AU2009230789A1

AU2009230789A1 - Nucleic acid and corresponding protein entitled 98P4B6 useful in treatment and detection of cancer

Info

Publication number: AU2009230789A1
Application number: AU2009230789A
Authority: AU
Inventors: Pia M. Challita-Eid; Mary Faris; Wangmao Ge; Aya Jakobovits; Arthur B. Raitano
Original assignee: Agensys Inc
Current assignee: Agensys Inc
Priority date: 2002-04-05
Filing date: 2009-10-27
Publication date: 2009-11-19
Also published as: JP2005534287A; BR0308953A; WO2003087306A2; EP1572916A4; NZ535762A; EP1572916A2; MXPA04009728A; WO2003087306A8; CA2481503A1; AU2003223469A1

Description

AUSTRALIA FB RICE & CO Patent and Trade Mark Attorneys Patents Act 1990 AGENSYS, INC. COMPLETE SPECIFICATION STANDARD PATENT Invention Title: Nucleic acid and corresponding protein entitled 98P4B6 useful in treatment and detection of cancer The following statement is a full description of this invention including the best method of performing it known to us:

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NUCLEIC ACID AND CORRESPONDING PROTEIN ENTITLED 98P4B6 USEFUL IN TREATMENT AND DETECTION OF CANCER This is a divisional of AU 2003223469, the entire contents of which are 5 incorporated herein by reference. CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation-in-part of pending United States patent application USSN 09/455,486, filed 06-December-1999, and claims priority from 10 United States patent application USSN 09/323, 873, now United States patent number 6,329,503 filed 01-June-1999, and this application claims priority from United States provisional application USSN not yet assigned, filed 20-December-2002 and United States provisional patent application number 60/317,840, filed September 6, 2001 and United States provisional patent application number 60/370,387 filed April 5, 2002. 15 This application relates to United States provisional patent application number 60/087,520, filed June 1, 1998 and United States provisional patent application number 60/091,183, filed June 30, 1998 and United States Patent application number 10/011,095, filed December 6, 2001 and United States patent application number 10/010,667, filed December 6, 2001 and United States provisional patent application 20 number 60/296,656, filed June 6, 2001, and United States patent application number 10/165,044, filed June 6, 2002. The contents of the applications listed in this paragraph are fully incorporated by reference herein. STATEMENT OF RIGHTS TO INVENTIONS MADE UNDER 25 FEDERALLY SPONSORED RESEARCH Not applicable. FIELD OF THE INVENTION The invention described herein relates to genes and their encoded proteins, 30 termed 98P4B6 or STEAP-2, expressed in certain cancers, and to diagnostic and therapeutic methods and compositions useful in the management of cancers that express 98P4B6. BACKGROUND OF THE INVENTION 35 Cancer is the second leading cause of human death next to coronary disease. Worldwide, millions of people die from cancer every year. In the United States alone,

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as reported by the American Cancer Society, cancer causes the death of well over a half-million people annually, with over 1.2 million new cases diagnosed per year. While deaths from heart disease have been declining significantly, those resulting from cancer generally are on the rise. In the early part of the next century, cancer is 5 predicted to become the leading cause of death. Worldwide, several cancers stand out as the leading killers. In particular, carcinomas of the lung, prostate, breast, colon, pancreas, and ovary represent the primary causes of cancer death. These and virtually all other carcinomas share a common lethal feature. With very few exceptions, metastatic disease from a carcinoma 10 is fatal. Moreover, even for those cancer patients who initially survive their primary cancers, common experience has shown that their lives are dramatically altered. Many cancer patients experience strong anxieties driven by the awareness of the potential for recurrence or treatment failure. Many cancer patients experience physical debilitations following treatment. Furthermore, many cancer patients experience a recurrence. 15 Worldwide, prostate cancer is the fourth most prevalent cancer in men. In North America and Northern Europe, it is by far the most common cancer in males and is the second leading cause of cancer death in men. In the United States alone, well over 30,000 men die annually of this disease-second only to lung cancer. Despite the magnitude of these figures, there is still no effective treatment for metastatic prostate 20 cancer. Surgical prostatectomy, radiation therapy,

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hormone ablation therapy, surgical castration and chemotherapy continue to be the main treatment modalities. Unfortunately, these treatments are ineffective for many and are often associated with undesirable consequences. On the diagnostic front, the lack of a prostate tumor marker that can accurately detect early-stage, localized tumors remains a significant limitation in the diagnosis and management of this disease. Although the serum prostate specific antigen (PSA) assay has been a very useful tool, however its specificity and general utility is widely regarded as lacking in several important respects. -Progress in identifying additional specific markers for prostate cancer has been improved by the generation of prostate cancer xenografts that can recapitulate different stages of the disease in mice. The LAPC Los Angeles prostate Cancer) xenografts are prostate cancer xenografts that have survived passage in severe combined immune deficient (SCID) mice and have exhibited the capacity to mimic the transition from androgen dependence to androgen independence (Klein et aL, 1997, Nat Med. 3:402). More recently identified prostate cancer markers include PCTA-1 (Su ef al., 1996, Proc. NaI. Acad. Sci. USA 93: 7252), prostate-specific membrane (PSM) antigen (Pinto et al., Clin Cancer Res 1996 Sep 2 (9): 1445 51), STEAP (Hubert, et al., Proc Natl Acad Sci U S A 1999 Dec 7; 96(25): 14523-8) and prostate stem cell antigen (PSCA) (Reiter et aL., 1998, Proc. NaU. Acad. Sci. USA 95: 1735). While previously identified markers such as PSA, PSM, PCTA and PSCA have facilitated efforts to diagnose and treat prostate cancer, there is need for the identification of additional markers and therapeutic targets for prostate and related cancers in order to further improve diagnosis and therapy. Renal cell carcinoma (RCC) accounts for approximately 3 percent of adult malignancies. Once adenomas reach a diameter of 2 to 3 cm, malignant potential exists. In the adult, the two principal malignant renal tumors are renal cell adenocarcinoma and transitional cell carcinoma of the renal pelvis or ureter. The incidence of renal cell adenocarcinoma is estimated at more than 29,000 cases in the United States, and more than 11,600 patients died of this disease in 1998. Transitional cell carcinoma is less frequent, with an incidence of approximately 500 cases per year in the United States. Surgery has been the primary therapy for renal cell adenocarcinoma for many decades. Until recently, metastatic disease has been refractory to any systemic therapy. With recent developments in systemic therapies, particularly immunotherapies, metastatic renal cell carcinoma may be approached aggressively in appropriate patients with a possibility of durable responses. Nevertheless, there is a remaining need for effective therapies for these patients. Of all new cases of cancer in the United States, bladder cancer represents approximately 5 percent in men (fifth most common neoplasm) and 3 percent in women (eighth most common neoplasm). The incidence is increasing slowly, concurrent with an increasing older population. In 1998, there was an estimated 54,500 cases, induding 39,500 in men and 15,000 in women. The age-adjusted incidence in the United States is 32 per 100,000 for men and eight per 100,000 in women. The historic male/female ratio of 3:1 may be decreasing related to smoking patterns in women. There were an estimated 11,000 deaths from bladder cancer in 1998 (7,800 in men and 3,900 in women). Bladder cancer incidence and mortality strongly increase with age and wil be an increasing problem as the population becomes more elderly. Most bladder cancers recur in the bladder. Bladder cancer is managed with a combination of transurethral resection of the bladder (TUR) and intravesical chemotherapy or immunotherapy. The multifocal and recurrent nature of bladder cancer points out the limitations of TUR Most muscle-Invasive cancers are not cured by TUR alone. Radical cystectomy and urinary diversion is the most effective means to eliminate the cancer but carry an undeniable impact on urinary and sexual function. There continues to be a significant need for treatment modalities that are beneficial for bladder cancer patients. An estimated 130,200 cases of colorectal cancer occurred in 2000 in the United States, including 93,800 cases of colon cancer and 36,400 of rectal cancer. Colorectal cancers are the third most common cancers in men and women. Incidence rates declined significantly during 1992-1996 (-2.1% per year). Research suggests that these declines have been 2 due to increased screening and polyp removal, preventing progression of polyps to invasive cancers. There were an estimated 56,300 deaths (47,700 from colon cancer, 8,600 from rectal cancer) in 2000, accounting for about 11% of all U.S. cancer deaths. At present, surgery is the most common form of therapy for colorectal cancer, and for cancers that have not spread, it is frequently curative. Chemotherapy, or chemotherapy plus radiation, is given before or after surgery to most patients whose cancer has deeply perforated the bowel wall or has spread to the lymph nodes. A permanent colostomy (creation of an abdominal opening for elimination of body wastes) is occasionally needed for colon cancer and is infrequently required for rectal cancer. There continues to be a need for effective diagnostic and treatment modalities for colorectal cancer. There were an estimated 164,100 new cases of lung and bronchial cancer in 2000, accounting for 14% of all U.S. cancer diagnoses.. The incidence rate of lung and bronchial cancer is declining significantly in men, from a high of 86.5 per 100,000 in 1984 to 70.0 in 1996. In the 1990s, the rate of increase among women began to slow. In 1996, the incidence rate in women was 42.3 per 100,000. Lung and bronchial cancer caused an estimated 156,900 deaths in 2000, accounting for 28% of all canetdeaths. During 1992-1996, mortality from lung cancer declined significantly among men (-1.7% per year) while rates for women were still significantly increasing (0.9% per year). Since 1987, more women have died each year of lung cancer than breast cancer, which, for over 40 years, was the major cause of cancer death in women. Decreasing lung cancer incidence and mortality rates most likely resulted from decreased smoking rates over the previous 30 years; however, decreasing smoking patterns among women lag behind those of men. Of concern, although the declines in adult tobacco use have slowed, tobacco use in youth is increasing again. Treatment options for lung and bronchial cancer are determined by the type and stage of the cancer and include surgery, radiation therapy, and chemotherapy. For many localized cancers, surgery is usually the treatment of choice. Because the disease has usually spread by the time it is discovered, radiation therapy and chemotherapy are often needed in combination with surgery. Chemotherapy alone or combined with radiation is the treatment of chdice for small cell lung cancer; on this regimen, a large percentage of patients experience remission, which in some cases is long lasting. There is however, an ongoing need for effective treatment and diagnostic approaches for lung and bronchial cancers. An estimated 182,800 new invasive cases of breast cancer were expected to occur among women in the United States during 2000. Additionally, about 1,400 new cases of breast cancer were expected to be diagnosed in men in 2000. After increasing about 4% per year in the 1980s, breast cancer incidence rates in women have leveled off in the 1990s to about 110.6 cases per 100,000. In the U.S. alone, there were an estimated 41,200 deaths (40,800 women, 400 men) in 2000 due to breast cancer. Breast cancer ranks second among cancer deaths in women. According to the most recent data, mortality rates declined significantly during 1992-1996 with the largest decreases in younger women, both white and black. These decreases were probably the result of earlier detection and improved treatment. Taking into account the medical circumstances and the patient's preferences, treatment of breast cancer may involve lumpectomy (local removal of the tumor) and removal of the lymph nodes under the arm; mastectomy (surgical removal of the breast) and removal of the lymph nodes under the arm; radiation therapy; chemotherapy; or hormone therapy. Often, two or more methods are used in combination. Numerous studies have shown that, for early stage disease, long-term survival rates after lumpectomy plus radiotherapy are similar to survival rates after modified radical mastectomy. Significant advances in reconstruction techniques provide several options for breast reconstruction after mastectomy. Recently, such reconstruction has been done at the same time as the mastectomy. 3 Local excision of ductal carcinoma in situ (DCIS) with adequate amounts of surrounding normal breast tissue may prevent the local recurrence of the DCIS. Radiation to the breast and/or tamoxifen may reduce the chance of DCIS occurring in the remaining breast tissue. This is important because DCIS, if left untreated, may 5 develop into invasive breast cancer. Nevertheless, there are serious side effects or sequelae to these treatments. There is, therefore, a need for efficacious breast cancer treatments. There were an estimated 23,100 new cases of ovarian cancer in the United States in 2000. It accounts for 4% of all cancers among women and ranks second 10 among gynecologic cancers. During 1992-1996, ovarian cancer incidence rates were significantly declining. Consequent to ovarian cancer, there were an estimated 14,000 deaths in 2000. Ovarian cancer causes more deaths than any other cancer of the female reproductive system. Surgery, radiation therapy, and chemotherapy are treatment options for ovarian 15 cancer. Surgery usually includes the removal of one or both ovaries, the fallopian tubes (salpingo-oophorectomy), and the uterus (hysterectomy). In some very early tumors, only the involved ovary will be removed, especially in young women who wish to have children. In advanced disease, an attempt is made to remove all intra-abdominal disease to enhance the effect of chemotherapy. There continues to be an important 20 need for effective treatment options for ovarian cancer. There were an estimated 28,300 new cases of pancreatic cancer in the United States in 2000. Over the past 20 years, rates of pancreatic cancer have declined in men. Rates among women have remained approximately constant but may be beginning to decline. Pancreatic cancer caused an estimated 28,200 deaths in 2000 in the United 25 States. Over the past 20 years, there has been a slight but significant decrease in mortality rates among men (about -0.9% per year) while rates have increased slightly among women. Surgery, radiation therapy, and chemotherapy are treatment options for pancreatic cancer. These treatment options can extend survival and/or relieve 30 symptoms in many patients but are not likely to produce a cure for most. There is a significant need for additional therapeutic and diagnostic options for pancreatic cancer. Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of 35 these matters form part of the prior art base or were common general knowledge in the

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field relevant to the present invention as it existed before the priority date of each claim of this application. SUMMARY OF THE INVENTION 5 The present invention relates to a gene, designated 98P4B6, that has now been found to be over-expressed in the cancer(s) listed in Table I. Northern blot expression analysis of 98P4B6 gene expression in normal tissues shows a restricted expression pattern in adult tissues. The nucleotide (Figure 2) and amino acid (Figure 2, and Figure 3) sequences of 98P4B6 are provided. The tissue-related profile of 98P4B6 in normal 10 adult tissues, combined with the over-expression observed in the tissues listed in Table I, shows that 98P4B6 is aberrantly over-expressed in at least some cancers, and thus serves as a useful diagnostic, prophylactic, prognostic, and/or therapeutic target for cancers of the tissue(s) such as those listed in Table I. The invention provides polynucleotides corresponding or complementary to all 15 or part of the 98P4B6 genes, mRNAs, and/or coding sequences, preferably in isolated form, including polynucleotides encoding 98P4B6-related proteins and fragments of 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 contiguous amino acids; at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100 or more than 100 contiguous amino acids of a 98P4B6-related protein, as well as 20 the peptides/proteins themselves; DNA, RNA, DNA/RNA hybrids, and related molecules, polynucleotides or oligonucleotides complementary or having at least a 90% homology to the 98P4B6 genes or mRNA sequences or parts thereof, and polynucleotides or oligonucleotides that hybridize to the 98P4B6 genes, mRNAs, or to 98P4B6-encoding polynucleotides. Also provided are means for isolating cDNAs and 25 the genes encoding 98P4B6. Recombinant DNA molecules containing 98P4B6 polynudeotides, cells transformed or transduced with such molecules, and host-vector systems for the expression of 98P4B6 gene products are also provided. The invention further provides antibodies that bind to 98P4B6 proteins and polypeptide fragments thereof, including polyclonal and monoclonal antibodies, murine and 30 4A other mammalian antibodies, chimeric antibodies, humanized and fully human antibodies, and antibodies labeled with a detectable marker or therapeutic agent. In certain embodiments, there is a proviso that the entire nucleic acid sequence of Figure 2 is not encoded and/or the entire amino acid sequence of Figure 2 is not prepared. In 5 certain embodiments, the entire nucleic acid sequence of Figure 2 is encoded and/or the entire amino acid sequence of Figure 2 is prepared, either of which are in respective human unit dose forms. The invention further provides methods for detecting the presence and status of 98P4B6 polynucleotides and proteins in various biological samples, as well as methods 10 for identifying cells that express 98P4B6. A typical embodiment of this invention provides methods for monitoring 98P4B6 gene products in a tissue or hematology sample having or suspected of having some form of growth dysregulation such as cancer. For example, the invention provides methods for detecting the presence and 15 status of 98P4B6 polynucleotides wherein semi-quantitative PCR is performed on cDNA prepared from a cancer patient tissue sample using primes to 98P4B6 V.1, V.13 and V.14(A), and when normalized by PCR using primers to actin, the expression of 98P4B6 is recorded as absent, low, medium or strong. In yet another embodiment, the invention provides methods for detecting the 20 presence and status of 98P4B6 polynucleotides, wherein a 98P4B6 polynucleotide is hybridised with RNA extracted from cancer patient specimens. In another embodiment, the invention provides methods for detecting the expression of 98P4B6 with polyclonal antibody, wherein a sample from a cancer patient is run on an SDS-PAGE acrylamide gel, blotted and stained with either anti 25 98P4B6 antibody generated against amino acids 198-389, or anti-98P4B6 antibody generated against amino acids 153-165. The present invention further provides a method for detecting the presence of a protein comprising the amino acid sequence of SEQ ID NO: 3 in a sample comprising: contacting the sample with an antibody or fragment thereof of the invention, and 30 determining that there is a complex of the antibody or fragment thereof and said protein. The invention further provides various immunogenic or therapeutic compositions and strategies for treating cancers that express 98P4B6 such as cancers of tissues listed in Table I, including therapies aimed at inhibiting the transcription, 35 translation, processing or function of 98P4B6 as well as cancer vaccines. In one aspect, the invention provides compositions, and methods comprising them, for treating a 5 cancer that expresses 98P4B6 in a human subject wherein the composition comprises a carrier suitable for human use and a human unit dose of one or more than one agent that inhibits the production or function of 98P4B6. Preferably, the carrier is a uniquely human carrier. In another aspect of the invention, the agent is a moiety that is 5 immunoreactive with 98P4B6 protein. Non-limiting examples of such moieties include, but are not limited to, antibodies (such as single chain, monoclonal, polyclonal, humanized, chimeric, or human antibodies), functional equivalents thereof (whether naturally occurring or synthetic), and combinations thereof. The antibodies can be conjugated to a diagnostic or therapeutic moiety. In another aspect, the agent is a small 10 molecule as defined herein. In another aspect, the agent comprises one or more than one peptide which comprises a cytotoxic T lymphocyte (CTL) epitope that binds an HLA class I molecule in a human to elicit a CTL response to 98P4B6 and/or one or more than one peptide which comprises a helper T lymphocyte (HTL) epitope which binds an HLA class II 15 molecule in a human to elicit an HTL response. The peptides of the invention may be on the same or on one or more separate polypeptide molecules. In a further aspect of the invention, the agent comprises one or more than one nucleic acid molecule that expresses one or more than one of the CTL or HTL response stimulating peptides as described above. In yet another aspect of the invention, the one or more than one 20 nucleic acid molecule may express a moiety that is immunologically reactive with 98P4B6 as described above. The one or more than one nucleic acid molecule may also be, or encodes, a molecule that inhibits production of 98P4B6. Non-limiting examples of such molecules include, but are not limited to, those complementary to a nucleotide sequence essential for production of 98P4B6 (e.g. antisense sequences or molecules 25 that form a triple helix with a nucleotide double helix essential for 98P4B6 production) or a ribozyme effective to lyse 98P4B6 mRNA. Note that to determine the starting position of any peptide set forth in Tables VIII-XXI and XXII to XLIX (collectively HLA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the 30 particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides of a particular for a particular variant. The position of each Search Peptide relative to its respective parent molecule is listed in Table VII. Accordingly, if a Search Peptide begins at position "X", one must add the value "X - I" to each position 35 in Tables VIII-XXI and XXII to XLIX to obtain the actual position of the HLA peptides in their parental molecule. For example, if a particular Search Peptide begins 6 at position 150 of its parental molecule, one must add 150 - 1, i.e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid in the parent molecule. One embodiment of the invention comprises an HLA peptide, that occurs at 5 least twice in Tables VIII-XXI and XXII to XLIX collectively, or an oligonucleotide that encodes the HLA peptide. Another embodiment of the invention comprises an HLA peptide that occurs at least once in Tables VIII-XXI and at least once in tables XXII to XLIX, or an oligonucleotide that encodes the HLA peptide. The present invention further provides a composition comprising: 10 a) a peptide of Tables VIII-IX or XII-XXI or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV; b) a peptide of Tables XXII, XXV, XXVII, XXXIII-XXXIV, XXXVII, and XXXIX or an analog thereof wherein an amino acid at a primary anchor site of the 15 peptide is substituted with a preferred amino acid as shown in Table IV; or c) a peptide of Tables XLVI to XLIX or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV. The present invention further provides a composition comprising: 20 a) a peptide of Tables VIII-IX or XII-XXI or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV; b) a peptide of Tables XXII, XXV, XXVII, XXXIV, XXXVII, and XXXIX or an analog thereof wherein an amino acid at a primary anchor site of the peptide is 25 substituted with a preferred amino acid as shown in Table IV; or c) a peptide of Tables XLVI to XLIX or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV; wherein the peptide is a peptide of SEQ ID NO: 3. 30 The present invention further provides an isolated polynucleotide that encodes a peptide of the invention. The present invention further provides a vector that comprises the polynucleotide of the invention. Another embodiment of the invention is antibody epitopes, which comprise a 35 peptide region, or an oligonucleotide encoding the peptide region, that has one two, three, four, or five of the following characteristics: 6A i) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 5 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Hopp and Woods (Hopp T.P., Woods K.R., 1981. Proc. Natl. Acad. Sci. U.S.A. 78:3824-3828) accessed on the Protscale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. 10 ii) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a value equal to 0.0, in the Hydropathicity profile of 98P4B6v. 1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of 15 Kyte and Doolittle (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132) accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi bin/protscale.pl) through the ExPasy molecular biology server. iii) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that 20 includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Percent Accessible Residues profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Janin (Janin J., 1979 Nature 277:491-492) accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale.pl) 25 through the ExPasy molecular biology server. iv) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of 98P4B6v. 1, 30 v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Bhaskaran and Ponnuswamy (Bhaskaran R., and Ponnuswamy P.K., 1988 Int. J. Pept. Protein Res. 32:242-255) accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. 35 v) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that 6B includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Deleage and Roux (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294) 5 accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi bin/protscale.pl) through the ExPasy molecular biology server. The present invention further provides a method of generating a mammalian immune response directed to a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 10 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising: exposing cells of the mammal's immune system to a) a peptide of the invention and/or b) a nucleotide sequence that encodes said peptide, whereby an immune response is generated to said protein. The present invention further provides a method of generating a mammalian 15 immune response directed to a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: exposing cells of the mammal's immune system to a) a peptide of the invention and/or b) a nucleotide sequence that encodes said peptide, whereby an immune response is generated to said protein. The present invention further provides an isolated antibody or fragment thereof 20 that specifically binds to a peptide of the invention. The present invention further provides an antibody-agent conjugate comprising the antibody or fragment the invention conjugated to a cytotoxic agent or diagnostic agent. The present invention further provides a method of delivering a cytotoxic agent 25 or a diagnostic agent to a cell that expresses a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, said method comprising: exposing said cells to the antibody-agent conjugate of the invention. 30 The present invention further provides a method of delivering a cytotoxic agent or a diagnostic agent to a cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, said method comprising: exposing said cells to the antibody-agent conjugate of the invention. The present invention further provides a method of inhibiting growth of cancer 35 cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 6C 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising: exposing said cells to an antibody-agent conjugate of the invention. The present invention further provides a method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the 5 method comprising: exposing said cells to an antibody-agent conjugate as in the invention. The present invention further provides a composition comprising a polynucleotide that encodes an antibody or fragment thereof of the invention. The present inventions further provides a method of inhibiting growth of cancer 10 cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising administering to said cells an antibody or fragment thereof of the invention. The present invention further provides a method of inhibiting growth of cancer 15 cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising administering to said cells an antibody or fragment thereof of the invention. The present invention further provides a method of inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID 20 NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising: administering to said cells a) a peptide of the invention and/or b) a nucleotide sequence that encodes said peptide. The present invention further provides a method of inhibiting growth of cancer 25 cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: administering to said cells a) a peptide of the invention and/or b) a nucleotide sequence that encodes said peptide. The present invention further provides a method of inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID 30 NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, and a particular HLA molecule, the method comprising: administering human T cells to said cancer cells, wherein said T cells specifically recognize a peptide of the invention, wherein the peptide is in the context of the particular HLA molecule. 6D The present invention further provides a method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, and a particular HLA molecule, the method comprising: administering human T cells to said cancer cells, wherein said T cells specifically recognize a peptide of the invention 5 wherein the peptide is in the context of the particular HLA molecule. The present invention further provides a method for inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising: 10 administering to the cancer cells a vector that delivers a nucleotide that encodes a single chain monoclonal antibody having the specificity of an antibody of the invention, whereby the encoded single chain antibody is expressed intracellularly within said cancer cells. The present invention further provides a method for inhibiting growth of cancer 15 cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: administering to the cancer cells a vector that delivers a nucleotide that encodes a single chain monoclonal antibody having the specificity of an antibody of the invention, whereby the encoded single chain antibody is expressed intracellularly within said cancer cells. 20 The present invention further provides a method of delivering a calcium channel inhibitor to a cancer cell that expresses a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising exposing the cell to an antibody-inhibitor conjugate comprising an 25 antibody or fragment thereof conjugated to a calcium channel inhibitor, wherein the antibody or fragment thereof specifically binds to the protein. The present invention further provides a method of delivering a calcium channel inhibitor to a cancer cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising exposing the cell to an antibody-inhibitor 30 conjugate comprising an antibody or fragment thereof conjugated to a calcium channel inhibitor, wherein the antibody or fragment thereof specifically binds to the protein. The present invention further provides a method of inhibiting the growth of a paclitaxel-resistant cancer cell that expresses a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID 35 NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51, the method comprising exposing the cell to an antibody-agent conjugate 6E comprising an antibody or fragment thereof conjugated to a cytotoxic agent or therapeutic agent, wherein the antibody or fragment thereof specifically bind to the protein. The present invention further provides a method of inhibiting the growth of a 5 paclitaxel-resistant cancer cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising exposing the cell to an antibody agent conjugate comprising an antibody or fragment thereof conjugated to a cytotoxic agent or therapeutic agent, wherein the antibody or fragment thereof specifically bind to the protein. 10 The present invention further provides an isolated polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 5, SEQ ID NO: 11 and SEQ ID NO: 15. The present invention further provides an isolated polynucleotide comprising a nucleic acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID 15 NO: 10 and SEQ ID NO: 14. The present invention further provides an isolated antibody or a fragment thereof that specifically binds to an amino acid sequence selected from the group consisting of SEQ ID NO: 5, SEQ ID NO: 11 and SEQ ID NO: 15. The present invention further provides use of the peptide of the invention and/or 20 a nucleotide sequence that encodes said peptide in the manufacture of a composition for generating a mammalian immune response directed to a protein selected from the groups and consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51. 25 The present invention further provides use of the antibody or fragment thereof of the invention or the antibody-agent conjugate of the invention in the manufacture of a medicament for inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and 30 SEQ ID NO: 51. The present invention further provides use of a peptide of the invention and/or a nucleotide sequence that encodes said peptide in the manufacture of a medicament for inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID 35 NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51.

The present invention further provides use of T cells which specifically recognise a peptide of the invention in the context of a particular HLA molecule in the manufacture of a medicament for inhibiting growth of cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID 5 NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51. The present invention further provides use of a vector comprising a nucleotide sequence that encodes a single chain monoclonal antibody having a specificity of an antibody of the invention in the manufacture of a medicament for inhibiting growth of 10 cancer cells that express a protein selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51. The present invention further provides use of an antibody-agent conjugate comprising an antibody or fragment thereof conjugated to a cytotoxic agent or 15 therapeutic agent in the manufacture of a medicament for inhibiting the growth of paclitaxel-resistant cancer cell that expresses a protein selected from a group consisting of SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 11; SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 27; SEQ ID NO: 29; SEQ ID NO: 43 and SEQ ID NO: 51. Throughout this specification the word "comprise", or variations such as 20 "comprises" or "comprising", will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. BRIEF DESCRIPTION OF THE FIGURES 25 Figure 1. The 98P4B6 SSH sequence of 183 nucleotides. Figure 2. A) The cDNA and amino acid sequence of 98P4B6 variant I (also called "98P4B6 v.1" or "98P4B6 variant 1") is shown in Figure 2A. The start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. 30 B) The cDNA and amino acid sequence of 98P4B6 variant 2 (also called "98P4B6 v.2") is shown in Figure 2B. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 4-138 including the stop codon. C) The cDNA and amino acid sequence of 98P4B6 variant 3 (also called 35 "98P4B6 v.3") is shown in Figure 2C. The codon for the start methionine is A G underlined. The open reading frame extends from nucleic acid 188-1552 including the stop codon. D) The cDNA and amino acid sequence of 98P4B6 variant 4 (also called "98P4B6 v.4") is shown in Figure 2D. The codon for the start methionine is 5 underlined. The open reading frame extends from nucleic acid 318-1682 including the stop codon. E) The cDNA and amino acid sequence of 98P4B6 variant 5 (also called "98P4B6 v.5") is shown in Figure 2E. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 318-1577 including the 10 stop codon. F) The cDNA and amino acid sequence of 98P4B6 variant 6 (also called "98P4B6 v.6") is shown in Figure 2F. The codon for the start methionine is underlined. The open reading frame extends from nucleic add 318-1790 including the stop codon. 15 G) The cDNA and amino acid sequence of 98P4B6 variant 7 (also called "98P4B6 v.7") is shown in Figure 2G. The codon for the start methionine is underlined. The open reading frame extends from nucleic add 295-2025 including the stop codon. 6H H) The cDNA and amino acid sequence of 98P486 variant 8 (also called "98P4B6 v.8') is shown in Figure 2H. The codon for the start methionine is undefined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. 1) The cDNA and amino acid sequence of 98P4B6 variant 9 (also called '98P4B6 v.9") is shown in Figure 21. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. J) The cDNA and amino acid sequence of 98P4B6 variant 10 (also called '98P4B6 v.10") is shown in Figure 2J. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. K) The cDNA and amino acid sequence of 98P4B6 variant 11 (also called '98P486 v.11') is shown in Figure 2K. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. L) The cDNA and amino acid sequence of 98P4B6 variant 12 (also called '98P4B6 v.12") is shown in Figure 2L. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. M) The cDNA and amino acid sequence of 98P4B6 variant 13 (also called '98P4B6 v.13') is shown in Figure 2M. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. N) The cDNA and amino acid sequence of 98P4B6 variant 14 (also called 98P4B6 v.14") is shown in Figure 2N. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. 0) The cDNA and amino acid sequence of 98P4B6 variant 15 (also called'98P4B6 v.15') is shown in Figure 20. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. P) The cDNA and amino acid sequence of 98P4B6 variant 16 (also called '98P4B6 v.16') is shown in Figure 2P. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. 0) The cDNA and amino acid sequence of 98P4B6 variant 17 (also called '98P4B6 v.17") is shown in Figure 2Q. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. R) The cDNA and amino acid sequence of 98P4B6 variant 18 (also called '98P4B6 v.18") is shown in Figure 2R. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. S) The cDNA and amino acid sequence of 98P4B6 variant 19 (also called '98P4B6 v.19") is shown in Figure 2S. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. T) The cDNA and amino acid sequence of 98P486 variant 20 (also called '98P4B6 v.20") is shown in Figure 2T. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. U) The cDNA and amino acid sequence of 98P4B6 variant 21 (also called '98P4B6 v.21') is shown in Figure 2U. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. 7 V) The cDNA and amino acid sequence of 98P4B6 variant 22 (also called '98P4B6 v.22") is shown in Figure 2V. The codon for the start methionine is undefined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. W) The cDNA and amino acid sequence of 98P4B6 variant 23 (also called '98P4B6 v.23") is shown in Figure 2W. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. X) The cDNA and amino acid sequence of 98P4B6 variant 24 (also called '98P4B6 v.24") is shown in Figure 2X. The codon for the start methionine is underlined. The open reading frame extends from nudeic acid 295-2025 including the stop codon. Y) The cDNA and amino acid sequence of 98P4B6 variant 25 (also called "98P486 v.25") is shown in Figure 2Y. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. Z) The cDNA and amino acid sequence of 98P416 variant 26 (also called 98P4B6 v.26") is shown in Figure 2Z. The codon for the start methionine is underlined. The open reading frame extends from nudeic acid 394-1866 including the stop codon. AA) The cONA and amino acid sequence of 98P4B6 variant 27 (also called '98P4B6 v.27") is shown in Figure 2AA. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AB) The cDNA and amino acid sequence of 98P486 variant 28 (also called 98P4B6 v.28') is shown in Figure 2AB. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AC) The cDNA and amino acid sequence of 98P486 variant 29 (also called '98P4B6 v.29') is shown in Figure 2AC. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 inducing the stop codon. AD) The cDNA and amino acid sequence of 98P486 variant 30 (also called '98P486 v.30") is shown in Figure 2AD. The codon for the start methionine is underlined. The open reading frame extends from nudeic acid 394-1866 including the stop codon. AE) The cDNA and amino acid sequence of 98P4B6 variant 31 (also called "98P486 v.31") is shown in Figure 2AE. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AF) The cDNA and amino acid sequence of 98P4B6 variant 32 (also called '98P4B6 v.32") is shown in Figure 2AF. The codon for the start methionine is underlined. The open reading frame extends from nudeic acid 394-1866 including the stop codon. AG) The cONA and amino acid sequence of 98P4B6 variant 33 (also called '98P4B6 v.33') is shown in Figure 2AG. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AH) The cDNA and amino acid sequence of 98P486 variant 34 (also called '98P4B6 v.34') is shown in Figure 2AH. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 induding the stop codon. Al) The cDNA and amino acid sequence of 98P4B6 variant 35 (also called '98P486 v.35") is shown in Figure 2A. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon.

