Pro Pro Pro Gly Pro Val Cys Gly Ser Asp Gly Val Thr Tyr Gly 625 630 635 640 Ser Ala Cys Glu Leu Arg Glu Ala Ala Cys Leu Gln Gln Thr Gln Ile 645 650 655 Glu Glu Ala Arg Ala Gly Pro Cys Glu Gln Ala Glu Cys Gly Ser Gly 660 665 670 Gly Ser Gly Ser Gly Glu Asp Gly Asp Cys Glu Gln Glu Leu Cys Arg 675 680 685 Gln Arg Gly Gly Ile Trp Asp Glu Asp Ser Glu Asp Gly Pro Cys Val 690 695 700 Cys Asp Phe Ser Cys Gln Ser Val Pro Gly Ser Pro Val Cys Gly Ser 705 710 715 720 Asp Gly Val Thr Tyr Ser Thr Glu Cys Glu Leu Lys Lys Ala Arg Cys 725 730 735 Glu Ser Gln Arg Gly Leu Tyr Val Ala Ala Gln Gly Ala Cys Arg Gly 740 745 750 Pro Thr Phe Ala Pro Leu Pro Pro Val Ala Pro Leu His Cys Ala Gln 755 760 765 Thr Pro Tyr Gly Cys Cys Gln Asp Asn Ile Thr Ala Ala Arg Gly Val 770 775 780 Gly Leu Ala Gly Cys Pro Ser Ala Cys Gln Cys Asn Pro His Gly Ser 785 790 795 800 Tyr Gly Gly Thr Cys Asp Pro Ala Thr Gly Gln Cys Ser Cys Arg Pro 805 810 815 Gly Val Gly Gly Leu Arg Cys Asp Arg Cys Glu Pro Gly Phe Trp Asn 820 825 830 Phe Arg Gly Ile Val Thr Asp Gly Arg Ser Gly Cys Thr Pro Cys Ser 835 840 845 Cys Asp Pro Gln Gly Ala Val Arg Asp Asp Cys Glu Gln Met Thr Gly 850 855 860 Leu Cys Ser Cys Lys Pro Gly Val Ala Gly Pro Lys Cys Gly Gln Cys 865 870 875 880 Pro Asp Gly Arg Ala Leu Gly Pro Ala Gly Cys Glu Ala Asp Ala Ser 885 890 895 Ala Pro Ala Thr Cys Ala Glu Met Arg Cys Glu Phe Gly Ala Arg Cys 900 905 910 Val Glu Glu Ser Gly Ser Ala His Cys Val Cys Pro Met Leu Thr Cys 915 920 925 Pro Glu Ala Asn Ala Thr Lys Val Cys Gly Ser Asp Gly Val Thr Tyr 930 935 940 Gly Asn Glu Cys Gln Leu Lys Thr Ile Ala Cys Arg Gln Gly Leu Gln 945 950 955 960 Ile Ser Ile Gln Ser Leu Gly Pro Cys Gln Glu Ala Val Ala Pro Ser 965 970 975 Thr His Pro Thr Ser Ala Ser Val Thr Val Thr Thr Pro Gly Leu Leu 980 985 990 Leu Ser Gln Ala Leu Pro Ala Pro Pro Gly Ala Leu Pro Leu Ala Pro 995 1000 1005 Ser Ser Thr Ala His Ser Gln Thr Thr Pro Pro Pro Ser Ser Arg 1010 1015 1020 Pro Arg Thr Thr Ala Ser Val Pro Arg Thr Thr Val Trp Pro Val 1025 1030 1035 Leu Thr Val Pro Pro Thr Ala Pro Ser Pro Ala Pro Ser Leu Val 1040 1045 1050 Ala Ser Ala Phe Gly Glu Ser Gly Ser Thr Asp Gly Ser Ser Asp 1055 1060 1065 Glu Glu Leu Ser Gly Asp Gln Glu Ala Ser Gly Gly Gly Ser Gly 1070 1075 1080 Gly Leu Glu Pro Leu Glu Gly Ser Ser Val Ala Thr Pro Gly Pro 1085 1090 1095 Pro Val Glu Arg Ala Ser Cys Tyr Asn Ser Ala Leu Gly Cys Cys 1100 1105 1110 Ser Asp Gly Lys Thr Pro Ser Leu Asp Ala Glu Gly Ser Asn Cys 1115 1120 1125 Pro Ala Thr Lys Val Phe Gln Gly Val Leu Glu Leu Glu Gly Val 1130 1135 1140 Glu Gly Gln Glu Leu Phe Tyr Thr Pro Glu Met Ala Asp Pro Lys 1145 1150 1155 Ser Glu Leu Phe Gly Glu Thr Ala Arg Ser Ile Glu Ser Thr Leu 1160 1165 1170 Asp Asp Leu Phe Arg Asn Ser Asp Val Lys Lys Asp Phe Arg Ser 1175 1180 1185 Val Arg Leu Arg Asp Leu Gly Pro Gly Lys Ser Val Arg Ala Ile 1190 1195 1200 Val Asp Val His Phe Asp Pro Thr Thr Ala Phe Arg Ala Pro Asp 1205 1210 1215 Val Ala Arg Ala Leu Leu Arg Gln Ile Gln Val Ser Arg Arg Arg 1220 1225 1230

Ser Leu Gly Val Arg Arg Pro Leu Gln Glu His Val Arg Phe Met 1235 1240 1245 Asp Phe Asp Trp Phe Pro Ala Phe Ile Thr Gly Ala Thr Ser Gly 1250 1255 1260 Ala Ile Ala Ala Gly Ala Thr Ala Arg Ala Thr Thr Ala Ser Arg 1265 1270 1275 Leu Pro Ser Ser Ala Val Thr Pro Arg Ala Pro His Pro Ser His 1280 1285 1290 Thr Ser Gln Pro Val Ala Lys Thr Thr Ala Ala Pro Thr Thr Arg 1295 1300 1305 Arg Pro Pro Thr Thr Ala Pro Ser Arg Val Pro Gly Arg Arg Pro 1310 1315 1320 Pro Ala Pro Gln Gln Pro Pro Lys Pro Cys Asp Ser Gln Pro Cys 1325 1330 1335 Phe His Gly Gly Thr Cys Gln Asp Trp Ala Leu Gly Gly Gly Phe 1340 1345 1350 Thr Cys Ser Cys Pro Ala Gly Arg Gly Gly Ala Val Cys Glu Lys 1355 1360 1365 Val Leu Gly Ala Pro Val Pro Ala Phe Glu Gly Arg Ser Phe Leu 1370 1375 1380 Ala Phe Pro Thr Leu Arg Ala Tyr His Thr Leu Arg Leu Ala Leu 1385 1390 1395 Glu Phe Arg Ala Leu Glu Pro Gln Gly Leu Leu Leu Tyr Asn Gly 1400 1405 1410 Asn Ala Arg Gly Lys Asp Phe Leu Ala Leu Ala Leu Leu Asp Gly 1415 1420 1425 Arg Val Gln Leu Arg Phe Asp Thr Gly Ser Gly Pro Ala Val Leu 1430 1435 1440 Thr Ser Ala Val Pro Val Glu Pro Gly Gln Trp His Arg Leu Glu 1445 1450 1455 Leu Ser Arg His Trp Arg Arg Gly Thr Leu Ser Val Asp Gly Glu 1460 1465 1470 Thr Pro Val Leu Gly Glu Ser Pro Ser Gly Thr Asp Gly Leu Asn 1475 1480 1485 Leu Asp Thr Asp Leu Phe Val Gly Gly Val Pro Glu Asp Gln Ala 1490 1495 1500 Ala Val Ala Leu Glu Arg Thr Phe Val Gly Ala Gly Leu Arg Gly 1505 1510 1515 Cys Ile Arg Leu Leu Asp Val Asn Asn Gln Arg Leu Glu Leu Gly 1520 1525 1530 Ile Gly Pro Gly Ala Ala Thr Arg Gly Ser Gly Val Gly Glu Cys 1535 1540 1545 Gly Asp His Pro Cys Leu Pro Asn Pro Cys His Gly Gly Ala Pro 1550 1555 1560 Cys Gln Asn Leu Glu Ala Gly Arg Phe His Cys Gln Cys Pro Pro 1565 1570 1575 Gly Arg Val Gly Pro Thr Cys Ala Asp Glu Lys Ser Pro Cys Gln 1580 1585 1590 Pro Asn Pro Cys His Gly Ala Ala Pro Cys Arg Val Leu Pro Glu 1595 1600 1605 Gly Gly Ala Gln Cys Glu Cys Pro Leu Gly Arg Glu Gly Thr Phe 1610 1615 1620 Cys Gln Thr Ala Ser Gly Gln Asp Gly Ser Gly Pro Phe Leu Ala 1625 1630 1635 Asp Phe Asn Gly Phe Ser His Leu Glu Leu Arg Gly Leu His Thr 1640 1645 1650 Phe Ala Arg Asp Leu Gly Glu Lys Met Ala Leu Glu Val Val Phe 1655 1660 1665 Leu Ala Arg Gly Pro Ser Gly Leu Leu Leu Tyr Asn Gly Gln Lys 1670 1675 1680 Thr Asp Gly Lys Gly Asp Phe Val Ser Leu Ala Leu Arg Asp Arg 1685 1690 1695 Arg Leu Glu Phe Arg Tyr Asp Leu Gly Lys Gly Ala Ala Val Ile 1700 1705 1710 Arg Ser Arg Glu Pro Val Thr Leu Gly Ala Trp Thr Arg Val Ser 1715 1720 1725 Leu Glu Arg Asn Gly Arg Lys Gly Ala Leu Arg Val Gly Asp Gly 1730 1735 1740 Pro Arg Val Leu Gly Glu Ser Pro Lys Ser Arg Lys Val Pro His 1745 1750 1755 Thr Val Leu Asn Leu Lys Glu Pro Leu Tyr Val Gly Gly Ala Pro 1760 1765 1770 Asp Phe Ser Lys Leu Ala Arg Ala Ala Ala Val Ser Ser Gly Phe 1775 1780 1785 Asp Gly Ala Ile Gln Leu Val Ser Leu Gly Gly Arg Gln Leu Leu 1790 1795 1800 Thr Pro Glu His Val Leu Arg Gln Val Asp Val Thr Ser Phe Ala 1805 1810 1815 Gly His Pro Cys Thr Arg Ala Ser Gly His Pro Cys Leu Asn Gly 1820 1825 1830 Ala Ser Cys Val Pro Arg Glu Ala Ala Tyr Val Cys Leu Cys Pro 1835 1840 1845 Gly Gly Phe Ser Gly Pro His Cys Glu Lys Gly Leu Val Glu Lys 1850 1855 1860 Ser Ala Gly Asp Val Asp Thr Leu Ala Phe Asp Gly Arg Thr Phe 1865 1870 1875 Val Glu Tyr Leu Asn Ala Val Thr Glu Ser Glu Leu Ala Asn Glu 1880 1885 1890 Ile Pro Val Pro Glu Thr Leu Asp Ser Gly Ala Leu His Glu Lys 1895 1900 1905 Ala Leu Gln Ser Asn His Phe Glu Leu Ser Leu Arg Thr Glu Ala 1910 1915 1920 Thr Gln Gly Leu Val Leu Trp Ser Gly Lys Ala Thr Glu Arg Ala 1925 1930 1935 Asp Tyr Val Ala Leu Ala Ile Val Asp Gly His Leu Gln Leu Ser 1940 1945 1950 Tyr Asn Leu Gly Ser Gln Pro Val Val Leu Arg Ser Thr Val Pro 1955 1960 1965 Val Asn Thr Asn Arg Trp Leu Arg Val Val Ala His Arg Glu Gln 1970 1975 1980 Arg Glu Gly Ser Leu Gln Val Gly Asn Glu Ala Pro Val Thr Gly 1985 1990 1995 Ser Ser Pro Leu Gly Ala Thr Gln Leu Asp Thr Asp Gly Ala Leu 2000 2005 2010 Trp Leu Gly Gly Leu Pro Glu Leu Pro Val Gly Pro Ala Leu Pro 2015 2020 2025 Lys Ala Tyr Gly Thr Gly Phe Val Gly Cys Leu Arg Asp Val Val 2030 2035 2040 Val Gly Arg His Pro Leu His Leu Leu Glu Asp Ala Val Thr Lys 2045 2050 2055 Pro Glu Leu Arg Pro Cys Pro Thr Pro 2060 2065 <210> SEQ ID NO 2 <211> LENGTH: 485 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01019 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(485) <400> SEQUENCE: 2 Met Arg Lys Arg Ala Pro Gln Ser Glu Met Ala Pro Ala Gly Val Ser 1 5 10 15 Leu Arg Ala Thr Ile Leu Cys Leu Leu Ala Trp Ala Gly Leu Ala Ala 20 25 30 Gly Asp Arg Val Tyr Ile His Pro Phe His Leu Val Ile His Asn Glu 35 40 45 Ser Thr Cys Glu Gln Leu Ala Lys Ala Asn Ala Gly Lys Pro Lys Asp 50 55 60 Pro Thr Phe Ile Pro Ala Pro Ile Gln Ala Lys Thr Ser Pro Val Asp 65 70 75 80 Glu Lys Ala Leu Gln Asp Gln Leu Val Leu Val Ala Ala Lys Leu Asp 85 90 95 Thr Glu Asp Lys Leu Arg Ala Ala Met Val Gly Met Leu Ala Asn Phe 100 105 110 Leu Gly Phe Arg Ile Tyr Gly Met His Ser Glu Leu Trp Gly Val Val 115 120 125 His Gly Ala Thr Val Leu Ser Pro Thr Ala Val Phe Gly Thr Leu Ala 130 135 140 Ser Leu Tyr Leu Gly Ala Leu Asp His Thr Ala Asp Arg Leu Gln Ala 145 150 155 160 Ile Leu Gly Val Pro Trp Lys Asp Lys Asn Cys Thr Ser Arg Leu Asp 165 170 175 Ala His Lys Val Leu Ser Ala Leu Gln Ala Val Gln Gly Leu Leu Val 180 185 190 Ala Gln Gly Arg Ala Asp Ser Gln Ala Gln Leu Leu Leu Ser Thr Val 195 200 205 Val Gly Val Phe Thr Ala Pro Gly Leu His Leu Lys Gln Pro Phe Val 210 215 220 Gln Gly Leu Ala Leu Tyr Thr Pro Val Val Leu Pro Arg Ser Leu Asp 225 230 235 240 Phe Thr Glu Leu Asp Val Ala Ala Glu Lys Ile Asp Arg Phe Met Gln 245 250 255 Ala Val Thr Gly Trp Lys Thr Gly Cys Ser Leu Met Gly Ala Ser Val 260 265 270 Asp Ser Thr Leu Ala Phe Asn Thr Tyr Val His Phe Gln Gly Lys Met 275 280 285 Lys Gly Phe Ser Leu Leu Ala Glu Pro Gln Glu Phe Trp Val Asp Asn 290 295 300 Ser Thr Ser Val Ser Val Pro Met Leu Ser Gly Met Gly Thr Phe Gln 305 310 315 320 His Trp Ser Asp Ile Gln Asp Asn Phe Ser Val Thr Gln Val Pro Phe 325 330 335 Thr Glu Ser Ala Cys Leu Leu Leu Ile Gln Pro His Tyr Ala Ser Asp 340 345 350 Leu Asp Lys Val Glu Gly Leu Thr Phe Gln Gln Asn Ser Leu Asn Trp 355 360 365 Met Lys Lys Leu Ser Pro Arg Thr Ile His Leu Thr Met Pro Gln Leu

370 375 380 Val Leu Gln Gly Ser Tyr Asp Leu Gln Asp Leu Leu Ala Gln Ala Glu 385 390 395 400 Leu Pro Ala Ile Leu His Thr Glu Leu Asn Leu Gln Lys Leu Ser Asn 405 410 415 Asp Arg Ile Arg Val Gly Glu Val Leu Asn Ser Ile Phe Phe Glu Leu 420 425 430 Glu Ala Asp Glu Arg Glu Pro Thr Glu Ser Thr Gln Gln Leu Asn Lys 435 440 445 Pro Glu Val Leu Glu Val Thr Leu Asn Arg Pro Phe Leu Phe Ala Val 450 455 460 Tyr Asp Gln Ser Ala Thr Ala Leu His Phe Leu Gly Arg Val Ala Asn 465 470 475 480 Pro Leu Ser Thr Ala 485 <210> SEQ ID NO 3 <211> LENGTH: 201 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P52566 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(201) <400> SEQUENCE: 3 Met Thr Glu Lys Ala Pro Glu Pro His Val Glu Glu Asp Asp Asp Asp 1 5 10 15 Glu Leu Asp Ser Lys Leu Asn Tyr Lys Pro Pro Pro Gln Lys Ser Leu 20 25 30 Lys Glu Leu Gln Glu Met Asp Lys Asp Asp Glu Ser Leu Ile Lys Tyr 35 40 45 Lys Lys Thr Leu Leu Gly Asp Gly Pro Val Val Thr Asp Pro Lys Ala 50 55 60 Pro Asn Val Val Val Thr Arg Leu Thr Leu Val Cys Glu Ser Ala Pro 65 70 75 80 Gly Pro Ile Thr Met Asp Leu Thr Gly Asp Leu Glu Ala Leu Lys Lys 85 90 95 Glu Thr Ile Val Leu Lys Glu Gly Ser Glu Tyr Arg Val Lys Ile His 100 105 110 Phe Lys Val Asn Arg Asp Ile Val Ser Gly Leu Lys Tyr Val Gln His 115 120 125 Thr Tyr Arg Thr Gly Val Lys Val Asp Lys Ala Thr Phe Met Val Gly 130 135 140 Ser Tyr Gly Pro Arg Pro Glu Glu Tyr Glu Phe Leu Thr Pro Val Glu 145 150 155 160 Glu Ala Pro Lys Gly Met Leu Ala Arg Gly Thr Tyr His Asn Lys Ser 165 170 175 Phe Phe Thr Asp Asp Asp Lys Gln Asp His Leu Ser Trp Glu Trp Asn 180 185 190 Leu Ser Ile Lys Lys Glu Trp Thr Glu 195 200 <210> SEQ ID NO 4 <211> LENGTH: 199 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9NWT8 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(199) <400> SEQUENCE: 4 Met Leu Leu Gly Arg Leu Thr Ser Gln Leu Leu Arg Ala Val Pro Trp 1 5 10 15 Ala Gly Gly Arg Pro Pro Trp Pro Val Ser Gly Val Leu Gly Ser Arg 20 25 30 Val Cys Gly Pro Leu Tyr Ser Thr Ser Pro Ala Gly Pro Gly Arg Ala 35 40 45 Ala Ser Leu Pro Arg Lys Gly Ala Gln Leu Glu Leu Glu Glu Met Leu 50 55 60 Val Pro Arg Lys Met Ser Val Ser Pro Leu Glu Ser Trp Leu Thr Ala 65 70 75 80 Arg Cys Phe Leu Pro Arg Leu Asp Thr Gly Thr Ala Gly Thr Val Ala 85 90 95 Pro Pro Gln Ser Tyr Gln Cys Pro Pro Ser Gln Ile Gly Glu Gly Ala 100 105 110 Glu Gln Gly Asp Glu Gly Val Ala Asp Ala Pro Gln Ile Gln Cys Lys 115 120 125 Asn Val Leu Lys Ile Arg Arg Arg Lys Met Asn His His Lys Tyr Arg 130 135 140 Lys Leu Val Lys Lys Thr Arg Phe Leu Arg Arg Lys Val Gln Glu Gly 145 150 155 160 Arg Leu Arg Arg Lys Gln Ile Lys Phe Glu Lys Asp Leu Arg Arg Ile 165 170 175 Trp Leu Lys Ala Gly Leu Lys Glu Ala Pro Glu Gly Trp Gln Thr Pro 180 185 190 Lys Ile Tyr Leu Arg Gly Lys 195 <210> SEQ ID NO 5 <211> LENGTH: 1744 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P0C0L5 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1744) <400> SEQUENCE: 5 Met Arg Leu Leu Trp Gly Leu Ile Trp Ala Ser Ser Phe Phe Thr Leu 1 5 10 15 Ser Leu Gln Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His 20 25 30 Leu Gly Val Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg 35 40 45 Gly Gln Val Val Lys Gly Ser Val Phe Leu Arg Asn Pro Ser Arg Asn 50 55 60 Asn Val Pro Cys Ser Pro Lys Val Asp Phe Thr Leu Ser Ser Glu Arg 65 70 75 80 Asp Phe Ala Leu Leu Ser Leu Gln Val Pro Leu Lys Asp Ala Lys Ser 85 90 95 Cys Gly Leu His Gln Leu Leu Arg Gly Pro Glu Val Gln Leu Val Ala 100 105 110 His Ser Pro Trp Leu Lys Asp Ser Leu Ser Arg Thr Thr Asn Ile Gln 115 120 125 Gly Ile Asn Leu Leu Phe Ser Ser Arg Arg Gly His Leu Phe Leu Gln 130 135 140 Thr Asp Gln Pro Ile Tyr Asn Pro Gly Gln Arg Val Arg Tyr Arg Val 145 150 155 160 Phe Ala Leu Asp Gln Lys Met Arg Pro Ser Thr Asp Thr Ile Thr Val 165 170 175 Met Val Glu Asn Ser His Gly Leu Arg Val Arg Lys Lys Glu Val Tyr 180 185 190 Met Pro Ser Ser Ile Phe Gln Asp Asp Phe Val Ile Pro Asp Ile Ser 195 200 205 Glu Pro Gly Thr Trp Lys Ile Ser Ala Arg Phe Ser Asp Gly Leu Glu 210 215 220 Ser Asn Ser Ser Thr Gln Phe Glu Val Lys Lys Tyr Val Leu Pro Asn 225 230 235 240 Phe Glu Val Lys Ile Thr Pro Gly Lys Pro Tyr Ile Leu Thr Val Pro 245 250 255 Gly His Leu Asp Glu Met Gln Leu Asp Ile Gln Ala Arg Tyr Ile Tyr 260 265 270 Gly Lys Pro Val Gln Gly Val Ala Tyr Val Arg Phe Gly Leu Leu Asp 275 280 285 Glu Asp Gly Lys Lys Thr Phe Phe Arg Gly Leu Glu Ser Gln Thr Lys 290 295 300 Leu Val Asn Gly Gln Ser His Ile Ser Leu Ser Lys Ala Glu Phe Gln 305 310 315 320 Asp Ala Leu Glu Lys Leu Asn Met Gly Ile Thr Asp Leu Gln Gly Leu 325 330 335 Arg Leu Tyr Val Ala Ala Ala Ile Ile Glu Ser Pro Gly Gly Glu Met 340 345 350 Glu Glu Ala Glu Leu Thr Ser Trp Tyr Phe Val Ser Ser Pro Phe Ser 355 360 365 Leu Asp Leu Ser Lys Thr Lys Arg His Leu Val Pro Gly Ala Pro Phe 370 375 380 Leu Leu Gln Ala Leu Val Arg Glu Met Ser Gly Ser Pro Ala Ser Gly 385 390 395 400 Ile Pro Val Lys Val Ser Ala Thr Val Ser Ser Pro Gly Ser Val Pro 405 410 415 Glu Val Gln Asp Ile Gln Gln Asn Thr Asp Gly Ser Gly Gln Val Ser 420 425 430 Ile Pro Ile Ile Ile Pro Gln Thr Ile Ser Glu Leu Gln Leu Ser Val 435 440 445 Ser Ala Gly Ser Pro His Pro Ala Ile Ala Arg Leu Thr Val Ala Ala 450 455 460 Pro Pro Ser Gly Gly Pro Gly Phe Leu Ser Ile Glu Arg Pro Asp Ser 465 470 475 480 Arg Pro Pro Arg Val Gly Asp Thr Leu Asn Leu Asn Leu Arg Ala Val 485 490 495 Gly Ser Gly Ala Thr Phe Ser His Tyr Tyr Tyr Met Ile Leu Ser Arg 500 505 510 Gly Gln Ile Val Phe Met Asn Arg Glu Pro Lys Arg Thr Leu Thr Ser 515 520 525 Val Ser Val Phe Val Asp His His Leu Ala Pro Ser Phe Tyr Phe Val 530 535 540 Ala Phe Tyr Tyr His Gly Asp His Pro Val Ala Asn Ser Leu Arg Val 545 550 555 560 Asp Val Gln Ala Gly Ala Cys Glu Gly Lys Leu Glu Leu Ser Val Asp 565 570 575 Gly Ala Lys Gln Tyr Arg Asn Gly Glu Ser Val Lys Leu His Leu Glu 580 585 590 Thr Asp Ser Leu Ala Leu Val Ala Leu Gly Ala Leu Asp Thr Ala Leu 595 600 605

Tyr Ala Ala Gly Ser Lys Ser His Lys Pro Leu Asn Met Gly Lys Val 610 615 620 Phe Glu Ala Met Asn Ser Tyr Asp Leu Gly Cys Gly Pro Gly Gly Gly 625 630 635 640 Asp Ser Ala Leu Gln Val Phe Gln Ala Ala Gly Leu Ala Phe Ser Asp 645 650 655 Gly Asp Gln Trp Thr Leu Ser Arg Lys Arg Leu Ser Cys Pro Lys Glu 660 665 670 Lys Thr Thr Arg Lys Lys Arg Asn Val Asn Phe Gln Lys Ala Ile Asn 675 680 685 Glu Lys Leu Gly Gln Tyr Ala Ser Pro Thr Ala Lys Arg Cys Cys Gln 690 695 700 Asp Gly Val Thr Arg Leu Pro Met Met Arg Ser Cys Glu Gln Arg Ala 705 710 715 720 Ala Arg Val Gln Gln Pro Asp Cys Arg Glu Pro Phe Leu Ser Cys Cys 725 730 735 Gln Phe Ala Glu Ser Leu Arg Lys Lys Ser Arg Asp Lys Gly Gln Ala 740 745 750 Gly Leu Gln Arg Ala Leu Glu Ile Leu Gln Glu Glu Asp Leu Ile Asp 755 760 765 Glu Asp Asp Ile Pro Val Arg Ser Phe Phe Pro Glu Asn Trp Leu Trp 770 775 780 Arg Val Glu Thr Val Asp Arg Phe Gln Ile Leu Thr Leu Trp Leu Pro 785 790 795 800 Asp Ser Leu Thr Thr Trp Glu Ile His Gly Leu Ser Leu Ser Lys Thr 805 810 815 Lys Gly Leu Cys Val Ala Thr Pro Val Gln Leu Arg Val Phe Arg Glu 820 825 830 Phe His Leu His Leu Arg Leu Pro Met Ser Val Arg Arg Phe Glu Gln 835 840 845 Leu Glu Leu Arg Pro Val Leu Tyr Asn Tyr Leu Asp Lys Asn Leu Thr 850 855 860 Val Ser Val His Val Ser Pro Val Glu Gly Leu Cys Leu Ala Gly Gly 865 870 875 880 Gly Gly Leu Ala Gln Gln Val Leu Val Pro Ala Gly Ser Ala Arg Pro 885 890 895 Val Ala Phe Ser Val Val Pro Thr Ala Ala Thr Ala Val Ser Leu Lys 900 905 910 Val Val Ala Arg Gly Ser Phe Glu Phe Pro Val Gly Asp Ala Val Ser 915 920 925 Lys Val Leu Gln Ile Glu Lys Glu Gly Ala Ile His Arg Glu Glu Leu 930 935 940 Val Tyr Glu Leu Asn Pro Leu Asp His Arg Gly Arg Thr Leu Glu Ile 945 950 955 960 Pro Gly Asn Ser Asp Pro Asn Met Ile Pro Asp Gly Asp Phe Asn Ser 965 970 975 Tyr Val Arg Val Thr Ala Ser Asp Pro Leu Asp Thr Leu Gly Ser Glu 980 985 990 Gly Ala Leu Ser Pro Gly Gly Val Ala Ser Leu Leu Arg Leu Pro Arg 995 1000 1005 Gly Cys Gly Glu Gln Thr Met Ile Tyr Leu Ala Pro Thr Leu Ala 1010 1015 1020 Ala Ser Arg Tyr Leu Asp Lys Thr Glu Gln Trp Ser Thr Leu Pro 1025 1030 1035 Pro Glu Thr Lys Asp His Ala Val Asp Leu Ile Gln Lys Gly Tyr 1040 1045 1050 Met Arg Ile Gln Gln Phe Arg Lys Ala Asp Gly Ser Tyr Ala Ala 1055 1060 1065 Trp Leu Ser Arg Gly Ser Ser Thr Trp Leu Thr Ala Phe Val Leu 1070 1075 1080 Lys Val Leu Ser Leu Ala Gln Glu Gln Val Gly Gly Ser Pro Glu 1085 1090 1095 Lys Leu Gln Glu Thr Ser Asn Trp Leu Leu Ser Gln Gln Gln Ala 1100 1105 1110 Asp Gly Ser Phe Gln Asp Leu Ser Pro Val Ile His Arg Ser Met 1115 1120 1125 Gln Gly Gly Leu Val Gly Asn Asp Glu Thr Val Ala Leu Thr Ala 1130 1135 1140 Phe Val Thr Ile Ala Leu His His Gly Leu Ala Val Phe Gln Asp 1145 1150 1155 Glu Gly Ala Glu Pro Leu Lys Gln Arg Val Glu Ala Ser Ile Ser 1160 1165 1170 Lys Ala Ser Ser Phe Leu Gly Glu Lys Ala Ser Ala Gly Leu Leu 1175 1180 1185 Gly Ala His Ala Ala Ala Ile Thr Ala Tyr Ala Leu Thr Leu Thr 1190 1195 1200 Lys Ala Pro Ala Asp Leu Arg Gly Val Ala His Asn Asn Leu Met 1205 1210 1215 Ala Met Ala Gln Glu Thr Gly Asp Asn Leu Tyr Trp Gly Ser Val 1220 1225 1230 Thr Gly Ser Gln Ser Asn Ala Val Ser Pro Thr Pro Ala Pro Arg 1235 1240 1245 Asn Pro Ser Asp Pro Met Pro Gln Ala Pro Ala Leu Trp Ile Glu 1250 1255 1260 Thr Thr Ala Tyr Ala Leu Leu His Leu Leu Leu His Glu Gly Lys 1265 1270 1275 Ala Glu Met Ala Asp Gln Ala Ala Ala Trp Leu Thr Arg Gln Gly 1280 1285 1290 Ser Phe Gln Gly Gly Phe Arg Ser Thr Gln Asp Thr Val Ile Ala 1295 1300 1305 Leu Asp Ala Leu Ser Ala Tyr Trp Ile Ala Ser His Thr Thr Glu 1310 1315 1320 Glu Arg Gly Leu Asn Val Thr Leu Ser Ser Thr Gly Arg Asn Gly 1325 1330 1335 Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg Gly 1340 1345 1350 Leu Glu Glu Glu Leu Gln Phe Ser Leu Gly Ser Lys Ile Asn Val 1355 1360 1365 Lys Val Gly Gly Asn Ser Lys Gly Thr Leu Lys Val Leu Arg Thr 1370 1375 1380 Tyr Asn Val Leu Asp Met Lys Asn Thr Thr Cys Gln Asp Leu Gln 1385 1390 1395 Ile Glu Val Thr Val Lys Gly His Val Glu Tyr Thr Met Glu Ala 1400 1405 1410 Asn Glu Asp Tyr Glu Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1415 1420 1425 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu 1430 1435 1440 Phe Glu Gly Arg Arg Asn Arg Arg Arg Arg Glu Ala Pro Lys Val 1445 1450 1455 Val Glu Glu Gln Glu Ser Arg Val His Tyr Thr Val Cys Ile Trp 1460 1465 1470 Arg Asn Gly Lys Val Gly Leu Ser Gly Met Ala Ile Ala Asp Val 1475 1480 1485 Thr Leu Leu Ser Gly Phe His Ala Leu Arg Ala Asp Leu Glu Lys 1490 1495 1500 Leu Thr Ser Leu Ser Asp Arg Tyr Val Ser His Phe Glu Thr Glu 1505 1510 1515 Gly Pro His Val Leu Leu Tyr Phe Asp Ser Val Pro Thr Ser Arg 1520 1525 1530 Glu Cys Val Gly Phe Glu Ala Val Gln Glu Val Pro Val Gly Leu 1535 1540 1545 Val Gln Pro Ala Ser Ala Thr Leu Tyr Asp Tyr Tyr Asn Pro Glu 1550 1555 1560 Arg Arg Cys Ser Val Phe Tyr Gly Ala Pro Ser Lys Ser Arg Leu 1565 1570 1575 Leu Ala Thr Leu Cys Ser Ala Glu Val Cys Gln Cys Ala Glu Gly 1580 1585 1590 Lys Cys Pro Arg Gln Arg Arg Ala Leu Glu Arg Gly Leu Gln Asp 1595 1600 1605 Glu Asp Gly Tyr Arg Met Lys Phe Ala Cys Tyr Tyr Pro Arg Val 1610 1615 1620 Glu Tyr Gly Phe Gln Val Lys Val Leu Arg Glu Asp Ser Arg Ala 1625 1630 1635 Ala Phe Arg Leu Phe Glu Thr Lys Ile Thr Gln Val Leu His Phe 1640 1645 1650 Thr Lys Asp Val Lys Ala Ala Ala Asn Gln Met Arg Asn Phe Leu 1655 1660 1665 Val Arg Ala Ser Cys Arg Leu Arg Leu Glu Pro Gly Lys Glu Tyr 1670 1675 1680 Leu Ile Met Gly Leu Asp Gly Ala Thr Tyr Asp Leu Glu Gly His 1685 1690 1695 Pro Gln Tyr Leu Leu Asp Ser Asn Ser Trp Ile Glu Glu Met Pro 1700 1705 1710 Ser Glu Arg Leu Cys Arg Ser Thr Arg Gln Arg Ala Ala Cys Ala 1715 1720 1725 Gln Leu Asn Asp Phe Leu Gln Glu Tyr Gly Thr Gln Gly Cys Gln 1730 1735 1740 Val <210> SEQ ID NO 6 <211> LENGTH: 559 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q13112 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(559) <400> SEQUENCE: 6 Met Lys Val Ile Thr Cys Glu Ile Ala Trp His Asn Lys Glu Pro Val 1 5 10 15 Tyr Ser Leu Asp Phe Gln His Gly Thr Ala Gly Arg Ile His Arg Leu 20 25 30 Ala Ser Ala Gly Val Asp Thr Asn Val Arg Ile Trp Lys Val Glu Lys 35 40 45 Gly Pro Asp Gly Lys Ala Ile Val Glu Phe Leu Ser Asn Leu Ala Arg 50 55 60 His Thr Lys Ala Val Asn Val Val Arg Phe Ser Pro Thr Gly Glu Ile 65 70 75 80

Leu Ala Ser Gly Gly Asp Asp Ala Val Ile Leu Leu Trp Lys Val Asn 85 90 95 Asp Asn Lys Glu Pro Glu Gln Ile Ala Phe Gln Asp Glu Asp Glu Ala 100 105 110 Gln Leu Asn Lys Glu Asn Trp Thr Val Val Lys Thr Leu Arg Gly His 115 120 125 Leu Glu Asp Val Tyr Asp Ile Cys Trp Ala Thr Asp Gly Asn Leu Met 130 135 140 Ala Ser Ala Ser Val Asp Asn Thr Ala Ile Ile Trp Asp Val Ser Lys 145 150 155 160 Gly Gln Lys Ile Ser Ile Phe Asn Glu His Lys Ser Tyr Val Gln Gly 165 170 175 Val Thr Trp Asp Pro Leu Gly Gln Tyr Val Ala Thr Leu Ser Cys Asp 180 185 190 Arg Val Leu Arg Val Tyr Ser Ile Gln Lys Lys Arg Val Ala Phe Asn 195 200 205 Val Ser Lys Met Leu Ser Gly Ile Gly Ala Glu Gly Glu Ala Arg Ser 210 215 220 Tyr Arg Met Phe His Asp Asp Ser Met Lys Ser Phe Phe Arg Arg Leu 225 230 235 240 Ser Phe Thr Pro Asp Gly Ser Leu Leu Leu Thr Pro Ala Gly Cys Val 245 250 255 Glu Ser Gly Glu Asn Val Met Asn Thr Thr Tyr Val Phe Ser Arg Lys 260 265 270 Asn Leu Lys Arg Pro Ile Ala His Leu Pro Cys Pro Gly Lys Ala Thr 275 280 285 Leu Ala Val Arg Cys Cys Pro Val Tyr Phe Glu Leu Arg Pro Val Val 290 295 300 Glu Thr Gly Val Glu Leu Met Ser Leu Pro Tyr Arg Leu Val Phe Ala 305 310 315 320 Val Ala Ser Glu Asp Ser Val Leu Leu Tyr Asp Thr Gln Gln Ser Phe 325 330 335 Pro Phe Gly Tyr Val Ser Asn Ile His Tyr His Thr Leu Ser Asp Ile 340 345 350 Ser Trp Ser Ser Asp Gly Ala Phe Leu Ala Ile Ser Ser Thr Asp Gly 355 360 365 Tyr Cys Ser Phe Val Thr Phe Glu Lys Asp Glu Leu Gly Ile Pro Leu 370 375 380 Lys Glu Lys Pro Val Leu Asn Met Arg Thr Pro Asp Thr Ala Lys Lys 385 390 395 400 Thr Lys Ser Gln Thr His Arg Gly Ser Ser Pro Gly Pro Arg Pro Val 405 410 415 Glu Gly Thr Pro Ala Ser Arg Thr Gln Asp Pro Ser Ser Pro Gly Thr 420 425 430 Thr Pro Pro Gln Ala Arg Gln Ala Pro Ala Pro Thr Val Ile Arg Asp 435 440 445 Pro Pro Ser Ile Thr Pro Ala Val Lys Ser Pro Leu Pro Gly Pro Ser 450 455 460 Glu Glu Lys Thr Leu Gln Pro Ser Ser Gln Asn Thr Lys Ala His Pro 465 470 475 480 Ser Arg Arg Val Thr Leu Asn Thr Leu Gln Ala Trp Ser Lys Thr Thr 485 490 495 Pro Arg Arg Ile Asn Leu Thr Pro Leu Lys Thr Asp Thr Pro Pro Ser 500 505 510 Ser Val Pro Thr Ser Val Ile Ser Thr Pro Ser Thr Glu Glu Ile Gln 515 520 525 Ser Glu Thr Pro Gly Asp Ala Gln Gly Ser Pro Pro Glu Leu Lys Arg 530 535 540 Pro Arg Leu Asp Glu Asn Lys Gly Gly Thr Glu Ser Leu Asp Pro 545 550 555 <210> SEQ ID NO 7 <211> LENGTH: 94 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O14625 <309> DATABASE ENTRY DATE: 2015-06-24 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(94) <400> SEQUENCE: 7 Met Ser Val Lys Gly Met Ala Ile Ala Leu Ala Val Ile Leu Cys Ala 1 5 10 15 Thr Val Val Gln Gly Phe Pro Met Phe Lys Arg Gly Arg Cys Leu Cys 20 25 30 Ile Gly Pro Gly Val Lys Ala Val Lys Val Ala Asp Ile Glu Lys Ala 35 40 45 Ser Ile Met Tyr Pro Ser Asn Asn Cys Asp Lys Ile Glu Val Ile Ile 50 55 60 Thr Leu Lys Glu Asn Lys Gly Gln Arg Cys Leu Asn Pro Lys Ser Lys 65 70 75 80 Gln Ala Arg Leu Ile Ile Lys Lys Val Glu Arg Lys Asn Phe 85 90 <210> SEQ ID NO 8 <211> LENGTH: 125 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q07325 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(125) <400> SEQUENCE: 8 Met Lys Lys Ser Gly Val Leu Phe Leu Leu Gly Ile Ile Leu Leu Val 1 5 10 15 Leu Ile Gly Val Gln Gly Thr Pro Val Val Arg Lys Gly Arg Cys Ser 20 25 30 Cys Ile Ser Thr Asn Gln Gly Thr Ile His Leu Gln Ser Leu Lys Asp 35 40 45 Leu Lys Gln Phe Ala Pro Ser Pro Ser Cys Glu Lys Ile Glu Ile Ile 50 55 60 Ala Thr Leu Lys Asn Gly Val Gln Thr Cys Leu Asn Pro Asp Ser Ala 65 70 75 80 Asp Val Lys Glu Leu Ile Lys Lys Trp Glu Lys Gln Val Ser Gln Lys 85 90 95 Lys Lys Gln Lys Asn Gly Lys Lys His Gln Lys Lys Lys Val Leu Lys 100 105 110 Val Arg Lys Ser Gln Arg Ser Arg Gln Lys Lys Thr Thr 115 120 125 <210> SEQ ID NO 9 <211> LENGTH: 165 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P62937 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(165) <400> SEQUENCE: 9 Met Val Asn Pro Thr Val Phe Phe Asp Ile Ala Val Asp Gly Glu Pro 1 5 10 15 Leu Gly Arg Val Ser Phe Glu Leu Phe Ala Asp Lys Val Pro Lys Thr 20 25 30 Ala Glu Asn Phe Arg Ala Leu Ser Thr Gly Glu Lys Gly Phe Gly Tyr 35 40 45 Lys Gly Ser Cys Phe His Arg Ile Ile Pro Gly Phe Met Cys Gln Gly 50 55 60 Gly Asp Phe Thr Arg His Asn Gly Thr Gly Gly Lys Ser Ile Tyr Gly 65 70 75 80 Glu Lys Phe Glu Asp Glu Asn Phe Ile Leu Lys His Thr Gly Pro Gly 85 90 95 Ile Leu Ser Met Ala Asn Ala Gly Pro Asn Thr Asn Gly Ser Gln Phe 100 105 110 Phe Ile Cys Thr Ala Lys Thr Glu Trp Leu Asp Gly Lys His Val Val 115 120 125 Phe Gly Lys Val Lys Glu Gly Met Asn Ile Val Glu Ala Met Glu Arg 130 135 140 Phe Gly Ser Arg Asn Gly Lys Thr Ser Lys Lys Ile Thr Ile Ala Asp 145 150 155 160 Cys Gly Gln Leu Glu 165 <210> SEQ ID NO 10 <211> LENGTH: 585 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BY44 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(585) <400> SEQUENCE: 10 Met Ala Pro Ser Thr Pro Leu Leu Thr Val Arg Gly Ser Glu Gly Leu 1 5 10 15 Tyr Met Val Asn Gly Pro Pro His Phe Thr Glu Ser Thr Val Phe Pro 20 25 30 Arg Glu Ser Gly Lys Asn Cys Lys Val Cys Ile Phe Ser Lys Asp Gly 35 40 45 Thr Leu Phe Ala Trp Gly Asn Gly Glu Lys Val Asn Ile Ile Ser Val 50 55 60 Thr Asn Lys Gly Leu Leu His Ser Phe Asp Leu Leu Lys Ala Val Cys 65 70 75 80 Leu Glu Phe Ser Pro Lys Asn Thr Val Leu Ala Thr Trp Gln Pro Tyr 85 90 95 Thr Thr Ser Lys Asp Gly Thr Ala Gly Ile Pro Asn Leu Gln Leu Tyr 100 105 110 Asp Val Lys Thr Gly Thr Cys Leu Lys Ser Phe Ile Gln Lys Lys Met 115 120 125 Gln Asn Trp Cys Pro Ser Trp Ser Glu Asp Glu Thr Leu Cys Ala Arg 130 135 140 Asn Val Asn Asn Glu Val His Phe Phe Glu Asn Asn Asn Phe Asn Thr 145 150 155 160 Ile Ala Asn Lys Leu His Leu Gln Lys Ile Asn Asp Phe Val Leu Ser 165 170 175 Pro Gly Pro Gln Pro Tyr Lys Val Ala Val Tyr Val Pro Gly Ser Lys 180 185 190 Gly Ala Pro Ser Phe Val Arg Leu Tyr Gln Tyr Pro Asn Phe Ala Gly 195 200 205

Pro His Ala Ala Leu Ala Asn Lys Ser Phe Phe Lys Ala Asp Lys Val 210 215 220 Thr Met Leu Trp Asn Lys Lys Ala Thr Ala Val Leu Val Ile Ala Ser 225 230 235 240 Thr Asp Val Asp Lys Thr Gly Ala Ser Tyr Tyr Gly Glu Gln Thr Leu 245 250 255 His Tyr Ile Ala Thr Asn Gly Glu Ser Ala Val Val Gln Leu Pro Lys 260 265 270 Asn Gly Pro Ile Tyr Asp Val Val Trp Asn Ser Ser Ser Thr Glu Phe 275 280 285 Cys Ala Val Tyr Gly Phe Met Pro Ala Lys Ala Thr Ile Phe Asn Leu 290 295 300 Lys Cys Asp Pro Val Phe Asp Phe Gly Thr Gly Pro Arg Asn Ala Ala 305 310 315 320 Tyr Tyr Ser Pro His Gly His Ile Leu Val Leu Ala Gly Phe Gly Asn 325 330 335 Leu Arg Gly Gln Met Glu Val Trp Asp Val Lys Asn Tyr Lys Leu Ile 340 345 350 Ser Lys Pro Val Ala Ser Asp Ser Thr Tyr Phe Ala Trp Cys Pro Asp 355 360 365 Gly Glu His Ile Leu Thr Ala Thr Cys Ala Pro Arg Leu Arg Val Asn 370 375 380 Asn Gly Tyr Lys Ile Trp His Tyr Thr Gly Ser Ile Leu His Lys Tyr 385 390 395 400 Asp Val Pro Ser Asn Ala Glu Leu Trp Gln Val Ser Trp Gln Pro Phe 405 410 415 Leu Asp Gly Ile Phe Pro Ala Lys Thr Ile Thr Tyr Gln Ala Val Pro 420 425 430 Ser Glu Val Pro Asn Glu Glu Pro Lys Val Ala Thr Ala Tyr Arg Pro 435 440 445 Pro Ala Leu Arg Asn Lys Pro Ile Thr Asn Ser Lys Leu His Glu Glu 450 455 460 Glu Pro Pro Gln Asn Met Lys Pro Gln Ser Gly Asn Asp Lys Pro Leu 465 470 475 480 Ser Lys Thr Ala Leu Lys Asn Gln Arg Lys His Glu Ala Lys Lys Ala 485 490 495 Ala Lys Gln Glu Ala Arg Ser Asp Lys Ser Pro Asp Leu Ala Pro Thr 500 505 510 Pro Ala Pro Gln Ser Thr Pro Arg Asn Thr Val Ser Gln Ser Ile Ser 515 520 525 Gly Asp Pro Glu Ile Asp Lys Lys Ile Lys Asn Leu Lys Lys Lys Leu 530 535 540 Lys Ala Ile Glu Gln Leu Lys Glu Gln Ala Ala Thr Gly Lys Gln Leu 545 550 555 560 Glu Lys Asn Gln Leu Glu Lys Ile Gln Lys Glu Thr Ala Leu Leu Gln 565 570 575 Glu Leu Glu Asp Leu Glu Leu Gly Ile 580 585 <210> SEQ ID NO 11 <211> LENGTH: 434 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P06733 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(434) <400> SEQUENCE: 11 Met Ser Ile Leu Lys Ile His Ala Arg Glu Ile Phe Asp Ser Arg Gly 1 5 10 15 Asn Pro Thr Val Glu Val Asp Leu Phe Thr Ser Lys Gly Leu Phe Arg 20 25 30 Ala Ala Val Pro Ser Gly Ala Ser Thr Gly Ile Tyr Glu Ala Leu Glu 35 40 45 Leu Arg Asp Asn Asp Lys Thr Arg Tyr Met Gly Lys Gly Val Ser Lys 50 55 60 Ala Val Glu His Ile Asn Lys Thr Ile Ala Pro Ala Leu Val Ser Lys 65 70 75 80 Lys Leu Asn Val Thr Glu Gln Glu Lys Ile Asp Lys Leu Met Ile Glu 85 90 95 Met Asp Gly Thr Glu Asn Lys Ser Lys Phe Gly Ala Asn Ala Ile Leu 100 105 110 Gly Val Ser Leu Ala Val Cys Lys Ala Gly Ala Val Glu Lys Gly Val 115 120 125 Pro Leu Tyr Arg His Ile Ala Asp Leu Ala Gly Asn Ser Glu Val Ile 130 135 140 Leu Pro Val Pro Ala Phe Asn Val Ile Asn Gly Gly Ser His Ala Gly 145 150 155 160 Asn Lys Leu Ala Met Gln Glu Phe Met Ile Leu Pro Val Gly Ala Ala 165 170 175 Asn Phe Arg Glu Ala Met Arg Ile Gly Ala Glu Val Tyr His Asn Leu 180 185 190 Lys Asn Val Ile Lys Glu Lys Tyr Gly Lys Asp Ala Thr Asn Val Gly 195 200 205 Asp Glu Gly Gly Phe Ala Pro Asn Ile Leu Glu Asn Lys Glu Gly Leu 210 215 220 Glu Leu Leu Lys Thr Ala Ile Gly Lys Ala Gly Tyr Thr Asp Lys Val 225 230 235 240 Val Ile Gly Met Asp Val Ala Ala Ser Glu Phe Phe Arg Ser Gly Lys 245 250 255 Tyr Asp Leu Asp Phe Lys Ser Pro Asp Asp Pro Ser Arg Tyr Ile Ser 260 265 270 Pro Asp Gln Leu Ala Asp Leu Tyr Lys Ser Phe Ile Lys Asp Tyr Pro 275 280 285 Val Val Ser Ile Glu Asp Pro Phe Asp Gln Asp Asp Trp Gly Ala Trp 290 295 300 Gln Lys Phe Thr Ala Ser Ala Gly Ile Gln Val Val Gly Asp Asp Leu 305 310 315 320 Thr Val Thr Asn Pro Lys Arg Ile Ala Lys Ala Val Asn Glu Lys Ser 325 330 335 Cys Asn Cys Leu Leu Leu Lys Val Asn Gln Ile Gly Ser Val Thr Glu 340 345 350 Ser Leu Gln Ala Cys Lys Leu Ala Gln Ala Asn Gly Trp Gly Val Met 355 360 365 Val Ser His Arg Ser Gly Glu Thr Glu Asp Thr Phe Ile Ala Asp Leu 370 375 380 Val Val Gly Leu Cys Thr Gly Gln Ile Lys Thr Gly Ala Pro Cys Arg 385 390 395 400 Ser Glu Arg Leu Ala Lys Tyr Asn Gln Leu Leu Arg Ile Glu Glu Glu 405 410 415 Leu Gly Ser Lys Ala Lys Phe Ala Gly Arg Asn Phe Arg Asn Pro Leu 420 425 430 Ala Lys <210> SEQ ID NO 12 <211> LENGTH: 585 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q05329 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(585) <400> SEQUENCE: 12 Met Ala Ser Pro Gly Ser Gly Phe Trp Ser Phe Gly Ser Glu Asp Gly 1 5 10 15 Ser Gly Asp Ser Glu Asn Pro Gly Thr Ala Arg Ala Trp Cys Gln Val 20 25 30 Ala Gln Lys Phe Thr Gly Gly Ile Gly Asn Lys Leu Cys Ala Leu Leu 35 40 45 Tyr Gly Asp Ala Glu Lys Pro Ala Glu Ser Gly Gly Ser Gln Pro Pro 50 55 60 Arg Ala Ala Ala Arg Lys Ala Ala Cys Ala Cys Asp Gln Lys Pro Cys 65 70 75 80 Ser Cys Ser Lys Val Asp Val Asn Tyr Ala Phe Leu His Ala Thr Asp 85 90 95 Leu Leu Pro Ala Cys Asp Gly Glu Arg Pro Thr Leu Ala Phe Leu Gln 100 105 110 Asp Val Met Asn Ile Leu Leu Gln Tyr Val Val Lys Ser Phe Asp Arg 115 120 125 Ser Thr Lys Val Ile Asp Phe His Tyr Pro Asn Glu Leu Leu Gln Glu 130 135 140 Tyr Asn Trp Glu Leu Ala Asp Gln Pro Gln Asn Leu Glu Glu Ile Leu 145 150 155 160 Met His Cys Gln Thr Thr Leu Lys Tyr Ala Ile Lys Thr Gly His Pro 165 170 175 Arg Tyr Phe Asn Gln Leu Ser Thr Gly Leu Asp Met Val Gly Leu Ala 180 185 190 Ala Asp Trp Leu Thr Ser Thr Ala Asn Thr Asn Met Phe Thr Tyr Glu 195 200 205 Ile Ala Pro Val Phe Val Leu Leu Glu Tyr Val Thr Leu Lys Lys Met 210 215 220 Arg Glu Ile Ile Gly Trp Pro Gly Gly Ser Gly Asp Gly Ile Phe Ser 225 230 235 240 Pro Gly Gly Ala Ile Ser Asn Met Tyr Ala Met Met Ile Ala Arg Phe 245 250 255 Lys Met Phe Pro Glu Val Lys Glu Lys Gly Met Ala Ala Leu Pro Arg 260 265 270 Leu Ile Ala Phe Thr Ser Glu His Ser His Phe Ser Leu Lys Lys Gly 275 280 285 Ala Ala Ala Leu Gly Ile Gly Thr Asp Ser Val Ile Leu Ile Lys Cys 290 295 300 Asp Glu Arg Gly Lys Met Ile Pro Ser Asp Leu Glu Arg Arg Ile Leu 305 310 315 320 Glu Ala Lys Gln Lys Gly Phe Val Pro Phe Leu Val Ser Ala Thr Ala 325 330 335 Gly Thr Thr Val Tyr Gly Ala Phe Asp Pro Leu Leu Ala Val Ala Asp 340 345 350 Ile Cys Lys Lys Tyr Lys Ile Trp Met His Val Asp Ala Ala Trp Gly 355 360 365 Gly Gly Leu Leu Met Ser Arg Lys His Lys Trp Lys Leu Ser Gly Val 370 375 380