AJ) The cDNA and amino acid sequence of 98P4B6 variant 36 (also called "98P4B6 v.36") is shown in Figure 2AJ. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the 5 stop codon. AK) The cDNA and amino acid sequence of 98P4B6 variant 37 (also called "98P4B6 v.37") is shown in Figure 2AK. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. 10 AL) The cDNA and amino acid sequence of 98P4B6 variant 38 (also called "98P4B6 v.38") is shown in Figure 2AL. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. Figure 3. 15 A) The amino acid sequence of 98P4B6 v.1 is shown in Figure 3A; it has 454 amino acids. B) The amino acid sequence of 98P4B6 v.2 is shown in Figure 3B; it has 45 amino acids. C) The amino acid sequence of 98P4B6 v.5 is shown in Figure 3C; it has 419 20 amino acids. D) The amino acid sequence of 98P4B6 v.6 is shown in Figure 3D; it has 490 amino acids. E) The amino acid sequence of 98P4B6 v.7 is shown in Figure 3E; it has 576 amino acids. 25 F) The amino acid sequence of 98P4B6 v.8 is shown in Figure 3F; it has 490 amino acids. G) The amino acid sequence of 98P4B6 v.13 is shown in Figure 3G; it has 454 amino acids. H) The amino acid sequence of 98P4B6 v.14 is shown in Figure 3H; it has 30 454 amino acids. I) The amino acid sequence of 98P4B6 v.21 is shown in Figure 31; it has 576 amino acids. J) The amino acid sequence of 98P4B6 v.25 is shown in Figure 3J; it has 490 amino acids. 35 As used herein, a reference to 98P4B6 includes all variants thereof, including those shown in Figures 2, 3, 10, and 11, unless the context clearly indicates otherwise. n Figure 4. Comparison of 98P4B6 with known genes: Human STAMP 1, human six transmembrane epithelial antigen of prostate 2 and mouse six transmembrane epithelial antigen of prostate 2. Figure 4(A) Alignment of 98P4B6 variant 1 to human STAMPI (gi 15418732). Figure 4(B) Alignment of 98P4B6 5 variant 1 with human STEAP2 (gi: 23308593). Figure 4(C) Alignment of 98P4B6 variant I with mouse STEAP2 (gi 28501136). Figure 4(D) Clustal Alignment of the three 98P4B6 variants, depicting that 98P4B6 VIB contains an additional 62 aa at its N-terminus relative to V1, and that 98P4B6 V2 carries a I to T point mutation at aa 225 relative to VI. 10 Figure 5. Hydrophilicity amino acid profile of 98P4B6 v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Hopp and Woods (Hopp T.P., Woods K.R., 1981. Proc. Natl. Acad. Sci. U.S.A. 78:3824-3828) accessed on the Protscale website located on the World Wide Web at (.expasy.ch/cgi bin/protscale.pl) through the ExPasy molecular biology server. 15 Figure 6. Hydropathicity amino acid profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Kyte and Doolittle (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pI) through the ExPasy molecular biology server. 20 Figure 7. Percent accessible residues amino acid profile of 98P4B6 v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Janin (Janin J., 1979 Nature 277:491-492) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. 25 Figure 8. Average flexibility amino acid profile of 98P4B6 v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Bhaskaran and Ponnuswamy (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept. Protein Res. 32:242-255) accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale. pl) through the ExPasy molecular biology server. 30 Figure 9. Beta-turn amino acid profile of 98P4B6 v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Deleage and Roux (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294) accessed on the ProtScale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. 35 Figure 10. Figure 10(a): Schematic alignment of SNP variants of 98P4B6 v.1. Variants 98P4B6 v.9 through v. 9 were variants with single nucleotide difference from I n v.1. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. SNP in regions of other transcript variants, such as v.2, v.6 and v.8, not common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.l. Black 5 box shows the same sequence as 98P4B6 v.1. SNPs are indicated above the box. Figure 10(b): Schematic alignment of SNP variants of 98P4B6 v.7. Variants 98P4B6 v.20 through v.24 were variants with single nucleotide difference from v.7. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. Those SNP 10 in regions common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.7. Black box shows the same sequence as 98P4B6 v.7. SNPs are indicated above the box. Figure 10(c): Schematic alignment of SNP variants of 98P4B6 v.8. Variants 98P4B6 v.25 through v.38 were variants with single nucleotide difference from v.8. Though these SNP variants were shown separately, they could also occur in 15 any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. Those SNP in regions of common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.8. Black box shows the same sequence as 98P4B6 v.8. SNPs are indicated above the box. Figure 11. Schematic alignment of protein variants of 98P4B6. Protein 20 variants corresponded to nucleotide variants. Nucleotide variants 98P4B6 v.3, v.4, v.9 through v.12, and v.15 through v.19 coded for the same protein as v.1. Nucleotide variants 98P4B6 v.6 and v.8 coded the same protein except for single amino acid at 475, which is an "M" in v.8. Variants v.25 was translated from v.25, a SNP variant of v.8, with one amino acid difference at 565. Similarly, v.21 differed from v.7 by one 25 amino acid at 565. Single amino acid differences were indicated above the boxes. Black boxes represent the same sequence as 98P4B6 v.1. Numbers underneath the box correspond to 98P4B6 v.1. Figure 12. Structure of transcript variants of 98P4B6. Variant 98P4B6 v.2 through v.8 were transcript variants of v.1. Variant v.2 was a single exon transcript 30 whose 3' portion was the same as the last exon of v.1. The first two exons of v.3 were in intron 1 of v.1. Variants v.4, v.5 and v.6 spliced out 224-334 in the first exon of v.1. In addition, v.5 spliced out exon 5 while v.6 spliced out exon 6 but extended exon 5 of v.1. Variant v.7 used alternative transcription start and different 3' exons. Variant v.8 extended 5' end and kept the whole intron 5 of v.1. The first 35 bases of v.1 were not 35 in the nearby 5' region of v.1 on the current assembly of the human genome. Ends of exons in the transcripts are marked above the boxes. Potential exons of this gene are 1 1 shown in order as on the human genome. Poly A tails and single nucleotide differences are not shown in the figure. Numbers in underneath the boxes correspond to those of 98P4B6 v.1. Lengths of introns and exons are not proportional. Figure 13. Secondary structure and transmembrane domains prediction for 5 98P4B6 protein variants. 13(A), 13(B), 13(C), 13(D), 13(E): The secondary structure of 98P4B6 protein variant 1 (SEQ ID NO: 193), Variant 2 (SEQ ID NO: 194), Variant 5 (SEQ ID NO: 195), Variant 6 (SEQ ID NO: 196), and Variant 7 (SEQ ID NO: 197) were predicted using the HNN-Hierarchical Neural Network method (Guermeur, 1997, located on the World Wide Web at .pbil.ibcp.fr/cgi-bin/npsa automat.pl? 10 page=npsann.html, accessed from the ExPasy molecular biology server located on the World Wide Web at .expasy.ch/tools. This method predicts the presence and location of alpha helices, extended strands, and random coils from the primary protein sequence. The percent of the protein in a given secondary structure is also listed. 13(F), 13(H), 13(J), 13(L), and 13(N): Schematic representations of the 15 probability of existence of transmembrane regions and orientation of 98P4B6 variants 1, 2, 5-7, respectively, based on the TMpred algorithm of Hofmann and Stoffel which utilizes TMBASE (K. Hofmann, W. Stoffe. TMBASE-A database of membrane spanning protein segments Biol. Chem. Hoppe-Seyler 374:166, 1993). 13(G), 13(I), 13(K), 13(M), and 13(0): Schematic representations of the probability of the existence 20 of transmembrane regions and the extraceffular and intracellular orientation of 98P4B6 variants 1, 2, 5-7, respectively, based on the TMHMM algorithm of Sonnhammer, von Heijne, and Krogh (Erik L.L. Sonnhammer, Gunnar von Heijne, and Anders Krogh: A hidden Markov model for predicting transmembrane helices in protein sequences. In Proc. of Sixth Int. Conf. on Intelligent Systems for Molecular Biology, p 175-182 Ed J. 25 Glasgow, T. Littlejohn, F. Major, R. Lathrop, D. Sankoff, and C. Sensen Menlo Park, CA: AAAI Press, 1998). The TMpred and TMHMM algorithms are accessed from the ExPasy molecular biology server located on the World Wide Web at .expasy.ch/tools/. Figure 14. 98P4B6 Expression in Human Normal and Patient Cancer Tissues. First strand cDNA was generated from normal stomach, normal brain, normal heart, 30 normal liver, normal skeletal muscle, normal testis, normal prostate, normal bladder, normal kidney, normal colon, normal lung, normal pancreas, and a pool of cancer specimens from prostate cancer patients, bladder cancer patients, kidney cancer patients, colon cancer patients, lung cancer patients, pancreas cancer patients, and a pool of 2 patient prostate metastasis to lymph node. Normalization was performed by 35 PCR using primers to actin. Semi-quantitative PCR, using primers directed to 98P4B6 v.1, v.13, and v.14(A), or directed specifically to the splice variants 98P4B6 v.6 and 12 v.8(B), was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Results show strong expression of 98P4B6 v.1, v.13, and v.14 and its splice variants v.6 and v.8 in normal prostate and in prostate cancer. Expression was also detected in 5 bladder cancer, kidney cancer, colon cancer, lung cancer, pancreas cancer, breast cancer, cancer metastasis as well as in the prostate cancer metastasis to lymph node specimens, compared to all normal tissues tested. Figure 15. 98P4B6 Expression in lung, ovary, prostate, bladder, cervix, uterus and pancreas patient cancer specimens. First strand cDNA was prepared from a panel 10 of patient cancer specimens. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 98P4B6 v.1, v.13, and v.14, was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Expression was recorded as absent, low, medium or strong. Results show expression of 98P4B6 in the 15 majority of all patient cancer specimens tested. Figure 16. Expression of 98P4B6 in stomach cancer patient specimens. (A) RNA was extracted from normal stomach (N) and from 10 different stomach cancer patient specimens (T). Northern blot with 10 pg of total RNA/lane was probed with 98P4B6 sequence. Results show strong expression of 98P4B6 in the stomach tumor 20 tissues and lower expression in normal stomach. The lower panel represents ethidium bromide staining of the blot showing quality of the RNA samples. (B) Expression of 98P4B6 was assayed in a panel of human stomach cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 98P4B6 was detected in 7 out of 8 stomach tumors but not in the matched normal tissue. 25 Figure 17. Detection of 98P4B6 expression with polyclonal antibody. 293T cells were transfected with 98P4B6.GFP.pcDNA3.1/mychis construct clone A12 or clone B12. STEAP1.GFP vector was used as a positive control. And as a negative control an empty vector was used. Forty hours later, cell lysates were collected. Samples were run on an SDS-PAGE acrylamide gel, blotted and stained with either 30 anti-GFP antibody (A), anti-98P4B6 antibody generated against amino acids 198-389 (B), or anti-98P4B6 antibody generated against amino acids 153-165. The blot was developed using the ECL chemiluminescence kit and visualized by autoradiography. Results show expression of the expected 98P4B6.GFP fusion protein as detected by the anti-GFP antibody. Also, we were able to raise 2 different polyclonal antibodies that 35 recognized the 98P4B6.GFP fusion proteins as shown in B and C. 12A Figure 18. Detection of 98P4B6 expression with polyclonal antibody. 293T cells were transfected with 98P4B6.GFP.pcDNA3.1/mychis construct clone A12 or clone B12. Expression of the 98P4B6.GFP fusion protein was detected by flow cytometry (A) and by flurorescent microscopy (B). Results show strong green 5 fluorescence in the majority of the cells. The fusion protein localized to the perinuclear area and to the cell membrane. Figure 19. STEAP-2 Characteristics. The expression of STEAP-2 in normal tissues is predominantly restricted to the prostate. STEAP-2 is expressed in several cancerous tissues. In patient-derived prostate, colon, and lung cancer specimens; and 10 Multiple cancer cell lines, including prostate, colon, Ewing's sarcoma, lung, kidney, pancreas and testis. By ISH, STEAP-2 expression appears to be primarily limited to ductal epithelial cells. Figure 20. STEAP-2 Induces Tyrosine Phosphorylation in PC3 Cells. STEAP-2 induces the tyrosine phosphorylation of proteins at 140-150, 120, 75-80, 62 15 and 40 kDa. Figure 21. STEAP-2 Enhances Tyrosine Phosphorylation in NIH 3T3 Cells. STEAP-2 enhances the phosphorylation of p135-140, p78-75 by STEAP-2 in NIH 3T3 cells. STEAP-2 C-Flag enhances the phosphorylation of p180, and induces the de phosphorylation of p132, p 8 2 and p75. 20 Figure 22. STEAP-2 Induces ERK Phosphorylation. STEAP-2 Induces ERK phosphorylation in PC3 and 3T3 cells in 0.5 and 10% FBS. Lack or ERK phosphorylation in 3T3-STEAP-2-cflag cells. Potential role as dominant negative. Figure 23. STEAP Enhances Calcium Flux in PC3 cells. PC-STEAP-1 and PC3-STEAP-2 exhibit enhanced calcium flux in response to LPA. PC3-STEAP-1 25 demonstrates susceptibility to the L type calcium channel inhibitor, conotoxin. PC3 STEAP-2 shown susceptibility to the PQ type calcium channel inhibitor, agatoxin. NDGA and TEA had no effect on the proliferation of PC3-STEAP-2 cells. Figure 24. STEAP-2 Alters the Effect of Paclitaxel on PC3 Cells. Other Chemotherapeutics Tested without yielding a differential response between STEAP 30 expressing and control cells were Flutamide, Genistein, Rapamycin. STEAP-2 confers partial resistance to Paclitaxel in PC3 cells. Over 8 fold increase in percent survival of PC3-STEAP-2 relative to PC3-Neo cells. Figure 25. Inhibition of Apoptosis by STEAP-2. PC3 cells were treated with paclitaxel for 60 hours and analyzed for apoptosis by annexinV-PI staining. Expression 35 of STEAP-2 partially inhibits apoptosis by paclitaxel. 12B Figure 26. STEAP-2 Attenuates Paclitaxel Mediated Apoptosis. PC3 cells were treated with paclitaxel for 68 hours and analyzed for apoptosis. Expression of STEAP-2, but not STEAP-2CFlag, partially inhibits apoptosis by paclitaxel. 5 DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions II.) 98P4B6 Polynucleotides II.A.) Uses of 98P4B6 Polynucleotides 10 II.A.1.) Monitoring of Genetic Abnormalities II.A.2.) Antisense Embodiments II.A.3.) Primers and Primer Pairs II.A.4.) Isolation of 98P4B6-Encoding Nucleic Acid Molecules II.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems 15 III.) 98P4B6-related Proteins III.A.) Motif-bearing Protein Embodiments III.B.) Expression of 98P4B6-related Proteins III.C.) Modifications of 98P4B6-related Proteins 12C III.D.) Uses of 98P4B6-related Proteins IV.) 98P4B6 Antibodies V.) 98P486 Cellular Immune Responses VI.) 98P4B6 Transgenic Animals VI.) Methods for the Detection of 98P486 ViII.) Methods for Monitoring the Status of 98P486-related Genes and Their Products IX.) Identification of Molecules That Interact With 98P4B6 X.) Therapeutic Methods and Compositions X.A.) Anti-Cancer Vaccines XB.) 98P4B6 as a Target for Antibody-Based Therapy XC.) 98P416 as a Target for Cellular Immune Responses XC.1. Minigene Vaccines X.C.2. Combinations of CTL Peptides with Helper Peptides X.C.3. Combinations of CTL Peptides with T Cell Priming Agents X.C.4. Vaccine Compositions Comprising DC Pulsed with CTL and/or HTL Peptides X.D.) Adoptive Immunotherapy XE.) Administration of Vaccines for Therapeutic or Prophylactic Purposes Xi.) Diagnostic and Prognostic Embodiments of 98P4B6. XII.) Inhibition of 98P4B6 Protein Function XIIA.) Inhibition of 98P4B6 With Intracellular Antibodies XII.B.) Inhibition of 98P4B6 with Recombinant Proteins XII.C.) Inhibition of 98P4B6 Transcription or Translation XII.D.) General Considerations for Therapeutic Strategies XJII.) Identification, Characterization and Use of Modulators of 98P4B6 XIV.) KITS/Articles of Manufacture 1.) Definitions: Unless otherwise defined, all terms of art, notations and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined herein for parity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. Many of the techniques and procedures described or referenced herein are well understood and commonly employed using conventional methodology by those skilled in the art, such as, for example, the widely utilized molecular cloning methodologies described in Sambrook et aL., Molecular Cloning: A Laboratory Manual 2nd. edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer defined protocols and/or parameters unless otherwise noted. The terms 'advanced prostate cancer, "locally advanced prostate cancer", 'advanced disease and 'locally advanced disease" mean prostate cancers that have extended through the prostate capsule, and are meant to indude stage C disease under the American Urological Association (AUA) system, stage C1 - C2 disease under the Whitmore-Jewett system, and stage T3 - T4 and N+ disease under the TNM (tumor, node, metastasis) system. In general, surgery is not recommended for patients with locally advanced disease, and these patients have substantially less favorable outcomes 13 compared to patients having clinically localized (organ-confined) prostate cancer. Locally advanced disease is clinically identified by palpable evidence of induration beyond the lateral border of the prostate, or asymmetry or induration above the prostate base. Locally advanced prostate cancer is presently diagnosed pathologically following radical prostatectomy if the tumor invades or penetrates the prostatic capsule, extends into the surgical margin, or invades the seminal vesides. "Altering the native glycosylation pattern" is intended for purposes herein to mean deleting one or more carbohydrate moieties found in native sequence 98P4B6 (either by removing the underlying glycosylation site or by deleting the glycosylation by chemical and/or enzymatic means), and/or adding one or more glycosylation sites that are not present in the native sequence 98P4B6. In addition, the phrase indudes qualitative changes in the glycosylation of the native proteins, involving a change in the nature and proportions of the various carbohydrate moieties present. The term "analog" refers to a molecule which is structurally similar or shares similar or corresponding attributes with another molecule (e.g. a 98P4B6-related protein). For example, an analog of a 98P486 protein can be specifically bound by an antibody or T cell that specifically binds to 98P486. The term "antibody" is used in the broadest sense. Therefore, an "antibody" can be naturally occurring or man-made such as monoclonal antibodies produced by conventional hybridoma technology. Anti-98P4B6 antibodies comprise monoclonal and polydonal antibodies as well as fragments containing the antigen-binding domain and/or one or more complementality determining regions of these antibodies. An "antibody fragment" is defined as at least a portion of the variable region of the immunoglobulin molecule that binds to its target i.e., the antigen-binding region. In one embodiment it specifically covers single anti-98P4B6 antibodies and clones thereof (induding agonist, antagonist and neutralizing antibodies) and anti-98P4B6 antibody compositions with polyepitopic specificity. The term "codon optimized sequences" refers to nucleotide sequences that have been optimized for a particular host species by replacing any codons having a usage frequency of less than about 20%. Nuceotide sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exonfintron splicing signals, elimination of transposon-like repeats and/or optimization of GC content in addition to codon optimization are referred to herein as an "expression enhanced sequences." A "combinatorial library" is a collection of diverse chemical compounds generated by either chemical synthesis or biological synthesis by combining a number of chemical "building blocks" such as reagents. For example, a linear combinatorial chemical library, such as a polypeptide (e.g., mutein) library, is formed by combining a set of chemical building blocks called amino acids in every possible way for a given compound length (i.e., the number of amino acids in a polypeptide compound). Numerous chemical compounds are synthesized through such combinatorial mixing of chemical building blocks (Gallop et al., J. Med. Chem. 37(9): 1233-1251 (1994)). Preparation and screening of combinatorial libraries is well known to those of skill in the art. Such combinatorial chemical libraries indude, but are not limited to, peptide libraries (see, e.g., U.S. Patent No. 5,010,175, Furka, Pept. Prot. Res. 37:487-493 (1991), Houghton et al., Nature, 354:84-88 (1991)), peptoids (PCT Publication No WO 91119735), encoded peptides (PCT Publication WO 93/20242), random bio- oligomers (PCT Publication WO 92/00091), benzodiazepines (U.S. Pat No. 5,288,514), diversomers such as hydantoins, benzodiazepines and dipeptides (Hobbs et al., Proc. Nat Acad. Sci. USA 90:6909-6913 (1993)), vinylogous polypeptides (Hagihara et al., J. Amer. Chem. Soc. 114:6568 (1992)), nonpeptidal peptidomimetics with a Beta-D-Glucose scaffolding (Hirschmann et al., J. Amer. Chem. Soc. 114:9217-9218 (1992)), analogous organic syntheses of small compound libraries (Chen et al., J. Amer. Chem. Soc. 116:2661 (1994)), oligocarbamates (Cho, et al., Science 261:1303 (1993)), and/or peptidyl phosphonates (Campbell et al., J. Org. Chem. 59:658 (1994)). See, generally, Gordon et al., J. Med. Chem. 37:1385 (1994), nudeic acid libraries (see, e.g., Stratagene, Corp.), peptide nucleic acid libraries (see, e.g., U.S. Patent 5,539,083), antibody libraries (see, e.g., Vaughn et al., Nature 14 Biotechnology 14(3): 309-314 (1996), and PCT/US96/10287), carbohydrate libraries (see, e.g., Uang et al., Science 274:1520-1522 (1996), and U.S. Patent No. 5,593,853), and small organic molecule libraries (see. e.g., benzodiazepines, Baum, C&EN, Jan 18. page 33 (1993); isoprenoids, U.S. Patent No. 5,569,588; thiazolidinones and metathiazanones, U.S. Patent No. 5,549,974; pyrrolidines, U.S. Patent Nos. 5,525,735 and 5,519,134; morpholino compounds, U.S. Patent No. 5,506, 337; benzodiazepines, U.S. Patent No. 5,288,514; and the like). Devices for the preparation of combinatorial libraries are commercialy available (see, e.g., 357 NIPS, 390 NIPS, Advanced Chem Tech, Louisville KY; Symphony, Rainin, Wobum, MA; 433A, Applied Biosystems, Foster City, CA; 9050, Plus, Millipore, Bedford, NIA). A number of well-known robotic systems have also been developed for solution phase chemistries. These systems indude automated workstations such as the automated synthesis apparatus developed by Takeda Chemical Industries, LTD. (Osaka, Japan) and many robotic systems utilizing robotic arms (Zymate H, Zymark Corporation, Hopkinton, Mass.; Orca, Hewlett-Packard, Palo Alto, Calif.), which mimic the manual synthetic operations performed by a chemist. Any of the above devices are suitable for use with the present invention. The nature and implementation of modifications to these devices (if any) so that they can operate as discussed herein will be apparent to persons skilled in the relevant art. In addition, numerous combinatorial libraries are themselves commercially available (see, e.g., ComGenex, Princeton, NJ; Asinex, Moscow. RU; Tripos, Inc., St. Louis, MO; ChemStar, Ltd, Moscow, RU; 30 Pharmaceuticals, Exton, PA; Martek Biosciences, Columbia, MD; etc.). The term "cytotoxic agent" refers to a substance that inhibits or prevents the expression activity of cells, function of cells and/or causes destruction of cells. The term is intended to include radioactive isotopes chemotherapeutic agents, and toxins such as small molecule toxins or enzymatically active toxins of bacterial, lungal, plant or animal origin, including fragments and/or variants thereof. Examples of cytotoxic agents include, but are not limited to auristatins, auromycins, maytansinoids, yttrium, bismuth, ricin, ricin A-chain, combrestatin. duocarmycins, dolostatins, doxorubicin, daunorubicin, taxol, cisplatin, cc1065, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE4O, abrin, abrin A chain, modeccin A chain, alpha-sarcin, gelonin, mitogellin, retstrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Sapaonaria officinalis inhibitor, and glucocorticoid and other chemotherapeutic agents, as well as radioisotopes such as At 21 1 , 1131, 1125, Y90, Re 1 8, ReIU, Sm 1 s3, Bi212or 213, p32 and radioactive isotopes of Lu including Lu 1 7 7 . Antibodies may also be conjugated to an anti cancer pro-drug activating enzyme capable of converting the pro-drug to its active form. The "gene product" is sometimes referred to herein as a protein or mRNA. For example, a "gene product of the invention" is sometimes referred to herein as a "cancer amino acid sequence", "cancer protein", "protein of a cancer listed in Table r, a "cancer mRNA", "mRNA of a cancer listed in Table I", etc. In one embodiment, the cancer protein is encoded by a nucleic acid of Figure 2. The cancer protein can be a fragment, or alternatively, be the full-length protein to the fragment encoded by the nucleic acids of Figure 2. In one embodiment, a cancer amino acid sequence is used to determine sequence identity or similarity. In another embodiment, the sequences are naturally occurring allelic variants of a protein encoded by a nudeic acid of Figure 2. In another embodiment, the sequences are sequence variants as further described herein. "High throughput screening" assays for the presence, absence, quantification, or other properties of particular nucleic acids or protein products are well known to those of skill in the art. Similarly, binding assays and reporter gene assays are similarly well known. Thus, e.g., U.S. Patent No. 5,559,410 discloses high throughput screening methods for proteins; U.S. Patent No. 5,585,639 discloses high throughput screening methods for nucleic acid binding (i.e., in arrays); while U.S. Patent Nos. 5,576,220 and 5,541,061 disclose high throughput methods of screening for ligand/antibody binding. In addition, high throughput screening systems are commercially available (see, e.g., Amersham Biosciences, Piscataway, NJ; Zymark Corp., Hopkinton, MA; Air Technical Industries, Mentor, OH; Beckman Instruments, Inc. Fullerton, 15 CA; Precision Systems, Inc., Natick, MA; etc.). These systems typically automate entire procedures, induding all sample and reagent pipetting, liquid dispensing, timed incubations, and final readings of the microplate in detector(s) appropriate for the assay. These configurable systems provide high throughput and rapid start up as well as a high degree of flexibility and customization. The manufacturers of such systems provide detailed protocols for various high throughput systems. Thus, e.g., Zymark Corp. provides technical bulletins describing screening systems for detecting the modulation of gene transcription, ligand binding, and the like. The term "homolog" refers to a molecule which exhibits homology to another molecule, by for example, having sequences of chemical residues that are the same or similar at corresponding positions. "Human Leukocyte Antigen' or "HLA" is a human dass I or class Il Major Histocompatibility Complex (MHC) protein (see, e.g., Stites, et a., IMMUNOLOGY, 8mEo., Lange Publishing, Los Altos, CA (1994). The terms 'hybridize". "hybridizing", 'hybridizes' and the like, used in the context of polynucleotides, are meant to refer to conventional hybridization conditions, preferably such as hybridization in 50% formamide/6XSSC/0.1 % SDS/100 pg/ml ssDNA, in which temperatures for hybridization are above 37 degrees C and temperatures for washing in 0.1XSSC/0.1% SDS are above 55 degrees C. The phrases 'isolated" or 'biologically pure" refer to material which is substantially or essentially free from components which normally accompany the material as it is found in its native state. Thus, isolated peptides in accordance with the invention preferably do not contain materials normally associated with the peptides in their in situ environment For example, a polynudeotide is said to be "isolated" when it is substantially separated from contaminant polynucleotides that correspond or are complementary to genes other than the 98P4B6 genes or that encode polypeptides other than 98P4B6 gene product or fragments thereof. A skilled artisan can readily employ nucleic acid isolation procedures to obtain an isolated 98P4B6 polynudeotide. A protein is said to be 'isolated,' for example, when physical, mechanical or chemical methods are employed to remove the 98P4B6 proteins from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated 98P486 protein. Alternatively, an isolated protein can be prepared by chemical means. The term "mammal'refers to any organism classified as a mammal, including mice, rats, rabbits, dogs, cats, cows, horses and humans. In one embodiment of the invention, the mammal is a mouse. In another embodiment of the invention, the mammal is a human. The terms "metastatic prostate cancer and "metastatic disease" mean prostate cancers that have spread to regional lymph nodes or to distant sites, and are meant to include stage D disease under the AUA system and stage TxNxM+ under the TNM system. As is the case with locally advanced prostate cancer, surgery is generally not indicated for patients with metastatic disease, and hormonal (androgen ablation) therapy is a preferred treatment modality. Patients with metastatic prostate cancer eventually develop an androgen-refractory state within 12 to 18 months of treatment initiation. Approximately half of these androgen-refractory patients die within 6 months after developing that status. The most common site for prostate cancer metastasis is bone. Prostate cancer bone metastases are often osteoblastic rather than osteolytic (i.e., resulting in net bone formation). Bone metastases are found most frequently in the spine, followed by the femur, pelvis, rib cage, skull and humerus. Other common sites for metastasis include lymph nodes, lung, liver and brain. Metastatic prostate cancer is typically diagnosed by open or laparoscopic pelvic lymphadenectomy, whole body radionuclide scans, skeletal radiography, and/or bone lesion biopsy. The term 'modulator' or 'test compound" or 'drug candidate" or grammatical equivalents as used herein describe any molecule, e.g., protein, oligopeptide, small organic molecule, polysaccharide, polynucleotide, etc., to be tested for the capacity to directly or indirectly alter the cancer phenotype or the expression of a cancer sequence, e.g., a nucleic acid or protein sequences, or effects of cancer sequences (e.g., signaling, gene expression, protein interaction, etc.) In one aspect, a modulator will neutralize the effect of a cancer protein of the invention. By 'neutralize" is meant that an activity of a protein is inhibited or blocked, along with the consequent effect on the cell. In another aspect, a modulator will neutralize the effect of a gene, and its corresponding protein, of the invention by normalizing levels of said protein. In preferred embodiments, modulators alter expression profiles, or expression profile nucleic acids or proteins provided herein, or downstream effector pathways. In one embodiment, the modulator suppresses a cancer phenotype, e.g. to a normal tissue fingerprint. In another embodiment, a modulator induced a cancer phenotype. Generally, a plurality of assay mixtures is run in parallel with different agent concentrations to obtain a differential response to the various concentrations. Typically, one of these concentrations serves as a negative control, i.e., at zero concentration or below the level of detection. Modulators, drug candidates or test compounds encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 100 and less than about 2,500 Daltons. Preferred small molecules are less than 2000, or less than 1500 or less than 1000 or less than 500 D. Candidate agents comprise functional groups necessary for structural interaction with proteins, particularly hydrogen bonding, and typically include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The candidate agents often comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Modulators also comprise biomolecules such as peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs or combinations thereof. Particularly preferred are peptides. One class of modulators are peptides, for example of from about five to about 35 amino acids, with from about five to about 20 amino acids being preferred, and from about 7 to about 15 being particularly preferred. Preferably, the cancer modulatory protein is soluble, includes a non-transmembrane region, and/or, has an N terminal Cys to aid in solubility. In one embodiment, the C-terminus of the fragment is kept as a free acid and the N-terminus is a free amine to aid in coupling, i.e., to cysteine. In one embodiment, a cancer protein of the invention is conjugated to an immunogenic agent as discussed herein. In one embodiment, the cancer protein is conjugated to BSA. The peptides of the invention, e.g., of preferred lengths, can be linked to each other or to other amino acids to create a longer peptide/protein. The modulatory peptides can be digests of naturally occurring proteins as is outlined above, random'peptides, or "biased' random peptides. In a preferred embodiment, peptide/protein-based modulators are antibodies, and fragments thereof, as defined herein. Modulators of cancer can also be nucleic acids. Nucleic acid modulating agents can be naturally occurring nucleic acids, random nucleic acids, or "biased" random nucleic acids. For example, digests of prokaryotic or eukaryotic genomes can be used in an approach analogous to that outlined above for proteins. The term Imonodonal antibody' refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the antibodies comprising the population are identical except for possible naturally occurring mutations that are present in minor amounts. A "motif", as in biological motif of a 98P4B6-related protein, refers to any patten of amino acids forming part of the primary sequence of a protein, that is associated with a particular function (e.g. protein-protein interaction, protein-DNA interaction, etc) or modification (e.g. that is phosphorylated, glycosylated or amidated), or localization (e.g. secretory sequence, nuclear localization sequence, etc.) or a sequence that is correlated with being immunogenic, either humorally or cellularly. A motif can be either contiguous or capable of being aligned to certain positions that are generally correlated with a certain function or property. In the context of HLA motifs, 'motif refers to the pattern of residues in a peptide of defined length, usually a peptide of from about 8 to about 13 amino acids for a class I HLA motif and from about 6 to about 25 amino acids for a class 11 HLA motif, which is recognized by a particular HLA molecule. Peptide motifs for HLA binding are typically different for each protein encoded by each human HLA allele and differ in the patten of the primary and secondary anchor residues. 17 A 'pharmaceutical excipienr comprises a material such as an adjuvant, a carrier, pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservative, and the like. 'Pharmaceutically acceptable' refers to a non-toxic, inert, and/or composition that is physiologically compatible with humans or other mammals. The term 'polynucleotide' means a polymeric form of nucleotides of at least 10 bases or base pairs in length, either ribonudeotides or deoxynudeotides or a modified form of either type of nucleotide, and is meant to indude single and double stranded forms of DNA and/or RNA. In the art, this term if often used interchangeably with 'oligonucleotide". A polynucleotide can comprise a nucleotide sequence disposed herein wherein thymidine (T), as shown for example in Figure 2, can also be uracil (U); this definition pertains to the differences between the chemical structures of.DNA and RNA, in particular the observation that one of the four major bases in RNA is uracil (U) instead of thymidine (T). The term 'polypeptide' means a polymer of at least about 4, 5, 6, 7, or 8 amino acids. Throughout the specification, standard three letter or single letter designations for amino acids are used. In the art, this term is often used interchangeably with 'peptide" or 'protein'. An HLA 'primary anchor residue" is an amino acid at a specific position along a peptide sequence which is understood to provide a contact point between the immunogenic peptide and the HLA molecule. One to three, usually two, primary anchor residues within a peptide of defined length generally defines a'motiF for an immunogenic peptide. These residues are understood to fit in close contact with peptide binding groove of an HLA molecule, with their side chains buried in specific pockets of the binding groove. In one embodiment, for example, the primary anchor residues for an HLA class I molecule are located at position 2 (from the amino terminal position) and at the carboxyl terminal position of a 8, 9, 10, 11, or 12 residue peptide epitope in accordance with the invention. Alternatively, in another embodiment, the primary anchor residues of a peptide binds an HLA dass It molecule are spaced relative to each other, rather than to the termini of a peptide, where the peptide is generally of at least 9 amino acids in length. The primary anchor positions for each motif and supermotif are set forth in Table IV. For example, analog peptides can be created by altering the presence or.absence of particular residues in the primary and/or secondary anchor positions shown in Table IV. Such analogs are used to modulate the binding affinity and/or population coverage of a peptide comprising a particular HLA motif or supermotif. 'Radioisotopes' include, but are not limited to the following (non-limiting exemplary uses are also set forth): Examples of Medical Isotopes: Isotope Description of use Actinium-225 (AC-225) See Thorium-229 (Th-229) Actinium-227 (AC-227) Parent of Radium-223 (Ra-223) which is an alpha emitter used to treat metastases in the skeleton resulting from cancer (i.e., breast and prostate cancers), and cancer radioimmunotherapy Bismuth-212 (Bi-212) See Thorium-228 (Th-228) Bismuth-213 (Bi-213) See Thorium-229 (Th-229) Cadmium-109 (Cd-109) Cancer detection Cobalt-60 (Co-60) Radiation source for radiotherapy of cancer, for food irradiators, and for sterilization of medical supplies Copper-64 (Cu-64) A positron emitter used for cancer therapy and SPECT imaging Copper-67 (Cu-67) Betafgamma emitter used in cancer radioimmunotherapy and diagnostic studies (i.e., breast and colon cancers, and lymphoma) Dysprosium-166 (Dy-166) Cancer radioimmunotherapy Erbium-169 (Er-169) Rheumatoid arthritis treatment, particularly for the small joints associated with fingers and toes Europium-152 (Eu-152) Radiation source for food irradiation and for sterilization of medical supplies Europium-154 (Eu-1 54) Radiation source for food irradiation and for sterilization of medical supplies Gadolinium-1 53 (Gd-153) Osteoporosis detection and nuclear medical quality assurance devices Gold-198 (Au-198) Implant and intracavity therapy of ovarian, prostate, and brain cancers Holmium-166 (Ho-166) Multiple myeloma treatment in targeted skeletal therapy, cancer radioimmunotherapy, bone marrow ablation, and rheumatoid arthritis treatment Iodine-125 (1-125) Osteoporosis detection, diagnostic imaging, tracer drugs, brain cancer treatment, radiolabeling, tumor imaging, mapping of receptors in the brain, interstitial radiation therapy, brachytherapy for treatment of prostate cancer, determination of glomerular filtration rate (GFR), determination of plasma volume, detection of deep vein thrombosis of the legs Iodine-131 (1-131) Thyroid function evaluation, thyroid disease detection, treatment of thyroid cancer as well as other non malignant thyroid diseases (i.e., Graves disease, goiters, and hyperthyroidism), treatment of leukemia, lymphoma, and other forms of cancer (e.g., breast cancer) using radioimmunotherapy fridium-192 (Ir-192) Brachytherapy, brain and spinal cord tumor treatment treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and implants for breast and prostate tumors Lutetium-177 (Lu-177) 19 Cancer radioimmunotherapy and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Molybdenum-99 (Mo-99) Parent of Technetium-99m (Tc-99m) which is used for imaging the brain, liver, lungs, heart, and other organs. Currently, Tc-99m is the most widely used radioisotope used for diagnostic imaging of various cancers and diseases involving the brain, heart, liver, lungs; also used in detection of deep vein thrombosis of the legs Osmium-194 (Os-194) Cancer radioimmunotherapy Palladium-103 (Pd-103) Prostate cancer treatment Platinum-195m (Pt-195m) . Studies on biodistribution and metabolism of cisplatin, a chemotherapeutic drug Phosphorus-32 (P-32) Polycythemia rubra vera (blood cell disease) and leukemia treatment, bone cancer diagnosis/treatment; colon, pancreatic, and liver cancer treatment; radiolabeling nucleic acids for in vitro research, diagnosis of superficial tumors, treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and intracavity therapy Phosphorus-33 (P-33) Leukemia treatment, bone disease diagnosis/treatment, radiolabeling, and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Radium-223 (Ra-223) See Actinium-227 (Ac-227) Rhenium-186 (Re-186) Bone cancer pain relief, rheumatoid arthritis treatment, and diagnosis and treatment of lymphoma and bone, breast, colon, and liver cancers using radioimmunotherapy Rhenium-188 (Re-188) Cancer diagnosis and treatment using radioimmunotherapy, bone cancer pain relief, treatment of rheumatoid arthritis, and treatment of prostate cancer Rhodium-105 (Rh-105) Cancer radioimmunotherapy Samarium-145 (Sm-145) Ocular cancer treatment Samarum-153 (Sm-153) Cancer radioimmunotherapy and bone cancer pain relief Scandium-47 (Sc-47) Cancer radioimmunotherapy and bone cancer pain relief Seleniun-75 (Se-75) 7411 Radiotracer used in brain studies, imaging of adrenal cortex by gamma-scintigraphy, lateral locations of steroid secreting tumors, pancreatic scanning, detection of hyperactive parathyroid glands, measure rate of bile acid loss from the endogenous pool Strontium-85 (Sr-85) Bone cancer detection and brain scans Strontium-89 (Sr-89) Bone cancer pain relief, multiple myeloma treatment, and osteoblastic therapy Technetium-99m (Tc-99m) See Molybdenum-99 (Mo-99) Thorium-228 (Th-228) Parent of Bismuth-212 (Bi-212) which is an alpha emitter used in cancer radioimmunotherapy Thorium-27' (Th-229) Parent of Actinium-225 (Ac-225) and grandparent of Bismuth-213 (Bi-213) which are alpha emitters used in cancer radioimmunotherapy Thulium-1 70 ( Tm-170) Gamma source for blood irradiators, energy source for implanted medical devices Tin-1 17m (Sn-1 17m) Cancer immunotherapy and bone cancer pain relief Tungsten-188 (W-i88) Parent for Rhenium-188 (Re-188) which is used for cancer diagnosticsltreatment, bone cancer pain relief, rheumatoid arthritis treatment, and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Xenon-127 (Xe-127) Neuroimaging of brain disorders, high resolution SPECT studies, pulmonary function tests, and cerebral blood flow studies Ytterbium-1 75 (Yb-175) Cancer radioimmunotherapy Yttrium-90 (Y-90) Microseeds obtained from irradiating Yttrium-89 (Y-89) for liver cancer treatment Yttrium-91 (Y-91) A gamma-emitting label for Yttrium-90 (Y-90) which is used for cancer radioimmunotherapy (i.e., lymphoma, breast, colon, kidney, lung, ovarian, prostate, pancreatic, and inoperable liver cancers) 21 By 'randomized" or grammatical equivalents as herein applied to nudeic acids and proteins is meant that each nucleic acid and peptide consists of essentially random nucleotides and amino acids, respectively. These random peptides (or nudeic acids, discussed herein) can incorporate any nucleotide or amino acid at any position. The synthetic process can be designed to generate randomized proteins or nucleic acids, to allow the formation of all or most of the possible combinations over the length of the sequence, thus forming a library of randomized candidate bioactive proteinaceous agents. In one embodiment, a library is "fully randomized,' with no sequence preferences or constants at any position. In another embodiment, the library is a 'biased random" library. That is, some positions within the sequence either are held constant, or are selected from a limited number of possibilities. For example, the nudeotides or amino acid residues are randomized within a defined class, e.g., of hydrophobic amino adds, hydrophilic residues, sterically biased (either small or large) residues, towards the creation of nucleic acid binding domains, the creation of cysteines, for cross-linking, prolines for SH-3 domains, series, threonines, tyrosines or histidines for phosphorylation sites, etc., or to purines, etc. A "recombinant DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vito. Non-limiting examples of small molecules include compounds that bind or interact with 98P486, ligands including hormones, neuropeptides, chemokines, odorants, phospholipids, and functional equivalents thereof that bind and preferably inhibit 98P4B6 protein function. Such non-limiting small molecules preferably have a molecular weight of less than about 10 kDa, more preferably below about 9, about 8, about 7, about 6, about 5 or about 4 kDa. In certain embodiments, small molecules physically associate with, or bind, 98P4B6 protein; are not found in naturally occurring metabolic pathways; and/or are more soluble in aqueous than non-aqueous solutions 'Stringency" of hybridization reactions is readily determinable by one of ordinary skill in the art, and generally is an empirical calculation dependent upon probe length, washing temperature, and salt concentration. In general, longer probes require higher temperatures for proper annealing, while shorter probes need lower temperatures. Hybridization generally depends on the ability of denatured nucleic acid sequences to reanneal when complementary strands are present in an environment below their melting temperature. The higher the degree of desired homology between the probe and hybridizable sequence, the higher the relative temperature that can be used. As a result, it follows that higher relative temperatures would tend to make the reaction conditions more stringent, while lower temperatures less so. For additional details and explanation of stringency of hybridization reactions, see Ausubel et al., Current Protocols in Molecular Biology, Wiley Interscience Publishers, (1995). "Stringent conditions'or "high stringency conditions', as defined herein, are identified by, but not limited to, those that (1) employ low ionic strength and high temperature for washing, for example 0.015 M sodium chloride/0.0015 M sodium citrate/0.1 % sodium dodecyl sulfate at 50OC; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (vlv) formamide with 0.1% bovine serum albumin/0.1% Ficoll/O.1% polyvinylpyrrolidone/50 mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42 OC; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCl, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhardt's solution, sonicated salmon sperm DNA (50 pg/ml), 0.1% SDS, and 10% dextran sulfate at 42 oC, with washes at 42oC in 0.2 x SSC (sodium chloride/sodium. citrate) and 50% formamide at 55 OC, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55 OC. 