Glu Arg Ala Asn Ser Val Thr Trp Asn Pro His Lys Met Met Gly Val 385 390 395 400 Pro Leu Gln Cys Ser Ala Leu Leu Val Arg Glu Glu Gly Leu Met Gln 405 410 415 Asn Cys Asn Gln Met His Ala Ser Tyr Leu Phe Gln Gln Asp Lys His 420 425 430 Tyr Asp Leu Ser Tyr Asp Thr Gly Asp Lys Ala Leu Gln Cys Gly Arg 435 440 445 His Val Asp Val Phe Lys Leu Trp Leu Met Trp Arg Ala Lys Gly Thr 450 455 460 Thr Gly Phe Glu Ala His Val Asp Lys Cys Leu Glu Leu Ala Glu Tyr 465 470 475 480 Leu Tyr Asn Ile Ile Lys Asn Arg Glu Gly Tyr Glu Met Val Phe Asp 485 490 495 Gly Lys Pro Gln His Thr Asn Val Cys Phe Trp Tyr Ile Pro Pro Ser 500 505 510 Leu Arg Thr Leu Glu Asp Asn Glu Glu Arg Met Ser Arg Leu Ser Lys 515 520 525 Val Ala Pro Val Ile Lys Ala Arg Met Met Glu Tyr Gly Thr Thr Met 530 535 540 Val Ser Tyr Gln Pro Leu Gly Asp Lys Val Asn Phe Phe Arg Met Val 545 550 555 560 Ile Ser Asn Pro Ala Ala Thr His Gln Asp Ile Asp Phe Leu Ile Glu 565 570 575 Glu Ile Glu Arg Leu Gly Gln Asp Leu 580 585 <210> SEQ ID NO 13 <211> LENGTH: 211 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P39905 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(211) <400> SEQUENCE: 13 Met Lys Leu Trp Asp Val Val Ala Val Cys Leu Val Leu Leu His Thr 1 5 10 15 Ala Ser Ala Phe Pro Leu Pro Ala Gly Lys Arg Pro Pro Glu Ala Pro 20 25 30 Ala Glu Asp Arg Ser Leu Gly Arg Arg Arg Ala Pro Phe Ala Leu Ser 35 40 45 Ser Asp Ser Asn Met Pro Glu Asp Tyr Pro Asp Gln Phe Asp Asp Val 50 55 60 Met Asp Phe Ile Gln Ala Thr Ile Lys Arg Leu Lys Arg Ser Pro Asp 65 70 75 80 Lys Gln Met Ala Val Leu Pro Arg Arg Glu Arg Asn Arg Gln Ala Ala 85 90 95 Ala Ala Asn Pro Glu Asn Ser Arg Gly Lys Gly Arg Arg Gly Gln Arg 100 105 110 Gly Lys Asn Arg Gly Cys Val Leu Thr Ala Ile His Leu Asn Val Thr 115 120 125 Asp Leu Gly Leu Gly Tyr Glu Thr Lys Glu Glu Leu Ile Phe Arg Tyr 130 135 140 Cys Ser Gly Ser Cys Asp Ala Ala Glu Thr Thr Tyr Asp Lys Ile Leu 145 150 155 160 Lys Asn Leu Ser Arg Asn Arg Arg Leu Val Ser Asp Lys Val Gly Gln 165 170 175 Ala Cys Cys Arg Pro Ile Ala Phe Asp Asp Asp Leu Ser Phe Leu Asp 180 185 190 Asp Asn Leu Val Tyr His Ile Leu Arg Lys His Ser Ala Lys Arg Cys 195 200 205 Gly Cys Ile 210 <210> SEQ ID NO 14 <211> LENGTH: 463 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P61978 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(463) <400> SEQUENCE: 14 Met Glu Thr Glu Gln Pro Glu Glu Thr Phe Pro Asn Thr Glu Thr Asn 1 5 10 15 Gly Glu Phe Gly Lys Arg Pro Ala Glu Asp Met Glu Glu Glu Gln Ala 20 25 30 Phe Lys Arg Ser Arg Asn Thr Asp Glu Met Val Glu Leu Arg Ile Leu 35 40 45 Leu Gln Ser Lys Asn Ala Gly Ala Val Ile Gly Lys Gly Gly Lys Asn 50 55 60 Ile Lys Ala Leu Arg Thr Asp Tyr Asn Ala Ser Val Ser Val Pro Asp 65 70 75 80 Ser Ser Gly Pro Glu Arg Ile Leu Ser Ile Ser Ala Asp Ile Glu Thr 85 90 95 Ile Gly Glu Ile Leu Lys Lys Ile Ile Pro Thr Leu Glu Glu Gly Leu 100 105 110 Gln Leu Pro Ser Pro Thr Ala Thr Ser Gln Leu Pro Leu Glu Ser Asp 115 120 125 Ala Val Glu Cys Leu Asn Tyr Gln His Tyr Lys Gly Ser Asp Phe Asp 130 135 140 Cys Glu Leu Arg Leu Leu Ile His Gln Ser Leu Ala Gly Gly Ile Ile 145 150 155 160 Gly Val Lys Gly Ala Lys Ile Lys Glu Leu Arg Glu Asn Thr Gln Thr 165 170 175 Thr Ile Lys Leu Phe Gln Glu Cys Cys Pro His Ser Thr Asp Arg Val 180 185 190 Val Leu Ile Gly Gly Lys Pro Asp Arg Val Val Glu Cys Ile Lys Ile 195 200 205 Ile Leu Asp Leu Ile Ser Glu Ser Pro Ile Lys Gly Arg Ala Gln Pro 210 215 220 Tyr Asp Pro Asn Phe Tyr Asp Glu Thr Tyr Asp Tyr Gly Gly Phe Thr 225 230 235 240 Met Met Phe Asp Asp Arg Arg Gly Arg Pro Val Gly Phe Pro Met Arg 245 250 255 Gly Arg Gly Gly Phe Asp Arg Met Pro Pro Gly Arg Gly Gly Arg Pro 260 265 270 Met Pro Pro Ser Arg Arg Asp Tyr Asp Asp Met Ser Pro Arg Arg Gly 275 280 285 Pro Pro Pro Pro Pro Pro Gly Arg Gly Gly Arg Gly Gly Ser Arg Ala 290 295 300 Arg Asn Leu Pro Leu Pro Pro Pro Pro Pro Pro Arg Gly Gly Asp Leu 305 310 315 320 Met Ala Tyr Asp Arg Arg Gly Arg Pro Gly Asp Arg Tyr Asp Gly Met 325 330 335 Val Gly Phe Ser Ala Asp Glu Thr Trp Asp Ser Ala Ile Asp Thr Trp 340 345 350 Ser Pro Ser Glu Trp Gln Met Ala Tyr Glu Pro Gln Gly Gly Ser Gly 355 360 365 Tyr Asp Tyr Ser Tyr Ala Gly Gly Arg Gly Ser Tyr Gly Asp Leu Gly 370 375 380 Gly Pro Ile Ile Thr Thr Gln Val Thr Ile Pro Lys Asp Leu Ala Gly 385 390 395 400 Ser Ile Ile Gly Lys Gly Gly Gln Arg Ile Lys Gln Ile Arg His Glu 405 410 415 Ser Gly Ala Ser Ile Lys Ile Asp Glu Pro Leu Glu Gly Ser Glu Asp 420 425 430 Arg Ile Ile Thr Ile Thr Gly Thr Gln Asp Gln Ile Gln Asn Ala Gln 435 440 445 Tyr Leu Leu Gln Asn Ser Val Lys Gln Tyr Ser Gly Lys Phe Phe 450 455 460 <210> SEQ ID NO 15 <211> LENGTH: 532 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P05362 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(532) <400> SEQUENCE: 15 Met Ala Pro Ser Ser Pro Arg Pro Ala Leu Pro Ala Leu Leu Val Leu 1 5 10 15 Leu Gly Ala Leu Phe Pro Gly Pro Gly Asn Ala Gln Thr Ser Val Ser 20 25 30 Pro Ser Lys Val Ile Leu Pro Arg Gly Gly Ser Val Leu Val Thr Cys 35 40 45 Ser Thr Ser Cys Asp Gln Pro Lys Leu Leu Gly Ile Glu Thr Pro Leu 50 55 60 Pro Lys Lys Glu Leu Leu Leu Pro Gly Asn Asn Arg Lys Val Tyr Glu 65 70 75 80 Leu Ser Asn Val Gln Glu Asp Ser Gln Pro Met Cys Tyr Ser Asn Cys 85 90 95 Pro Asp Gly Gln Ser Thr Ala Lys Thr Phe Leu Thr Val Tyr Trp Thr 100 105 110 Pro Glu Arg Val Glu Leu Ala Pro Leu Pro Ser Trp Gln Pro Val Gly 115 120 125 Lys Asn Leu Thr Leu Arg Cys Gln Val Glu Gly Gly Ala Pro Arg Ala 130 135 140 Asn Leu Thr Val Val Leu Leu Arg Gly Glu Lys Glu Leu Lys Arg Glu 145 150 155 160 Pro Ala Val Gly Glu Pro Ala Glu Val Thr Thr Thr Val Leu Val Arg 165 170 175 Arg Asp His His Gly Ala Asn Phe Ser Cys Arg Thr Glu Leu Asp Leu 180 185 190 Arg Pro Gln Gly Leu Glu Leu Phe Glu Asn Thr Ser Ala Pro Tyr Gln 195 200 205 Leu Gln Thr Phe Val Leu Pro Ala Thr Pro Pro Gln Leu Val Ser Pro 210 215 220 Arg Val Leu Glu Val Asp Thr Gln Gly Thr Val Val Cys Ser Leu Asp 225 230 235 240 Gly Leu Phe Pro Val Ser Glu Ala Gln Val His Leu Ala Leu Gly Asp

245 250 255 Gln Arg Leu Asn Pro Thr Val Thr Tyr Gly Asn Asp Ser Phe Ser Ala 260 265 270 Lys Ala Ser Val Ser Val Thr Ala Glu Asp Glu Gly Thr Gln Arg Leu 275 280 285 Thr Cys Ala Val Ile Leu Gly Asn Gln Ser Gln Glu Thr Leu Gln Thr 290 295 300 Val Thr Ile Tyr Ser Phe Pro Ala Pro Asn Val Ile Leu Thr Lys Pro 305 310 315 320 Glu Val Ser Glu Gly Thr Glu Val Thr Val Lys Cys Glu Ala His Pro 325 330 335 Arg Ala Lys Val Thr Leu Asn Gly Val Pro Ala Gln Pro Leu Gly Pro 340 345 350 Arg Ala Gln Leu Leu Leu Lys Ala Thr Pro Glu Asp Asn Gly Arg Ser 355 360 365 Phe Ser Cys Ser Ala Thr Leu Glu Val Ala Gly Gln Leu Ile His Lys 370 375 380 Asn Gln Thr Arg Glu Leu Arg Val Leu Tyr Gly Pro Arg Leu Asp Glu 385 390 395 400 Arg Asp Cys Pro Gly Asn Trp Thr Trp Pro Glu Asn Ser Gln Gln Thr 405 410 415 Pro Met Cys Gln Ala Trp Gly Asn Pro Leu Pro Glu Leu Lys Cys Leu 420 425 430 Lys Asp Gly Thr Phe Pro Leu Pro Ile Gly Glu Ser Val Thr Val Thr 435 440 445 Arg Asp Leu Glu Gly Thr Tyr Leu Cys Arg Ala Arg Ser Thr Gln Gly 450 455 460 Glu Val Thr Arg Lys Val Thr Val Asn Val Leu Ser Pro Arg Tyr Glu 465 470 475 480 Ile Val Ile Ile Thr Val Val Ala Ala Ala Val Ile Met Gly Thr Ala 485 490 495 Gly Leu Ser Thr Tyr Leu Tyr Asn Arg Gln Arg Lys Ile Lys Lys Tyr 500 505 510 Arg Leu Gln Gln Ala Gln Lys Gly Thr Pro Met Lys Pro Asn Thr Gln 515 520 525 Ala Thr Pro Pro 530 <210> SEQ ID NO 16 <211> LENGTH: 785 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q16666 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(785) <400> SEQUENCE: 16 Met Gly Lys Lys Tyr Lys Asn Ile Val Leu Leu Lys Gly Leu Glu Val 1 5 10 15 Ile Asn Asp Tyr His Phe Arg Met Val Lys Ser Leu Leu Ser Asn Asp 20 25 30 Leu Lys Leu Asn Leu Lys Met Arg Glu Glu Tyr Asp Lys Ile Gln Ile 35 40 45 Ala Asp Leu Met Glu Glu Lys Phe Arg Gly Asp Ala Gly Leu Gly Lys 50 55 60 Leu Ile Lys Ile Phe Glu Asp Ile Pro Thr Leu Glu Asp Leu Ala Glu 65 70 75 80 Thr Leu Lys Lys Glu Lys Leu Lys Val Lys Gly Pro Ala Leu Ser Arg 85 90 95 Lys Arg Lys Lys Glu Val Asp Ala Thr Ser Pro Ala Pro Ser Thr Ser 100 105 110 Ser Thr Val Lys Thr Glu Gly Ala Glu Ala Thr Pro Gly Ala Gln Lys 115 120 125 Arg Lys Lys Ser Thr Lys Glu Lys Ala Gly Pro Lys Gly Ser Lys Val 130 135 140 Ser Glu Glu Gln Thr Gln Pro Pro Ser Pro Ala Gly Ala Gly Met Ser 145 150 155 160 Thr Ala Met Gly Arg Ser Pro Ser Pro Lys Thr Ser Leu Ser Ala Pro 165 170 175 Pro Asn Ser Ser Ser Thr Glu Asn Pro Lys Thr Val Ala Lys Cys Gln 180 185 190 Val Thr Pro Arg Arg Asn Val Leu Gln Lys Arg Pro Val Ile Val Lys 195 200 205 Val Leu Ser Thr Thr Lys Pro Phe Glu Tyr Glu Thr Pro Glu Met Glu 210 215 220 Lys Lys Ile Met Phe His Ala Thr Val Ala Thr Gln Thr Gln Phe Phe 225 230 235 240 His Val Lys Val Leu Asn Thr Ser Leu Lys Glu Lys Phe Asn Gly Lys 245 250 255 Lys Ile Ile Ile Ile Ser Asp Tyr Leu Glu Tyr Asp Ser Leu Leu Glu 260 265 270 Val Asn Glu Glu Ser Thr Val Ser Glu Ala Gly Pro Asn Gln Thr Phe 275 280 285 Glu Val Pro Asn Lys Ile Ile Asn Arg Ala Lys Glu Thr Leu Lys Ile 290 295 300 Asp Ile Leu His Lys Gln Ala Ser Gly Asn Ile Val Tyr Gly Val Phe 305 310 315 320 Met Leu His Lys Lys Thr Val Asn Gln Lys Thr Thr Ile Tyr Glu Ile 325 330 335 Gln Asp Asp Arg Gly Lys Met Asp Val Val Gly Thr Gly Gln Cys His 340 345 350 Asn Ile Pro Cys Glu Glu Gly Asp Lys Leu Gln Leu Phe Cys Phe Arg 355 360 365 Leu Arg Lys Lys Asn Gln Met Ser Lys Leu Ile Ser Glu Met His Ser 370 375 380 Phe Ile Gln Ile Lys Lys Lys Thr Asn Pro Arg Asn Asn Asp Pro Lys 385 390 395 400 Ser Met Lys Leu Pro Gln Glu Gln Arg Gln Leu Pro Tyr Pro Ser Glu 405 410 415 Ala Ser Thr Thr Phe Pro Glu Ser His Leu Arg Thr Pro Gln Met Pro 420 425 430 Pro Thr Thr Pro Ser Ser Ser Phe Phe Thr Lys Lys Ser Glu Asp Thr 435 440 445 Ile Ser Lys Met Asn Asp Phe Met Arg Met Gln Ile Leu Lys Glu Gly 450 455 460 Ser His Phe Pro Gly Pro Phe Met Thr Ser Ile Gly Pro Ala Glu Ser 465 470 475 480 His Pro His Thr Pro Gln Met Pro Pro Ser Thr Pro Ser Ser Ser Phe 485 490 495 Leu Thr Thr Lys Ser Glu Asp Thr Ile Ser Lys Met Asn Asp Phe Met 500 505 510 Arg Met Gln Ile Leu Lys Glu Gly Ser His Phe Pro Gly Pro Phe Met 515 520 525 Thr Ser Ile Gly Pro Ala Glu Ser His Pro His Thr Pro Gln Met Pro 530 535 540 Pro Ser Thr Pro Ser Ser Ser Phe Leu Thr Thr Leu Lys Pro Arg Leu 545 550 555 560 Lys Thr Glu Pro Glu Glu Val Ser Ile Glu Asp Ser Ala Gln Ser Asp 565 570 575 Leu Lys Glu Val Met Val Leu Asn Ala Thr Glu Ser Phe Val Tyr Glu 580 585 590 Pro Lys Glu Gln Lys Lys Met Phe His Ala Thr Val Ala Thr Glu Asn 595 600 605 Glu Val Phe Arg Val Lys Val Phe Asn Ile Asp Leu Lys Glu Lys Phe 610 615 620 Thr Pro Lys Lys Ile Ile Ala Ile Ala Asn Tyr Val Cys Arg Asn Gly 625 630 635 640 Phe Leu Glu Val Tyr Pro Phe Thr Leu Val Ala Asp Val Asn Ala Asp 645 650 655 Arg Asn Met Glu Ile Pro Lys Gly Leu Ile Arg Ser Ala Ser Val Thr 660 665 670 Pro Lys Ile Asn Gln Leu Cys Ser Gln Thr Lys Gly Ser Phe Val Asn 675 680 685 Gly Val Phe Glu Val His Lys Lys Asn Val Arg Gly Glu Phe Thr Tyr 690 695 700 Tyr Glu Ile Gln Asp Asn Thr Gly Lys Met Glu Val Val Val His Gly 705 710 715 720 Arg Leu Thr Thr Ile Asn Cys Glu Glu Gly Asp Lys Leu Lys Leu Thr 725 730 735 Cys Phe Glu Leu Ala Pro Lys Ser Gly Asn Thr Gly Glu Leu Arg Ser 740 745 750 Val Ile His Ser His Ile Lys Val Ile Lys Thr Arg Lys Asn Lys Lys 755 760 765 Asp Ile Leu Asn Pro Asp Ser Ser Met Glu Thr Ser Pro Asp Phe Phe 770 775 780 Phe 785 <210> SEQ ID NO 17 <211> LENGTH: 166 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P17803 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(166) <400> SEQUENCE: 17 Met Ser Tyr Thr Thr Tyr Phe Leu Ala Phe Gln Leu Cys Val Thr Leu 1 5 10 15 Cys Phe Ser Gly Ser Tyr Cys Gln Ala Pro Phe Phe Lys Glu Ile Thr 20 25 30 Ile Leu Lys Asp Tyr Phe Asn Ala Ser Thr Ser Asp Val Pro Asn Gly 35 40 45 Gly Pro Leu Phe Leu Glu Ile Leu Lys Asn Trp Lys Glu Glu Ser Asp 50 55 60 Lys Lys Ile Ile Gln Ser Gln Ile Val Ser Phe Tyr Phe Lys Phe Phe 65 70 75 80 Glu Ile Phe Lys Asp Asn Gln Ala Ile Gln Arg Ser Met Asp Val Ile 85 90 95 Lys Gln Asp Met Phe Gln Arg Phe Leu Asn Gly Ser Ser Gly Lys Leu 100 105 110

Asn Asp Phe Glu Lys Leu Ile Lys Ile Pro Val Asp Asn Leu Gln Ile 115 120 125 Gln Arg Lys Ala Ile Ser Glu Leu Ile Lys Val Met Asn Asp Leu Ser 130 135 140 Pro Arg Ser Asn Leu Arg Lys Arg Lys Arg Ser Gln Thr Met Phe Gln 145 150 155 160 Gly Gln Arg Ala Ser Lys 165 <210> SEQ ID NO 18 <211> LENGTH: 272 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01589 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(272) <400> SEQUENCE: 18 Met Asp Ser Tyr Leu Leu Met Trp Gly Leu Leu Thr Phe Ile Met Val 1 5 10 15 Pro Gly Cys Gln Ala Glu Leu Cys Asp Asp Asp Pro Pro Glu Ile Pro 20 25 30 His Ala Thr Phe Lys Ala Met Ala Tyr Lys Glu Gly Thr Met Leu Asn 35 40 45 Cys Glu Cys Lys Arg Gly Phe Arg Arg Ile Lys Ser Gly Ser Leu Tyr 50 55 60 Met Leu Cys Thr Gly Asn Ser Ser His Ser Ser Trp Asp Asn Gln Cys 65 70 75 80 Gln Cys Thr Ser Ser Ala Thr Arg Asn Thr Thr Lys Gln Val Thr Pro 85 90 95 Gln Pro Glu Glu Gln Lys Glu Arg Lys Thr Thr Glu Met Gln Ser Pro 100 105 110 Met Gln Pro Val Asp Gln Ala Ser Leu Pro Gly His Cys Arg Glu Pro 115 120 125 Pro Pro Trp Glu Asn Glu Ala Thr Glu Arg Ile Tyr His Phe Val Val 130 135 140 Gly Gln Met Val Tyr Tyr Gln Cys Val Gln Gly Tyr Arg Ala Leu His 145 150 155 160 Arg Gly Pro Ala Glu Ser Val Cys Lys Met Thr His Gly Lys Thr Arg 165 170 175 Trp Thr Gln Pro Gln Leu Ile Cys Thr Gly Glu Met Glu Thr Ser Gln 180 185 190 Phe Pro Gly Glu Glu Lys Pro Gln Ala Ser Pro Glu Gly Arg Pro Glu 195 200 205 Ser Glu Thr Ser Cys Leu Val Thr Thr Thr Asp Phe Gln Ile Gln Thr 210 215 220 Glu Met Ala Ala Thr Met Glu Thr Ser Ile Phe Thr Thr Glu Tyr Gln 225 230 235 240 Val Ala Val Ala Gly Cys Val Phe Leu Leu Ile Ser Val Leu Leu Leu 245 250 255 Ser Gly Leu Thr Trp Gln Arg Arg Gln Arg Lys Ser Arg Arg Thr Ile 260 265 270 <210> SEQ ID NO 19 <211> LENGTH: 459 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16871 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(459) <400> SEQUENCE: 19 Met Thr Ile Leu Gly Thr Thr Phe Gly Met Val Phe Ser Leu Leu Gln 1 5 10 15 Val Val Ser Gly Glu Ser Gly Tyr Ala Gln Asn Gly Asp Leu Glu Asp 20 25 30 Ala Glu Leu Asp Asp Tyr Ser Phe Ser Cys Tyr Ser Gln Leu Glu Val 35 40 45 Asn Gly Ser Gln His Ser Leu Thr Cys Ala Phe Glu Asp Pro Asp Val 50 55 60 Asn Thr Thr Asn Leu Glu Phe Glu Ile Cys Gly Ala Leu Val Glu Val 65 70 75 80 Lys Cys Leu Asn Phe Arg Lys Leu Gln Glu Ile Tyr Phe Ile Glu Thr 85 90 95 Lys Lys Phe Leu Leu Ile Gly Lys Ser Asn Ile Cys Val Lys Val Gly 100 105 110 Glu Lys Ser Leu Thr Cys Lys Lys Ile Asp Leu Thr Thr Ile Val Lys 115 120 125 Pro Glu Ala Pro Phe Asp Leu Ser Val Ile Tyr Arg Glu Gly Ala Asn 130 135 140 Asp Phe Val Val Thr Phe Asn Thr Ser His Leu Gln Lys Lys Tyr Val 145 150 155 160 Lys Val Leu Met His Asp Val Ala Tyr Arg Gln Glu Lys Asp Glu Asn 165 170 175 Lys Trp Thr His Val Asn Leu Ser Ser Thr Lys Leu Thr Leu Leu Gln 180 185 190 Arg Lys Leu Gln Pro Ala Ala Met Tyr Glu Ile Lys Val Arg Ser Ile 195 200 205 Pro Asp His Tyr Phe Lys Gly Phe Trp Ser Glu Trp Ser Pro Ser Tyr 210 215 220 Tyr Phe Arg Thr Pro Glu Ile Asn Asn Ser Ser Gly Glu Met Asp Pro 225 230 235 240 Ile Leu Leu Thr Ile Ser Ile Leu Ser Phe Phe Ser Val Ala Leu Leu 245 250 255 Val Ile Leu Ala Cys Val Leu Trp Lys Lys Arg Ile Lys Pro Ile Val 260 265 270 Trp Pro Ser Leu Pro Asp His Lys Lys Thr Leu Glu His Leu Cys Lys 275 280 285 Lys Pro Arg Lys Asn Leu Asn Val Ser Phe Asn Pro Glu Ser Phe Leu 290 295 300 Asp Cys Gln Ile His Arg Val Asp Asp Ile Gln Ala Arg Asp Glu Val 305 310 315 320 Glu Gly Phe Leu Gln Asp Thr Phe Pro Gln Gln Leu Glu Glu Ser Glu 325 330 335 Lys Gln Arg Leu Gly Gly Asp Val Gln Ser Pro Asn Cys Pro Ser Glu 340 345 350 Asp Val Val Ile Thr Pro Glu Ser Phe Gly Arg Asp Ser Ser Leu Thr 355 360 365 Cys Leu Ala Gly Asn Val Ser Ala Cys Asp Ala Pro Ile Leu Ser Ser 370 375 380 Ser Arg Ser Leu Asp Cys Arg Glu Ser Gly Lys Asn Gly Pro His Val 385 390 395 400 Tyr Gln Asp Leu Leu Leu Ser Leu Gly Thr Thr Asn Ser Thr Leu Pro 405 410 415 Pro Pro Phe Ser Leu Gln Ser Gly Ile Leu Thr Leu Asn Pro Val Ala 420 425 430 Gln Gly Gln Pro Ile Leu Thr Ser Leu Gly Ser Asn Gln Glu Glu Ala 435 440 445 Tyr Val Thr Met Ser Ser Phe Tyr Gln Asn Gln 450 455 <210> SEQ ID NO 20 <211> LENGTH: 110 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01308 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(110) <400> SEQUENCE: 20 Met Ala Leu Trp Met Arg Leu Leu Pro Leu Leu Ala Leu Leu Ala Leu 1 5 10 15 Trp Gly Pro Asp Pro Ala Ala Ala Phe Val Asn Gln His Leu Cys Gly 20 25 30 Ser His Leu Val Glu Ala Leu Tyr Leu Val Cys Gly Glu Arg Gly Phe 35 40 45 Phe Tyr Thr Pro Lys Thr Arg Arg Glu Ala Glu Asp Leu Gln Val Gly 50 55 60 Gln Val Glu Leu Gly Gly Gly Pro Gly Ala Gly Ser Leu Gln Pro Leu 65 70 75 80 Ala Leu Glu Gly Ser Leu Gln Lys Arg Gly Ile Val Glu Gln Cys Cys 85 90 95 Thr Ser Ile Cys Ser Leu Tyr Gln Leu Glu Asn Tyr Cys Asn 100 105 110 <210> SEQ ID NO 21 <211> LENGTH: 711 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q92945 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(459) <400> SEQUENCE: 21 Met Ser Asp Tyr Ser Thr Gly Gly Pro Pro Pro Gly Pro Pro Pro Pro 1 5 10 15 Ala Gly Gly Gly Gly Gly Ala Gly Gly Ala Gly Gly Gly Pro Pro Pro 20 25 30 Gly Pro Pro Gly Ala Gly Asp Arg Gly Gly Gly Gly Pro Gly Gly Gly 35 40 45 Gly Pro Gly Gly Gly Ser Ala Gly Gly Pro Ser Gln Pro Pro Gly Gly 50 55 60 Gly Gly Pro Gly Ile Arg Lys Asp Ala Phe Ala Asp Ala Val Gln Arg 65 70 75 80 Ala Arg Gln Ile Ala Ala Lys Ile Gly Gly Asp Ala Ala Thr Thr Val 85 90 95 Asn Asn Ser Thr Pro Asp Phe Gly Phe Gly Gly Gln Lys Arg Gln Leu 100 105 110 Glu Asp Gly Asp Gln Pro Glu Ser Lys Lys Leu Ala Ser Gln Gly Asp 115 120 125 Ser Ile Ser Ser Gln Leu Gly Pro Ile His Pro Pro Pro Arg Thr Ser 130 135 140 Met Thr Glu Glu Tyr Arg Val Pro Asp Gly Met Val Gly Leu Ile Ile 145 150 155 160 Gly Arg Gly Gly Glu Gln Ile Asn Lys Ile Gln Gln Asp Ser Gly Cys 165 170 175

Lys Val Gln Ile Ser Pro Asp Ser Gly Gly Leu Pro Glu Arg Ser Val 180 185 190 Ser Leu Thr Gly Ala Pro Glu Ser Val Gln Lys Ala Lys Met Met Leu 195 200 205 Asp Asp Ile Val Ser Arg Gly Arg Gly Gly Pro Pro Gly Gln Phe His 210 215 220 Asp Asn Ala Asn Gly Gly Gln Asn Gly Thr Val Gln Glu Ile Met Ile 225 230 235 240 Pro Ala Gly Lys Ala Gly Leu Val Ile Gly Lys Gly Gly Glu Thr Ile 245 250 255 Lys Gln Leu Gln Glu Arg Ala Gly Val Lys Met Ile Leu Ile Gln Asp 260 265 270 Gly Ser Gln Asn Thr Asn Val Asp Lys Pro Leu Arg Ile Ile Gly Asp 275 280 285 Pro Tyr Lys Val Gln Gln Ala Cys Glu Met Val Met Asp Ile Leu Arg 290 295 300 Glu Arg Asp Gln Gly Gly Phe Gly Asp Arg Asn Glu Tyr Gly Ser Arg 305 310 315 320 Ile Gly Gly Gly Ile Asp Val Pro Val Pro Arg His Ser Val Gly Val 325 330 335 Val Ile Gly Arg Ser Gly Glu Met Ile Lys Lys Ile Gln Asn Asp Ala 340 345 350 Gly Val Arg Ile Gln Phe Lys Gln Asp Asp Gly Thr Gly Pro Glu Lys 355 360 365 Ile Ala His Ile Met Gly Pro Pro Asp Arg Cys Glu His Ala Ala Arg 370 375 380 Ile Ile Asn Asp Leu Leu Gln Ser Leu Arg Ser Gly Pro Pro Gly Pro 385 390 395 400 Pro Gly Gly Pro Gly Met Pro Pro Gly Gly Arg Gly Arg Gly Arg Gly 405 410 415 Gln Gly Asn Trp Gly Pro Pro Gly Gly Glu Met Thr Phe Ser Ile Pro 420 425 430 Thr His Lys Cys Gly Leu Val Ile Gly Arg Gly Gly Glu Asn Val Lys 435 440 445 Ala Ile Asn Gln Gln Thr Gly Ala Phe Val Glu Ile Ser Arg Gln Leu 450 455 460 Pro Pro Asn Gly Asp Pro Asn Phe Lys Leu Phe Ile Ile Arg Gly Ser 465 470 475 480 Pro Gln Gln Ile Asp His Ala Lys Gln Leu Ile Glu Glu Lys Ile Glu 485 490 495 Gly Pro Leu Cys Pro Val Gly Pro Gly Pro Gly Gly Pro Gly Pro Ala 500 505 510 Gly Pro Met Gly Pro Phe Asn Pro Gly Pro Phe Asn Gln Gly Pro Pro 515 520 525 Gly Ala Pro Pro His Ala Gly Gly Pro Pro Pro His Gln Tyr Pro Pro 530 535 540 Gln Gly Trp Gly Asn Thr Tyr Pro Gln Trp Gln Pro Pro Ala Pro His 545 550 555 560 Asp Pro Ser Lys Ala Ala Ala Ala Ala Ala Asp Pro Asn Ala Ala Trp 565 570 575 Ala Ala Tyr Tyr Ser His Tyr Tyr Gln Gln Pro Pro Gly Pro Val Pro 580 585 590 Gly Pro Ala Pro Ala Pro Ala Ala Pro Pro Ala Gln Gly Glu Pro Pro 595 600 605 Gln Pro Pro Pro Thr Gly Gln Ser Asp Tyr Thr Lys Ala Trp Glu Glu 610 615 620 Tyr Tyr Lys Lys Ile Gly Gln Gln Pro Gln Gln Pro Gly Ala Pro Pro 625 630 635 640 Gln Gln Asp Tyr Thr Lys Ala Trp Glu Glu Tyr Tyr Lys Lys Gln Ala 645 650 655 Gln Val Ala Thr Gly Gly Gly Pro Gly Ala Pro Pro Gly Ser Gln Pro 660 665 670 Asp Tyr Ser Ala Ala Trp Ala Glu Tyr Tyr Arg Gln Gln Ala Ala Tyr 675 680 685 Tyr Gly Gln Thr Pro Gly Pro Gly Gly Pro Gln Pro Pro Pro Thr Gln 690 695 700 Gln Gly Gln Gln Gln Ala Gln 705 710 <210> SEQ ID NO 22 <211> LENGTH: 664 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02545 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(664) <400> SEQUENCE: 22 Met Glu Thr Pro Ser Gln Arg Arg Ala Thr Arg Ser Gly Ala Gln Ala 1 5 10 15 Ser Ser Thr Pro Leu Ser Pro Thr Arg Ile Thr Arg Leu Gln Glu Lys 20 25 30 Glu Asp Leu Gln Glu Leu Asn Asp Arg Leu Ala Val Tyr Ile Asp Arg 35 40 45 Val Arg Ser Leu Glu Thr Glu Asn Ala Gly Leu Arg Leu Arg Ile Thr 50 55 60 Glu Ser Glu Glu Val Val Ser Arg Glu Val Ser Gly Ile Lys Ala Ala 65 70 75 80 Tyr Glu Ala Glu Leu Gly Asp Ala Arg Lys Thr Leu Asp Ser Val Ala 85 90 95 Lys Glu Arg Ala Arg Leu Gln Leu Glu Leu Ser Lys Val Arg Glu Glu 100 105 110 Phe Lys Glu Leu Lys Ala Arg Asn Thr Lys Lys Glu Gly Asp Leu Ile 115 120 125 Ala Ala Gln Ala Arg Leu Lys Asp Leu Glu Ala Leu Leu Asn Ser Lys 130 135 140 Glu Ala Ala Leu Ser Thr Ala Leu Ser Glu Lys Arg Thr Leu Glu Gly 145 150 155 160 Glu Leu His Asp Leu Arg Gly Gln Val Ala Lys Leu Glu Ala Ala Leu 165 170 175 Gly Glu Ala Lys Lys Gln Leu Gln Asp Glu Met Leu Arg Arg Val Asp 180 185 190 Ala Glu Asn Arg Leu Gln Thr Met Lys Glu Glu Leu Asp Phe Gln Lys 195 200 205 Asn Ile Tyr Ser Glu Glu Leu Arg Glu Thr Lys Arg Arg His Glu Thr 210 215 220 Arg Leu Val Glu Ile Asp Asn Gly Lys Gln Arg Glu Phe Glu Ser Arg 225 230 235 240 Leu Ala Asp Ala Leu Gln Glu Leu Arg Ala Gln His Glu Asp Gln Val 245 250 255 Glu Gln Tyr Lys Lys Glu Leu Glu Lys Thr Tyr Ser Ala Lys Leu Asp 260 265 270 Asn Ala Arg Gln Ser Ala Glu Arg Asn Ser Asn Leu Val Gly Ala Ala 275 280 285 His Glu Glu Leu Gln Gln Ser Arg Ile Arg Ile Asp Ser Leu Ser Ala 290 295 300 Gln Leu Ser Gln Leu Gln Lys Gln Leu Ala Ala Lys Glu Ala Lys Leu 305 310 315 320 Arg Asp Leu Glu Asp Ser Leu Ala Arg Glu Arg Asp Thr Ser Arg Arg 325 330 335 Leu Leu Ala Glu Lys Glu Arg Glu Met Ala Glu Met Arg Ala Arg Met 340 345 350 Gln Gln Gln Leu Asp Glu Tyr Gln Glu Leu Leu Asp Ile Lys Leu Ala 355 360 365 Leu Asp Met Glu Ile His Ala Tyr Arg Lys Leu Leu Glu Gly Glu Glu 370 375 380 Glu Arg Leu Arg Leu Ser Pro Ser Pro Thr Ser Gln Arg Ser Arg Gly 385 390 395 400 Arg Ala Ser Ser His Ser Ser Gln Thr Gln Gly Gly Gly Ser Val Thr 405 410 415 Lys Lys Arg Lys Leu Glu Ser Thr Glu Ser Arg Ser Ser Phe Ser Gln 420 425 430 His Ala Arg Thr Ser Gly Arg Val Ala Val Glu Glu Val Asp Glu Glu 435 440 445 Gly Lys Phe Val Arg Leu Arg Asn Lys Ser Asn Glu Asp Gln Ser Met 450 455 460 Gly Asn Trp Gln Ile Lys Arg Gln Asn Gly Asp Asp Pro Leu Leu Thr 465 470 475 480 Tyr Arg Phe Pro Pro Lys Phe Thr Leu Lys Ala Gly Gln Val Val Thr 485 490 495 Ile Trp Ala Ala Gly Ala Gly Ala Thr His Ser Pro Pro Thr Asp Leu 500 505 510 Val Trp Lys Ala Gln Asn Thr Trp Gly Cys Gly Asn Ser Leu Arg Thr 515 520 525 Ala Leu Ile Asn Ser Thr Gly Glu Glu Val Ala Met Arg Lys Leu Val 530 535 540 Arg Ser Val Thr Val Val Glu Asp Asp Glu Asp Glu Asp Gly Asp Asp 545 550 555 560 Leu Leu His His His His Gly Ser His Cys Ser Ser Ser Gly Asp Pro 565 570 575 Ala Glu Tyr Asn Leu Arg Ser Arg Thr Val Leu Cys Gly Thr Cys Gly 580 585 590 Gln Pro Ala Asp Lys Ala Ser Ala Ser Gly Ser Gly Ala Gln Val Gly 595 600 605 Gly Pro Ile Ser Ser Gly Ser Ser Ala Ser Ser Val Thr Val Thr Arg 610 615 620 Ser Tyr Arg Ser Val Gly Gly Ser Gly Gly Gly Ser Phe Gly Asp Asn 625 630 635 640 Leu Val Thr Arg Ser Tyr Leu Leu Gly Asn Ser Ser Pro Arg Thr Gln 645 650 655 Ser Pro Gln Asn Cys Ser Ile Met 660 <210> SEQ ID NO 23 <211> LENGTH: 586 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P20700 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(586)

<400> SEQUENCE: 23 Met Ala Thr Ala Thr Pro Val Pro Pro Arg Met Gly Ser Arg Ala Gly 1 5 10 15 Gly Pro Thr Thr Pro Leu Ser Pro Thr Arg Leu Ser Arg Leu Gln Glu 20 25 30 Lys Glu Glu Leu Arg Glu Leu Asn Asp Arg Leu Ala Val Tyr Ile Asp 35 40 45 Lys Val Arg Ser Leu Glu Thr Glu Asn Ser Ala Leu Gln Leu Gln Val 50 55 60 Thr Glu Arg Glu Glu Val Arg Gly Arg Glu Leu Thr Gly Leu Lys Ala 65 70 75 80 Leu Tyr Glu Thr Glu Leu Ala Asp Ala Arg Arg Ala Leu Asp Asp Thr 85 90 95 Ala Arg Glu Arg Ala Lys Leu Gln Ile Glu Leu Gly Lys Cys Lys Ala 100 105 110 Glu His Asp Gln Leu Leu Leu Asn Tyr Ala Lys Lys Glu Ser Asp Leu 115 120 125 Asn Gly Ala Gln Ile Lys Leu Arg Glu Tyr Glu Ala Ala Leu Asn Ser 130 135 140 Lys Asp Ala Ala Leu Ala Thr Ala Leu Gly Asp Lys Lys Ser Leu Glu 145 150 155 160 Gly Asp Leu Glu Asp Leu Lys Asp Gln Ile Ala Gln Leu Glu Ala Ser 165 170 175 Leu Ala Ala Ala Lys Lys Gln Leu Ala Asp Glu Thr Leu Leu Lys Val 180 185 190 Asp Leu Glu Asn Arg Cys Gln Ser Leu Thr Glu Asp Leu Glu Phe Arg 195 200 205 Lys Ser Met Tyr Glu Glu Glu Ile Asn Glu Thr Arg Arg Lys His Glu 210 215 220 Thr Arg Leu Val Glu Val Asp Ser Gly Arg Gln Ile Glu Tyr Glu Tyr 225 230 235 240 Lys Leu Ala Gln Ala Leu His Glu Met Arg Glu Gln His Asp Ala Gln 245 250 255 Val Arg Leu Tyr Lys Glu Glu Leu Glu Gln Thr Tyr His Ala Lys Leu 260 265 270 Glu Asn Ala Arg Leu Ser Ser Glu Met Asn Thr Ser Thr Val Asn Ser 275 280 285 Ala Arg Glu Glu Leu Met Glu Ser Arg Met Arg Ile Glu Ser Leu Ser 290 295 300 Ser Gln Leu Ser Asn Leu Gln Lys Glu Ser Arg Ala Cys Leu Glu Arg 305 310 315 320 Ile Gln Glu Leu Glu Asp Leu Leu Ala Lys Glu Lys Asp Asn Ser Arg 325 330 335 Arg Met Leu Thr Asp Lys Glu Arg Glu Met Ala Glu Ile Arg Asp Gln 340 345 350 Met Gln Gln Gln Leu Asn Asp Tyr Glu Gln Leu Leu Asp Val Lys Leu 355 360 365 Ala Leu Asp Met Glu Ile Ser Ala Tyr Arg Lys Leu Leu Glu Gly Glu 370 375 380 Glu Glu Arg Leu Lys Leu Ser Pro Ser Pro Ser Ser Arg Val Thr Val 385 390 395 400 Ser Arg Ala Ser Ser Ser Arg Ser Val Arg Thr Thr Arg Gly Lys Arg 405 410 415 Lys Arg Val Asp Val Glu Glu Ser Glu Ala Ser Ser Ser Val Ser Ile 420 425 430 Ser His Ser Ala Ser Ala Thr Gly Asn Val Cys Ile Glu Glu Ile Asp 435 440 445 Val Asp Gly Lys Phe Ile Arg Leu Lys Asn Thr Ser Glu Gln Asp Gln 450 455 460 Pro Met Gly Gly Trp Glu Met Ile Arg Lys Ile Gly Asp Thr Ser Val 465 470 475 480 Ser Tyr Lys Tyr Thr Ser Arg Tyr Val Leu Lys Ala Gly Gln Thr Val 485 490 495 Thr Ile Trp Ala Ala Asn Ala Gly Val Thr Ala Ser Pro Pro Thr Asp 500 505 510 Leu Ile Trp Lys Asn Gln Asn Ser Trp Gly Thr Gly Glu Asp Val Lys 515 520 525 Val Ile Leu Lys Asn Ser Gln Gly Glu Glu Val Ala Gln Arg Ser Thr 530 535 540 Val Phe Lys Thr Thr Ile Pro Glu Glu Glu Glu Glu Glu Glu Glu Ala 545 550 555 560 Ala Gly Val Val Val Glu Glu Glu Leu Phe His Gln Gln Gly Thr Pro 565 570 575 Arg Ala Ser Asn Arg Ser Cys Ala Ile Met 580 585 <210> SEQ ID NO 24 <211> LENGTH: 923 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O14786 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(923) <400> SEQUENCE: 24 Met Glu Arg Gly Leu Pro Leu Leu Cys Ala Val Leu Ala Leu Val Leu 1 5 10 15 Ala Pro Ala Gly Ala Phe Arg Asn Asp Lys Cys Gly Asp Thr Ile Lys 20 25 30 Ile Glu Ser Pro Gly Tyr Leu Thr Ser Pro Gly Tyr Pro His Ser Tyr 35 40 45 His Pro Ser Glu Lys Cys Glu Trp Leu Ile Gln Ala Pro Asp Pro Tyr 50 55 60 Gln Arg Ile Met Ile Asn Phe Asn Pro His Phe Asp Leu Glu Asp Arg 65 70 75 80 Asp Cys Lys Tyr Asp Tyr Val Glu Val Phe Asp Gly Glu Asn Glu Asn 85 90 95 Gly His Phe Arg Gly Lys Phe Cys Gly Lys Ile Ala Pro Pro Pro Val 100 105 110 Val Ser Ser Gly Pro Phe Leu Phe Ile Lys Phe Val Ser Asp Tyr Glu 115 120 125 Thr His Gly Ala Gly Phe Ser Ile Arg Tyr Glu Ile Phe Lys Arg Gly 130 135 140 Pro Glu Cys Ser Gln Asn Tyr Thr Thr Pro Ser Gly Val Ile Lys Ser 145 150 155 160 Pro Gly Phe Pro Glu Lys Tyr Pro Asn Ser Leu Glu Cys Thr Tyr Ile 165 170 175 Val Phe Val Pro Lys Met Ser Glu Ile Ile Leu Glu Phe Glu Ser Phe 180 185 190 Asp Leu Glu Pro Asp Ser Asn Pro Pro Gly Gly Met Phe Cys Arg Tyr 195 200 205 Asp Arg Leu Glu Ile Trp Asp Gly Phe Pro Asp Val Gly Pro His Ile 210 215 220 Gly Arg Tyr Cys Gly Gln Lys Thr Pro Gly Arg Ile Arg Ser Ser Ser 225 230 235 240 Gly Ile Leu Ser Met Val Phe Tyr Thr Asp Ser Ala Ile Ala Lys Glu 245 250 255 Gly Phe Ser Ala Asn Tyr Ser Val Leu Gln Ser Ser Val Ser Glu Asp 260 265 270 Phe Lys Cys Met Glu Ala Leu Gly Met Glu Ser Gly Glu Ile His Ser 275 280 285 Asp Gln Ile Thr Ala Ser Ser Gln Tyr Ser Thr Asn Trp Ser Ala Glu 290 295 300 Arg Ser Arg Leu Asn Tyr Pro Glu Asn Gly Trp Thr Pro Gly Glu Asp 305 310 315 320 Ser Tyr Arg Glu Trp Ile Gln Val Asp Leu Gly Leu Leu Arg Phe Val 325 330 335 Thr Ala Val Gly Thr Gln Gly Ala Ile Ser Lys Glu Thr Lys Lys Lys 340 345 350 Tyr Tyr Val Lys Thr Tyr Lys Ile Asp Val Ser Ser Asn Gly Glu Asp 355 360 365 Trp Ile Thr Ile Lys Glu Gly Asn Lys Pro Val Leu Phe Gln Gly Asn 370 375 380 Thr Asn Pro Thr Asp Val Val Val Ala Val Phe Pro Lys Pro Leu Ile 385 390 395 400 Thr Arg Phe Val Arg Ile Lys Pro Ala Thr Trp Glu Thr Gly Ile Ser 405 410 415 Met Arg Phe Glu Val Tyr Gly Cys Lys Ile Thr Asp Tyr Pro Cys Ser 420 425 430 Gly Met Leu Gly Met Val Ser Gly Leu Ile Ser Asp Ser Gln Ile Thr 435 440 445 Ser Ser Asn Gln Gly Asp Arg Asn Trp Met Pro Glu Asn Ile Arg Leu 450 455 460 Val Thr Ser Arg Ser Gly Trp Ala Leu Pro Pro Ala Pro His Ser Tyr 465 470 475 480 Ile Asn Glu Trp Leu Gln Ile Asp Leu Gly Glu Glu Lys Ile Val Arg 485 490 495 Gly Ile Ile Ile Gln Gly Gly Lys His Arg Glu Asn Lys Val Phe Met 500 505 510 Arg Lys Phe Lys Ile Gly Tyr Ser Asn Asn Gly Ser Asp Trp Lys Met 515 520 525 Ile Met Asp Asp Ser Lys Arg Lys Ala Lys Ser Phe Glu Gly Asn Asn 530 535 540 Asn Tyr Asp Thr Pro Glu Leu Arg Thr Phe Pro Ala Leu Ser Thr Arg 545 550 555 560 Phe Ile Arg Ile Tyr Pro Glu Arg Ala Thr His Gly Gly Leu Gly Leu 565 570 575 Arg Met Glu Leu Leu Gly Cys Glu Val Glu Ala Pro Thr Ala Gly Pro 580 585 590 Thr Thr Pro Asn Gly Asn Leu Val Asp Glu Cys Asp Asp Asp Gln Ala 595 600 605 Asn Cys His Ser Gly Thr Gly Asp Asp Phe Gln Leu Thr Gly Gly Thr 610 615 620 Thr Val Leu Ala Thr Glu Lys Pro Thr Val Ile Asp Ser Thr Ile Gln 625 630 635 640 Ser Glu Phe Pro Thr Tyr Gly Phe Asn Cys Glu Phe Gly Trp Gly Ser 645 650 655 His Lys Thr Phe Cys His Trp Glu His Asp Asn His Val Gln Leu Lys 660 665 670

Trp Ser Val Leu Thr Ser Lys Thr Gly Pro Ile Gln Asp His Thr Gly 675 680 685 Asp Gly Asn Phe Ile Tyr Ser Gln Ala Asp Glu Asn Gln Lys Gly Lys 690 695 700 Val Ala Arg Leu Val Ser Pro Val Val Tyr Ser Gln Asn Ser Ala His 705 710 715 720 Cys Met Thr Phe Trp Tyr His Met Ser Gly Ser His Val Gly Thr Leu 725 730 735 Arg Val Lys Leu Arg Tyr Gln Lys Pro Glu Glu Tyr Asp Gln Leu Val 740 745 750 Trp Met Ala Ile Gly His Gln Gly Asp His Trp Lys Glu Gly Arg Val 755 760 765 Leu Leu His Lys Ser Leu Lys Leu Tyr Gln Val Ile Phe Glu Gly Glu 770 775 780 Ile Gly Lys Gly Asn Leu Gly Gly Ile Ala Val Asp Asp Ile Ser Ile 785 790 795 800 Asn Asn His Ile Ser Gln Glu Asp Cys Ala Lys Pro Ala Asp Leu Asp 805 810 815 Lys Lys Asn Pro Glu Ile Lys Ile Asp Glu Thr Gly Ser Thr Pro Gly 820 825 830 Tyr Glu Gly Glu Gly Glu Gly Asp Lys Asn Ile Ser Arg Lys Pro Gly 835 840 845 Asn Val Leu Lys Thr Leu Asp Pro Ile Leu Ile Thr Ile Ile Ala Met 850 855 860 Ser Ala Leu Gly Val Leu Leu Gly Ala Val Cys Gly Val Val Leu Tyr 865 870 875 880 Cys Ala Cys Trp His Asn Gly Met Ser Glu Arg Asn Leu Ser Ala Leu 885 890 895 Glu Asn Tyr Asn Phe Glu Leu Val Asp Gly Val Lys Leu Lys Lys Asp 900 905 910 Lys Leu Asn Thr Gln Ser Thr Tyr Ser Glu Ala 915 920 <210> SEQ ID NO 25 <211> LENGTH: 441 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BXS6 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(441) <400> SEQUENCE: 25 Met Ile Ile Pro Ser Leu Glu Glu Leu Asp Ser Leu Lys Tyr Ser Asp 1 5 10 15 Leu Gln Asn Leu Ala Lys Ser Leu Gly Leu Arg Ala Asn Leu Arg Ala 20 25 30 Thr Lys Leu Leu Lys Ala Leu Lys Gly Tyr Ile Lys His Glu Ala Arg 35 40 45 Lys Gly Asn Glu Asn Gln Asp Glu Ser Gln Thr Ser Ala Ser Ser Cys 50 55 60 Asp Glu Thr Glu Ile Gln Ile Ser Asn Gln Glu Glu Ala Glu Arg Gln 65 70 75 80 Pro Leu Gly His Val Thr Lys Thr Arg Arg Arg Cys Lys Thr Val Arg 85 90 95 Val Asp Pro Asp Ser Gln Gln Asn His Ser Glu Ile Lys Ile Ser Asn 100 105 110 Pro Thr Glu Phe Gln Asn His Glu Lys Gln Glu Ser Gln Asp Leu Arg 115 120 125 Ala Thr Ala Lys Val Pro Ser Pro Pro Asp Glu His Gln Glu Ala Glu 130 135 140 Asn Ala Val Ser Ser Gly Asn Arg Asp Ser Lys Val Pro Ser Glu Gly 145 150 155 160 Lys Lys Ser Leu Tyr Thr Asp Glu Ser Ser Lys Pro Gly Lys Asn Lys 165 170 175 Arg Thr Ala Ile Thr Thr Pro Asn Phe Lys Lys Leu His Glu Ala His 180 185 190 Phe Lys Glu Met Glu Ser Ile Asp Gln Tyr Ile Glu Arg Lys Lys Lys 195 200 205 His Phe Glu Glu His Asn Ser Met Asn Glu Leu Lys Gln Gln Pro Ile 210 215 220 Asn Lys Gly Gly Val Arg Thr Pro Val Pro Pro Arg Gly Arg Leu Ser 225 230 235 240 Val Ala Ser Thr Pro Ile Ser Gln Arg Arg Ser Gln Gly Arg Ser Cys 245 250 255 Gly Pro Ala Ser Gln Ser Thr Leu Gly Leu Lys Gly Ser Leu Lys Arg 260 265 270 Ser Ala Ile Ser Ala Ala Lys Thr Gly Val Arg Phe Ser Ala Ala Thr 275 280 285 Lys Asp Asn Glu His Lys Arg Ser Leu Thr Lys Thr Pro Ala Arg Lys 290 295 300 Ser Ala His Val Thr Val Ser Gly Gly Thr Pro Lys Gly Glu Ala Val 305 310 315 320 Leu Gly Thr His Lys Leu Lys Thr Ile Thr Gly Asn Ser Ala Ala Val 325 330 335 Ile Thr Pro Phe Lys Leu Thr Thr Glu Ala Thr Gln Thr Pro Val Ser 340 345 350 Asn Lys Lys Pro Val Phe Asp Leu Lys Ala Ser Leu Ser Arg Pro Leu 355 360 365 Asn Tyr Glu Pro His Lys Gly Lys Leu Lys Pro Trp Gly Gln Ser Lys 370 375 380 Glu Asn Asn Tyr Leu Asn Gln His Val Asn Arg Ile Asn Phe Tyr Lys 385 390 395 400 Lys Thr Tyr Lys Gln Pro His Leu Gln Thr Lys Glu Glu Gln Arg Lys 405 410 415 Lys Arg Glu Gln Glu Arg Lys Glu Lys Lys Ala Lys Val Leu Gly Met 420 425 430 Arg Arg Gly Leu Ile Leu Ala Glu Asp 435 440 <210> SEQ ID NO 26 <211> LENGTH: 394 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9UQ80 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(394) <400> SEQUENCE: 26 Met Ser Gly Glu Asp Glu Gln Gln Glu Gln Thr Ile Ala Glu Asp Leu 1 5 10 15 Val Val Thr Lys Tyr Lys Met Gly Gly Asp Ile Ala Asn Arg Val Leu 20 25 30 Arg Ser Leu Val Glu Ala Ser Ser Ser Gly Val Ser Val Leu Ser Leu 35 40 45 Cys Glu Lys Gly Asp Ala Met Ile Met Glu Glu Thr Gly Lys Ile Phe 50 55 60 Lys Lys Glu Lys Glu Met Lys Lys Gly Ile Ala Phe Pro Thr Ser Ile 65 70 75 80 Ser Val Asn Asn Cys Val Cys His Phe Ser Pro Leu Lys Ser Asp Gln 85 90 95 Asp Tyr Ile Leu Lys Glu Gly Asp Leu Val Lys Ile Asp Leu Gly Val 100 105 110 His Val Asp Gly Phe Ile Ala Asn Val Ala His Thr Phe Val Val Asp 115 120 125 Val Ala Gln Gly Thr Gln Val Thr Gly Arg Lys Ala Asp Val Ile Lys 130 135 140 Ala Ala His Leu Cys Ala Glu Ala Ala Leu Arg Leu Val Lys Pro Gly 145 150 155 160 Asn Gln Asn Thr Gln Val Thr Glu Ala Trp Asn Lys Val Ala His Ser 165 170 175 Phe Asn Cys Thr Pro Ile Glu Gly Met Leu Ser His Gln Leu Lys Gln 180 185 190 His Val Ile Asp Gly Glu Lys Thr Ile Ile Gln Asn Pro Thr Asp Gln 195 200 205 Gln Lys Lys Asp His Glu Lys Ala Glu Phe Glu Val His Glu Val Tyr 210 215 220 Ala Val Asp Val Leu Val Ser Ser Gly Glu Gly Lys Ala Lys Asp Ala 225 230 235 240 Gly Gln Arg Thr Thr Ile Tyr Lys Arg Asp Pro Ser Lys Gln Tyr Gly 245 250 255 Leu Lys Met Lys Thr Ser Arg Ala Phe Phe Ser Glu Val Glu Arg Arg 260 265 270 Phe Asp Ala Met Pro Phe Thr Leu Arg Ala Phe Glu Asp Glu Lys Lys 275 280 285 Ala Arg Met Gly Val Val Glu Cys Ala Lys His Glu Leu Leu Gln Pro 290 295 300 Phe Asn Val Leu Tyr Glu Lys Glu Gly Glu Phe Val Ala Gln Phe Lys 305 310 315 320 Phe Thr Val Leu Leu Met Pro Asn Gly Pro Met Arg Ile Thr Ser Gly 325 330 335 Pro Phe Glu Pro Asp Leu Tyr Lys Ser Glu Met Glu Val Gln Asp Ala 340 345 350 Glu Leu Lys Ala Leu Leu Gln Ser Ser Ala Ser Arg Lys Thr Gln Lys 355 360 365 Lys Lys Lys Lys Lys Ala Ser Lys Thr Ala Glu Asn Ala Thr Ser Gly 370 375 380 Glu Thr Leu Glu Glu Asn Glu Ala Gly Asp 385 390 <210> SEQ ID NO 27 <211> LENGTH: 198 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P32119 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(198) <400> SEQUENCE: 27 Met Ala Ser Gly Asn Ala Arg Ile Gly Lys Pro Ala Pro Asp Phe Lys 1 5 10 15 Ala Thr Ala Val Val Asp Gly Ala Phe Lys Glu Val Lys Leu Ser Asp 20 25 30 Tyr Lys Gly Lys Tyr Val Val Leu Phe Phe Tyr Pro Leu Asp Phe Thr 35 40 45

Phe Val Cys Pro Thr Glu Ile Ile Ala Phe Ser Asn Arg Ala Glu Asp 50 55 60 Phe Arg Lys Leu Gly Cys Glu Val Leu Gly Val Ser Val Asp Ser Gln 65 70 75 80 Phe Thr His Leu Ala Trp Ile Asn Thr Pro Arg Lys Glu Gly Gly Leu 85 90 95 Gly Pro Leu Asn Ile Pro Leu Leu Ala Asp Val Thr Arg Arg Leu Ser 100 105 110 Glu Asp Tyr Gly Val Leu Lys Thr Asp Glu Gly Ile Ala Tyr Arg Gly 115 120 125 Leu Phe Ile Ile Asp Gly Lys Gly Val Leu Arg Gln Ile Thr Val Asn 130 135 140 Asp Leu Pro Val Gly Arg Ser Val Asp Glu Ala Leu Arg Leu Val Gln 145 150 155 160 Ala Phe Gln Tyr Thr Asp Glu His Gly Glu Val Cys Pro Ala Gly Trp 165 170 175 Lys Pro Gly Ser Asp Thr Ile Lys Pro Asn Val Asp Asp Ser Lys Glu 180 185 190 Tyr Phe Ser Lys His Asn 195 <210> SEQ ID NO 28 <211> LENGTH: 592 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q05513 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(592) <400> SEQUENCE: 28 Met Pro Ser Arg Thr Gly Pro Lys Met Glu Gly Ser Gly Gly Arg Val 1 5 10 15 Arg Leu Lys Ala His Tyr Gly Gly Asp Ile Phe Ile Thr Ser Val Asp 20 25 30 Ala Ala Thr Thr Phe Glu Glu Leu Cys Glu Glu Val Arg Asp Met Cys 35 40 45 Arg Leu His Gln Gln His Pro Leu Thr Leu Lys Trp Val Asp Ser Glu 50 55 60 Gly Asp Pro Cys Thr Val Ser Ser Gln Met Glu Leu Glu Glu Ala Phe 65 70 75 80 Arg Leu Ala Arg Gln Cys Arg Asp Glu Gly Leu Ile Ile His Val Phe 85 90 95 Pro Ser Thr Pro Glu Gln Pro Gly Leu Pro Cys Pro Gly Glu Asp Lys 100 105 110 Ser Ile Tyr Arg Arg Gly Ala Arg Arg Trp Arg Lys Leu Tyr Arg Ala 115 120 125 Asn Gly His Leu Phe Gln Ala Lys Arg Phe Asn Arg Arg Ala Tyr Cys 130 135 140 Gly Gln Cys Ser Glu Arg Ile Trp Gly Leu Ala Arg Gln Gly Tyr Arg 145 150 155 160 Cys Ile Asn Cys Lys Leu Leu Val His Lys Arg Cys His Gly Leu Val 165 170 175 Pro Leu Thr Cys Arg Lys His Met Asp Ser Val Met Pro Ser Gln Glu 180 185 190 Pro Pro Val Asp Asp Lys Asn Glu Asp Ala Asp Leu Pro Ser Glu Glu 195 200 205 Thr Asp Gly Ile Ala Tyr Ile Ser Ser Ser Arg Lys His Asp Ser Ile 210 215 220 Lys Asp Asp Ser Glu Asp Leu Lys Pro Val Ile Asp Gly Met Asp Gly 225 230 235 240 Ile Lys Ile Ser Gln Gly Leu Gly Leu Gln Asp Phe Asp Leu Ile Arg 245 250 255 Val Ile Gly Arg Gly Ser Tyr Ala Lys Val Leu Leu Val Arg Leu Lys 260 265 270 Lys Asn Asp Gln Ile Tyr Ala Met Lys Val Val Lys Lys Glu Leu Val 275 280 285 His Asp Asp Glu Asp Ile Asp Trp Val Gln Thr Glu Lys His Val Phe 290 295 300 Glu Gln Ala Ser Ser Asn Pro Phe Leu Val Gly Leu His Ser Cys Phe 305 310 315 320 Gln Thr Thr Ser Arg Leu Phe Leu Val Ile Glu Tyr Val Asn Gly Gly 325 330 335 Asp Leu Met Phe His Met Gln Arg Gln Arg Lys Leu Pro Glu Glu His 340 345 350 Ala Arg Phe Tyr Ala Ala Glu Ile Cys Ile Ala Leu Asn Phe Leu His 355 360 365 Glu Arg Gly Ile Ile Tyr Arg Asp Leu Lys Leu Asp Asn Val Leu Leu 370 375 380 Asp Ala Asp Gly His Ile Lys Leu Thr Asp Tyr Gly Met Cys Lys Glu 385 390 395 400 Gly Leu Gly Pro Gly Asp Thr Thr Ser Thr Phe Cys Gly Thr Pro Asn 405 410 415 Tyr Ile Ala Pro Glu Ile Leu Arg Gly Glu Glu Tyr Gly Phe Ser Val 420 425 430 Asp Trp Trp Ala Leu Gly Val Leu Met Phe Glu Met Met Ala Gly Arg 435 440 445 Ser Pro Phe Asp Ile Ile Thr Asp Asn Pro Asp Met Asn Thr Glu Asp 450 455 460 Tyr Leu Phe Gln Val Ile Leu Glu Lys Pro Ile Arg Ile Pro Arg Phe 465 470 475 480 Leu Ser Val Lys Ala Ser His Val Leu Lys Gly Phe Leu Asn Lys Asp 485 490 495 Pro Lys Glu Arg Leu Gly Cys Arg Pro Gln Thr Gly Phe Ser Asp Ile 500 505 510 Lys Ser His Ala Phe Phe Arg Ser Ile Asp Trp Asp Leu Leu Glu Lys 515 520 525 Lys Gln Ala Leu Pro Pro Phe Gln Pro Gln Ile Thr Asp Asp Tyr Gly 530 535 540 Leu Asp Asn Phe Asp Thr Gln Phe Thr Ser Glu Pro Val Gln Leu Thr 545 550 555 560 Pro Asp Asp Glu Asp Ala Ile Lys Arg Ile Asp Gln Ser Glu Phe Glu 565 570 575 Gly Phe Glu Tyr Ile Asn Pro Leu Leu Leu Ser Thr Glu Glu Ser Val 580 585 590 <210> SEQ ID NO 29 <211> LENGTH: 256 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9NP55 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(256) <400> SEQUENCE: 29 Met Phe Gln Thr Gly Gly Leu Ile Val Phe Tyr Gly Leu Leu Ala Gln 1 5 10 15 Thr Met Ala Gln Phe Gly Gly Leu Pro Val Pro Leu Asp Gln Thr Leu 20 25 30 Pro Leu Asn Val Asn Pro Ala Leu Pro Leu Ser Pro Thr Gly Leu Ala 35 40 45 Gly Ser Leu Thr Asn Ala Leu Ser Asn Gly Leu Leu Ser Gly Gly Leu 50 55 60 Leu Gly Ile Leu Glu Asn Leu Pro Leu Leu Asp Ile Leu Lys Pro Gly 65 70 75 80 Gly Gly Thr Ser Gly Gly Leu Leu Gly Gly Leu Leu Gly Lys Val Thr 85 90 95 Ser Val Ile Pro Gly Leu Asn Asn Ile Ile Asp Ile Lys Val Thr Asp 100 105 110 Pro Gln Leu Leu Glu Leu Gly Leu Val Gln Ser Pro Asp Gly His Arg 115 120 125 Leu Tyr Val Thr Ile Pro Leu Gly Ile Lys Leu Gln Val Asn Thr Pro 130 135 140 Leu Val Gly Ala Ser Leu Leu Arg Leu Ala Val Lys Leu Asp Ile Thr 145 150 155 160 Ala Glu Ile Leu Ala Val Arg Asp Lys Gln Glu Arg Ile His Leu Val 165 170 175 Leu Gly Asp Cys Thr His Ser Pro Gly Ser Leu Gln Ile Ser Leu Leu 180 185 190 Asp Gly Leu Gly Pro Leu Pro Ile Gln Gly Leu Leu Asp Ser Leu Thr 195 200 205 Gly Ile Leu Asn Lys Val Leu Pro Glu Leu Val Gln Gly Asn Val Cys 210 215 220 Pro Leu Val Asn Glu Val Leu Arg Gly Leu Asp Ile Thr Leu Val His 225 230 235 240 Asp Ile Val Asn Met Leu Ile His Gly Leu Gln Phe Val Ile Lys Val 245 250 255 <210> SEQ ID NO 30 <211> LENGTH: 418 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P43686 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(418) <400> SEQUENCE: 30 Met Glu Glu Ile Gly Ile Leu Val Glu Lys Ala Gln Asp Glu Ile Pro 1 5 10 15 Ala Leu Ser Val Ser Arg Pro Gln Thr Gly Leu Ser Phe Leu Gly Pro 20 25 30 Glu Pro Glu Asp Leu Glu Asp Leu Tyr Ser Arg Tyr Lys Lys Leu Gln 35 40 45 Gln Glu Leu Glu Phe Leu Glu Val Gln Glu Glu Tyr Ile Lys Asp Glu 50 55 60 Gln Lys Asn Leu Lys Lys Glu Phe Leu His Ala Gln Glu Glu Val Lys 65 70 75 80 Arg Ile Gln Ser Ile Pro Leu Val Ile Gly Gln Phe Leu Glu Ala Val 85 90 95 Asp Gln Asn Thr Ala Ile Val Gly Ser Thr Thr Gly Ser Asn Tyr Tyr 100 105 110 Val Arg Ile Leu Ser Thr Ile Asp Arg Glu Leu Leu Lys Pro Asn Ala 115 120 125 Ser Val Ala Leu His Lys His Ser Asn Ala Leu Val Asp Val Leu Pro

130 135 140 Pro Glu Ala Asp Ser Ser Ile Met Met Leu Thr Ser Asp Gln Lys Pro 145 150 155 160 Asp Val Met Tyr Ala Asp Ile Gly Gly Met Asp Ile Gln Lys Gln Glu 165 170 175 Val Arg Glu Ala Val Glu Leu Pro Leu Thr His Phe Glu Leu Tyr Lys 180 185 190 Gln Ile Gly Ile Asp Pro Pro Arg Gly Val Leu Met Tyr Gly Pro Pro 195 200 205 Gly Cys Gly Lys Thr Met Leu Ala Lys Ala Val Ala His His Thr Thr 210 215 220 Ala Ala Phe Ile Arg Val Val Gly Ser Glu Phe Val Gln Lys Tyr Leu 225 230 235 240 Gly Glu Gly Pro Arg Met Val Arg Asp Val Phe Arg Leu Ala Lys Glu 245 250 255 Asn Ala Pro Ala Ile Ile Phe Ile Asp Glu Ile Asp Ala Ile Ala Thr 260 265 270 Lys Arg Phe Asp Ala Gln Thr Gly Ala Asp Arg Glu Val Gln Arg Ile 275 280 285 Leu Leu Glu Leu Leu Asn Gln Met Asp Gly Phe Asp Gln Asn Val Asn 290 295 300 Val Lys Val Ile Met Ala Thr Asn Arg Ala Asp Thr Leu Asp Pro Ala 305 310 315 320 Leu Leu Arg Pro Gly Arg Leu Asp Arg Lys Ile Glu Phe Pro Leu Pro 325 330 335 Asp Arg Arg Gln Lys Arg Leu Ile Phe Ser Thr Ile Thr Ser Lys Met 340 345 350 Asn Leu Ser Glu Glu Val Asp Leu Glu Asp Tyr Val Ala Arg Pro Asp 355 360 365 Lys Ile Ser Gly Ala Asp Ile Asn Ser Ile Cys Gln Glu Ser Gly Met 370 375 380 Leu Ala Val Arg Glu Asn Arg Tyr Ile Val Leu Ala Lys Asp Phe Glu 385 390 395 400 Lys Ala Tyr Lys Thr Val Ile Lys Lys Asp Glu Gln Glu His Glu Phe 405 410 415 Tyr Lys <210> SEQ ID NO 31 <211> LENGTH: 979 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q16849 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(979) <400> SEQUENCE: 31 Met Arg Arg Pro Arg Arg Pro Gly Gly Leu Gly Gly Ser Gly Gly Leu 1 5 10 15 Arg Leu Leu Leu Cys Leu Leu Leu Leu Ser Ser Arg Pro Gly Gly Cys 20 25 30 Ser Ala Val Ser Ala His Gly Cys Leu Phe Asp Arg Arg Leu Cys Ser 35 40 45 His Leu Glu Val Cys Ile Gln Asp Gly Leu Phe Gly Gln Cys Gln Val 50 55 60 Gly Val Gly Gln Ala Arg Pro Leu Leu Gln Val Thr Ser Pro Val Leu 65 70 75 80 Gln Arg Leu Gln Gly Val Leu Arg Gln Leu Met Ser Gln Gly Leu Ser 85 90 95 Trp His Asp Asp Leu Thr Gln Tyr Val Ile Ser Gln Glu Met Glu Arg 100 105 110 Ile Pro Arg Leu Arg Pro Pro Glu Pro Arg Pro Arg Asp Arg Ser Gly 115 120 125 Leu Ala Pro Lys Arg Pro Gly Pro Ala Gly Glu Leu Leu Leu Gln Asp 130 135 140 Ile Pro Thr Gly Ser Ala Pro Ala Ala Gln His Arg Leu Pro Gln Pro 145 150 155 160 Pro Val Gly Lys Gly Gly Ala Gly Ala Ser Ser Ser Leu Ser Pro Leu 165 170 175 Gln Ala Glu Leu Leu Pro Pro Leu Leu Glu His Leu Leu Leu Pro Pro 180 185 190 Gln Pro Pro His Pro Ser Leu Ser Tyr Glu Pro Ala Leu Leu Gln Pro 195 200 205 Tyr Leu Phe His Gln Phe Gly Ser Arg Asp Gly Ser Arg Val Ser Glu 210 215 220 Gly Ser Pro Gly Met Val Ser Val Gly Pro Leu Pro Lys Ala Glu Ala 225 230 235 240 Pro Ala Leu Phe Ser Arg Thr Ala Ser Lys Gly Ile Phe Gly Asp His 245 250 255 Pro Gly His Ser Tyr Gly Asp Leu Pro Gly Pro Ser Pro Ala Gln Leu 260 265 270 Phe Gln Asp Ser Gly Leu Leu Tyr Leu Ala Gln Glu Leu Pro Ala Pro 275 280 285 Ser Arg Ala Arg Val Pro Arg Leu Pro Glu Gln Gly Ser Ser Ser Arg 290 295 300 Ala Glu Asp Ser Pro Glu Gly Tyr Glu Lys Glu Gly Leu Gly Asp Arg 305 310 315 320 Gly Glu Lys Pro Ala Ser Pro Ala Val Gln Pro Asp Ala Ala Leu Gln 325 330 335 Arg Leu Ala Ala Val Leu Ala Gly Tyr Gly Val Glu Leu Arg Gln Leu 340 345 350 Thr Pro Glu Gln Leu Ser Thr Leu Leu Thr Leu Leu Gln Leu Leu Pro 355 360 365 Lys Gly Ala Gly Arg Asn Pro Gly Gly Val Val Asn Val Gly Ala Asp 370 375 380 Ile Lys Lys Thr Met Glu Gly Pro Val Glu Gly Arg Asp Thr Ala Glu 385 390 395 400 Leu Pro Ala Arg Thr Ser Pro Met Pro Gly His Pro Thr Ala Ser Pro 405 410 415 Thr Ser Ser Glu Val Gln Gln Val Pro Ser Pro Val Ser Ser Glu Pro 420 425 430 Pro Lys Ala Ala Arg Pro Pro Val Thr Pro Val Leu Leu Glu Lys Lys 435 440 445 Ser Pro Leu Gly Gln Ser Gln Pro Thr Val Ala Gly Gln Pro Ser Ala 450 455 460 Arg Pro Ala Ala Glu Glu Tyr Gly Tyr Ile Val Thr Asp Gln Lys Pro 465 470 475 480 Leu Ser Leu Ala Ala Gly Val Lys Leu Leu Glu Ile Leu Ala Glu His 485 490 495 Val His Met Ser Ser Gly Ser Phe Ile Asn Ile Ser Val Val Gly Pro 500 505 510 Ala Leu Thr Phe Arg Ile Arg His Asn Glu Gln Asn Leu Ser Leu Ala 515 520 525 Asp Val Thr Gln Gln Ala Gly Leu Val Lys Ser Glu Leu Glu Ala Gln 530 535 540 Thr Gly Leu Gln Ile Leu Gln Thr Gly Val Gly Gln Arg Glu Glu Ala 545 550 555 560 Ala Ala Val Leu Pro Gln Thr Ala His Ser Thr Ser Pro Met Arg Ser 565 570 575 Val Leu Leu Thr Leu Val Ala Leu Ala Gly Val Ala Gly Leu Leu Val 580 585 590 Ala Leu Ala Val Ala Leu Cys Val Arg Gln His Ala Arg Gln Gln Asp 595 600 605 Lys Glu Arg Leu Ala Ala Leu Gly Pro Glu Gly Ala His Gly Asp Thr 610 615 620 Thr Phe Glu Tyr Gln Asp Leu Cys Arg Gln His Met Ala Thr Lys Ser 625 630 635 640 Leu Phe Asn Arg Ala Glu Gly Pro Pro Glu Pro Ser Arg Val Ser Ser 645 650 655 Val Ser Ser Gln Phe Ser Asp Ala Ala Gln Ala Ser Pro Ser Ser His 660 665 670 Ser Ser Thr Pro Ser Trp Cys Glu Glu Pro Ala Gln Ala Asn Met Asp 675 680 685 Ile Ser Thr Gly His Met Ile Leu Ala Tyr Met Glu Asp His Leu Arg 690 695 700 Asn Arg Asp Arg Leu Ala Lys Glu Trp Gln Ala Leu Cys Ala Tyr Gln 705 710 715 720 Ala Glu Pro Asn Thr Cys Ala Thr Ala Gln Gly Glu Gly Asn Ile Lys 725 730 735 Lys Asn Arg His Pro Asp Phe Leu Pro Tyr Asp His Ala Arg Ile Lys 740 745 750 Leu Lys Val Glu Ser Ser Pro Ser Arg Ser Asp Tyr Ile Asn Ala Ser 755 760 765 Pro Ile Ile Glu His Asp Pro Arg Met Pro Ala Tyr Ile Ala Thr Gln 770 775 780 Gly Pro Leu Ser His Thr Ile Ala Asp Phe Trp Gln Met Val Trp Glu 785 790 795 800 Ser Gly Cys Thr Val Ile Val Met Leu Thr Pro Leu Val Glu Asp Gly 805 810 815 Val Lys Gln Cys Asp Arg Tyr Trp Pro Asp Glu Gly Ala Ser Leu Tyr 820 825 830 His Val Tyr Glu Val Asn Leu Val Ser Glu His Ile Trp Cys Glu Asp 835 840 845 Phe Leu Val Arg Ser Phe Tyr Leu Lys Asn Val Gln Thr Gln Glu Thr 850 855 860 Arg Thr Leu Thr Gln Phe His Phe Leu Ser Trp Pro Ala Glu Gly Thr 865 870 875 880 Pro Ala Ser Thr Arg Pro Leu Leu Asp Phe Arg Arg Lys Val Asn Lys 885 890 895 Cys Tyr Arg Gly Arg Ser Cys Pro Ile Ile Val His Cys Ser Asp Gly 900 905 910 Ala Gly Arg Thr Gly Thr Tyr Ile Leu Ile Asp Met Val Leu Asn Arg 915 920 925 Met Ala Lys Gly Val Lys Glu Ile Asp Ile Ala Ala Thr Leu Glu His 930 935 940 Val Arg Asp Gln Arg Pro Gly Leu Val Arg Ser Lys Asp Gln Phe Glu 945 950 955 960 Phe Ala Leu Thr Ala Val Ala Glu Glu Val Asn Ala Ile Leu Lys Ala 965 970 975 Leu Pro Gln

<210> SEQ ID NO 32 <211> LENGTH: 807 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9Y2R2 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(807) <400> SEQUENCE: 32 Met Asp Gln Arg Glu Ile Leu Gln Lys Phe Leu Asp Glu Ala Gln Ser 1 5 10 15 Lys Lys Ile Thr Lys Glu Glu Phe Ala Asn Glu Phe Leu Lys Leu Lys 20 25 30 Arg Gln Ser Thr Lys Tyr Lys Ala Asp Lys Thr Tyr Pro Thr Thr Val 35 40 45 Ala Glu Lys Pro Lys Asn Ile Lys Lys Asn Arg Tyr Lys Asp Ile Leu 50 55 60 Pro Tyr Asp Tyr Ser Arg Val Glu Leu Ser Leu Ile Thr Ser Asp Glu 65 70 75 80 Asp Ser Ser Tyr Ile Asn Ala Asn Phe Ile Lys Gly Val Tyr Gly Pro 85 90 95 Lys Ala Tyr Ile Ala Thr Gln Gly Pro Leu Ser Thr Thr Leu Leu Asp 100 105 110 Phe Trp Arg Met Ile Trp Glu Tyr Ser Val Leu Ile Ile Val Met Ala 115 120 125 Cys Met Glu Tyr Glu Met Gly Lys Lys Lys Cys Glu Arg Tyr Trp Ala 130 135 140 Glu Pro Gly Glu Met Gln Leu Glu Phe Gly Pro Phe Ser Val Ser Cys 145 150 155 160 Glu Ala Glu Lys Arg Lys Ser Asp Tyr Ile Ile Arg Thr Leu Lys Val 165 170 175 Lys Phe Asn Ser Glu Thr Arg Thr Ile Tyr Gln Phe His Tyr Lys Asn 180 185 190 Trp Pro Asp His Asp Val Pro Ser Ser Ile Asp Pro Ile Leu Glu Leu 195 200 205 Ile Trp Asp Val Arg Cys Tyr Gln Glu Asp Asp Ser Val Pro Ile Cys 210 215 220 Ile His Cys Ser Ala Gly Cys Gly Arg Thr Gly Val Ile Cys Ala Ile 225 230 235 240 Asp Tyr Thr Trp Met Leu Leu Lys Asp Gly Ile Ile Pro Glu Asn Phe 245 250 255 Ser Val Phe Ser Leu Ile Arg Glu Met Arg Thr Gln Arg Pro Ser Leu 260 265 270 Val Gln Thr Gln Glu Gln Tyr Glu Leu Val Tyr Asn Ala Val Leu Glu 275 280 285 Leu Phe Lys Arg Gln Met Asp Val Ile Arg Asp Lys His Ser Gly Thr 290 295 300 Glu Ser Gln Ala Lys His Cys Ile Pro Glu Lys Asn His Thr Leu Gln 305 310 315 320 Ala Asp Ser Tyr Ser Pro Asn Leu Pro Lys Ser Thr Thr Lys Ala Ala 325 330 335 Lys Met Met Asn Gln Gln Arg Thr Lys Met Glu Ile Lys Glu Ser Ser 340 345 350 Ser Phe Asp Phe Arg Thr Ser Glu Ile Ser Ala Lys Glu Glu Leu Val 355 360 365 Leu His Pro Ala Lys Ser Ser Thr Ser Phe Asp Phe Leu Glu Leu Asn 370 375 380 Tyr Ser Phe Asp Lys Asn Ala Asp Thr Thr Met Lys Trp Gln Thr Lys 385 390 395 400 Ala Phe Pro Ile Val Gly Glu Pro Leu Gln Lys His Gln Ser Leu Asp 405 410 415 Leu Gly Ser Leu Leu Phe Glu Gly Cys Ser Asn Ser Lys Pro Val Asn 420 425 430 Ala Ala Gly Arg Tyr Phe Asn Ser Lys Val Pro Ile Thr Arg Thr Lys 435 440 445 Ser Thr Pro Phe Glu Leu Ile Gln Gln Arg Glu Thr Lys Glu Val Asp 450 455 460 Ser Lys Glu Asn Phe Ser Tyr Leu Glu Ser Gln Pro His Asp Ser Cys 465 470 475 480 Phe Val Glu Met Gln Ala Gln Lys Val Met His Val Ser Ser Ala Glu 485 490 495 Leu Asn Tyr Ser Leu Pro Tyr Asp Ser Lys His Gln Ile Arg Asn Ala 500 505 510 Ser Asn Val Lys His His Asp Ser Ser Ala Leu Gly Val Tyr Ser Tyr 515 520 525 Ile Pro Leu Val Glu Asn Pro Tyr Phe Ser Ser Trp Pro Pro Ser Gly 530 535 540 Thr Ser Ser Lys Met Ser Leu Asp Leu Pro Glu Lys Gln Asp Gly Thr 545 550 555 560 Val Phe Pro Ser Ser Leu Leu Pro Thr Ser Ser Thr Ser Leu Phe Ser 565 570 575 Tyr Tyr Asn Ser His Asp Ser Leu Ser Leu Asn Ser Pro Thr Asn Ile 580 585 590 Ser Ser Leu Leu Asn Gln Glu Ser Ala Val Leu Ala Thr Ala Pro Arg 595 600 605 Ile Asp Asp Glu Ile Pro Pro Pro Leu Pro Val Arg Thr Pro Glu Ser 610 615 620 Phe Ile Val Val Glu Glu Ala Gly Glu Phe Ser Pro Asn Val Pro Lys 625 630 635 640 Ser Leu Ser Ser Ala Val Lys Val Lys Ile Gly Thr Ser Leu Glu Trp 645 650 655 Gly Gly Thr Ser Glu Pro Lys Lys Phe Asp Asp Ser Val Ile Leu Arg 660 665 670 Pro Ser Lys Ser Val Lys Leu Arg Ser Pro Lys Ser Glu Leu His Gln 675 680 685 Asp Arg Ser Ser Pro Pro Pro Pro Leu Pro Glu Arg Thr Leu Glu Ser 690 695 700 Phe Phe Leu Ala Asp Glu Asp Cys Met Gln Ala Gln Ser Ile Glu Thr 705 710 715 720 Tyr Ser Thr Ser Tyr Pro Asp Thr Met Glu Asn Ser Thr Ser Ser Lys 725 730 735 Gln Thr Leu Lys Thr Pro Gly Lys Ser Phe Thr Arg Ser Lys Ser Leu 740 745 750 Lys Ile Leu Arg Asn Met Lys Lys Ser Ile Cys Asn Ser Cys Pro Pro 755 760 765 Asn Lys Pro Ala Glu Ser Val Gln Ser Asn Asn Ser Ser Ser Phe Leu 770 775 780 Asn Phe Gly Phe Ala Asn Arg Phe Ser Lys Pro Lys Gly Pro Arg Asn 785 790 795 800 Pro Pro Pro Thr Trp Asn Ile 805 <210> SEQ ID NO 33 <211> LENGTH: 248 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P18124 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(248) <400> SEQUENCE: 33 Met Glu Gly Val Glu Glu Lys Lys Lys Glu Val Pro Ala Val Pro Glu 1 5 10 15 Thr Leu Lys Lys Lys Arg Arg Asn Phe Ala Glu Leu Lys Ile Lys Arg 20 25 30 Leu Arg Lys Lys Phe Ala Gln Lys Met Leu Arg Lys Ala Arg Arg Lys 35 40 45 Leu Ile Tyr Glu Lys Ala Lys His Tyr His Lys Glu Tyr Arg Gln Met 50 55 60 Tyr Arg Thr Glu Ile Arg Met Ala Arg Met Ala Arg Lys Ala Gly Asn 65 70 75 80 Phe Tyr Val Pro Ala Glu Pro Lys Leu Ala Phe Val Ile Arg Ile Arg 85 90 95 Gly Ile Asn Gly Val Ser Pro Lys Val Arg Lys Val Leu Gln Leu Leu 100 105 110 Arg Leu Arg Gln Ile Phe Asn Gly Thr Phe Val Lys Leu Asn Lys Ala 115 120 125 Ser Ile Asn Met Leu Arg Ile Val Glu Pro Tyr Ile Ala Trp Gly Tyr 130 135 140 Pro Asn Leu Lys Ser Val Asn Glu Leu Ile Tyr Lys Arg Gly Tyr Gly 145 150 155 160 Lys Ile Asn Lys Lys Arg Ile Ala Leu Thr Asp Asn Ala Leu Ile Ala 165 170 175 Arg Ser Leu Gly Lys Tyr Gly Ile Ile Cys Met Glu Asp Leu Ile His 180 185 190 Glu Ile Tyr Thr Val Gly Lys Arg Phe Lys Glu Ala Asn Asn Phe Leu 195 200 205 Trp Pro Phe Lys Leu Ser Ser Pro Arg Gly Gly Met Lys Lys Lys Thr 210 215 220 Thr His Phe Val Glu Gly Gly Asp Ala Gly Asn Arg Glu Asp Gln Ile 225 230 235 240 Asn Arg Leu Ile Arg Arg Met Asn 245 <210> SEQ ID NO 34 <211> LENGTH: 313 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q5MJ70 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(313) <400> SEQUENCE: 34 Met Arg His Asn Gln Met Cys Cys Glu Thr Pro Pro Thr Val Thr Val 1 5 10 15 Tyr Val Lys Ser Gly Ser Asn Arg Ser His Gln Pro Lys Lys Pro Ile 20 25 30 Thr Leu Lys Arg Pro Ile Cys Lys Asp Asn Trp Gln Ala Phe Glu Lys 35 40 45 Asn Thr His Asn Asn Asn Lys Ser Lys Arg Pro Lys Gly Pro Cys Leu 50 55 60 Val Ile Gln Arg Gln Asp Met Thr Ala Phe Phe Lys Leu Phe Asp Asp

65 70 75 80 Asp Leu Ile Gln Asp Phe Leu Trp Met Asp Cys Cys Cys Lys Ile Ala 85 90 95 Asp Lys Tyr Leu Leu Ala Met Thr Phe Val Tyr Phe Lys Arg Ala Lys 100 105 110 Phe Thr Ile Ser Glu His Thr Arg Ile Asn Phe Phe Ile Ala Leu Tyr 115 120 125 Leu Ala Asn Thr Val Glu Glu Asp Glu Glu Glu Thr Lys Tyr Glu Ile 130 135 140 Phe Pro Trp Ala Leu Gly Lys Asn Trp Arg Lys Leu Phe Pro Asn Phe 145 150 155 160 Leu Lys Leu Arg Asp Gln Leu Trp Asp Arg Ile Asp Tyr Arg Ala Ile 165 170 175 Val Ser Arg Arg Cys Cys Glu Glu Val Met Ala Ile Ala Pro Thr His 180 185 190 Tyr Ile Trp Gln Arg Glu Arg Ser Val His His Ser Gly Ala Val Arg 195 200 205 Asn Tyr Asn Arg Asp Glu Val Gln Leu Pro Arg Gly Pro Ser Ala Thr 210 215 220 Pro Val Asp Cys Ser Leu Cys Gly Lys Lys Arg Arg Tyr Val Arg Leu 225 230 235 240 Gly Leu Ser Ser Ser Ser Ser Leu Ser Ser His Thr Ala Gly Val Thr 245 250 255 Glu Lys His Ser Gln Asp Ser Tyr Asn Ser Leu Ser Met Asp Ile Ile 260 265 270 Gly Asp Pro Ser Gln Ala Tyr Thr Gly Ser Glu Val Val Asn Asp His 275 280 285 Gln Ser Asn Lys Gly Lys Lys Thr Asn Phe Leu Lys Lys Asp Lys Ser 290 295 300 Met Glu Trp Phe Thr Gly Ser Glu Glu 305 310 <210> SEQ ID NO 35 <211> LENGTH: 233 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01375 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(233) <400> SEQUENCE: 35 Met Ser Thr Glu Ser Met Ile Arg Asp Val Glu Leu Ala Glu Glu Ala 1 5 10 15 Leu Pro Lys Lys Thr Gly Gly Pro Gln Gly Ser Arg Arg Cys Leu Phe 20 25 30 Leu Ser Leu Phe Ser Phe Leu Ile Val Ala Gly Ala Thr Thr Leu Phe 35 40 45 Cys Leu Leu His Phe Gly Val Ile Gly Pro Gln Arg Glu Glu Phe Pro 50 55 60 Arg Asp Leu Ser Leu Ile Ser Pro Leu Ala Gln Ala Val Arg Ser Ser 65 70 75 80 Ser Arg Thr Pro Ser Asp Lys Pro Val Ala His Val Val Ala Asn Pro 85 90 95 Gln Ala Glu Gly Gln Leu Gln Trp Leu Asn Arg Arg Ala Asn Ala Leu 100 105 110 Leu Ala Asn Gly Val Glu Leu Arg Asp Asn Gln Leu Val Val Pro Ser 115 120 125 Glu Gly Leu Tyr Leu Ile Tyr Ser Gln Val Leu Phe Lys Gly Gln Gly 130 135 140 Cys Pro Ser Thr His Val Leu Leu Thr His Thr Ile Ser Arg Ile Ala 145 150 155 160 Val Ser Tyr Gln Thr Lys Val Asn Leu Leu Ser Ala Ile Lys Ser Pro 165 170 175 Cys Gln Arg Glu Thr Pro Glu Gly Ala Glu Ala Lys Pro Trp Tyr Glu 180 185 190 Pro Ile Tyr Leu Gly Gly Val Phe Gln Leu Glu Lys Gly Asp Arg Leu 195 200 205 Ser Ala Glu Ile Asn Arg Pro Asp Tyr Leu Asp Phe Ala Glu Ser Gly 210 215 220 Gln Val Tyr Phe Gly Ile Ile Ala Leu 225 230 <210> SEQ ID NO 36 <211> LENGTH: 175 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q06141 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(175) <400> SEQUENCE: 36 Met Leu Pro Pro Met Ala Leu Pro Ser Val Ser Trp Met Leu Leu Ser 1 5 10 15 Cys Leu Met Leu Leu Ser Gln Val Gln Gly Glu Glu Pro Gln Arg Glu 20 25 30 Leu Pro Ser Ala Arg Ile Arg Cys Pro Lys Gly Ser Lys Ala Tyr Gly 35 40 45 Ser His Cys Tyr Ala Leu Phe Leu Ser Pro Lys Ser Trp Thr Asp Ala 50 55 60 Asp Leu Ala Cys Gln Lys Arg Pro Ser Gly Asn Leu Val Ser Val Leu 65 70 75 80 Ser Gly Ala Glu Gly Ser Phe Val Ser Ser Leu Val Lys Ser Ile Gly 85 90 95 Asn Ser Tyr Ser Tyr Val Trp Ile Gly Leu His Asp Pro Thr Gln Gly 100 105 110 Thr Glu Pro Asn Gly Glu Gly Trp Glu Trp Ser Ser Ser Asp Val Met 115 120 125 Asn Tyr Phe Ala Trp Glu Arg Asn Pro Ser Thr Ile Ser Ser Pro Gly 130 135 140 His Cys Ala Ser Leu Ser Arg Ser Thr Ala Phe Leu Arg Trp Lys Asp 145 150 155 160 Tyr Asn Cys Asn Val Arg Leu Pro Tyr Val Cys Lys Phe Thr Asp 165 170 175 <210> SEQ ID NO 37 <211> LENGTH: 1342 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P21860 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1342) <400> SEQUENCE: 37 Met Arg Ala Asn Asp Ala Leu Gln Val Leu Gly Leu Leu Phe Ser Leu 1 5 10 15 Ala Arg Gly Ser Glu Val Gly Asn Ser Gln Ala Val Cys Pro Gly Thr 20 25 30 Leu Asn Gly Leu Ser Val Thr Gly Asp Ala Glu Asn Gln Tyr Gln Thr 35 40 45 Leu Tyr Lys Leu Tyr Glu Arg Cys Glu Val Val Met Gly Asn Leu Glu 50 55 60 Ile Val Leu Thr Gly His Asn Ala Asp Leu Ser Phe Leu Gln Trp Ile 65 70 75 80 Arg Glu Val Thr Gly Tyr Val Leu Val Ala Met Asn Glu Phe Ser Thr 85 90 95 Leu Pro Leu Pro Asn Leu Arg Val Val Arg Gly Thr Gln Val Tyr Asp 100 105 110 Gly Lys Phe Ala Ile Phe Val Met Leu Asn Tyr Asn Thr Asn Ser Ser 115 120 125 His Ala Leu Arg Gln Leu Arg Leu Thr Gln Leu Thr Glu Ile Leu Ser 130 135 140 Gly Gly Val Tyr Ile Glu Lys Asn Asp Lys Leu Cys His Met Asp Thr 145 150 155 160 Ile Asp Trp Arg Asp Ile Val Arg Asp Arg Asp Ala Glu Ile Val Val 165 170 175 Lys Asp Asn Gly Arg Ser Cys Pro Pro Cys His Glu Val Cys Lys Gly 180 185 190 Arg Cys Trp Gly Pro Gly Ser Glu Asp Cys Gln Thr Leu Thr Lys Thr 195 200 205 Ile Cys Ala Pro Gln Cys Asn Gly His Cys Phe Gly Pro Asn Pro Asn 210 215 220 Gln Cys Cys His Asp Glu Cys Ala Gly Gly Cys Ser Gly Pro Gln Asp 225 230 235 240 Thr Asp Cys Phe Ala Cys Arg His Phe Asn Asp Ser Gly Ala Cys Val 245 250 255 Pro Arg Cys Pro Gln Pro Leu Val Tyr Asn Lys Leu Thr Phe Gln Leu 260 265 270 Glu Pro Asn Pro His Thr Lys Tyr Gln Tyr Gly Gly Val Cys Val Ala 275 280 285 Ser Cys Pro His Asn Phe Val Val Asp Gln Thr Ser Cys Val Arg Ala 290 295 300 Cys Pro Pro Asp Lys Met Glu Val Asp Lys Asn Gly Leu Lys Met Cys 305 310 315 320 Glu Pro Cys Gly Gly Leu Cys Pro Lys Ala Cys Glu Gly Thr Gly Ser 325 330 335 Gly Ser Arg Phe Gln Thr Val Asp Ser Ser Asn Ile Asp Gly Phe Val 340 345 350 Asn Cys Thr Lys Ile Leu Gly Asn Leu Asp Phe Leu Ile Thr Gly Leu 355 360 365 Asn Gly Asp Pro Trp His Lys Ile Pro Ala Leu Asp Pro Glu Lys Leu 370 375 380 Asn Val Phe Arg Thr Val Arg Glu Ile Thr Gly Tyr Leu Asn Ile Gln 385 390 395 400 Ser Trp Pro Pro His Met His Asn Phe Ser Val Phe Ser Asn Leu Thr 405 410 415 Thr Ile Gly Gly Arg Ser Leu Tyr Asn Arg Gly Phe Ser Leu Leu Ile 420 425 430 Met Lys Asn Leu Asn Val Thr Ser Leu Gly Phe Arg Ser Leu Lys Glu 435 440 445 Ile Ser Ala Gly Arg Ile Tyr Ile Ser Ala Asn Arg Gln Leu Cys Tyr 450 455 460 His His Ser Leu Asn Trp Thr Lys Val Leu Arg Gly Pro Thr Glu Glu 465 470 475 480

Arg Leu Asp Ile Lys His Asn Arg Pro Arg Arg Asp Cys Val Ala Glu 485 490 495 Gly Lys Val Cys Asp Pro Leu Cys Ser Ser Gly Gly Cys Trp Gly Pro 500 505 510 Gly Pro Gly Gln Cys Leu Ser Cys Arg Asn Tyr Ser Arg Gly Gly Val 515 520 525 Cys Val Thr His Cys Asn Phe Leu Asn Gly Glu Pro Arg Glu Phe Ala 530 535 540 His Glu Ala Glu Cys Phe Ser Cys His Pro Glu Cys Gln Pro Met Glu 545 550 555 560 Gly Thr Ala Thr Cys Asn Gly Ser Gly Ser Asp Thr Cys Ala Gln Cys 565 570 575 Ala His Phe Arg Asp Gly Pro His Cys Val Ser Ser Cys Pro His Gly 580 585 590 Val Leu Gly Ala Lys Gly Pro Ile Tyr Lys Tyr Pro Asp Val Gln Asn 595 600 605 Glu Cys Arg Pro Cys His Glu Asn Cys Thr Gln Gly Cys Lys Gly Pro 610 615 620 Glu Leu Gln Asp Cys Leu Gly Gln Thr Leu Val Leu Ile Gly Lys Thr 625 630 635 640 His Leu Thr Met Ala Leu Thr Val Ile Ala Gly Leu Val Val Ile Phe 645 650 655 Met Met Leu Gly Gly Thr Phe Leu Tyr Trp Arg Gly Arg Arg Ile Gln 660 665 670 Asn Lys Arg Ala Met Arg Arg Tyr Leu Glu Arg Gly Glu Ser Ile Glu 675 680 685 Pro Leu Asp Pro Ser Glu Lys Ala Asn Lys Val Leu Ala Arg Ile Phe 690 695 700 Lys Glu Thr Glu Leu Arg Lys Leu Lys Val Leu Gly Ser Gly Val Phe 705 710 715 720 Gly Thr Val His Lys Gly Val Trp Ile Pro Glu Gly Glu Ser Ile Lys 725 730 735 Ile Pro Val Cys Ile Lys Val Ile Glu Asp Lys Ser Gly Arg Gln Ser 740 745 750 Phe Gln Ala Val Thr Asp His Met Leu Ala Ile Gly Ser Leu Asp His 755 760 765 Ala His Ile Val Arg Leu Leu Gly Leu Cys Pro Gly Ser Ser Leu Gln 770 775 780 Leu Val Thr Gln Tyr Leu Pro Leu Gly Ser Leu Leu Asp His Val Arg 785 790 795 800 Gln His Arg Gly Ala Leu Gly Pro Gln Leu Leu Leu Asn Trp Gly Val 805 810 815 Gln Ile Ala Lys Gly Met Tyr Tyr Leu Glu Glu His Gly Met Val His 820 825 830 Arg Asn Leu Ala Ala Arg Asn Val Leu Leu Lys Ser Pro Ser Gln Val 835 840 845 Gln Val Ala Asp Phe Gly Val Ala Asp Leu Leu Pro Pro Asp Asp Lys 850 855 860 Gln Leu Leu Tyr Ser Glu Ala Lys Thr Pro Ile Lys Trp Met Ala Leu 865 870 875 880 Glu Ser Ile His Phe Gly Lys Tyr Thr His Gln Ser Asp Val Trp Ser 885 890 895 Tyr Gly Val Thr Val Trp Glu Leu Met Thr Phe Gly Ala Glu Pro Tyr 900 905 910 Ala Gly Leu Arg Leu Ala Glu Val Pro Asp Leu Leu Glu Lys Gly Glu 915 920 925 Arg Leu Ala Gln Pro Gln Ile Cys Thr Ile Asp Val Tyr Met Val Met 930 935 940 Val Lys Cys Trp Met Ile Asp Glu Asn Ile Arg Pro Thr Phe Lys Glu 945 950 955 960 Leu Ala Asn Glu Phe Thr Arg Met Ala Arg Asp Pro Pro Arg Tyr Leu 965 970 975 Val Ile Lys Arg Glu Ser Gly Pro Gly Ile Ala Pro Gly Pro Glu Pro 980 985 990 His Gly Leu Thr Asn Lys Lys Leu Glu Glu Val Glu Leu Glu Pro Glu 995 1000 1005 Leu Asp Leu Asp Leu Asp Leu Glu Ala Glu Glu Asp Asn Leu Ala 1010 1015 1020 Thr Thr Thr Leu Gly Ser Ala Leu Ser Leu Pro Val Gly Thr Leu 1025 1030 1035 Asn Arg Pro Arg Gly Ser Gln Ser Leu Leu Ser Pro Ser Ser Gly 1040 1045 1050 Tyr Met Pro Met Asn Gln Gly Asn Leu Gly Glu Ser Cys Gln Glu 1055 1060 1065 Ser Ala Val Ser Gly Ser Ser Glu Arg Cys Pro Arg Pro Val Ser 1070 1075 1080 Leu His Pro Met Pro Arg Gly Cys Leu Ala Ser Glu Ser Ser Glu 1085 1090 1095 Gly His Val Thr Gly Ser Glu Ala Glu Leu Gln Glu Lys Val Ser 1100 1105 1110 Met Cys Arg Ser Arg Ser Arg Ser Arg Ser Pro Arg Pro Arg Gly 1115 1120 1125 Asp Ser Ala Tyr His Ser Gln Arg His Ser Leu Leu Thr Pro Val 1130 1135 1140 Thr Pro Leu Ser Pro Pro Gly Leu Glu Glu Glu Asp Val Asn Gly 1145 1150 1155 Tyr Val Met Pro Asp Thr His Leu Lys Gly Thr Pro Ser Ser Arg 1160 1165 1170 Glu Gly Thr Leu Ser Ser Val Gly Leu Ser Ser Val Leu Gly Thr 1175 1180 1185 Glu Glu Glu Asp Glu Asp Glu Glu Tyr Glu Tyr Met Asn Arg Arg 1190 1195 1200 Arg Arg His Ser Pro Pro His Pro Pro Arg Pro Ser Ser Leu Glu 1205 1210 1215 Glu Leu Gly Tyr Glu Tyr Met Asp Val Gly Ser Asp Leu Ser Ala 1220 1225 1230 Ser Leu Gly Ser Thr Gln Ser Cys Pro Leu His Pro Val Pro Ile 1235 1240 1245 Met Pro Thr Ala Gly Thr Thr Pro Asp Glu Asp Tyr Glu Tyr Met 1250 1255 1260 Asn Arg Gln Arg Asp Gly Gly Gly Pro Gly Gly Asp Tyr Ala Ala 1265 1270 1275 Met Gly Ala Cys Pro Ala Ser Glu Gln Gly Tyr Glu Glu Met Arg 1280 1285 1290 Ala Phe Gln Gly Pro Gly His Gln Ala Pro His Val His Tyr Ala 1295 1300 1305 Arg Leu Lys Thr Leu Arg Ser Leu Glu Ala Thr Asp Ser Ala Phe 1310 1315 1320 Asp Asn Pro Asp Tyr Trp His Ser Arg Leu Phe Pro Lys Ala Asn 1325 1330 1335 Ala Gln Arg Thr 1340 <210> SEQ ID NO 38 <211> LENGTH: 472 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16671 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(472) <400> SEQUENCE: 38 Met Gly Cys Asp Arg Asn Cys Gly Leu Ile Ala Gly Ala Val Ile Gly 1 5 10 15 Ala Val Leu Ala Val Phe Gly Gly Ile Leu Met Pro Val Gly Asp Leu 20 25 30 Leu Ile Gln Lys Thr Ile Lys Lys Gln Val Val Leu Glu Glu Gly Thr 35 40 45 Ile Ala Phe Lys Asn Trp Val Lys Thr Gly Thr Glu Val Tyr Arg Gln 50 55 60 Phe Trp Ile Phe Asp Val Gln Asn Pro Gln Glu Val Met Met Asn Ser 65 70 75 80 Ser Asn Ile Gln Val Lys Gln Arg Gly Pro Tyr Thr Tyr Arg Val Arg 85 90 95 Phe Leu Ala Lys Glu Asn Val Thr Gln Asp Ala Glu Asp Asn Thr Val 100 105 110 Ser Phe Leu Gln Pro Asn Gly Ala Ile Phe Glu Pro Ser Leu Ser Val 115 120 125 Gly Thr Glu Ala Asp Asn Phe Thr Val Leu Asn Leu Ala Val Ala Ala 130 135 140 Ala Ser His Ile Tyr Gln Asn Gln Phe Val Gln Met Ile Leu Asn Ser 145 150 155 160 Leu Ile Asn Lys Ser Lys Ser Ser Met Phe Gln Val Arg Thr Leu Arg 165 170 175 Glu Leu Leu Trp Gly Tyr Arg Asp Pro Phe Leu Ser Leu Val Pro Tyr 180 185 190 Pro Val Thr Thr Thr Val Gly Leu Phe Tyr Pro Tyr Asn Asn Thr Ala 195 200 205 Asp Gly Val Tyr Lys Val Phe Asn Gly Lys Asp Asn Ile Ser Lys Val 210 215 220 Ala Ile Ile Asp Thr Tyr Lys Gly Lys Arg Asn Leu Ser Tyr Trp Glu 225 230 235 240 Ser His Cys Asp Met Ile Asn Gly Thr Asp Ala Ala Ser Phe Pro Pro 245 250 255 Phe Val Glu Lys Ser Gln Val Leu Gln Phe Phe Ser Ser Asp Ile Cys 260 265 270 Arg Ser Ile Tyr Ala Val Phe Glu Ser Asp Val Asn Leu Lys Gly Ile 275 280 285 Pro Val Tyr Arg Phe Val Leu Pro Ser Lys Ala Phe Ala Ser Pro Val 290 295 300 Glu Asn Pro Asp Asn Tyr Cys Phe Cys Thr Glu Lys Ile Ile Ser Lys 305 310 315 320 Asn Cys Thr Ser Tyr Gly Val Leu Asp Ile Ser Lys Cys Lys Glu Gly 325 330 335 Arg Pro Val Tyr Ile Ser Leu Pro His Phe Leu Tyr Ala Ser Pro Asp 340 345 350 Val Ser Glu Pro Ile Asp Gly Leu Asn Pro Asn Glu Glu Glu His Arg 355 360 365 Thr Tyr Leu Asp Ile Glu Pro Ile Thr Gly Phe Thr Leu Gln Phe Ala 370 375 380

Lys Arg Leu Gln Val Asn Leu Leu Val Lys Pro Ser Glu Lys Ile Gln 385 390 395 400 Val Leu Lys Asn Leu Lys Arg Asn Tyr Ile Val Pro Ile Leu Trp Leu 405 410 415 Asn Glu Thr Gly Thr Ile Gly Asp Glu Lys Ala Asn Met Phe Arg Ser 420 425 430 Gln Val Thr Gly Lys Ile Asn Leu Leu Gly Leu Ile Glu Met Ile Leu 435 440 445 Leu Ser Val Gly Val Val Met Phe Val Ala Phe Met Ile Ser Tyr Cys 450 455 460 Ala Cys Arg Ser Lys Thr Ile Lys 465 470 <210> SEQ ID NO 39 <211> LENGTH: 710 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P19338 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(710) <400> SEQUENCE: 39 Met Val Lys Leu Ala Lys Ala Gly Lys Asn Gln Gly Asp Pro Lys Lys 1 5 10 15 Met Ala Pro Pro Pro Lys Glu Val Glu Glu Asp Ser Glu Asp Glu Glu 20 25 30 Met Ser Glu Asp Glu Glu Asp Asp Ser Ser Gly Glu Glu Val Val Ile 35 40 45 Pro Gln Lys Lys Gly Lys Lys Ala Ala Ala Thr Ser Ala Lys Lys Val 50 55 60 Val Val Ser Pro Thr Lys Lys Val Ala Val Ala Thr Pro Ala Lys Lys 65 70 75 80 Ala Ala Val Thr Pro Gly Lys Lys Ala Ala Ala Thr Pro Ala Lys Lys 85 90 95 Thr Val Thr Pro Ala Lys Ala Val Thr Thr Pro Gly Lys Lys Gly Ala 100 105 110 Thr Pro Gly Lys Ala Leu Val Ala Thr Pro Gly Lys Lys Gly Ala Ala 115 120 125 Ile Pro Ala Lys Gly Ala Lys Asn Gly Lys Asn Ala Lys Lys Glu Asp 130 135 140 Ser Asp Glu Glu Glu Asp Asp Asp Ser Glu Glu Asp Glu Glu Asp Asp 145 150 155 160 Glu Asp Glu Asp Glu Asp Glu Asp Glu Ile Glu Pro Ala Ala Met Lys 165 170 175 Ala Ala Ala Ala Ala Pro Ala Ser Glu Asp Glu Asp Asp Glu Asp Asp 180 185 190 Glu Asp Asp Glu Asp Asp Asp Asp Asp Glu Glu Asp Asp Ser Glu Glu 195 200 205 Glu Ala Met Glu Thr Thr Pro Ala Lys Gly Lys Lys Ala Ala Lys Val 210 215 220 Val Pro Val Lys Ala Lys Asn Val Ala Glu Asp Glu Asp Glu Glu Glu 225 230 235 240 Asp Asp Glu Asp Glu Asp Asp Asp Asp Asp Glu Asp Asp Glu Asp Asp 245 250 255 Asp Asp Glu Asp Asp Glu Glu Glu Glu Glu Glu Glu Glu Glu Glu Pro 260 265 270 Val Lys Glu Ala Pro Gly Lys Arg Lys Lys Glu Met Ala Lys Gln Lys 275 280 285 Ala Ala Pro Glu Ala Lys Lys Gln Lys Val Glu Gly Thr Glu Pro Thr 290 295 300 Thr Ala Phe Asn Leu Phe Val Gly Asn Leu Asn Phe Asn Lys Ser Ala 305 310 315 320 Pro Glu Leu Lys Thr Gly Ile Ser Asp Val Phe Ala Lys Asn Asp Leu 325 330 335 Ala Val Val Asp Val Arg Ile Gly Met Thr Arg Lys Phe Gly Tyr Val 340 345 350 Asp Phe Glu Ser Ala Glu Asp Leu Glu Lys Ala Leu Glu Leu Thr Gly 355 360 365 Leu Lys Val Phe Gly Asn Glu Ile Lys Leu Glu Lys Pro Lys Gly Lys 370 375 380 Asp Ser Lys Lys Glu Arg Asp Ala Arg Thr Leu Leu Ala Lys Asn Leu 385 390 395 400 Pro Tyr Lys Val Thr Gln Asp Glu Leu Lys Glu Val Phe Glu Asp Ala 405 410 415 Ala Glu Ile Arg Leu Val Ser Lys Asp Gly Lys Ser Lys Gly Ile Ala 420 425 430 Tyr Ile Glu Phe Lys Thr Glu Ala Asp Ala Glu Lys Thr Phe Glu Glu 435 440 445 Lys Gln Gly Thr Glu Ile Asp Gly Arg Ser Ile Ser Leu Tyr Tyr Thr 450 455 460 Gly Glu Lys Gly Gln Asn Gln Asp Tyr Arg Gly Gly Lys Asn Ser Thr 465 470 475 480 Trp Ser Gly Glu Ser Lys Thr Leu Val Leu Ser Asn Leu Ser Tyr Ser 485 490 495 Ala Thr Glu Glu Thr Leu Gln Glu Val Phe Glu Lys Ala Thr Phe Ile 500 505 510 Lys Val Pro Gln Asn Gln Asn Gly Lys Ser Lys Gly Tyr Ala Phe Ile 515 520 525 Glu Phe Ala Ser Phe Glu Asp Ala Lys Glu Ala Leu Asn Ser Cys Asn 530 535 540 Lys Arg Glu Ile Glu Gly Arg Ala Ile Arg Leu Glu Leu Gln Gly Pro 545 550 555 560 Arg Gly Ser Pro Asn Ala Arg Ser Gln Pro Ser Lys Thr Leu Phe Val 565 570 575 Lys Gly Leu Ser Glu Asp Thr Thr Glu Glu Thr Leu Lys Glu Ser Phe 580 585 590 Asp Gly Ser Val Arg Ala Arg Ile Val Thr Asp Arg Glu Thr Gly Ser 595 600 605 Ser Lys Gly Phe Gly Phe Val Asp Phe Asn Ser Glu Glu Asp Ala Lys 610 615 620 Ala Ala Lys Glu Ala Met Glu Asp Gly Glu Ile Asp Gly Asn Lys Val 625 630 635 640 Thr Leu Asp Trp Ala Lys Pro Lys Gly Glu Gly Gly Phe Gly Gly Arg 645 650 655 Gly Gly Gly Arg Gly Gly Phe Gly Gly Arg Gly Gly Gly Arg Gly Gly 660 665 670 Arg Gly Gly Phe Gly Gly Arg Gly Arg Gly Gly Phe Gly Gly Arg Gly 675 680 685 Gly Phe Arg Gly Gly Arg Gly Gly Gly Gly Asp His Lys Pro Gln Gly 690 695 700 Lys Lys Thr Lys Phe Glu 705 710 <210> SEQ ID NO 40 <211> LENGTH: 303 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BY49 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(303) <400> SEQUENCE: 40 Met Ala Ser Trp Ala Lys Gly Arg Ser Tyr Leu Ala Pro Gly Leu Leu 1 5 10 15 Gln Gly Gln Val Ala Ile Val Thr Gly Gly Ala Thr Gly Ile Gly Lys 20 25 30 Ala Ile Val Lys Glu Leu Leu Glu Leu Gly Ser Asn Val Val Ile Ala 35 40 45 Ser Arg Lys Leu Glu Arg Leu Lys Ser Ala Ala Asp Glu Leu Gln Ala 50 55 60 Asn Leu Pro Pro Thr Lys Gln Ala Arg Val Ile Pro Ile Gln Cys Asn 65 70 75 80 Ile Arg Asn Glu Glu Glu Val Asn Asn Leu Val Lys Ser Thr Leu Asp 85 90 95 Thr Phe Gly Lys Ile Asn Phe Leu Val Asn Asn Gly Gly Gly Gln Phe 100 105 110 Leu Ser Pro Ala Glu His Ile Ser Ser Lys Gly Trp His Ala Val Leu 115 120 125 Glu Thr Asn Leu Thr Gly Thr Phe Tyr Met Cys Lys Ala Val Tyr Ser 130 135 140 Ser Trp Met Lys Glu His Gly Gly Ser Ile Val Asn Ile Ile Val Pro 145 150 155 160 Thr Lys Ala Gly Phe Pro Leu Ala Val His Ser Gly Ala Ala Arg Ala 165 170 175 Gly Val Tyr Asn Leu Thr Lys Ser Leu Ala Leu Glu Trp Ala Cys Ser 180 185 190 Gly Ile Arg Ile Asn Cys Val Ala Pro Gly Val Ile Tyr Ser Gln Thr 195 200 205 Ala Val Glu Asn Tyr Gly Ser Trp Gly Gln Ser Phe Phe Glu Gly Ser 210 215 220 Phe Gln Lys Ile Pro Ala Lys Arg Ile Gly Val Pro Glu Glu Val Ser 225 230 235 240 Ser Val Val Cys Phe Leu Leu Ser Pro Ala Ala Ser Phe Ile Thr Gly 245 250 255 Gln Ser Val Asp Val Asp Gly Gly Arg Ser Leu Tyr Thr His Ser Tyr 260 265 270 Glu Val Pro Asp His Asp Asn Trp Pro Lys Gly Ala Gly Asp Leu Ser 275 280 285 Val Val Lys Lys Met Lys Glu Thr Phe Lys Glu Lys Ala Lys Leu 290 295 300 <210> SEQ ID NO 41 <211> LENGTH: 475 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P19474 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(475) <400> SEQUENCE: 41 Met Ala Ser Ala Ala Arg Leu Thr Met Met Trp Glu Glu Val Thr Cys 1 5 10 15 Pro Ile Cys Leu Asp Pro Phe Val Glu Pro Val Ser Ile Glu Cys Gly