'Moderately stringent conditions" are described by, but not limited to, those in Sambrook et aL., Molecular Cloning: A Laboratory Manual, New York: Cold Spring Harbor Press, 1989, and include the use of washing solution and hybridization conditions (e.g., temperature, ionic strength and %SDS) less stringent than those described above. An example of moderately stringent conditions is ovemight incubation at 37oC in a solution comprising: 20% formamide, 5 x SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5 x 22 Denhardt's solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in 1 x SSC at about 37-500C. The skilled artisan will recognize how to adjust the temperature, ionic strength, etc. as necessary to accommodate factors such as probe length and the like. An HLA *supermotif' is a peptide binding specificity shared by HLA molecules encoded by two or more HLA alleles. Overall phenotypic frequencies of HLA-supertypes in different ethnic populations are set forth in Table IV (F). The non limiting constituents of various supetypes are as follows: A2: A*0201, A*0202, A*0203, A*0204, A* 0205, A*0206, A*6802, A*6901, A*0207 A3: A3, All, A31, A*3301, A*6801, A*0301, A*1101, A*3101 87: B7, B*3501-03, 8*51, B*5301, B*5401, B*5501, 8*5502, B*5601, B*6701, B*7801, B*0702, B*5101, B*5602 B.44: 8*3701, B*4402, B*4403, 8*60 (8*4001), 861 (8*4006) Al: A*0102, A*2604, A*3601, A*4301, A*8001 A24: A*24, A*30, A*2403, A*2404, A*3002, A*3003 827: B*1401-02, B*1503, B*1509, B*1510, 6*1518, 8*3801-02, B*3901, B*3902, B*3903-04, 8*4801-02, 8*7301, B*2701-08 858: 8*1516, B*1517, 6*5701, 8*5702, B58 B62: B*4601, B52, B*1501 (B62), 8*1502 (875), B*1513 (877) Calculated population coverage afforded by different HLA-supertype combinations are set forth in Table IV (G). As used herein 'to treat" or "therapeutic" and grammatically related terms, refer to any improvement of any consequence of disease, such as prolonged survival, less morbidity, and/or a lessening of side effects which are the byproducts of an alternative therapeutic modality; full eradication of disease is not required. A transgenic animal" (e.g., a mouse or rat) is an animal having cells that contain a transgene, which transgene was introduced into the animal or an ancestor of the animal at a prenatal, e.g., an embryonic stage. A transgene' is a DNA that is integrated into the genome of a cell from which a transgenic animal develops. As used herein, an HLA or celular immune response "vaccine" is a composition that contains or encodes one or more peptides of the invention. There are numerous embodiments of such vaccines, such as a cocktail of one or more individual peptides; one or more peptides of the invention comprised by a polyepitopic peptide; or nucleic acids that encode such individual peptides or polypeptides, e.g., a minigene that encodes a polyepitopic peptide. The "one or more peptides" can include any whole unit integer from 1-150 or more, e.g., at least 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, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, or 150 or more peptides of the invention. The peptides or polypeptides can optionally be modified, such as by lipidation, addition of targeting or other sequences. HLA class I peptides of the invention can be admixed with, or linked to, HLA class 11 peptides, to facilitate activation of both cytotoxic T lymphocytes and helper T lymphocytes. HLA vaccines can also comprise peptide-pulsed antigen presenting cells, e.g., dendritic cells. The term "variant' refers to a molecule that exhibits a variation from a described type or norm, such as a protein that has one or more different amino acid residues in the corresponding position(s) of a specifically described protein (e.g. the 98P486 protein shown in Figure 2 or Figure 3. An analog is an example of a variant protein. Splice isoforms and single nucleotides polymorphisms (SNPs) are further examples of variants. The "98P4B6-related proteins" of the invention include those specifically identified herein, as well as allelic variants, conservative substitution variants, analogs and homologs that can be isolated/generated and characterized without undue experimentation following the methods outlined herein or readily available in the art Fusion proteins that combine parts of different 98P486 proteins or fragments thereof, as well as fusion proteins of a 98P4B6 protein and a heterologous polypeptide are 23 also included. Such 98P486 proteins are collectively referred to as the 98P486-related proteins, the proteins of the invention, or 98P4B6. The term "98P4B6-related protein' refers to a polypeptide fragment or a 98P4B6 protein sequence of 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 amino acids; or, at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90,95, 100, 105, 110, 115,120, 125, 130,135, 140,145, 150, 155, 160, 165,170,175, 180, 185, 190, 195, 200, 225, 250, 275, 300, 325, 350, 375,400, 425, 450, 475, 500, 525, 550, 575, or 576 or more amino acids. 11.) 98P486 Polynucleotides One aspect of the invention provides polynucleotides corresponding or complementary to all or part of a 98P4B6 gene, mRNA, and/or coding sequence, preferably in isolated form, including polynudeotides encoding a 98P486-related protein and fragments thereof, DNA, RNA, DNAIRNA hybrid, and related molecules, polynucleotides or oligonucleotides complementary to a 98P4B6 gene or mRNA sequence or a part thereof, and polynucleotides or oligonudeotides that hybridize to a 98P486 gene, mRNA, or to a 98P4B6 encoding polynucleotide (collectively, '98P486 polynudeotides"). In all instances when referred to in this section, T can also be U in Figure 2. Embodiments of a 98P486 polynudeotide include: a 98P486 polynuceotide having the sequence shown in Figure 2, the nudeoid rluence of 98P4B6 as shown in Figure 2 wherein T is U; at least 10 contiguous nudeotides of a polynudeotide having the sequence as shown in Figure 2; or, at least 10 contiguous nucleotides of a polynucleotide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 98P486 nuceotides comprise, without limitation: (1) a polynudeotide comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2, wherein T can also be U; (II) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (ll) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2B, from nucleotide residue number 4 through nucleotide residue number 138, including the stop codon, wherein T can also be U; (IV) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2C, from nucleotide residue number 188 through nucleotide residue number 1552, including the a stop codon, wherein T can also be U; (V) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2D, from nucleotide residue number 318 through nucleotide residue number 1682, including the stop codon, wherein T can also be U; (VI) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2E, from nucleotide residue number 318 through nudeotide residue number 1577, including the stop codon, wherein T can also be U; (VII) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2F, from nucleotide residue number 318 through nudeotide residue number 1790, induding the stop codon, wherein T can also be U; 24 (Vill) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2G. from nucleotide residue number 295 through nucleotide residue number 2025, induding the stop codon, wherein T can also be U; (IX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2H, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (X) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 21, from nuceotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2J, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2K, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2L, from nudeotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XIV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2M, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2N, from nucleotide residue number 355 through nucleotide residue number 1719, induding the stop codon, wherein T can also be U; (XVI) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 20, from nucleotide residue number 355 through nucleotide residue number 1719, induding the stop codon, wherein T can also be U; (XVII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2P, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 20, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; 25 (XIX) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2R, from nucleotide residue number 355 through nudeotide residue number 1719, including the stop codon, wherein T can also be U; (XX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2S, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XXI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2T, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXII) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2U, from nucleotide residue number 295 through nucleotide residue number 2025, induding the stop codon, wherein T can also be U; (XXII) 'a polynudeotide comprising, consisting essenially of, or consisting of the sequence as shown in Figure 2V, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXIV) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2W, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2X, from nucleotide residue number 295 through nucleotide residue number 2025, including'the stop codon, wherein T can also be U; (XXVI) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2Y, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXVII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2Z, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AA, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXIX) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AB, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; 26 (XXX) a polynuceotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AC, from nucleotide residue number 394 through nucleotide residue number 1866, induding the stop codon, wherein T can also be U; (XXXI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AD. from nucleotide residue number 394 through nudeotide residue number 1866, including the stop codon, wherein T can also be U; (XXXII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AE, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXIII) a polynudeotide comprising, consisting essentially of. or consisting of the sequence as shown in Figure 2AF, from nucleotide residue number 394 through nucleotide residue number 1866, induding the stop codon, wherein T can also be U; (XXIV) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AG, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXV) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AH, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVII) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AJ, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AK, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXIX) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AL, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XL) a polynudeotide that encodes a 98P486-related protein that is at least 90. 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-AL; (XLI) a polynucleotide that encodes a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical to an entire amino acid sequence shown in Figure 2A-AL; 27 (XLII) a polynucleotide that encodes at least one peptide set forth in Tables VIII XXI and XXII-XLIX; (XLIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 5 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes at least 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of 98P4B6v.1, v.2, v.5, v.6 10 and v.7; (XL1V) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment 15 up to 454 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (XLV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 20 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of 98P4B6v. 1, v.2, 25 v.5, v.6 and v.7; (XLVI) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment 30 up to 454 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; 35 (XLVII) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 5 (XLVIII) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 10 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; (XLIX) a polynucleotide that encodes a peptide region of at least 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, 15 35 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 20 (L) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater 25 than 0.5 in the Percent Accessible Residues profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LI) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that 30 includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 35 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 38 in any whole number increment up to 45 that 29 includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 5 (LIII) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater 10 than 0.5 in the Hydrophilicity profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; (LIV) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that 15 includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 20 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that includes 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, 31, 32, 33, 34, 35 amino add position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 25 (LVI) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 30 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; (LVII) a polynucleotide that encodes a peptide region of at least 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 35 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LVIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 5 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 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of 98P4B6v. 1, 10 v.2, v.5, v.6 and v.7; (LIX) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment 15 up to 490 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LX) a polynudeotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 20 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of 98P4B6v.1, v.2, 25 v.5, v.6 and v.7; (LXI) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment 30 up to 490 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 31 (LXII) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 5 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LXIII) a polynucleotide that encodes a peptide region of at least 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, 10 35 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 15 (LXIV) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a 20 value less than 0.5 in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LXV) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 25 576 that includes 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 30 (LXVI) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 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, 31, 32, 33, 34, 35 amino add position(s) having a 35 value greater than 0.5 in the Average Flexibility profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 31A (LXVII) a polynucleotide that encodes a peptide region of at least 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 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 5 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (LXVIII) a polynucleotide that is fully complementary to a polynucleotide of any one of (I)-(LXVII). 10 (LXIX) a peptide that is encoded by any of (1) to (LXVIII); and (LXX) a composition comprising a polynucleotide of any of (I)-(LXVIII) or peptide of (LXIX) together with a pharmaceutical excipient and/or in a human unit 15 dose form. (LXXI) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to modulate a cell expressing 98P4B6, 20 (LXXII) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6 (LXXIII) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of 25 (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6, said cell from a cancer of a tissue listed in Table I; (LXXIV) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of 30 (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat a cancer; (LXXV) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or 35 treat a cancer of a tissue listed in Table I; and, 31B (LXXVI) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to identify or characterize a modulator of a cell expressing 98P4B6. 5 31C As used herein, a range is understood to dispose specifically all whole unit positions thereof. Typical embodiments of the invention disclosed herein include 98P4B6 polynucleotides that encode specific portions of 98P4B6 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: . (a) 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75,80, 85,90, 95, 100, 105,110,115, 120,125,130, 135,140,145,150, 155, 160,165,170,175, 180,185, 1.90,195, 200, 225, 250, 275, 300, 325, 350, 375, 400, 410, 420, 430, 440, 450 or 454 or more contiguous amino acids of 98P4B6 variant 1; the maximal lengths relevant for other variants are: variant 2, 44 amino acids; variant 5, 419 amino acids, variant 6, 490 amino acids, variant 7, 576 amino acids, variant 8, 490 amino acids, variant 13, 454 amino acids, variant 14, 454 amino acids, variant 21, 576 amino acids, and variant 25, 490 amino acids. For example, representative embodiments of the invention disclosed herein include: polynudeotides and their encoded peptides themselves encoding about amino acid 1 to about amino acid 10 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 10 to about amino acid 20 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 20 to about amino acid 30 of the 98P4B6 protein shown in Figure 2 or Figure 3,.polynudeotides encoding about amino acid 30 to about amino acid 40 of the 98P486 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 40 to about amino acid 50 of the 98P486 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 50 to about amino acid 60 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 60 to about amino acid 70 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 70 to about amino acid 80 of the 98P486 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 80 to about amino acid 90 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 90 to about amino acid 100 of the 98P4B6 protein shown in Figure 2 or Figure 3, in increments of about 10 amino acids, ending at the carboxyl terminal amino acid set forth in Figure 2 or Figure 3. Accordingly, polynudeotides encoding portions of the amino acid sequence (of about 10 amino acids), of amino acids, 100 through the carboxyl terminal amino acid of the 98P466 protein are embodiments of the invention. Wherein it is understood that each particular amino acid position discloses that position plus or minus five amino acid residues. Polynucleotides encoding relatively long portions of a 98P4B6 protein are also within the scope of the invention. For example, polynudeotides encoding from about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 30, or 40 or 50 etc.) of the 98P4B6 protein 'or variant shown in Figure 2 or Figure 3 can be generated by a variety of techniques well known in the art. These polynudeotide fragments can include any portion of the 98P4B6 sequence as shown in Figure 2. Additional illustrative embodiments of the invention disclosed herein include 98P4B6 polynucleotide fragments encoding one or more of the biological motifs contained within a 98P4B6 protein "or variant' sequence, including one or more of the motif-bearing subsequences of a 98P4B6 protein 'or varianr set forth in Tables Vill-XXI and XXII-XLIX. In another embodiment, typical polynucleotide fragments of the invention encode one or more of the regions of 98P4B6 protein or variant that exhibit homology to a known molecule. In another embodiment of the invention, typical polynucleotide fragments can encode one or more of the 98P486 protein or variant N-glycosylation sites, cAMP and cGMP-dependent protein kinase phosphorylation sites, casein kinase I phosphorylation sites or N-myristoylation site and amidation sites. Note that to determine the starting position of any peptide set forth in Tables Vill-XXI and Tables XXII to XLIX (coltectively HLA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides listed in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides for a particular variant The position of each Search Peptide relative to its respective parent molecule is listed in Table VII. Accordingly, if a Search Peptide begins at position 'X", one must add the value 'X minus 1" to each position in Tables VIII-XXI and Tables XXII-IL to obtain the actual position of 32 the HLA peptides in their parental molecule. For example if a particular Search Peptide begins at position 150 of its parental molecule, one must add 150 -1, i.e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid in the parent molecule. II.A.) Uses of 98P4B6 Polynucleotides ll.A.1.) Monitoring of Genetic Abnormalities The polynucleotides of the preceding paragraphs have a number of different specific uses. The human 98P4B6 gene maps to the chromosomal location set forth in the Example entitled 'Chromosomal Mapping of 98P4B6." For example, because the 98P486 gene maps to this chromosome, polynudeotides that encode different regions of the 98P4B6 proteins are used to characterize cytogenetic abnormalities of this chromosomal locale, such as abnormalities.that are identified as being associated with various cancers. In certain genes, a variety of chromosomal abnormalities including rearrangements have been identified as frequent cytogenetic abnormalities in a number of different cancers (see e.g. Krajinovic et a., Mutat. Res. 382(3-4): 81-83 (1998); Johansson el al., Blood 86(10): 3905-3914 (1995) and Finger et a., P.N.A.S. 85(23): 9158 9162 (1988)). Thus, polynucleotides encoding specific regions of the 98P4B6 proteins provide new tools that can be used to delineate, with greater precision than previously possible, cytogenetic abnormalities in the chromosomal region that encodes 98P4B6 that may contribute to the malignant phenotype. In this context, these polynucleotides satisfy a need in the art for expanding the sensitivity of chromosomal screening in order to identify more subtle and less common chromosomal abnormalities (see e.g. Evans et a., Am. J. Obstet. Gynecol 171(4): 1055-1057 (1994)). Furthermore, as 98P4B6 was shown to be highly expressed in prostate and other cancers, 98P4B6 polynudeotides are used in methods assessing the status of 98P4B6 gene products in normal versus cancerous tissues. Typically, polynucleotides that encode specific regions of the 98P4B6 proteins are used to assess the presence of perturbations (such as deletions, insertions, point mutations, or alterations resulting in a loss of an antigen etc.) in specific regions of the 98P4B6 gene, such as regions containing one or more motifs. Exemplary assays include both RT-PCR assays as well as single-strand conformation polymorphism (SSCP) analysis (see, e.g., Marrogi et a., J. Cutan. Pathol. 26(8): 369-378 (1999), both of which utilize polynucleotides encoding specific regions of a protein togxamine these regions within the protein. II.A.2.) Antisense Embodiments Other specifically contemplated nucleic acid related embodiments of the invention disclosed herein are genomic DNA, cDNAs, ribozymes, and antisense molecules, as well as nudeic acid molecules based on an alternative backbone, or including alternative bases, whether derived from natural sources or synthesized, and include molecules capable of inhibiting the RNA or protein expression of 98P4B6. For example, antisense molecules can be RNAs or other molecules, including peptide nucleic acids (PNAs) or non-nucleic acid molecules such as phosphorothioate derivatives that specifically bind DNA or RNA in a base pair-dependent manner. A skilled artisan can readily obtain these passes of nudeic acid molecules using the 98P486 polynudeotides and polynudeotide sequences disclosed herein. Antisense technology entails the administration of exogenous oligonudeotides that bind to a target polynucleotide located within the cells. The term 'antisense" refers to the fact that such oligonucleotides are complementary to their intracellular targets, e.g., 98P4B6. See for example, Jack Cohen, Oligodeoxynucleotides, Antisense Inhibitors of Gene Expression, CRO Press, 1989; and Synthesis 1:1-5 (1988). The 98P4B6 antisense oligonudeotides of the present invention include derivatives such as S-oligonucleotides (phosphorothioate derivatives or S-oligos, see, Jack Cohen, supra), which exhibit enhanced cancer cell growth inhibitory action. S-oligos (nucleoside phosphorothioates) are isoelectronic analogs of an oligonudeotide (0-oligo) in which a nonbridging oxygen atom of the phosphate group is replaced by a sulfur atom. The S-oligos of the present invention can be prepared by treatment of the corresponding 0-oligos with 3H-1,2-benzodithiol-3-one 1,1-dioxide, which is a sulfur transfer reagent. See, e.g., lyer, R. P. et a., J. Org. Chem. 55:4693-4698 (1990); and lyer, R. 33 P. et al., J. Am. Chem. Soc. 112:1253-1254 (1990). Additional 98P4B6 antisense oligonucleotides of the present invention indude morpholino antisense oligonucleotides known in the art (see, e.g., Partridge et al., 1996, Antisense & Nucleic Acid Drug Development 6: 169-175). The 98P416 antisense oligonucleotides of the present invention typically can be RNA or DNA that is complementary to and stably hybridizes with the first 100S' codons or last 100 3' coons of a 98P486 genomic sequence or the corresponding mRNA. Absolute complementarity is not required, although high degrees of complementarity are preferred. Use of an oligonucleotide complementary to this region allows for the selective hybridization to 98P4B6 mRNA and not to mRNA specifying other regulatory subunits of protein kinase. In one embodiment, 98P4B6 antisense oligonudeotides of the present invention are 15 to 30-mer fragments of the antisense DNA molecule that have a sequence that hybridizes to 98P486 mRNA. Optionally, 98P486 antisense oligonucleotide is a 30-mer oligonucleotide that is complementary to a region in the first 10 5' codons or last 103' coons of 98P486. Alternatively, the antisense molecules are modified to employ ribozymes in the inhibition of 98P4B6 expression, see, e.g., L A. Couture & D. T. Stinchcomb; Trends Genet 12: 510-515 (1996). II.A.3.) Primers and Primer Pairs Further specific embodiments of these nucleotides of the invention include primers and primer pairs, which allow the specific anipification of polynucleotides of the invention or of any specific parts thereof, and probes that selectively or specifically hybridize to nucleic acid molecules of the invention or to any part thereof. Probes can be labeled with a detectable marker, such as, for example, a radioisotope, fluorescent compound, bioluminescent compound, a chemiluminescent compound, metal chelator or enzyme. Such probes and primers are used to detect the presence of a 98P486 polynucleotide in a sample and as a means for detecting a cell expressing a 98P486 protein. Examples of such probes include polypeptides comprising all or part of the human 98P4B6 cDNA sequence shown in Figure 2 Examples of primer pairs capable of specifically amplifying 98P4B6 mRNAs are also described in the Examples. As will be understood by the skilled artisan, a great many different primers and probes can be prepared based on the sequences provided herein and used effectively to amplify and/or detect a 98P4B6 mRNA. The 98P486 polynucleotides of the invention are useful for a variety of purposes, including but not limited to their use as probes and primers for the amplification and/or detection of the 98P4B6 gene(s), mRNA(s), or fragments thereof, as reagents for the diagnosis and/or prognosis of prostate cancer and other cancers; as coding sequences capable of directing the expression of 98P4B6 polypeptides; as tools for modulating or inhibiting the expression of the 98P4B6 gene(s) and/or translation of the 98P486 transcript(s); and as therapeutic agents. The present invention includes the use of any probe as described herein to identify and isolate a 98P4B6 or 98P486 related nucleic acid sequence from a naturally occurring source, such as humans or other mammals, as well as the isolated nucleic acid sequence per so, which would comprise all or most of the sequences found in the probe used. II.A.4.) Isolation of 98P4B6-Encoding Nucleic Acid Molecules The 98P4B6 cDNA sequences described herein enable the isolation of other polynudeotides encoding 98P416 gene product(s), as well as the isolation of polynudeotides encoding 98P4B6 gene product homologs, alternatively spliced isoforms, allelic variants, and mutant forms of a 98P4B6 gene product as well as polynudeotides that encode analogs of 98P4B6-related proteins. Various molecular cloning methods that can be employed to isolate full length cDNAs encoding a 98P486 gene are well known (see, for example, Sambrook, J. et al., Molecular Cloning: A Laboratory Manual, 2d edition, Cold Spring Harbor Press, New York, 1989; Current Protocols in Molecular Biology. Ausubel et al., Eds., Wiley and Sons, 1995). For example, lambda phage cloning methodologies can be conveniently employed, using commercially available cloning systems (e.g., Lambda ZAP Express, Stratagene). Phage clones containing 98P4B6 gene cDNAs can be identified by probing with a labeled 98P416 cDNA or a fragment thereof. For example, in one embodiment, a 98P486 cDNA (e.g., Figure 2) or a portion thereof can be synthesized 34t and used as a probe to retrieve ovedapping and full-length cDNAs corresponding to a 98P4B6 gene. A 98P4B6 gene itself can be isolated by screening genomic DNA libraries, bacterial artificial chromosome libraries (BACs), yeast artificial chromosome libraries (YACs), and the like, with 98P4B6 DNA probes or primers. iLA.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems The invention also provides recombinant DNA or RNA molecules containing a 98P486 polynucleotide, a fragment, analog or homologue thereof, including but not limited to phages, plasmids, phagemids, cosmids, YACs, BACs, as well as various viral and non-viral vectors well known in the art, and cells transformed or transfecled with such recombinant DNA or RNA molecules. Methods for generating such molecules are well known (see, for example, Sambrook et al., 1989, supra). The invention further provides a host-vector system comprising a recombinant DNA molecule-containing a 98P486 polynucleotide, fragment, analog or homologue thereof within a suitable prokaryotic or eukaryofic host cell. Examples of suitable eukaryotic host cells include a yeast cell, a plant cell, or an animal cell, such as a mammalian cell or an insect cell (e.g., a baculovirus-infectible cell such as an Sf9 or HighFive cell). Examples of suitable mammalian cells include various prostate cancer cell lines such as DU145 and TsuPr1, other transfectable or transducible prostate cancer cell lines, primary cells (PrEC), as well as a number of mammalian cells routinely used for the expression of recombinant proteins (e.g., COS, CHO, 293, 293T cells). More particularly, a polynucleotide comprising the coding sequence of 98P4B6 or a fragment, analog or homolog thereof can be used to generate 98P4B6 proteins or fragments thereof using any number of host-vector systems routinely used and widely known in the art. A wide range of host-vector systems suitable for the expression of 98P4B6 proteins or fragments thereof are available, see for example, Sambrook et al., 1989, supra; Current Protocols in Molecular Biology, 1995, supra). Preferred vectors for mammalian expression include but are not limited to pcDNA 3.1 myc-His-tag (Invitrogen) and the retroviral vector pSRatkneo (Muller et al., 1991, MCB 11:1785). Using these expression vectors, 98P4B6 can be expressed in several prostate cancer and non-prostate cell lines, including for example 293, 293T, rat-1, NIH 3T3 and TsuPr1. The host-vector systems of the invention are useful for the production of a 98P486 protein or fragment thereof. Such host-vector systems can be employed to study the functional properties of 98P4B6 and 98P4B6 mutations or analogs. Recombinant human 98P4B6 protein or an analog or homolog or fragment thereof can be produced by mammalian cells transfected with a construct encoding a 98P4B6-related nucleotide. For example, 293T cells can be transfected with an. expression plasmid encoding 98P4B6 or fragment, analog or homolog thereof, a 98P4B6-related protein is expressed in the 293T cells, and the recombinant 98P486 protein is isolated using standard purification methods (e.g., affinity purification using anti-98P4B6 antibodies). In another embodiment, a 98P4B6 coding sequence is subcloned into the retroviral vector pSRcaMSVlkneo and used to infect various mammalian cell lines, such as NIH 3T3, TsuPr1, 293 and rat-1 in order to establish 98P4B6 expressing cell lines. Various other expression systems well known in the art can also be employed. Expression constructs encoding a leader peptide joined in frame to a 98P486 coding sequence can be used for the generation of a secreted form of recombinant 98P486 protein. As discussed herein, redundancy in the genetic code permits variation in 98P486 gene sequences. In particular, it is known in the art that specific host species often have specific codon preferences, and thus one can adapt the disclosed sequence as preferred for a desired host. For example, preferred analog codon sequences typically have rare codons (i.e., codons having a usage frequency of less than about 20% in known sequences of the desired host) replaced with higher frequency codons. Codon preferences for a specific species are calculated, for example, by utilizing codon usage tables available on the INTERNET such as at URL dna.affrc.go.jpl-nakamura/codon.html. Additional sequence modifications are known to enhance protein expression in a cellular host These include elimination of sequences encoding spurious polyadenylation signals, exon/intron splice site signals, transposon-like repeats, and/or other such well-characterized sequences that are deleterious to gene expression. The GC content of the sequence is 35 adjusted to levels average for a given cellular host, as calculated by reference to known genes expressed in the host cell. Where possible, the sequence is modified to avoid predicted hairpin secondary mRNA structures. Other useful modifications include the addition of a translational initiation consensus sequence at the start of the open reading frame, as described in Kozak, Mol. Cell Biol., 9:5073-5080 (1989). Skilled artisans understand that the general rule that eukaryotic ribosomes initiate translation exclusively at the 5' proximal AUG codon is abrogated only under rare conditions (see, e.g., Kozak PNAS 92(7): 2662-2666, (1995) and Kozak NAR 15(20): 8125-8148 (1987)). 1ll.) 98P4B6-related Proteins Another aspect of the present invention provides 98P4B6-related proteins. Specific embodiments of 98P4B6 proteins comprise a polypeptide having aU or part of the amino acid sequence of human 98P4B6 as shown in Figure 2 or Figure 3. Alternatively, embodiments of 98P4B6 proteins comprise variant, homolog or analog polypeptides that have alterations in the amino acid sequence of 98P4B6 shown in Figure 2 or Figure 3. Embodiments of a 98P486 polypeptide include: a 98P486 polypeptide having a sequence shown in Figure 2, a peptide sequence of a 98P416 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polypeptide having the sequence as shown in Figure 2; or, at least 10 contiguous peptides of a polypeptide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 98P4B6 peptides comprise, without limitation: (I) a protein comprising, consisting essentially of, or consisting of an amino acid sequence as shown in Figure 2A-AL or Figure 3A-J; (II) a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98,99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-AL; (ll) a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical to an entire amino acid sequence shown in Figure 2A-AL or 3A-J; (IV) a protein that comprises at least one peptide set forth in Tables Vill to XLIX, optionally with a proviso that it is not an entire protein of Figure 2; (V) a protein that comprises at least one peptide set forth in Tables VIII-XXI, collectively, which peptide is also set forth in Tables XXII to XLIX, collectively, optionally with a proviso that it is not an entire protein of Figure 2; (VI) a protein that comprises at least two peptides selected from the peptides set forth in Tables Vill-XLIX, optionally with a proviso that it is not an entire protein of Figure 2; (VII) a protein that comprises at least two peptides selected from the peptides set forth in Tables Vill to XLIX collectively, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (Vill) a protein that comprises at least one peptide selected from the peptides set forth in Tables VIII-XXI; and at least one peptide selected from the peptides set forth in Tables XXII to XLIX, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (IX) a polypeptide comprising at least 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 amino acids of a protein of Figure 3A, 38, 3C, 3D, 3E, 3F, 3G, 3H; 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 5 (X) a polypeptide comprising at least 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 amino acids of a protein of Figure 3A, 3B. 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 10 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; (XI) a polypeptide comprising at least 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 amino acids of a 15 protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of 98P4B6v.1, v.2, 20 v.5, v.6 and v.7; (XII) a polypeptide comprising at least 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 amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number 25 increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 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, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; 30 (XIII) a polypeptide comprising at least 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, amino acids of a protein of Figure 3A, 3B. 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least 35 at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 37 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; (XIV) a peptide that occurs at least twice in Tables VII-XXI and XXII to XLIX, 5 collectively; (XV) a peptide that occurs at least three times in Tables VII-XXI and XXI to XLIX, collectively; 10 (XVI) a peptide that occurs at least four times in Tables VIII-XXI and XXII to XLIX, collectively; (XVII) a peptide that occurs at least five times in Tables VIII-XXI and XXII to XLIX, collectively; 15 (XVIII) a peptide that occurs at least once in Tables VIII-XXI, and at least once in tables XXII to XLIX; (XIX) a peptide that occurs at least once in Tables VIII-XXI, and at least twice in 20 tables XXII to XLIX; (XX) a peptide that occurs at least twice in Tables VIH-XXI, and at least once in tables XXII to XLIX; 25 (XXI) a peptide that occurs at least twice in Tables VIII-XXI, and at least twice in tables XXII to XLIX; (XXII) a peptide which comprises one two, three, four, or five of the following characteristics, or an oligonucleotide encoding such peptide: 30 i) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; 35 ii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes 38 an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a value equal to 0.0, in the Hydropathicity profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; iii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any 5 whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Percent Accessible Residues profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; iv) a region of at least 5 amino acids of a particular peptide of Figure 3, in any 10 whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of 98P4B6v.1, v.2, v.5, v.6 and v.7; v) a region of at least 5 amino acids of a particular peptide of Figure 3, in any 15 whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Beta-turn profile of 98P4B6v. 1, v.2, v.5, v.6 and v.7; (XXIII) a composition comprising a peptide of (I)-(XXII) or an antibody or binding 20 region thereof together with a pharmaceutical excipient and/or in a human unit dose form. (XXIV) a method of using a peptide of (I)-(XXII), or an antibody or binding region thereof or a composition of (XXIII) in a method to modulate a cell expressing 98P4B6, 25 (XXV) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6 30 (XXVI) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition (XXIII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6, said cell from a cancer of a tissue listed in Table I; 38A (XXVII) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat a cancer; 5 (XXVIII) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat a cancer of a tissue listed in Table I; and, (XXIX) a method of using a peptide of (I)-(XXII) or an antibody or binding region 10 thereof or a composition (XXIII) in a method to identify or characterize a modulator of a cell expressing 98P4B6. As used herein, a range is understood to specifically disclose all whole unit positions thereof. 15 Typical embodiments of the invention disclosed herein include 98P4B6 polynucleotides that encode specific portions of 98P4B6 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: (a) 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 20 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 38B 225, 250, 275, 300, 325, 350, 375, 400, 410,420, 430,440, 450, or 454 more contiguous amino acids of 98P4B6 variant 1; the maximal lengths relevant for other variants are: variant 52, 45 amino acids; variant 5, 419 amino acids, variant 6, 490, variant 7, 576 amino acids, variant 8, 490 amino acids, variant 13, 454, variant 14, 454 amino acids, variant 21, 576 amino acids, and variant 25, 490 amino acids.. In general, naturally occurring allelic variants of human 98P4B6 share a high degree of stuctural identity and homology (e.g., 90% or more homology). Typically, allelic variants of a 98P4B6 protein contain conservative amino acid substitutions within the 98P4B6 sequences described herein or contain a substitution of an amino acid from a corresponding position in a homologue of 98P486. One class of 98P4B6 allelic variants are proteins that share a high degree of homology with at least a small region of a particular 98P486 amino acid sequence, but further contain a radical departure from the sequence, such as a non-conservative substitution, truncation, insertion or frame shift. In comparisons of protein sequences, the terms, similarity, identity, and homology each have a distinct meaning as appreciated in the field of genetics. Moreover, orthology and paraogy can be important concepts describing the relationship of members of a given protein family in one organism to the members of the same family in other organisms. Amino acid abbreviations are provided in Table 11. Conservative amino acid substitutions can frequency be made in a protein without altering either the conformation or the function of the protein. Proteins of the invention can comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15 conservative substitutions. Such changes include substituting any of isoleucine (1), valine (V), and leucine (L) for any other of these hydrophobic amino acids; aspartc acid (D) for glutamic acid (E) and vice versa; glutamine (Q) for asparagine (N) and vice versa; and seine (S) for threonine (T) and vice versa. Other substitutions can also be considered conservative, depending on the environment of the particular amino acid and its role in the three dimensional structure of the protein. For example, glycine (G) and alanine (A) can frequently be interchangeable, as can alanine (A) and valine (V). Methionine (M), which is relatively hydrophobic, can frequently be interchanged with leucine and isoleucine, and sometimes with valine. Lysine (K) and arginine (R) are frequently interchangeable in locations in which the significant feature of the amino acid residue is its charge and the differing pK's of these two amino acid residues are not significant. Still other changes can be considered "conservative' in particular environments (see, e.g Aable Il herein; pages 13-15"Biochemistry" 2nd ED. Lubert Stryer ed (Stanford University); Henikoff et al., PNAS 1992 Vol 89 10915-10919; Lei et al., J Biol Chem 1995 May 19; 270(20):11882-6). Embodiments of the invention disposed herein include a wide variety of art-accepted variants or analogs of 98P4B6 proteins such as polypeptides having amino acid insertions, deletions and substitutions. 98P4B6 variants can be made using methods known in the art such as site-directed mutagenesis, alanine scanning, and PCR mutagenesis. Site directed mutagenesis (Carter et a., Nucl. Acids Res., 13:4331 (1986); Zoller et al., Nuc. Acids Res., 10:6487 (1987)), cassette mutagenesis (Wells et al., Gene, 34:315 (1985)), restriction selection mutagenesis (Wells et al., Philos. Trans. R. Soc. London SerA, 317:415 (1986)) or other known techniques can be performed on the cloned DNA to produce the 98P4B6 variant DNA. Scanning amino acid analysis can also be employed to identify one or more amino acids along a contiguous sequence that is involved in a specific biological activity such as a protein-protein interaction. Among the preferred scanning amino acids are relatively small, neutral amino acids. Such amino acids include alanine, glycine, seine, and cysteine. Alanine is typically a preferred scanning amino acid among this group because it eliminates the side-chain beyond the beta carbon and is less likely to alter the main-chain conformation of the variant. Alanine is also typically preferred because it is the most common amino acid. Further, it is frequently found in both buried and exposed positions (Creighton, The Proteins, (W.H. Freeman & Co., N.Y.); Chothia, J. Mol. Biol., 150:1 (1976)). If alanine substitution does not yield adequate amounts of variant, an isosteic amino acid can be used. 39 As defined herein, 98P486 variants, analogs or homologs, have the distinguishing attribute of having at least one epitope that is 'cross reactive" with a 98P4B6 protein having an amino acid sequence of Figure 3. As used in this sentence, "cross reactive" means that an antibody or T cell that specifically binds to a 98P4B6 variant also specifically binds to a 98P486 protein having an amino acid sequence set forth in Figure 3. A polypeptide ceases to be a variant of a protein shown in Figure 3, when it no longer contains any epitope capable of being recognized by an antibody or T cell that specifically binds to the starting 98P4B6 protein. Those skilled in the art understand that antibodies that recognize proteins bind to epitopes of varying size, and a grouping of the order of about four or five amino acids, contiguous or not, is regarded as a typical number of amino acids in a minimal epitope. See, e.g., Nair et al., J. Immunol 2000 165(12): 6949-6955; Hebbes et a., Mol Immunol (1989) 26(9):865-73; Schwartz et a., J Immunol (1985) 135(4):2598-608. Other classes of 98P4B6-related protein variants share 70%, 75%, 80%, 85% or 90% or more similarity with an amino acid sequence of Figure 3, or a fragment thereof. Another specific class of 98P4B6 protein variants or analogs comprises one or more of the 98P4B6 biological motifs described herein or presently known in the art. Thus, encompassed by the present invention are analogs of 98P4B6 fragments (nucleic or amino acid) that have altered functional (e.g. immunogenic) properties relative to the starting fragment. It is to be appreciated that motifs now or which become part of the art are to be applied to the nucleic or amino acid sequences of Figure 2 or Figure 3. As discussed herein, embodiments of the claimed invention include polypeptides containing less than the full amino acid sequence of a 98P4B6 protein shown in Figure 2 or Figure 3. For example, representative embodiments of the invention comprise peptides/proteins having any 4, 5, 6,7,8, 9,10, 11, 12, 13, 14, 15 or more contiguous amino acids of a 98P4B6 protein shown in Figure 2 or Figure 3. Moreover, representative embodiments of the invention disclosed herein include polypeptides consisting of about amino acid I to about amino acid 10 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 10 to about amino acid 20 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 20 to about amino acid 30 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 30 to about amino acid 40 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 40 to about amino acid 50 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 50 to about amino acid 60 of a 98P486 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 60 to about amino acid 70 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 70 to about amino acid 80 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 80 to about amino acid 90 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 90 to about amino acid 100 of a 98P4B6 protein shown in Figure 2 or Figure 3, etc. throughout the entirety of a 98P4B6 amino acid sequence. Moreover, polypeptides consisting of about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 130, or 140 or 150 etc.) of a 98P4B6 protein shown in Figure 2 or Figure 3 are embodiments of the invention. It is to be appreciated that the starting and stopping positions in this paragraph refer to the specified position as well as that position plus or minus 5 residues. 