20 25 30 His Ser Phe Cys Gln Glu Cys Ile Ser Gln Val Gly Lys Gly Gly Gly 35 40 45 Ser Val Cys Pro Val Cys Arg Gln Arg Phe Leu Leu Lys Asn Leu Arg 50 55 60 Pro Asn Arg Gln Leu Ala Asn Met Val Asn Asn Leu Lys Glu Ile Ser 65 70 75 80 Gln Glu Ala Arg Glu Gly Thr Gln Gly Glu Arg Cys Ala Val His Gly 85 90 95 Glu Arg Leu His Leu Phe Cys Glu Lys Asp Gly Lys Ala Leu Cys Trp 100 105 110 Val Cys Ala Gln Ser Arg Lys His Arg Asp His Ala Met Val Pro Leu 115 120 125 Glu Glu Ala Ala Gln Glu Tyr Gln Glu Lys Leu Gln Val Ala Leu Gly 130 135 140 Glu Leu Arg Arg Lys Gln Glu Leu Ala Glu Lys Leu Glu Val Glu Ile 145 150 155 160 Ala Ile Lys Arg Ala Asp Trp Lys Lys Thr Val Glu Thr Gln Lys Ser 165 170 175 Arg Ile His Ala Glu Phe Val Gln Gln Lys Asn Phe Leu Val Glu Glu 180 185 190 Glu Gln Arg Gln Leu Gln Glu Leu Glu Lys Asp Glu Arg Glu Gln Leu 195 200 205 Arg Ile Leu Gly Glu Lys Glu Ala Lys Leu Ala Gln Gln Ser Gln Ala 210 215 220 Leu Gln Glu Leu Ile Ser Glu Leu Asp Arg Arg Cys His Ser Ser Ala 225 230 235 240 Leu Glu Leu Leu Gln Glu Val Ile Ile Val Leu Glu Arg Ser Glu Ser 245 250 255 Trp Asn Leu Lys Asp Leu Asp Ile Thr Ser Pro Glu Leu Arg Ser Val 260 265 270 Cys His Val Pro Gly Leu Lys Lys Met Leu Arg Thr Cys Ala Val His 275 280 285 Ile Thr Leu Asp Pro Asp Thr Ala Asn Pro Trp Leu Ile Leu Ser Glu 290 295 300 Asp Arg Arg Gln Val Arg Leu Gly Asp Thr Gln Gln Ser Ile Pro Gly 305 310 315 320 Asn Glu Glu Arg Phe Asp Ser Tyr Pro Met Val Leu Gly Ala Gln His 325 330 335 Phe His Ser Gly Lys His Tyr Trp Glu Val Asp Val Thr Gly Lys Glu 340 345 350 Ala Trp Asp Leu Gly Val Cys Arg Asp Ser Val Arg Arg Lys Gly His 355 360 365 Phe Leu Leu Ser Ser Lys Ser Gly Phe Trp Thr Ile Trp Leu Trp Asn 370 375 380 Lys Gln Lys Tyr Glu Ala Gly Thr Tyr Pro Gln Thr Pro Leu His Leu 385 390 395 400 Gln Val Pro Pro Cys Gln Val Gly Ile Phe Leu Asp Tyr Glu Ala Gly 405 410 415 Met Val Ser Phe Tyr Asn Ile Thr Asp His Gly Ser Leu Ile Tyr Ser 420 425 430 Phe Ser Glu Cys Ala Phe Thr Gly Pro Leu Arg Pro Phe Phe Ser Pro 435 440 445 Gly Phe Asn Asp Gly Gly Lys Asn Thr Ala Pro Leu Thr Leu Cys Pro 450 455 460 Leu Asn Ile Gly Ser Gln Gly Ser Thr Asp Tyr 465 470 475 <210> SEQ ID NO 42 <211> LENGTH: 261 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P25789 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(261) <400> SEQUENCE: 42 Met Ser Arg Arg Tyr Asp Ser Arg Thr Thr Ile Phe Ser Pro Glu Gly 1 5 10 15 Arg Leu Tyr Gln Val Glu Tyr Ala Met Glu Ala Ile Gly His Ala Gly 20 25 30 Thr Cys Leu Gly Ile Leu Ala Asn Asp Gly Val Leu Leu Ala Ala Glu 35 40 45 Arg Arg Asn Ile His Lys Leu Leu Asp Glu Val Phe Phe Ser Glu Lys 50 55 60 Ile Tyr Lys Leu Asn Glu Asp Met Ala Cys Ser Val Ala Gly Ile Thr 65 70 75 80 Ser Asp Ala Asn Val Leu Thr Asn Glu Leu Arg Leu Ile Ala Gln Arg 85 90 95 Tyr Leu Leu Gln Tyr Gln Glu Pro Ile Pro Cys Glu Gln Leu Val Thr 100 105 110 Ala Leu Cys Asp Ile Lys Gln Ala Tyr Thr Gln Phe Gly Gly Lys Arg 115 120 125 Pro Phe Gly Val Ser Leu Leu Tyr Ile Gly Trp Asp Lys His Tyr Gly 130 135 140 Phe Gln Leu Tyr Gln Ser Asp Pro Ser Gly Asn Tyr Gly Gly Trp Lys 145 150 155 160 Ala Thr Cys Ile Gly Asn Asn Ser Ala Ala Ala Val Ser Met Leu Lys 165 170 175 Gln Asp Tyr Lys Glu Gly Glu Met Thr Leu Lys Ser Ala Leu Ala Leu 180 185 190 Ala Ile Lys Val Leu Asn Lys Thr Met Asp Val Ser Lys Leu Ser Ala 195 200 205 Glu Lys Val Glu Ile Ala Thr Leu Thr Arg Glu Asn Gly Lys Thr Val 210 215 220 Ile Arg Val Leu Lys Gln Lys Glu Val Glu Gln Leu Ile Lys Lys His 225 230 235 240 Glu Glu Glu Glu Ala Lys Ala Glu Arg Glu Lys Lys Glu Lys Glu Gln 245 250 255 Lys Glu Lys Asp Lys 260 <210> SEQ ID NO 43 <211> LENGTH: 295 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P13726 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(295) <400> SEQUENCE: 43 Met Glu Thr Pro Ala Trp Pro Arg Val Pro Arg Pro Glu Thr Ala Val 1 5 10 15 Ala Arg Thr Leu Leu Leu Gly Trp Val Phe Ala Gln Val Ala Gly Ala 20 25 30 Ser Gly Thr Thr Asn Thr Val Ala Ala Tyr Asn Leu Thr Trp Lys Ser 35 40 45 Thr Asn Phe Lys Thr Ile Leu Glu Trp Glu Pro Lys Pro Val Asn Gln 50 55 60 Val Tyr Thr Val Gln Ile Ser Thr Lys Ser Gly Asp Trp Lys Ser Lys 65 70 75 80 Cys Phe Tyr Thr Thr Asp Thr Glu Cys Asp Leu Thr Asp Glu Ile Val 85 90 95 Lys Asp Val Lys Gln Thr Tyr Leu Ala Arg Val Phe Ser Tyr Pro Ala 100 105 110 Gly Asn Val Glu Ser Thr Gly Ser Ala Gly Glu Pro Leu Tyr Glu Asn 115 120 125 Ser Pro Glu Phe Thr Pro Tyr Leu Glu Thr Asn Leu Gly Gln Pro Thr 130 135 140 Ile Gln Ser Phe Glu Gln Val Gly Thr Lys Val Asn Val Thr Val Glu 145 150 155 160 Asp Glu Arg Thr Leu Val Arg Arg Asn Asn Thr Phe Leu Ser Leu Arg 165 170 175 Asp Val Phe Gly Lys Asp Leu Ile Tyr Thr Leu Tyr Tyr Trp Lys Ser 180 185 190 Ser Ser Ser Gly Lys Lys Thr Ala Lys Thr Asn Thr Asn Glu Phe Leu 195 200 205 Ile Asp Val Asp Lys Gly Glu Asn Tyr Cys Phe Ser Val Gln Ala Val 210 215 220 Ile Pro Ser Arg Thr Val Asn Arg Lys Ser Thr Asp Ser Pro Val Glu 225 230 235 240 Cys Met Gly Gln Glu Lys Gly Glu Phe Arg Glu Ile Phe Tyr Ile Ile 245 250 255 Gly Ala Val Val Phe Val Val Ile Ile Leu Val Ile Ile Leu Ala Ile 260 265 270 Ser Leu His Lys Cys Arg Lys Ala Gly Val Gly Gln Ser Trp Lys Glu 275 280 285 Asn Ser Pro Leu Asn Val Ser 290 295 <210> SEQ ID NO 44 <211> LENGTH: 538 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P10155 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(538) <400> SEQUENCE: 44 Met Glu Glu Ser Val Asn Gln Met Gln Pro Leu Asn Glu Lys Gln Ile 1 5 10 15 Ala Asn Ser Gln Asp Gly Tyr Val Trp Gln Val Thr Asp Met Asn Arg 20 25 30 Leu His Arg Phe Leu Cys Phe Gly Ser Glu Gly Gly Thr Tyr Tyr Ile 35 40 45 Lys Glu Gln Lys Leu Gly Leu Glu Asn Ala Glu Ala Leu Ile Arg Leu 50 55 60 Ile Glu Asp Gly Arg Gly Cys Glu Val Ile Gln Glu Ile Lys Ser Phe 65 70 75 80 Ser Gln Glu Gly Arg Thr Thr Lys Gln Glu Pro Met Leu Phe Ala Leu 85 90 95 Ala Ile Cys Ser Gln Cys Ser Asp Ile Ser Thr Lys Gln Ala Ala Phe 100 105 110

Lys Ala Val Ser Glu Val Cys Arg Ile Pro Thr His Leu Phe Thr Phe 115 120 125 Ile Gln Phe Lys Lys Asp Leu Lys Glu Ser Met Lys Cys Gly Met Trp 130 135 140 Gly Arg Ala Leu Arg Lys Ala Ile Ala Asp Trp Tyr Asn Glu Lys Gly 145 150 155 160 Gly Met Ala Leu Ala Leu Ala Val Thr Lys Tyr Lys Gln Arg Asn Gly 165 170 175 Trp Ser His Lys Asp Leu Leu Arg Leu Ser His Leu Lys Pro Ser Ser 180 185 190 Glu Gly Leu Ala Ile Val Thr Lys Tyr Ile Thr Lys Gly Trp Lys Glu 195 200 205 Val His Glu Leu Tyr Lys Glu Lys Ala Leu Ser Val Glu Thr Glu Lys 210 215 220 Leu Leu Lys Tyr Leu Glu Ala Val Glu Lys Val Lys Arg Thr Arg Asp 225 230 235 240 Glu Leu Glu Val Ile His Leu Ile Glu Glu His Arg Leu Val Arg Glu 245 250 255 His Leu Leu Thr Asn His Leu Lys Ser Lys Glu Val Trp Lys Ala Leu 260 265 270 Leu Gln Glu Met Pro Leu Thr Ala Leu Leu Arg Asn Leu Gly Lys Met 275 280 285 Thr Ala Asn Ser Val Leu Glu Pro Gly Asn Ser Glu Val Ser Leu Val 290 295 300 Cys Glu Lys Leu Cys Asn Glu Lys Leu Leu Lys Lys Ala Arg Ile His 305 310 315 320 Pro Phe His Ile Leu Ile Ala Leu Glu Thr Tyr Lys Thr Gly His Gly 325 330 335 Leu Arg Gly Lys Leu Lys Trp Arg Pro Asp Glu Glu Ile Leu Lys Ala 340 345 350 Leu Asp Ala Ala Phe Tyr Lys Thr Phe Lys Thr Val Glu Pro Thr Gly 355 360 365 Lys Arg Phe Leu Leu Ala Val Asp Val Ser Ala Ser Met Asn Gln Arg 370 375 380 Val Leu Gly Ser Ile Leu Asn Ala Ser Thr Val Ala Ala Ala Met Cys 385 390 395 400 Met Val Val Thr Arg Thr Glu Lys Asp Ser Tyr Val Val Ala Phe Ser 405 410 415 Asp Glu Met Val Pro Cys Pro Val Thr Thr Asp Met Thr Leu Gln Gln 420 425 430 Val Leu Met Ala Met Ser Gln Ile Pro Ala Gly Gly Thr Asp Cys Ser 435 440 445 Leu Pro Met Ile Trp Ala Gln Lys Thr Asn Thr Pro Ala Asp Val Phe 450 455 460 Ile Val Phe Thr Asp Asn Glu Thr Phe Ala Gly Gly Val His Pro Ala 465 470 475 480 Ile Ala Leu Arg Glu Tyr Arg Lys Lys Met Asp Ile Pro Ala Lys Leu 485 490 495 Ile Val Cys Gly Met Thr Ser Asn Gly Phe Thr Ile Ala Asp Pro Asp 500 505 510 Asp Arg Gly Met Leu Asp Met Cys Gly Phe Asp Thr Gly Ala Leu Asp 515 520 525 Val Ile Arg Asn Phe Thr Leu Asp Met Ile 530 535 <210> SEQ ID NO 45 <211> LENGTH: 1025 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BYX4 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1025) <400> SEQUENCE: 45 Met Ser Asn Gly Tyr Ser Thr Asp Glu Asn Phe Arg Tyr Leu Ile Ser 1 5 10 15 Cys Phe Arg Ala Arg Val Lys Met Tyr Ile Gln Val Glu Pro Val Leu 20 25 30 Asp Tyr Leu Thr Phe Leu Pro Ala Glu Val Lys Glu Gln Ile Gln Arg 35 40 45 Thr Val Ala Thr Ser Gly Asn Met Gln Ala Val Glu Leu Leu Leu Ser 50 55 60 Thr Leu Glu Lys Gly Val Trp His Leu Gly Trp Thr Arg Glu Phe Val 65 70 75 80 Glu Ala Leu Arg Arg Thr Gly Ser Pro Leu Ala Ala Arg Tyr Met Asn 85 90 95 Pro Glu Leu Thr Asp Leu Pro Ser Pro Ser Phe Glu Asn Ala His Asp 100 105 110 Glu Tyr Leu Gln Leu Leu Asn Leu Leu Gln Pro Thr Leu Val Asp Lys 115 120 125 Leu Leu Val Arg Asp Val Leu Asp Lys Cys Met Glu Glu Glu Leu Leu 130 135 140 Thr Ile Glu Asp Arg Asn Arg Ile Ala Ala Ala Glu Asn Asn Gly Asn 145 150 155 160 Glu Ser Gly Val Arg Glu Leu Leu Lys Arg Ile Val Gln Lys Glu Asn 165 170 175 Trp Phe Ser Ala Phe Leu Asn Val Leu Arg Gln Thr Gly Asn Asn Glu 180 185 190 Leu Val Gln Glu Leu Thr Gly Ser Asp Cys Ser Glu Ser Asn Ala Glu 195 200 205 Ile Glu Asn Leu Ser Gln Val Asp Gly Pro Gln Val Glu Glu Gln Leu 210 215 220 Leu Ser Thr Thr Val Gln Pro Asn Leu Glu Lys Glu Val Trp Gly Met 225 230 235 240 Glu Asn Asn Ser Ser Glu Ser Ser Phe Ala Asp Ser Ser Val Val Ser 245 250 255 Glu Ser Asp Thr Ser Leu Ala Glu Gly Ser Val Ser Cys Leu Asp Glu 260 265 270 Ser Leu Gly His Asn Ser Asn Met Gly Ser Asp Ser Gly Thr Met Gly 275 280 285 Ser Asp Ser Asp Glu Glu Asn Val Ala Ala Arg Ala Ser Pro Glu Pro 290 295 300 Glu Leu Gln Leu Arg Pro Tyr Gln Met Glu Val Ala Gln Pro Ala Leu 305 310 315 320 Glu Gly Lys Asn Ile Ile Ile Cys Leu Pro Thr Gly Ser Gly Lys Thr 325 330 335 Arg Val Ala Val Tyr Ile Ala Lys Asp His Leu Asp Lys Lys Lys Lys 340 345 350 Ala Ser Glu Pro Gly Lys Val Ile Val Leu Val Asn Lys Val Leu Leu 355 360 365 Val Glu Gln Leu Phe Arg Lys Glu Phe Gln Pro Phe Leu Lys Lys Trp 370 375 380 Tyr Arg Val Ile Gly Leu Ser Gly Asp Thr Gln Leu Lys Ile Ser Phe 385 390 395 400 Pro Glu Val Val Lys Ser Cys Asp Ile Ile Ile Ser Thr Ala Gln Ile 405 410 415 Leu Glu Asn Ser Leu Leu Asn Leu Glu Asn Gly Glu Asp Ala Gly Val 420 425 430 Gln Leu Ser Asp Phe Ser Leu Ile Ile Ile Asp Glu Cys His His Thr 435 440 445 Asn Lys Glu Ala Val Tyr Asn Asn Ile Met Arg His Tyr Leu Met Gln 450 455 460 Lys Leu Lys Asn Asn Arg Leu Lys Lys Glu Asn Lys Pro Val Ile Pro 465 470 475 480 Leu Pro Gln Ile Leu Gly Leu Thr Ala Ser Pro Gly Val Gly Gly Ala 485 490 495 Thr Lys Gln Ala Lys Ala Glu Glu His Ile Leu Lys Leu Cys Ala Asn 500 505 510 Leu Asp Ala Phe Thr Ile Lys Thr Val Lys Glu Asn Leu Asp Gln Leu 515 520 525 Lys Asn Gln Ile Gln Glu Pro Cys Lys Lys Phe Ala Ile Ala Asp Ala 530 535 540 Thr Arg Glu Asp Pro Phe Lys Glu Lys Leu Leu Glu Ile Met Thr Arg 545 550 555 560 Ile Gln Thr Tyr Cys Gln Met Ser Pro Met Ser Asp Phe Gly Thr Gln 565 570 575 Pro Tyr Glu Gln Trp Ala Ile Gln Met Glu Lys Lys Ala Ala Lys Glu 580 585 590 Gly Asn Arg Lys Glu Arg Val Cys Ala Glu His Leu Arg Lys Tyr Asn 595 600 605 Glu Ala Leu Gln Ile Asn Asp Thr Ile Arg Met Ile Asp Ala Tyr Thr 610 615 620 His Leu Glu Thr Phe Tyr Asn Glu Glu Lys Asp Lys Lys Phe Ala Val 625 630 635 640 Ile Glu Asp Asp Ser Asp Glu Gly Gly Asp Asp Glu Tyr Cys Asp Gly 645 650 655 Asp Glu Asp Glu Asp Asp Leu Lys Lys Pro Leu Lys Leu Asp Glu Thr 660 665 670 Asp Arg Phe Leu Met Thr Leu Phe Phe Glu Asn Asn Lys Met Leu Lys 675 680 685 Arg Leu Ala Glu Asn Pro Glu Tyr Glu Asn Glu Lys Leu Thr Lys Leu 690 695 700 Arg Asn Thr Ile Met Glu Gln Tyr Thr Arg Thr Glu Glu Ser Ala Arg 705 710 715 720 Gly Ile Ile Phe Thr Lys Thr Arg Gln Ser Ala Tyr Ala Leu Ser Gln 725 730 735 Trp Ile Thr Glu Asn Glu Lys Phe Ala Glu Val Gly Val Lys Ala His 740 745 750 His Leu Ile Gly Ala Gly His Ser Ser Glu Phe Lys Pro Met Thr Gln 755 760 765 Asn Glu Gln Lys Glu Val Ile Ser Lys Phe Arg Thr Gly Lys Ile Asn 770 775 780 Leu Leu Ile Ala Thr Thr Val Ala Glu Glu Gly Leu Asp Ile Lys Glu 785 790 795 800 Cys Asn Ile Val Ile Arg Tyr Gly Leu Val Thr Asn Glu Ile Ala Met 805 810 815 Val Gln Ala Arg Gly Arg Ala Arg Ala Asp Glu Ser Thr Tyr Val Leu 820 825 830 Val Ala His Ser Gly Ser Gly Val Ile Glu His Glu Thr Val Asn Asp 835 840 845

Phe Arg Glu Lys Met Met Tyr Lys Ala Ile His Cys Val Gln Asn Met 850 855 860 Lys Pro Glu Glu Tyr Ala His Lys Ile Leu Glu Leu Gln Met Gln Ser 865 870 875 880 Ile Met Glu Lys Lys Met Lys Thr Lys Arg Asn Ile Ala Lys His Tyr 885 890 895 Lys Asn Asn Pro Ser Leu Ile Thr Phe Leu Cys Lys Asn Cys Ser Val 900 905 910 Leu Ala Cys Ser Gly Glu Asp Ile His Val Ile Glu Lys Met His His 915 920 925 Val Asn Met Thr Pro Glu Phe Lys Glu Leu Tyr Ile Val Arg Glu Asn 930 935 940 Lys Ala Leu Gln Lys Lys Cys Ala Asp Tyr Gln Ile Asn Gly Glu Ile 945 950 955 960 Ile Cys Lys Cys Gly Gln Ala Trp Gly Thr Met Met Val His Lys Gly 965 970 975 Leu Asp Leu Pro Cys Leu Lys Ile Arg Asn Phe Val Val Val Phe Lys 980 985 990 Asn Asn Ser Thr Lys Lys Gln Tyr Lys Lys Trp Val Glu Leu Pro Ile 995 1000 1005 Thr Phe Pro Asn Leu Asp Tyr Ser Glu Cys Cys Leu Phe Ser Asp 1010 1015 1020 Glu Asp 1025 <210> SEQ ID NO 46 <211> LENGTH: 451 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q71U36 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(451) <400> SEQUENCE: 46 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro 20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Gly Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Ser Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Thr Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Ile 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Val Asp Ser Val Glu Gly Glu Gly Glu Glu Glu Gly 435 440 445 Glu Glu Tyr 450 <210> SEQ ID NO 47 <211> LENGTH: 451 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P68363 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(451) <400> SEQUENCE: 47 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro 20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Ser Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Ser Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Ser Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Ile 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Val Asp Ser Val Glu Gly Glu Gly Glu Glu Glu Gly 435 440 445 Glu Glu Tyr 450 <210> SEQ ID NO 48 <211> LENGTH: 449 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9BQE3 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(449) <400> SEQUENCE: 48 Met Arg Glu Cys Ile Ser Ile His Val Gly Gln Ala Gly Val Gln Ile 1 5 10 15 Gly Asn Ala Cys Trp Glu Leu Tyr Cys Leu Glu His Gly Ile Gln Pro

20 25 30 Asp Gly Gln Met Pro Ser Asp Lys Thr Ile Gly Gly Gly Asp Asp Ser 35 40 45 Phe Asn Thr Phe Phe Ser Glu Thr Gly Ala Gly Lys His Val Pro Arg 50 55 60 Ala Val Phe Val Asp Leu Glu Pro Thr Val Ile Asp Glu Val Arg Thr 65 70 75 80 Gly Thr Tyr Arg Gln Leu Phe His Pro Glu Gln Leu Ile Thr Gly Lys 85 90 95 Glu Asp Ala Ala Asn Asn Tyr Ala Arg Gly His Tyr Thr Ile Gly Lys 100 105 110 Glu Ile Ile Asp Leu Val Leu Asp Arg Ile Arg Lys Leu Ala Asp Gln 115 120 125 Cys Thr Gly Leu Gln Gly Phe Leu Val Phe His Ser Phe Gly Gly Gly 130 135 140 Thr Gly Ser Gly Phe Thr Ser Leu Leu Met Glu Arg Leu Ser Val Asp 145 150 155 160 Tyr Gly Lys Lys Ser Lys Leu Glu Phe Ser Ile Tyr Pro Ala Pro Gln 165 170 175 Val Ser Thr Ala Val Val Glu Pro Tyr Asn Ser Ile Leu Thr Thr His 180 185 190 Thr Thr Leu Glu His Ser Asp Cys Ala Phe Met Val Asp Asn Glu Ala 195 200 205 Ile Tyr Asp Ile Cys Arg Arg Asn Leu Asp Ile Glu Arg Pro Thr Tyr 210 215 220 Thr Asn Leu Asn Arg Leu Ile Ser Gln Ile Val Ser Ser Ile Thr Ala 225 230 235 240 Ser Leu Arg Phe Asp Gly Ala Leu Asn Val Asp Leu Thr Glu Phe Gln 245 250 255 Thr Asn Leu Val Pro Tyr Pro Arg Ile His Phe Pro Leu Ala Thr Tyr 260 265 270 Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu Thr Val 275 280 285 Ala Glu Ile Thr Asn Ala Cys Phe Glu Pro Ala Asn Gln Met Val Lys 290 295 300 Cys Asp Pro Arg His Gly Lys Tyr Met Ala Cys Cys Leu Leu Tyr Arg 305 310 315 320 Gly Asp Val Val Pro Lys Asp Val Asn Ala Ala Ile Ala Thr Ile Lys 325 330 335 Thr Lys Arg Thr Ile Gln Phe Val Asp Trp Cys Pro Thr Gly Phe Lys 340 345 350 Val Gly Ile Asn Tyr Gln Pro Pro Thr Val Val Pro Gly Gly Asp Leu 355 360 365 Ala Lys Val Gln Arg Ala Val Cys Met Leu Ser Asn Thr Thr Ala Val 370 375 380 Ala Glu Ala Trp Ala Arg Leu Asp His Lys Phe Asp Leu Met Tyr Ala 385 390 395 400 Lys Arg Ala Phe Val His Trp Tyr Val Gly Glu Gly Met Glu Glu Gly 405 410 415 Glu Phe Ser Glu Ala Arg Glu Asp Met Ala Ala Leu Glu Lys Asp Tyr 420 425 430 Glu Glu Val Gly Ala Asp Ser Ala Asp Gly Glu Asp Glu Gly Glu Glu 435 440 445 Tyr <210> SEQ ID NO 49 <211> LENGTH: 444 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P07437 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(444) <400> SEQUENCE: 49 Met Arg Glu Ile Val His Ile Gln Ala Gly Gln Cys Gly Asn Gln Ile 1 5 10 15 Gly Ala Lys Phe Trp Glu Val Ile Ser Asp Glu His Gly Ile Asp Pro 20 25 30 Thr Gly Thr Tyr His Gly Asp Ser Asp Leu Gln Leu Asp Arg Ile Ser 35 40 45 Val Tyr Tyr Asn Glu Ala Thr Gly Gly Lys Tyr Val Pro Arg Ala Ile 50 55 60 Leu Val Asp Leu Glu Pro Gly Thr Met Asp Ser Val Arg Ser Gly Pro 65 70 75 80 Phe Gly Gln Ile Phe Arg Pro Asp Asn Phe Val Phe Gly Gln Ser Gly 85 90 95 Ala Gly Asn Asn Trp Ala Lys Gly His Tyr Thr Glu Gly Ala Glu Leu 100 105 110 Val Asp Ser Val Leu Asp Val Val Arg Lys Glu Ala Glu Ser Cys Asp 115 120 125 Cys Leu Gln Gly Phe Gln Leu Thr His Ser Leu Gly Gly Gly Thr Gly 130 135 140 Ser Gly Met Gly Thr Leu Leu Ile Ser Lys Ile Arg Glu Glu Tyr Pro 145 150 155 160 Asp Arg Ile Met Asn Thr Phe Ser Val Val Pro Ser Pro Lys Val Ser 165 170 175 Asp Thr Val Val Glu Pro Tyr Asn Ala Thr Leu Ser Val His Gln Leu 180 185 190 Val Glu Asn Thr Asp Glu Thr Tyr Cys Ile Asp Asn Glu Ala Leu Tyr 195 200 205 Asp Ile Cys Phe Arg Thr Leu Lys Leu Thr Thr Pro Thr Tyr Gly Asp 210 215 220 Leu Asn His Leu Val Ser Ala Thr Met Ser Gly Val Thr Thr Cys Leu 225 230 235 240 Arg Phe Pro Gly Gln Leu Asn Ala Asp Leu Arg Lys Leu Ala Val Asn 245 250 255 Met Val Pro Phe Pro Arg Leu His Phe Phe Met Pro Gly Phe Ala Pro 260 265 270 Leu Thr Ser Arg Gly Ser Gln Gln Tyr Arg Ala Leu Thr Val Pro Glu 275 280 285 Leu Thr Gln Gln Val Phe Asp Ala Lys Asn Met Met Ala Ala Cys Asp 290 295 300 Pro Arg His Gly Arg Tyr Leu Thr Val Ala Ala Val Phe Arg Gly Arg 305 310 315 320 Met Ser Met Lys Glu Val Asp Glu Gln Met Leu Asn Val Gln Asn Lys 325 330 335 Asn Ser Ser Tyr Phe Val Glu Trp Ile Pro Asn Asn Val Lys Thr Ala 340 345 350 Val Cys Asp Ile Pro Pro Arg Gly Leu Lys Met Ala Val Thr Phe Ile 355 360 365 Gly Asn Ser Thr Ala Ile Gln Glu Leu Phe Lys Arg Ile Ser Glu Gln 370 375 380 Phe Thr Ala Met Phe Arg Arg Lys Ala Phe Leu His Trp Tyr Thr Gly 385 390 395 400 Glu Gly Met Asp Glu Met Glu Phe Thr Glu Ala Glu Ser Asn Met Asn 405 410 415 Asp Leu Val Ser Glu Tyr Gln Gln Tyr Gln Asp Ala Thr Ala Glu Glu 420 425 430 Glu Glu Asp Phe Gly Glu Glu Ala Glu Glu Glu Ala 435 440 <210> SEQ ID NO 50 <211> LENGTH: 4391 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P98160 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(4391) <400> SEQUENCE: 50 Met Gly Trp Arg Ala Ala Gly Ala Leu Leu Leu Ala Leu Leu Leu His 1 5 10 15 Gly Arg Leu Leu Ala Val Thr His Gly Leu Arg Ala Tyr Asp Gly Leu 20 25 30 Ser Leu Pro Glu Asp Ile Glu Thr Val Thr Ala Ser Gln Met Arg Trp 35 40 45 Thr His Ser Tyr Leu Ser Asp Asp Glu Asp Met Leu Ala Asp Ser Ile 50 55 60 Ser Gly Asp Asp Leu Gly Ser Gly Asp Leu Gly Ser Gly Asp Phe Gln 65 70 75 80 Met Val Tyr Phe Arg Ala Leu Val Asn Phe Thr Arg Ser Ile Glu Tyr 85 90 95 Ser Pro Gln Leu Glu Asp Ala Gly Ser Arg Glu Phe Arg Glu Val Ser 100 105 110 Glu Ala Val Val Asp Thr Leu Glu Ser Glu Tyr Leu Lys Ile Pro Gly 115 120 125 Asp Gln Val Val Ser Val Val Phe Ile Lys Glu Leu Asp Gly Trp Val 130 135 140 Phe Val Glu Leu Asp Val Gly Ser Glu Gly Asn Ala Asp Gly Ala Gln 145 150 155 160 Ile Gln Glu Met Leu Leu Arg Val Ile Ser Ser Gly Ser Val Ala Ser 165 170 175 Tyr Val Thr Ser Pro Gln Gly Phe Gln Phe Arg Arg Leu Gly Thr Val 180 185 190 Pro Gln Phe Pro Arg Ala Cys Thr Glu Ala Glu Phe Ala Cys His Ser 195 200 205 Tyr Asn Glu Cys Val Ala Leu Glu Tyr Arg Cys Asp Arg Arg Pro Asp 210 215 220 Cys Arg Asp Met Ser Asp Glu Leu Asn Cys Glu Glu Pro Val Leu Gly 225 230 235 240 Ile Ser Pro Thr Phe Ser Leu Leu Val Glu Thr Thr Ser Leu Pro Pro 245 250 255 Arg Pro Glu Thr Thr Ile Met Arg Gln Pro Pro Val Thr His Ala Pro 260 265 270 Gln Pro Leu Leu Pro Gly Ser Val Arg Pro Leu Pro Cys Gly Pro Gln 275 280 285 Glu Ala Ala Cys Arg Asn Gly His Cys Ile Pro Arg Asp Tyr Leu Cys 290 295 300 Asp Gly Gln Glu Asp Cys Glu Asp Gly Ser Asp Glu Leu Asp Cys Gly 305 310 315 320 Pro Pro Pro Pro Cys Glu Pro Asn Glu Phe Pro Cys Gly Asn Gly His

325 330 335 Cys Ala Leu Lys Leu Trp Arg Cys Asp Gly Asp Phe Asp Cys Glu Asp 340 345 350 Arg Thr Asp Glu Ala Asn Cys Pro Thr Lys Arg Pro Glu Glu Val Cys 355 360 365 Gly Pro Thr Gln Phe Arg Cys Val Ser Thr Asn Met Cys Ile Pro Ala 370 375 380 Ser Phe His Cys Asp Glu Glu Ser Asp Cys Pro Asp Arg Ser Asp Glu 385 390 395 400 Phe Gly Cys Met Pro Pro Gln Val Val Thr Pro Pro Arg Glu Ser Ile 405 410 415 Gln Ala Ser Arg Gly Gln Thr Val Thr Phe Thr Cys Val Ala Ile Gly 420 425 430 Val Pro Thr Pro Ile Ile Asn Trp Arg Leu Asn Trp Gly His Ile Pro 435 440 445 Ser His Pro Arg Val Thr Val Thr Ser Glu Gly Gly Arg Gly Thr Leu 450 455 460 Ile Ile Arg Asp Val Lys Glu Ser Asp Gln Gly Ala Tyr Thr Cys Glu 465 470 475 480 Ala Met Asn Ala Arg Gly Met Val Phe Gly Ile Pro Asp Gly Val Leu 485 490 495 Glu Leu Val Pro Gln Arg Gly Pro Cys Pro Asp Gly His Phe Tyr Leu 500 505 510 Glu His Ser Ala Ala Cys Leu Pro Cys Phe Cys Phe Gly Ile Thr Ser 515 520 525 Val Cys Gln Ser Thr Arg Arg Phe Arg Asp Gln Ile Arg Leu Arg Phe 530 535 540 Asp Gln Pro Asp Asp Phe Lys Gly Val Asn Val Thr Met Pro Ala Gln 545 550 555 560 Pro Gly Thr Pro Pro Leu Ser Ser Thr Gln Leu Gln Ile Asp Pro Ser 565 570 575 Leu His Glu Phe Gln Leu Val Asp Leu Ser Arg Arg Phe Leu Val His 580 585 590 Asp Ser Phe Trp Ala Leu Pro Glu Gln Phe Leu Gly Asn Lys Val Asp 595 600 605 Ser Tyr Gly Gly Ser Leu Arg Tyr Asn Val Arg Tyr Glu Leu Ala Arg 610 615 620 Gly Met Leu Glu Pro Val Gln Arg Pro Asp Val Val Leu Met Gly Ala 625 630 635 640 Gly Tyr Arg Leu Leu Ser Arg Gly His Thr Pro Thr Gln Pro Gly Ala 645 650 655 Leu Asn Gln Arg Gln Val Gln Phe Ser Glu Glu His Trp Val His Glu 660 665 670 Ser Gly Arg Pro Val Gln Arg Ala Glu Leu Leu Gln Val Leu Gln Ser 675 680 685 Leu Glu Ala Val Leu Ile Gln Thr Val Tyr Asn Thr Lys Met Ala Ser 690 695 700 Val Gly Leu Ser Asp Ile Ala Met Asp Thr Thr Val Thr His Ala Thr 705 710 715 720 Ser His Gly Arg Ala His Ser Val Glu Glu Cys Arg Cys Pro Ile Gly 725 730 735 Tyr Ser Gly Leu Ser Cys Glu Ser Cys Asp Ala His Phe Thr Arg Val 740 745 750 Pro Gly Gly Pro Tyr Leu Gly Thr Cys Ser Gly Cys Asn Cys Asn Gly 755 760 765 His Ala Ser Ser Cys Asp Pro Val Tyr Gly His Cys Leu Asn Cys Gln 770 775 780 His Asn Thr Glu Gly Pro Gln Cys Asn Lys Cys Lys Ala Gly Phe Phe 785 790 795 800 Gly Asp Ala Met Lys Ala Thr Ala Thr Ser Cys Arg Pro Cys Pro Cys 805 810 815 Pro Tyr Ile Asp Ala Ser Arg Arg Phe Ser Asp Thr Cys Phe Leu Asp 820 825 830 Thr Asp Gly Gln Ala Thr Cys Asp Ala Cys Ala Pro Gly Tyr Thr Gly 835 840 845 Arg Arg Cys Glu Ser Cys Ala Pro Gly Tyr Glu Gly Asn Pro Ile Gln 850 855 860 Pro Gly Gly Lys Cys Arg Pro Val Asn Gln Glu Ile Val Arg Cys Asp 865 870 875 880 Glu Arg Gly Ser Met Gly Thr Ser Gly Glu Ala Cys Arg Cys Lys Asn 885 890 895 Asn Val Val Gly Arg Leu Cys Asn Glu Cys Ala Asp Gly Ser Phe His 900 905 910 Leu Ser Thr Arg Asn Pro Asp Gly Cys Leu Lys Cys Phe Cys Met Gly 915 920 925 Val Ser Arg His Cys Thr Ser Ser Ser Trp Ser Arg Ala Gln Leu His 930 935 940 Gly Ala Ser Glu Glu Pro Gly His Phe Ser Leu Thr Asn Ala Ala Ser 945 950 955 960 Thr His Thr Thr Asn Glu Gly Ile Phe Ser Pro Thr Pro Gly Glu Leu 965 970 975 Gly Phe Ser Ser Phe His Arg Leu Leu Ser Gly Pro Tyr Phe Trp Ser 980 985 990 Leu Pro Ser Arg Phe Leu Gly Asp Lys Val Thr Ser Tyr Gly Gly Glu 995 1000 1005 Leu Arg Phe Thr Val Thr Gln Arg Ser Gln Pro Gly Ser Thr Pro 1010 1015 1020 Leu His Gly Gln Pro Leu Val Val Leu Gln Gly Asn Asn Ile Ile 1025 1030 1035 Leu Glu His His Val Ala Gln Glu Pro Ser Pro Gly Gln Pro Ser 1040 1045 1050 Thr Phe Ile Val Pro Phe Arg Glu Gln Ala Trp Gln Arg Pro Asp 1055 1060 1065 Gly Gln Pro Ala Thr Arg Glu His Leu Leu Met Ala Leu Ala Gly 1070 1075 1080 Ile Asp Thr Leu Leu Ile Arg Ala Ser Tyr Ala Gln Gln Pro Ala 1085 1090 1095 Glu Ser Arg Val Ser Gly Ile Ser Met Asp Val Ala Val Pro Glu 1100 1105 1110 Glu Thr Gly Gln Asp Pro Ala Leu Glu Val Glu Gln Cys Ser Cys 1115 1120 1125 Pro Pro Gly Tyr Arg Gly Pro Ser Cys Gln Asp Cys Asp Thr Gly 1130 1135 1140 Tyr Thr Arg Thr Pro Ser Gly Leu Tyr Leu Gly Thr Cys Glu Arg 1145 1150 1155 Cys Ser Cys His Gly His Ser Glu Ala Cys Glu Pro Glu Thr Gly 1160 1165 1170 Ala Cys Gln Gly Cys Gln His His Thr Glu Gly Pro Arg Cys Glu 1175 1180 1185 Gln Cys Gln Pro Gly Tyr Tyr Gly Asp Ala Gln Arg Gly Thr Pro 1190 1195 1200 Gln Asp Cys Gln Leu Cys Pro Cys Tyr Gly Asp Pro Ala Ala Gly 1205 1210 1215 Gln Ala Ala His Thr Cys Phe Leu Asp Thr Asp Gly His Pro Thr 1220 1225 1230 Cys Asp Ala Cys Ser Pro Gly His Ser Gly Arg His Cys Glu Arg 1235 1240 1245 Cys Ala Pro Gly Tyr Tyr Gly Asn Pro Ser Gln Gly Gln Pro Cys 1250 1255 1260 Gln Arg Asp Ser Gln Val Pro Gly Pro Ile Gly Cys Asn Cys Asp 1265 1270 1275 Pro Gln Gly Ser Val Ser Ser Gln Cys Asp Ala Ala Gly Gln Cys 1280 1285 1290 Gln Cys Lys Ala Gln Val Glu Gly Leu Thr Cys Ser His Cys Arg 1295 1300 1305 Pro His His Phe His Leu Ser Ala Ser Asn Pro Asp Gly Cys Leu 1310 1315 1320 Pro Cys Phe Cys Met Gly Ile Thr Gln Gln Cys Ala Ser Ser Ala 1325 1330 1335 Tyr Thr Arg His Leu Ile Ser Thr His Phe Ala Pro Gly Asp Phe 1340 1345 1350 Gln Gly Phe Ala Leu Val Asn Pro Gln Arg Asn Ser Arg Leu Thr 1355 1360 1365 Gly Glu Phe Thr Val Glu Pro Val Pro Glu Gly Ala Gln Leu Ser 1370 1375 1380 Phe Gly Asn Phe Ala Gln Leu Gly His Glu Ser Phe Tyr Trp Gln 1385 1390 1395 Leu Pro Glu Thr Tyr Gln Gly Asp Lys Val Ala Ala Tyr Gly Gly 1400 1405 1410 Lys Leu Arg Tyr Thr Leu Ser Tyr Thr Ala Gly Pro Gln Gly Ser 1415 1420 1425 Pro Leu Ser Asp Pro Asp Val Gln Ile Thr Gly Asn Asn Ile Met 1430 1435 1440 Leu Val Ala Ser Gln Pro Ala Leu Gln Gly Pro Glu Arg Arg Ser 1445 1450 1455 Tyr Glu Ile Met Phe Arg Glu Glu Phe Trp Arg Arg Pro Asp Gly 1460 1465 1470 Gln Pro Ala Thr Arg Glu His Leu Leu Met Ala Leu Ala Asp Leu 1475 1480 1485 Asp Glu Leu Leu Ile Arg Ala Thr Phe Ser Ser Val Pro Leu Ala 1490 1495 1500 Ala Ser Ile Ser Ala Val Ser Leu Glu Val Ala Gln Pro Gly Pro 1505 1510 1515 Ser Asn Arg Pro Arg Ala Leu Glu Val Glu Glu Cys Arg Cys Pro 1520 1525 1530 Pro Gly Tyr Ile Gly Leu Ser Cys Gln Asp Cys Ala Pro Gly Tyr 1535 1540 1545 Thr Arg Thr Gly Ser Gly Leu Tyr Leu Gly His Cys Glu Leu Cys 1550 1555 1560 Glu Cys Asn Gly His Ser Asp Leu Cys His Pro Glu Thr Gly Ala 1565 1570 1575 Cys Ser Gln Cys Gln His Asn Ala Ala Gly Glu Phe Cys Glu Leu 1580 1585 1590 Cys Ala Pro Gly Tyr Tyr Gly Asp Ala Thr Ala Gly Thr Pro Glu 1595 1600 1605 Asp Cys Gln Pro Cys Ala Cys Pro Leu Thr Asn Pro Glu Asn Met 1610 1615 1620

Phe Ser Arg Thr Cys Glu Ser Leu Gly Ala Gly Gly Tyr Arg Cys 1625 1630 1635 Thr Ala Cys Glu Pro Gly Tyr Thr Gly Gln Tyr Cys Glu Gln Cys 1640 1645 1650 Gly Pro Gly Tyr Val Gly Asn Pro Ser Val Gln Gly Gly Gln Cys 1655 1660 1665 Leu Pro Glu Thr Asn Gln Ala Pro Leu Val Val Glu Val His Pro 1670 1675 1680 Ala Arg Ser Ile Val Pro Gln Gly Gly Ser His Ser Leu Arg Cys 1685 1690 1695 Gln Val Ser Gly Ser Pro Pro His Tyr Phe Tyr Trp Ser Arg Glu 1700 1705 1710 Asp Gly Arg Pro Val Pro Ser Gly Thr Gln Gln Arg His Gln Gly 1715 1720 1725 Ser Glu Leu His Phe Pro Ser Val Gln Pro Ser Asp Ala Gly Val 1730 1735 1740 Tyr Ile Cys Thr Cys Arg Asn Leu His Gln Ser Asn Thr Ser Arg 1745 1750 1755 Ala Glu Leu Leu Val Thr Glu Ala Pro Ser Lys Pro Ile Thr Val 1760 1765 1770 Thr Val Glu Glu Gln Arg Ser Gln Ser Val Arg Pro Gly Ala Asp 1775 1780 1785 Val Thr Phe Ile Cys Thr Ala Lys Ser Lys Ser Pro Ala Tyr Thr 1790 1795 1800 Leu Val Trp Thr Arg Leu His Asn Gly Lys Leu Pro Thr Arg Ala 1805 1810 1815 Met Asp Phe Asn Gly Ile Leu Thr Ile Arg Asn Val Gln Leu Ser 1820 1825 1830 Asp Ala Gly Thr Tyr Val Cys Thr Gly Ser Asn Met Phe Ala Met 1835 1840 1845 Asp Gln Gly Thr Ala Thr Leu His Val Gln Ala Ser Gly Thr Leu 1850 1855 1860 Ser Ala Pro Val Val Ser Ile His Pro Pro Gln Leu Thr Val Gln 1865 1870 1875 Pro Gly Gln Leu Ala Glu Phe Arg Cys Ser Ala Thr Gly Ser Pro 1880 1885 1890 Thr Pro Thr Leu Glu Trp Thr Gly Gly Pro Gly Gly Gln Leu Pro 1895 1900 1905 Ala Lys Ala Gln Ile His Gly Gly Ile Leu Arg Leu Pro Ala Val 1910 1915 1920 Glu Pro Thr Asp Gln Ala Gln Tyr Leu Cys Arg Ala His Ser Ser 1925 1930 1935 Ala Gly Gln Gln Val Ala Arg Ala Val Leu His Val His Gly Gly 1940 1945 1950 Gly Gly Pro Arg Val Gln Val Ser Pro Glu Arg Thr Gln Val His 1955 1960 1965 Ala Gly Arg Thr Val Arg Leu Tyr Cys Arg Ala Ala Gly Val Pro 1970 1975 1980 Ser Ala Thr Ile Thr Trp Arg Lys Glu Gly Gly Ser Leu Pro Pro 1985 1990 1995 Gln Ala Arg Ser Glu Arg Thr Asp Ile Ala Thr Leu Leu Ile Pro 2000 2005 2010 Ala Ile Thr Thr Ala Asp Ala Gly Phe Tyr Leu Cys Val Ala Thr 2015 2020 2025 Ser Pro Ala Gly Thr Ala Gln Ala Arg Ile Gln Val Val Val Leu 2030 2035 2040 Ser Ala Ser Asp Ala Ser Pro Pro Pro Val Lys Ile Glu Ser Ser 2045 2050 2055 Ser Pro Ser Val Thr Glu Gly Gln Thr Leu Asp Leu Asn Cys Val 2060 2065 2070 Val Ala Gly Ser Ala His Ala Gln Val Thr Trp Tyr Arg Arg Gly 2075 2080 2085 Gly Ser Leu Pro Pro His Thr Gln Val His Gly Ser Arg Leu Arg 2090 2095 2100 Leu Pro Gln Val Ser Pro Ala Asp Ser Gly Glu Tyr Val Cys Arg 2105 2110 2115 Val Glu Asn Gly Ser Gly Pro Lys Glu Ala Ser Ile Thr Val Ser 2120 2125 2130 Val Leu His Gly Thr His Ser Gly Pro Ser Tyr Thr Pro Val Pro 2135 2140 2145 Gly Ser Thr Arg Pro Ile Arg Ile Glu Pro Ser Ser Ser His Val 2150 2155 2160 Ala Glu Gly Gln Thr Leu Asp Leu Asn Cys Val Val Pro Gly Gln 2165 2170 2175 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Ser Leu Pro 2180 2185 2190 Ala Arg His Gln Thr His Gly Ser Leu Leu Arg Leu His Gln Val 2195 2200 2205 Thr Pro Ala Asp Ser Gly Glu Tyr Val Cys His Val Val Gly Thr 2210 2215 2220 Ser Gly Pro Leu Glu Ala Ser Val Leu Val Thr Ile Glu Ala Ser 2225 2230 2235 Val Ile Pro Gly Pro Ile Pro Pro Val Arg Ile Glu Ser Ser Ser 2240 2245 2250 Ser Thr Val Ala Glu Gly Gln Thr Leu Asp Leu Ser Cys Val Val 2255 2260 2265 Ala Gly Gln Ala His Ala Gln Val Thr Trp Tyr Lys Arg Gly Gly 2270 2275 2280 Ser Leu Pro Ala Arg His Gln Val Arg Gly Ser Arg Leu Tyr Ile 2285 2290 2295 Phe Gln Ala Ser Pro Ala Asp Ala Gly Gln Tyr Val Cys Arg Ala 2300 2305 2310 Ser Asn Gly Met Glu Ala Ser Ile Thr Val Thr Val Thr Gly Thr 2315 2320 2325 Gln Gly Ala Asn Leu Ala Tyr Pro Ala Gly Ser Thr Gln Pro Ile 2330 2335 2340 Arg Ile Glu Pro Ser Ser Ser Gln Val Ala Glu Gly Gln Thr Leu 2345 2350 2355 Asp Leu Asn Cys Val Val Pro Gly Gln Ser His Ala Gln Val Thr 2360 2365 2370 Trp His Lys Arg Gly Gly Ser Leu Pro Val Arg His Gln Thr His 2375 2380 2385 Gly Ser Leu Leu Arg Leu Tyr Gln Ala Ser Pro Ala Asp Ser Gly 2390 2395 2400 Glu Tyr Val Cys Arg Val Leu Gly Ser Ser Val Pro Leu Glu Ala 2405 2410 2415 Ser Val Leu Val Thr Ile Glu Pro Ala Gly Ser Val Pro Ala Leu 2420 2425 2430 Gly Val Thr Pro Thr Val Arg Ile Glu Ser Ser Ser Ser Gln Val 2435 2440 2445 Ala Glu Gly Gln Thr Leu Asp Leu Asn Cys Leu Val Ala Gly Gln 2450 2455 2460 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Ser Leu Pro 2465 2470 2475 Ala Arg His Gln Val His Gly Ser Arg Leu Arg Leu Leu Gln Val 2480 2485 2490 Thr Pro Ala Asp Ser Gly Glu Tyr Val Cys Arg Val Val Gly Ser 2495 2500 2505 Ser Gly Thr Gln Glu Ala Ser Val Leu Val Thr Ile Gln Gln Arg 2510 2515 2520 Leu Ser Gly Ser His Ser Gln Gly Val Ala Tyr Pro Val Arg Ile 2525 2530 2535 Glu Ser Ser Ser Ala Ser Leu Ala Asn Gly His Thr Leu Asp Leu 2540 2545 2550 Asn Cys Leu Val Ala Ser Gln Ala Pro His Thr Ile Thr Trp Tyr 2555 2560 2565 Lys Arg Gly Gly Ser Leu Pro Ser Arg His Gln Ile Val Gly Ser 2570 2575 2580 Arg Leu Arg Ile Pro Gln Val Thr Pro Ala Asp Ser Gly Glu Tyr 2585 2590 2595 Val Cys His Val Ser Asn Gly Ala Gly Ser Arg Glu Thr Ser Leu 2600 2605 2610 Ile Val Thr Ile Gln Gly Ser Gly Ser Ser His Val Pro Ser Val 2615 2620 2625 Ser Pro Pro Ile Arg Ile Glu Ser Ser Ser Pro Thr Val Val Glu 2630 2635 2640 Gly Gln Thr Leu Asp Leu Asn Cys Val Val Ala Arg Gln Pro Gln 2645 2650 2655 Ala Ile Ile Thr Trp Tyr Lys Arg Gly Gly Ser Leu Pro Ser Arg 2660 2665 2670 His Gln Thr His Gly Ser His Leu Arg Leu His Gln Met Ser Val 2675 2680 2685 Ala Asp Ser Gly Glu Tyr Val Cys Arg Ala Asn Asn Asn Ile Asp 2690 2695 2700 Ala Leu Glu Ala Ser Ile Val Ile Ser Val Ser Pro Ser Ala Gly 2705 2710 2715 Ser Pro Ser Ala Pro Gly Ser Ser Met Pro Ile Arg Ile Glu Ser 2720 2725 2730 Ser Ser Ser His Val Ala Glu Gly Glu Thr Leu Asp Leu Asn Cys 2735 2740 2745 Val Val Pro Gly Gln Ala His Ala Gln Val Thr Trp His Lys Arg 2750 2755 2760 Gly Gly Ser Leu Pro Ser His His Gln Thr Arg Gly Ser Arg Leu 2765 2770 2775 Arg Leu His His Val Ser Pro Ala Asp Ser Gly Glu Tyr Val Cys 2780 2785 2790 Arg Val Met Gly Ser Ser Gly Pro Leu Glu Ala Ser Val Leu Val 2795 2800 2805 Thr Ile Glu Ala Ser Gly Ser Ser Ala Val His Val Pro Ala Pro 2810 2815 2820 Gly Gly Ala Pro Pro Ile Arg Ile Glu Pro Ser Ser Ser Arg Val 2825 2830 2835 Ala Glu Gly Gln Thr Leu Asp Leu Lys Cys Val Val Pro Gly Gln 2840 2845 2850 Ala His Ala Gln Val Thr Trp His Lys Arg Gly Gly Asn Leu Pro 2855 2860 2865 Ala Arg His Gln Val His Gly Pro Leu Leu Arg Leu Asn Gln Val 2870 2875 2880