98P4B6-related proteins are generated using standard peptide synthesis technology or using chemical cleavage methods well known in the art Altematively, recombinant methods can be used to generate nucleic acid molecules that encode a 98P4B6-related protein. In one embodiment nudeic acid molecules provide a means to generate defined fragments of a 98P4B6 protein (or variants, homologs or analogs thereof). Ill.A.) Motif-bearinq Protein Embodiments Additional illustrative embodiments of the invention disclosed herein include 98P4B6 polypeptides comprising the amino acid residues of one or more of the biological motifs contained within a 98P486 polypeptide sequence set forth in Figure 2 or Figure 3. Various motifs are known in the art, and a protein can be evaluated for the presence of such motifs by 40 a number of publicly available Internet sites (see, e g., URL addresses: pfam.wusfl.edul; searchlauncher.bcm.tmc.edu/seq search/struc-predict.html; psortims.u-tokyo.ac.jp/; cbs.dtu.dkl; ebi.ac.uklinterprolscan.htm; expasy.ch/toofs/scnpsitl.html; Epimatrix" and Epimer7M, Brown University, brown.edu/Research/TB-HIVLab/epimarix/epmatixhtml; and BIMAS, bimas.dcrt.nih.gov/.). Motif bearing subsequences of all 98P4B6 variant proteins are set forth and identified in Tables Vill-XXI and XXII XLIX. Table V sets forth several frequently occurring motifs based on pfam searches (see URL address pfam.wusti.edu/). The columns of Table V list (1) motif name abbreviation, (2) percent identity found amongst the different member of the motif family, (3) motif name or description and (4) most common function; location information is included if the motif is relevant for location. Polypeptides comprising one or more of the 98P4B6 motifs discussed above are useful in elucidating the specific characteristics of a malignant phenotype in view of the observation that the 98P486 motifs discussed above are associated with growth dysregulation and because 98P4B6 is overexpressed in certain cancers (See, e.g., Table I). Casein kinase 11, cAMP and camp-dependent protein kinase, and Protein Kinase C, for example, are enzymes known to be associated with the development of the malignant phenotype (see e.g. Chen et al., Lab Invest., 78(2): 165-174 (1998); Gaiddon et al., Endocrinology 136(10): 4331-4338 (1995); Hall et al., Nucleic Acids Research 24(6): 1119-1126 (1996); Peterziel et aL., Oncogene 18(46): 6322-6329 (1999) and O'Brian, Oncol. Rep. 5(2): 305-309 (1998)). Moreover, both glycosylation and myristoylation are protein modifications also associated with cancer and cancer progression (see e.g. Dennis et al., Biochem. Biophys. Acta 1473(1):21-34 (1999); Raju et al., Exp. Cell Res. 235(1): 145-154 (1997)). Amidation is another protein modification also associated with cancer and cancer progression (see e.g. Treston et al., J. Natl. Cancer Inst. Monogr. (13): 169-175 (1992)). In another embodiment, proteins of the invention comprise one or more of the immunoreactive epitopes identified in accordance with art-accepted methods, such as the peptides set forth in Tables VIII-XXI and XXIl-XLIX CTL epitopes can be determined using specific algorithms to identify peptides within a 98P4B6 protein that are capable of optimally binding to specified HLA alleles (e.g., Table IV; Epimatrix T m and Epimer"4, Brown University, URL brown.edu/Research/TB HIV_Lablepimatrixlepimatrix.html; and BIMAS, URL bimas.dcitnih.govl.) Moreover, processes for identifying peptides that have sufficient binding affinity for HLA molecules and which are correlated with being immunogenic epitopes, are well known in the art, and are carried out without undue experimentation. In addition, processes for identifying peptides that are immunogenic epitopes, are well known in the art, and are carried out without undue experimentation either in vitro or in vivo. Also known in the art are principles for creating analogs of such epitopes in order to modulate immunogenicity. For example, one begins with an epitope that bears a CTL or HTL motif (see, e.g., the HLA Class I and HLA Class Il motifs/supermotifs of Table IV). The epitope is analoged by substituting out an amino acid at one of the specified positions, and replacing it with another amino acid specified for that position. For example, on the basis of residues defined in Table IV, one can substitute out a deleterious residue in favor of any other residue, such as a preferred residue; substitute a less preferred residue with a preferred residue; or substitute an originally-occurring preferred residue with another preferred residue. Substitutions can occur at primary anchor positions or at other positions in a peptide; see, e.g., Table IV. A variety of references reflect the art regarding the identification and generation of epitopes in a protein of interest as well as analogs thereof. See, for example, WO 97/33602 to Chesnut et a.; Sette, Immunogenetics 1999 50(3-4): 201 212; Sette et al., J. Immunol. 2001 166(2): 1389-1397; Sidney et al., Hum. Immunol. 1997 58(1): 12-20; Kondo et al., Immunogenetics 1997 45(4): 249-258; Sidney et al., J. Immunol. 1996 157(8): 3480-90; and Falk et al., Nature 351: 290-6 (1991); Hunt et al, Science 255:1261-3 (1992); Parker et al., J. Immunol. 149:3580-7 (1992); Parker el al., J. Immunol. 152:163-75 (1994)); Kast et al., 1994 152(8): 3904-12; Borras-Cuesta et aL., Hum. Immunol. 2000 61(3): 266-278; Alexander 41 et aL., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et al., PMID: 7895164, Ut: 95202582; O'Sullivan et aL., J. Immunol. 1991 147(8): 2663-2669; Alexander et aL, Immunity 1994 1(9): 751-761 and Alexander et aL., Immunol. Res. 1998 18(2): 79-92. Related embodiments of the invention include polypeptides comprising combinations of the different motifs set forth in Table VI, and/or, one or more of the predicted CTL epitopes of Tables Vill-XXI and XXII-XLIX, and/or, one or more of the predicted HTL epitopes of Tables XLVI-XLIX, and/or, one or more of the T cell binding motifs known in the art. Preferred embodiments contain no insertions, deletions or substitutions either within the motifs or within the intervening sequences of the polypeptides. In addition, embodiments which include a number of either N-terminal and/or C-terminal amino acid residues on either side of these motifs may be desirable (to, for example, include a greater portion of the polypeptide architecture in which the motif is located). Typically, the number of N-terminal and/or C-terminal amino acid residues on either side of a motif is between about 1 to about 100 amino acid residues, preferably 5 to about 50 amino acid residues. 98P486-related proteins are embodied in many forms, preferably in isolated form. A purified 98P486 protein molecule will be substantially free of other proteins or molecules that impair the binding of 98P486 to antibody, T cell or other ligand. The nature and degree of isolation and purification will depend on the intended use. Embodiments of a 98P486-related proteins include purified 98P486-related proteins and functional, soluble 98P486-related proteins. In one embodiment, a functional, soluble 98P4B6 protein or fragment thereof retains the ability to be bound by antibody, T cell or other ligand. The invention also provides 98P4B6 proteins comprising biologically active fragments of a 98P4B6 amino acid sequence shown in Figure 2 or Figure 3. Such proteins exhibit properties of the starting 98P4B6 protein, such as the ability to elicit the generation of antibodies that specifically bind an epitope associated with the starting 98P4B6 protein; to be bound by such antibodies; to elicit the activation of HTL or CTL; and/or, to be recognized by HTL or CTL that also specifically bind to the starting protein. 98P4B6-related polypeptides that contain particularly interesting structures can be predicted and/or identified using various analytical techniques well known in the art including, for example, the methods of Chou-Fasman, Gamier-Robson, Kyle Doolittle, Eisenberg, Karplus-Schultz or Jameson-Wolf analysis, or based on immunogenicity. Fragmentshat contain such structures are particularly useful in generating subunit-specific ant-98P4B6 antibodies or T cells or in identifying cellular factors that bind to 98P4B6. For example, hydrophilicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Hopp, T.P. and Woods, K.R., 1981, Proc. Nati. Acad. Sci. U.S.A. 78:3824-3828. Hydropathicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Kyte, J. and Doolitte, R.F., 1982, J. Mol. Biol. 157:105-132. Percent (%) Accessible Residues profiles can be generated, and immunogenic peptide fragments identified, using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated, and immunogenic peptide fragments identified, using the method of Bhaskaran R., Ponnuswamy P.K., 1988, Int. J. Pept. Protein Res. 32:242-255. Beta-tum profiles can be generated, and immunogenic peptide fragments identified, using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. CTL epitopes can be determined using specific algorithms to identify peptides within a 98P4B6 protein that are capable of optimally binding to specified HLA alleles (e.g., by using the SYFPEITHI site at World Wide Web URL syfpeithi.bmi heidelberg.com/; the listings in Table IV(ANE); Epimatrix7" and Epimer m , Brown University, URL (brown.edu/Research/TB HIVLab/epimatrixlepimatrix.htm); and BIMAS, URL bimas.dcrtnih gov/. IlUustrating this, peptide epitopes from 98P486 that are presented in the context of human MHC Class I molecules, e.g., HLA-A1, A2, A3, Al1, A24, B7 and B35 were predicted (see, e.g., Tables Vill-XXI, XXII-XLIX). Specifically, the complete amino acid sequence of the 98P4B6 protein and relevant portions of other variants, i.e., for HLA Class I predictions 9 flanking residues on either side of a point mutation or exon juction, and for HLA Class It predictions 14 flanking residues on either side of a point mutation or exon junction corresponding to that variant, were entered into the HLA Peptide Motif Search algorithm found in the Bioinformatics and 42 Molecular Analysis Section (BIMAS) web site listed above; in addition to the site SYFPEITHI, at URL syfpeithi.bmi heidelberg.com/. The HLA peptide motif search algorithm was developed by Dr. Ken Parker based on binding of specific peptide sequences in the groove of HLA Class I molecules, in particular HLA-A2 (see, e.g., Falk et al., Nature 351: 290-6 (1991); Hunt et al., Science 255:1261-3 (1992); Parker el al., J. Immunol. 149:3580-7 (1992); Parker et al., J. Immunol. 152:163-75 (1994)). This algorithm allows location and ranking of 8-mer, 9-mer, and 10-mer peptides from a complete protein sequence for predicted binding to HLA-A2 as well as numerous other HLA Class I molecules. Many HLA class I binding peptides are 8 ,9-, 10 or 1 1-mers. For example, for Class I HLA-A2, the epitopes preferably contain a leucine (L) or methionine (M) at position 2 and a valine (V) or leucine (L) at the C-terminus (see, e.g., Parker et al., J. Immunol. 149:3580-7 (1992)). Selected results of 98P486 predicted binding peptides are shown in Tables Vill-XXI and XXII-XLIX herein. In Tables VIII-XXI and XXII-XLVII, selected candidates, 9-mers and 1O-mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. In Tables XLVI-XLIX, selected candidates, 15 mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. The binding. score corresponds to the estimated half time of dissociation of complexes containing the peptide at 370C at pH 6.5. Peptides with the highest binding score are predicted to be the most tightly bound to HLA Class I on the cell surface for the greatest period of time and thus represent the best immunogenic targets for T-cell recognition. Actual binding of peptides to an HLA allele can be evaluated by stabilization of HLA expression on the antigen processing defective cell line T2 (see, e.g., Xue et aL., Prostate 30:73-8 (1997) and Peshwa et al., Prostate 36:129-38 (1998)). Immunogenicity of specific peptides can be evaluated in vitro by stimulation of CD8+ cytotoxic T lymphocytes (CTL) in the presence of antigen presenting cells such as dendritic cells. It is to be appreciated that every epitope predicted by the BIMAS site, Epimerr" and EpimatrixTM sites, or specified by the HLA class I or class 11 motifs available in the art or which become part of the art such as set forth in Table IV (or determined using World Wide Web site URL syfpeithi.bmi-heidelberg.coml, or BIMAS, bimas.dcrt.nih.gov/) are to be 'applied" to a 98P486 protein in accordance with the invention. As used in this context "applied" means that a 98P4B6 protein is evaluated, e.g., visually or by computer-based patterns finding methods, as appreciated by those of skill in the relevant art. Every subsequence of a 98P4B6 protein of 8, 9, 10, or 11 amino acid residues that bears an HLA Class I motif, or a subsequence of 9 or more amino acid residues that bear an HLA Class Il motif are within the scope of the invention. lif.B.) Expression of 98P4B6-related Proteins In an embodiment described in the examples that follow, 98P4B6 can be conveniently expressed in cells (such as 293T cells) transfected with a commercially available expression vector such as a CMV-driven expression vector encoding 98P486 with a C-terminal 6XHis and MYC tag (pcDNA3. 1/mycHIS, Invitrogen or Tag5, GenHunter Corporation, Nashville TN). The Tag5 vector provides an IgGK secretion signal that can be used to facilitate the production of a secreted 98P4B6 protein in transfected cells. The secreted HIS-tagged 98P4B6 in the culture media can be purified, e.g., using a nickel column using standard techniques. IlI.C.) Modifications of 98P486-related Proteins Modifications of 98P4B6-related proteins such as covalent modifications are included within the scope of this invention. One type of covalent modification includes reacting targeted amino acid residues of a 98P4B6 polypeptide with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of a 98P4B6 protein. Another type of covalent modification of a 98P4B6 polypeptide included within the scope of this invention comprises 43 altering the native glycosylation pattern of a protein of the invention. Another type of covalent modification of 98P4B6 comprises linking a 98P486 polypeptide to one of a variety of nonproteinaceous polymers, e.g., polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes, in the manner set forth in U.S. Patent Nos. 4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192 or 4,179,337. The 98P486-related proteins of the present invention can also be modified to form a chimeric molecule comprising 98P4B6 fused to another, heterologous polypeptide or amino acid sequence. Such a chimeric molecule can be synthesized chemically or recombinantly. A chimeric molecule can have a protein of the invention fused to another tumor-associated antigen or fragment thereof. Altematively, a protein in accordance with the invention can comprise a fusion of fragments of a 98P4B6 sequence (amino or nucleic acid) such that a molecule is created that is not, through its length, directly homologous to the amino or nucleic acid sequences shown in Figure 2 or Figure 3. Such a chimeric molecule can comprise multiples of the same subsequence of 98P4B6. A chimeric molecule can comprise a fusion of a 98P4B6-related protein with a polyhistidine epitope tag, which provides an epitope to which immobilized nickel can selectively bind, with cytokines or with growth factors. The epitope tag is generally placed at the amino- or carboxy- terminus of a 98P4B6 protein. In an alternative embodiment, the chimeric molecule can comprise a fusion of a 98P4B6-related protein with an immunoglobuin or a particular region of an immunoglobulin. For a bivalent form of the chimeric molecule (also referred to as an 'immunoadhesin"), such a fusion could be to the Fc region of an IgG molecule. The Ig fusions preferably include the substitution of a soluble (transmembrane domain deleted or inactivated) form of a 98P4B6 polypeptide in place of at least one variable region within an Ig molecule. In a preferred embodiment, the immunoglobulin fusion includes the hinge, CH2 and CH3, or the hinge, CHI, CH2 and CH3 regions of an IgGI molecule. For the production of immunoglobulin fusions see, e.g., U.S. Patent No. 5,428,130 issued June 27, 1995. Ill.D.) Uses of 98P4B6-related Proteins The proteins of the invention have a number of different specific uses. As 98P4B6 is highly expressed in prostate and other cancers, 98P4B6-related proteins are used in methods that assess the status of 98P4B6 gene products. in normal versus cancerous Ussues, thereby elucidating the malignant phenotype. Typically, polypeptides from specific regions of a 98P416 protein are used to assess the presence of perturbations (such as deletions, insertions, point mutations etc.) in those regions (such as regions containing one or more motifs). Exemplary assays utilize antibodies or T cells targeting 98P4B6-related proteins comprising the amino acid residues of one or more of the biological motifs contained within a 98P4B6 polypeptide sequence in order to evaluate the characteristics of this region in normal versus cancerous tissues or to elicit an immune response to the epitope. Alternatively, 98P466-related proteins that contain the amino acid residues of one or more of the biological motifs in a 98P4B6 protein are used to screen for factors that interact with that region of 98P486. 98P486 protein fragments/subsequences are particularly useful in generating and characterizing domain-specific antibodies (e.g., antibodies recognizing an extracellular or intracellular epitope of a 98P4B6 protein), for identifying agents or cellular factors that bind to 98P4B6 or a particular structural domain thereof, and in various therapeutic and diagnostic contexts, including but not limited to diagnostic assays, cancer vaccines and methods of preparing such vaccines. Proteins encoded by the 98P486 genes, or by analogs, homologs or fragments thereof, have a variety of uses, including but not limited to generating antibodies and in methods for identifying ligands and other agents and cellular constituents that bind to a 98P4B6 gene product. Antibodies raised against a 98P486 protein or fragment thereof are useful in diagnostic and prognostic assays, and imaging methodologies in the management of human cancers characterized by expression of 98P486 protein, such as those listed in Table 1. Such antibodies can be expressed intracellularly and used in methods of treating patients with such cancers. 98P486-related nucleic acids or proteins are also used in generating HTL or CTL responses. 44 Various immunological assays useful for the detection of 98P486 proteins are used, induding but not limited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-linked immunofluorescent assays (ELIFA), immunocytochemical methods, and the like. Antibodies can be labeled and used as immunological imaging reagents capable of detecting 98P4B6-expressing cells (e.g.. in radioscintigraphic imaging methods). 98P4B6 proteins are also particularly useful in generating cancer vaccines, as further described herein. IV.) 98P4B6 Antibodies Another aspect of the invention provides antibodies that bind to 98P486-related proteins. Preferred antibodies specifically bind to a 98P4B6-related protein and do not bind (or bind weakly) to peptides or proteins that are not 98P4B6-related proteins under physiological conditions. In this context examples of physiological conditions indude: 1) phosphate buffered saline; 2) Tris-buffered saline containing 25mM Tris and 150 mM NaC; or normal saline (0.9% NaC); 4) animal serum such as human serum; or, 5) a combination of any of 1) through 4); these reactions preferably taking place at pH 7.5, alternatively in a range of pH 7.0 to 8., or alternatively in a range of pH 6.5 to 8.5; also, these reactions taking place at a temperature between 4 0 C to 37*C. For example, antibodies that bind 98P486 can bind 98P486-related proteins such as the hornologs or analogs thereof. 98P4B6 antibodies of the invention are particularly useful in cancer (see, e.g., Table 1) diagnostic and prognostic assays, and imaging methodologies. Similarly, such antibodies are useful in the treatment, diagnosis, and/or prognosis of other cancers, to the extent 98P4B6 is also expressed or overexpressed in these other cancers. Moreover, intracellulady expressed antibodies (e.g., single chain antibodies) are therapeutically useful in treating cancers in which the expression of 98P4B6 is involved, such as advanced or metastatic prostate cancers. The invention also provides various immunological assays useful for the detection and quantification of 98P4B6 and mutant 98P4B6-related proteins. Such assays can comprise one or more 98P4B6 antibodies capable of recognizing and binding a 98P486-related protein, as appropriate. These assays are performed within various immunological assay formats well known in the art, including but not limited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme linked immunoffuorescent assays (ELIFA), and the like. Immunological non-antibody assays of the invention also comprise T cell immunogenicity assays (inhibitory or stimulatory) as well as major histocompatibility complex (MHC) binding assays. In addition, immunological imaging methods capable of detecting prostate cancer and other cancers expressing 98P4B6 are also provided by the invention, including but not limited to radioscintigraphic imaging methods using labeled 98P486 antibodies. Such assays are clinically useful in the detection, monitoring, and prognosis of 98P4B6 expressing cancers such as prostate cancer. 98P486 antibodies are also used in methods for purifying a 98P4B6-related protein and for isolating 98P4B6 homologues and related molecules. For example, a method of purifying a 98P486-related protein comprises incubating a 98P486 antibody, which has been coupled to a solid matrix, with a lysate or other solution containing a 98P4B6-related protein under conditions that permit the 98P4B6 antibody to bind to the 98P4B6-related protein; washing the solid matrix to eliminate impurities; and eluting the 98P486-related protein from the coupled antibody. Other uses of 98P4B6 antibodies in accordance with the invention include generating anti-idiotypic antibodies that mimic a 98P4B6 protein. Various methods for the preparation of antibodies are well known in the art. For example, antibodies can be prepared by immunizing a suitable mammalian host using a 98P486-related protein, peptide, or fragment, in isolated or immunoconjugated form (Antibodies: A Laboratory Manual, CSH Press, Eds., Halow, and Lane (1988); Hardow, Antibodies, Cold Spring Harbor Press, NY (1989)). In addition, fusion proteins of 98P4B6 can also be used, such as a 98P4B6 GST-fusion protein. In a particular embodiment, a GST fusion protein comprising all or most of the amino acid sequence of Figure 2 or Figure 3 is produced, then 45 used as an immunogen to generate appropriate antibodies. In another embodiment, a 98P4B6-related protein is synthesized and used as an immunogen. In addition, naked DNA immunization techniques known in the art are used (with or without purified 98P4B6-related protein or 98P4B6 expressing cells) to generate an immune response to the encoded immunogen (for review, see Donnelly et aL, 1997, Ann. Rev. Immunol. 15: 617-648). The amino acid sequence of a 98P4B6 protein as shown in Figure 2 or Figure 3 can be analyzed to select specific regions of the 98P486 protein for generating antibodies. For example, hydrophobicity and hydrophilicity analyses of a 98P486 amino acid sequence are used to identify hydrophilic regions in the 98P486 structure. Regions of a 98P4B6 protein that show immunogenic structure, as well as other regions and domains, can readily be identified using various other methods known in the art, such as Chou-Fasman, Gamier-Robson, Kyte-Doolittle, Eisenberg, Karplus-Schultz or Jameson-Wolf analysis. Hydrophilicity profiles can be generated using the method of Hopp, T.P. and Woods, K.R., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:3824 3828. Hydropathicity profiles can be generated using the method of Kyte, J. and Doolittle, R.F., 1982, J. Mol. Biol. 157:105 132. Percent (%) Accessible Residues profiles can be generated using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated using the method of Bhaskaran R., Ponnuswamy P.K., 1988, Int. J. Pept. Protein Res. 32:242-255. Beta-turn profiles can be generated using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. Thus, each region identified by any of these programs or methods is within the scope of the present invention. Methods for the generation of 98P4B6 antibodies are further illustrated by way of the examples provided herein. Methods for preparing a protein or polypeptide for use as an immunogen are well known in the art. Also well known in the art are methods for preparing immunogenic conjugates of a protein with a carrier, such as BSA, KLH or other carrier protein. In some circumstances, direct conjugation using, for example, carbodiimide reagents are used; in other instances linking reagents such as those supplied by Pierce Chemical Co., Rockford, IL, are effective. Administration of a 98P4B6 immunogen is often conducted by injection over a suitable time period and with use of a suitable adjuvant, as is understood in the art. During the immunization schedule, titers of antibodies can be taken to determine adequacy of antibody formation. 98P4B6 monoclonal antibodies can be produced by various means well known in the art. For example, immortalized cell lines that secrete a desired monoclonal antibody are prepared using the standard hybridoma technology of Kohler and Milstein or modifications that immortalize antibody-producing B cells, as is generally known. Immortalized cell lines that secrete the desired antibodies are screened by immunoassay in which the antigen is a 98P4B6-related protein. When the appropriate immortalized cell culture is identified, the cells can be expanded and antibodies produced either from in v cultures or from ascites fluid. The antibodies or fragments of the invention can also be produced, by recombinant means. Regions that bind specifically to the desired regions of a 98P4B6 protein can also be produced in the context of chimeric or complementarity determining region (COR) grafted antibodies of multiple species origin. Humanized or human 98P4B6 antibodies can also be produced, and are preferred for use in therapeutic contexts. Methods for humanizing murine and other non-human antibodies, by substituting one or more of the non-human antibody CDRs for corresponding human antibody sequences, are well known (see for example, Jones et a., 1986, Nature 321: 522-525; Riechmann et at., 1988, Nature 332-323-327; Verhoeyen et at., 1988, Science 239: 1534-1536). See also, Carter et aL., 1993, Proc. Nad. Acad. Sci. USA 89: 4285 and Sims et aL, 1993, J. Immunol. 151: 2296. Methods for producing fully human monoclonal antibodies include phage display and transgenic methods (for review, see Vaughan et al., 1998, Nature Biotechnology 16: 535-539). Fully human 98P486 monoconal antibodies can be generated using cloning technologies employing large human Ig gene combinatorial libraries (i.e., phage display) (Grifliths and Hoogenboom, Building an in vit immune system: human antibodies from phage display libraries. In: Protein Engineering of Antibody Molecules for Prophylactic and Therapeutic Applications in Man, Clark, M. (Ed.), Nottingham Academic, pp 45-64 (1993); Burton and Barbas, Human Antibodies from combinatorial libraries. I., pp 65-82). Fully human 98P416 monoclonal antibodies can also be produced using transgenic mice engineered to contain human immunoglobulin gene loci as described in PCT Patent Application W098/24893, Kuchertapati and Jakobovits et al., published December 3,1997 (see also, Jakobovits, 1998, Exp. Opin. Invest Drugs 7(4): 607-614; U.S. patents 6,162,963 issued 19 December 2000; 6,150,584 issued 12 November 2000; and, 6,114598 issued 5 September 2000). This method avoids the in vitro manipulation required with phage display technology and efficiently produces high affinity authentic human antibodies. Reactivity of 98P4B6 antibodies with a 98P4B6-related protein can be established by a number of well known means, including Western blot, immunoprecipitation, ELISA, and FACS analyses using, as appropriate, 98P4B6-related proteins, 98P4B6-expressing cells or extracts thereof. A 98P4B6 antibody or fragment thereof can be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers include, but are not limited to, a radioisotope, a fluorescent compound, a bioluminescent compound, chemiluminescent compound, a metal chelator or an enzyme. Further, bi-specific antibodies specific for two or more 98P4B6 epitopes are generated using methods generally known in the art. Homodimeric antibodies can also be generated by cross-linking techniques known in the art (e.g., Wolff et at., Cancer Res. 53: 2560-2565). V.) 98P486 Cellular Immune Responses The mechanism by which T cells recognize antigens has been delineated. Efficacious peptide epitope vaccine compositions of the invention induce a therapeutic or prophylactic immune responses in very broad segments of the world wide population. For an understanding of the value and efficacy of compositions of the invention that induce cellular immune responses, a brief review of immunology-related technology is provided. A complex of an HLA molecule and a peptidic antigen acts as the ligand recognized by HLA-restricted T cells (Buus, S. et al., Cell 47:1071, 1986; Babbitt, B. P. et a., Nature 317:359, 1985; Townsend, A. and Bodmer, H., Annu. Rev. Immunol. 7:601, 1989; Germain, R. N., Annu. Rev. lmmunol. 11:403, 1993). Through the study of single amino acid substituted antigen analogs and the sequencing of endogenously bound, naturally processed peptides, critical residues that correspond to motifs required for specific binding to HLA antigen molecules have been identified and -are set forth in Table IV (see also, e.g., Southwood, et a., J. Immuno. 160:3363, 1998; Rammensee, et a., Immunogedetics 41:178, 1995; Rammensee et al., SYFPEITHI, access via Word Wide Web at URL (134.2.96.221/scrpts.hlaserver.dlllhome.htm); Sette, A. and Sidney, J. Curr. Opin. Immuno. 10:478, 1998; Engelhard, V. H., Cur. Opin. Immunol. 6:13, 1994; Sette, A. and Grey, H. M., Cur. Opin. Immunol. 4:79, 1992; Sinigaglia, F. and Hammer, J. Cur. Biol. 6:52, 1994; Ruppert et al., Cell 74:929-937, 1993; Kondo et a., J. Immunol. 155:4307-4312,1995; Sidney et a., J. Immunol. 157:3480-3490, 1996; Sidney et al., Human Immunol. 45:79-93, 1996; Sette, A. and Sidney, J. Immunogenetics 1999 Nov; 50(3-4):201-12, Review). Furthermore, x-ey crystallographic analyses of HLA-peptide complexes have revealed pockets within the peptide binding cleft/groove of HLA molecules which accommodate, in an allele-specific mode, residues borne by peptide ligands; these residues in turn determine the HLA binding capacity of the peptides in which they are present. (See, e.g., Madden, D.R. Annu. Rev. Immuno. 13:587, 1995; Smith, et a., Immunity 4:203, 1996; Fremont et al., Immunity 8:305, 1998; Stem et at., Structure 2:245, 1994; Jones, E.Y. Cur. Opin. ImmunoL. 9:75, 1997; Brown, J. H. et al., Nature 364:33, 1993; Guo, H. C. et a., Proc. Nat. Acad. Sci. USA 90:8053,1993; Guo, H. C. et a., Nature 360:364,1992; Silver, M. L. et a., Nature 360:367, 1992; Matsumura, M. et at, Science 257:927, 1992; Madden et a., Cell 70:1035, 1992; Fremont, D. H. et a., Science 257:919, 1992; Saper, M. A. , Bjorkman, P. J. and Wiley, D. C., J. Mol. Biol. 219:277, 1991.) Accordingly, the definition of class I and class 1I allele-specific HLA binding motifs, or class I or class Il supermotifs allows identification of regions within a protein that are correlated with binding to particular HLA antigen(s). Thus, by a process of HLA motif identification, candidates for epitope-based vaccines have been identified; such candidates can be further evaluated by HLA-peptide binding assays to determine binding affinity and/or the time period of 47 association of the epitope and its corresponding HLA molecule. Additional confirmatory work can be performed to select, amongst these vaccine candidates, epitopes with preferred characteristics in terms of population coverage, and/or immunogenicity. Various strategies can be utilized to evaluate cellular immunogenicity, including: 1) Evaluation of primary T cell cultures from normal individuals (see, e.g., Wentworth, P. A. et al, Mo. Immunol. 32:603,1995; Celis, E. et al., Proc. Natt. Acad. Sci. USA 91:2105, 1994; Tsai, V. et a., J. Immuno. 158:1796,1997; Kawashima, 1. et al., Human Immunol. 59:1, 1998). This procedure involves the stimulation of peripheral blood lymphocytes (PBL) from normal subjects with a test peptide in the presence of antigen presenting cells in vitro over a period of several weeks. T cells specific for the peptide become activated during this time and are detected using, e.g.-, a lymphokine- or 5 1 Cr-release assay involving peptide sensitized target cells. 2) Immunization of HLA transgenic mice (see, e.g., Wentworth, P. A. et at., J. Immunol. 26:97, 1996; Wentworth, P. A. et at., Int. Immunol. 8:651, 1996; Alexander, J. et al., J. Immunol. 159:4753, 1997). For example, in such methods peptides in incomplete Freund's adjuvant are administered subcutaneously to HLA transgenic mice. Several weeks following immunization, splenocytes are removed and cultured in vitro in the presence of test peptide for approximately one week. Peptide-specific T cells are detected using, e.g., a 51 Cr-release assay involving peptide sensitized target cells and target cells expressing endogenously generated antigen. 3) Demonstration of recall T cell responses from immune individuals who have been either effectively vaccinated and/or from chronically ill patients (see, e.g., Rehermann, B. et aL., J. Exp. Med. 181:1047, 1995; Doolan, D. L. et al., Immunity 7:97, 1997; Bertoni, R. et al., J. Clin. Invest. 100:503, 1997; Threlkeld, S. C. et a., J. Immunol. 159:1648, 1997; Diepolder, H. M. et at, J. Virol. 71:6011, 1997). Accordingly, recall responses are detected by culturing PBL from subjects that have been exposed to the antigen due to disease and thus have generated an immune response "naturally", or from patients who were vaccinated against the antigen. PBL from subjects are cultured in vitro for 1-2 weeks in the presence of test peptide plus antigen presenting cells (APC) to allow activation of 'memory" T cells, as compared to 'naive' T cells. At the end of the culture period, T cell activity is detected using assays including 51 Cr release involving peptide-sensitized targets, T cell proliferation, or lymphokine release. VI.) 98P486 Trans-genic Animals Nucleic acids that encode a 98P4B6-related protein can also be used to generate either transgenic animals or 'knock our animals that, in turn, are useful in the development and screening of therapeutically useful reagents. In accordance with established techniques, cONA encoding 98P4B6 can be used to done genomic DNA that encodes 98P4B6. The cloned genomic sequences can then be used to generate transgenic animals containing cells that express DNA that encode 98P4B6. Methods for generating transgenic animals, particularly animals such as mice or rats, have become conventional in the art and are described, for example, in U.S. Patent Nos. 4,736,866 issued 12 April 1988, and 4,870,009 issued 26 September 1989. Typically, particular cells would be targeted for 98P486 transgene incorporation with tissue specific enhancers. Transgenic animals that include a copy of a transgene encoding 98P416 can be used to examine the effect of increased expression of DNA that encodes 98P4B6. Such animals can be used as tester animals for reagents thought to confer protection from, for example, pathological conditions associated with its overexpression. In accordance with this aspect of the invention, an animal is treated with a reagent and a reduced incidence of a pathological condition, compared to untreated animals that bear the transgene, would indicate a potential therapeutic intervention for the pathological condition. Alternatively, non-human homologues of 98P486 can be used to construct a 98P4B6 'knock out" animal that has a defective or altered gene encoding 98P4B6 as a result of homologous recombination between the endogenous gene encoding 98P4B6 and altered genomic DNA encoding 98P4B6 introduced into an embryonic cell of the animal. For example, cDNA that encodes 98P4B6 can be used to done genomic DNA encoding 98P4B6 in accordance with established techniques. A portion of the genomic DNA encoding 98P4B6 can be deleted or replaced with another gene, such as a gene encoding a selectable marker that can be used to monitor integration. Typically, several kilobases of unaltered flanking DNA (both at the 5' and 3' ends) are included in the vector (see, e.g., Thomas and Capecchi, Cell, 1:503 (1987) for a description of homologous recombination vectors). The vector is introduced into an embryonic stem cell line (e.g., by electroporation) and cells in which the introduced DNA has homologously recombined with the endogenous DNA are selected (see, e.g., Li et al., Cell, 69:915 (1992)). The selected cells are then injected into a blastocyst of an animal (e.g., a mouse or rat) to form aggregation chimeras (see, e.g., Bradley, in Teratocarcinomas and Embryonic Stem Cells: A PracticakAppmach, E. J. Robertson, ed. (IRL, Oxford, 1987), pp. 113-152). A chimeric embryo can then be implanted into a suitable pseudopregnant female foster animal, and the embryo brought to term to create a "knock our animal. Progeny harboring the homologously recombined DNA in their germ cells can be identified by standard techniques and used to breed animals in which all cells of the animal contain the homologously recombined DNA. Knock out animals can be characterized, for example, for their ability to defend against certain pathological conditions or for their development of pathological conditions due to absence of a 98P486 polypeptide. VII.) Methods for the Detection of 98P4B6 Another aspect of the present invention relates to methods for detecting 98P486 polynudeotides and 98P486-related proteins, as well as methods for identifying a cell that expresses 98P486. The expression profile of 98P4B6 makes it a diagnostic marker for metastasized disease. Accordingly, the status of 98P486 gene products provides information useful for predicting a variety of factors including susceptibility to advanced stage disease, rate of progression, and/or tumor aggressiveness. As discussed in detail herein, the status of 98P4B6 gene products in patient samples can be analyzed by a variety protocols that are well known in the art including immunohistochemical analysis, the variety of Northern blotting techniques including in situ hybridization, RT-PCR analysis (for example on laser capture micro-dissected samples), Western blot analysis and tissue array analysis. More particularly, the invention provides assays for the detection of 98P4B6 polynudeotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, cell preparations, and the like. Detectable 98P4B6 polynucleotides include, for example, a 98P4B6 gene or fragment thereof, 98P486 mRNA, alternative splice variant 98P4B6 mRNAs, and recombinant DNA or RNA molecules that contain a 98P486 polynudeotide. A number of methods for amplifying and/or detecting the presence of 98P486 polynucleotides are well known in the art and can be employed in the practice of this aspect of the invention. In one embodiment, a method for detecting a 98P4B6 mRNA in a biological sample comprises producing cDNA from the sample by reverse transcription using at least one primer; amplifying the cDNA so produced using a 98P416 polynuceotides as sense and antisense primers to amplify 98P486 cDNAs therein; and detecting the presence of the amplified 98P4B6 cDNA. Optionally, the sequence of the amplified 98P4B6 cDNA can be determined. In another embodiment, a method of detecting a 98P4B6 gene in a biological sample comprises first isolating genomic DNA from the sample; amplifying the isolated genomic DNA using 98P486 polynudeotides as sense and antisense primers; and detecting the presence of the amplified 98P4B6 gene. Any number of appropriate sense and antisense probe combinations can be designed from a 98P4B6 nucleotide sequence (see, e.g., Figure 2) and used for this purpose. The invention also provides assays for detecting the presence of a 98P486 protein in a tissue or other biological sample such as serum, semen, bone, prostate, urine, cell preparations, and the like. Methods for detecting a 98P4B6-related protein are also well known and include, for example, immunoprecipitation, immunohistochemical analysis, Western blot analysis, molecular 49 binding assays, ELISA, ELIFA and the like. For example, a method of detecting the presence of a 98P4B6-related protein in a biological sample comprises first contacting the sample with a 98P4B6 antibody, a 98P486-reactive fragment thereof, or a recombinant protein containing an antigen-binding region of a 98P4B6 antibody; and then detecting the binding of 98P4B6 related protein in the sample. Methods for idenifying a cell that expresses 98P4B6 are also within the scope of the invention. In one embodiment, an assay for identifying a cell that expresses a 98P4B6 gene comprises detecting the presence of 98P4B6 mRNA in the cell. Methods for the detection of particular mRNAs in cells are wel known and include, for example, hybridization assays using complementary DNA probes (such as in situ hybridization using labeled 98P4B6 riboprobes, Northern blot and related techniques) and various nucleic acid amplification assays (such as RT-PCR using complementary primers specific for 98P486, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like). Alternatively, an assay for identifying a cel that expresses a 98P4B6 gene comprises detecting the presence of 98P4B6-related protein in the cell or secreted by the cell. Various methods for the detection of proteins are well known in the art and are employed for the detection of 98P4B6-related proteins and cells that express 98P4B6-related proteins. 98P4B6 expression analysis is also useful as a tool for identifying and evaluating agents that modulate 98P4B6 gene expression. For example, 98P4B6 expression is significantly upregulated in prostate cancer, and is expressed in cancers of the tissues listed in Table 1. Identification of a molecule or biological agent that inhibits 98P4B6 expression or over expression in cancer cells is of therapeutic value. For example, such an agent can be identified by using a screen that quantifies 98P4B6 expression by RT-PCR, nucleic acid hybridization or antibody binding. VIII.) Methods for Monitoring the Status of 98P4B6-related Genes and Their Products Oncogenesis is known to be a multistep process where cellular growth becomes progressively dysregulated and cells progress from a normal physiological state to precancerous and then cancerous states (see, e.g., Alers et aL., Lab Invest. 77(5): 437-438 (1997) and Isaacs el al., Cancer Surv. 23: 19-32 (1995)). In this context, examining a biological sample for evidence of dysregulated cell growth (such as aberrant 98P4B6 expression in cancers) allows for early detection of such aberrant physiology, before a pathologic state such as cancer has progressed to a stage that therapeutic options are more limited and or the prognosis is worse. In such examinations, the status of 98P486 in a biological sample of interest can be compared, for example, to the status of 98P4B6 in a corresponding normal sample (e.g. a sample from that individual or alternatively another individual that is not affected by a pathology). An alteration in the status of 98P4B6 in the biological sample (as compared to the normal sample) provides evidence of dysregulated cellular growth. In addition to using a biological sample that is not affected by a pathology as a normal sample, one can also use a predetermined normative value such as a predetermined normal level of mRNA expression (see, e.g., Grever et al., J. Comp. Neurol. 1996 Dec 9; 376(2): 306-14 and U.S. Patent No. 5,837,501) to compare 98P4B6 status in a sample. The term status" in this context is used according to its art accepted meaning and refers to the condition or state of a gene and its products. Typically, skilled artisans use a number of parameters to evaluate the condition or state of a gene and its products. These indude, but are not limited to the location of expressed gene products includingg the location of 98P4B6 expressing cells) as well as the level, and biological activity of expressed gene products (such as 98P4B6 mRNA, polynucleotides and polypeptides). Typically, an alteration in the status of 98P4B6 comprises a change in the location of 98P486 and/or 98P486 expressing cells and/or an increase in 98P486 mRNA and/or protein expression. 98P4B6 status in a sample can be analyzed by a number of means well known in the art, including without limitation, immunohistochemical analysis, in situ hybridization, RT-PCR analysis on laser capture micro-dissected samples, Western blot analysis, and tissue array analysis. Typical protocols for evaluating the status of a 98P4B6 gene and gene products are found, for example in Ausubel et aL. eds., 1995, Current Protocols In Molecular Biology, Units 2 (Northern Blotting), 4 (Southern 50 Blotting), 15 (Immunoblotting) and 18 (PCR Analysis). Thus, the status of 98P486 in a biological sample is evaluated by various methods utilized by skilled artisans including, but not limited to genomic Southern analysis (to examine, for example perturbations in a 98P486 gene), Northern analysis and/or PCR analysis of 98P4B6 mRNA (to examine, for example alterations in the polynucleotide sequences or expression levels of 98P4B6 mRNAs), and, Western and/or immunohistochemical analysis (to examine, for example alterations in polypeptide sequences, alterations in polypeptide localization within a sample, alterations in expression levels of 98P4B6 proteins and/or associations of 98P4B6 proteins with polypeptide binding partners). Detectable 98P4B6 polynucleotides include, for example, a 98P4B6 gene or fragment thereof, 98P4B6 mRNA, alternative splice variants, 98P4B6 mRNAs, and recombinant DNA or RNA molecules containing a 98P486 polynucleotide. The expression profile of 98P4B6 makes it a diagnostic marker for local and/or metastasized disease, and provides information on the growth or oncogenic potential of a biological sample. In particular, the status of 98P4B6 provides information useful for predicting susceptibility to particular disease stages, progression, and/or tumor aggressiveness. The invention provides methods and assays for determining 98P4B6 status and diagnosing cancers that express 98P486, such as cancers of the tissues listed in Table I. For example, because 98P486 mRNA is so highly expressed in prostate and other cancers relative to normal prostate tissue, assays that evaluate the levels of 98P486 mRNA transcripts or proteins in a biological sample can be used to diagnose a disease associated with 98P4B6 dysregulation, and can provide prognostic information useful in defining appropriate therapeutic options. The expression status of 98P4B6 provides information including the presence, stage and location of dysplastic, precancerous and cancerous cells, predicting susceptibility to various stages of disease, and/or for gauging tumor aggressiveness. Moreover, the expression profile makes it useful as an imaging reagent for metastasized disease. Consequenty, an aspect of the invention is directed to the various molecular prognostic and diagnostic methods for examining the status of 98P486 in biological samples such as those from individuals suffering from, or suspected of suffering from a pathology characterized by dysregulated cellular growth, such as cancer. As described above, the status of 98P4B6 in a biological sample can be examined by a number of well-known procedures in the art. For example, the status of 98P4B6 in a biological sample taken from a specific location in the body can be examined by evaluating the sample for the presence or absence of 98P4B6 expressing cells (e.g. those that express 98P4B6 mRNAs or proteins). This examination can provide evidence of dysregulated cellular growth, for example, when 98P4B6-expressing cells are found in a biological sample that does not normally contain such cells (such as a lymph node), because such alterations in the status of 98P486 in a biological sample are often associated with dysregulated cellular growth. Specifically, one indicator of dysregulated cellular growth is the metastases of cancer cells from an organ of origin (such as the prostate) to a different area of the body (such as a lymph node). In this context, evidence of dysregulated cellular growth is important for example because occult lymph node metastases can be detected in a substantial proportion of patients with prostate cancer, and such metastases are associated with known predictors of disease progression (see, e.g., Murphy ef at., Prostate 42(4): 315-317 (2000);Su et at., Semin. Surg. Oncol. 18(1): 17-28 (2000) and Freeman el a., J Urol 1995 Aug 154(2 Pt 1):474-8). In one aspect, the invention provides methods for monitoring 98P4B6 gene products by determining the status of 98P4B6 gene products expressed by cells from an individual suspected of having a disease associated with dysregulated cell growth (such as hyperplasia or cancer) and then comparing the status so determined to the status of 98P486 gene products in a corresponding normal sample. The presence of aberrant 98P4B6 gene products in the test sample relative to the normal sample provides an indication of the presence of dysregulated cell growth within the cells of the individual. In another aspect, the invention provides assays useful in determining the presence of cancer in an individual, comprising detecting a significant increase in 98P4B6 mRNA or protein expression in a test cell or tissue sample relative to 51 expression levels in the corresponding normal cell or tissue. The presence of 98P486 mRNA can, for example, be evaluated in tissues induding but not limited to those listed in Table 1. The presence of significant 98P4B6 expression in any of these tissues is useful to indicate the emergence, presence and/or severity of a cancer, since the corresponding normal tissues do not express 98P486 mRNA or express it at lower levels. In a related embodiment, 98P486 status is determined at the protein level rather than at the nucleic acid level. For example, such a method comprises determining the level of 98P4B6 protein expressed by cells in a test tissue sample and comparing the level so determined to the level of 98P4B6 expressed in a corresponding normal sample. In one embodiment, the presence of 98P4B6 protein is evaluated, for example, using immunohistochemical methods. 98P4B6 antibodies or binding partners capable of detecting 98P4B6 protein expression are used in a variety of assay formats well known in the art for this purpose. In a further embodiment, one can evaluate the status of 98P4B6 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules. These perturbations can indude insertions, deletions, substitutions and the like. Such evaluations are useful because perturbations in the nuceotide and amino acid sequences are observed in a large number of proteins associated with a growth dysregulated phenotype (see, e.g., Marrogi et a., 1999, J. Cutan. Pathol. 26(8):369-378). For example, a mutation in the sequence of 98P486 may be indicative of the presence or promotion of a tumor. Such assays therefore have diagnostic and predictive value where a mutation in 98P4B6 indicates a potential loss of function or increase in tumor growth. A wide variety of assays for observing perturbations in nucleotide and amino acd sequences are well known in the art For example, the size and structure of nucleic acid or amino acid sequences of 98P466 gene products are observed by the Northern, Southem, Western, PCR and DNA sequencing protocols discussed herein. In addition, other methods for observing perturbations in nucleotide and amino acid sequences such as single strand conformation polymorphism analysis are well known in the art (see, e.g., U.S. Patent Nos. 5,382,510 issued 7 September 1999, and 5,952,170 issued 17 January 1995). Additionally, one can examine the methylation status of a 98P4B6 gene in a biological sample. Aberrant demethylation and/or hypermethylation of CpG islands in gene 5' regulatory regions frequently occurs in immortalized and transformed cells, and can result in altered expression of various genes. For example, promoter hypermethylation of the pi-class glutathione S transferase (a protein expressed in normal prostate but not expressed in >90% of prostate carcinomas) appears to permanently silence transcription of this gene and is the most frequently detected genomic alteration in prostate carcinomas (De Marzo et al., Am. J. Pathol. 155(6): 1985-1992 (1999)). In addition, this alteration is present in at least 70% of cases of high-grade prostatic intraepithelial neoplasia (PIN) (Brooks et a., Cancer Epidemiol. Biomarkers Prev., 1998, 7:531-536). In another example, expression of the LAGE-1 tumor specific gene (which is not expressed in normal prostate but is expressed in 25-50% of prostate cancers) is induced by deoxy-azacytidine in lymphoblastoid cells, suggesting that tumoral expression is due to demethylation (Lethe et al., Int. J. Cancer 76(6): 903-908 (1998)). A variety of assays for examining methylation status of a gene are well known in the art. For example, one can utilize, in Southern hybridization approaches, methylation sensitive restriction enzymes that cannot cleave sequences that contain methylated CpG sites to assess the methylation status of CpG islands. In addition, MSP (methylation specific PCR) can rapidly profile the methylation status of all the CpG sites present in a CpG island of a given gene. This procedure involves initial modification of DNA by sodium bisultite (which will convert all unmethylated cytosines to uracil) followed by amplification using primers specific for methylated versus unmethylated DNA Protocols involving methylation interference can also be found for example in Current Protocols In Molecular Biology, Unit 12, Frederick M. Ausubel et a. eds., 1995. Gene amplification is an additional method for assessing the status of 98P4B6. Gene amplification is measured in a sample directly, for example, by conventional Southem blotting or Northern blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Nai. Acad. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or in situ hybridization, using an 52 appropriately labeled probe, based on the sequences provided herein. Alternatively, antibodies are employed that recognize specific duplexes, induding DNA duplexes, RNA duplexes, and DNA-RNA hybrid duplexes or DNA-protein duplexes. The antibodies in turn are labeled and the assay carried out where the duplex is bound to a surface, so that upon the formation of duplex on the surface, the presence of antibody bound to the duplex can be detected. Biopsied tissue or peripheral blood can be convenienty assayed for the presence of cancer cells using for example, Northern, dot blot or RT-PCR analysis to detect 98P4B6 expression. The presence of RT-PCR amplifiable 98P4B6 mRNA provides an indication of the presence of cancer. RT-PCR assays are well known in the art. RT-PCR detection assays for tumor cells in peripheral blood are currently being evaluated for use in the diagnosis and management of a number of human solid tumors. In the prostate cancer field, these indude RT-PCR assays for the detection of cells expressing PSA and PSM (Verkaik et at., 1997, Urol. Res. 25:373-384; Ghossein et a., 1995, J. Clin. Oncol. 13:1195-2000; Heston et al., 1995, Clin. Chem. 41:1687 1688). A further aspect of the invention is an assessment of the susceptibility that an individual has for developing cancer. In one embodiment a method for predicting susceptibility to cancer comprises detecting 98P4B6 mRNA or 98P4B6 protein in a tissue sample, its presence indicating susceptibility to cancer, wherein the degree of 98P4B6 mRNA expression correlates to (he degree of susceptibility. In a specific embodiment, the presence of 98P4B6 in prostate or other tissue is examined, with the presence of 98P486 in the sample providing an indication of prostate cancer susceptibility (or the emergence or existence of a prostate tumor). Similarly, one can evaluate the integrity 98P4B6 nudeotide and amino acid sequences in a biological sample, in order to identify perturbations in the stiucture of these molecules such as insertions, deletions, substitutions and the like. The presence of one or more perturbations in 98P4B6 gene products in the sample is an indication of cancer susceptibility (or the emergence or existence of a tumor). The invention also comprises methods for gauging tumor aggressiveness. In one embodiment, a method for gauging aggressiveness of a tumor comprises determining the level of 98P4B6 mRNA or 98P4B6 protein expressed by tumor cells, comparing the level so determined to the level of 98P4B6 mRNA or 98P4B6 protein expressed in a corresponding normal tissue taken from the san*e individual or a normal tissue reference sample, wherein the degree of 98P4B6 mRNA or 98P486 protein expression in the tumor sample relative to the normal sample indicates the degree of aggressiveness. In a specific embodiment, aggressiveness of a tumor is evaluated by determining the extent to which 98P4B6 is expressed in the tumor cells, with higher expression levels indicating more aggressive tumors. Another embodiment is the evaluation of the integrity of 98P4B6 nucleotide and amino acid sequences in a biological sample, in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like. The presence of one or more perturbations indicates more aggressive tumors. Another embodiment of the invention is directed to methods for observing the progression of a malignancy in an individual over time. In one embodiment, methods for observing the progression of a malignancy in an individual over time comprise determining the level of 98P4B6 mRNA or 98P4B6 protein expressed by cells in a sample of the tumor, comparing the level so determined to the level of 98P486 mRNA or 98P486 protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of 98P4B6 mRNA or 98P4B6 protein expression in the tumor sample over time provides information on the progression of the cancer. In a specific embodiment, the progression of a cancer is evaluated by determining 98P4B6 expression in the tumor cells over time, where increased expression over time indicates a progression of the cancer. Also, one can evaluate the integrity 98P4B6 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like, where the presence of one or more perturbations indicates a progression of the cancer. The above diagnostic approaches can be combined with any one of a wide variety of prognostic and diagnostic protocols known in the art For example, another embodiment of the invention is directed to methods for observing a coincidence between the expression of 98P486 gene and 98P4B6 gene products (or perturbations in 98P4B6 gene and 98P4B6 gene 53 products) and a factor that is associated with malignancy, as a means for diagnosing and prognosticating the status of a tissue sample. A wide variety of factors associated with malignancy can be utilized, such as the expression of genes associated with malignancy (e.g. PSA, PSCA and PSM expression for prostate cancer etc.) as well as gross cytological observations (see, e.g., Bocking et al., 1984, Anal. Quant. Cytol. 6(2):74-88; Epstein, 1995, Hum. Pathol. 26(2):223-9; Thorson et a., 1998, Mod. Pathol. 11(6):543-51; Baisden et al., 1999, Am. J. Surg. Pathol. 23(8):918-24). Methods for observing a coincidence between the expression of 98P4B6 gene and 98P4B6 gene products (or perturbations in 98P416 gene and 98P4B6 gene products) and another factor that is associated with malignancy are useful, for example, because the presence of a set of specific factors that coincide with disease provides information crucial for diagnosing and prognosticating the status of a tissue sample. In one embodiment, methods for observing a coincidence between the expression of 98P4B6 gene and 98P406 gene products (or perturbations in 98P486 gene and 98P486 gene products) and another factor associated with malignancy entails detecting the overexpression of 98P4B6 mRNA or protein in a tissue sample, detecting the overexpression of PSA mRNA or protein in a tissue sample (or PSCA or PSM expression), and observing a coincidence of 98P4B6 mRNA or protein and PSA mRNA or protein overexpression (or PSCA or PSM expression). In a specific embodiment, the expression of 98P4B6 and PSA mRNA in prostate issue is examined, where the coincidence of 98P486 and PSA mRNA overexpression in the sample indicates the existence of prostate cancer, prostate cancer susceptibility or the emergence or status of a prostate tumor. Methods for detecting and quantifying the expression of 98P4B6 mRNA or protein are described herein, and standard nucleic acid and protein detection and quantification technologies are well known in the art. Standard methods for the detection and quantification of 98P4B6 mRNA indude in situ hybridization using labeled 98P4B6 riboprobes, Northern blot and related techniques using 98P4B6 polynudeotide probes, RT-PCR analysis using primers specific for 98P486, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like. In a specific embodiment, semi-quantitative RT-PCR is used to detect and quantify 98P4B6 mRNA expression. Any number of primers capable of amplifying 98P4B6 can be used for this purpose, induding but not limited to the various primer sets specifically described herein. In a specific embodiment, polyclonal or monoclonal antibodies specifically reactive with the wild-type 98P4B6 protein can be used in an immunohistochemical assay of biopsied tissue. IX.) Identification of Molecules That Interact With 98P4B6 The 98P4B6 protein and nucleic acid sequences disclosed herein allow a skilled artisan to identify proteins, small molecules and other agents that interact with 98P486, as well as pathways activated by 98P4B6 via any one of a variety of art accepted protocols. For example, one can utilize one of the so-called interaction trap systems (also referred to as the "two-hybrid assay"). In such systems, molecules interact and reconstitute a transcription factor which directs expression of a reporter gene, whereupon the expression of the reporter gene is assayed. Other systems identify protein-protein interactions in vivo through reconstitution of a eukaryotic transcriptional activator, see, e.g., U.S. Patent Nos. 5,955,280 issued 21 September 1999, 5,925,523 issued 20 July 1999, 5,846,722 issued 8 December 1998 and 6,004,746 issued 21 December 1999. Algorithms are also available in the art for genome-based predictions of protein function (see, e.g., Marcotte, et al., Nature 402: 4 November 1999,83-86). Alternatively one can screen peptide libraries to identify molecules that interact with 98P4B6 protein sequences. In such methods, peptides that bind to 98P4B6 are identified by screening libraries that encode a random or controlled collection of amino acids. Peptides encoded by the libraries are expressed as fusion proteins of bacteriophage coat proteins, the bacteriophage particles are then screened against the 98P4B6 protein(s). Accordingly, peptides having a wide variety of uses, such as therapeutic, prognostic or diagnostic reagents, are thus identified without any prior information on the structure of the expected ligand or receptor molecule. Typical peptide libraries and screening methods that can be used to identify molecules that interact with 98P4B6 protein sequences are disclosed for example in U.S. Patent Nos. 5,723,286 issued 3 March 1998 and 5,733,731 issued 31 March 1998. Alternatively, cell lines that express 98P4B6 are used to identify protein-protein interactions mediated by 98P4B6. Such interactions can be examined using immunoprecipitation techniques (see, e.g., Hamilton B.J., et al. Biochem. Biophys. Res. Commun. 1999, 261:646-51). 98P486 protein can be immunoprecipitated from 98P4B6-expressing cell lines using anti-98P4B6 antibodies. Alternatively, antibodies against His-tag can be used in a cell line engineered to express fusions of 98P4B6 and a His-tag (vectors mentioned above). The immunoprecipitated complex can be examined for protein association by procedures such as Western blotting, MS-methionine labeling of proteins, protein microsequencing, silver staining and two-dimensional gel electrophoresis. Small molecules and ligands that interact with 98P416 can be identified through related embodiments of such screening assays. For example, small molecules can be identified that interfere with protein function, including molecules that interfere with 98P486's ability to mediate phosphorylation and de-phosphorylation, interaction with DNA or RNA molecules as an indication of regulation of cell cycles, second messenger signaling or tumorigenesis. Similarly, small molecules that modulate 98P4B6-related ion channel, protein pump, or cell communication functions are identified and used to treat patients that have a cancer that expresses 98P4B6 (see, e.g., Hille, B., Ionic Channels of Excitable Membranes 2nd Ed., Sinauer Assoc., Sunderland, MA, 1992). Moreover, ligands that regulate 98P4B6 function can be identified based on their ability to bind 98P4B6 and activate a reporter construct. Typical methods are discussed for example in U.S. Patent No. 5,928,868 issued 27 July 1999, and include methods for forming hybrid ligands in which at least one ligand is a small molecule. In an illustrative embodiment, cells engineered to express a fusion protein of 98P486 and a DNA-binding protein are used to co-express a fusion protein of a hybrid ligandlsmall molecule and a cONA library transcriptional activator protein. The cells further contain a reporter gene, the expression of which is conditioned on the proximity of the first and second fusion proteins to each other, an event that occurs only if the hybrid ligand binds to target sites on both hybrid proteins. Those cells that express the reporter gene are selected and the unknown small molecule or the unknown ligand is identified. This method provides a means of identifying modulators, which activate or inhibit 98P4B6. An embodiment of this invention comprises a method of screening for a molecule that interacts with a 98P4B6 amino acid sequence shown in Figure 2 or Figure 3, comprising the steps of contacting a population of molecules with a 98P4B6 amino acid sequence, allowing the population of molecules and the 98P4B6 amino acid sequence to interact under conditions that facilitate an interaction, determining the presence of a molecule that interacts with the 98P486 amino acid sequence, and then separating molecules that do not interact with the 98P4B6 amino acid sequence from molecules that do. In a specific embodiment, the method further comprises purifying, characterizing and identifying a molecule that interacts with the 98P4B6 amino acid sequence. The identified molecule can be used to modulate a function performed by 98P4B6. In a preferred embodiment, the 98P4B6 amino acid sequence is contacted with a library of peptides. X.) Therapeutic Methods and Compositions The identification of 98P486 as a protein that is normally expressed in a restricted set of tissues, but which is also expressed in prostate and other cancers, opens a number of therapeutic approaches to the treatment of such cancers. As contemplated herein, 98P4B6 functions as a transcription factor involved in activating tumor-promoting genes or repressing genes that block tumorigenesis. Accordingly, therapeutic approaches that inhibit the activity of a 98P4B6 protein are useful for patients suffering from a cancer that expresses 98P4B6. These therapeutic approaches generally fall into two classes. One class comprises various methods for inhibiting the binding or association of a 98P4B6 protein with its binding partner or with other proteins. 55 Another class comprises a variety of methods for inhibiting the transcription of a 98P4B6 gene or translation of 98P4B6 mRNA. X.A.) Anti-Cancer Vaccines 5 The invention provides cancer vaccines comprising a 98P4B6-related protein or 98P4B6-related nucleic acid. In view of the expression of 98P4B6, cancer vaccines prevent and/or treat 98P4B6-expressing cancers with minimal or no effects on non target tissues. The use of a tumor antigen in a vaccine that generates humoral and/or cell-mediated immune responses as anti-cancer therapy is well known in the art and has 10 been employed in prostate cancer using human PSMA and rodent PAP immunogens (Hodge et al., 1995, Int. J. Cancer 63:231-237; Fong et al., 1997, J. Immunol. 159:3113-3117). Such methods can be readily practiced by employing a 98P4B6-related protein, or a 98P4B6-encoding nucleic acid molecule and recombinant vectors capable of 15 expressing and presenting the 98P4B6 immunogen (which typically comprises a number of antibody or T cell epitopes). Skilled artisans understand that a wide variety of vaccine systems for delivery of immunoreactive epitopes are known in the art (see, e.g., Heryln et al., Ann Med 1999 Feb 31(l):66-78; Maruyama et al., Cancer Immunol Immunother 2000 Jun 49(3):123-32). Briefly, such methods of generating an immune 20 response (e.g. humoral and/or cell-mediated) in a mammal, comprise the steps of: exposing the mammal's immune system to an immunoreactive epitope (e.g. an epitope present in a 98P4B6 protein shown in Figure 3 or analog or homolog thereof) so that the mammal generates an immune response that is specific for that epitope (e.g. generates antibodies that specifically recognize that epitope). In a preferred method, a 25 98P4B6 immunogen contains a biological motif, see e.g., Tables VIII-XXI and XXU-XLIX. The entire 98P4B6 protein, immunogenic regions or epitopes thereof can be combined and delivered by various means. Such vaccine compositions can include, for example, lipopeptides (e.g.,Vitiello, A. et al., J. Clin. Invest. 95:341, 1995), peptide 30 compositions encapsulated in poly(DL-lactide-co-glycolide) ("PLG") microspheres (see, e.g., Eldridge, et al., Molec. Immunol. 28:287-294, 1991: Alonso et al., Vaccine 12:299-306, 1994; Jones et al., Vaccine 13:675-681, 1995), peptide compositions contained in immune stimulating complexes (ISCOMS) (see, e.g., Takahashi et al., Nature 344:873-875, 1990; Hu et al., Clin Exp Immunol. 113:235-243, 1998), multiple 35 antigen peptide systems (MAPs) (see e.g., Tam, J.P., Proc. Nati. Acad. Sci. U.S.A. 85:5409-5413, 1988; Tam, J.P., J. Immunol. Methods 196:17-32, 1996), peptides 56 formulated as multivalent peptides; peptides for use in ballistic delivery systems, typically crystallized peptides, viral delivery vectors (Perkus, M. E. et al., In: Concepts in vaccine development, Kaufnann, S. H. E., ed., p. 379, 1996; Chakrabarti, S. et al., Nature 320:535, 1986; Hu, S. L. et al., Nature 320:537, 1986; Kieny, M.-P. et al., 5 AIDS Bio/Technology 4:790, 1986; Top, F. H. et al., J. Infect. Dis. 124:148, 1971; Chanda, P. K. et al, Virology 175:535, 1990), particles of viral or synthetic origin (e.g., Kofler, N. et al., J. Immunol. Methods. 192:25, 1996; Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993; Falo, L. D., Jr. et al., Nature Med. 7:649, 1995), adjuvants (Warren, H. S., Vogel, F. R., and Chedid, L. A. Annu. Rev. Immunol. 4:369, 1986; 10 Gupta, R. K et al., Vaccine 11:293, 1993), liposomes (Reddy, R. et al., J. Immunol 148:1585, 1992; Rock, K. L., Immunol, Today 17:131, 1996), or, naked or particle absorbed cDNA (Ulmer, J. B. et al., Science 259:1745, 1993; Robinson, H. L., Hunt, L. A., and Webster, R. G., Vaccine 11:957, 1993; Shiver, J. W. et al., In: Concepts in vaccine development, Kaufmnann, S. H. E., ed., p. 423, 1996; Cease, K. B., and 15 Berzofsky, J. A., Annu. Rev. Immunol. 12:923, 1994 and Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993). Toxin-targeted delivery technologies, also known as receptor mediated targeting, such as those of Avant Immunotherapeutics, Inc. (Needham, Massachusetts) may also be used. In patients with 98P4B6-associated cancer, the vaccine compositions of the 20 invention can also be used in conjunction with other treatments used for cancer, e.g., surgery, chemotherapy, drug therapies, radiation therapies, etc. including use in combination with immune adjuvants such as IL-2, IL-12, GM-CSF, and the like. Cellular Vaccines: 25 56A CTL epitopes can be determined using specific algorithms to identify peptides within 98P4B6 protein that bind corresponding HLA alleles (see e.g., Table IV; Epimer and Epimatrix-, Bown University (URL brown.edu/Research/TB HIV_Lab/epimatrixlepimatrix.html); and, BIMAS, (URL bimas.dcrtnih.gov; SYFPEITHI at URL syfpeithi.bmi-heidelberg.com/). In a preferred embodiment, a 98P4B6 immunogen contains one or more amino acid sequences identified using techniques well known in the art, such as the sequences shown in Tables VIII-XXI and XXII-XLIX or a peptide of 8, 9, 10 or 11 amino acids specified by an HLA Class I motif/supermotif (e.g., Table IV (A), Table IV (D), or Table IV (E)) and/or a peptide of at least 9 amino acids that comprises an HLA Class |1 motif/supermotif (e.g., Table IV (B) or Table IV (C)). As is appreciated in the art, the HLA Class I binding groove is essentially closed ended so that peptides of only a particular size range can fit into the groove and be bound, generally HLA Class I epitopes are 8, 9, 10, or 11 amino acids tong. In contrast, the HLA Class I binding groove is essentially open ended; therefore a peptide of about 9 or more amino acids can be bound by an HLA Class Il molecule. Due to the binding groove differences between HLA Class I and 1I, HLA Class I motifs are length specific, i.e., position two of a Class I motif is the second amino acid in an amino to carboxyl direction of the peptide. The amino acid positions in a Class I motif are relative only to each other, not the overall peptide, i.e., additional amino acids can be attached to the amino and/or carboxyl termini of a motif-bearing sequence. HLA Class Il epitopes are often 9, 10,11,12,13, 14,15, 16,17, 18,19, 20, 21, 22, 23, 24, or 25 amino acids long, or longer than 25 amino acids. Antibody-based Vaccines A wide variety of methods for generating an immune response in a mammal are known in the art (for example as the first step in the generation of hybridomas). Methods of generating an immune response in a mammal comprise exposing the mammal's immune system to an immunogenic epitope on a protein (e.g. a 98P4B6 protein) so that an immune response is generated. A typical embodiment consists of a method for generating an immune response to 98P416 in a host, by contacting the host with a sufficient amount of at least one 98P4B6 B cell or cytotoxic T-cell epitopeor analog thereof; and at least one periodic interval thereafter re-contacting the host with the 98P4B6 B cell or cytotoxic T-cell epitope or analog thereof. A specific embodiment consists of a method of generating an immune response against a 98P4B6-related protein or a man-made multiepitopic peptide comprising: administering 98P4B6 immunogen (e.g. a 98P4B6 protein or a peptide fragment thereof, a 98P4B6 fusion protein or analog etc.) in a vaccine preparation to a human or another mammal. Typically, such vaccine preparations further contain a suitable adjuvant (see, e.g., U.S. Patent No. 6,146,635) or a universal helper epitope such as a PADREM peptide (Epimmune Inc., San Diego, CA; see, e.g., Alexander ef aL., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander el al., Immunity 1994 1(9): 751-761 and Alexander et al., Immunol. Res. 1998 18(2): 79-92). An alternative method comprises generating an immune response in an individual against a 98P486 immunogen by: administering in vivo to muscle or skin of the individual's body a DNA molecule that comprises a DNA sequence that encodes a 98P4B6 immunogen, the DNA sequence operatively linked to regulatory sequences which control the expression of the DNA sequence; wherein the DNA molecule is taken up by cells, the DNA sequence is expressed in the cells and an immune response is generated against the immunogen (see, e.g., U.S. Patent No. 5,962,428). Optionally a genetic vaccine facilitator such as anionic lipids; saponins; lectins; estrogenic compounds; hydroxylated lower alkyls; dimethyl sulfoxide; and urea is also administered. In addition, an antiidiotypic antibody can be administered that mimics 98P4B6, in order to generate a response to the target antigen. Nucleic Acid Vaccines: Vaccine compositions of the invention include nucleic acid-mediated modalities. DNA or RNA that encode protein(s) of the invention can be administered to a patient. Genetic immunization methods can be employed to generate prophylactic or therapeutic humoral and cellular immune responses directed against cancer cells expressing 98P4B6. Constructs comprising DNA encoding a 98P4B6-related protein/immunogen and appropriate regulatory sequences can be injected directly into musde or skin of an individual, such that the cells of the muscle or skin take-up the construct and 57 express the encoded 98P486 protein/immunogen. Alternatively, a vaccine comprises a 98P486-related protein. Expression of the 98P4B6-related protein immunogen results in the generation of prophylactic or therapeutic humoral and cellular immunity against cells that bear a 98P4B6 protein. Various prophylactic and therapeutic genetic immunization techniques known in the art can be used (for review, see information and references published at Internet address genweb.com). Nucleic acid-based delivery is described, for instance, in Wolff et. at., Science 247:1465 (1990) as well as U.S. Patent Nos. 5,580,859; 5,589,466; 5,804,566; 5,739,118; 5,736,524; 5,679,647; WO 98/04720. Examples of DNA-based delivery technologies include "naked DNA, facilitated (bupivicaine, polymers, peptide-mediated) delivery, cationic lipid complexes, and particle-mediated ("gene gun) or pressure-mediated delivery (see, e.g., U.S. Patent No. 5,922,687). For therapeutic or prophylactic immunization purposes, proteins of the invention can be expressed via viral or bacterial vectors. Various viral gene delivery systems that can be used in the practice of the invention include, but are not limited to, vaccinia, fowipox, canarypox, adenovirus, influenza, poliovirus, adeno-associated virus, lentivirus, and sindbis virus (see, e.g., Restifo, 1996, Curr. Opin. Immunol. 8:658-663; Tsang et a. J. Nal. Cancer Inst. 87:982-990 (1995)). Non-viral delivery systems can also be employed by introducing naked DNA encoding a 98P4B6-related protein into the patient (e.g., intramuscularly or intradermally) to induce an anti-tumor response. Vaccinia virus is used, for example, as a vector to express nucleotide sequences that encode the peptides of the invention. Upon introduction into a host the recombinant vaccinia virus expresses the protein immunogenic peptide, and thereby elicits a host immune response. Vaccinia vectors and methods useful in immunization protocols are described in, e.g., U.S. Patent No. 4,722,848. Another vector is BCG (Bacille Calmette Guerin). BCG vectors are described in Stover et al., Nature 351:456-460 (1991). A wide variety of other vectors useful for therapeutic administration or immunization of the peptides of the invention, e.g. adeno and adeno-associated virus vectors, retroviral vectors, Salmonella typhi vectors, detoxified anthrax toxin vectors, and the like, will be apparent to those skilled in the art from the description herein. Thus, gene delivery systems are used to deliver a 98P4Bf-elated nucleic acid molecule. In one embodiment the full length human 98P4B6 cDNA is employed. In another embodiment, 98P486 nucleic acid molecules encoding specific cytotoxic T lymphocyte (CTL) and/or antibody epitopes are employed. Ex Vivo Vaccines Various ex vivo strategies can also be employed to generate an immune response. One approach involves the use of antigen presenting cells (APCs) such as dendritic cells (DC) to present 98P4B6 antigen to a patients immune system. Dendritic cells express MHC class I and Il molecules, B7 co-stimulator, and IL-12, and are thus highly specialized antigen presenting cells. In prostate cancer, autologous dendritic cells pulsed with peptides of the prostate-specific membrane antigen (PSMA) are being used in a Phase I clinical trial to stimulate prostate cancer patients'immune systems (Tjoa et al., 1996, Prostate 28:65 69; Murphy et al., 1996, Prostate 29:371-380). Thus, dendritic cells can be used to present 98P4B6 peptides to T cells in the context of MHC class I or II molecules. In one embodiment, autologous dendritic cells are pulsed with 98P486 peptides capable of binding to MHC class I and/or class I molecules. In another embodiment, dendritic cells are pulsed with the complete 98P4B6 protein. Yet another embodiment involves engineering the overexpression of a 98P4B6 gene in dendritic cells using various implementing vectors known in the art, such as adenovirus (Arthur et al., 1997, Cancer Gene Ther. 4:17 25), retrovirus (Henderson et aL, 1996, Cancer Res. 56:3763-3770), lentivirus, adeno-associated virus, DNA transfection (Ribas et at., 1997, Cancer Res. 57:2865-2869), or tumor-derived RNA transfection (Ashley et a., 1997, J. Exp. Med. 186:1177-1182). Cells that express 98P486 can also be engineered to express immune modulators, such as GM-CSF, and used as immunizing agents. X.B.) 98P486 as a Target for Antibody-based Therapy 58 98P4B6 is an attractive target for antibody-based therapeutic strategies. A number of antibody strategies are known in the art for targeting both extracellular and intracellular molecules (see, e.g., complement and ADCC mediated killing as well as the use of intrabodies). Because 98P4B6 is expressed by cancer cells of various lineages relative to corresponding normal cells, systemic administration of 98P4B6-immunoreactive compositions are prepared that exhibit excellent sensitivity without toxic, non-specific and/or non-target effects caused by binding of the immunoreactive composition to non-target organs and tissues. Antibodies specifically reactive with domains of 98P4B6 are useful to treat 98P4B6-expressing cancers systemically, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting cell proliferation or function. 98P4B6 antibodies can be introduced into a patient such that the antibody binds to 98P4B6 and modulates a function, such as an interaction with a binding partner, and consequently mediates destruction of the tumor cells and/or inhibits the growth of the tumor cells. Mechanisms by which such antibodies exert a therapeutic effect can include complement-mediated cytolysis, antibody-dependent cellular cytotoxicity, modulation of the physiological function of 98P4B6, inhibition of ligand binding or signal transduction pathways, modulation of tumor cell differentiation, alteration of tumor angiogenesis factor profiles, and/or apoptosis. Those skilled in the art understand that antibodies can be used to specifically target and bind immunogenic molecules such as an immunogenic region of a 98P486 sequence shown in Figure 2 or Figure 3. In addition, skilled artisans understand that it is routine to conjugate antibodies to cytotoxic agents (see, e.g., Slevers et a. Blood 93:11 3678-3684 (June 1, 1999)). When cytotoxic and/or therapeutic agents are delivered directly to cells, such as by conjugating them to antibodies specific for a molecule expressed by that cell (e.g. 98P4B6), the cytotoxic agent will exert its known biological effect (i.e. cytotoxicity) on those cells. A wide variety of compositions and methods for using antibody-cytotoxic agent conjugates to kill cells are known in the art. In the context of cancers, typical methods entail administering to an animal having a tumor a biologically effective amount of a conjugate comprising a selected cytotoxic and/or therapeutic agent linked to a targeting agent (e.g. an anti 98P4B6 antibody) that binds to a marker (e.g. 98P4B6) expressed, accessible to binding or localized on the cell surfaces. A typical embodiment is a method of delivering a cytotoxic and/or therapeutic agent to a cell expressing 98P4B6, comprising conjugating the cytotoxic agent to an antibody that immunospecifically binds to a 98P4B6 epitope, and, exposing the cell to the antibody-agent conjugate. Another illustrative embodiment is a method of treating an individual suspected of suffering from metastasized cancer, comprising a step of administering parenterally to said individual a pharmaceutical composition comprising a therapeutically effective amount of an antibody conjugated to a cytotoxic and/or therapeutic agent. Cancer immunotherapy using anti-98P4B6 antibodies can be done in accordance with various approaches that have been successfully employed in the treatment of other types of cancer, including but not limited to colon cancer (Aren et at., 1998. Crit. Rev. Immunol. 18:133-138). multiple myeloma (Ozaki et a., 1997, Blood 90:3179-3186, Tsunenar et a., 1997, Blood 90:2437-2444), gastric cancer (Kasprzyk et al., 1992, Cancer Res. 52:2771-2776), B-cell lymphoma (Funakoshi ef al., 1996, J. Immunother. Emphasis Tumor Immunol. 19:93-101), leukemia (Zhong et al., 1996, Leuk. Res. 20:581-589), colorectal cancer (Moun et al., 1994, Cancer Res. 54:6160-6166; Velders et a., 1995, Cancer Res. 55:4398-4403), and breast cancer (Shepard et al., 1991,~J. Clin. Immunol. 11:117-127). Some therapeutic approaches involve conjugation of naked antibody to a toxin or radioisotope, such as the conjugation of Y91 or 1131 to anti-CD20 antibodies (e.g., ZevalinTM, IDEC Pharmaceuticals Corp. or Bexxarm, Coulter Pharmaceuticals), while others involve co-administration of antibodies and other therapeutic agents, such as HerceptinTM (trastuzumab) with paclitaxel (Genentech, Inc.). The antibodies can be conjugated to a therapeutic agent To treat prostate cancer, for example, 98P486 antibodies can be administered in conjunction with radiation, chemotherapy or hormone ablation. Also, antibodies can be conjugated to a toxin such as calicheanicin (e.g., MylotargT", Wyeth-Ayerst, Madison, NJ, a recombinant humanized IgG4 kappa antibody conjugated to antitumor antibiotic 59 calicheamicin) or a maytansinoid (e.g., taxane-based Tumor-Activated Prodrug, TAP, platform, ImmunoGen, Cambridge, MA, also see e.g., US Patent 5,416,064). Although 98P4B6 antibody therapy is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention is indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment. Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Fan et al. (Cancer Res. 53:4637-4642, 1993), Prewett et al. (International J. of Onco. 9:217-224, 1996), and Hancock et al. (Cancer Res. 51:4575-4580, 1991) describe the use of various antibodies together with chemotherapeutic agents. Although 98P4B6 antibody therapy is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention is indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Cancer patients can be evaluated for the presence and level of 98P486 expression, preferably using immunohistochemical assessments of tumor tissue, quantitative 98P4B6 imaging, or other techniques that reliably indicate the presence and degree of 98P486 expression. Immunohistochemical analysis of tumor biopsies or surgical specimens is preferred for this purpose. Methods for immunohistochemical analysis of tumor tissues are well known in the art Anti-98P4B6 monoclonal antibodies that treat prostate and other cancers indude those that initiate a potent immune response against the tumor or those that are directly cytotoxic. In this regard, anti-98P4B6 monoclonal antibodies (mAbs) can elicit tumor cell tysis by either complement-mediated or antibody-dependent cell cytotoxicity (ADCC) mechanisms, both of which require an intact Fc portion of the immunoglobulin molecule for interactionwith effector cell Fc receptor sites on complement proteins. In addition, anti-98P486 mAbs that exert a direct biological effect on tumor growth are useful to treat cancers that express 98P4B86. Mechanisms by which directly cytotoxic mAbs act include: inhibition of cell growth, modulation of cellular differentiation, modulation of tumor angiogenesis factor profiles, and the induction of apoptosis. The mechanism(s) by which a particular anti-98P4B6 mAb exerts an anti-tumor effect is evaluated using any number of in vitro assays that evaluate cell death such as ADCC, ADMMC, complement-mediated cell lysis, and so forth, as is generally known in the art. In some patients, the use of murine or other non-human monoclonal antibodies, or human/mouse chimeric mAbs can induce moderate to strong immune responses against the non-human antibody. This can result in dearance of the antibody from circulation and reduced efficacy. In the most severe cases, such an immune response can lead to the extensive formation of immune complexes which, potentially, can cause renal failure. Accordingly, preferred monoclonal antibodies used in the therapeutic methods of the invention are those that are either fully human or humanized and that bind specifically to the target 98P4B6 antigen with high affinity but exhibit low or no antigenicity in the patient. Therapeutic methods of the invention contemplate the administration of single anti-98P4B6 mAbs as well as combinations, or cocktails, of different mAbs. Such mAb cocktails can have certain advantages inasmuch as they contain mAbs that target different epitopes, exploit different effector mechanisms or combine directly cytotoxic mAbs with mAbs that rely on immune effector functionality. Such mAbs in combination can exhibit synergistic therapeutic effects. In addition, anti 98P486 mAbs can be administered concomitantly with other therapeutic modalities, including but not limited to various chemotherapeutic agents, androgen-blockers, immune modulators (e.g., IL-2, GM-CSF), surgery or radiation. The anti 60 98P486 mAbs are administered in their "naked" or unconjugated form, or can have a therapeutic agent(s) conjugated to them. Anti-98P4B6 antibody formulations are administered via any route capable of delivering the antibodies to a tumor cell. Routes of administration include, but are not limited to, intravenous, intraperitoneal, intramuscular, intratumor, intradermal, and the like. Treatmentgenerally involves repeated administration of the anti-98P4B6 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1, .2, .3, .4,.5,.6,.7,.8,.9., 1, 2, 3,4, 5, 6, 7, 8, 9,10,15, 20, or 25 mg/kg body weight. In general, doses in the range of 10-1000 mg mAb per week are effective and well tolerated. Based on clinical experience with the Herceptinm mAb in the treatment of metastatic breast cancer, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the anti 98P486 mAb preparation represents an acceptable dosing regimen. Preferably, the initial loading dose is administered as a 90-minute or longer infusion. The periodic maintenance dose is administered as a 30 minute or longer infusion, provided the initial dose was well tolerated. As appreciated by those of skill in the art, various factors can influence the ideal dose regimen in a particular case. Such factors include, for example, the binding affinity and half life of the Ab or mAbs used, the degree of 98P486 expression in the patient, the extent of circulating shed 98P486 antigen, the desired steady-state antibody concentration level, frequency of treatment and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Optionally, patients should be evaluated for the levels of 98P4B6 in a given sample (e.g. the levels of circulating 98P4B6 antigen and/or 98P486 expressing cells) in order to assist in the determination of the most effective dosing regimen, etc. Such evaluations are also used for monitoring purposes throughout therapy, and are useful to gauge therapeutic success in combination with the evaluation of other parameters (for example, urine cytology and/or ImmunoCyt levels in bladder cancer therapy, or by analogy, serum PSA levels in prostate cancer therapy). Anti-idiotypic anti-98P4B6 antibodies can also be used in anti-cancer therapy as a vaccine for inducing an immune response to cells expressing a 98P4B6-related protein. In particular, the generation of anti-idiotypic antibodies is well known in the art; this methodology can readily be adapted to generate anti-idiotypic anti-98P4B6 antibodies that mimic an epitope on a 98P4B6-related protein (see, for example, Wagner et aL., 1997, Hybridoma 16: 33-40; Foon et at., 1995, J. Clin. Invest. 96:334-342; Herlyn et a., 1996, Cancer Immunol. Immunother. 43:65-76). Such an anti-idiotypic antibody can be used in cancer vaccine strategies. KC.) 98P4B6 as a Target for Cellular Immune Responses Vaccines and methods of preparing vaccines that contain an immunogenically effective amount of one or more HLA-binding peptides as described herein are further embodiments of the invention. Furthermore, vaccines in accordance with the invention encompass compositions of one or more of the claimed peptides. A peptide can be present in a vaccine individually. Alternatively, the peptide can exist as a homopolymer comprising multiple copies of the same peptide, or as a heteropolymer of various peptides. Polymers have the advantage of increased immunological reaction and, where different peptide epitopes are used to make up the polymer, the additional ability to induce antibodies and/or CTLs that react with different antigenic determinants of the pathogenic organism or tumor-related peptide targeted for an immune response. The composition can be a naturally occurring region of an antigen or can be prepared, e.g., recombinandy or by chemical synthesis. Carriers that can be used with vaccines of the invention are wel known in the art, and include, e.g., thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acids such as poly L-lysine, poly L-glutamic acid, influenza, hepatitis B virus core protein, and the like. The vaccines can contain a physiologically tolerable (i.e., acceptable) 61 diluent such as water, or saline, preferably phosphate buffered saline. The vaccines also typically include an adjuvant. Adjuvants such as incomplete Freund's adjuvant, aluminum phosphate, aluminum hydroxide, or alum are examples of materials well known in the art. Additionally, as disclosed herein, CTL responses can be primed by conjugating peptides of the invention to Upids, such as tripalmitoyl-S-glycerytcysteinlyseryl- seine (P3CSS). Moreover, an adjuvant such as a synthetic cytosine-phosphorothiolated-guanine-containing (CpG) oligonucleotides has been found to increase CTL responses 10- to 100-fold. (see, e.g. Davila and Celis, J. Immunol. 165:539-547 (2000)) Upon immunization with a peptide composition in accordance with the invention, via injection, aerosol, oral, transdermal, transmucosal, intrapleural, intrathecal, or other suitable routes, the immune system of the host responds to the vaccine by producing large amounts of CTLs and/or HTLs specific for the desired antigen. Consequently, the host becomes at least partially immune to later development of cells that express or overexpress 98P486 antigen, or derives at least some therapeutic benefit when the antigen was tumor-associated. In some embodiments, it may be desirable to combine the class I peptide components with components that induce or facilitate neutralizing antibody and or helper T cell responses directed to the target antigen. A preferred embodiment of such a composition comprises class I and class i epitopes in accordance with the invention. An alternative embodiment of such a composition comprises a class I and/or class 1I epitope in accordance with the invention, along with a cross reactive HTL epitope such as PADRETI (Epimmune, San Diego, CA) molecule (described e.g., in U.S. Patent Number 5,736,142). A vaccine of the invention can also include antigen-presenting cells (APC), such as dendriic cells (DC), as a vehicle to present peptides of the invention. Vaccine compositions can be created in vitro, following dendritic cell mobilization and harvesting, whereby loading of dendritic cells occurs in vitro. For example, dendritic cells are transfected, e.g., with a minigene in accordance with the invention, or are pulsed with peptides. The dendritic cell can then be administered to a patient to elicit immune responses in vivo. Vaccine compositions, either DNA- or peptide-based, can also be administered in vivo in combination with dendritic cell mobilization whereby loading of dendritic cells occurs in vivo. Preferably, the following principles are utilized when selecting an array of epitopes for inclusion in a polyepitopic composition for use in a vaccine, or for selecting discrete epitopes to be induded in a vaccine and/or to be encoded by nucleic acids such as a minigene. It is preferred that each of the following principles be balanced in order to make the selection. The multiple epitopes to be incorporated in a given vaccine composition may be, but need not be, contiguous in sequence in the native antigen from which the epitopes are derived. 1.) Epitopes are selected which, upon administration, mimic immune responses that have been observed to be correlated with tumor clearance. For HLA Class I this includes 3-4 epitopes that come from at least one tumor associated antigen (TAA). For HLA Class 11 a similar rationale is employed; again 3-4 epitopes are selected from at least one TAA (see, e.g., Rosenberg et a., Science 278:1447-1450). Epitopes from one TAA may be used in combination with epitopes from one or more additional TAAs to produce a vaccine that targets tumors with varying expression patterns of frequently-expressed TAAs. 2.) Epitopes are selected that have the requisite binding affinity established to be correlated with immunogenicity: for HLA Class I an ICso of 500 nM or less, often 200 nM or less; and for Class 11 an ICso of 1000 nM or less. 3.) Sufficient supermotif bearing-peptides, or a sufficient array of allele-specific motif-bearing peptides, are selected to give broad population coverage. For example, it is preferable to have at least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known in the art, can be employed to assess the breadth, or redundancy of, population coverage. 4.) When selecting epitopes from cancer-related antgens it is often useful to select analogs because the patient may have developed tolerance to the native epitope.