Ser Pro Ala Asp Ser Gly Glu Tyr Ser Cys Gln Val Thr Gly Ser 2885 2890 2895 Ser Gly Thr Leu Glu Ala Ser Val Leu Val Thr Ile Glu Pro Ser 2900 2905 2910 Ser Pro Gly Pro Ile Pro Ala Pro Gly Leu Ala Gln Pro Ile Tyr 2915 2920 2925 Ile Glu Ala Ser Ser Ser His Val Thr Glu Gly Gln Thr Leu Asp 2930 2935 2940 Leu Asn Cys Val Val Pro Gly Gln Ala His Ala Gln Val Thr Trp 2945 2950 2955 Tyr Lys Arg Gly Gly Ser Leu Pro Ala Arg His Gln Thr His Gly 2960 2965 2970 Ser Gln Leu Arg Leu His Leu Val Ser Pro Ala Asp Ser Gly Glu 2975 2980 2985 Tyr Val Cys Arg Ala Ala Ser Gly Pro Gly Pro Glu Gln Glu Ala 2990 2995 3000 Ser Phe Thr Val Thr Val Pro Pro Ser Glu Gly Ser Ser Tyr Arg 3005 3010 3015 Leu Arg Ser Pro Val Ile Ser Ile Asp Pro Pro Ser Ser Thr Val 3020 3025 3030 Gln Gln Gly Gln Asp Ala Ser Phe Lys Cys Leu Ile His Asp Gly 3035 3040 3045 Ala Ala Pro Ile Ser Leu Glu Trp Lys Thr Arg Asn Gln Glu Leu 3050 3055 3060 Glu Asp Asn Val His Ile Ser Pro Asn Gly Ser Ile Ile Thr Ile 3065 3070 3075 Val Gly Thr Arg Pro Ser Asn His Gly Thr Tyr Arg Cys Val Ala 3080 3085 3090 Ser Asn Ala Tyr Gly Val Ala Gln Ser Val Val Asn Leu Ser Val 3095 3100 3105 His Gly Pro Pro Thr Val Ser Val Leu Pro Glu Gly Pro Val Trp 3110 3115 3120 Val Lys Val Gly Lys Ala Val Thr Leu Glu Cys Val Ser Ala Gly 3125 3130 3135 Glu Pro Arg Ser Ser Ala Arg Trp Thr Arg Ile Ser Ser Thr Pro 3140 3145 3150 Ala Lys Leu Glu Gln Arg Thr Tyr Gly Leu Met Asp Ser His Ala 3155 3160 3165 Val Leu Gln Ile Ser Ser Ala Lys Pro Ser Asp Ala Gly Thr Tyr 3170 3175 3180 Val Cys Leu Ala Gln Asn Ala Leu Gly Thr Ala Gln Lys Gln Val 3185 3190 3195 Glu Val Ile Val Asp Thr Gly Ala Met Ala Pro Gly Ala Pro Gln 3200 3205 3210 Val Gln Ala Glu Glu Ala Glu Leu Thr Val Glu Ala Gly His Thr 3215 3220 3225 Ala Thr Leu Arg Cys Ser Ala Thr Gly Ser Pro Ala Pro Thr Ile 3230 3235 3240 His Trp Ser Lys Leu Arg Ser Pro Leu Pro Trp Gln His Arg Leu 3245 3250 3255 Glu Gly Asp Thr Leu Ile Ile Pro Arg Val Ala Gln Gln Asp Ser 3260 3265 3270 Gly Gln Tyr Ile Cys Asn Ala Thr Ser Pro Ala Gly His Ala Glu 3275 3280 3285 Ala Thr Ile Ile Leu His Val Glu Ser Pro Pro Tyr Ala Thr Thr 3290 3295 3300 Val Pro Glu His Ala Ser Val Gln Ala Gly Glu Thr Val Gln Leu 3305 3310 3315 Gln Cys Leu Ala His Gly Thr Pro Pro Leu Thr Phe Gln Trp Ser 3320 3325 3330 Arg Val Gly Ser Ser Leu Pro Gly Arg Ala Thr Ala Arg Asn Glu 3335 3340 3345 Leu Leu His Phe Glu Arg Ala Ala Pro Glu Asp Ser Gly Arg Tyr 3350 3355 3360 Arg Cys Arg Val Thr Asn Lys Val Gly Ser Ala Glu Ala Phe Ala 3365 3370 3375 Gln Leu Leu Val Gln Gly Pro Pro Gly Ser Leu Pro Ala Thr Ser 3380 3385 3390 Ile Pro Ala Gly Ser Thr Pro Thr Val Gln Val Thr Pro Gln Leu 3395 3400 3405 Glu Thr Lys Ser Ile Gly Ala Ser Val Glu Phe His Cys Ala Val 3410 3415 3420 Pro Ser Asp Arg Gly Thr Gln Leu Arg Trp Phe Lys Glu Gly Gly 3425 3430 3435 Gln Leu Pro Pro Gly His Ser Val Gln Asp Gly Val Leu Arg Ile 3440 3445 3450 Gln Asn Leu Asp Gln Ser Cys Gln Gly Thr Tyr Ile Cys Gln Ala 3455 3460 3465 His Gly Pro Trp Gly Lys Ala Gln Ala Ser Ala Gln Leu Val Ile 3470 3475 3480 Gln Ala Leu Pro Ser Val Leu Ile Asn Ile Arg Thr Ser Val Gln 3485 3490 3495 Thr Val Val Val Gly His Ala Val Glu Phe Glu Cys Leu Ala Leu 3500 3505 3510 Gly Asp Pro Lys Pro Gln Val Thr Trp Ser Lys Val Gly Gly His 3515 3520 3525 Leu Arg Pro Gly Ile Val Gln Ser Gly Gly Val Val Arg Ile Ala 3530 3535 3540 His Val Glu Leu Ala Asp Ala Gly Gln Tyr Arg Cys Thr Ala Thr 3545 3550 3555 Asn Ala Ala Gly Thr Thr Gln Ser His Val Leu Leu Leu Val Gln 3560 3565 3570 Ala Leu Pro Gln Ile Ser Met Pro Gln Glu Val Arg Val Pro Ala 3575 3580 3585 Gly Ser Ala Ala Val Phe Pro Cys Ile Ala Ser Gly Tyr Pro Thr 3590 3595 3600 Pro Asp Ile Ser Trp Ser Lys Leu Asp Gly Ser Leu Pro Pro Asp 3605 3610 3615 Ser Arg Leu Glu Asn Asn Met Leu Met Leu Pro Ser Val Arg Pro 3620 3625 3630 Gln Asp Ala Gly Thr Tyr Val Cys Thr Ala Thr Asn Arg Gln Gly 3635 3640 3645 Lys Val Lys Ala Phe Ala His Leu Gln Val Pro Glu Arg Val Val 3650 3655 3660 Pro Tyr Phe Thr Gln Thr Pro Tyr Ser Phe Leu Pro Leu Pro Thr 3665 3670 3675 Ile Lys Asp Ala Tyr Arg Lys Phe Glu Ile Lys Ile Thr Phe Arg 3680 3685 3690 Pro Asp Ser Ala Asp Gly Met Leu Leu Tyr Asn Gly Gln Lys Arg 3695 3700 3705 Val Pro Gly Ser Pro Thr Asn Leu Ala Asn Arg Gln Pro Asp Phe 3710 3715 3720 Ile Ser Phe Gly Leu Val Gly Gly Arg Pro Glu Phe Arg Phe Asp 3725 3730 3735 Ala Gly Ser Gly Met Ala Thr Ile Arg His Pro Thr Pro Leu Ala 3740 3745 3750 Leu Gly His Phe His Thr Val Thr Leu Leu Arg Ser Leu Thr Gln 3755 3760 3765 Gly Ser Leu Ile Val Gly Asp Leu Ala Pro Val Asn Gly Thr Ser 3770 3775 3780 Gln Gly Lys Phe Gln Gly Leu Asp Leu Asn Glu Glu Leu Tyr Leu 3785 3790 3795 Gly Gly Tyr Pro Asp Tyr Gly Ala Ile Pro Lys Ala Gly Leu Ser 3800 3805 3810 Ser Gly Phe Ile Gly Cys Val Arg Glu Leu Arg Ile Gln Gly Glu 3815 3820 3825 Glu Ile Val Phe His Asp Leu Asn Leu Thr Ala His Gly Ile Ser 3830 3835 3840 His Cys Pro Thr Cys Arg Asp Arg Pro Cys Gln Asn Gly Gly Gln 3845 3850 3855 Cys His Asp Ser Glu Ser Ser Ser Tyr Val Cys Val Cys Pro Ala 3860 3865 3870 Gly Phe Thr Gly Ser Arg Cys Glu His Ser Gln Ala Leu His Cys 3875 3880 3885 His Pro Glu Ala Cys Gly Pro Asp Ala Thr Cys Val Asn Arg Pro 3890 3895 3900 Asp Gly Arg Gly Tyr Thr Cys Arg Cys His Leu Gly Arg Ser Gly 3905 3910 3915 Leu Arg Cys Glu Glu Gly Val Thr Val Thr Thr Pro Ser Leu Ser 3920 3925 3930 Gly Ala Gly Ser Tyr Leu Ala Leu Pro Ala Leu Thr Asn Thr His 3935 3940 3945 His Glu Leu Arg Leu Asp Val Glu Phe Lys Pro Leu Ala Pro Asp 3950 3955 3960 Gly Val Leu Leu Phe Ser Gly Gly Lys Ser Gly Pro Val Glu Asp 3965 3970 3975 Phe Val Ser Leu Ala Met Val Gly Gly His Leu Glu Phe Arg Tyr 3980 3985 3990 Glu Leu Gly Ser Gly Leu Ala Val Leu Arg Ser Ala Glu Pro Leu 3995 4000 4005 Ala Leu Gly Arg Trp His Arg Val Ser Ala Glu Arg Leu Asn Lys 4010 4015 4020 Asp Gly Ser Leu Arg Val Asn Gly Gly Arg Pro Val Leu Arg Ser 4025 4030 4035 Ser Pro Gly Lys Ser Gln Gly Leu Asn Leu His Thr Leu Leu Tyr 4040 4045 4050 Leu Gly Gly Val Glu Pro Ser Val Pro Leu Ser Pro Ala Thr Asn 4055 4060 4065 Met Ser Ala His Phe Arg Gly Cys Val Gly Glu Val Ser Val Asn 4070 4075 4080 Gly Lys Arg Leu Asp Leu Thr Tyr Ser Phe Leu Gly Ser Gln Gly 4085 4090 4095 Ile Gly Gln Cys Tyr Asp Ser Ser Pro Cys Glu Arg Gln Pro Cys 4100 4105 4110 Gln His Gly Ala Thr Cys Met Pro Ala Gly Glu Tyr Glu Phe Gln 4115 4120 4125 Cys Leu Cys Arg Asp Gly Phe Lys Gly Asp Leu Cys Glu His Glu

4130 4135 4140 Glu Asn Pro Cys Gln Leu Arg Glu Pro Cys Leu His Gly Gly Thr 4145 4150 4155 Cys Gln Gly Thr Arg Cys Leu Cys Leu Pro Gly Phe Ser Gly Pro 4160 4165 4170 Arg Cys Gln Gln Gly Ser Gly His Gly Ile Ala Glu Ser Asp Trp 4175 4180 4185 His Leu Glu Gly Ser Gly Gly Asn Asp Ala Pro Gly Gln Tyr Gly 4190 4195 4200 Ala Tyr Phe His Asp Asp Gly Phe Leu Ala Phe Pro Gly His Val 4205 4210 4215 Phe Ser Arg Ser Leu Pro Glu Val Pro Glu Thr Ile Glu Leu Glu 4220 4225 4230 Val Arg Thr Ser Thr Ala Ser Gly Leu Leu Leu Trp Gln Gly Val 4235 4240 4245 Glu Val Gly Glu Ala Gly Gln Gly Lys Asp Phe Ile Ser Leu Gly 4250 4255 4260 Leu Gln Asp Gly His Leu Val Phe Arg Tyr Gln Leu Gly Ser Gly 4265 4270 4275 Glu Ala Arg Leu Val Ser Glu Asp Pro Ile Asn Asp Gly Glu Trp 4280 4285 4290 His Arg Val Thr Ala Leu Arg Glu Gly Arg Arg Gly Ser Ile Gln 4295 4300 4305 Val Asp Gly Glu Glu Leu Val Ser Gly Arg Ser Pro Gly Pro Asn 4310 4315 4320 Val Ala Val Asn Ala Lys Gly Ser Val Tyr Ile Gly Gly Ala Pro 4325 4330 4335 Asp Val Ala Thr Leu Thr Gly Gly Arg Phe Ser Ser Gly Ile Thr 4340 4345 4350 Gly Cys Val Lys Asn Leu Val Leu His Ser Ala Arg Pro Gly Ala 4355 4360 4365 Pro Pro Pro Gln Pro Leu Asp Leu Gln His Arg Ala Gln Ala Gly 4370 4375 4380 Ala Asn Thr Arg Pro Cys Pro Ser 4385 4390 <210> SEQ ID NO 51 <211> LENGTH: 184 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q9H875 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(184) <400> SEQUENCE: 51 Met Ala Ser Pro Ala Ala Ser Ser Val Arg Pro Pro Arg Pro Lys Lys 1 5 10 15 Glu Pro Gln Thr Leu Val Ile Pro Lys Asn Ala Ala Glu Glu Gln Lys 20 25 30 Leu Lys Leu Glu Arg Leu Met Lys Asn Pro Asp Lys Ala Val Pro Ile 35 40 45 Pro Glu Lys Met Ser Glu Trp Ala Pro Arg Pro Pro Pro Glu Phe Val 50 55 60 Arg Asp Val Met Gly Ser Ser Ala Gly Ala Gly Ser Gly Glu Phe His 65 70 75 80 Val Tyr Arg His Leu Arg Arg Arg Glu Tyr Gln Arg Gln Asp Tyr Met 85 90 95 Asp Ala Met Ala Glu Lys Gln Lys Leu Asp Ala Glu Phe Gln Lys Arg 100 105 110 Leu Glu Lys Asn Lys Ile Ala Ala Glu Glu Gln Thr Ala Lys Arg Arg 115 120 125 Lys Lys Arg Gln Lys Leu Lys Glu Lys Lys Leu Leu Ala Lys Lys Met 130 135 140 Lys Leu Glu Gln Lys Lys Gln Glu Gly Pro Gly Gln Pro Lys Glu Gln 145 150 155 160 Gly Ser Ser Ser Ser Ala Glu Ala Ser Gly Thr Glu Glu Glu Glu Glu 165 170 175 Val Pro Ser Phe Thr Met Gly Arg 180 <210> SEQ ID NO 52 <211> LENGTH: 427 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P25101 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(427) <400> SEQUENCE: 52 Met Glu Thr Leu Cys Leu Arg Ala Ser Phe Trp Leu Ala Leu Val Gly 1 5 10 15 Cys Val Ile Ser Asp Asn Pro Glu Arg Tyr Ser Thr Asn Leu Ser Asn 20 25 30 His Val Asp Asp Phe Thr Thr Phe Arg Gly Thr Glu Leu Ser Phe Leu 35 40 45 Val Thr Thr His Gln Pro Thr Asn Leu Val Leu Pro Ser Asn Gly Ser 50 55 60 Met His Asn Tyr Cys Pro Gln Gln Thr Lys Ile Thr Ser Ala Phe Lys 65 70 75 80 Tyr Ile Asn Thr Val Ile Ser Cys Thr Ile Phe Ile Val Gly Met Val 85 90 95 Gly Asn Ala Thr Leu Leu Arg Ile Ile Tyr Gln Asn Lys Cys Met Arg 100 105 110 Asn Gly Pro Asn Ala Leu Ile Ala Ser Leu Ala Leu Gly Asp Leu Ile 115 120 125 Tyr Val Val Ile Asp Leu Pro Ile Asn Val Phe Lys Leu Leu Ala Gly 130 135 140 Arg Trp Pro Phe Asp His Asn Asp Phe Gly Val Phe Leu Cys Lys Leu 145 150 155 160 Phe Pro Phe Leu Gln Lys Ser Ser Val Gly Ile Thr Val Leu Asn Leu 165 170 175 Cys Ala Leu Ser Val Asp Arg Tyr Arg Ala Val Ala Ser Trp Ser Arg 180 185 190 Val Gln Gly Ile Gly Ile Pro Leu Val Thr Ala Ile Glu Ile Val Ser 195 200 205 Ile Trp Ile Leu Ser Phe Ile Leu Ala Ile Pro Glu Ala Ile Gly Phe 210 215 220 Val Met Val Pro Phe Glu Tyr Arg Gly Glu Gln His Lys Thr Cys Met 225 230 235 240 Leu Asn Ala Thr Ser Lys Phe Met Glu Phe Tyr Gln Asp Val Lys Asp 245 250 255 Trp Trp Leu Phe Gly Phe Tyr Phe Cys Met Pro Leu Val Cys Thr Ala 260 265 270 Ile Phe Tyr Thr Leu Met Thr Cys Glu Met Leu Asn Arg Arg Asn Gly 275 280 285 Ser Leu Arg Ile Ala Leu Ser Glu His Leu Lys Gln Arg Arg Glu Val 290 295 300 Ala Lys Thr Val Phe Cys Leu Val Val Ile Phe Ala Leu Cys Trp Phe 305 310 315 320 Pro Leu His Leu Ser Arg Ile Leu Lys Lys Thr Val Tyr Asn Glu Met 325 330 335 Asp Lys Asn Arg Cys Glu Leu Leu Ser Phe Leu Leu Leu Met Asp Tyr 340 345 350 Ile Gly Ile Asn Leu Ala Thr Met Asn Ser Cys Ile Asn Pro Ile Ala 355 360 365 Leu Tyr Phe Val Ser Lys Lys Phe Lys Asn Cys Phe Gln Ser Cys Leu 370 375 380 Cys Cys Cys Cys Tyr Gln Ser Lys Ser Leu Met Thr Ser Val Pro Met 385 390 395 400 Asn Gly Thr Ser Ile Gln Trp Lys Asn His Asp Gln Asn Asn His Asn 405 410 415 Thr Asp Arg Ser Ser His Lys Asp Ser Met Asn 420 425 <210> SEQ ID NO 53 <211> LENGTH: 660 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O43155 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(660) <400> SEQUENCE: 53 Met Gly Leu Gln Thr Thr Lys Trp Pro Ser His Gly Ala Phe Phe Leu 1 5 10 15 Lys Ser Trp Leu Ile Ile Ser Leu Gly Leu Tyr Ser Gln Val Ser Lys 20 25 30 Leu Leu Ala Cys Pro Ser Val Cys Arg Cys Asp Arg Asn Phe Val Tyr 35 40 45 Cys Asn Glu Arg Ser Leu Thr Ser Val Pro Leu Gly Ile Pro Glu Gly 50 55 60 Val Thr Val Leu Tyr Leu His Asn Asn Gln Ile Asn Asn Ala Gly Phe 65 70 75 80 Pro Ala Glu Leu His Asn Val Gln Ser Val His Thr Val Tyr Leu Tyr 85 90 95 Gly Asn Gln Leu Asp Glu Phe Pro Met Asn Leu Pro Lys Asn Val Arg 100 105 110 Val Leu His Leu Gln Glu Asn Asn Ile Gln Thr Ile Ser Arg Ala Ala 115 120 125 Leu Ala Gln Leu Leu Lys Leu Glu Glu Leu His Leu Asp Asp Asn Ser 130 135 140 Ile Ser Thr Val Gly Val Glu Asp Gly Ala Phe Arg Glu Ala Ile Ser 145 150 155 160 Leu Lys Leu Leu Phe Leu Ser Lys Asn His Leu Ser Ser Val Pro Val 165 170 175 Gly Leu Pro Val Asp Leu Gln Glu Leu Arg Val Asp Glu Asn Arg Ile 180 185 190 Ala Val Ile Ser Asp Met Ala Phe Gln Asn Leu Thr Ser Leu Glu Arg 195 200 205 Leu Ile Val Asp Gly Asn Leu Leu Thr Asn Lys Gly Ile Ala Glu Gly 210 215 220 Thr Phe Ser His Leu Thr Lys Leu Lys Glu Phe Ser Ile Val Arg Asn 225 230 235 240

Ser Leu Ser His Pro Pro Pro Asp Leu Pro Gly Thr His Leu Ile Arg 245 250 255 Leu Tyr Leu Gln Asp Asn Gln Ile Asn His Ile Pro Leu Thr Ala Phe 260 265 270 Ser Asn Leu Arg Lys Leu Glu Arg Leu Asp Ile Ser Asn Asn Gln Leu 275 280 285 Arg Met Leu Thr Gln Gly Val Phe Asp Asn Leu Ser Asn Leu Lys Gln 290 295 300 Leu Thr Ala Arg Asn Asn Pro Trp Phe Cys Asp Cys Ser Ile Lys Trp 305 310 315 320 Val Thr Glu Trp Leu Lys Tyr Ile Pro Ser Ser Leu Asn Val Arg Gly 325 330 335 Phe Met Cys Gln Gly Pro Glu Gln Val Arg Gly Met Ala Val Arg Glu 340 345 350 Leu Asn Met Asn Leu Leu Ser Cys Pro Thr Thr Thr Pro Gly Leu Pro 355 360 365 Leu Phe Thr Pro Ala Pro Ser Thr Ala Ser Pro Thr Thr Gln Pro Pro 370 375 380 Thr Leu Ser Ile Pro Asn Pro Ser Arg Ser Tyr Thr Pro Pro Thr Pro 385 390 395 400 Thr Thr Ser Lys Leu Pro Thr Ile Pro Asp Trp Asp Gly Arg Glu Arg 405 410 415 Val Thr Pro Pro Ile Ser Glu Arg Ile Gln Leu Ser Ile His Phe Val 420 425 430 Asn Asp Thr Ser Ile Gln Val Ser Trp Leu Ser Leu Phe Thr Val Met 435 440 445 Ala Tyr Lys Leu Thr Trp Val Lys Met Gly His Ser Leu Val Gly Gly 450 455 460 Ile Val Gln Glu Arg Ile Val Ser Gly Glu Lys Gln His Leu Ser Leu 465 470 475 480 Val Asn Leu Glu Pro Arg Ser Thr Tyr Arg Ile Cys Leu Val Pro Leu 485 490 495 Asp Ala Phe Asn Tyr Arg Ala Val Glu Asp Thr Ile Cys Ser Glu Ala 500 505 510 Thr Thr His Ala Ser Tyr Leu Asn Asn Gly Ser Asn Thr Ala Ser Ser 515 520 525 His Glu Gln Thr Thr Ser His Ser Met Gly Ser Pro Phe Leu Leu Ala 530 535 540 Gly Leu Ile Gly Gly Ala Val Ile Phe Val Leu Val Val Leu Leu Ser 545 550 555 560 Val Phe Cys Trp His Met His Lys Lys Gly Arg Tyr Thr Ser Gln Lys 565 570 575 Trp Lys Tyr Asn Arg Gly Arg Arg Lys Asp Asp Tyr Cys Glu Ala Gly 580 585 590 Thr Lys Lys Asp Asn Ser Ile Leu Glu Met Thr Glu Thr Ser Phe Gln 595 600 605 Ile Val Ser Leu Asn Asn Asp Gln Leu Leu Lys Gly Asp Phe Arg Leu 610 615 620 Gln Pro Ile Tyr Thr Pro Asn Gly Gly Ile Asn Tyr Thr Asp Cys His 625 630 635 640 Ile Pro Asn Asn Met Arg Tyr Cys Asn Ser Ser Val Pro Asp Leu Glu 645 650 655 His Cys His Thr 660 <210> SEQ ID NO 54 <211> LENGTH: 466 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P08670 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(466) <400> SEQUENCE: 54 Met Ser Thr Arg Ser Val Ser Ser Ser Ser Tyr Arg Arg Met Phe Gly 1 5 10 15 Gly Pro Gly Thr Ala Ser Arg Pro Ser Ser Ser Arg Ser Tyr Val Thr 20 25 30 Thr Ser Thr Arg Thr Tyr Ser Leu Gly Ser Ala Leu Arg Pro Ser Thr 35 40 45 Ser Arg Ser Leu Tyr Ala Ser Ser Pro Gly Gly Val Tyr Ala Thr Arg 50 55 60 Ser Ser Ala Val Arg Leu Arg Ser Ser Val Pro Gly Val Arg Leu Leu 65 70 75 80 Gln Asp Ser Val Asp Phe Ser Leu Ala Asp Ala Ile Asn Thr Glu Phe 85 90 95 Lys Asn Thr Arg Thr Asn Glu Lys Val Glu Leu Gln Glu Leu Asn Asp 100 105 110 Arg Phe Ala Asn Tyr Ile Asp Lys Val Arg Phe Leu Glu Gln Gln Asn 115 120 125 Lys Ile Leu Leu Ala Glu Leu Glu Gln Leu Lys Gly Gln Gly Lys Ser 130 135 140 Arg Leu Gly Asp Leu Tyr Glu Glu Glu Met Arg Glu Leu Arg Arg Gln 145 150 155 160 Val Asp Gln Leu Thr Asn Asp Lys Ala Arg Val Glu Val Glu Arg Asp 165 170 175 Asn Leu Ala Glu Asp Ile Met Arg Leu Arg Glu Lys Leu Gln Glu Glu 180 185 190 Met Leu Gln Arg Glu Glu Ala Glu Asn Thr Leu Gln Ser Phe Arg Gln 195 200 205 Asp Val Asp Asn Ala Ser Leu Ala Arg Leu Asp Leu Glu Arg Lys Val 210 215 220 Glu Ser Leu Gln Glu Glu Ile Ala Phe Leu Lys Lys Leu His Glu Glu 225 230 235 240 Glu Ile Gln Glu Leu Gln Ala Gln Ile Gln Glu Gln His Val Gln Ile 245 250 255 Asp Val Asp Val Ser Lys Pro Asp Leu Thr Ala Ala Leu Arg Asp Val 260 265 270 Arg Gln Gln Tyr Glu Ser Val Ala Ala Lys Asn Leu Gln Glu Ala Glu 275 280 285 Glu Trp Tyr Lys Ser Lys Phe Ala Asp Leu Ser Glu Ala Ala Asn Arg 290 295 300 Asn Asn Asp Ala Leu Arg Gln Ala Lys Gln Glu Ser Thr Glu Tyr Arg 305 310 315 320 Arg Gln Val Gln Ser Leu Thr Cys Glu Val Asp Ala Leu Lys Gly Thr 325 330 335 Asn Glu Ser Leu Glu Arg Gln Met Arg Glu Met Glu Glu Asn Phe Ala 340 345 350 Val Glu Ala Ala Asn Tyr Gln Asp Thr Ile Gly Arg Leu Gln Asp Glu 355 360 365 Ile Gln Asn Met Lys Glu Glu Met Ala Arg His Leu Arg Glu Tyr Gln 370 375 380 Asp Leu Leu Asn Val Lys Met Ala Leu Asp Ile Glu Ile Ala Thr Tyr 385 390 395 400 Arg Lys Leu Leu Glu Gly Glu Glu Ser Arg Ile Ser Leu Pro Leu Pro 405 410 415 Asn Phe Ser Ser Leu Asn Leu Arg Glu Thr Asn Leu Asp Ser Leu Pro 420 425 430 Leu Val Asp Thr His Ser Lys Arg Thr Leu Leu Ile Lys Thr Val Glu 435 440 445 Thr Arg Asp Gly Gln Val Ile Asn Glu Thr Ser Gln His His Asp Asp 450 455 460 Leu Glu 465 <210> SEQ ID NO 55 <211> LENGTH: 359 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P30556 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(359) <400> SEQUENCE: 55 Met Ile Leu Asn Ser Ser Thr Glu Asp Gly Ile Lys Arg Ile Gln Asp 1 5 10 15 Asp Cys Pro Lys Ala Gly Arg His Asn Tyr Ile Phe Val Met Ile Pro 20 25 30 Thr Leu Tyr Ser Ile Ile Phe Val Val Gly Ile Phe Gly Asn Ser Leu 35 40 45 Val Val Ile Val Ile Tyr Phe Tyr Met Lys Leu Lys Thr Val Ala Ser 50 55 60 Val Phe Leu Leu Asn Leu Ala Leu Ala Asp Leu Cys Phe Leu Leu Thr 65 70 75 80 Leu Pro Leu Trp Ala Val Tyr Thr Ala Met Glu Tyr Arg Trp Pro Phe 85 90 95 Gly Asn Tyr Leu Cys Lys Ile Ala Ser Ala Ser Val Ser Phe Asn Leu 100 105 110 Tyr Ala Ser Val Phe Leu Leu Thr Cys Leu Ser Ile Asp Arg Tyr Leu 115 120 125 Ala Ile Val His Pro Met Lys Ser Arg Leu Arg Arg Thr Met Leu Val 130 135 140 Ala Lys Val Thr Cys Ile Ile Ile Trp Leu Leu Ala Gly Leu Ala Ser 145 150 155 160 Leu Pro Ala Ile Ile His Arg Asn Val Phe Phe Ile Glu Asn Thr Asn 165 170 175 Ile Thr Val Cys Ala Phe His Tyr Glu Ser Gln Asn Ser Thr Leu Pro 180 185 190 Ile Gly Leu Gly Leu Thr Lys Asn Ile Leu Gly Phe Leu Phe Pro Phe 195 200 205 Leu Ile Ile Leu Thr Ser Tyr Thr Leu Ile Trp Lys Ala Leu Lys Lys 210 215 220 Ala Tyr Glu Ile Gln Lys Asn Lys Pro Arg Asn Asp Asp Ile Phe Lys 225 230 235 240 Ile Ile Met Ala Ile Val Leu Phe Phe Phe Phe Ser Trp Ile Pro His 245 250 255 Gln Ile Phe Thr Phe Leu Asp Val Leu Ile Gln Leu Gly Ile Ile Arg 260 265 270 Asp Cys Arg Ile Ala Asp Ile Val Asp Thr Ala Met Pro Ile Thr Ile 275 280 285 Cys Ile Ala Tyr Phe Asn Asn Cys Leu Asn Pro Leu Phe Tyr Gly Phe 290 295 300

Leu Gly Lys Lys Phe Lys Arg Tyr Phe Leu Gln Leu Leu Lys Tyr Ile 305 310 315 320 Pro Pro Lys Ala Lys Ser His Ser Asn Leu Ser Thr Lys Met Ser Thr 325 330 335 Leu Ser Tyr Arg Pro Ser Asp Asn Val Ser Ser Ser Thr Lys Lys Pro 340 345 350 Ala Pro Cys Phe Glu Val Glu 355 <210> SEQ ID NO 56 <211> LENGTH: 1053 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q2KHT3 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1053) <400> SEQUENCE: 56 Met Phe Gly Arg Ser Arg Ser Trp Val Gly Gly Gly His Gly Lys Thr 1 5 10 15 Ser Arg Asn Ile His Ser Leu Asp His Leu Lys Tyr Leu Tyr His Val 20 25 30 Leu Thr Lys Asn Thr Thr Val Thr Glu Gln Asn Arg Asn Leu Leu Val 35 40 45 Glu Thr Ile Arg Ser Ile Thr Glu Ile Leu Ile Trp Gly Asp Gln Asn 50 55 60 Asp Ser Ser Val Phe Asp Phe Phe Leu Glu Lys Asn Met Phe Val Phe 65 70 75 80 Phe Leu Asn Ile Leu Arg Gln Lys Ser Gly Arg Tyr Val Cys Val Gln 85 90 95 Leu Leu Gln Thr Leu Asn Ile Leu Phe Glu Asn Ile Ser His Glu Thr 100 105 110 Ser Leu Tyr Tyr Leu Leu Ser Asn Asn Tyr Val Asn Ser Ile Ile Val 115 120 125 His Lys Phe Asp Phe Ser Asp Glu Glu Ile Met Ala Tyr Tyr Ile Ser 130 135 140 Phe Leu Lys Thr Leu Ser Leu Lys Leu Asn Asn His Thr Val His Phe 145 150 155 160 Phe Tyr Asn Glu His Thr Asn Asp Phe Ala Leu Tyr Thr Glu Ala Ile 165 170 175 Lys Phe Phe Asn His Pro Glu Ser Met Val Arg Ile Ala Val Arg Thr 180 185 190 Ile Thr Leu Asn Val Tyr Lys Val Ser Leu Asp Asn Gln Ala Met Leu 195 200 205 His Tyr Ile Arg Asp Lys Thr Ala Val Pro Tyr Phe Ser Asn Leu Val 210 215 220 Trp Phe Ile Gly Ser His Val Ile Glu Leu Asp Asp Cys Val Gln Thr 225 230 235 240 Asp Glu Glu His Arg Asn Arg Gly Lys Leu Ser Asp Leu Val Ala Glu 245 250 255 His Leu Asp His Leu His Tyr Leu Asn Asp Ile Leu Ile Ile Asn Cys 260 265 270 Glu Phe Leu Asn Asp Val Leu Thr Asp His Leu Leu Asn Arg Leu Phe 275 280 285 Leu Pro Leu Tyr Val Tyr Ser Leu Glu Asn Gln Asp Lys Gly Gly Glu 290 295 300 Arg Pro Lys Ile Ser Leu Pro Val Ser Leu Tyr Leu Leu Ser Gln Val 305 310 315 320 Phe Leu Ile Ile His His Ala Pro Leu Val Asn Ser Leu Ala Glu Val 325 330 335 Ile Leu Asn Gly Asp Leu Ser Glu Met Tyr Ala Lys Thr Glu Gln Asp 340 345 350 Ile Gln Arg Ser Ser Ala Lys Pro Ser Ile Arg Cys Phe Ile Lys Pro 355 360 365 Thr Glu Thr Leu Glu Arg Ser Leu Glu Met Asn Lys His Lys Gly Lys 370 375 380 Arg Arg Val Gln Lys Arg Pro Asn Tyr Lys Asn Val Gly Glu Glu Glu 385 390 395 400 Asp Glu Glu Lys Gly Pro Thr Glu Asp Ala Gln Glu Asp Ala Glu Lys 405 410 415 Ala Lys Gly Thr Glu Gly Gly Ser Lys Gly Ile Lys Thr Ser Gly Glu 420 425 430 Ser Glu Glu Ile Glu Met Val Ile Met Glu Arg Ser Lys Leu Ser Glu 435 440 445 Leu Ala Ala Ser Thr Ser Val Gln Glu Gln Asn Thr Thr Asp Glu Glu 450 455 460 Lys Ser Ala Ala Ala Thr Cys Ser Glu Ser Thr Gln Trp Ser Arg Pro 465 470 475 480 Phe Leu Asp Met Val Tyr His Ala Leu Asp Ser Pro Asp Asp Asp Tyr 485 490 495 His Ala Leu Phe Val Leu Cys Leu Leu Tyr Ala Met Ser His Asn Lys 500 505 510 Gly Met Asp Pro Glu Lys Leu Glu Arg Ile Gln Leu Pro Val Pro Asn 515 520 525 Ala Ala Glu Lys Thr Thr Tyr Asn His Pro Leu Ala Glu Arg Leu Ile 530 535 540 Arg Ile Met Asn Asn Ala Ala Gln Pro Asp Gly Lys Ile Arg Leu Ala 545 550 555 560 Thr Leu Glu Leu Ser Cys Leu Leu Leu Lys Gln Gln Val Leu Met Ser 565 570 575 Ala Gly Cys Ile Met Lys Asp Val His Leu Ala Cys Leu Glu Gly Ala 580 585 590 Arg Glu Glu Ser Val His Leu Val Arg His Phe Tyr Lys Gly Glu Asp 595 600 605 Ile Phe Leu Asp Met Phe Glu Asp Glu Tyr Arg Ser Met Thr Met Lys 610 615 620 Pro Met Asn Val Glu Tyr Leu Met Met Asp Ala Ser Ile Leu Leu Pro 625 630 635 640 Pro Thr Gly Thr Pro Leu Thr Gly Ile Asp Phe Val Lys Arg Leu Pro 645 650 655 Cys Gly Asp Val Glu Lys Thr Arg Arg Ala Ile Arg Val Phe Phe Met 660 665 670 Leu Arg Ser Leu Ser Leu Gln Leu Arg Gly Glu Pro Glu Thr Gln Leu 675 680 685 Pro Leu Thr Arg Glu Glu Asp Leu Ile Lys Thr Asp Asp Val Leu Asp 690 695 700 Leu Asn Asn Ser Asp Leu Ile Ala Cys Thr Val Ile Thr Lys Asp Gly 705 710 715 720 Gly Met Val Gln Arg Phe Leu Ala Val Asp Ile Tyr Gln Met Ser Leu 725 730 735 Val Glu Pro Asp Val Ser Arg Leu Gly Trp Gly Val Val Lys Phe Ala 740 745 750 Gly Leu Leu Gln Asp Met Gln Val Thr Gly Val Glu Asp Asp Ser Arg 755 760 765 Ala Leu Asn Ile Thr Ile His Lys Pro Ala Ser Ser Pro His Ser Lys 770 775 780 Pro Phe Pro Ile Leu Gln Ala Thr Phe Ile Phe Ser Asp His Ile Arg 785 790 795 800 Cys Ile Ile Ala Lys Gln Arg Leu Ala Lys Gly Arg Ile Gln Ala Arg 805 810 815 Arg Met Lys Met Gln Arg Ile Ala Ala Leu Leu Asp Leu Pro Ile Gln 820 825 830 Pro Thr Thr Glu Val Leu Gly Phe Gly Leu Gly Ser Ser Thr Ser Thr 835 840 845 Gln His Leu Pro Phe Arg Phe Tyr Asp Gln Gly Arg Arg Gly Ser Ser 850 855 860 Asp Pro Thr Val Gln Arg Ser Val Phe Ala Ser Val Asp Lys Val Pro 865 870 875 880 Gly Phe Ala Val Ala Gln Cys Ile Asn Gln His Ser Ser Pro Ser Leu 885 890 895 Ser Ser Gln Ser Pro Pro Ser Ala Ser Gly Ser Pro Ser Gly Ser Gly 900 905 910 Ser Thr Ser His Cys Asp Ser Gly Gly Thr Ser Ser Ser Ser Thr Pro 915 920 925 Ser Thr Ala Gln Ser Pro Ala Asp Ala Pro Met Ser Pro Glu Leu Pro 930 935 940 Lys Pro His Leu Pro Asp Gln Leu Val Ile Val Asn Glu Thr Glu Ala 945 950 955 960 Asp Ser Lys Pro Ser Lys Asn Val Ala Arg Ser Ala Ala Val Glu Thr 965 970 975 Ala Ser Leu Ser Pro Ser Leu Val Pro Ala Arg Gln Pro Thr Ile Ser 980 985 990 Leu Leu Cys Glu Asp Thr Ala Asp Thr Leu Ser Val Glu Ser Leu Thr 995 1000 1005 Leu Val Pro Pro Val Asp Pro His Ser Leu Arg Ser Leu Thr Gly 1010 1015 1020 Met Pro Pro Leu Ser Thr Pro Ala Ala Ala Cys Thr Glu Pro Val 1025 1030 1035 Gly Glu Glu Ala Ala Cys Ala Glu Pro Val Gly Thr Ala Glu Asp 1040 1045 1050 <210> SEQ ID NO 57 <211> LENGTH: 1464 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02452 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1464) <400> SEQUENCE: 57 Met Phe Ser Phe Val Asp Leu Arg Leu Leu Leu Leu Leu Ala Ala Thr 1 5 10 15 Ala Leu Leu Thr His Gly Gln Glu Glu Gly Gln Val Glu Gly Gln Asp 20 25 30 Glu Asp Ile Pro Pro Ile Thr Cys Val Gln Asn Gly Leu Arg Tyr His 35 40 45 Asp Arg Asp Val Trp Lys Pro Glu Pro Cys Arg Ile Cys Val Cys Asp 50 55 60 Asn Gly Lys Val Leu Cys Asp Asp Val Ile Cys Asp Glu Thr Lys Asn 65 70 75 80 Cys Pro Gly Ala Glu Val Pro Glu Gly Glu Cys Cys Pro Val Cys Pro

85 90 95 Asp Gly Ser Glu Ser Pro Thr Asp Gln Glu Thr Thr Gly Val Glu Gly 100 105 110 Pro Lys Gly Asp Thr Gly Pro Arg Gly Pro Arg Gly Pro Ala Gly Pro 115 120 125 Pro Gly Arg Asp Gly Ile Pro Gly Gln Pro Gly Leu Pro Gly Pro Pro 130 135 140 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly Gly Asn Phe Ala 145 150 155 160 Pro Gln Leu Ser Tyr Gly Tyr Asp Glu Lys Ser Thr Gly Gly Ile Ser 165 170 175 Val Pro Gly Pro Met Gly Pro Ser Gly Pro Arg Gly Leu Pro Gly Pro 180 185 190 Pro Gly Ala Pro Gly Pro Gln Gly Phe Gln Gly Pro Pro Gly Glu Pro 195 200 205 Gly Glu Pro Gly Ala Ser Gly Pro Met Gly Pro Arg Gly Pro Pro Gly 210 215 220 Pro Pro Gly Lys Asn Gly Asp Asp Gly Glu Ala Gly Lys Pro Gly Arg 225 230 235 240 Pro Gly Glu Arg Gly Pro Pro Gly Pro Gln Gly Ala Arg Gly Leu Pro 245 250 255 Gly Thr Ala Gly Leu Pro Gly Met Lys Gly His Arg Gly Phe Ser Gly 260 265 270 Leu Asp Gly Ala Lys Gly Asp Ala Gly Pro Ala Gly Pro Lys Gly Glu 275 280 285 Pro Gly Ser Pro Gly Glu Asn Gly Ala Pro Gly Gln Met Gly Pro Arg 290 295 300 Gly Leu Pro Gly Glu Arg Gly Arg Pro Gly Ala Pro Gly Pro Ala Gly 305 310 315 320 Ala Arg Gly Asn Asp Gly Ala Thr Gly Ala Ala Gly Pro Pro Gly Pro 325 330 335 Thr Gly Pro Ala Gly Pro Pro Gly Phe Pro Gly Ala Val Gly Ala Lys 340 345 350 Gly Glu Ala Gly Pro Gln Gly Pro Arg Gly Ser Glu Gly Pro Gln Gly 355 360 365 Val Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Ala Ala Gly Pro 370 375 380 Ala Gly Asn Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Ala Asn 385 390 395 400 Gly Ala Pro Gly Ile Ala Gly Ala Pro Gly Phe Pro Gly Ala Arg Gly 405 410 415 Pro Ser Gly Pro Gln Gly Pro Gly Gly Pro Pro Gly Pro Lys Gly Asn 420 425 430 Ser Gly Glu Pro Gly Ala Pro Gly Ser Lys Gly Asp Thr Gly Ala Lys 435 440 445 Gly Glu Pro Gly Pro Val Gly Val Gln Gly Pro Pro Gly Pro Ala Gly 450 455 460 Glu Glu Gly Lys Arg Gly Ala Arg Gly Glu Pro Gly Pro Thr Gly Leu 465 470 475 480 Pro Gly Pro Pro Gly Glu Arg Gly Gly Pro Gly Ser Arg Gly Phe Pro 485 490 495 Gly Ala Asp Gly Val Ala Gly Pro Lys Gly Pro Ala Gly Glu Arg Gly 500 505 510 Ser Pro Gly Pro Ala Gly Pro Lys Gly Ser Pro Gly Glu Ala Gly Arg 515 520 525 Pro Gly Glu Ala Gly Leu Pro Gly Ala Lys Gly Leu Thr Gly Ser Pro 530 535 540 Gly Ser Pro Gly Pro Asp Gly Lys Thr Gly Pro Pro Gly Pro Ala Gly 545 550 555 560 Gln Asp Gly Arg Pro Gly Pro Pro Gly Pro Pro Gly Ala Arg Gly Gln 565 570 575 Ala Gly Val Met Gly Phe Pro Gly Pro Lys Gly Ala Ala Gly Glu Pro 580 585 590 Gly Lys Ala Gly Glu Arg Gly Val Pro Gly Pro Pro Gly Ala Val Gly 595 600 605 Pro Ala Gly Lys Asp Gly Glu Ala Gly Ala Gln Gly Pro Pro Gly Pro 610 615 620 Ala Gly Pro Ala Gly Glu Arg Gly Glu Gln Gly Pro Ala Gly Ser Pro 625 630 635 640 Gly Phe Gln Gly Leu Pro Gly Pro Ala Gly Pro Pro Gly Glu Ala Gly 645 650 655 Lys Pro Gly Glu Gln Gly Val Pro Gly Asp Leu Gly Ala Pro Gly Pro 660 665 670 Ser Gly Ala Arg Gly Glu Arg Gly Phe Pro Gly Glu Arg Gly Val Gln 675 680 685 Gly Pro Pro Gly Pro Ala Gly Pro Arg Gly Ala Asn Gly Ala Pro Gly 690 695 700 Asn Asp Gly Ala Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly Ser 705 710 715 720 Gln Gly Ala Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Ala Ala 725 730 735 Gly Leu Pro Gly Pro Lys Gly Asp Arg Gly Asp Ala Gly Pro Lys Gly 740 745 750 Ala Asp Gly Ser Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro 755 760 765 Ile Gly Pro Pro Gly Pro Ala Gly Ala Pro Gly Asp Lys Gly Glu Ser 770 775 780 Gly Pro Ser Gly Pro Ala Gly Pro Thr Gly Ala Arg Gly Ala Pro Gly 785 790 795 800 Asp Arg Gly Glu Pro Gly Pro Pro Gly Pro Ala Gly Phe Ala Gly Pro 805 810 815 Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys Gly Glu Pro Gly Asp Ala 820 825 830 Gly Ala Lys Gly Asp Ala Gly Pro Pro Gly Pro Ala Gly Pro Ala Gly 835 840 845 Pro Pro Gly Pro Ile Gly Asn Val Gly Ala Pro Gly Ala Lys Gly Ala 850 855 860 Arg Gly Ser Ala Gly Pro Pro Gly Ala Thr Gly Phe Pro Gly Ala Ala 865 870 875 880 Gly Arg Val Gly Pro Pro Gly Pro Ser Gly Asn Ala Gly Pro Pro Gly 885 890 895 Pro Pro Gly Pro Ala Gly Lys Glu Gly Gly Lys Gly Pro Arg Gly Glu 900 905 910 Thr Gly Pro Ala Gly Arg Pro Gly Glu Val Gly Pro Pro Gly Pro Pro 915 920 925 Gly Pro Ala Gly Glu Lys Gly Ser Pro Gly Ala Asp Gly Pro Ala Gly 930 935 940 Ala Pro Gly Thr Pro Gly Pro Gln Gly Ile Ala Gly Gln Arg Gly Val 945 950 955 960 Val Gly Leu Pro Gly Gln Arg Gly Glu Arg Gly Phe Pro Gly Leu Pro 965 970 975 Gly Pro Ser Gly Glu Pro Gly Lys Gln Gly Pro Ser Gly Ala Ser Gly 980 985 990 Glu Arg Gly Pro Pro Gly Pro Met Gly Pro Pro Gly Leu Ala Gly Pro 995 1000 1005 Pro Gly Glu Ser Gly Arg Glu Gly Ala Pro Gly Ala Glu Gly Ser 1010 1015 1020 Pro Gly Arg Asp Gly Ser Pro Gly Ala Lys Gly Asp Arg Gly Glu 1025 1030 1035 Thr Gly Pro Ala Gly Pro Pro Gly Ala Pro Gly Ala Pro Gly Ala 1040 1045 1050 Pro Gly Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu 1055 1060 1065 Thr Gly Pro Ala Gly Pro Thr Gly Pro Val Gly Pro Val Gly Ala 1070 1075 1080 Arg Gly Pro Ala Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu 1085 1090 1095 Thr Gly Glu Gln Gly Asp Arg Gly Ile Lys Gly His Arg Gly Phe 1100 1105 1110 Ser Gly Leu Gln Gly Pro Pro Gly Pro Pro Gly Ser Pro Gly Glu 1115 1120 1125 Gln Gly Pro Ser Gly Ala Ser Gly Pro Ala Gly Pro Arg Gly Pro 1130 1135 1140 Pro Gly Ser Ala Gly Ala Pro Gly Lys Asp Gly Leu Asn Gly Leu 1145 1150 1155 Pro Gly Pro Ile Gly Pro Pro Gly Pro Arg Gly Arg Thr Gly Asp 1160 1165 1170 Ala Gly Pro Val Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro 1175 1180 1185 Pro Gly Pro Pro Ser Ala Gly Phe Asp Phe Ser Phe Leu Pro Gln 1190 1195 1200 Pro Pro Gln Glu Lys Ala His Asp Gly Gly Arg Tyr Tyr Arg Ala 1205 1210 1215 Asp Asp Ala Asn Val Val Arg Asp Arg Asp Leu Glu Val Asp Thr 1220 1225 1230 Thr Leu Lys Ser Leu Ser Gln Gln Ile Glu Asn Ile Arg Ser Pro 1235 1240 1245 Glu Gly Ser Arg Lys Asn Pro Ala Arg Thr Cys Arg Asp Leu Lys 1250 1255 1260 Met Cys His Ser Asp Trp Lys Ser Gly Glu Tyr Trp Ile Asp Pro 1265 1270 1275 Asn Gln Gly Cys Asn Leu Asp Ala Ile Lys Val Phe Cys Asn Met 1280 1285 1290 Glu Thr Gly Glu Thr Cys Val Tyr Pro Thr Gln Pro Ser Val Ala 1295 1300 1305 Gln Lys Asn Trp Tyr Ile Ser Lys Asn Pro Lys Asp Lys Arg His 1310 1315 1320 Val Trp Phe Gly Glu Ser Met Thr Asp Gly Phe Gln Phe Glu Tyr 1325 1330 1335 Gly Gly Gln Gly Ser Asp Pro Ala Asp Val Ala Ile Gln Leu Thr 1340 1345 1350 Phe Leu Arg Leu Met Ser Thr Glu Ala Ser Gln Asn Ile Thr Tyr 1355 1360 1365 His Cys Lys Asn Ser Val Ala Tyr Met Asp Gln Gln Thr Gly Asn 1370 1375 1380 Leu Lys Lys Ala Leu Leu Leu Gln Gly Ser Asn Glu Ile Glu Ile 1385 1390 1395