5.) Of particular relevance are epitopes referred to as "nested epitopes.' Nested epitopes occur where at least two epitopes overlap in a given peptide sequence. A nested peptide sequence can comprise B cell, HLA class I and/or HLA class Il epitopes. When providing nested epitopes, a general objective is to provide the greatest number of epitopes per sequence. Thus, an aspect is to avoid providing a peptide that is any longer than the amino terminus of the amino terminal epitope and the carboxyl terminus of the carboxyl terminal epitope in the peptide. When providing a multi-epitopic sequence, such as a sequence comprising nested epitopes, it is generally important to screen the sequence in order to insure that it does not have pathological or other deleterious biological properties. 6.) If a polyepitopic protein is created, or when creating a minigene, an objective is to generate the smallest peptide that encompasses the epitopes of interest. This principle is similar, if not the same as that employed when selecting a peptide comprising nested epitopes. However, with an artificial polyepitopic peptide, the size minimization objective is balanced against the need to integrate any spacer sequences between epitopes in the polyepitopic protein. Spacer amino acid residues can, for example, be introduced to avoid junctional epitopes (an epitope recognized by the immune system, not present in the target antigen, and only created by the man-made juxtaposition of epitopes), or to facilitate cleavage between epitopes and thereby enhance epitope presentation. Junctional epitopes are generally to be avoided because the recipient may generate an immune response to that non-native epitope. Of particular concern is a junctional epitope that is a "dominant epitope." A dominant epitope may lead to such a zealous response that immune responses to other epitopes are diminished or suppressed. 7.) Where the sequences of multiple variants of the same target protein are present, potential peptide epitopes can also be selected on the basis of their conservancy. For example, a criterion for conservancy may define that the entire sequence of an HLA class I binding peptide or the entire 9-mer core of a class I binding peptide be conserved in a designated percentage of the sequences evaluated for a specific protein antigen. X.C.1. Minigene Vaccines A number of different approaches are available which allow simultaneous delivery of multiple epitopes. Nucleic acids encoding the peptides of the invention are a particularly useful embodiment of the invention. Epitopes for inclusion in a minigene are preferably selected according to the guidelines set forth in the previous section. A preferred means of administering nucleic acids encoding the peptides of the invention uses minigene constructs encoding a peptide comprising one or multiple epitopes of the invention. The use of multi-epitope minigenes is described below and in, Ishioka et at., J. Immunol. 162:3915-3925, 1999; An, L. and Whitton, J. L., J. Virol. 71:2292,1997; Thomson, S. A. et a., J. Immunol. 157:822, 1996; Whitton, J. L. et a., J. Vim!. 67:348, 1993; Hanke, R. et al., Vaccine 16:426, 1998. For example, a multi-epitope DNA plasmid encoding supermotif and/or motif-bearing epitopes derived 98P4B6, the PADRE@ universal helper T cell epitope or multiple HTL epitopes from 98P4B6 (see e.g., Tables VIll-XX and XXII to XLIX), and an endoplasmic reticulum-translocating signal sequence can be engineered. A vaccine may also comprise epitopes that are derived from other TAAs. The immunogenicity of a multi-epitopic minigene can be confirmed in transgenic mice to evaluate the magnitude of CTL induction responses against the epitopes tested. Further, the immunogenicity of DNA-encoded epitopes in vivo can be correlated with the in vitro responses of specific CTL lines against target cells transfected with the DNA plasmid. Thus, these experiments can show that the minigene serves to both: 1.) generate a CTL response and 2.) that the induced CTLs recognized cells expressing the encoded epitopes. For example, to create a DNA sequence encoding the selected epitopes (minigene) for expression in human cells, the amino acid sequences of the epitopes may be reverse translated. A human codon usage table can be used to guide the codon choice for each amino acid. These epitope-encoding DNA sequences may be directly adjoined, so that when translated, a continuous polypeptide sequence is created. To optimize expression and/or immunogenicity, additional 63 elements can be incorporated into the minigene design. Examples of amino acid sequences that can be reverse translated and included in the minigene sequence include: HLA class I epitopes, HLA class 11 epitopes, antibody epitopes, a ubiquitination signal sequence, and/or an endoplasmic reticulum targeting signal. In addition, HLA presentation of CTL and HTL epitopes may be improved by including synthetic (e.g. poly-alanine) or naturally-occurring flanking sequences adjacent to the CTL or HTL epitopes; these larger peptides comprising the epitope(s) are within the scope of the invention. The minigene sequence may be converted to DNA by assembling oligonucleotides that encode the plus and minus strands of the minigene. Overlapping oligonucleotides (30-100 bases long) may be synthesized, phosphorylated, purified and annealed under appropriate conditions using well known techniques. The ends of the oligonucleotides can be joined, for example, using T4 DNA ligase. This synthetic minigene, encoding the epitope polypeptide, can then.be cloned into a desired expression vector. Standard regulatory sequences well known to those of skill in the art are preferably included in the vector to ensure expression in the target cels. Several vector elements are desirable: a promoter with a down-stream cloning site for minigene insertion; a polyadenylation signal for efficient transcription termination; an E. coli origin of replication; and an E. coli selectable marker (e.g. ampicillin or kanamycin resistance). Numerous promoters can be used for this purpose, e.g., the human cytomegalovirus (hCMV) promoter. See, e.g., U.S. Patent Nos. 5,580,859 and 5,589,466 for other suitable promoter sequences. Additional vector modifications may be desired to optimize minigene expression and immunogenicity. In some cases, introns are required for efficient gene expression, and one or more synthetic or naturally-occurring introns could be incorporated into the transcribed region of the minigene. The inclusion of mRNA stabilization sequences and sequences for replication in mammalian cells may also be considered for increasing minigene expression. Once an expression vector is selected, the minigene is cloned into the polylinker region downstream of the promoter. This plasmid is transformed into an appropriate E. coli strain, and DNA is prepared using standard techniques. The orientation and DNA sequence of the minigene, as well as all other elements included in the vector, are confirmed using restriction mapping and DNA sequence analysis. Bacterial cells harboring the correct plasmid can be stored as a master cell bank and a working cell bank. In addition, immunostimulatory sequences (ISSs or CpGs) appear to play a role in the immunogenicity of DNA vaccines. These sequences may be included in the vector, outside the minigene coding sequence, if desired to enhance immunogenicity. In some embodiments, a bi-cistronic expression vector which allows production of both the minigene-encoded epitopes and a second protein (included to enhance or decrease immunogenicity) can be used. Examples of proteins or polypeptides that could beneficially enhance the immune response if co-expressed include cytokines (e.g., IL-2, IL-1 2, GM CSF), cytokine-inducing molecules (e.g., LeIF), costimulatory molecules, or for HTL responses, pan-DR binding proteins