Arg Ala Glu Gly Asn Ser Arg Phe Thr Tyr Ser Val Thr Val Asp 1400 1405 1410 Gly Cys Thr Ser His Thr Gly Ala Trp Gly Lys Thr Val Ile Glu 1415 1420 1425 Tyr Lys Thr Thr Lys Thr Ser Arg Leu Pro Ile Ile Asp Val Ala 1430 1435 1440 Pro Leu Asp Val Gly Ala Pro Asp Gln Glu Phe Gly Phe Asp Val 1445 1450 1455 Gly Pro Val Cys Phe Leu 1460 <210> SEQ ID NO 58 <211> LENGTH: 1487 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02458 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1487) <400> SEQUENCE: 58 Met Ile Arg Leu Gly Ala Pro Gln Thr Leu Val Leu Leu Thr Leu Leu 1 5 10 15 Val Ala Ala Val Leu Arg Cys Gln Gly Gln Asp Val Gln Glu Ala Gly 20 25 30 Ser Cys Val Gln Asp Gly Gln Arg Tyr Asn Asp Lys Asp Val Trp Lys 35 40 45 Pro Glu Pro Cys Arg Ile Cys Val Cys Asp Thr Gly Thr Val Leu Cys 50 55 60 Asp Asp Ile Ile Cys Glu Asp Val Lys Asp Cys Leu Ser Pro Glu Ile 65 70 75 80 Pro Phe Gly Glu Cys Cys Pro Ile Cys Pro Thr Asp Leu Ala Thr Ala 85 90 95 Ser Gly Gln Pro Gly Pro Lys Gly Gln Lys Gly Glu Pro Gly Asp Ile 100 105 110 Lys Asp Ile Val Gly Pro Lys Gly Pro Pro Gly Pro Gln Gly Pro Ala 115 120 125 Gly Glu Gln Gly Pro Arg Gly Asp Arg Gly Asp Lys Gly Glu Lys Gly 130 135 140 Ala Pro Gly Pro Arg Gly Arg Asp Gly Glu Pro Gly Thr Pro Gly Asn 145 150 155 160 Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Leu Gly 165 170 175 Gly Asn Phe Ala Ala Gln Met Ala Gly Gly Phe Asp Glu Lys Ala Gly 180 185 190 Gly Ala Gln Leu Gly Val Met Gln Gly Pro Met Gly Pro Met Gly Pro 195 200 205 Arg Gly Pro Pro Gly Pro Ala Gly Ala Pro Gly Pro Gln Gly Phe Gln 210 215 220 Gly Asn Pro Gly Glu Pro Gly Glu Pro Gly Val Ser Gly Pro Met Gly 225 230 235 240 Pro Arg Gly Pro Pro Gly Pro Pro Gly Lys Pro Gly Asp Asp Gly Glu 245 250 255 Ala Gly Lys Pro Gly Lys Ala Gly Glu Arg Gly Pro Pro Gly Pro Gln 260 265 270 Gly Ala Arg Gly Phe Pro Gly Thr Pro Gly Leu Pro Gly Val Lys Gly 275 280 285 His Arg Gly Tyr Pro Gly Leu Asp Gly Ala Lys Gly Glu Ala Gly Ala 290 295 300 Pro Gly Val Lys Gly Glu Ser Gly Ser Pro Gly Glu Asn Gly Ser Pro 305 310 315 320 Gly Pro Met Gly Pro Arg Gly Leu Pro Gly Glu Arg Gly Arg Thr Gly 325 330 335 Pro Ala Gly Ala Ala Gly Ala Arg Gly Asn Asp Gly Gln Pro Gly Pro 340 345 350 Ala Gly Pro Pro Gly Pro Val Gly Pro Ala Gly Gly Pro Gly Phe Pro 355 360 365 Gly Ala Pro Gly Ala Lys Gly Glu Ala Gly Pro Thr Gly Ala Arg Gly 370 375 380 Pro Glu Gly Ala Gln Gly Pro Arg Gly Glu Pro Gly Thr Pro Gly Ser 385 390 395 400 Pro Gly Pro Ala Gly Ala Ser Gly Asn Pro Gly Thr Asp Gly Ile Pro 405 410 415 Gly Ala Lys Gly Ser Ala Gly Ala Pro Gly Ile Ala Gly Ala Pro Gly 420 425 430 Phe Pro Gly Pro Arg Gly Pro Pro Gly Pro Gln Gly Ala Thr Gly Pro 435 440 445 Leu Gly Pro Lys Gly Gln Thr Gly Glu Pro Gly Ile Ala Gly Phe Lys 450 455 460 Gly Glu Gln Gly Pro Lys Gly Glu Pro Gly Pro Ala Gly Pro Gln Gly 465 470 475 480 Ala Pro Gly Pro Ala Gly Glu Glu Gly Lys Arg Gly Ala Arg Gly Glu 485 490 495 Pro Gly Gly Val Gly Pro Ile Gly Pro Pro Gly Glu Arg Gly Ala Pro 500 505 510 Gly Asn Arg Gly Phe Pro Gly Gln Asp Gly Leu Ala Gly Pro Lys Gly 515 520 525 Ala Pro Gly Glu Arg Gly Pro Ser Gly Leu Ala Gly Pro Lys Gly Ala 530 535 540 Asn Gly Asp Pro Gly Arg Pro Gly Glu Pro Gly Leu Pro Gly Ala Arg 545 550 555 560 Gly Leu Thr Gly Arg Pro Gly Asp Ala Gly Pro Gln Gly Lys Val Gly 565 570 575 Pro Ser Gly Ala Pro Gly Glu Asp Gly Arg Pro Gly Pro Pro Gly Pro 580 585 590 Gln Gly Ala Arg Gly Gln Pro Gly Val Met Gly Phe Pro Gly Pro Lys 595 600 605 Gly Ala Asn Gly Glu Pro Gly Lys Ala Gly Glu Lys Gly Leu Pro Gly 610 615 620 Ala Pro Gly Leu Arg Gly Leu Pro Gly Lys Asp Gly Glu Thr Gly Ala 625 630 635 640 Ala Gly Pro Pro Gly Pro Ala Gly Pro Ala Gly Glu Arg Gly Glu Gln 645 650 655 Gly Ala Pro Gly Pro Ser Gly Phe Gln Gly Leu Pro Gly Pro Pro Gly 660 665 670 Pro Pro Gly Glu Gly Gly Lys Pro Gly Asp Gln Gly Val Pro Gly Glu 675 680 685 Ala Gly Ala Pro Gly Leu Val Gly Pro Arg Gly Glu Arg Gly Phe Pro 690 695 700 Gly Glu Arg Gly Ser Pro Gly Ala Gln Gly Leu Gln Gly Pro Arg Gly 705 710 715 720 Leu Pro Gly Thr Pro Gly Thr Asp Gly Pro Lys Gly Ala Ser Gly Pro 725 730 735 Ala Gly Pro Pro Gly Ala Gln Gly Pro Pro Gly Leu Gln Gly Met Pro 740 745 750 Gly Glu Arg Gly Ala Ala Gly Ile Ala Gly Pro Lys Gly Asp Arg Gly 755 760 765 Asp Val Gly Glu Lys Gly Pro Glu Gly Ala Pro Gly Lys Asp Gly Gly 770 775 780 Arg Gly Leu Thr Gly Pro Ile Gly Pro Pro Gly Pro Ala Gly Ala Asn 785 790 795 800 Gly Glu Lys Gly Glu Val Gly Pro Pro Gly Pro Ala Gly Ser Ala Gly 805 810 815 Ala Arg Gly Ala Pro Gly Glu Arg Gly Glu Thr Gly Pro Pro Gly Pro 820 825 830 Ala Gly Phe Ala Gly Pro Pro Gly Ala Asp Gly Gln Pro Gly Ala Lys 835 840 845 Gly Glu Gln Gly Glu Ala Gly Gln Lys Gly Asp Ala Gly Ala Pro Gly 850 855 860 Pro Gln Gly Pro Ser Gly Ala Pro Gly Pro Gln Gly Pro Thr Gly Val 865 870 875 880 Thr Gly Pro Lys Gly Ala Arg Gly Ala Gln Gly Pro Pro Gly Ala Thr 885 890 895 Gly Phe Pro Gly Ala Ala Gly Arg Val Gly Pro Pro Gly Ser Asn Gly 900 905 910 Asn Pro Gly Pro Pro Gly Pro Pro Gly Pro Ser Gly Lys Asp Gly Pro 915 920 925 Lys Gly Ala Arg Gly Asp Ser Gly Pro Pro Gly Arg Ala Gly Glu Pro 930 935 940 Gly Leu Gln Gly Pro Ala Gly Pro Pro Gly Glu Lys Gly Glu Pro Gly 945 950 955 960 Asp Asp Gly Pro Ser Gly Ala Glu Gly Pro Pro Gly Pro Gln Gly Leu 965 970 975 Ala Gly Gln Arg Gly Ile Val Gly Leu Pro Gly Gln Arg Gly Glu Arg 980 985 990 Gly Phe Pro Gly Leu Pro Gly Pro Ser Gly Glu Pro Gly Lys Gln Gly 995 1000 1005 Ala Pro Gly Ala Ser Gly Asp Arg Gly Pro Pro Gly Pro Val Gly 1010 1015 1020 Pro Pro Gly Leu Thr Gly Pro Ala Gly Glu Pro Gly Arg Glu Gly 1025 1030 1035 Ser Pro Gly Ala Asp Gly Pro Pro Gly Arg Asp Gly Ala Ala Gly 1040 1045 1050 Val Lys Gly Asp Arg Gly Glu Thr Gly Ala Val Gly Ala Pro Gly 1055 1060 1065 Ala Pro Gly Pro Pro Gly Ser Pro Gly Pro Ala Gly Pro Thr Gly 1070 1075 1080 Lys Gln Gly Asp Arg Gly Glu Ala Gly Ala Gln Gly Pro Met Gly 1085 1090 1095 Pro Ser Gly Pro Ala Gly Ala Arg Gly Ile Gln Gly Pro Gln Gly 1100 1105 1110 Pro Arg Gly Asp Lys Gly Glu Ala Gly Glu Pro Gly Glu Arg Gly 1115 1120 1125 Leu Lys Gly His Arg Gly Phe Thr Gly Leu Gln Gly Leu Pro Gly 1130 1135 1140 Pro Pro Gly Pro Ser Gly Asp Gln Gly Ala Ser Gly Pro Ala Gly 1145 1150 1155 Pro Ser Gly Pro Arg Gly Pro Pro Gly Pro Val Gly Pro Ser Gly 1160 1165 1170 Lys Asp Gly Ala Asn Gly Ile Pro Gly Pro Ile Gly Pro Pro Gly 1175 1180 1185

Pro Arg Gly Arg Ser Gly Glu Thr Gly Pro Ala Gly Pro Pro Gly 1190 1195 1200 Asn Pro Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Pro Gly Ile 1205 1210 1215 Asp Met Ser Ala Phe Ala Gly Leu Gly Pro Arg Glu Lys Gly Pro 1220 1225 1230 Asp Pro Leu Gln Tyr Met Arg Ala Asp Gln Ala Ala Gly Gly Leu 1235 1240 1245 Arg Gln His Asp Ala Glu Val Asp Ala Thr Leu Lys Ser Leu Asn 1250 1255 1260 Asn Gln Ile Glu Ser Ile Arg Ser Pro Glu Gly Ser Arg Lys Asn 1265 1270 1275 Pro Ala Arg Thr Cys Arg Asp Leu Lys Leu Cys His Pro Glu Trp 1280 1285 1290 Lys Ser Gly Asp Tyr Trp Ile Asp Pro Asn Gln Gly Cys Thr Leu 1295 1300 1305 Asp Ala Met Lys Val Phe Cys Asn Met Glu Thr Gly Glu Thr Cys 1310 1315 1320 Val Tyr Pro Asn Pro Ala Asn Val Pro Lys Lys Asn Trp Trp Ser 1325 1330 1335 Ser Lys Ser Lys Glu Lys Lys His Ile Trp Phe Gly Glu Thr Ile 1340 1345 1350 Asn Gly Gly Phe His Phe Ser Tyr Gly Asp Asp Asn Leu Ala Pro 1355 1360 1365 Asn Thr Ala Asn Val Gln Met Thr Phe Leu Arg Leu Leu Ser Thr 1370 1375 1380 Glu Gly Ser Gln Asn Ile Thr Tyr His Cys Lys Asn Ser Ile Ala 1385 1390 1395 Tyr Leu Asp Glu Ala Ala Gly Asn Leu Lys Lys Ala Leu Leu Ile 1400 1405 1410 Gln Gly Ser Asn Asp Val Glu Ile Arg Ala Glu Gly Asn Ser Arg 1415 1420 1425 Phe Thr Tyr Thr Ala Leu Lys Asp Gly Cys Thr Lys His Thr Gly 1430 1435 1440 Lys Trp Gly Lys Thr Val Ile Glu Tyr Arg Ser Gln Lys Thr Ser 1445 1450 1455 Arg Leu Pro Ile Ile Asp Ile Ala Pro Met Asp Ile Gly Gly Pro 1460 1465 1470 Glu Gln Glu Phe Gly Val Asp Ile Gly Pro Val Cys Phe Leu 1475 1480 1485 <210> SEQ ID NO 59 <211> LENGTH: 1466 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02461 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1466) <400> SEQUENCE: 59 Met Met Ser Phe Val Gln Lys Gly Ser Trp Leu Leu Leu Ala Leu Leu 1 5 10 15 His Pro Thr Ile Ile Leu Ala Gln Gln Glu Ala Val Glu Gly Gly Cys 20 25 30 Ser His Leu Gly Gln Ser Tyr Ala Asp Arg Asp Val Trp Lys Pro Glu 35 40 45 Pro Cys Gln Ile Cys Val Cys Asp Ser Gly Ser Val Leu Cys Asp Asp 50 55 60 Ile Ile Cys Asp Asp Gln Glu Leu Asp Cys Pro Asn Pro Glu Ile Pro 65 70 75 80 Phe Gly Glu Cys Cys Ala Val Cys Pro Gln Pro Pro Thr Ala Pro Thr 85 90 95 Arg Pro Pro Asn Gly Gln Gly Pro Gln Gly Pro Lys Gly Asp Pro Gly 100 105 110 Pro Pro Gly Ile Pro Gly Arg Asn Gly Asp Pro Gly Ile Pro Gly Gln 115 120 125 Pro Gly Ser Pro Gly Ser Pro Gly Pro Pro Gly Ile Cys Glu Ser Cys 130 135 140 Pro Thr Gly Pro Gln Asn Tyr Ser Pro Gln Tyr Asp Ser Tyr Asp Val 145 150 155 160 Lys Ser Gly Val Ala Val Gly Gly Leu Ala Gly Tyr Pro Gly Pro Ala 165 170 175 Gly Pro Pro Gly Pro Pro Gly Pro Pro Gly Thr Ser Gly His Pro Gly 180 185 190 Ser Pro Gly Ser Pro Gly Tyr Gln Gly Pro Pro Gly Glu Pro Gly Gln 195 200 205 Ala Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly Ala Ile Gly Pro Ser 210 215 220 Gly Pro Ala Gly Lys Asp Gly Glu Ser Gly Arg Pro Gly Arg Pro Gly 225 230 235 240 Glu Arg Gly Leu Pro Gly Pro Pro Gly Ile Lys Gly Pro Ala Gly Ile 245 250 255 Pro Gly Phe Pro Gly Met Lys Gly His Arg Gly Phe Asp Gly Arg Asn 260 265 270 Gly Glu Lys Gly Glu Thr Gly Ala Pro Gly Leu Lys Gly Glu Asn Gly 275 280 285 Leu Pro Gly Glu Asn Gly Ala Pro Gly Pro Met Gly Pro Arg Gly Ala 290 295 300 Pro Gly Glu Arg Gly Arg Pro Gly Leu Pro Gly Ala Ala Gly Ala Arg 305 310 315 320 Gly Asn Asp Gly Ala Arg Gly Ser Asp Gly Gln Pro Gly Pro Pro Gly 325 330 335 Pro Pro Gly Thr Ala Gly Phe Pro Gly Ser Pro Gly Ala Lys Gly Glu 340 345 350 Val Gly Pro Ala Gly Ser Pro Gly Ser Asn Gly Ala Pro Gly Gln Arg 355 360 365 Gly Glu Pro Gly Pro Gln Gly His Ala Gly Ala Gln Gly Pro Pro Gly 370 375 380 Pro Pro Gly Ile Asn Gly Ser Pro Gly Gly Lys Gly Glu Met Gly Pro 385 390 395 400 Ala Gly Ile Pro Gly Ala Pro Gly Leu Met Gly Ala Arg Gly Pro Pro 405 410 415 Gly Pro Ala Gly Ala Asn Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly 420 425 430 Glu Pro Gly Lys Asn Gly Ala Lys Gly Glu Pro Gly Pro Arg Gly Glu 435 440 445 Arg Gly Glu Ala Gly Ile Pro Gly Val Pro Gly Ala Lys Gly Glu Asp 450 455 460 Gly Lys Asp Gly Ser Pro Gly Glu Pro Gly Ala Asn Gly Leu Pro Gly 465 470 475 480 Ala Ala Gly Glu Arg Gly Ala Pro Gly Phe Arg Gly Pro Ala Gly Pro 485 490 495 Asn Gly Ile Pro Gly Glu Lys Gly Pro Ala Gly Glu Arg Gly Ala Pro 500 505 510 Gly Pro Ala Gly Pro Arg Gly Ala Ala Gly Glu Pro Gly Arg Asp Gly 515 520 525 Val Pro Gly Gly Pro Gly Met Arg Gly Met Pro Gly Ser Pro Gly Gly 530 535 540 Pro Gly Ser Asp Gly Lys Pro Gly Pro Pro Gly Ser Gln Gly Glu Ser 545 550 555 560 Gly Arg Pro Gly Pro Pro Gly Pro Ser Gly Pro Arg Gly Gln Pro Gly 565 570 575 Val Met Gly Phe Pro Gly Pro Lys Gly Asn Asp Gly Ala Pro Gly Lys 580 585 590 Asn Gly Glu Arg Gly Gly Pro Gly Gly Pro Gly Pro Gln Gly Pro Pro 595 600 605 Gly Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro Pro Gly Pro Thr Gly 610 615 620 Pro Gly Gly Asp Lys Gly Asp Thr Gly Pro Pro Gly Pro Gln Gly Leu 625 630 635 640 Gln Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly Glu Asn Gly Lys Pro 645 650 655 Gly Glu Pro Gly Pro Lys Gly Asp Ala Gly Ala Pro Gly Ala Pro Gly 660 665 670 Gly Lys Gly Asp Ala Gly Ala Pro Gly Glu Arg Gly Pro Pro Gly Leu 675 680 685 Ala Gly Ala Pro Gly Leu Arg Gly Gly Ala Gly Pro Pro Gly Pro Glu 690 695 700 Gly Gly Lys Gly Ala Ala Gly Pro Pro Gly Pro Pro Gly Ala Ala Gly 705 710 715 720 Thr Pro Gly Leu Gln Gly Met Pro Gly Glu Arg Gly Gly Leu Gly Ser 725 730 735 Pro Gly Pro Lys Gly Asp Lys Gly Glu Pro Gly Gly Pro Gly Ala Asp 740 745 750 Gly Val Pro Gly Lys Asp Gly Pro Arg Gly Pro Thr Gly Pro Ile Gly 755 760 765 Pro Pro Gly Pro Ala Gly Gln Pro Gly Asp Lys Gly Glu Gly Gly Ala 770 775 780 Pro Gly Leu Pro Gly Ile Ala Gly Pro Arg Gly Ser Pro Gly Glu Arg 785 790 795 800 Gly Glu Thr Gly Pro Pro Gly Pro Ala Gly Phe Pro Gly Ala Pro Gly 805 810 815 Gln Asn Gly Glu Pro Gly Gly Lys Gly Glu Arg Gly Ala Pro Gly Glu 820 825 830 Lys Gly Glu Gly Gly Pro Pro Gly Val Ala Gly Pro Pro Gly Gly Ser 835 840 845 Gly Pro Ala Gly Pro Pro Gly Pro Gln Gly Val Lys Gly Glu Arg Gly 850 855 860 Ser Pro Gly Gly Pro Gly Ala Ala Gly Phe Pro Gly Ala Arg Gly Leu 865 870 875 880 Pro Gly Pro Pro Gly Ser Asn Gly Asn Pro Gly Pro Pro Gly Pro Ser 885 890 895 Gly Ser Pro Gly Lys Asp Gly Pro Pro Gly Pro Ala Gly Asn Thr Gly 900 905 910 Ala Pro Gly Ser Pro Gly Val Ser Gly Pro Lys Gly Asp Ala Gly Gln 915 920 925 Pro Gly Glu Lys Gly Ser Pro Gly Ala Gln Gly Pro Pro Gly Ala Pro 930 935 940 Gly Pro Leu Gly Ile Ala Gly Ile Thr Gly Ala Arg Gly Leu Ala Gly

945 950 955 960 Pro Pro Gly Met Pro Gly Pro Arg Gly Ser Pro Gly Pro Gln Gly Val 965 970 975 Lys Gly Glu Ser Gly Lys Pro Gly Ala Asn Gly Leu Ser Gly Glu Arg 980 985 990 Gly Pro Pro Gly Pro Gln Gly Leu Pro Gly Leu Ala Gly Thr Ala Gly 995 1000 1005 Glu Pro Gly Arg Asp Gly Asn Pro Gly Ser Asp Gly Leu Pro Gly 1010 1015 1020 Arg Asp Gly Ser Pro Gly Gly Lys Gly Asp Arg Gly Glu Asn Gly 1025 1030 1035 Ser Pro Gly Ala Pro Gly Ala Pro Gly His Pro Gly Pro Pro Gly 1040 1045 1050 Pro Val Gly Pro Ala Gly Lys Ser Gly Asp Arg Gly Glu Ser Gly 1055 1060 1065 Pro Ala Gly Pro Ala Gly Ala Pro Gly Pro Ala Gly Ser Arg Gly 1070 1075 1080 Ala Pro Gly Pro Gln Gly Pro Arg Gly Asp Lys Gly Glu Thr Gly 1085 1090 1095 Glu Arg Gly Ala Ala Gly Ile Lys Gly His Arg Gly Phe Pro Gly 1100 1105 1110 Asn Pro Gly Ala Pro Gly Ser Pro Gly Pro Ala Gly Gln Gln Gly 1115 1120 1125 Ala Ile Gly Ser Pro Gly Pro Ala Gly Pro Arg Gly Pro Val Gly 1130 1135 1140 Pro Ser Gly Pro Pro Gly Lys Asp Gly Thr Ser Gly His Pro Gly 1145 1150 1155 Pro Ile Gly Pro Pro Gly Pro Arg Gly Asn Arg Gly Glu Arg Gly 1160 1165 1170 Ser Glu Gly Ser Pro Gly His Pro Gly Gln Pro Gly Pro Pro Gly 1175 1180 1185 Pro Pro Gly Ala Pro Gly Pro Cys Cys Gly Gly Val Gly Ala Ala 1190 1195 1200 Ala Ile Ala Gly Ile Gly Gly Glu Lys Ala Gly Gly Phe Ala Pro 1205 1210 1215 Tyr Tyr Gly Asp Glu Pro Met Asp Phe Lys Ile Asn Thr Asp Glu 1220 1225 1230 Ile Met Thr Ser Leu Lys Ser Val Asn Gly Gln Ile Glu Ser Leu 1235 1240 1245 Ile Ser Pro Asp Gly Ser Arg Lys Asn Pro Ala Arg Asn Cys Arg 1250 1255 1260 Asp Leu Lys Phe Cys His Pro Glu Leu Lys Ser Gly Glu Tyr Trp 1265 1270 1275 Val Asp Pro Asn Gln Gly Cys Lys Leu Asp Ala Ile Lys Val Phe 1280 1285 1290 Cys Asn Met Glu Thr Gly Glu Thr Cys Ile Ser Ala Asn Pro Leu 1295 1300 1305 Asn Val Pro Arg Lys His Trp Trp Thr Asp Ser Ser Ala Glu Lys 1310 1315 1320 Lys His Val Trp Phe Gly Glu Ser Met Asp Gly Gly Phe Gln Phe 1325 1330 1335 Ser Tyr Gly Asn Pro Glu Leu Pro Glu Asp Val Leu Asp Val His 1340 1345 1350 Leu Ala Phe Leu Arg Leu Leu Ser Ser Arg Ala Ser Gln Asn Ile 1355 1360 1365 Thr Tyr His Cys Lys Asn Ser Ile Ala Tyr Met Asp Gln Ala Ser 1370 1375 1380 Gly Asn Val Lys Lys Ala Leu Lys Leu Met Gly Ser Asn Glu Gly 1385 1390 1395 Glu Phe Lys Ala Glu Gly Asn Ser Lys Phe Thr Tyr Thr Val Leu 1400 1405 1410 Glu Asp Gly Cys Thr Lys His Thr Gly Glu Trp Ser Lys Thr Val 1415 1420 1425 Phe Glu Tyr Arg Thr Arg Lys Ala Val Arg Leu Pro Ile Val Asp 1430 1435 1440 Ile Ala Pro Tyr Asp Ile Gly Gly Pro Asp Gln Glu Phe Gly Val 1445 1450 1455 Asp Val Gly Pro Val Cys Phe Leu 1460 1465 <210> SEQ ID NO 60 <211> LENGTH: 1669 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02462 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1669) <400> SEQUENCE: 60 Met Gly Pro Arg Leu Ser Val Trp Leu Leu Leu Leu Pro Ala Ala Leu 1 5 10 15 Leu Leu His Glu Glu His Ser Arg Ala Ala Ala Lys Gly Gly Cys Ala 20 25 30 Gly Ser Gly Cys Gly Lys Cys Asp Cys His Gly Val Lys Gly Gln Lys 35 40 45 Gly Glu Arg Gly Leu Pro Gly Leu Gln Gly Val Ile Gly Phe Pro Gly 50 55 60 Met Gln Gly Pro Glu Gly Pro Gln Gly Pro Pro Gly Gln Lys Gly Asp 65 70 75 80 Thr Gly Glu Pro Gly Leu Pro Gly Thr Lys Gly Thr Arg Gly Pro Pro 85 90 95 Gly Ala Ser Gly Tyr Pro Gly Asn Pro Gly Leu Pro Gly Ile Pro Gly 100 105 110 Gln Asp Gly Pro Pro Gly Pro Pro Gly Ile Pro Gly Cys Asn Gly Thr 115 120 125 Lys Gly Glu Arg Gly Pro Leu Gly Pro Pro Gly Leu Pro Gly Phe Ala 130 135 140 Gly Asn Pro Gly Pro Pro Gly Leu Pro Gly Met Lys Gly Asp Pro Gly 145 150 155 160 Glu Ile Leu Gly His Val Pro Gly Met Leu Leu Lys Gly Glu Arg Gly 165 170 175 Phe Pro Gly Ile Pro Gly Thr Pro Gly Pro Pro Gly Leu Pro Gly Leu 180 185 190 Gln Gly Pro Val Gly Pro Pro Gly Phe Thr Gly Pro Pro Gly Pro Pro 195 200 205 Gly Pro Pro Gly Pro Pro Gly Glu Lys Gly Gln Met Gly Leu Ser Phe 210 215 220 Gln Gly Pro Lys Gly Asp Lys Gly Asp Gln Gly Val Ser Gly Pro Pro 225 230 235 240 Gly Val Pro Gly Gln Ala Gln Val Gln Glu Lys Gly Asp Phe Ala Thr 245 250 255 Lys Gly Glu Lys Gly Gln Lys Gly Glu Pro Gly Phe Gln Gly Met Pro 260 265 270 Gly Val Gly Glu Lys Gly Glu Pro Gly Lys Pro Gly Pro Arg Gly Lys 275 280 285 Pro Gly Lys Asp Gly Asp Lys Gly Glu Lys Gly Ser Pro Gly Phe Pro 290 295 300 Gly Glu Pro Gly Tyr Pro Gly Leu Ile Gly Arg Gln Gly Pro Gln Gly 305 310 315 320 Glu Lys Gly Glu Ala Gly Pro Pro Gly Pro Pro Gly Ile Val Ile Gly 325 330 335 Thr Gly Pro Leu Gly Glu Lys Gly Glu Arg Gly Tyr Pro Gly Thr Pro 340 345 350 Gly Pro Arg Gly Glu Pro Gly Pro Lys Gly Phe Pro Gly Leu Pro Gly 355 360 365 Gln Pro Gly Pro Pro Gly Leu Pro Val Pro Gly Gln Ala Gly Ala Pro 370 375 380 Gly Phe Pro Gly Glu Arg Gly Glu Lys Gly Asp Arg Gly Phe Pro Gly 385 390 395 400 Thr Ser Leu Pro Gly Pro Ser Gly Arg Asp Gly Leu Pro Gly Pro Pro 405 410 415 Gly Ser Pro Gly Pro Pro Gly Gln Pro Gly Tyr Thr Asn Gly Ile Val 420 425 430 Glu Cys Gln Pro Gly Pro Pro Gly Asp Gln Gly Pro Pro Gly Ile Pro 435 440 445 Gly Gln Pro Gly Phe Ile Gly Glu Ile Gly Glu Lys Gly Gln Lys Gly 450 455 460 Glu Ser Cys Leu Ile Cys Asp Ile Asp Gly Tyr Arg Gly Pro Pro Gly 465 470 475 480 Pro Gln Gly Pro Pro Gly Glu Ile Gly Phe Pro Gly Gln Pro Gly Ala 485 490 495 Lys Gly Asp Arg Gly Leu Pro Gly Arg Asp Gly Val Ala Gly Val Pro 500 505 510 Gly Pro Gln Gly Thr Pro Gly Leu Ile Gly Gln Pro Gly Ala Lys Gly 515 520 525 Glu Pro Gly Glu Phe Tyr Phe Asp Leu Arg Leu Lys Gly Asp Lys Gly 530 535 540 Asp Pro Gly Phe Pro Gly Gln Pro Gly Met Thr Gly Arg Ala Gly Ser 545 550 555 560 Pro Gly Arg Asp Gly His Pro Gly Leu Pro Gly Pro Lys Gly Ser Pro 565 570 575 Gly Ser Val Gly Leu Lys Gly Glu Arg Gly Pro Pro Gly Gly Val Gly 580 585 590 Phe Pro Gly Ser Arg Gly Asp Thr Gly Pro Pro Gly Pro Pro Gly Tyr 595 600 605 Gly Pro Ala Gly Pro Ile Gly Asp Lys Gly Gln Ala Gly Phe Pro Gly 610 615 620 Gly Pro Gly Ser Pro Gly Leu Pro Gly Pro Lys Gly Glu Pro Gly Lys 625 630 635 640 Ile Val Pro Leu Pro Gly Pro Pro Gly Ala Glu Gly Leu Pro Gly Ser 645 650 655 Pro Gly Phe Pro Gly Pro Gln Gly Asp Arg Gly Phe Pro Gly Thr Pro 660 665 670 Gly Arg Pro Gly Leu Pro Gly Glu Lys Gly Ala Val Gly Gln Pro Gly 675 680 685 Ile Gly Phe Pro Gly Pro Pro Gly Pro Lys Gly Val Asp Gly Leu Pro 690 695 700 Gly Asp Met Gly Pro Pro Gly Thr Pro Gly Arg Pro Gly Phe Asn Gly 705 710 715 720

Leu Pro Gly Asn Pro Gly Val Gln Gly Gln Lys Gly Glu Pro Gly Val 725 730 735 Gly Leu Pro Gly Leu Lys Gly Leu Pro Gly Leu Pro Gly Ile Pro Gly 740 745 750 Thr Pro Gly Glu Lys Gly Ser Ile Gly Val Pro Gly Val Pro Gly Glu 755 760 765 His Gly Ala Ile Gly Pro Pro Gly Leu Gln Gly Ile Arg Gly Glu Pro 770 775 780 Gly Pro Pro Gly Leu Pro Gly Ser Val Gly Ser Pro Gly Val Pro Gly 785 790 795 800 Ile Gly Pro Pro Gly Ala Arg Gly Pro Pro Gly Gly Gln Gly Pro Pro 805 810 815 Gly Leu Ser Gly Pro Pro Gly Ile Lys Gly Glu Lys Gly Phe Pro Gly 820 825 830 Phe Pro Gly Leu Asp Met Pro Gly Pro Lys Gly Asp Lys Gly Ala Gln 835 840 845 Gly Leu Pro Gly Ile Thr Gly Gln Ser Gly Leu Pro Gly Leu Pro Gly 850 855 860 Gln Gln Gly Ala Pro Gly Ile Pro Gly Phe Pro Gly Ser Lys Gly Glu 865 870 875 880 Met Gly Val Met Gly Thr Pro Gly Gln Pro Gly Ser Pro Gly Pro Val 885 890 895 Gly Ala Pro Gly Leu Pro Gly Glu Lys Gly Asp His Gly Phe Pro Gly 900 905 910 Ser Ser Gly Pro Arg Gly Asp Pro Gly Leu Lys Gly Asp Lys Gly Asp 915 920 925 Val Gly Leu Pro Gly Lys Pro Gly Ser Met Asp Lys Val Asp Met Gly 930 935 940 Ser Met Lys Gly Gln Lys Gly Asp Gln Gly Glu Lys Gly Gln Ile Gly 945 950 955 960 Pro Ile Gly Glu Lys Gly Ser Arg Gly Asp Pro Gly Thr Pro Gly Val 965 970 975 Pro Gly Lys Asp Gly Gln Ala Gly Gln Pro Gly Gln Pro Gly Pro Lys 980 985 990 Gly Asp Pro Gly Ile Ser Gly Thr Pro Gly Ala Pro Gly Leu Pro Gly 995 1000 1005 Pro Lys Gly Ser Val Gly Gly Met Gly Leu Pro Gly Thr Pro Gly 1010 1015 1020 Glu Lys Gly Val Pro Gly Ile Pro Gly Pro Gln Gly Ser Pro Gly 1025 1030 1035 Leu Pro Gly Asp Lys Gly Ala Lys Gly Glu Lys Gly Gln Ala Gly 1040 1045 1050 Pro Pro Gly Ile Gly Ile Pro Gly Leu Arg Gly Glu Lys Gly Asp 1055 1060 1065 Gln Gly Ile Ala Gly Phe Pro Gly Ser Pro Gly Glu Lys Gly Glu 1070 1075 1080 Lys Gly Ser Ile Gly Ile Pro Gly Met Pro Gly Ser Pro Gly Leu 1085 1090 1095 Lys Gly Ser Pro Gly Ser Val Gly Tyr Pro Gly Ser Pro Gly Leu 1100 1105 1110 Pro Gly Glu Lys Gly Asp Lys Gly Leu Pro Gly Leu Asp Gly Ile 1115 1120 1125 Pro Gly Val Lys Gly Glu Ala Gly Leu Pro Gly Thr Pro Gly Pro 1130 1135 1140 Thr Gly Pro Ala Gly Gln Lys Gly Glu Pro Gly Ser Asp Gly Ile 1145 1150 1155 Pro Gly Ser Ala Gly Glu Lys Gly Glu Pro Gly Leu Pro Gly Arg 1160 1165 1170 Gly Phe Pro Gly Phe Pro Gly Ala Lys Gly Asp Lys Gly Ser Lys 1175 1180 1185 Gly Glu Val Gly Phe Pro Gly Leu Ala Gly Ser Pro Gly Ile Pro 1190 1195 1200 Gly Ser Lys Gly Glu Gln Gly Phe Met Gly Pro Pro Gly Pro Gln 1205 1210 1215 Gly Gln Pro Gly Leu Pro Gly Ser Pro Gly His Ala Thr Glu Gly 1220 1225 1230 Pro Lys Gly Asp Arg Gly Pro Gln Gly Gln Pro Gly Leu Pro Gly 1235 1240 1245 Leu Pro Gly Pro Met Gly Pro Pro Gly Leu Pro Gly Ile Asp Gly 1250 1255 1260 Val Lys Gly Asp Lys Gly Asn Pro Gly Trp Pro Gly Ala Pro Gly 1265 1270 1275 Val Pro Gly Pro Lys Gly Asp Pro Gly Phe Gln Gly Met Pro Gly 1280 1285 1290 Ile Gly Gly Ser Pro Gly Ile Thr Gly Ser Lys Gly Asp Met Gly 1295 1300 1305 Pro Pro Gly Val Pro Gly Phe Gln Gly Pro Lys Gly Leu Pro Gly 1310 1315 1320 Leu Gln Gly Ile Lys Gly Asp Gln Gly Asp Gln Gly Val Pro Gly 1325 1330 1335 Ala Lys Gly Leu Pro Gly Pro Pro Gly Pro Pro Gly Pro Tyr Asp 1340 1345 1350 Ile Ile Lys Gly Glu Pro Gly Leu Pro Gly Pro Glu Gly Pro Pro 1355 1360 1365 Gly Leu Lys Gly Leu Gln Gly Leu Pro Gly Pro Lys Gly Gln Gln 1370 1375 1380 Gly Val Thr Gly Leu Val Gly Ile Pro Gly Pro Pro Gly Ile Pro 1385 1390 1395 Gly Phe Asp Gly Ala Pro Gly Gln Lys Gly Glu Met Gly Pro Ala 1400 1405 1410 Gly Pro Thr Gly Pro Arg Gly Phe Pro Gly Pro Pro Gly Pro Asp 1415 1420 1425 Gly Leu Pro Gly Ser Met Gly Pro Pro Gly Thr Pro Ser Val Asp 1430 1435 1440 His Gly Phe Leu Val Thr Arg His Ser Gln Thr Ile Asp Asp Pro 1445 1450 1455 Gln Cys Pro Ser Gly Thr Lys Ile Leu Tyr His Gly Tyr Ser Leu 1460 1465 1470 Leu Tyr Val Gln Gly Asn Glu Arg Ala His Gly Gln Asp Leu Gly 1475 1480 1485 Thr Ala Gly Ser Cys Leu Arg Lys Phe Ser Thr Met Pro Phe Leu 1490 1495 1500 Phe Cys Asn Ile Asn Asn Val Cys Asn Phe Ala Ser Arg Asn Asp 1505 1510 1515 Tyr Ser Tyr Trp Leu Ser Thr Pro Glu Pro Met Pro Met Ser Met 1520 1525 1530 Ala Pro Ile Thr Gly Glu Asn Ile Arg Pro Phe Ile Ser Arg Cys 1535 1540 1545 Ala Val Cys Glu Ala Pro Ala Met Val Met Ala Val His Ser Gln 1550 1555 1560 Thr Ile Gln Ile Pro Pro Cys Pro Ser Gly Trp Ser Ser Leu Trp 1565 1570 1575 Ile Gly Tyr Ser Phe Val Met His Thr Ser Ala Gly Ala Glu Gly 1580 1585 1590 Ser Gly Gln Ala Leu Ala Ser Pro Gly Ser Cys Leu Glu Glu Phe 1595 1600 1605 Arg Ser Ala Pro Phe Ile Glu Cys His Gly Arg Gly Thr Cys Asn 1610 1615 1620 Tyr Tyr Ala Asn Ala Tyr Ser Phe Trp Leu Ala Thr Ile Glu Arg 1625 1630 1635 Ser Glu Met Phe Lys Lys Pro Thr Pro Ser Thr Leu Lys Ala Gly 1640 1645 1650 Glu Leu Arg Thr His Val Ser Arg Cys Gln Val Cys Met Arg Arg 1655 1660 1665 Thr <210> SEQ ID NO 61 <211> LENGTH: 1838 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P20908 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1838) <400> SEQUENCE: 61 Met Asp Val His Thr Arg Trp Lys Ala Arg Ser Ala Leu Arg Pro Gly 1 5 10 15 Ala Pro Leu Leu Pro Pro Leu Leu Leu Leu Leu Leu Trp Ala Pro Pro 20 25 30 Pro Ser Arg Ala Ala Gln Pro Ala Asp Leu Leu Lys Val Leu Asp Phe 35 40 45 His Asn Leu Pro Asp Gly Ile Thr Lys Thr Thr Gly Phe Cys Ala Thr 50 55 60 Arg Arg Ser Ser Lys Gly Pro Asp Val Ala Tyr Arg Val Thr Lys Asp 65 70 75 80 Ala Gln Leu Ser Ala Pro Thr Lys Gln Leu Tyr Pro Ala Ser Ala Phe 85 90 95 Pro Glu Asp Phe Ser Ile Leu Thr Thr Val Lys Ala Lys Lys Gly Ser 100 105 110 Gln Ala Phe Leu Val Ser Ile Tyr Asn Glu Gln Gly Ile Gln Gln Ile 115 120 125 Gly Leu Glu Leu Gly Arg Ser Pro Val Phe Leu Tyr Glu Asp His Thr 130 135 140 Gly Lys Pro Gly Pro Glu Asp Tyr Pro Leu Phe Arg Gly Ile Asn Leu 145 150 155 160 Ser Asp Gly Lys Trp His Arg Ile Ala Leu Ser Val His Lys Lys Asn 165 170 175 Val Thr Leu Ile Leu Asp Cys Lys Lys Lys Thr Thr Lys Phe Leu Asp 180 185 190 Arg Ser Asp His Pro Met Ile Asp Ile Asn Gly Ile Ile Val Phe Gly 195 200 205 Thr Arg Ile Leu Asp Glu Glu Val Phe Glu Gly Asp Ile Gln Gln Leu 210 215 220 Leu Phe Val Ser Asp His Arg Ala Ala Tyr Asp Tyr Cys Glu His Tyr 225 230 235 240 Ser Pro Asp Cys Asp Thr Ala Val Pro Asp Thr Pro Gln Ser Gln Asp 245 250 255 Pro Asn Pro Asp Glu Tyr Tyr Thr Glu Gly Asp Gly Glu Gly Glu Thr 260 265 270

Tyr Tyr Tyr Glu Tyr Pro Tyr Tyr Glu Asp Pro Glu Asp Leu Gly Lys 275 280 285 Glu Pro Thr Pro Ser Lys Lys Pro Val Glu Ala Ala Lys Glu Thr Thr 290 295 300 Glu Val Pro Glu Glu Leu Thr Pro Thr Pro Thr Glu Ala Ala Pro Met 305 310 315 320 Pro Glu Thr Ser Glu Gly Ala Gly Lys Glu Glu Asp Val Gly Ile Gly 325 330 335 Asp Tyr Asp Tyr Val Pro Ser Glu Asp Tyr Tyr Thr Pro Ser Pro Tyr 340 345 350 Asp Asp Leu Thr Tyr Gly Glu Gly Glu Glu Asn Pro Asp Gln Pro Thr 355 360 365 Asp Pro Gly Ala Gly Ala Glu Ile Pro Thr Ser Thr Ala Asp Thr Ser 370 375 380 Asn Ser Ser Asn Pro Ala Pro Pro Pro Gly Glu Gly Ala Asp Asp Leu 385 390 395 400 Glu Gly Glu Phe Thr Glu Glu Thr Ile Arg Asn Leu Asp Glu Asn Tyr 405 410 415 Tyr Asp Pro Tyr Tyr Asp Pro Thr Ser Ser Pro Ser Glu Ile Gly Pro 420 425 430 Gly Met Pro Ala Asn Gln Asp Thr Ile Tyr Glu Gly Ile Gly Gly Pro 435 440 445 Arg Gly Glu Lys Gly Gln Lys Gly Glu Pro Ala Ile Ile Glu Pro Gly 450 455 460 Met Leu Ile Glu Gly Pro Pro Gly Pro Glu Gly Pro Ala Gly Leu Pro 465 470 475 480 Gly Pro Pro Gly Thr Met Gly Pro Thr Gly Gln Val Gly Asp Pro Gly 485 490 495 Glu Arg Gly Pro Pro Gly Arg Pro Gly Leu Pro Gly Ala Asp Gly Leu 500 505 510 Pro Gly Pro Pro Gly Thr Met Leu Met Leu Pro Phe Arg Phe Gly Gly 515 520 525 Gly Gly Asp Ala Gly Ser Lys Gly Pro Met Val Ser Ala Gln Glu Ser 530 535 540 Gln Ala Gln Ala Ile Leu Gln Gln Ala Arg Leu Ala Leu Arg Gly Pro 545 550 555 560 Ala Gly Pro Met Gly Leu Thr Gly Arg Pro Gly Pro Val Gly Pro Pro 565 570 575 Gly Ser Gly Gly Leu Lys Gly Glu Pro Gly Asp Val Gly Pro Gln Gly 580 585 590 Pro Arg Gly Val Gln Gly Pro Pro Gly Pro Ala Gly Lys Pro Gly Arg 595 600 605 Arg Gly Arg Ala Gly Ser Asp Gly Ala Arg Gly Met Pro Gly Gln Thr 610 615 620 Gly Pro Lys Gly Asp Arg Gly Phe Asp Gly Leu Ala Gly Leu Pro Gly 625 630 635 640 Glu Lys Gly His Arg Gly Asp Pro Gly Pro Ser Gly Pro Pro Gly Pro 645 650 655 Pro Gly Asp Asp Gly Glu Arg Gly Asp Asp Gly Glu Val Gly Pro Arg 660 665 670 Gly Leu Pro Gly Glu Pro Gly Pro Arg Gly Leu Leu Gly Pro Lys Gly 675 680 685 Pro Pro Gly Pro Pro Gly Pro Pro Gly Val Thr Gly Met Asp Gly Gln 690 695 700 Pro Gly Pro Lys Gly Asn Val Gly Pro Gln Gly Glu Pro Gly Pro Pro 705 710 715 720 Gly Gln Gln Gly Asn Pro Gly Ala Gln Gly Leu Pro Gly Pro Gln Gly 725 730 735 Ala Ile Gly Pro Pro Gly Glu Lys Gly Pro Leu Gly Lys Pro Gly Leu 740 745 750 Pro Gly Met Pro Gly Ala Asp Gly Pro Pro Gly His Pro Gly Lys Glu 755 760 765 Gly Pro Pro Gly Glu Lys Gly Gly Gln Gly Pro Pro Gly Pro Gln Gly 770 775 780 Pro Ile Gly Tyr Pro Gly Pro Arg Gly Val Lys Gly Ala Asp Gly Ile 785 790 795 800 Arg Gly Leu Lys Gly Thr Lys Gly Glu Lys Gly Glu Asp Gly Phe Pro 805 810 815 Gly Phe Lys Gly Asp Met Gly Ile Lys Gly Asp Arg Gly Glu Ile Gly 820 825 830 Pro Pro Gly Pro Arg Gly Glu Asp Gly Pro Glu Gly Pro Lys Gly Arg 835 840 845 Gly Gly Pro Asn Gly Asp Pro Gly Pro Leu Gly Pro Pro Gly Glu Lys 850 855 860 Gly Lys Leu Gly Val Pro Gly Leu Pro Gly Tyr Pro Gly Arg Gln Gly 865 870 875 880 Pro Lys Gly Ser Ile Gly Phe Pro Gly Phe Pro Gly Ala Asn Gly Glu 885 890 895 Lys Gly Gly Arg Gly Thr Pro Gly Lys Pro Gly Pro Arg Gly Gln Arg 900 905 910 Gly Pro Thr Gly Pro Arg Gly Glu Arg Gly Pro Arg Gly Ile Thr Gly 915 920 925 Lys Pro Gly Pro Lys Gly Asn Ser Gly Gly Asp Gly Pro Ala Gly Pro 930 935 940 Pro Gly Glu Arg Gly Pro Asn Gly Pro Gln Gly Pro Thr Gly Phe Pro 945 950 955 960 Gly Pro Lys Gly Pro Pro Gly Pro Pro Gly Lys Asp Gly Leu Pro Gly 965 970 975 His Pro Gly Gln Arg Gly Glu Thr Gly Phe Gln Gly Lys Thr Gly Pro 980 985 990 Pro Gly Pro Pro Gly Val Val Gly Pro Gln Gly Pro Thr Gly Glu Thr 995 1000 1005 Gly Pro Met Gly Glu Arg Gly His Pro Gly Pro Pro Gly Pro Pro 1010 1015 1020 Gly Glu Gln Gly Leu Pro Gly Leu Ala Gly Lys Glu Gly Thr Lys 1025 1030 1035 Gly Asp Pro Gly Pro Ala Gly Leu Pro Gly Lys Asp Gly Pro Pro 1040 1045 1050 Gly Leu Arg Gly Phe Pro Gly Asp Arg Gly Leu Pro Gly Pro Val 1055 1060 1065 Gly Ala Leu Gly Leu Lys Gly Asn Glu Gly Pro Pro Gly Pro Pro 1070 1075 1080 Gly Pro Ala Gly Ser Pro Gly Glu Arg Gly Pro Ala Gly Ala Ala 1085 1090 1095 Gly Pro Ile Gly Ile Pro Gly Arg Pro Gly Pro Gln Gly Pro Pro 1100 1105 1110 Gly Pro Ala Gly Glu Lys Gly Ala Pro Gly Glu Lys Gly Pro Gln 1115 1120 1125 Gly Pro Ala Gly Arg Asp Gly Leu Gln Gly Pro Val Gly Leu Pro 1130 1135 1140 Gly Pro Ala Gly Pro Val Gly Pro Pro Gly Glu Asp Gly Asp Lys 1145 1150 1155 Gly Glu Ile Gly Glu Pro Gly Gln Lys Gly Ser Lys Gly Asp Lys 1160 1165 1170 Gly Glu Gln Gly Pro Pro Gly Pro Thr Gly Pro Gln Gly Pro Ile 1175 1180 1185 Gly Gln Pro Gly Pro Ser Gly Ala Asp Gly Glu Pro Gly Pro Arg 1190 1195 1200 Gly Gln Gln Gly Leu Phe Gly Gln Lys Gly Asp Glu Gly Pro Arg 1205 1210 1215 Gly Phe Pro Gly Pro Pro Gly Pro Val Gly Leu Gln Gly Leu Pro 1220 1225 1230 Gly Pro Pro Gly Glu Lys Gly Glu Thr Gly Asp Val Gly Gln Met 1235 1240 1245 Gly Pro Pro Gly Pro Pro Gly Pro Arg Gly Pro Ser Gly Ala Pro 1250 1255 1260 Gly Ala Asp Gly Pro Gln Gly Pro Pro Gly Gly Ile Gly Asn Pro 1265 1270 1275 Gly Ala Val Gly Glu Lys Gly Glu Pro Gly Glu Ala Gly Glu Pro 1280 1285 1290 Gly Leu Pro Gly Glu Gly Gly Pro Pro Gly Pro Lys Gly Glu Arg 1295 1300 1305 Gly Glu Lys Gly Glu Ser Gly Pro Ser Gly Ala Ala Gly Pro Pro 1310 1315 1320 Gly Pro Lys Gly Pro Pro Gly Asp Asp Gly Pro Lys Gly Ser Pro 1325 1330 1335 Gly Pro Val Gly Phe Pro Gly Asp Pro Gly Pro Pro Gly Glu Pro 1340 1345 1350 Gly Pro Ala Gly Gln Asp Gly Pro Pro Gly Asp Lys Gly Asp Asp 1355 1360 1365 Gly Glu Pro Gly Gln Thr Gly Ser Pro Gly Pro Thr Gly Glu Pro 1370 1375 1380 Gly Pro Ser Gly Pro Pro Gly Lys Arg Gly Pro Pro Gly Pro Ala 1385 1390 1395 Gly Pro Glu Gly Arg Gln Gly Glu Lys Gly Ala Lys Gly Glu Ala 1400 1405 1410 Gly Leu Glu Gly Pro Pro Gly Lys Thr Gly Pro Ile Gly Pro Gln 1415 1420 1425 Gly Ala Pro Gly Lys Pro Gly Pro Asp Gly Leu Arg Gly Ile Pro 1430 1435 1440 Gly Pro Val Gly Glu Gln Gly Leu Pro Gly Ser Pro Gly Pro Asp 1445 1450 1455 Gly Pro Pro Gly Pro Met Gly Pro Pro Gly Leu Pro Gly Leu Lys 1460 1465 1470 Gly Asp Ser Gly Pro Lys Gly Glu Lys Gly His Pro Gly Leu Ile 1475 1480 1485 Gly Leu Ile Gly Pro Pro Gly Glu Gln Gly Glu Lys Gly Asp Arg 1490 1495 1500 Gly Leu Pro Gly Pro Gln Gly Ser Ser Gly Pro Lys Gly Glu Gln 1505 1510 1515 Gly Ile Thr Gly Pro Ser Gly Pro Ile Gly Pro Pro Gly Pro Pro 1520 1525 1530 Gly Leu Pro Gly Pro Pro Gly Pro Lys Gly Ala Lys Gly Ser Ser 1535 1540 1545 Gly Pro Thr Gly Pro Lys Gly Glu Ala Gly His Pro Gly Pro Pro 1550 1555 1560 Gly Pro Pro Gly Pro Pro Gly Glu Val Ile Gln Pro Leu Pro Ile 1565 1570 1575

Gln Ala Ser Arg Thr Arg Arg Asn Ile Asp Ala Ser Gln Leu Leu 1580 1585 1590 Asp Asp Gly Asn Gly Glu Asn Tyr Val Asp Tyr Ala Asp Gly Met 1595 1600 1605 Glu Glu Ile Phe Gly Ser Leu Asn Ser Leu Lys Leu Glu Ile Glu 1610 1615 1620 Gln Met Lys Arg Pro Leu Gly Thr Gln Gln Asn Pro Ala Arg Thr 1625 1630 1635 Cys Lys Asp Leu Gln Leu Cys His Pro Asp Phe Pro Asp Gly Glu 1640 1645 1650 Tyr Trp Val Asp Pro Asn Gln Gly Cys Ser Arg Asp Ser Phe Lys 1655 1660 1665 Val Tyr Cys Asn Phe Thr Ala Gly Gly Ser Thr Cys Val Phe Pro 1670 1675 1680 Asp Lys Lys Ser Glu Gly Ala Arg Ile Thr Ser Trp Pro Lys Glu 1685 1690 1695 Asn Pro Gly Ser Trp Phe Ser Glu Phe Lys Arg Gly Lys Leu Leu 1700 1705 1710 Ser Tyr Val Asp Ala Glu Gly Asn Pro Val Gly Val Val Gln Met 1715 1720 1725 Thr Phe Leu Arg Leu Leu Ser Ala Ser Ala His Gln Asn Val Thr 1730 1735 1740 Tyr His Cys Tyr Gln Ser Val Ala Trp Gln Asp Ala Ala Thr Gly 1745 1750 1755 Ser Tyr Asp Lys Ala Leu Arg Phe Leu Gly Ser Asn Asp Glu Glu 1760 1765 1770 Met Ser Tyr Asp Asn Asn Pro Tyr Ile Arg Ala Leu Val Asp Gly 1775 1780 1785 Cys Ala Thr Lys Lys Gly Tyr Gln Lys Thr Val Leu Glu Ile Asp 1790 1795 1800 Thr Pro Lys Val Glu Gln Val Pro Ile Val Asp Ile Met Phe Asn 1805 1810 1815 Asp Phe Gly Glu Ala Ser Gln Lys Phe Gly Phe Glu Val Gly Pro 1820 1825 1830 Ala Cys Phe Met Gly 1835 <210> SEQ ID NO 62 <211> LENGTH: 223 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P16410 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(223) <400> SEQUENCE: 62 Met Ala Cys Leu Gly Phe Gln Arg His Lys Ala Gln Leu Asn Leu Ala 1 5 10 15 Thr Arg Thr Trp Pro Cys Thr Leu Leu Phe Phe Leu Leu Phe Ile Pro 20 25 30 Val Phe Cys Lys Ala Met His Val Ala Gln Pro Ala Val Val Leu Ala 35 40 45 Ser Ser Arg Gly Ile Ala Ser Phe Val Cys Glu Tyr Ala Ser Pro Gly 50 55 60 Lys Ala Thr Glu Val Arg Val Thr Val Leu Arg Gln Ala Asp Ser Gln 65 70 75 80 Val Thr Glu Val Cys Ala Ala Thr Tyr Met Met Gly Asn Glu Leu Thr 85 90 95 Phe Leu Asp Asp Ser Ile Cys Thr Gly Thr Ser Ser Gly Asn Gln Val 100 105 110 Asn Leu Thr Ile Gln Gly Leu Arg Ala Met Asp Thr Gly Leu Tyr Ile 115 120 125 Cys Lys Val Glu Leu Met Tyr Pro Pro Pro Tyr Tyr Leu Gly Ile Gly 130 135 140 Asn Gly Thr Gln Ile Tyr Val Ile Asp Pro Glu Pro Cys Pro Asp Ser 145 150 155 160 Asp Phe Leu Leu Trp Ile Leu Ala Ala Val Ser Ser Gly Leu Phe Phe 165 170 175 Tyr Ser Phe Leu Leu Thr Ala Val Ser Leu Ser Lys Met Leu Lys Lys 180 185 190 Arg Ser Pro Leu Thr Thr Gly Val Tyr Val Lys Met Pro Pro Thr Glu 195 200 205 Pro Glu Cys Glu Lys Gln Phe Gln Pro Tyr Phe Ile Pro Ile Asn 210 215 220 <210> SEQ ID NO 63 <211> LENGTH: 339 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / O94905 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(339) <400> SEQUENCE: 63 Met Ala Gln Leu Gly Ala Val Val Ala Val Ala Ser Ser Phe Phe Cys 1 5 10 15 Ala Ser Leu Phe Ser Ala Val His Lys Ile Glu Glu Gly His Ile Gly 20 25 30 Val Tyr Tyr Arg Gly Gly Ala Leu Leu Thr Ser Thr Ser Gly Pro Gly 35 40 45 Phe His Leu Met Leu Pro Phe Ile Thr Ser Tyr Lys Ser Val Gln Thr 50 55 60 Thr Leu Gln Thr Asp Glu Val Lys Asn Val Pro Cys Gly Thr Ser Gly 65 70 75 80 Gly Val Met Ile Tyr Phe Asp Arg Ile Glu Val Val Asn Phe Leu Val 85 90 95 Pro Asn Ala Val Tyr Asp Ile Val Lys Asn Tyr Thr Ala Asp Tyr Asp 100 105 110 Lys Ala Leu Ile Phe Asn Lys Ile His His Glu Leu Asn Gln Phe Cys 115 120 125 Ser Val His Thr Leu Gln Glu Val Tyr Ile Glu Leu Phe Asp Gln Ile 130 135 140 Asp Glu Asn Leu Lys Leu Ala Leu Gln Gln Asp Leu Thr Ser Met Ala 145 150 155 160 Pro Gly Leu Val Ile Gln Ala Val Arg Val Thr Lys Pro Asn Ile Pro 165 170 175 Glu Ala Ile Arg Arg Asn Tyr Glu Leu Met Glu Ser Glu Lys Thr Lys 180 185 190 Leu Leu Ile Ala Ala Gln Lys Gln Lys Val Val Glu Lys Glu Ala Glu 195 200 205 Thr Glu Arg Lys Lys Ala Leu Ile Glu Ala Glu Lys Val Ala Gln Val 210 215 220 Ala Glu Ile Thr Tyr Gly Gln Lys Val Met Glu Lys Glu Thr Glu Lys 225 230 235 240 Lys Ile Ser Glu Ile Glu Asp Ala Ala Phe Leu Ala Arg Glu Lys Ala 245 250 255 Lys Ala Asp Ala Glu Cys Tyr Thr Ala Met Lys Ile Ala Glu Ala Asn 260 265 270 Lys Leu Lys Leu Thr Pro Glu Tyr Leu Gln Leu Met Lys Tyr Lys Ala 275 280 285 Ile Ala Ser Asn Ser Lys Ile Tyr Phe Gly Lys Asp Ile Pro Asn Met 290 295 300 Phe Met Asp Ser Ala Gly Ser Val Ser Lys Gln Phe Glu Gly Leu Ala 305 310 315 320 Asp Lys Leu Ser Phe Gly Leu Glu Asp Glu Pro Leu Glu Thr Ala Thr 325 330 335 Lys Glu Asn <210> SEQ ID NO 64 <211> LENGTH: 2386 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P02751 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(2386) <400> SEQUENCE: 64 Met Leu Arg Gly Pro Gly Pro Gly Leu Leu Leu Leu Ala Val Gln Cys 1 5 10 15 Leu Gly Thr Ala Val Pro Ser Thr Gly Ala Ser Lys Ser Lys Arg Gln 20 25 30 Ala Gln Gln Met Val Gln Pro Gln Ser Pro Val Ala Val Ser Gln Ser 35 40 45 Lys Pro Gly Cys Tyr Asp Asn Gly Lys His Tyr Gln Ile Asn Gln Gln 50 55 60 Trp Glu Arg Thr Tyr Leu Gly Asn Ala Leu Val Cys Thr Cys Tyr Gly 65 70 75 80 Gly Ser Arg Gly Phe Asn Cys Glu Ser Lys Pro Glu Ala Glu Glu Thr 85 90 95 Cys Phe Asp Lys Tyr Thr Gly Asn Thr Tyr Arg Val Gly Asp Thr Tyr 100 105 110 Glu Arg Pro Lys Asp Ser Met Ile Trp Asp Cys Thr Cys Ile Gly Ala 115 120 125 Gly Arg Gly Arg Ile Ser Cys Thr Ile Ala Asn Arg Cys His Glu Gly 130 135 140 Gly Gln Ser Tyr Lys Ile Gly Asp Thr Trp Arg Arg Pro His Glu Thr 145 150 155 160 Gly Gly Tyr Met Leu Glu Cys Val Cys Leu Gly Asn Gly Lys Gly Glu 165 170 175 Trp Thr Cys Lys Pro Ile Ala Glu Lys Cys Phe Asp His Ala Ala Gly 180 185 190 Thr Ser Tyr Val Val Gly Glu Thr Trp Glu Lys Pro Tyr Gln Gly Trp 195 200 205 Met Met Val Asp Cys Thr Cys Leu Gly Glu Gly Ser Gly Arg Ile Thr 210 215 220 Cys Thr Ser Arg Asn Arg Cys Asn Asp Gln Asp Thr Arg Thr Ser Tyr 225 230 235 240 Arg Ile Gly Asp Thr Trp Ser Lys Lys Asp Asn Arg Gly Asn Leu Leu 245 250 255 Gln Cys Ile Cys Thr Gly Asn Gly Arg Gly Glu Trp Lys Cys Glu Arg 260 265 270 His Thr Ser Val Gln Thr Thr Ser Ser Gly Ser Gly Pro Phe Thr Asp 275 280 285