(PADRE

T

U, Epimmune, San Diego, CA). Helper (HTL) epitopes can be joined to intraocular targeting signals and expressed separately from expressed CTL epitopes; this allows direction of the HTL epitopes to a cell compartment different than that of the CTL epitopes. If required, this could facilitate more efficient entry of HTL epitopes into the HLA class Il pathway, thereby improving HTL induction. In contrast to HTL or CTL induction, specifically decreasing the immune response by co-expression of immunosuppressive molecules (e.g. TGF-0) may be beneficial in certain diseases. Therapeutic quantities of plasmid DNA can be produced for example, by fermentation in E. coli, followed by purification. Aliquots from the working cel bank are used to inoculate growth medium, and grown to saturation in shaker flasks or a bioreactor according to wel-known techniques. Plasmid DNA can be purified using standard bioseparation technologies such as solid phase anion-exchange resins supplied by QIAGEN, Inc. (Valencia, California). If required, supercoiled DNA can be isolated from the open circular and linear forms using gel electrophoresis or other methods.

Purified plasmid DNA can be prepared for injection using a variety of formulations. The simplest of these is reconstitution of lyophilized DNA in sterile phosphate-buffer saline (PBS). This approach, known as "naked DNA,' is currently being used for intramuscular (IM) administration in clinical trials. To maximize the immunotherapeutic effects of minigene DNA vaccines, an alternative method for formulating purified plasmid DNA may be desirable. A variety of methods have been described, and new techniques may become available. Cationic lipids, glycolipids, and fusogenic liposomes can also be used in the formulation (see, e.g., as described by WO 93/24640; Mannino & Gould-Fogerite, BioTechniques 6(7): 682 (1988); U.S. Pat No. 5,279,833; WO 91/06309; and Feigner, et al., Proc. Nat'l Acad. Sci. USA 84:7413 (1987). In addition, peptides and compounds referred to collectively as protective, interactive, non-condensing compounds (PINC) could also be complexed to purified plasmid DNA to influence variables such as stability, intramuscular dispersion, or trafficking to specific organs or cell types. Target cell sensitization can be used as a functional assay for expression and HLA class I presentation of minigene-encoded CTL epitopes. For example, the plasmid DNA is introduced into a mammalian cell line that is suitable as a target for standard CTL chromium release assays. The transfection method used will be dependent on the final formulation. Electroporation can be used for 'naked" DNA, whereas cationic lipids allow direct in vitro transfection. A plasmid expressing green fluorescent protein (GFP) can be co-transfected to allow enrichment of transfected cells using fluorescence activated cell sorting (FACS). These cells are then chromium-51 ( 5 1 Cr) labeled and used as target cells for epitope-specific CTL lines; cytolysis, detected by 51 Cr release, indicates both production of, and HLA presentation of, minigene-encoded CTL epitopes. Expression of HTL epitopes may be evaluated in an analogous manner using assays to assess HTL activity. In vivo immunogenicity is a second approach for functional testing of minigene DNA formulations. Transgenic mice expressing appropriate human HLA proteins are immunized with the DNA product. The dose and route of administration are formulation dependent (e.g., IM for DNA in PBS, intraperitoneal (i.p.) for lipid-complexed DNA). Twenty-one days after immunization, splenocytes are harvested and restimulated for one week in the presence of peptides encoding each epitope being tested. Thereafter, for CTL effector cells, assays are conducted for cytolysis of peptide-loaded, 5 1 Cr-labeled target cells using standard techniques. Lysis of target cells that were sensitized by HLA loaded with peptide epitopes, corresponding to minigene-encoded epitopes, demonstrates DNA vaccine function for in vivo induction of CTI-s. Immunogenicity of HTL epitopes is confirmed in transgenic mice in an analogous manner. Atematively, the nucleic adds can be administered using ballistic delivery as described, for instance, in U.S. Patent No. 5,204,253. Using this technique, particles comprised solely of DNA are administered. In a further alternative embodiment, DNArcan be adhered to particles, such as gold particles. Minigenes can also be delivered using other bacterial or viral delivery systems well known in the art, e.g., an expression construct encoding epitopes of the invention can be incorporated into a viral vector such as vaccinia. X.C.2. Combinations of CTL Peptides with Helper Peptides Vaccine compositions comprising CTL peptides of the invention can be modified, e.g., analoged, to provide desired attributes, such as improved serum half life, broadened population coverage or enhanced immunogenicity. For instance, the ability of a peptide to induce CTL activity can be enhanced by linking the peptide to a sequence which contains at least one epitope that is capable of inducing a T helper cell response. Although a CTL peptide can be directly linked to a T helper peptide, often CTL epitope/HTL epitope conjugates are linked by a spacer molecule. The spacer is typically comprised of relatively small, neutral molecules, such as amino acids or amino acid mimetics, which are substantially uncharged under physiological conditions. The spacers are typically selected from, e.g., Ala, Gly, or other neutral spacers of nonpolar amino acids or neutral polar amino acids. It will be understood that the optionally present spacer need not be comprised of the same residues and thus may be a hetero- or homo-oligomer. When present the spacer will 65 usually be at least one or two residues, more usually three to six residues and sometimes 10 or more residues. The CTL peptide epitope can be linked to the T helper peptide epitope either directly or via a spacer either at the amino or carboxy terminus of the CTL peptide. The amino terminus of either the immunogenic peptide or the T helper peptide may be acylated. In certain embodiments, the T helper peptide is one that is recognized by T helper cells present in a majority of a geneticaly diverse population. This can be accomplished by selecting peptides that bind to many, most, or all of the HLA class I molecules. Examples of such amino acid bind many HLA Class i molecules include sequences from antigens such as tetanus toxoid at positions 830-843 (QYIKANSKFIGITE; SEQ ID NO: 97), Plasmodium falciparum circumsporozoite (CS) protein at positions 378-398 (DIEKKIAKMEKASSVFNVVNS; SEQ ID NO: 98), and Streptococcus 18kD protein at positions 116-131 (GAVDSILGGVATYGAA; SEQ fD NO: 99). Other examples include peptides bearing a DR 1-4-7 supermotif, or either of the DR3 motifs. Alternatively, it is possible to prepare synthetic peptides capable of stimulating T helper lymphocytes, in a loosely HLA-restricted fashion, using amino acid sequences not found in nature (see, e.g., PCT publication WO 95107707). These synthetic compounds called Pan-DR-binding epitopes (e.g., PADRET', Epimmune, Inc., San Diego, CA) are designed, most preferably, to bind most HLA-DR (human HLA class 11) molecules. For instance, a pan-DR-binding epitope peptide having the formula: XKXVAAWTLKAAX (SEQ ID NO: 100), where X is either cyclohexylalanine, phenylalanine, or tyrosine, and a is either D-alanine or L-alanine, has been found to bind to most HLA-DR alleles, and to stimulate the response of T helper lymphocytes from most individuals, regardless of their HLA type. An alternative of a pan-DR binding epitope comprises all 1" natural amino acids and can be provided in the form of nucleic acids that encode the epitope. HTL peptide epitopes can also be modified to alter their biological properties. For example, they can be modified to include D-amino acids to increase their resistance to proteases and thus extend their serum half life, or they can be conjugated to other molecules such as lipids, proteins, carbohydrates, and the like to increase their biological activity. For example, a T helper peptide can be conjugated to one or more palmitic acid chains at either the amino or carboxyl termini. X.C.3. Combinations of CTL Peptides with T Cell Priming Agents In some embodiments it may be desirable to include in the pharmaceutical compositions of the invention at least one component which primes B lymphocytes or T lymphocytes. Lipids have been identified as agents capable of priming CTL in vivo. For example, palmitic acid residues can be attached to the s-and a- amino groups of a lysine residue and then linked, e.g., via one or more linking residues such as Gly, Gly-Gly-, Ser, Ser-Ser, or the like, to an immunogenic peptide. The Upidated peptide can then be administered either directly in a micelle or particle, incorporated into a iposome, or emulsified in an adjuvant, e.g., incomplete Freund's adjuvant. In a preferred embodiment, a particularly effective immunogenic composition comprises palmitic acid attached to E- and a- amino groups of Lys, which is attached via linkage, e.g., Ser-Ser, to the amino terminus of the immunogenic peptide. As another example of lipid priming of CTL responses, E coli lipoproteins, such as tripalmitoyl-S glycerylcysteinlyseryl- seine (P3CSS) can be used to prime virus specific CTL when covalently attached to an appropriate peptide (see, e.g., Deres, et at., Nature 342:561, 1989). Peptides of the invention can be coupled to P3CSS, for example, and the lipopeptide administered to an individual to prime specifically an immune response to the target antigen. Moreover, because the induction of neutralizing antibodies can also be primed with PaCSS-conjugated epitopes, two such compositions can be combined to more effectively elicit both humoral and cell-mediated responses. X.C.4. Vaccine Compositions Comprising DC Pulsed with CTL andlor HTL Peptides An embodiment of a vaccine composition in accordance with the invention comprises ex vivo administration of a cocktail of epitope-bearing peptides to PBMC, or isolated DC therefrom, from the patient's blood. A pharmaceutical to facilitate harvesting of DC can be used, such as ProgenipoietinT m (Pharmacia-Monsanto, St. Louis, MO) or GM-CSF/IL-4.