Val Arg Ala Ala Val Tyr Gln Pro Gln Pro His Pro Gln Pro Pro Pro 290 295 300 Tyr Gly His Cys Val Thr Asp Ser Gly Val Val Tyr Ser Val Gly Met 305 310 315 320 Gln Trp Leu Lys Thr Gln Gly Asn Lys Gln Met Leu Cys Thr Cys Leu 325 330 335 Gly Asn Gly Val Ser Cys Gln Glu Thr Ala Val Thr Gln Thr Tyr Gly 340 345 350 Gly Asn Ser Asn Gly Glu Pro Cys Val Leu Pro Phe Thr Tyr Asn Gly 355 360 365 Arg Thr Phe Tyr Ser Cys Thr Thr Glu Gly Arg Gln Asp Gly His Leu 370 375 380 Trp Cys Ser Thr Thr Ser Asn Tyr Glu Gln Asp Gln Lys Tyr Ser Phe 385 390 395 400 Cys Thr Asp His Thr Val Leu Val Gln Thr Arg Gly Gly Asn Ser Asn 405 410 415 Gly Ala Leu Cys His Phe Pro Phe Leu Tyr Asn Asn His Asn Tyr Thr 420 425 430 Asp Cys Thr Ser Glu Gly Arg Arg Asp Asn Met Lys Trp Cys Gly Thr 435 440 445 Thr Gln Asn Tyr Asp Ala Asp Gln Lys Phe Gly Phe Cys Pro Met Ala 450 455 460 Ala His Glu Glu Ile Cys Thr Thr Asn Glu Gly Val Met Tyr Arg Ile 465 470 475 480 Gly Asp Gln Trp Asp Lys Gln His Asp Met Gly His Met Met Arg Cys 485 490 495 Thr Cys Val Gly Asn Gly Arg Gly Glu Trp Thr Cys Ile Ala Tyr Ser 500 505 510 Gln Leu Arg Asp Gln Cys Ile Val Asp Asp Ile Thr Tyr Asn Val Asn 515 520 525 Asp Thr Phe His Lys Arg His Glu Glu Gly His Met Leu Asn Cys Thr 530 535 540 Cys Phe Gly Gln Gly Arg Gly Arg Trp Lys Cys Asp Pro Val Asp Gln 545 550 555 560 Cys Gln Asp Ser Glu Thr Gly Thr Phe Tyr Gln Ile Gly Asp Ser Trp 565 570 575 Glu Lys Tyr Val His Gly Val Arg Tyr Gln Cys Tyr Cys Tyr Gly Arg 580 585 590 Gly Ile Gly Glu Trp His Cys Gln Pro Leu Gln Thr Tyr Pro Ser Ser 595 600 605 Ser Gly Pro Val Glu Val Phe Ile Thr Glu Thr Pro Ser Gln Pro Asn 610 615 620 Ser His Pro Ile Gln Trp Asn Ala Pro Gln Pro Ser His Ile Ser Lys 625 630 635 640 Tyr Ile Leu Arg Trp Arg Pro Lys Asn Ser Val Gly Arg Trp Lys Glu 645 650 655 Ala Thr Ile Pro Gly His Leu Asn Ser Tyr Thr Ile Lys Gly Leu Lys 660 665 670 Pro Gly Val Val Tyr Glu Gly Gln Leu Ile Ser Ile Gln Gln Tyr Gly 675 680 685 His Gln Glu Val Thr Arg Phe Asp Phe Thr Thr Thr Ser Thr Ser Thr 690 695 700 Pro Val Thr Ser Asn Thr Val Thr Gly Glu Thr Thr Pro Phe Ser Pro 705 710 715 720 Leu Val Ala Thr Ser Glu Ser Val Thr Glu Ile Thr Ala Ser Ser Phe 725 730 735 Val Val Ser Trp Val Ser Ala Ser Asp Thr Val Ser Gly Phe Arg Val 740 745 750 Glu Tyr Glu Leu Ser Glu Glu Gly Asp Glu Pro Gln Tyr Leu Asp Leu 755 760 765 Pro Ser Thr Ala Thr Ser Val Asn Ile Pro Asp Leu Leu Pro Gly Arg 770 775 780 Lys Tyr Ile Val Asn Val Tyr Gln Ile Ser Glu Asp Gly Glu Gln Ser 785 790 795 800 Leu Ile Leu Ser Thr Ser Gln Thr Thr Ala Pro Asp Ala Pro Pro Asp 805 810 815 Thr Thr Val Asp Gln Val Asp Asp Thr Ser Ile Val Val Arg Trp Ser 820 825 830 Arg Pro Gln Ala Pro Ile Thr Gly Tyr Arg Ile Val Tyr Ser Pro Ser 835 840 845 Val Glu Gly Ser Ser Thr Glu Leu Asn Leu Pro Glu Thr Ala Asn Ser 850 855 860 Val Thr Leu Ser Asp Leu Gln Pro Gly Val Gln Tyr Asn Ile Thr Ile 865 870 875 880 Tyr Ala Val Glu Glu Asn Gln Glu Ser Thr Pro Val Val Ile Gln Gln 885 890 895 Glu Thr Thr Gly Thr Pro Arg Ser Asp Thr Val Pro Ser Pro Arg Asp 900 905 910 Leu Gln Phe Val Glu Val Thr Asp Val Lys Val Thr Ile Met Trp Thr 915 920 925 Pro Pro Glu Ser Ala Val Thr Gly Tyr Arg Val Asp Val Ile Pro Val 930 935 940 Asn Leu Pro Gly Glu His Gly Gln Arg Leu Pro Ile Ser Arg Asn Thr 945 950 955 960 Phe Ala Glu Val Thr Gly Leu Ser Pro Gly Val Thr Tyr Tyr Phe Lys 965 970 975 Val Phe Ala Val Ser His Gly Arg Glu Ser Lys Pro Leu Thr Ala Gln 980 985 990 Gln Thr Thr Lys Leu Asp Ala Pro Thr Asn Leu Gln Phe Val Asn Glu 995 1000 1005 Thr Asp Ser Thr Val Leu Val Arg Trp Thr Pro Pro Arg Ala Gln 1010 1015 1020 Ile Thr Gly Tyr Arg Leu Thr Val Gly Leu Thr Arg Arg Gly Gln 1025 1030 1035 Pro Arg Gln Tyr Asn Val Gly Pro Ser Val Ser Lys Tyr Pro Leu 1040 1045 1050 Arg Asn Leu Gln Pro Ala Ser Glu Tyr Thr Val Ser Leu Val Ala 1055 1060 1065 Ile Lys Gly Asn Gln Glu Ser Pro Lys Ala Thr Gly Val Phe Thr 1070 1075 1080 Thr Leu Gln Pro Gly Ser Ser Ile Pro Pro Tyr Asn Thr Glu Val 1085 1090 1095 Thr Glu Thr Thr Ile Val Ile Thr Trp Thr Pro Ala Pro Arg Ile 1100 1105 1110 Gly Phe Lys Leu Gly Val Arg Pro Ser Gln Gly Gly Glu Ala Pro 1115 1120 1125 Arg Glu Val Thr Ser Asp Ser Gly Ser Ile Val Val Ser Gly Leu 1130 1135 1140 Thr Pro Gly Val Glu Tyr Val Tyr Thr Ile Gln Val Leu Arg Asp 1145 1150 1155 Gly Gln Glu Arg Asp Ala Pro Ile Val Asn Lys Val Val Thr Pro 1160 1165 1170 Leu Ser Pro Pro Thr Asn Leu His Leu Glu Ala Asn Pro Asp Thr 1175 1180 1185 Gly Val Leu Thr Val Ser Trp Glu Arg Ser Thr Thr Pro Asp Ile 1190 1195 1200 Thr Gly Tyr Arg Ile Thr Thr Thr Pro Thr Asn Gly Gln Gln Gly 1205 1210 1215 Asn Ser Leu Glu Glu Val Val His Ala Asp Gln Ser Ser Cys Thr 1220 1225 1230 Phe Asp Asn Leu Ser Pro Gly Leu Glu Tyr Asn Val Ser Val Tyr 1235 1240 1245 Thr Val Lys Asp Asp Lys Glu Ser Val Pro Ile Ser Asp Thr Ile 1250 1255 1260 Ile Pro Ala Val Pro Pro Pro Thr Asp Leu Arg Phe Thr Asn Ile 1265 1270 1275 Gly Pro Asp Thr Met Arg Val Thr Trp Ala Pro Pro Pro Ser Ile 1280 1285 1290 Asp Leu Thr Asn Phe Leu Val Arg Tyr Ser Pro Val Lys Asn Glu 1295 1300 1305 Glu Asp Val Ala Glu Leu Ser Ile Ser Pro Ser Asp Asn Ala Val 1310 1315 1320 Val Leu Thr Asn Leu Leu Pro Gly Thr Glu Tyr Val Val Ser Val 1325 1330 1335 Ser Ser Val Tyr Glu Gln His Glu Ser Thr Pro Leu Arg Gly Arg 1340 1345 1350 Gln Lys Thr Gly Leu Asp Ser Pro Thr Gly Ile Asp Phe Ser Asp 1355 1360 1365 Ile Thr Ala Asn Ser Phe Thr Val His Trp Ile Ala Pro Arg Ala 1370 1375 1380 Thr Ile Thr Gly Tyr Arg Ile Arg His His Pro Glu His Phe Ser 1385 1390 1395 Gly Arg Pro Arg Glu Asp Arg Val Pro His Ser Arg Asn Ser Ile 1400 1405 1410 Thr Leu Thr Asn Leu Thr Pro Gly Thr Glu Tyr Val Val Ser Ile 1415 1420 1425 Val Ala Leu Asn Gly Arg Glu Glu Ser Pro Leu Leu Ile Gly Gln 1430 1435 1440 Gln Ser Thr Val Ser Asp Val Pro Arg Asp Leu Glu Val Val Ala 1445 1450 1455 Ala Thr Pro Thr Ser Leu Leu Ile Ser Trp Asp Ala Pro Ala Val 1460 1465 1470 Thr Val Arg Tyr Tyr Arg Ile Thr Tyr Gly Glu Thr Gly Gly Asn 1475 1480 1485 Ser Pro Val Gln Glu Phe Thr Val Pro Gly Ser Lys Ser Thr Ala 1490 1495 1500 Thr Ile Ser Gly Leu Lys Pro Gly Val Asp Tyr Thr Ile Thr Val 1505 1510 1515 Tyr Ala Val Thr Gly Arg Gly Asp Ser Pro Ala Ser Ser Lys Pro 1520 1525 1530 Ile Ser Ile Asn Tyr Arg Thr Glu Ile Asp Lys Pro Ser Gln Met 1535 1540 1545 Gln Val Thr Asp Val Gln Asp Asn Ser Ile Ser Val Lys Trp Leu 1550 1555 1560 Pro Ser Ser Ser Pro Val Thr Gly Tyr Arg Val Thr Thr Thr Pro 1565 1570 1575 Lys Asn Gly Pro Gly Pro Thr Lys Thr Lys Thr Ala Gly Pro Asp

1580 1585 1590 Gln Thr Glu Met Thr Ile Glu Gly Leu Gln Pro Thr Val Glu Tyr 1595 1600 1605 Val Val Ser Val Tyr Ala Gln Asn Pro Ser Gly Glu Ser Gln Pro 1610 1615 1620 Leu Val Gln Thr Ala Val Thr Asn Ile Asp Arg Pro Lys Gly Leu 1625 1630 1635 Ala Phe Thr Asp Val Asp Val Asp Ser Ile Lys Ile Ala Trp Glu 1640 1645 1650 Ser Pro Gln Gly Gln Val Ser Arg Tyr Arg Val Thr Tyr Ser Ser 1655 1660 1665 Pro Glu Asp Gly Ile His Glu Leu Phe Pro Ala Pro Asp Gly Glu 1670 1675 1680 Glu Asp Thr Ala Glu Leu Gln Gly Leu Arg Pro Gly Ser Glu Tyr 1685 1690 1695 Thr Val Ser Val Val Ala Leu His Asp Asp Met Glu Ser Gln Pro 1700 1705 1710 Leu Ile Gly Thr Gln Ser Thr Ala Ile Pro Ala Pro Thr Asp Leu 1715 1720 1725 Lys Phe Thr Gln Val Thr Pro Thr Ser Leu Ser Ala Gln Trp Thr 1730 1735 1740 Pro Pro Asn Val Gln Leu Thr Gly Tyr Arg Val Arg Val Thr Pro 1745 1750 1755 Lys Glu Lys Thr Gly Pro Met Lys Glu Ile Asn Leu Ala Pro Asp 1760 1765 1770 Ser Ser Ser Val Val Val Ser Gly Leu Met Val Ala Thr Lys Tyr 1775 1780 1785 Glu Val Ser Val Tyr Ala Leu Lys Asp Thr Leu Thr Ser Arg Pro 1790 1795 1800 Ala Gln Gly Val Val Thr Thr Leu Glu Asn Val Ser Pro Pro Arg 1805 1810 1815 Arg Ala Arg Val Thr Asp Ala Thr Glu Thr Thr Ile Thr Ile Ser 1820 1825 1830 Trp Arg Thr Lys Thr Glu Thr Ile Thr Gly Phe Gln Val Asp Ala 1835 1840 1845 Val Pro Ala Asn Gly Gln Thr Pro Ile Gln Arg Thr Ile Lys Pro 1850 1855 1860 Asp Val Arg Ser Tyr Thr Ile Thr Gly Leu Gln Pro Gly Thr Asp 1865 1870 1875 Tyr Lys Ile Tyr Leu Tyr Thr Leu Asn Asp Asn Ala Arg Ser Ser 1880 1885 1890 Pro Val Val Ile Asp Ala Ser Thr Ala Ile Asp Ala Pro Ser Asn 1895 1900 1905 Leu Arg Phe Leu Ala Thr Thr Pro Asn Ser Leu Leu Val Ser Trp 1910 1915 1920 Gln Pro Pro Arg Ala Arg Ile Thr Gly Tyr Ile Ile Lys Tyr Glu 1925 1930 1935 Lys Pro Gly Ser Pro Pro Arg Glu Val Val Pro Arg Pro Arg Pro 1940 1945 1950 Gly Val Thr Glu Ala Thr Ile Thr Gly Leu Glu Pro Gly Thr Glu 1955 1960 1965 Tyr Thr Ile Tyr Val Ile Ala Leu Lys Asn Asn Gln Lys Ser Glu 1970 1975 1980 Pro Leu Ile Gly Arg Lys Lys Thr Asp Glu Leu Pro Gln Leu Val 1985 1990 1995 Thr Leu Pro His Pro Asn Leu His Gly Pro Glu Ile Leu Asp Val 2000 2005 2010 Pro Ser Thr Val Gln Lys Thr Pro Phe Val Thr His Pro Gly Tyr 2015 2020 2025 Asp Thr Gly Asn Gly Ile Gln Leu Pro Gly Thr Ser Gly Gln Gln 2030 2035 2040 Pro Ser Val Gly Gln Gln Met Ile Phe Glu Glu His Gly Phe Arg 2045 2050 2055 Arg Thr Thr Pro Pro Thr Thr Ala Thr Pro Ile Arg His Arg Pro 2060 2065 2070 Arg Pro Tyr Pro Pro Asn Val Gly Glu Glu Ile Gln Ile Gly His 2075 2080 2085 Ile Pro Arg Glu Asp Val Asp Tyr His Leu Tyr Pro His Gly Pro 2090 2095 2100 Gly Leu Asn Pro Asn Ala Ser Thr Gly Gln Glu Ala Leu Ser Gln 2105 2110 2115 Thr Thr Ile Ser Trp Ala Pro Phe Gln Asp Thr Ser Glu Tyr Ile 2120 2125 2130 Ile Ser Cys His Pro Val Gly Thr Asp Glu Glu Pro Leu Gln Phe 2135 2140 2145 Arg Val Pro Gly Thr Ser Thr Ser Ala Thr Leu Thr Gly Leu Thr 2150 2155 2160 Arg Gly Ala Thr Tyr Asn Val Ile Val Glu Ala Leu Lys Asp Gln 2165 2170 2175 Gln Arg His Lys Val Arg Glu Glu Val Val Thr Val Gly Asn Ser 2180 2185 2190 Val Asn Glu Gly Leu Asn Gln Pro Thr Asp Asp Ser Cys Phe Asp 2195 2200 2205 Pro Tyr Thr Val Ser His Tyr Ala Val Gly Asp Glu Trp Glu Arg 2210 2215 2220 Met Ser Glu Ser Gly Phe Lys Leu Leu Cys Gln Cys Leu Gly Phe 2225 2230 2235 Gly Ser Gly His Phe Arg Cys Asp Ser Ser Arg Trp Cys His Asp 2240 2245 2250 Asn Gly Val Asn Tyr Lys Ile Gly Glu Lys Trp Asp Arg Gln Gly 2255 2260 2265 Glu Asn Gly Gln Met Met Ser Cys Thr Cys Leu Gly Asn Gly Lys 2270 2275 2280 Gly Glu Phe Lys Cys Asp Pro His Glu Ala Thr Cys Tyr Asp Asp 2285 2290 2295 Gly Lys Thr Tyr His Val Gly Glu Gln Trp Gln Lys Glu Tyr Leu 2300 2305 2310 Gly Ala Ile Cys Ser Cys Thr Cys Phe Gly Gly Gln Arg Gly Trp 2315 2320 2325 Arg Cys Asp Asn Cys Arg Arg Pro Gly Gly Glu Pro Ser Pro Glu 2330 2335 2340 Gly Thr Thr Gly Gln Ser Tyr Asn Gln Tyr Ser Gln Arg Tyr His 2345 2350 2355 Gln Arg Thr Asn Thr Asn Val Asn Cys Pro Ile Glu Cys Phe Met 2360 2365 2370 Pro Leu Asp Val Gln Ala Asp Arg Glu Asp Ser Arg Glu 2375 2380 2385 <210> SEQ ID NO 65 <211> LENGTH: 240 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P30711 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(240) <400> SEQUENCE: 65 Met Gly Leu Glu Leu Tyr Leu Asp Leu Leu Ser Gln Pro Cys Arg Ala 1 5 10 15 Val Tyr Ile Phe Ala Lys Lys Asn Asp Ile Pro Phe Glu Leu Arg Ile 20 25 30 Val Asp Leu Ile Lys Gly Gln His Leu Ser Asp Ala Phe Ala Gln Val 35 40 45 Asn Pro Leu Lys Lys Val Pro Ala Leu Lys Asp Gly Asp Phe Thr Leu 50 55 60 Thr Glu Ser Val Ala Ile Leu Leu Tyr Leu Thr Arg Lys Tyr Lys Val 65 70 75 80 Pro Asp Tyr Trp Tyr Pro Gln Asp Leu Gln Ala Arg Ala Arg Val Asp 85 90 95 Glu Tyr Leu Ala Trp Gln His Thr Thr Leu Arg Arg Ser Cys Leu Arg 100 105 110 Ala Leu Trp His Lys Val Met Phe Pro Val Phe Leu Gly Glu Pro Val 115 120 125 Ser Pro Gln Thr Leu Ala Ala Thr Leu Ala Glu Leu Asp Val Thr Leu 130 135 140 Gln Leu Leu Glu Asp Lys Phe Leu Gln Asn Lys Ala Phe Leu Thr Gly 145 150 155 160 Pro His Ile Ser Leu Ala Asp Leu Val Ala Ile Thr Glu Leu Met His 165 170 175 Pro Val Gly Ala Gly Cys Gln Val Phe Glu Gly Arg Pro Lys Leu Ala 180 185 190 Thr Trp Arg Gln Arg Val Glu Ala Ala Val Gly Glu Asp Leu Phe Gln 195 200 205 Glu Ala His Glu Val Ile Leu Lys Ala Lys Asp Phe Pro Pro Ala Asp 210 215 220 Pro Thr Ile Lys Gln Lys Leu Met Pro Trp Val Leu Ala Met Ile Arg 225 230 235 240 <210> SEQ ID NO 66 <211> LENGTH: 644 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P04264 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(644) <400> SEQUENCE: 66 Met Ser Arg Gln Phe Ser Ser Arg Ser Gly Tyr Arg Ser Gly Gly Gly 1 5 10 15 Phe Ser Ser Gly Ser Ala Gly Ile Ile Asn Tyr Gln Arg Arg Thr Thr 20 25 30 Ser Ser Ser Thr Arg Arg Ser Gly Gly Gly Gly Gly Arg Phe Ser Ser 35 40 45 Cys Gly Gly Gly Gly Gly Ser Phe Gly Ala Gly Gly Gly Phe Gly Ser 50 55 60 Arg Ser Leu Val Asn Leu Gly Gly Ser Lys Ser Ile Ser Ile Ser Val 65 70 75 80 Ala Arg Gly Gly Gly Arg Gly Ser Gly Phe Gly Gly Gly Tyr Gly Gly 85 90 95 Gly Gly Phe Gly Gly Gly Gly Phe Gly Gly Gly Gly Phe Gly Gly Gly 100 105 110

Gly Ile Gly Gly Gly Gly Phe Gly Gly Phe Gly Ser Gly Gly Gly Gly 115 120 125 Phe Gly Gly Gly Gly Phe Gly Gly Gly Gly Tyr Gly Gly Gly Tyr Gly 130 135 140 Pro Val Cys Pro Pro Gly Gly Ile Gln Glu Val Thr Ile Asn Gln Ser 145 150 155 160 Leu Leu Gln Pro Leu Asn Val Glu Ile Asp Pro Glu Ile Gln Lys Val 165 170 175 Lys Ser Arg Glu Arg Glu Gln Ile Lys Ser Leu Asn Asn Gln Phe Ala 180 185 190 Ser Phe Ile Asp Lys Val Arg Phe Leu Glu Gln Gln Asn Gln Val Leu 195 200 205 Gln Thr Lys Trp Glu Leu Leu Gln Gln Val Asp Thr Ser Thr Arg Thr 210 215 220 His Asn Leu Glu Pro Tyr Phe Glu Ser Phe Ile Asn Asn Leu Arg Arg 225 230 235 240 Arg Val Asp Gln Leu Lys Ser Asp Gln Ser Arg Leu Asp Ser Glu Leu 245 250 255 Lys Asn Met Gln Asp Met Val Glu Asp Tyr Arg Asn Lys Tyr Glu Asp 260 265 270 Glu Ile Asn Lys Arg Thr Asn Ala Glu Asn Glu Phe Val Thr Ile Lys 275 280 285 Lys Asp Val Asp Gly Ala Tyr Met Thr Lys Val Asp Leu Gln Ala Lys 290 295 300 Leu Asp Asn Leu Gln Gln Glu Ile Asp Phe Leu Thr Ala Leu Tyr Gln 305 310 315 320 Ala Glu Leu Ser Gln Met Gln Thr Gln Ile Ser Glu Thr Asn Val Ile 325 330 335 Leu Ser Met Asp Asn Asn Arg Ser Leu Asp Leu Asp Ser Ile Ile Ala 340 345 350 Glu Val Lys Ala Gln Tyr Glu Asp Ile Ala Gln Lys Ser Lys Ala Glu 355 360 365 Ala Glu Ser Leu Tyr Gln Ser Lys Tyr Glu Glu Leu Gln Ile Thr Ala 370 375 380 Gly Arg His Gly Asp Ser Val Arg Asn Ser Lys Ile Glu Ile Ser Glu 385 390 395 400 Leu Asn Arg Val Ile Gln Arg Leu Arg Ser Glu Ile Asp Asn Val Lys 405 410 415 Lys Gln Ile Ser Asn Leu Gln Gln Ser Ile Ser Asp Ala Glu Gln Arg 420 425 430 Gly Glu Asn Ala Leu Lys Asp Ala Lys Asn Lys Leu Asn Asp Leu Glu 435 440 445 Asp Ala Leu Gln Gln Ala Lys Glu Asp Leu Ala Arg Leu Leu Arg Asp 450 455 460 Tyr Gln Glu Leu Met Asn Thr Lys Leu Ala Leu Asp Leu Glu Ile Ala 465 470 475 480 Thr Tyr Arg Thr Leu Leu Glu Gly Glu Glu Ser Arg Met Ser Gly Glu 485 490 495 Cys Ala Pro Asn Val Ser Val Ser Val Ser Thr Ser His Thr Thr Ile 500 505 510 Ser Gly Gly Gly Ser Arg Gly Gly Gly Gly Gly Gly Tyr Gly Ser Gly 515 520 525 Gly Ser Ser Tyr Gly Ser Gly Gly Gly Ser Tyr Gly Ser Gly Gly Gly 530 535 540 Gly Gly Gly Gly Arg Gly Ser Tyr Gly Ser Gly Gly Ser Ser Tyr Gly 545 550 555 560 Ser Gly Gly Gly Ser Tyr Gly Ser Gly Gly Gly Gly Gly Gly His Gly 565 570 575 Ser Tyr Gly Ser Gly Ser Ser Ser Gly Gly Tyr Arg Gly Gly Ser Gly 580 585 590 Gly Gly Gly Gly Gly Ser Ser Gly Gly Arg Gly Ser Gly Gly Gly Ser 595 600 605 Ser Gly Gly Ser Ile Gly Gly Arg Gly Ser Ser Ser Gly Gly Val Lys 610 615 620 Ser Ser Gly Gly Ser Ser Ser Val Lys Phe Val Ser Thr Thr Tyr Ser 625 630 635 640 Gly Val Thr Arg <210> SEQ ID NO 67 <211> LENGTH: 1939 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P13533 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1939) <400> SEQUENCE: 67 Met Thr Asp Ala Gln Met Ala Asp Phe Gly Ala Ala Ala Gln Tyr Leu 1 5 10 15 Arg Lys Ser Glu Lys Glu Arg Leu Glu Ala Gln Thr Arg Pro Phe Asp 20 25 30 Ile Arg Thr Glu Cys Phe Val Pro Asp Asp Lys Glu Glu Phe Val Lys 35 40 45 Ala Lys Ile Leu Ser Arg Glu Gly Gly Lys Val Ile Ala Glu Thr Glu 50 55 60 Asn Gly Lys Thr Val Thr Val Lys Glu Asp Gln Val Leu Gln Gln Asn 65 70 75 80 Pro Pro Lys Phe Asp Lys Ile Glu Asp Met Ala Met Leu Thr Phe Leu 85 90 95 His Glu Pro Ala Val Leu Phe Asn Leu Lys Glu Arg Tyr Ala Ala Trp 100 105 110 Met Ile Tyr Thr Tyr Ser Gly Leu Phe Cys Val Thr Val Asn Pro Tyr 115 120 125 Lys Trp Leu Pro Val Tyr Asn Ala Glu Val Val Ala Ala Tyr Arg Gly 130 135 140 Lys Lys Arg Ser Glu Ala Pro Pro His Ile Phe Ser Ile Ser Asp Asn 145 150 155 160 Ala Tyr Gln Tyr Met Leu Thr Asp Arg Glu Asn Gln Ser Ile Leu Ile 165 170 175 Thr Gly Glu Ser Gly Ala Gly Lys Thr Val Asn Thr Lys Arg Val Ile 180 185 190 Gln Tyr Phe Ala Ser Ile Ala Ala Ile Gly Asp Arg Gly Lys Lys Asp 195 200 205 Asn Ala Asn Ala Asn Lys Gly Thr Leu Glu Asp Gln Ile Ile Gln Ala 210 215 220 Asn Pro Ala Leu Glu Ala Phe Gly Asn Ala Lys Thr Val Arg Asn Asp 225 230 235 240 Asn Ser Ser Arg Phe Gly Lys Phe Ile Arg Ile His Phe Gly Ala Thr 245 250 255 Gly Lys Leu Ala Ser Ala Asp Ile Glu Thr Tyr Leu Leu Glu Lys Ser 260 265 270 Arg Val Ile Phe Gln Leu Lys Ala Glu Arg Asn Tyr His Ile Phe Tyr 275 280 285 Gln Ile Leu Ser Asn Lys Lys Pro Glu Leu Leu Asp Met Leu Leu Val 290 295 300 Thr Asn Asn Pro Tyr Asp Tyr Ala Phe Val Ser Gln Gly Glu Val Ser 305 310 315 320 Val Ala Ser Ile Asp Asp Ser Glu Glu Leu Met Ala Thr Asp Ser Ala 325 330 335 Phe Asp Val Leu Gly Phe Thr Ser Glu Glu Lys Ala Gly Val Tyr Lys 340 345 350 Leu Thr Gly Ala Ile Met His Tyr Gly Asn Met Lys Phe Lys Gln Lys 355 360 365 Gln Arg Glu Glu Gln Ala Glu Pro Asp Gly Thr Glu Asp Ala Asp Lys 370 375 380 Ser Ala Tyr Leu Met Gly Leu Asn Ser Ala Asp Leu Leu Lys Gly Leu 385 390 395 400 Cys His Pro Arg Val Lys Val Gly Asn Glu Tyr Val Thr Lys Gly Gln 405 410 415 Ser Val Gln Gln Val Tyr Tyr Ser Ile Gly Ala Leu Ala Lys Ala Val 420 425 430 Tyr Glu Lys Met Phe Asn Trp Met Val Thr Arg Ile Asn Ala Thr Leu 435 440 445 Glu Thr Lys Gln Pro Arg Gln Tyr Phe Ile Gly Val Leu Asp Ile Ala 450 455 460 Gly Phe Glu Ile Phe Asp Phe Asn Ser Phe Glu Gln Leu Cys Ile Asn 465 470 475 480 Phe Thr Asn Glu Lys Leu Gln Gln Phe Phe Asn His His Met Phe Val 485 490 495 Leu Glu Gln Glu Glu Tyr Lys Lys Glu Gly Ile Glu Trp Thr Phe Ile 500 505 510 Asp Phe Gly Met Asp Leu Gln Ala Cys Ile Asp Leu Ile Glu Lys Pro 515 520 525 Met Gly Ile Met Ser Ile Leu Glu Glu Glu Cys Met Phe Pro Lys Ala 530 535 540 Thr Asp Met Thr Phe Lys Ala Lys Leu Tyr Asp Asn His Leu Gly Lys 545 550 555 560 Ser Asn Asn Phe Gln Lys Pro Arg Asn Ile Lys Gly Lys Gln Glu Ala 565 570 575 His Phe Ser Leu Ile His Tyr Ala Gly Thr Val Asp Tyr Asn Ile Leu 580 585 590 Gly Trp Leu Glu Lys Asn Lys Asp Pro Leu Asn Glu Thr Val Val Ala 595 600 605 Leu Tyr Gln Lys Ser Ser Leu Lys Leu Met Ala Thr Leu Phe Ser Ser 610 615 620 Tyr Ala Thr Ala Asp Thr Gly Asp Ser Gly Lys Ser Lys Gly Gly Lys 625 630 635 640 Lys Lys Gly Ser Ser Phe Gln Thr Val Ser Ala Leu His Arg Glu Asn 645 650 655 Leu Asn Lys Leu Met Thr Asn Leu Arg Thr Thr His Pro His Phe Val 660 665 670 Arg Cys Ile Ile Pro Asn Glu Arg Lys Ala Pro Gly Val Met Asp Asn 675 680 685 Pro Leu Val Met His Gln Leu Arg Cys Asn Gly Val Leu Glu Gly Ile 690 695 700 Arg Ile Cys Arg Lys Gly Phe Pro Asn Arg Ile Leu Tyr Gly Asp Phe 705 710 715 720 Arg Gln Arg Tyr Arg Ile Leu Asn Pro Val Ala Ile Pro Glu Gly Gln 725 730 735

Phe Ile Asp Ser Arg Lys Gly Thr Glu Lys Leu Leu Ser Ser Leu Asp 740 745 750 Ile Asp His Asn Gln Tyr Lys Phe Gly His Thr Lys Val Phe Phe Lys 755 760 765 Ala Gly Leu Leu Gly Leu Leu Glu Glu Met Arg Asp Glu Arg Leu Ser 770 775 780 Arg Ile Ile Thr Arg Met Gln Ala Gln Ala Arg Gly Gln Leu Met Arg 785 790 795 800 Ile Glu Phe Lys Lys Ile Val Glu Arg Arg Asp Ala Leu Leu Val Ile 805 810 815 Gln Trp Asn Ile Arg Ala Phe Met Gly Val Lys Asn Trp Pro Trp Met 820 825 830 Lys Leu Tyr Phe Lys Ile Lys Pro Leu Leu Lys Ser Ala Glu Thr Glu 835 840 845 Lys Glu Met Ala Thr Met Lys Glu Glu Phe Gly Arg Ile Lys Glu Thr 850 855 860 Leu Glu Lys Ser Glu Ala Arg Arg Lys Glu Leu Glu Glu Lys Met Val 865 870 875 880 Ser Leu Leu Gln Glu Lys Asn Asp Leu Gln Leu Gln Val Gln Ala Glu 885 890 895 Gln Asp Asn Leu Asn Asp Ala Glu Glu Arg Cys Asp Gln Leu Ile Lys 900 905 910 Asn Lys Ile Gln Leu Glu Ala Lys Val Lys Glu Met Asn Glu Arg Leu 915 920 925 Glu Asp Glu Glu Glu Met Asn Ala Glu Leu Thr Ala Lys Lys Arg Lys 930 935 940 Leu Glu Asp Glu Cys Ser Glu Leu Lys Lys Asp Ile Asp Asp Leu Glu 945 950 955 960 Leu Thr Leu Ala Lys Val Glu Lys Glu Lys His Ala Thr Glu Asn Lys 965 970 975 Val Lys Asn Leu Thr Glu Glu Met Ala Gly Leu Asp Glu Ile Ile Ala 980 985 990 Lys Leu Thr Lys Glu Lys Lys Ala Leu Gln Glu Ala His Gln Gln Ala 995 1000 1005 Leu Asp Asp Leu Gln Val Glu Glu Asp Lys Val Asn Ser Leu Ser 1010 1015 1020 Lys Ser Lys Val Lys Leu Glu Gln Gln Val Asp Asp Leu Glu Gly 1025 1030 1035 Ser Leu Glu Gln Glu Lys Lys Val Arg Met Asp Leu Glu Arg Ala 1040 1045 1050 Lys Arg Lys Leu Glu Gly Asp Leu Lys Leu Thr Gln Glu Ser Ile 1055 1060 1065 Met Asp Leu Glu Asn Asp Lys Leu Gln Leu Glu Glu Lys Leu Lys 1070 1075 1080 Lys Lys Glu Phe Asp Ile Asn Gln Gln Asn Ser Lys Ile Glu Asp 1085 1090 1095 Glu Gln Val Leu Ala Leu Gln Leu Gln Lys Lys Leu Lys Glu Asn 1100 1105 1110 Gln Ala Arg Ile Glu Glu Leu Glu Glu Glu Leu Glu Ala Glu Arg 1115 1120 1125 Thr Ala Arg Ala Lys Val Glu Lys Leu Arg Ser Asp Leu Ser Arg 1130 1135 1140 Glu Leu Glu Glu Ile Ser Glu Arg Leu Glu Glu Ala Gly Gly Ala 1145 1150 1155 Thr Ser Val Gln Ile Glu Met Asn Lys Lys Arg Glu Ala Glu Phe 1160 1165 1170 Gln Lys Met Arg Arg Asp Leu Glu Glu Ala Thr Leu Gln His Glu 1175 1180 1185 Ala Thr Ala Ala Ala Leu Arg Lys Lys His Ala Asp Ser Val Ala 1190 1195 1200 Glu Leu Gly Glu Gln Ile Asp Asn Leu Gln Arg Val Lys Gln Lys 1205 1210 1215 Leu Glu Lys Glu Lys Ser Glu Phe Lys Leu Glu Leu Asp Asp Val 1220 1225 1230 Thr Ser Asn Met Glu Gln Ile Ile Lys Ala Lys Ala Asn Leu Glu 1235 1240 1245 Lys Val Ser Arg Thr Leu Glu Asp Gln Ala Asn Glu Tyr Arg Val 1250 1255 1260 Lys Leu Glu Glu Ala Gln Arg Ser Leu Asn Asp Phe Thr Thr Gln 1265 1270 1275 Arg Ala Lys Leu Gln Thr Glu Asn Gly Glu Leu Ala Arg Gln Leu 1280 1285 1290 Glu Glu Lys Glu Ala Leu Ile Ser Gln Leu Thr Arg Gly Lys Leu 1295 1300 1305 Ser Tyr Thr Gln Gln Met Glu Asp Leu Lys Arg Gln Leu Glu Glu 1310 1315 1320 Glu Gly Lys Ala Lys Asn Ala Leu Ala His Ala Leu Gln Ser Ala 1325 1330 1335 Arg His Asp Cys Asp Leu Leu Arg Glu Gln Tyr Glu Glu Glu Thr 1340 1345 1350 Glu Ala Lys Ala Glu Leu Gln Arg Val Leu Ser Lys Ala Asn Ser 1355 1360 1365 Glu Val Ala Gln Trp Arg Thr Lys Tyr Glu Thr Asp Ala Ile Gln 1370 1375 1380 Arg Thr Glu Glu Leu Glu Glu Ala Lys Lys Lys Leu Ala Gln Arg 1385 1390 1395 Leu Gln Asp Ala Glu Glu Ala Val Glu Ala Val Asn Ala Lys Cys 1400 1405 1410 Ser Ser Leu Glu Lys Thr Lys His Arg Leu Gln Asn Glu Ile Glu 1415 1420 1425 Asp Leu Met Val Asp Val Glu Arg Ser Asn Ala Ala Ala Ala Ala 1430 1435 1440 Leu Asp Lys Lys Gln Arg Asn Phe Asp Lys Ile Leu Ala Glu Trp 1445 1450 1455 Lys Gln Lys Tyr Glu Glu Ser Gln Ser Glu Leu Glu Ser Ser Gln 1460 1465 1470 Lys Glu Ala Arg Ser Leu Ser Thr Glu Leu Phe Lys Leu Lys Asn 1475 1480 1485 Ala Tyr Glu Glu Ser Leu Glu His Leu Glu Thr Phe Lys Arg Glu 1490 1495 1500 Asn Lys Asn Leu Gln Glu Glu Ile Ser Asp Leu Thr Glu Gln Leu 1505 1510 1515 Gly Glu Gly Gly Lys Asn Val His Glu Leu Glu Lys Val Arg Lys 1520 1525 1530 Gln Leu Glu Val Glu Lys Leu Glu Leu Gln Ser Ala Leu Glu Glu 1535 1540 1545 Ala Glu Ala Ser Leu Glu His Glu Glu Gly Lys Ile Leu Arg Ala 1550 1555 1560 Gln Leu Glu Phe Asn Gln Ile Lys Ala Glu Ile Glu Arg Lys Leu 1565 1570 1575 Ala Glu Lys Asp Glu Glu Met Glu Gln Ala Lys Arg Asn His Gln 1580 1585 1590 Arg Val Val Asp Ser Leu Gln Thr Ser Leu Asp Ala Glu Thr Arg 1595 1600 1605 Ser Arg Asn Glu Val Leu Arg Val Lys Lys Lys Met Glu Gly Asp 1610 1615 1620 Leu Asn Glu Met Glu Ile Gln Leu Ser His Ala Asn Arg Met Ala 1625 1630 1635 Ala Glu Ala Gln Lys Gln Val Lys Ser Leu Gln Ser Leu Leu Lys 1640 1645 1650 Asp Thr Gln Ile Gln Leu Asp Asp Ala Val Arg Ala Asn Asp Asp 1655 1660 1665 Leu Lys Glu Asn Ile Ala Ile Val Glu Arg Arg Asn Asn Leu Leu 1670 1675 1680 Gln Ala Glu Leu Glu Glu Leu Arg Ala Val Val Glu Gln Thr Glu 1685 1690 1695 Arg Ser Arg Lys Leu Ala Glu Gln Glu Leu Ile Glu Thr Ser Glu 1700 1705 1710 Arg Val Gln Leu Leu His Ser Gln Asn Thr Ser Leu Ile Asn Gln 1715 1720 1725 Lys Lys Lys Met Glu Ser Asp Leu Thr Gln Leu Gln Ser Glu Val 1730 1735 1740 Glu Glu Ala Val Gln Glu Cys Arg Asn Ala Glu Glu Lys Ala Lys 1745 1750 1755 Lys Ala Ile Thr Asp Ala Ala Met Met Ala Glu Glu Leu Lys Lys 1760 1765 1770 Glu Gln Asp Thr Ser Ala His Leu Glu Arg Met Lys Lys Asn Met 1775 1780 1785 Glu Gln Thr Ile Lys Asp Leu Gln His Arg Leu Asp Glu Ala Glu 1790 1795 1800 Gln Ile Ala Leu Lys Gly Gly Lys Lys Gln Leu Gln Lys Leu Glu 1805 1810 1815 Ala Arg Val Arg Glu Leu Glu Gly Glu Leu Glu Ala Glu Gln Lys 1820 1825 1830 Arg Asn Ala Glu Ser Val Lys Gly Met Arg Lys Ser Glu Arg Arg 1835 1840 1845 Ile Lys Glu Leu Thr Tyr Gln Thr Glu Glu Asp Lys Lys Asn Leu 1850 1855 1860 Leu Arg Leu Gln Asp Leu Val Asp Lys Leu Gln Leu Lys Val Lys 1865 1870 1875 Ala Tyr Lys Arg Gln Ala Glu Glu Ala Glu Glu Gln Ala Asn Thr 1880 1885 1890 Asn Leu Ser Lys Phe Arg Lys Val Gln His Glu Leu Asp Glu Ala 1895 1900 1905 Glu Glu Arg Ala Asp Ile Ala Glu Ser Gln Val Asn Lys Leu Arg 1910 1915 1920 Ala Lys Ser Arg Asp Ile Gly Ala Lys Gln Lys Met His Asp Glu 1925 1930 1935 Glu <210> SEQ ID NO 68 <211> LENGTH: 1935 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P12883 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1935) <400> SEQUENCE: 68

Met Gly Asp Ser Glu Met Ala Val Phe Gly Ala Ala Ala Pro Tyr Leu 1 5 10 15 Arg Lys Ser Glu Lys Glu Arg Leu Glu Ala Gln Thr Arg Pro Phe Asp 20 25 30 Leu Lys Lys Asp Val Phe Val Pro Asp Asp Lys Gln Glu Phe Val Lys 35 40 45 Ala Lys Ile Val Ser Arg Glu Gly Gly Lys Val Thr Ala Glu Thr Glu 50 55 60 Tyr Gly Lys Thr Val Thr Val Lys Glu Asp Gln Val Met Gln Gln Asn 65 70 75 80 Pro Pro Lys Phe Asp Lys Ile Glu Asp Met Ala Met Leu Thr Phe Leu 85 90 95 His Glu Pro Ala Val Leu Tyr Asn Leu Lys Asp Arg Tyr Gly Ser Trp 100 105 110 Met Ile Tyr Thr Tyr Ser Gly Leu Phe Cys Val Thr Val Asn Pro Tyr 115 120 125 Lys Trp Leu Pro Val Tyr Thr Pro Glu Val Val Ala Ala Tyr Arg Gly 130 135 140 Lys Lys Arg Ser Glu Ala Pro Pro His Ile Phe Ser Ile Ser Asp Asn 145 150 155 160 Ala Tyr Gln Tyr Met Leu Thr Asp Arg Glu Asn Gln Ser Ile Leu Ile 165 170 175 Thr Gly Glu Ser Gly Ala Gly Lys Thr Val Asn Thr Lys Arg Val Ile 180 185 190 Gln Tyr Phe Ala Val Ile Ala Ala Ile Gly Asp Arg Ser Lys Lys Asp 195 200 205 Gln Ser Pro Gly Lys Gly Thr Leu Glu Asp Gln Ile Ile Gln Ala Asn 210 215 220 Pro Ala Leu Glu Ala Phe Gly Asn Ala Lys Thr Val Arg Asn Asp Asn 225 230 235 240 Ser Ser Arg Phe Gly Lys Phe Ile Arg Ile His Phe Gly Ala Thr Gly 245 250 255 Lys Leu Ala Ser Ala Asp Ile Glu Thr Tyr Leu Leu Glu Lys Ser Arg 260 265 270 Val Ile Phe Gln Leu Lys Ala Glu Arg Asp Tyr His Ile Phe Tyr Gln 275 280 285 Ile Leu Ser Asn Lys Lys Pro Glu Leu Leu Asp Met Leu Leu Ile Thr 290 295 300 Asn Asn Pro Tyr Asp Tyr Ala Phe Ile Ser Gln Gly Glu Thr Thr Val 305 310 315 320 Ala Ser Ile Asp Asp Ala Glu Glu Leu Met Ala Thr Asp Asn Ala Phe 325 330 335 Asp Val Leu Gly Phe Thr Ser Glu Glu Lys Asn Ser Met Tyr Lys Leu 340 345 350 Thr Gly Ala Ile Met His Phe Gly Asn Met Lys Phe Lys Leu Lys Gln 355 360 365 Arg Glu Glu Gln Ala Glu Pro Asp Gly Thr Glu Glu Ala Asp Lys Ser 370 375 380 Ala Tyr Leu Met Gly Leu Asn Ser Ala Asp Leu Leu Lys Gly Leu Cys 385 390 395 400 His Pro Arg Val Lys Val Gly Asn Glu Tyr Val Thr Lys Gly Gln Asn 405 410 415 Val Gln Gln Val Ile Tyr Ala Thr Gly Ala Leu Ala Lys Ala Val Tyr 420 425 430 Glu Arg Met Phe Asn Trp Met Val Thr Arg Ile Asn Ala Thr Leu Glu 435 440 445 Thr Lys Gln Pro Arg Gln Tyr Phe Ile Gly Val Leu Asp Ile Ala Gly 450 455 460 Phe Glu Ile Phe Asp Phe Asn Ser Phe Glu Gln Leu Cys Ile Asn Phe 465 470 475 480 Thr Asn Glu Lys Leu Gln Gln Phe Phe Asn His His Met Phe Val Leu 485 490 495 Glu Gln Glu Glu Tyr Lys Lys Glu Gly Ile Glu Trp Thr Phe Ile Asp 500 505 510 Phe Gly Met Asp Leu Gln Ala Cys Ile Asp Leu Ile Glu Lys Pro Met 515 520 525 Gly Ile Met Ser Ile Leu Glu Glu Glu Cys Met Phe Pro Lys Ala Thr 530 535 540 Asp Met Thr Phe Lys Ala Lys Leu Phe Asp Asn His Leu Gly Lys Ser 545 550 555 560 Ala Asn Phe Gln Lys Pro Arg Asn Ile Lys Gly Lys Pro Glu Ala His 565 570 575 Phe Ser Leu Ile His Tyr Ala Gly Ile Val Asp Tyr Asn Ile Ile Gly 580 585 590 Trp Leu Gln Lys Asn Lys Asp Pro Leu Asn Glu Thr Val Val Gly Leu 595 600 605 Tyr Gln Lys Ser Ser Leu Lys Leu Leu Ser Thr Leu Phe Ala Asn Tyr 610 615 620 Ala Gly Ala Asp Ala Pro Ile Glu Lys Gly Lys Gly Lys Ala Lys Lys 625 630 635 640 Gly Ser Ser Phe Gln Thr Val Ser Ala Leu His Arg Glu Asn Leu Asn 645 650 655 Lys Leu Met Thr Asn Leu Arg Ser Thr His Pro His Phe Val Arg Cys 660 665 670 Ile Ile Pro Asn Glu Thr Lys Ser Pro Gly Val Met Asp Asn Pro Leu 675 680 685 Val Met His Gln Leu Arg Cys Asn Gly Val Leu Glu Gly Ile Arg Ile 690 695 700 Cys Arg Lys Gly Phe Pro Asn Arg Ile Leu Tyr Gly Asp Phe Arg Gln 705 710 715 720 Arg Tyr Arg Ile Leu Asn Pro Ala Ala Ile Pro Glu Gly Gln Phe Ile 725 730 735 Asp Ser Arg Lys Gly Ala Glu Lys Leu Leu Ser Ser Leu Asp Ile Asp 740 745 750 His Asn Gln Tyr Lys Phe Gly His Thr Lys Val Phe Phe Lys Ala Gly 755 760 765 Leu Leu Gly Leu Leu Glu Glu Met Arg Asp Glu Arg Leu Ser Arg Ile 770 775 780 Ile Thr Arg Ile Gln Ala Gln Ser Arg Gly Val Leu Ala Arg Met Glu 785 790 795 800 Tyr Lys Lys Leu Leu Glu Arg Arg Asp Ser Leu Leu Val Ile Gln Trp 805 810 815 Asn Ile Arg Ala Phe Met Gly Val Lys Asn Trp Pro Trp Met Lys Leu 820 825 830 Tyr Phe Lys Ile Lys Pro Leu Leu Lys Ser Ala Glu Arg Glu Lys Glu 835 840 845 Met Ala Ser Met Lys Glu Glu Phe Thr Arg Leu Lys Glu Ala Leu Glu 850 855 860 Lys Ser Glu Ala Arg Arg Lys Glu Leu Glu Glu Lys Met Val Ser Leu 865 870 875 880 Leu Gln Glu Lys Asn Asp Leu Gln Leu Gln Val Gln Ala Glu Gln Asp 885 890 895 Asn Leu Ala Asp Ala Glu Glu Arg Cys Asp Gln Leu Ile Lys Asn Lys 900 905 910 Ile Gln Leu Glu Ala Lys Val Lys Glu Met Asn Glu Arg Leu Glu Asp 915 920 925 Glu Glu Glu Met Asn Ala Glu Leu Thr Ala Lys Lys Arg Lys Leu Glu 930 935 940 Asp Glu Cys Ser Glu Leu Lys Arg Asp Ile Asp Asp Leu Glu Leu Thr 945 950 955 960 Leu Ala Lys Val Glu Lys Glu Lys His Ala Thr Glu Asn Lys Val Lys 965 970 975 Asn Leu Thr Glu Glu Met Ala Gly Leu Asp Glu Ile Ile Ala Lys Leu 980 985 990 Thr Lys Glu Lys Lys Ala Leu Gln Glu Ala His Gln Gln Ala Leu Asp 995 1000 1005 Asp Leu Gln Ala Glu Glu Asp Lys Val Asn Thr Leu Thr Lys Ala 1010 1015 1020 Lys Val Lys Leu Glu Gln Gln Val Asp Asp Leu Glu Gly Ser Leu 1025 1030 1035 Glu Gln Glu Lys Lys Val Arg Met Asp Leu Glu Arg Ala Lys Arg 1040 1045 1050 Lys Leu Glu Gly Asp Leu Lys Leu Thr Gln Glu Ser Ile Met Asp 1055 1060 1065 Leu Glu Asn Asp Lys Gln Gln Leu Asp Glu Arg Leu Lys Lys Lys 1070 1075 1080 Asp Phe Glu Leu Asn Ala Leu Asn Ala Arg Ile Glu Asp Glu Gln 1085 1090 1095 Ala Leu Gly Ser Gln Leu Gln Lys Lys Leu Lys Glu Leu Gln Ala 1100 1105 1110 Arg Ile Glu Glu Leu Glu Glu Glu Leu Glu Ala Glu Arg Thr Ala 1115 1120 1125 Arg Ala Lys Val Glu Lys Leu Arg Ser Asp Leu Ser Arg Glu Leu 1130 1135 1140 Glu Glu Ile Ser Glu Arg Leu Glu Glu Ala Gly Gly Ala Thr Ser 1145 1150 1155 Val Gln Ile Glu Met Asn Lys Lys Arg Glu Ala Glu Phe Gln Lys 1160 1165 1170 Met Arg Arg Asp Leu Glu Glu Ala Thr Leu Gln His Glu Ala Thr 1175 1180 1185 Ala Ala Ala Leu Arg Lys Lys His Ala Asp Ser Val Ala Glu Leu 1190 1195 1200 Gly Glu Gln Ile Asp Asn Leu Gln Arg Val Lys Gln Lys Leu Glu 1205 1210 1215 Lys Glu Lys Ser Glu Phe Lys Leu Glu Leu Asp Asp Val Thr Ser 1220 1225 1230 Asn Met Glu Gln Ile Ile Lys Ala Lys Ala Asn Leu Glu Lys Met 1235 1240 1245 Cys Arg Thr Leu Glu Asp Gln Met Asn Glu His Arg Ser Lys Ala 1250 1255 1260 Glu Glu Thr Gln Arg Ser Val Asn Asp Leu Thr Ser Gln Arg Ala 1265 1270 1275 Lys Leu Gln Thr Glu Asn Gly Glu Leu Ser Arg Gln Leu Asp Glu 1280 1285 1290 Lys Glu Ala Leu Ile Ser Gln Leu Thr Arg Gly Lys Leu Thr Tyr 1295 1300 1305 Thr Gln Gln Leu Glu Asp Leu Lys Arg Gln Leu Glu Glu Glu Val 1310 1315 1320

Lys Ala Lys Asn Ala Leu Ala His Ala Leu Gln Ser Ala Arg His 1325 1330 1335 Asp Cys Asp Leu Leu Arg Glu Gln Tyr Glu Glu Glu Thr Glu Ala 1340 1345 1350 Lys Ala Glu Leu Gln Arg Val Leu Ser Lys Ala Asn Ser Glu Val 1355 1360 1365 Ala Gln Trp Arg Thr Lys Tyr Glu Thr Asp Ala Ile Gln Arg Thr 1370 1375 1380 Glu Glu Leu Glu Glu Ala Lys Lys Lys Leu Ala Gln Arg Leu Gln 1385 1390 1395 Glu Ala Glu Glu Ala Val Glu Ala Val Asn Ala Lys Cys Ser Ser 1400 1405 1410 Leu Glu Lys Thr Lys His Arg Leu Gln Asn Glu Ile Glu Asp Leu 1415 1420 1425 Met Val Asp Val Glu Arg Ser Asn Ala Ala Ala Ala Ala Leu Asp 1430 1435 1440 Lys Lys Gln Arg Asn Phe Asp Lys Ile Leu Ala Glu Trp Lys Gln 1445 1450 1455 Lys Tyr Glu Glu Ser Gln Ser Glu Leu Glu Ser Ser Gln Lys Glu 1460 1465 1470 Ala Arg Ser Leu Ser Thr Glu Leu Phe Lys Leu Lys Asn Ala Tyr 1475 1480 1485 Glu Glu Ser Leu Glu His Leu Glu Thr Phe Lys Arg Glu Asn Lys 1490 1495 1500 Asn Leu Gln Glu Glu Ile Ser Asp Leu Thr Glu Gln Leu Gly Ser 1505 1510 1515 Ser Gly Lys Thr Ile His Glu Leu Glu Lys Val Arg Lys Gln Leu 1520 1525 1530 Glu Ala Glu Lys Met Glu Leu Gln Ser Ala Leu Glu Glu Ala Glu 1535 1540 1545 Ala Ser Leu Glu His Glu Glu Gly Lys Ile Leu Arg Ala Gln Leu 1550 1555 1560 Glu Phe Asn Gln Ile Lys Ala Glu Ile Glu Arg Lys Leu Ala Glu 1565 1570 1575 Lys Asp Glu Glu Met Glu Gln Ala Lys Arg Asn His Leu Arg Val 1580 1585 1590 Val Asp Ser Leu Gln Thr Ser Leu Asp Ala Glu Thr Arg Ser Arg 1595 1600 1605 Asn Glu Ala Leu Arg Val Lys Lys Lys Met Glu Gly Asp Leu Asn 1610 1615 1620 Glu Met Glu Ile Gln Leu Ser His Ala Asn Arg Met Ala Ala Glu 1625 1630 1635 Ala Gln Lys Gln Val Lys Ser Leu Gln Ser Leu Leu Lys Asp Thr 1640 1645 1650 Gln Ile Gln Leu Asp Asp Ala Val Arg Ala Asn Asp Asp Leu Lys 1655 1660 1665 Glu Asn Ile Ala Ile Val Glu Arg Arg Asn Asn Leu Leu Gln Ala 1670 1675 1680 Glu Leu Glu Glu Leu Arg Ala Val Val Glu Gln Thr Glu Arg Ser 1685 1690 1695 Arg Lys Leu Ala Glu Gln Glu Leu Ile Glu Thr Ser Glu Arg Val 1700 1705 1710 Gln Leu Leu His Ser Gln Asn Thr Ser Leu Ile Asn Gln Lys Lys 1715 1720 1725 Lys Met Asp Ala Asp Leu Ser Gln Leu Gln Thr Glu Val Glu Glu 1730 1735 1740 Ala Val Gln Glu Cys Arg Asn Ala Glu Glu Lys Ala Lys Lys Ala 1745 1750 1755 Ile Thr Asp Ala Ala Met Met Ala Glu Glu Leu Lys Lys Glu Gln 1760 1765 1770 Asp Thr Ser Ala His Leu Glu Arg Met Lys Lys Asn Met Glu Gln 1775 1780 1785 Thr Ile Lys Asp Leu Gln His Arg Leu Asp Glu Ala Glu Gln Ile 1790 1795 1800 Ala Leu Lys Gly Gly Lys Lys Gln Leu Gln Lys Leu Glu Ala Arg 1805 1810 1815 Val Arg Glu Leu Glu Asn Glu Leu Glu Ala Glu Gln Lys Arg Asn 1820 1825 1830 Ala Glu Ser Val Lys Gly Met Arg Lys Ser Glu Arg Arg Ile Lys 1835 1840 1845 Glu Leu Thr Tyr Gln Thr Glu Glu Asp Arg Lys Asn Leu Leu Arg 1850 1855 1860 Leu Gln Asp Leu Val Asp Lys Leu Gln Leu Lys Val Lys Ala Tyr 1865 1870 1875 Lys Arg Gln Ala Glu Glu Ala Glu Glu Gln Ala Asn Thr Asn Leu 1880 1885 1890 Ser Lys Phe Arg Lys Val Gln His Glu Leu Asp Glu Ala Glu Glu 1895 1900 1905 Arg Ala Asp Ile Ala Glu Ser Gln Val Asn Lys Leu Arg Ala Lys 1910 1915 1920 Ser Arg Asp Ile Gly Thr Lys Gly Leu Asn Glu Glu 1925 1930 1935 <210> SEQ ID NO 69 <211> LENGTH: 197 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P12829 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(197) <400> SEQUENCE: 69 Met Ala Pro Lys Lys Pro Glu Pro Lys Lys Glu Ala Ala Lys Pro Ala 1 5 10 15 Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Ala Pro Glu 20 25 30 Ala Pro Lys Glu Pro Ala Phe Asp Pro Lys Ser Val Lys Ile Asp Phe 35 40 45 Thr Ala Asp Gln Ile Glu Glu Phe Lys Glu Ala Phe Ser Leu Phe Asp 50 55 60 Arg Thr Pro Thr Gly Glu Met Lys Ile Thr Tyr Gly Gln Cys Gly Asp 65 70 75 80 Val Leu Arg Ala Leu Gly Gln Asn Pro Thr Asn Ala Glu Val Leu Arg 85 90 95 Val Leu Gly Lys Pro Lys Pro Glu Glu Met Asn Val Lys Met Leu Asp 100 105 110 Phe Glu Thr Phe Leu Pro Ile Leu Gln His Ile Ser Arg Asn Lys Glu 115 120 125 Gln Gly Thr Tyr Glu Asp Phe Val Glu Gly Leu Arg Val Phe Asp Lys 130 135 140 Glu Ser Asn Gly Thr Val Met Gly Ala Glu Leu Arg His Val Leu Ala 145 150 155 160 Thr Leu Gly Glu Lys Met Thr Glu Ala Glu Val Glu Gln Leu Leu Ala 165 170 175 Gly Gln Glu Asp Ala Asn Gly Cys Ile Asn Tyr Glu Ala Phe Val Lys 180 185 190 His Ile Met Ser Gly 195 <210> SEQ ID NO 70 <211> LENGTH: 810 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q06730 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(810) <400> SEQUENCE: 70 Met Asn Lys Val Glu Gln Lys Ser Gln Glu Ser Val Ser Phe Lys Asp 1 5 10 15 Val Thr Val Gly Phe Thr Gln Glu Glu Trp Gln His Leu Asp Pro Ser 20 25 30 Gln Arg Ala Leu Tyr Arg Asp Val Met Leu Glu Asn Tyr Ser Asn Leu 35 40 45 Val Ser Val Gly Tyr Cys Val His Lys Pro Glu Val Ile Phe Arg Leu 50 55 60 Gln Gln Gly Glu Glu Pro Trp Lys Gln Glu Glu Glu Phe Pro Ser Gln 65 70 75 80 Ser Phe Pro Val Trp Thr Ala Asp His Leu Lys Glu Arg Ser Gln Glu 85 90 95 Asn Gln Ser Lys His Leu Trp Glu Val Val Phe Ile Asn Asn Glu Met 100 105 110 Leu Thr Lys Glu Gln Gly Asp Val Ile Gly Ile Pro Phe Asn Val Asp 115 120 125 Val Ser Ser Phe Pro Ser Arg Lys Met Phe Cys Gln Cys Asp Ser Cys 130 135 140 Gly Met Ser Phe Asn Thr Val Ser Glu Leu Val Ile Ser Lys Ile Asn 145 150 155 160 Tyr Leu Gly Lys Lys Ser Asp Glu Phe Asn Ala Cys Gly Lys Leu Leu 165 170 175 Leu Asn Ile Lys His Asp Glu Thr His Thr Gln Glu Lys Asn Glu Val 180 185 190 Leu Lys Asn Arg Asn Thr Leu Ser His His Glu Glu Thr Leu Gln His 195 200 205 Glu Lys Ile Gln Thr Leu Glu His Asn Phe Glu Tyr Ser Ile Cys Gln 210 215 220 Glu Thr Leu Leu Glu Lys Ala Val Phe Asn Thr Gln Lys Arg Glu Asn 225 230 235 240 Ala Glu Glu Asn Asn Cys Asp Tyr Asn Glu Phe Gly Arg Thr Leu Cys 245 250 255 Asp Ser Ser Ser Leu Leu Phe His Gln Ile Ser Pro Ser Arg Asp Asn 260 265 270 His Tyr Glu Phe Ser Asp Cys Glu Lys Phe Leu Cys Val Lys Ser Thr 275 280 285 Leu Ser Lys Pro His Gly Val Ser Met Lys His Tyr Asp Cys Gly Glu 290 295 300 Ser Gly Asn Asn Phe Arg Arg Lys Leu Cys Leu Ser His Leu Gln Lys 305 310 315 320 Gly Asp Lys Gly Glu Lys His Phe Glu Cys Asn Glu Cys Gly Lys Ala 325 330 335 Phe Trp Glu Lys Ser His Leu Thr Arg His Gln Arg Val His Thr Gly

340 345 350 Gln Lys Pro Phe Gln Cys Asn Glu Cys Glu Lys Ala Phe Trp Asp Lys 355 360 365 Ser Asn Leu Thr Lys His Gln Arg Ser His Thr Gly Glu Lys Pro Phe 370 375 380 Glu Cys Asn Glu Cys Gly Lys Ala Phe Ser His Lys Ser Ala Leu Thr 385 390 395 400 Leu His Gln Arg Thr His Thr Gly Glu Lys Pro Tyr Gln Cys Asn Ala 405 410 415 Cys Gly Lys Thr Phe Cys Gln Lys Ser Asp Leu Thr Lys His Gln Arg 420 425 430 Thr His Thr Gly Leu Lys Pro Tyr Glu Cys Tyr Glu Cys Gly Lys Ser 435 440 445 Phe Arg Val Thr Ser His Leu Lys Val His Gln Arg Thr His Thr Gly 450 455 460 Glu Lys Pro Phe Glu Cys Leu Glu Cys Gly Lys Ser Phe Ser Glu Lys 465 470 475 480 Ser Asn Leu Thr Gln His Gln Arg Ile His Ile Gly Asp Lys Ser Tyr 485 490 495 Glu Cys Asn Ala Cys Gly Lys Thr Phe Tyr His Lys Ser Leu Leu Thr 500 505 510 Arg His Gln Ile Ile His Thr Gly Trp Lys Pro Tyr Glu Cys Tyr Glu 515 520 525 Cys Gly Lys Thr Phe Cys Leu Lys Ser Asp Leu Thr Val His Gln Arg 530 535 540 Thr His Thr Gly Gln Lys Pro Phe Ala Cys Pro Glu Cys Gly Lys Phe 545 550 555 560 Phe Ser His Lys Ser Thr Leu Ser Gln His Tyr Arg Thr His Thr Gly 565 570 575 Glu Lys Pro Tyr Glu Cys His Glu Cys Gly Lys Ile Phe Tyr Asn Lys 580 585 590 Ser Tyr Leu Thr Lys His Asn Arg Thr His Thr Gly Glu Lys Pro Tyr 595 600 605 Glu Cys Asn Glu Cys Gly Lys Ala Phe Tyr Gln Lys Ser Gln Leu Thr 610 615 620 Gln His Gln Arg Ile His Ile Gly Glu Lys Pro Tyr Lys Cys Asn Glu 625 630 635 640 Cys Gly Lys Ala Phe Cys His Lys Ser Ala Leu Ile Val His Gln Arg 645 650 655 Thr His Thr Gln Glu Lys Pro Tyr Lys Cys Asn Glu Cys Gly Lys Ser 660 665 670 Phe Cys Val Lys Ser Gly Leu Ile Phe His Glu Arg Lys His Thr Gly 675 680 685 Glu Lys Pro Tyr Glu Cys Asn Glu Cys Gly Lys Phe Phe Arg His Lys 690 695 700 Ser Ser Leu Thr Val His His Arg Ala His Thr Gly Glu Lys Ser Cys 705 710 715 720 Gln Cys Asn Glu Cys Gly Lys Ile Phe Tyr Arg Lys Ser Glu Leu Ala 725 730 735 Gln His Gln Arg Ser His Thr Gly Glu Lys Pro Tyr Glu Cys Asn Thr 740 745 750 Cys Arg Lys Thr Phe Ser Gln Lys Ser Asn Leu Ile Val His Gln Arg 755 760 765 Arg His Ile Gly Glu Asn Leu Met Asn Glu Met Asp Ile Arg Asn Phe 770 775 780 Gln Pro Gln Val Ser Leu His Asn Ala Ser Glu Tyr Ser His Cys Gly 785 790 795 800 Glu Ser Pro Asp Asp Ile Leu Asn Val Gln 805 810 <210> SEQ ID NO 71 <211> LENGTH: 369 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / Q8IWU4 <309> DATABASE ENTRY DATE: 2015-07-22 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(369) <400> SEQUENCE: 71 Met Glu Phe Leu Glu Arg Thr Tyr Leu Val Asn Asp Lys Ala Ala Lys 1 5 10 15 Met Tyr Ala Phe Thr Leu Glu Ser Val Glu Leu Gln Gln Lys Pro Val 20 25 30 Asn Lys Asp Gln Cys Pro Arg Glu Arg Pro Glu Glu Leu Glu Ser Gly 35 40 45 Gly Met Tyr His Cys His Ser Gly Ser Lys Pro Thr Glu Lys Gly Ala 50 55 60 Asn Glu Tyr Ala Tyr Ala Lys Trp Lys Leu Cys Ser Ala Ser Ala Ile 65 70 75 80 Cys Phe Ile Phe Met Ile Ala Glu Val Val Gly Gly His Ile Ala Gly 85 90 95 Ser Leu Ala Val Val Thr Asp Ala Ala His Leu Leu Ile Asp Leu Thr 100 105 110 Ser Phe Leu Leu Ser Leu Phe Ser Leu Trp Leu Ser Ser Lys Pro Pro 115 120 125 Ser Lys Arg Leu Thr Phe Gly Trp His Arg Ala Glu Ile Leu Gly Ala 130 135 140 Leu Leu Ser Ile Leu Cys Ile Trp Val Val Thr Gly Val Leu Val Tyr 145 150 155 160 Leu Ala Cys Glu Arg Leu Leu Tyr Pro Asp Tyr Gln Ile Gln Ala Thr 165 170 175 Val Met Ile Ile Val Ser Ser Cys Ala Val Ala Ala Asn Ile Val Leu 180 185 190 Thr Val Val Leu His Gln Arg Cys Leu Gly His Asn His Lys Glu Val 195 200 205 Gln Ala Asn Ala Ser Val Arg Ala Ala Phe Val His Ala Leu Gly Asp 210 215 220 Leu Phe Gln Ser Ile Ser Val Leu Ile Ser Ala Leu Ile Ile Tyr Phe 225 230 235 240 Lys Pro Glu Tyr Lys Ile Ala Asp Pro Ile Cys Thr Phe Ile Phe Ser 245 250 255 Ile Leu Val Leu Ala Ser Thr Ile Thr Ile Leu Lys Asp Phe Ser Ile 260 265 270 Leu Leu Met Glu Gly Val Pro Lys Ser Leu Asn Tyr Ser Gly Val Lys 275 280 285 Glu Leu Ile Leu Ala Val Asp Gly Val Leu Ser Val His Ser Leu His 290 295 300 Ile Trp Ser Leu Thr Met Asn Gln Val Ile Leu Ser Ala His Val Ala 305 310 315 320 Thr Ala Ala Ser Arg Asp Ser Gln Val Val Arg Arg Glu Ile Ala Lys 325 330 335 Ala Leu Ser Lys Ser Phe Thr Met His Ser Leu Thr Ile Gln Met Glu 340 345 350 Ser Pro Val Asp Gln Asp Pro Asp Cys Leu Phe Cys Glu Asp Pro Cys 355 360 365 Asp <210> SEQ ID NO 72 <211> LENGTH: 1231 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P08603 <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1231) <400> SEQUENCE: 72 Met Arg Leu Leu Ala Lys Ile Ile Cys Leu Met Leu Trp Ala Ile Cys 1 5 10 15 Val Ala Glu Asp Cys Asn Glu Leu Pro Pro Arg Arg Asn Thr Glu Ile 20 25 30 Leu Thr Gly Ser Trp Ser Asp Gln Thr Tyr Pro Glu Gly Thr Gln Ala 35 40 45 Ile Tyr Lys Cys Arg Pro Gly Tyr Arg Ser Leu Gly Asn Val Ile Met 50 55 60 Val Cys Arg Lys Gly Glu Trp Val Ala Leu Asn Pro Leu Arg Lys Cys 65 70 75 80 Gln Lys Arg Pro Cys Gly His Pro Gly Asp Thr Pro Phe Gly Thr Phe 85 90 95 Thr Leu Thr Gly Gly Asn Val Phe Glu Tyr Gly Val Lys Ala Val Tyr 100 105 110 Thr Cys Asn Glu Gly Tyr Gln Leu Leu Gly Glu Ile Asn Tyr Arg Glu 115 120 125 Cys Asp Thr Asp Gly Trp Thr Asn Asp Ile Pro Ile Cys Glu Val Val 130 135 140 Lys Cys Leu Pro Val Thr Ala Pro Glu Asn Gly Lys Ile Val Ser Ser 145 150 155 160 Ala Met Glu Pro Asp Arg Glu Tyr His Phe Gly Gln Ala Val Arg Phe 165 170 175 Val Cys Asn Ser Gly Tyr Lys Ile Glu Gly Asp Glu Glu Met His Cys 180 185 190 Ser Asp Asp Gly Phe Trp Ser Lys Glu Lys Pro Lys Cys Val Glu Ile 195 200 205 Ser Cys Lys Ser Pro Asp Val Ile Asn Gly Ser Pro Ile Ser Gln Lys 210 215 220 Ile Ile Tyr Lys Glu Asn Glu Arg Phe Gln Tyr Lys Cys Asn Met Gly 225 230 235 240 Tyr Glu Tyr Ser Glu Arg Gly Asp Ala Val Cys Thr Glu Ser Gly Trp 245 250 255 Arg Pro Leu Pro Ser Cys Glu Glu Lys Ser Cys Asp Asn Pro Tyr Ile 260 265 270 Pro Asn Gly Asp Tyr Ser Pro Leu Arg Ile Lys His Arg Thr Gly Asp 275 280 285 Glu Ile Thr Tyr Gln Cys Arg Asn Gly Phe Tyr Pro Ala Thr Arg Gly 290 295 300 Asn Thr Ala Lys Cys Thr Ser Thr Gly Trp Ile Pro Ala Pro Arg Cys 305 310 315 320 Thr Leu Lys Pro Cys Asp Tyr Pro Asp Ile Lys His Gly Gly Leu Tyr 325 330 335 His Glu Asn Met Arg Arg Pro Tyr Phe Pro Val Ala Val Gly Lys Tyr 340 345 350 Tyr Ser Tyr Tyr Cys Asp Glu His Phe Glu Thr Pro Ser Gly Ser Tyr

355 360 365 Trp Asp His Ile His Cys Thr Gln Asp Gly Trp Ser Pro Ala Val Pro 370 375 380 Cys Leu Arg Lys Cys Tyr Phe Pro Tyr Leu Glu Asn Gly Tyr Asn Gln 385 390 395 400 Asn Tyr Gly Arg Lys Phe Val Gln Gly Lys Ser Ile Asp Val Ala Cys 405 410 415 His Pro Gly Tyr Ala Leu Pro Lys Ala Gln Thr Thr Val Thr Cys Met 420 425 430 Glu Asn Gly Trp Ser Pro Thr Pro Arg Cys Ile Arg Val Lys Thr Cys 435 440 445 Ser Lys Ser Ser Ile Asp Ile Glu Asn Gly Phe Ile Ser Glu Ser Gln 450 455 460 Tyr Thr Tyr Ala Leu Lys Glu Lys Ala Lys Tyr Gln Cys Lys Leu Gly 465 470 475 480 Tyr Val Thr Ala Asp Gly Glu Thr Ser Gly Ser Ile Thr Cys Gly Lys 485 490 495 Asp Gly Trp Ser Ala Gln Pro Thr Cys Ile Lys Ser Cys Asp Ile Pro 500 505 510 Val Phe Met Asn Ala Arg Thr Lys Asn Asp Phe Thr Trp Phe Lys Leu 515 520 525 Asn Asp Thr Leu Asp Tyr Glu Cys His Asp Gly Tyr Glu Ser Asn Thr 530 535 540 Gly Ser Thr Thr Gly Ser Ile Val Cys Gly Tyr Asn Gly Trp Ser Asp 545 550 555 560 Leu Pro Ile Cys Tyr Glu Arg Glu Cys Glu Leu Pro Lys Ile Asp Val 565 570 575 His Leu Val Pro Asp Arg Lys Lys Asp Gln Tyr Lys Val Gly Glu Val 580 585 590 Leu Lys Phe Ser Cys Lys Pro Gly Phe Thr Ile Val Gly Pro Asn Ser 595 600 605 Val Gln Cys Tyr His Phe Gly Leu Ser Pro Asp Leu Pro Ile Cys Lys 610 615 620 Glu Gln Val Gln Ser Cys Gly Pro Pro Pro Glu Leu Leu Asn Gly Asn 625 630 635 640 Val Lys Glu Lys Thr Lys Glu Glu Tyr Gly His Ser Glu Val Val Glu 645 650 655 Tyr Tyr Cys Asn Pro Arg Phe Leu Met Lys Gly Pro Asn Lys Ile Gln 660 665 670 Cys Val Asp Gly Glu Trp Thr Thr Leu Pro Val Cys Ile Val Glu Glu 675 680 685 Ser Thr Cys Gly Asp Ile Pro Glu Leu Glu His Gly Trp Ala Gln Leu 690 695 700 Ser Ser Pro Pro Tyr Tyr Tyr Gly Asp Ser Val Glu Phe Asn Cys Ser 705 710 715 720 Glu Ser Phe Thr Met Ile Gly His Arg Ser Ile Thr Cys Ile His Gly 725 730 735 Val Trp Thr Gln Leu Pro Gln Cys Val Ala Ile Asp Lys Leu Lys Lys 740 745 750 Cys Lys Ser Ser Asn Leu Ile Ile Leu Glu Glu His Leu Lys Asn Lys 755 760 765 Lys Glu Phe Asp His Asn Ser Asn Ile Arg Tyr Arg Cys Arg Gly Lys 770 775 780 Glu Gly Trp Ile His Thr Val Cys Ile Asn Gly Arg Trp Asp Pro Glu 785 790 795 800 Val Asn Cys Ser Met Ala Gln Ile Gln Leu Cys Pro Pro Pro Pro Gln 805 810 815 Ile Pro Asn Ser His Asn Met Thr Thr Thr Leu Asn Tyr Arg Asp Gly 820 825 830 Glu Lys Val Ser Val Leu Cys Gln Glu Asn Tyr Leu Ile Gln Glu Gly 835 840 845 Glu Glu Ile Thr Cys Lys Asp Gly Arg Trp Gln Ser Ile Pro Leu Cys 850 855 860 Val Glu Lys Ile Pro Cys Ser Gln Pro Pro Gln Ile Glu His Gly Thr 865 870 875 880 Ile Asn Ser Ser Arg Ser Ser Gln Glu Ser Tyr Ala His Gly Thr Lys 885 890 895 Leu Ser Tyr Thr Cys Glu Gly Gly Phe Arg Ile Ser Glu Glu Asn Glu 900 905 910 Thr Thr Cys Tyr Met Gly Lys Trp Ser Ser Pro Pro Gln Cys Glu Gly 915 920 925 Leu Pro Cys Lys Ser Pro Pro Glu Ile Ser His Gly Val Val Ala His 930 935 940 Met Ser Asp Ser Tyr Gln Tyr Gly Glu Glu Val Thr Tyr Lys Cys Phe 945 950 955 960 Glu Gly Phe Gly Ile Asp Gly Pro Ala Ile Ala Lys Cys Leu Gly Glu 965 970 975 Lys Trp Ser His Pro Pro Ser Cys Ile Lys Thr Asp Cys Leu Ser Leu 980 985 990 Pro Ser Phe Glu Asn Ala Ile Pro Met Gly Glu Lys Lys Asp Val Tyr 995 1000 1005 Lys Ala Gly Glu Gln Val Thr Tyr Thr Cys Ala Thr Tyr Tyr Lys 1010 1015 1020 Met Asp Gly Ala Ser Asn Val Thr Cys Ile Asn Ser Arg Trp Thr 1025 1030 1035 Gly Arg Pro Thr Cys Arg Asp Thr Ser Cys Val Asn Pro Pro Thr 1040 1045 1050 Val Gln Asn Ala Tyr Ile Val Ser Arg Gln Met Ser Lys Tyr Pro 1055 1060 1065 Ser Gly Glu Arg Val Arg Tyr Gln Cys Arg Ser Pro Tyr Glu Met 1070 1075 1080 Phe Gly Asp Glu Glu Val Met Cys Leu Asn Gly Asn Trp Thr Glu 1085 1090 1095 Pro Pro Gln Cys Lys Asp Ser Thr Gly Lys Cys Gly Pro Pro Pro 1100 1105 1110 Pro Ile Asp Asn Gly Asp Ile Thr Ser Phe Pro Leu Ser Val Tyr 1115 1120 1125 Ala Pro Ala Ser Ser Val Glu Tyr Gln Cys Gln Asn Leu Tyr Gln 1130 1135 1140 Leu Glu Gly Asn Lys Arg Ile Thr Cys Arg Asn Gly Gln Trp Ser 1145 1150 1155 Glu Pro Pro Lys Cys Leu His Pro Cys Val Ile Ser Arg Glu Ile 1160 1165 1170 Met Glu Asn Tyr Asn Ile Ala Leu Arg Trp Thr Ala Lys Gln Lys 1175 1180 1185 Leu Tyr Ser Arg Thr Gly Glu Ser Val Glu Phe Val Cys Lys Arg 1190 1195 1200 Gly Tyr Arg Leu Ser Ser Arg Ser His Thr Leu Arg Thr Thr Cys 1205 1210 1215 Trp Asp Gly Lys Leu Glu Tyr Pro Thr Cys Ala Lys Arg 1220 1225 1230 <210> SEQ ID NO 73 <211> LENGTH: 1663 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt / P01024 <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1663) <400> SEQUENCE: 73 Met Gly Pro Thr Ser Gly Pro Ser Leu Leu Leu Leu Leu Leu Thr His 1 5 10 15 Leu Pro Leu Ala Leu Gly Ser Pro Met Tyr Ser Ile Ile Thr Pro Asn 20 25 30 Ile Leu Arg Leu Glu Ser Glu Glu Thr Met Val Leu Glu Ala His Asp 35 40 45 Ala Gln Gly Asp Val Pro Val Thr Val Thr Val His Asp Phe Pro Gly 50 55 60 Lys Lys Leu Val Leu Ser Ser Glu Lys Thr Val Leu Thr Pro Ala Thr 65 70 75 80 Asn His Met Gly Asn Val Thr Phe Thr Ile Pro Ala Asn Arg Glu Phe 85 90 95 Lys Ser Glu Lys Gly Arg Asn Lys Phe Val Thr Val Gln Ala Thr Phe 100 105 110 Gly Thr Gln Val Val Glu Lys Val Val Leu Val Ser Leu Gln Ser Gly 115 120 125 Tyr Leu Phe Ile Gln Thr Asp Lys Thr Ile Tyr Thr Pro Gly Ser Thr 130 135 140 Val Leu Tyr Arg Ile Phe Thr Val Asn His Lys Leu Leu Pro Val Gly 145 150 155 160 Arg Thr Val Met Val Asn Ile Glu Asn Pro Glu Gly Ile Pro Val Lys 165 170 175 Gln Asp Ser Leu Ser Ser Gln Asn Gln Leu Gly Val Leu Pro Leu Ser 180 185 190 Trp Asp Ile Pro Glu Leu Val Asn Met Gly Gln Trp Lys Ile Arg Ala 195 200 205 Tyr Tyr Glu Asn Ser Pro Gln Gln Val Phe Ser Thr Glu Phe Glu Val 210 215 220 Lys Glu Tyr Val Leu Pro Ser Phe Glu Val Ile Val Glu Pro Thr Glu 225 230 235 240 Lys Phe Tyr Tyr Ile Tyr Asn Glu Lys Gly Leu Glu Val Thr Ile Thr 245 250 255 Ala Arg Phe Leu Tyr Gly Lys Lys Val Glu Gly Thr Ala Phe Val Ile 260 265 270 Phe Gly Ile Gln Asp Gly Glu Gln Arg Ile Ser Leu Pro Glu Ser Leu 275 280 285 Lys Arg Ile Pro Ile Glu Asp Gly Ser Gly Glu Val Val Leu Ser Arg 290 295 300 Lys Val Leu Leu Asp Gly Val Gln Asn Pro Arg Ala Glu Asp Leu Val 305 310 315 320 Gly Lys Ser Leu Tyr Val Ser Ala Thr Val Ile Leu His Ser Gly Ser 325 330 335 Asp Met Val Gln Ala Glu Arg Ser Gly Ile Pro Ile Val Thr Ser Pro 340 345 350 Tyr Gln Ile His Phe Thr Lys Thr Pro Lys Tyr Phe Lys Pro Gly Met 355 360 365 Pro Phe Asp Leu Met Val Phe Val Thr Asn Pro Asp Gly Ser Pro Ala 370 375 380

Tyr Arg Val Pro Val Ala Val Gln Gly Glu Asp Thr Val Gln Ser Leu 385 390 395 400 Thr Gln Gly Asp Gly Val Ala Lys Leu Ser Ile Asn Thr His Pro Ser 405 410 415 Gln Lys Pro Leu Ser Ile Thr Val Arg Thr Lys Lys Gln Glu Leu Ser 420 425 430 Glu Ala Glu Gln Ala Thr Arg Thr Met Gln Ala Leu Pro Tyr Ser Thr 435 440 445 Val Gly Asn Ser Asn Asn Tyr Leu His Leu Ser Val Leu Arg Thr Glu 450 455 460 Leu Arg Pro Gly Glu Thr Leu Asn Val Asn Phe Leu Leu Arg Met Asp 465 470 475 480 Arg Ala His Glu Ala Lys Ile Arg Tyr Tyr Thr Tyr Leu Ile Met Asn 485 490 495 Lys Gly Arg Leu Leu Lys Ala Gly Arg Gln Val Arg Glu Pro Gly Gln 500 505 510 Asp Leu Val Val Leu Pro Leu Ser Ile Thr Thr Asp Phe Ile Pro Ser 515 520 525 Phe Arg Leu Val Ala Tyr Tyr Thr Leu Ile Gly Ala Ser Gly Gln Arg 530 535 540 Glu Val Val Ala Asp Ser Val Trp Val Asp Val Lys Asp Ser Cys Val 545 550 555 560 Gly Ser Leu Val Val Lys Ser Gly Gln Ser Glu Asp Arg Gln Pro Val 565 570 575 Pro Gly Gln Gln Met Thr Leu Lys Ile Glu Gly Asp His Gly Ala Arg 580 585 590 Val Val Leu Val Ala Val Asp Lys Gly Val Phe Val Leu Asn Lys Lys 595 600 605 Asn Lys Leu Thr Gln Ser Lys Ile Trp Asp Val Val Glu Lys Ala Asp 610 615 620 Ile Gly Cys Thr Pro Gly Ser Gly Lys Asp Tyr Ala Gly Val Phe Ser 625 630 635 640 Asp Ala Gly Leu Thr Phe Thr Ser Ser Ser Gly Gln Gln Thr Ala Gln 645 650 655 Arg Ala Glu Leu Gln Cys Pro Gln Pro Ala Ala Arg Arg Arg Arg Ser 660 665 670 Val Gln Leu Thr Glu Lys Arg Met Asp Lys Val Gly Lys Tyr Pro Lys 675 680 685 Glu Leu Arg Lys Cys Cys Glu Asp Gly Met Arg Glu Asn Pro Met Arg 690 695 700 Phe Ser Cys Gln Arg Arg Thr Arg Phe Ile Ser Leu Gly Glu Ala Cys 705 710 715 720 Lys Lys Val Phe Leu Asp Cys Cys Asn Tyr Ile Thr Glu Leu Arg Arg 725 730 735 Gln His Ala Arg Ala Ser His Leu Gly Leu Ala Arg Ser Asn Leu Asp 740 745 750 Glu Asp Ile Ile Ala Glu Glu Asn Ile Val Ser Arg Ser Glu Phe Pro 755 760 765 Glu Ser Trp Leu Trp Asn Val Glu Asp Leu Lys Glu Pro Pro Lys Asn 770 775 780 Gly Ile Ser Thr Lys Leu Met Asn Ile Phe Leu Lys Asp Ser Ile Thr 785 790 795 800 Thr Trp Glu Ile Leu Ala Val Ser Met Ser Asp Lys Lys Gly Ile Cys 805 810 815 Val Ala Asp Pro Phe Glu Val Thr Val Met Gln Asp Phe Phe Ile Asp 820 825 830 Leu Arg Leu Pro Tyr Ser Val Val Arg Asn Glu Gln Val Glu Ile Arg 835 840 845 Ala Val Leu Tyr Asn Tyr Arg Gln Asn Gln Glu Leu Lys Val Arg Val 850 855 860 Glu Leu Leu His Asn Pro Ala Phe Cys Ser Leu Ala Thr Thr Lys Arg 865 870 875 880 Arg His Gln Gln Thr Val Thr Ile Pro Pro Lys Ser Ser Leu Ser Val 885 890 895 Pro Tyr Val Ile Val Pro Leu Lys Thr Gly Leu Gln Glu Val Glu Val 900 905 910 Lys Ala Ala Val Tyr His His Phe Ile Ser Asp Gly Val Arg Lys Ser 915 920 925 Leu Lys Val Val Pro Glu Gly Ile Arg Met Asn Lys Thr Val Ala Val 930 935 940 Arg Thr Leu Asp Pro Glu Arg Leu Gly Arg Glu Gly Val Gln Lys Glu 945 950 955 960 Asp Ile Pro Pro Ala Asp Leu Ser Asp Gln Val Pro Asp Thr Glu Ser 965 970 975 Glu Thr Arg Ile Leu Leu Gln Gly Thr Pro Val Ala Gln Met Thr Glu 980 985 990 Asp Ala Val Asp Ala Glu Arg Leu Lys His Leu Ile Val Thr Pro Ser 995 1000 1005 Gly Cys Gly Glu Gln Asn Met Ile Gly Met Thr Pro Thr Val Ile 1010 1015 1020 Ala Val His Tyr Leu Asp Glu Thr Glu Gln Trp Glu Lys Phe Gly 1025 1030 1035 Leu Glu Lys Arg Gln Gly Ala Leu Glu Leu Ile Lys Lys Gly Tyr 1040 1045 1050 Thr Gln Gln Leu Ala Phe Arg Gln Pro Ser Ser Ala Phe Ala Ala 1055 1060 1065 Phe Val Lys Arg Ala Pro Ser Thr Trp Leu Thr Ala Tyr Val Val 1070 1075 1080 Lys Val Phe Ser Leu Ala Val Asn Leu Ile Ala Ile Asp Ser Gln 1085 1090 1095 Val Leu Cys Gly Ala Val Lys Trp Leu Ile Leu Glu Lys Gln Lys 1100 1105 1110 Pro Asp Gly Val Phe Gln Glu Asp Ala Pro Val Ile His Gln Glu 1115 1120 1125 Met Ile Gly Gly Leu Arg Asn Asn Asn Glu Lys Asp Met Ala Leu 1130 1135 1140 Thr Ala Phe Val Leu Ile Ser Leu Gln Glu Ala Lys Asp Ile Cys 1145 1150 1155 Glu Glu Gln Val Asn Ser Leu Pro Gly Ser Ile Thr Lys Ala Gly 1160 1165 1170 Asp Phe Leu Glu Ala Asn Tyr Met Asn Leu Gln Arg Ser Tyr Thr 1175 1180 1185 Val Ala Ile Ala Gly Tyr Ala Leu Ala Gln Met Gly Arg Leu Lys 1190 1195 1200 Gly Pro Leu Leu Asn Lys Phe Leu Thr Thr Ala Lys Asp Lys Asn 1205 1210 1215 Arg Trp Glu Asp Pro Gly Lys Gln Leu Tyr Asn Val Glu Ala Thr 1220 1225 1230 Ser Tyr Ala Leu Leu Ala Leu Leu Gln Leu Lys Asp Phe Asp Phe 1235 1240 1245 Val Pro Pro Val Val Arg Trp Leu Asn Glu Gln Arg Tyr Tyr Gly 1250 1255 1260 Gly Gly Tyr Gly Ser Thr Gln Ala Thr Phe Met Val Phe Gln Ala 1265 1270 1275 Leu Ala Gln Tyr Gln Lys Asp Ala Pro Asp His Gln Glu Leu Asn 1280 1285 1290 Leu Asp Val Ser Leu Gln Leu Pro Ser Arg Ser Ser Lys Ile Thr 1295 1300 1305 His Arg Ile His Trp Glu Ser Ala Ser Leu Leu Arg Ser Glu Glu 1310 1315 1320 Thr Lys Glu Asn Glu Gly Phe Thr Val Thr Ala Glu Gly Lys Gly 1325 1330 1335 Gln Gly Thr Leu Ser Val Val Thr Met Tyr His Ala Lys Ala Lys 1340 1345 1350 Asp Gln Leu Thr Cys Asn Lys Phe Asp Leu Lys Val Thr Ile Lys 1355 1360 1365 Pro Ala Pro Glu Thr Glu Lys Arg Pro Gln Asp Ala Lys Asn Thr 1370 1375 1380 Met Ile Leu Glu Ile Cys Thr Arg Tyr Arg Gly Asp Gln Asp Ala 1385 1390 1395 Thr Met Ser Ile Leu Asp Ile Ser Met Met Thr Gly Phe Ala Pro 1400 1405 1410 Asp Thr Asp Asp Leu Lys Gln Leu Ala Asn Gly Val Asp Arg Tyr 1415 1420 1425 Ile Ser Lys Tyr Glu Leu Asp Lys Ala Phe Ser Asp Arg Asn Thr 1430 1435 1440 Leu Ile Ile Tyr Leu Asp Lys Val Ser His Ser Glu Asp Asp Cys 1445 1450 1455 Leu Ala Phe Lys Val His Gln Tyr Phe Asn Val Glu Leu Ile Gln 1460 1465 1470 Pro Gly Ala Val Lys Val Tyr Ala Tyr Tyr Asn Leu Glu Glu Ser 1475 1480 1485 Cys Thr Arg Phe Tyr His Pro Glu Lys Glu Asp Gly Lys Leu Asn 1490 1495 1500 Lys Leu Cys Arg Asp Glu Leu Cys Arg Cys Ala Glu Glu Asn Cys 1505 1510 1515 Phe Ile Gln Lys Ser Asp Asp Lys Val Thr Leu Glu Glu Arg Leu 1520 1525 1530 Asp Lys Ala Cys Glu Pro Gly Val Asp Tyr Val Tyr Lys Thr Arg 1535 1540 1545 Leu Val Lys Val Gln Leu Ser Asn Asp Phe Asp Glu Tyr Ile Met 1550 1555 1560 Ala Ile Glu Gln Thr Ile Lys Ser Gly Ser Asp Glu Val Gln Val 1565 1570 1575 Gly Gln Gln Arg Thr Phe Ile Ser Pro Ile Lys Cys Arg Glu Ala 1580 1585 1590 Leu Lys Leu Glu Glu Lys Lys His Tyr Leu Met Trp Gly Leu Ser 1595 1600 1605 Ser Asp Phe Trp Gly Glu Lys Pro Asn Leu Ser Tyr Ile Ile Gly 1610 1615 1620 Lys Asp Thr Trp Val Glu His Trp Pro Glu Glu Asp Glu Cys Gln 1625 1630 1635 Asp Glu Glu Asn Gln Lys Gln Cys Gln Asp Leu Gly Ala Phe Thr 1640 1645 1650 Glu Ser Met Val Val Phe Gly Cys Pro Asn 1655 1660 <210> SEQ ID NO 74

<211> LENGTH: 1463 <212> TYPE: PRT <213> ORGANISM: Homo sapiens <300> PUBLICATION INFORMATION: <308> DATABASE ACCESSION NUMBER: UniProt <309> DATABASE ENTRY DATE: 2015-09-16 <313> RELEVANT RESIDUES IN SEQ ID NO: (1)..(1463) <400> SEQUENCE: 74 Met Leu Leu Ser Pro Ser Leu Leu Leu Leu Leu Leu Leu Gly Ala Pro 1 5 10 15 Arg Gly Cys Ala Glu Gly Val Ala Ala Ala Leu Thr Pro Glu Arg Leu 20 25 30 Leu Glu Trp Gln Asp Lys Gly Ile Phe Val Ile Gln Ser Glu Ser Leu 35 40 45 Lys Lys Cys Ile Gln Ala Gly Lys Ser Val Leu Thr Leu Glu Asn Cys 50 55 60 Lys Gln Ala Asn Lys His Met Leu Trp Lys Trp Val Ser Asn His Gly 65 70 75 80 Leu Phe Asn Ile Gly Gly Ser Gly Cys Leu Gly Leu Asn Phe Ser Ala 85 90 95 Pro Glu Gln Pro Leu Ser Leu Tyr Glu Cys Asp Ser Thr Leu Val Ser 100 105 110 Leu Arg Trp Arg Cys Asn Arg Lys Met Ile Thr Gly Pro Leu Gln Tyr 115 120 125 Ser Val Gln Val Ala His Asp Asn Thr Val Val Ala Ser Arg Lys Tyr 130 135 140 Ile His Lys Trp Ile Ser Tyr Gly Ser Gly Gly Gly Asp Ile Cys Glu 145 150 155 160 Tyr Leu His Lys Asp Leu His Thr Ile Lys Gly Asn Thr His Gly Met 165 170 175 Pro Cys Met Phe Pro Phe Gln Tyr Asn His Gln Trp His His Glu Cys 180 185 190 Thr Arg Glu Gly Arg Glu Asp Asp Leu Leu Trp Cys Ala Thr Thr Ser 195 200 205 Arg Tyr Glu Arg Asp Glu Lys Trp Gly Phe Cys Pro Asp Pro Thr Ser 210 215 220 Ala Glu Val Gly Cys Asp Thr Ile Trp Glu Lys Asp Leu Asn Ser His 225 230 235 240 Ile Cys Tyr Gln Phe Asn Leu Leu Ser Ser Leu Ser Trp Ser Glu Ala 245 250 255 His Ser Ser Cys Gln Met Gln Gly Gly Thr Leu Leu Ser Ile Thr Asp 260 265 270 Glu Thr Glu Glu Asn Phe Ile Arg Glu His Met Ser Ser Lys Thr Val 275 280 285 Glu Val Trp Met Gly Leu Asn Gln Leu Asp Glu His Ala Gly Trp Gln 290 295 300 Trp Ser Asp Gly Thr Pro Leu Asn Tyr Leu Asn Trp Ser Pro Glu Val 305 310 315 320 Asn Phe Glu Pro Phe Val Glu Asp His Cys Gly Thr Phe Ser Ser Phe 325 330 335 Met Pro Ser Ala Trp Arg Ser Arg Asp Cys Glu Ser Thr Leu Pro Tyr 340 345 350 Ile Cys Lys Lys Tyr Leu Asn His Ile Asp His Glu Ile Val Glu Lys 355 360 365 Asp Ala Trp Lys Tyr Tyr Ala Thr His Cys Glu Pro Gly Trp Asn Pro 370 375 380 Tyr Asn Arg Asn Cys Tyr Lys Leu Gln Lys Glu Glu Lys Thr Trp His 385 390 395 400 Glu Ala Leu Arg Ser Cys Gln Ala Asp Asn Ser Ala Leu Ile Asp Ile 405 410 415 Thr Ser Leu Ala Glu Val Glu Phe Leu Val Thr Leu Leu Gly Asp Glu 420 425 430 Asn Ala Ser Glu Thr Trp Ile Gly Leu Ser Ser Asn Lys Ile Pro Val 435 440 445 Ser Phe Glu Trp Ser Asn Asp Ser Ser Val Ile Phe Thr Asn Trp His 450 455 460 Thr Leu Glu Pro His Ile Phe Pro Asn Arg Ser Gln Leu Cys Val Ser 465 470 475 480 Ala Glu Gln Ser Glu Gly His Trp Lys Val Lys Asn Cys Glu Glu Arg 485 490 495 Leu Phe Tyr Ile Cys Lys Lys Ala Gly His Val Leu Ser Asp Ala Glu 500 505 510 Ser Gly Cys Gln Glu Gly Trp Glu Arg His Gly Gly Phe Cys Tyr Lys 515 520 525 Ile Asp Thr Val Leu Arg Ser Phe Asp Gln Ala Ser Ser Gly Tyr Tyr 530 535 540 Cys Pro Pro Ala Leu Val Thr Ile Thr Asn Arg Phe Glu Gln Ala Phe 545 550 555 560 Ile Thr Ser Leu Ile Ser Ser Val Val Lys Met Lys Asp Ser Tyr Phe 565 570 575 Trp Ile Ala Leu Gln Asp Gln Asn Asp Thr Gly Glu Tyr Thr Trp Lys 580 585 590 Pro Val Gly Gln Lys Pro Glu Pro Val Gln Tyr Thr His Trp Asn Thr 595 600 605 His Gln Pro Arg Tyr Ser Gly Gly Cys Val Ala Met Arg Gly Arg His 610 615 620 Pro Leu Gly Arg Trp Glu Val Lys His Cys Arg His Phe Lys Ala Met 625 630 635 640 Ser Leu Cys Lys Gln Pro Val Glu Asn Gln Glu Lys Ala Glu Tyr Glu 645 650 655 Glu Arg Trp Pro Phe His Pro Cys Tyr Leu Asp Trp Glu Ser Glu Pro 660 665 670 Gly Leu Ala Ser Cys Phe Lys Val Phe His Ser Glu Lys Val Leu Met 675 680 685 Lys Arg Thr Trp Arg Glu Ala Glu Ala Phe Cys Glu Glu Phe Gly Ala 690 695 700 His Leu Ala Ser Phe Ala His Ile Glu Glu Glu Asn Phe Val Asn Glu 705 710 715 720 Leu Leu His Ser Lys Phe Asn Trp Thr Glu Glu Arg Gln Phe Trp Ile 725 730 735 Gly Phe Asn Lys Arg Asn Pro Leu Asn Ala Gly Ser Trp Glu Trp Ser 740 745 750 Asp Arg Thr Pro Val Val Ser Ser Phe Leu Asp Asn Thr Tyr Phe Gly 755 760 765 Glu Asp Ala Arg Asn Cys Ala Val Tyr Lys Ala Asn Lys Thr Leu Leu 770 775 780 Pro Leu His Cys Gly Ser Lys Arg Glu Trp Ile Cys Lys Ile Pro Arg 785 790 795 800 Asp Val Lys Pro Lys Ile Pro Phe Trp Tyr Gln Tyr Asp Val Pro Trp 805 810 815 Leu Phe Tyr Gln Asp Ala Glu Tyr Leu Phe His Thr Phe Ala Ser Glu 820 825 830 Trp Leu Asn Phe Glu Phe Val Cys Ser Trp Leu His Ser Asp Leu Leu 835 840 845 Thr Ile His Ser Ala His Glu Gln Glu Phe Ile His Ser Lys Ile Lys 850 855 860 Ala Leu Ser Lys Tyr Gly Ala Ser Trp Trp Ile Gly Leu Gln Glu Glu 865 870 875 880 Arg Ala Asn Asp Glu Phe Arg Trp Arg Asp Gly Thr Pro Val Ile Tyr 885 890 895 Gln Asn Trp Asp Thr Gly Arg Glu Arg Thr Val Asn Asn Gln Ser Gln 900 905 910 Arg Cys Gly Phe Ile Ser Ser Ile Thr Gly Leu Trp Gly Ser Glu Glu 915 920 925 Cys Ser Val Ser Met Pro Ser Ile Cys Lys Arg Lys Lys Val Trp Leu 930 935 940 Ile Glu Lys Lys Lys Asp Thr Pro Lys Gln His Gly Thr Cys Pro Lys 945 950 955 960 Gly Trp Leu Tyr Phe Asn Tyr Lys Cys Leu Leu Leu Asn Ile Pro Lys 965 970 975 Asp Pro Ser Ser Trp Lys Asn Trp Thr His Ala Gln His Phe Cys Ala 980 985 990 Glu Glu Gly Gly Thr Leu Val Ala Ile Glu Ser Glu Val Glu Gln Ala 995 1000 1005 Phe Ile Thr Met Asn Leu Phe Gly Gln Thr Thr Ser Val Trp Ile 1010 1015 1020 Gly Leu Gln Asn Asp Asp Tyr Glu Thr Trp Leu Asn Gly Lys Pro 1025 1030 1035 Val Val Tyr Ser Asn Trp Ser Pro Phe Asp Ile Ile Asn Ile Pro 1040 1045 1050 Ser His Asn Thr Thr Glu Val Gln Lys His Ile Pro Leu Cys Ala 1055 1060 1065 Leu Leu Ser Ser Asn Pro Asn Phe His Phe Thr Gly Lys Trp Tyr 1070 1075 1080 Phe Glu Asp Cys Gly Lys Glu Gly Tyr Gly Phe Val Cys Glu Lys 1085 1090 1095 Met Gln Asp Thr Ser Gly His Gly Val Asn Thr Ser Asp Met Tyr 1100 1105 1110 Pro Met Pro Asn Thr Leu Glu Tyr Gly Asn Arg Thr Tyr Lys Ile 1115 1120 1125 Ile Asn Ala Asn Met Thr Trp Tyr Ala Ala Ile Lys Thr Cys Leu 1130 1135 1140 Met His Lys Ala Gln Leu Val Ser Ile Thr Asp Gln Tyr His Gln 1145 1150 1155 Ser Phe Leu Thr Val Val Leu Asn Arg Leu Gly Tyr Ala His Trp 1160 1165 1170 Ile Gly Leu Phe Thr Thr Asp Asn Gly Leu Asn Phe Asp Trp Ser 1175 1180 1185 Asp Gly Thr Lys Ser Ser Phe Thr Phe Trp Lys Asp Glu Glu Ser 1190 1195 1200 Ser Leu Leu Gly Asp Cys Val Phe Ala Asp Ser Asn Gly Arg Trp 1205 1210 1215 His Ser Thr Ala Cys Glu Ser Phe Leu Gln Gly Ala Ile Cys His 1220 1225 1230 Val Pro Pro Glu Thr Arg Gln Ser Glu His Pro Glu Leu Cys Ser 1235 1240 1245 Glu Thr Ser Ile Pro Trp Ile Lys Phe Lys Ser Asn Cys Tyr Ser 1250 1255 1260 Phe Ser Thr Val Leu Asp Ser Met Ser Phe Glu Ala Ala His Glu

1265 1270 1275 Phe Cys Lys Lys Glu Gly Ser Asn Leu Leu Thr Ile Lys Asp Glu 1280 1285 1290 Ala Glu Asn Ala Phe Leu Leu Glu Glu Leu Phe Ala Phe Gly Ser 1295 1300 1305 Ser Val Gln Met Val Trp Leu Asn Ala Gln Phe Asp Gly Asn Asn 1310 1315 1320 Glu Thr Ile Lys Trp Phe Asp Gly Thr Pro Thr Asp Gln Ser Asn 1325 1330 1335 Trp Gly Ile Arg Lys Pro Asp Thr Asp Tyr Phe Lys Pro His His 1340 1345 1350 Cys Val Ala Leu Arg Ile Pro Glu Gly Leu Trp Gln Leu Ser Pro 1355 1360 1365 Cys Gln Glu Lys Lys Gly Phe Ile Cys Lys Met Glu Ala Asp Ile 1370 1375 1380 His Thr Ala Glu Ala Leu Pro Glu Lys Gly Pro Ser His Ser Ile 1385 1390 1395 Ile Pro Leu Ala Val Val Leu Thr Leu Ile Val Ile Val Ala Ile 1400 1405 1410 Cys Thr Leu Ser Phe Cys Ile Tyr Lys His Asn Gly Gly Phe Phe 1415 1420 1425 Arg Arg Leu Ala Gly Phe Arg Asn Pro Tyr Tyr Pro Ala Thr Asn 1430 1435 1440 Phe Ser Thr Val Tyr Leu Glu Glu Asn Ile Leu Ile Ser Asp Leu 1445 1450 1455 Glu Lys Ser Asp Gln 1460

Claims

1. A composition comprising a first collection of solid-phase substrates each coated with a different purified human leukocytes antigen (HLA) to represent the HLA antigen population of a single cell line and a second collection of solid-phase substrates each coated with at a different non-HLA antigen listed in Table 1 or Table 1A.

2. The composition of claim 1 wherein the different purified HLA antigens are Class I HLA antigens or Class II HLA antigens.

3. (canceled)

4. The composition of claim 1, wherein the non-HLA antigen is a fusion protein comprising at least one domain, wherein the domain is a signal peptide, a modified cytoplasmic domain, purification tag or detection tag.

5. The composition of claim 4 wherein the domain is the B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag.

6-10. (canceled)

11. The composition of claim 1, wherein each solid phase substrates is detectably distinguishable the other solid-phase substrates within the composition.

12. (canceled)

13. A kit for determining the percentage of panel reactive antibodies in serum of a subject against HLA antigens comprising a first collection of solid-phase substrates wherein each solid-phase substrate is coated with different purified HLA antigens to represent the HLA antigen population of a single cell line such that said collection simulates the distribution of HLA antigens in a normal human population and a second collection of solid phase substrates wherein each substrate is coated with different purified non-HLA antigens listed in Table 1 or Table 1A.

14. (canceled)

15. The kit of claim 13 wherein the HLA antigens are selected such that the HLA antigens presented on the solid phase substrate comprise Class I HLA antigens so as to simulate the distribution of Class I HLA antigens in a normal human population.

16. (canceled)

17. The kit of claim 13 wherein the first collection comprises 54 different Class I HLA antigens.

18. The kit of claim 17 wherein the 54 different Class I HLA antigens are purified from 30 different cell lines.

19. The kit of claim 13 wherein the first collection comprises 22 different Class II HLA antigens.

20. The kit of claim 13 wherein the non-HLA antigen is a fusion protein comprising at least one domain, wherein the domain is a signal peptide, a modified cytoplasmic domain, purification tag or detection tag.

21. The kit of claim 20 wherein the domain is the B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag.

22. (canceled)

23. (canceled)

24. The kit of claim 13, wherein at least one solid-phase substrate is detectably distinguishable from at least one other solid phase substrate.

25-29. (canceled)

30. The kit of claim 22 wherein said first collection comprises at least one 3 .mu.m microbead presenting Class I HLA antigens and at least one 5 .mu.m microbead presenting Class II HLA antigens.

31. A method for determining the percentage of panel reactive antibodies in serum of a subject against human leukocyte antigens (HLA) antigens, said method comprising: a. contacting a first collection of solid-phase substrates subtypes and a second collection of solid-phase substrate subtypes with serum from said subject for a sufficient time for anti-HLA antibodies in said serum to bind to said HLA-antigens to form a complex, wherein each substrate subtype in the first collection is coated with different purified HLA antigens to present HLA antigens derived from a cell population of a single cell, wherein each substrate subtype of the second collection is coated with different purified non-HLA antigens listed in Table 1 or Table 1A, b. detecting the presence of the complex to determine the presence or absence of panel reactive antibodies, and c. determining the percentage of panel reactive antibodies in the serum.

32. The method of claim 31 wherein the detecting step comprises detecting labeled ligand bound to the complex to determine the presence or absence of panel reactive antibodies.

33. (canceled)

34. The method of claim 31 wherein the detection step comprises detecting the presence of the complex using a solid phase immunoassay or a multiplexed bead immunoassay.

35-38. (canceled)

39. The method of claim 31, wherein the first collection of substrates is selected such that the HLA antigens presented thereon simulate distribution of Class I HLA antigens in a normal human population.

40. The method of claim 31, wherein said first collection of substrates comprises 54 different Class I HLA antigens.

41. The method of claim 31, wherein said first collection of substrates comprises 54 different Class I HLA antigens purified from 30 different cells.

42-43. (canceled)

44. The method of claim 31, wherein the non-HLA antigen is a fusion protein comprising at least one domain, wherein the domain is a signal peptide, a modified cytoplasmic domain, purification tag or detection tag.

45. The composition of claim 44, wherein the domain is the B2 signal peptide, HLA cytoplasmic domain, EK Tag, V5 Tag or DPD Tag.

46. The method of claim 31, wherein each solid-phase substrate is detectably distinguishable from the other solid phase substrates within a collection.

47-49. (canceled)

50. The method of claim 35, wherein said microbeads comprise a mixture of 3 .mu.m microbeads presenting Class I HLA antigens and 5 .mu.m microbeads presenting Class II HLA antigens.

51. The method of claim 31, wherein the subject is a transplant or transfusion recipient.

52. The method of claim 31, wherein the serum sample is collected before the subject has received a transplant or transfusion.

53. The method of claim 31, wherein the serum sample is collected after the subject has received a transplant or transfusion.

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