After pulsing the DC with peptides and prior to reinfusion into patients, the DC are washed to remove unbound peptides. In this embodiment, a vaccine comprises peptide-pulsed DCs which present the pulsed peptide epitopes complexed with HLA molecules on their surfaces. The DC can be pulsed ex vivo with a cocktail of peptides, some of which stimulate CTL responses to 98P4B6. Optionally, a helper T cell (HTL) peptide, such as a natural or artificial loosely restricted HLA Class i peptide, can be included to facilitate the CTL response. Thus, a vaccine in accordance with the invention is used to treat a cancer which expresses or overexpresses 98P4B6. X.D. Adoptive lmmunotherapy Antigenic 98P4B6-related peptides are used to elicit a CTL and/or HTL response ex vivo, as well. The resulting CTL or HTL cells, can be used to treat tumors in patients that do not respond to other conventional forms of therapy, or will not respond to a therapeutic vaccine peptide or nucleic acid in accordance with the invention. Ex vivo CTL or HTL responses to a particular antigen are induced by incubating in tissue culture the patient's, or genetically compatible, CTL or HTL precursor cells together with a source of antigen-presenting cells (APC), such as dendritic cells, and the appropriate immunogenic peptide. After an appropriate incubation time (typically about 7-28 days), in which the precursor cells are activated and expanded into effector cells, the cells are infused back into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cell (e.g., a tumor cell). Transfected dendritic cells may also be used as -antigen presenting cells. X.E. Administration of Vaccines for Therapeutic or Prophylactic Purposes Pharmaceutical and vaccine compositions of the invention are typically used to treat and/or prevent a cancer that expresses or overexpresses 98P4B6. In therapeutic applications, peptide and/or nucleic acid compositions are administered to a patient in an amount sufficient to elicit an effective B cell, CTL and/or HTL response to the antigen and to cure or at least partially arrest or slow symptoms and/or complications. An amount adequate to accomplish this is defined as therapeutically effective dose.' Amounts effective for this use will depend on, e.g., the particular composition administered, the manner of administration, the stage and severity of the disease being treated, the weight and general state of health of the patient, and the judgment of the prescribing physician. For pharmaceutical compositions, the immunogenic peptides of the invention, or DNA encoding them, are generally administered to an individual already bearing a tumor that expresses 98P4B6. The peptides or DNA encoding them can be administered individually or as fusions of one or more peptide sequences. Patients can be treated with the immunogenic peptides separately or in conjunction with other treatments, such as surgery, as appropriate. For therapeutic use, administration should generally begin at the first diagnosis of 98P486-associated cancer. This is followed by boosting doses until at least symptoms are substantially abated and for a period thereafter. The embodiment of the vaccine composition (i.e., including, but not limited to embodiments such as peptide cocktails, polyepitopic polypeptides, minigenes, or TAA-specific CTLs or pulsed dendritic cells) delivered to the patient may vary according to the stage of the disease or the patient's health status. For example, in a patient with a tumor that expresses 98P466, a vaccine comprising 98P486-specific CTL may be more efficacious in killing tumor cells in patient with advanced disease than alternative embodiments. It is generally important to provide an amount of the peptide epitope delivered by a mode of administration sufficient to stimulate effectively a cytotoxic T cell response; compositions which stimulate helper T cell responses can also be given in accordance with this embodiment of the invention. 67 The dosage for an initial therapeutic immunization generally occurs in a unit dosage range where the lower value is about 1, 5, 50, 500, or 1,000 pg and the higher value is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient. Boosting dosages of between about 1.0 pg to about 50,000 pg of peptide pursuant to a boosting regimen over weeks to months may be administered depending upon the patients response and condition as determined by measuring the specific activity of CTL and HTL obtained from the patient's blood. Administration should continue until at least clinical symptoms or laboratory tests indicate that the neoplasia, has been eliminated or reduced and for a period thereafter. The dosages, routes of administration, and dose schedules are adjusted in accordance with methodologies known in the art In certain embodiments, the peptides and compositions of the present invention are employed in serious disease states, that is, life-threatening or potentially life threatening situations. In such cases, as a result of the minimal amounts of extraneous substances and the relative nontoxic nature of the peptides in preferred compositions of the invention, it is possible and may be felt desirable by the treating physician to administer substantial excesses of these peptide compositions relative to these stated dosage amounts. The vaccine compositions of the invention can also be used purely as prophylactic agents. Generally the dosage for an initial prophylactic immunization generally occurs in a unit dosage range where the lower value is about 1, 5, 50, 500, or 1000 pg and the higher value is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient. This is followed by boosting dosages of between about 1.0 pg to about 50,000 pg of peptide administered at defined intervals from about four weeks to six months after the initial administration of vaccine. The immunogenicity of the vaccine can be assessed by measuring the specific activity of CTL and HTL obtained from a sample of the patient's blood. The pharmaceutical compositions for therapeutic treatment are intended for parenteral, topical, oral, nasal, intrathecal, or local (e.g. as a cream or topical ointment) administration. Preferably, the pharmaceutical compositions are administered parentally, e.g., intravenously, subcutaneously, intradermally, or intramuscularly. Thus, the invention provides compositions for parenteral administration which comprise a solution of the immunogenic peptides dissolved or suspended in an acceptable canier, preferably an aqueous carrier. A variety of aqueous carriers may be used, e.g., water, buffered water, 0.8% saline, 0.3% glycine, hyaluronic acid and the like. These compositions may be sterilized by conventional, well-known sterilization techniques, or may be sterile filtered. The resulting aqueous solutions may be packaged for use as is, or lyophilized, the lyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservatives, and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, sorbitan monolaurate, triethanolamine oleate, etc. The concentration of peptides of the invention in the pharmaceutical formulations can vary widely, i.e., from less than about 0.1%, usually at or at least about 2% to as much as 20% to 50% or more by weight, and will be selected primarily by fluid volumes, viscosities, etc., in accordance with the particular mode of administration selected. A human unit dose form of a composition is typically included in a pharmaceutical composition that comprises a human unit dose of an acceptable carrier, in one embodiment an aqueous carrier, and is administered in a volume/quantity that is known by those of skill in the art to be used for administration of such compositions to humans (see, e.g., Remington's Pharmaceutical Sciences, 17i Edition, A. Gennaro, Editor, Mack Publishing Co., Easton, Pennsylvania, 1985). For example a peptide dose for initial immunization can be from about I to about 50,000 pg, generally 100-5,000 pg, for a 70 kg patient. For example, for nucleic acids an initial immunization may be performed using an expression vector in the form of naked 6R nucleic acid administered IM (or SC or ID) in the amounts of 0 .5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 Pg) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose is then administered. The booster can be recombinant fowlpox virus administered at a dose of 5-107 to 5x10 9 pfu. For antibodies, a treatment generally involves repeated administration of the anti-98P4B6 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1 to about 10 mg/kg body weight In general, doses in the range of 10

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50 0 mg mAb per week are effective and well tolerated. Moreover, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the anti- 98P486 mAb preparation represents an acceptable dosing regimen. As appreciated by those of skill in the art, various factors can influence the ideal dose in a particular case. Such factors include, for example, half life of a composition, the binding affinity of an Ab, the immunogenicity of a substance, the degree of 98P4B6 expression in the patient, the extent of circulating shed 98P486 antigen, the desired steady-state concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Non-limiting preferred human unit doses are, for example, 500pg - 1mg, 1mg - 50mg, 50mg - 100mg, 100mg - 200mg, 200mg - 300mg, 400mg - 500mg, 500mg - 600mg, 600mg - 700mg, 700mg 800mg, 800mg - 900mg, 900mg - 1g, or 1mg - 700mg. In certain embodiments, the dose is in a range of 2-5 mg/kg body weight, e.g., with follow on weekly doses of 1-3 mg/kg; 0.5mg, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10mg/kg body weight followed, e.g., in two, three or four weeks by weekly doses; 0.5 - 10mg/kg body weight, e.g., followed in two, three or four weeks by weekly doses; 225, 250, 275, 300, 325, 350, 375, 400mg m 2 of body area weekly; 1-600mg m 2 of body area weekly; 225-400mg m 2 of body area weekly; these does can be followed by weekly doses for 2, 3, 4, 5, 6, 7, 8, 9, 19, 11, 12 or more weeks. In one embodiment, human unit dose forms of polynucleotides comprise a suitable dosage range or effective amount that provides any therapeutic effect. As appreciated by one of ordinary skill in the art a therapeutic effect depends on a number of factors, including the sequence of the polynucleotide, molecular weight of the polynucleotide and route of administration. Dosages are generally selected by the physician or other health care professional in accordance with a variety of parameters known in the art, such as severity of symptoms, history of the patient and the like. Generally, for a polynucleotide of about 20 bases, a dosage range may be selected from, for example, an independently selected lower limit such as about 0.1, 0.25, 0.5,1, 2, 5, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 200, 300,400 or 500 mg/kg up to an independently selected upper limit, greater than the lower limit, of about 60, 80, 100, 200, 300, 400, 500, 750, 1000, 1500, 2000, 3000, 4000, 5000, 6000, 7000, 8000, 9000 or 10,000 mg/kg. For example, a dose may be about any of the following: 0.1 to 100 mg/kg, 0.1 to 50 mg/kg, 0.1 to 25 mg/kg, 0.1 to 10 mg/kg, I to 500 mg/kg, 100 to 400 mg/kg, 200 to 300 mg/kg, 1 to 100 mg/kg, 100 to 200 mg/kg, 300 to 400 mg/kg, 400 to 500 mg/kg, 500 to 1000 mg/kg, 500 to 5000 mg/kg, or 500 to 10,000 mg/kg. Generally, parenteral routes of administration may require higher doses of polynucleotide compared to more direct application to the nucleotide to diseased tissue, as do polynucleotides of increasing length. In one embodiment, human unit dose forms of T-cells comprise a suitable dosage range or effective amount that provides any therapeutic effect. As appreciated by one of ordinary skill in the art, a therapeutic effect depends on a number of factors. Dosages are generally selected by the physician or other health care professional in accordance with a variety of parameters known in the art, such as severity of symptoms, history of the patient and the like. A dose may be about 10' cells to about 106 cells, about 106 cells to about 108 cells, about 108 to about 1011 cells, or about 108 to about 5 x 1010 cells. A dose may also about 106 cells/m 2 to about 10'0 cels/nm 2 , or about 106 cells/m 2 to about 108 cells/m 2 . Proteins(s) of the invention, and/or nucleic acids encoding the protein(s), can also be administered via liposomes, which may also serve to: 1) target the proteins(s) to a particular tissue, such as lymphoid tissue; 2) to target selectively to diseases cells; or, 3) to increase the half-life of the peptide composition. Uposomes include emulsions, foams, micelles, insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. In these preparations, the 69 peptide to be delivered is incorporated as part of a liposome, alone or in conjunction with a molecule which binds to a receptor prevalent among lymphoid cells, such as monoclonal antibodies which bind to the CD45 antigen, or with other therapeutic or immunogenic compositions. Thus, liposomes either filled or decorated with a desired peptide of the invention can be directed to the site of lymphoid cells, where the liposomes then deliver the peptide compositions. Liposomes for use in accordance with the invention are formed from standard vesicle-forming lipids, which generally include neutral and negatively charged phospholipids and a sterol, such as cholesterol. The selection of lipids is generally guided by consideration of, e.g., liposome size, acid lability and stability of the liposomes in the blood stream. A variety of methods are available for preparing liposomes, as described in, e.g., Szoka, et al., Ann. Rev. Biophys. Bioeng. 9:467 (1980), and U.S. Patent Nos. 4,235,871, 4,501,728, 4,837,028, and 5,019,369. For targeting cells of the immune system, a ligand to be incorporated into the liposome can include, e.g., antibodies or fragments thereof specific for cell surface determinants of the desired immune system cells. A liposome suspension containing a peptide may be administered intravenously, locally, topically, etc. in a dose which varies according to, inter alia, the manner of administration, the peptide being delivered, and the stage of the disease being treated. For solid compositions, conventional nontoxic solid carriers may be used which include, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium carbonate, and the like. For oral administration, a pharmaceutically acceptable nontoxic composition is formed by incorporating any of the normally employed excipients, such as those carriers previously listed, and generally 10 95% of active ingredient, that is, one or more peptides of the invention, and more preferably at a concentration of 25%-75%. For aerosol administration, immunogenic peptides are preferably supplied in finely divided form along with a surfactant and propellant. Typical percentages of peptides are about 0.01 %-20% by weight preferably about 1%-10%. The surfactant must, of course, be nontoxic, and preferably soluble in the propellant. Representative of such agents are the esters or partial esters of fatty acids containing from about 6 to 22 carbon atoms, such as caproic, octanoic, lauric, palmitic, stearic, inoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cydic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. The surfactant may constitute about 0.1 %-20% by weight of the composition, preferably about 0.25-5%. The balance of the composition is ordinarily propellant. A carrier can also be induded, as desired, as with, e.g., lecithin for intranasal delivery. X1.) Diagnostic and Prognostic Embodiments of 98P486. As disclosed herein, 98P4B6 polynucleotides, polypeptides, reactive cytotoxic T cells (CTL), reactive helper T cells (HTL) and anti-polypeptide antibodies are used in well known diagnostic, prognostic and therapeutic assays that examine conditions associated with dysregulated cell growth such as cancer, in particular the cancers listed in Table I (see, e.g., both its specific pattern of tissue expression as well as its overexpression in certain cancers as described for example in the Example entitled "Expression analysis of 98P4B6 in normal tissues, and patient specimens). 98P4B6 can be analogized to a prostate associated antigen PSA, the archetypal marker that has been used by medical practitioners for years to identify and monitor the presence of prostate cancer (see, e.g., Merrill et al., J. Urol. 163(2): 503-5120 (2000); Polascik et al., J. Urol. Aug; 162(2):293-306 (1999) and Fortier et al., J. Nal Cancer Inst. 91(19): 1635 1640(1999)). A variety of other diagnostic markers are also used in similar contexts including p53 and K-ras (see, e.g., Tulchinsky et al., Int J Mol Med 1999 Jul 4(1):99-102 and Minimoto et al., Cancer Detect Prev 2000;24(1):1-12). Therefore, this disclosure of 98P4B6 polynudeotides and polypeptides (as well as 98P486 polynudeotide probes and anti-98P4B6 antibodies used to identify the presence of these molecules) and their properties allows skilled artisans to utilize these molecules in methods that are analogous to those used, for example, in a variety of diagnostic assays directed to examining conditions associated with cancer. 70 Typical embodiments of diagnostic methods which utilize the 98P486 polynucleotides, polypeptides, reactive T cells and antibodies are analogous to those methods from well-established diagnostic assays, which employ, e.g., PSA polynucleotides, polypeptides, reactive T cells and antibodies. For example, just as PSA polynucleotides are used as probes (for example in Northern analysis, see, e.g., Sharief et al., Biochem. Mol. Biol. Int. 33(3):567-74(1994)) and primers (for example in PCR analysis, see, e.g., Okegawa et al, J. Urol. 163(4): 1189-1190 (2000)) to observe the presence and/or the level of PSA mRNAs in methods of monitoring PSA overexpression or the metastasis of prostate cancers, the 98P4B6 polynucleotides described herein can be utilized in the same way to detect 98P486 overexpression or the metastasis of prostate and other cancers expressing this gene. Alternatively, just as PSA polypeptides are used to generate antibodies specific for PSA which can then be used to observe the presence and/or the level of PSA proteins in methods to monitor PSA protein overexpression (see, e.g., Stephan et al., Urology 55(4):560-3 (2000)) or the metastasis of prostate cells (see, e.g., Alanen et al, Pathol. Res. Pract. 192(3):233-7 (1996)), the 98P4B6 polypeptides described herein can be utilized to generate antibodies for use in detecting 98P4B6 overexpression or the metastasis of prostate cells and cells of other cancers expressing this gene. Specifically, because metastases involves the movement of cancer cells from an organ of origin (such as the lung or prostate gland etc.) to a different area of the body (such as a lyiph node), assays which examine a biological sample for the presence of cells expressing 98P4B6 polynucleotides and/or polypeptides can be used to provide evidence of metastasis. For example, when a biological sample from tissue that does not normally contain 98P4B6-expressing cells (lymph node) is found to contain 98P4B6-expressing cells such as the 98P4B6 expression seen in LAPC4 and LAPC9, xenografts isolated from lymph node and bone metastasis, respectively, this finding is indicative of metastasis. Alternatively 98P486 polynucleotides and/or polypeptides can be used to provide evidence of cancer, for example, when cells in a biological sample that do not normally express 98P486 or express 98P4B6 at a different level are found to express 98P486 or have an increased expression of 98P4B6 (see, e.g., the 98P4B6 expression in the cancers listed in Table I and in patient samples etc. shown in the accompanying Figures). In such assays, artisans may further wish to generate supplementary evidence of metastasis by testing the biological sample for the presence of second tissue restricted marker (in addition to 98P4B6) such as PSA, PSCA etc. (see, e.g., Alanen et al, Pathol. Res. Pract. 192(3): 233 237 (1996)). Just as PSA polynucleotide fragments and polynucleotide variants are employed by skilled artisans for use in methods of monitoring PSA, 98P486 polynucleotide fragments and polynudeotide variants are used in an analogous manner. In particular, typical PSA polynudeotides used in methods of monitoring PSA are probes or primers which consist of fragments of the PSA cONA sequence. Illustrating this, primers used to PCR amplify a PSA polynucleotide must include less than the whole PSA sequence to function in the polymerase chain reaction. In the context of such PCR reactions, skilled artisans generally create a variety of different polynucleotide fragments that can be used as primers in order to amplify different portions of a polynucleotide of interest or to optimize amplification reactions (see, e.g., Caetano-Anolles, G. Biotechniques 25(3): 472-476, 478-480 (1998); Robertson et al., Methods Mol. Biol. 98:121-154 (1998)). An additional illustration of the use of such fragments is provided in the Example entitled "Expression analysis of 98P4B6 in normal tissues, and patient specimens,' where a 98P4B6 polynudeotide fragment is used as a probe to show the expression of 98P4B6 RNAs in cancer cells. In addition, variant polynucleotide sequences are typically used as primers and probes for the corresponding mRNAs in PCR and Northern analyses (see, e.g., Sawai et al., Fetal Diagn. Ther. 1996 Nov-Dec 1 1(6):407-13 and Current Protocols In Molecular Biology, Volume 2, Unit 2, Frederick M. Ausubel et a. eds., 1995)). Polynucleotide fragments and variants are useful in this context where they are capable of binding to a target polynucleotide sequence (e.g., a 98P486 polynucleotide shown in Figure 2 or variant thereof) under conditions of high stringency. 71 Furthermore, PSA polypeptides which contain an epitope that can be recognized by an antibody or T cell that specifically binds to that epitope are used in methods of monitoring PSA. 98P4B6 polypeptide fragments and polypeptide analogs or variants can also be used in an analogous manner. This practice of using polypeptide fragments or polypeptide variants to generate antibodies (such as anti-PSA antibodies or T cells) is typical in the art with a wide variety of systems such as fusion proteins being used by practitioners (see, e.g., Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubel et al. eds., 1995). In this context, each epitope(s) functions to provide the architecture with which an antibody or T cell is reactive. Typically, skilled artisans create a variety of different polypeptide fragments that can be used in order to generate immune responses specific for different portions of a polypeptide of interest (see, e.g., U.S. Patent No. 5,840,501 and U.S. Patent No. 5,939,533). For example it may be preferable to utilize a polypeptide comprising one of the 98P4B6 biological motifs discussed herein or a motif-bearing subsequence which is readily identified by one of skill in the art based on motifs available in the art. Polypeptide fragments, variants or analogs are typically useful in this context as long as they comprise an epitope capable of generating an antibody or T cell specific for a target polypeptide sequence (e.g. a 98P486 polypeptide shown in Figure 3). As shown herein, the 98P4B6 polynucleotides and polypeptides (as well as the 98P4B6 polynudeotide probes and anti-98P4B6 antibodies or T cells used to identify the presence of these molecules) exhibit specific properties that make them useful in diagnosing cancers such as those listed in Table 1. Diagnostic assays that measure the presence of 98P486 gene products, in order to evaluate the presence or onset of a disease condition described herein, such as prostate cancer, are used to identify patients for preventive measures or further monitoring, as has been done so successfully with PSA. Moreover, these materials satisfy a need in the art for molecules having similar or complementary characteristics to PSA in situations where, for example, a definite diagnosis of metastasis of prostatic origin cannot be made on the basis of a test for PSA alone (see, e.g., Alanen et at., Pathol. Res. Pract. 192(3): 233-237 (1996)), and consequently, materials such as 98P4B6 polynudeotides and polypeptides (as well as the 98P4B6 polynucleotide probes and anti-98P4B6 antibodies used to identify the presence of these molecules) need to be employed to confirm a metastases of prostatic origin. Finally, in addition to their use in diagnostic assays, the 98P4B6 polynudeotides disclosed'herein have a number of other utilities such as their use in the identification of oncogenetic associated chromosomal abnormalities in the chromosomal region to which the 98P4B6 gene maps (see the Example entitled "Chromosomal Mapping of 98P4B6" below). Moreover, in addition to their use in diagnostic assays, the 98P486-related proteins and polynucleotides disclosed herein have other utilities such as their use in the forensic analysis of tissues of unknown origin (see, e.g., Takahama K Forensic Sci Int 1996 Jun 28;80(1-2): 63-9). Additionally, 98P4B6-related proteins or polynucteotides of the invention can be used to treat a pathologic condition characterized by the over-expression of 98P4B6. For example, the amino acid or nucleic acid sequence of Figure 2 or Figure 3, or fragments of either, can be used to generate an immune response to a 98P486 antigen. Antibodies or other molecules that react with 98P4B6 can be used to modulate the function of this molecule, and thereby provide a therapeutic benefit XII.) Inhibition of 98P4B6 Protein Function The invention includes various methods and compositions for inhibiting the binding of 98P4B6 to its binding partner or its association with other protein(s) as well as methods for inhibiting 98P486 function. XII.A.) Inhibition of 98P4B6 With Intracellular Antibodies In one approach, a recombinant vector that encodes single chain antibodies that specifically bind to 98P486 are introduced into 98P4B6 expressing cells via gene transfer technologies. Accordingly, the encoded single chain anti-98P4B6 72 antibody is expressed intracellulaly, binds to 98P4B6 protein, and thereby inhibits its function. Methods for engineering such intracellular single chain antibodies are well known. Such intracellular antibodies, also known as 'intrabodies", are specifically targeted to a particular compartment within the cell, providing control over where the inhibitory activity of the treatment is focused. This technology has been successfully applied in the art (for review, see Richardson and Marasco, 1995, TIBTECH vol. 13). Intrabodies have been shown to virtually eliminate the expression of otherwise abundant cell surface receptors (see, e.g., Richardson et al., 1995, Proc. Nati. Acad. Sci. USA 92: 3137-3141; Beedi et a., 1994, J. Biol. Chem. 289: 23931-23936; Deshane et aL., 1994, Gene Ther. 1: 332-337). Single chain antibodies comprise the variable domains of the heavy and light chain joined by a flexible linker polypeptide, and are expressed as a single polypeptide. Optionally, single chain antibodies are expressed as a single chain variable region fragment joined to the light chain constant region. Well-known intracellular trafficking signals are engineered into recombinant polynucleotide vectors encoding such single chain antibodies in order to target precisely the intrabody to the desired intracellular compartment. For example, intrabodies targeted to the endoplasmic reticulum (ER) are engineered to incorporate a leader peptide and, optionally, a C-terminal ER retention signal, such as the KDEL amino acid motif. Intrabodies intended to exert activity in the nucleus are engineered to include a nuclear localization signal. Lipid moieties are joined to intrabodies in order to tether the intrabody to the cytosolic side of the plasma membrane. Intrabodies can also be targeted to exert function in the cytosol. For example, cytosolic intrabodies are used to sequester factors within the cytosol, thereby preventing them from being transported to their natural cellular destination. In one embodiment, intrabodies are used to capture 98P4B6 in the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals are engineered into such 98P4B6 intrabodies in order to achieve the desired targeting. Such 98P4B6 intrabodies are designed to bind specifically to a particular 98P4B6 domain. In another embodiment, cytosolic intrabodies that specifically bind to a 98P4B6 protein are used to prevent 98P4B6 from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 98P4B6 from forming transcription complexes with other factors). In order to specifically direct the expression of such intrabodies to particular cells, the transcription of the intrabody is placed under the regulatory control of an appropriate tumor-specific promoter and/or enhancer. In order to target intrabody expression specifically to prostate, for example, the PSA promoter and/or promoter/enhancer can be utilized (See, for example, U.S. Patent No. 5,919,652 issued 6 July 1999). XII.B.) Inhibition of 98P486 with Recombinant Proteins In another approach, recombinant molecules bind to 98P4B6 and thereby inhibit 98P4B6 function. For example, these recombinant molecules prevent or inhibit 98P4B6 from accessing/binding to its binding partner(s) or associating with other protein(s). Such recombinant molecules can, for example, contain the reactive parts) of a 98P4B6 specific antibody molecule. In a particular embodiment, the 98P486 binding domain of a 98P486 binding partner is engineered into a dimeric fusion protein, whereby the fusion protein comprises two 98P4B6 ligand binding domains linked to the Fc portion of a human IgG, such as human IgG1. Such IgG portion can contain, for example, the CH2 and CH 3 domains and the hinge region, but not the CH1 domain. Such dimeric fusion proteins are administered in soluble form to patients suffering from a cancer associated with the expression of 98P4B6, whereby the dimeric fusion protein specifically binds to 98P486 and blocks 98P4B6 interaction with a binding partner. Such dimeric fusion proteins are further combined into multimeric proteins using known antibody linking technologies. 73 Xll.C.) Inhibition of 98P4B6 Transcription or Translation The present invention also comprises various methods and compositions for inhibiting the transcription of the 98P4B6 gene. Similarly, the invention also provides methods and compositions for inhibiting the translation of 98P4B6 mRNA into protein. In one approach, a method of inhibiting the transcription of the 98P4B6 gene comprises contacting the 98P4B6 gene with a 98P486 antisense polynudeotide. In another approach, a method of inhibiting 98P4B6 mRNA translation comprises contacting a 98P4B6 mRNA with an antisense polynudeotide. In another approach, a 98P4B6 specific ribozyme is used to deave a 98P4B6 message, thereby inhibiting translation. Such antisense and ribozyme based methods can also be directed to the regulatory regions of the 98P4B6 gene, such as 98P4B6 promoter and/or enhancer elements. Similarly, proteins capable of inhibiting a 98P4B6 gene transcription factor are used to inhibit 98P486 mRNA transcription. The various polynucleotides and compositions useful in the aforementioned methods have been described above. The use of antisense and ribozyme molecules to inhibit transcription and translation is well known in the art. Other factors that inhibit the transcription of 98P4B6 by interfering with 98P4B6 transcriptional activation are also useful to treat cancers expressing 98P486. Similarly, factors that interfere with 98P4B6 processing are useful to treat cancers that express 98P4B6. Cancer treatment methods utilizing such factors are also within the scope of the invention. XII.D.) General Considerations for Therapeutic Strategies Gene transfer and gene therapy technologies can be used to deliver therapeutic polynudeotide molecules to tumor cells synthesizing 98P4B6 (i.e., antisense, ribozyme, polynudeotides encoding intrabodies and other 98P4B6 inhibitory molecules). A number of gene therapy approaches are known in the art Recombinant vectors encoding 98P4B6 antisense polynudeotides, ribozymes, factors capable of interfering with 98P486 transcription, and so forth, can be delivered to target tumor cells using such gene therapy approaches. The above therapeutic approaches can be combined with any one of a wide variety of surgical, chemotherapy or radiation therapy regimens. The therapeutic approaches of the invention can enable the use of reduced dosages of chemotherapy (or other therapies) and/or less frequent administration, an advantage for all patients and particularly for those that do not tolerate the toxicity of the chemotherapeutic agent well. The anti-tumor activity of a particular composition (e.g., antisense, ribozyme, intrabody), or a combination of such compositions, can be evaluated using various in vtro and in vivo assay systems. In vto assays that evaluate therapeutic activity indude cell growth assays, soft agar assays and other assays indicative of tumor promoting activity, binding assays capable of determining the extent to which a therapeutic composition will inhibit the binding of 98P486 to a binding partner, etc. In vivo, the effect of a 98P4B6 therapeutic composition can be evaluated in a suitable animal model. For example, xenogenic prostate cancer models can be used, wherein human prostate cancer explants or passaged xenograft tissues are introduced into immune compromised animals, such as nude or SCID mice (Klein et al., 1997, Nature Medicine 3: 402-408). For example, PCT Patent Application W098/16628 and U.S. Patent 6,107,540 describe various xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micrometastasis, and the formation of osteoblastic metastases characteristic of late stage disease. Efficacy can be predicted using assays that measure inhibition of tumor formation, tumor regression or metastasis, and the like. In idvo assays that evaluate the promotion of apoptosis are useful in evaluating therapeutic compositions. In one embodiment, xenografts from tumor bearing mice treated with the therapeutic composition can be examined for the presence of apoptotic foci and compared to untreated control xenograft-bearing mice. The extent to which apoptotic foci are found in the tumors of the treated mice provides an indication of the therapeutic efficacy of the composition. 74 The therapeutic compositions used in the practice of the foregoing methods can be fonrulated into pharmaceutical compositions comprising a carrier suitable for the desired delivery method. Suitable carriers indude any material that when combined with the therapeutic composition retains the anti-tumor function of the therapeutic composition and is generally non-reactive with the patient's immune system. Examples include, but are not limited to, any of a number of standard pharmaceutical carriers such as sterile phosphate buffered saline solutions, bacteriostatic water, and the like (see, generally, Remington's Pharmaceutical Sciences 16* Edition, A. Osal., Ed., 1980). Therapeutic formulations can be solubilized and administered via any route capable of delivering the therapeutic composition to the tumor site. Potentially effective routes of administration include, but are not limited to, intravenous, parenteral, intraperitoneal, intramuscular, intratumor, intradermal, intraorgan, orthotopic, and the like.- A preferred formulation for intravenous injection comprises the therapeutic composition in a solution of preserved bacteriostatic water, sterile unpreserved water, and/or diluted in polyvinyichloride or polyethylene bags containing 0.9% sterile Sodium Chloride for Injection, USP. Therapeutic protein preparations can be lyophilized and stored as sterile powders, preferably under vacuum, and then reconstituted in bacteriostatic water (containing for example, benzyl alcohol preservative) or in sterile water prior to injection. Dosages and administration protocols for the treatment of cancers using the foregoing methods will vary with the method and the target cancer, and will generally depend on a number of other factors appreciated in the art XIII.) Identification, Characterization and Use of Modulators of 98P4B6 Methods to Identify and Use Modulators In one embodiment, screening is performed to identify modulators that induce or suppress a particular expression profile, suppress or induce specific pathways, preferably generating the associated phenotype thereby. In another embodiment, having identified differentially expressed genes important in a particular state; screens are performed to identify modulators that alter expression of individual genes, either increase or decrease. In another embodiment screening is performed to identify modulators that alter a biological function of the expression product of a differentially expressed gene. Again, having identified the importance of a gene in a particular state, screens are performed to identify agents that bind and/or modulate the biological activity of the gene product. In addition, screens are done for genes that are induced in response to a candidate agent After identifying a modulator (one that suppresses a cancer expression pattern leading to a normal expression pattern, or a modulator of a cancer gene that leads to expression of the gene as in normal tissue) a screen is performed to identify genes that are specifically modulated in response to the agent. Comparing expression profiles between normal tissue and agent-treated cancer tissue reveals genes that are not expressed in normal tissue or cancer tissue, but are expressed in agent treated tissue, and vice versa. These agent-specific sequences are identified and used by methods described herein for cancer genes or proteins. In particular these sequences and the proteins they encode are used in marking or identifying agent treated cells. In addition, antibodies are raised against the agent-induced proteins and used to target novel therapeutics to the treated cancer tissue sample. Modulator-related Identification and Screening Assays: Gene Expression-related Assays Proteins, nucleic acids, and antibodies of the invention are used in screening assays. The cancer-associated proteins, antibodies, nucleic acids, modified proteins and cels containing these sequences are used in screening assays, such as evaluating the effect of drug candidates on a "gene expression profile," expression profile of polypeptides or alteration of biological function. In one embodiment, the expression profiles are used, preferably in conjunction with high 75 throughput screening techniques to allow monitoring for expression profile genes after treatment with a candidate agent (e.g., Davis, GF, et al, J Biol Screen 7:69 (2002); Zlokamik, et al., Science 279:84-8 (1998); Heid, Genome Res 6:986 94,1996). The cancer proteins, antibodies, nucleic acids, modified proteins and cells containing the native or modified cancer proteins or genes are used in screening assays. That is, the present invention comprises methods for screening for compositions which modulate the cancer phenotype or a physiological function of a cancer protein of the invention. This is done on a gene itself or by evaluating the effect of drug candidates on a "gene expression profile" or biological function. In one embodiment, expression profiles are used, preferably in conjunction with high throughput screening techniques to allow monitoring after treatment with a candidate agent see Zlokamik, supra. A variety of assays are executed directed to the genes and proteins of the invention. Assays are run on an individual nucleic acid or protein level. That is, having identified a particular gene as up regulated in cancer, test compounds are screened for the ability to modulate gene expression or for binding to the cancer protein of the invention. "Modulation" in this context includes an increase or a decrease in gene expression. The preferred amount of modulation will depend on the original change of the gene expression in normal versus tissue undergoing cancer, with changes of at least 10%, preferably 50%, more preferably 100-300%, and in some embodiments 300-1000% or greater. Thus, if a gene exhibits a 4-fold increase in cancer tissue compared to normal tissue, a decrease of about four-fold is often desired; similarly, a 10-fold decrease in cancer tissue compared to normal tissue a target value of a 10-fold increase in expression by the test compound is often desired. Modulators that exacerbate the type of gene expression seen in cancer are also useful, e.g., as an upregulated target in further analyses. The amount of gene expression is monitored using nucleic acid probes and the quantification of gene expression levels, or, altematively, a gene product itself is monitored, e.g., through the use of antibodies to the cancer protein and standard immunoassays. Proteomics and separation techniques also allow for quantification of expression. Expression Monitoring to Identify Compounds that Modify Gene Expression In one embodiment, gene expression monitoring, i.e., an expression profile, is monitored simultaneously for a number of entities. Such profiles will typically involve one or more of the genes of Figure 2. In this embodiment, e.g., cancer nucleic acid probes are attached to biochips to detect and quantify cancer sequences in a particular cell. Alternatively, PCR can be used. Thus, a series, e.g., wells of a microtiter plate, can be used with dispensed primers in desired wells. A PCR reaction can then be performed and analyzed for each well. Expression monitoring is performed to identify compounds that modify the expression of one or more cancer associated sequences, e.g., a polynucleotide sequence set out in Figure 2. Generally, a test modulator is added to the cells prior to analysis. Moreover, screens are also provided to identify agents that modulate cancer, modulate cancer proteins of the invention, bind to a cancer protein of the invention, or interfere with the binding of a cancer protein of the invention and an antibody or other binding partner. In one embodiment, high throughput screening methods involve providing a library containing a large number of potential therapeutic compounds (candidate compounds). Such "combinatorial chemical libraries' are then screened in one or more assays to identify those library members (particular chemical species or subclasses) that display a desired characteristic activity. The compounds thus identified can serve as conventional "lead compounds,' as compounds for screening, or as therapeutics. In certain embodiments, combinatorial libraries of potential modulators are screened for an ability to bind to a cancer polypeptide or to modulate activity. Conventionally, new chemical entities with useful properties are generated by identifying a chemical compound (called a "lead compound') with some desirable property or activity, e.g., inhibiting activity, 7'i creating variants of the lead compound, and evaluating the property and activity of those variant compounds. Often, high throughput screening (HTS) methods are employed for such an analysis. As noted above, gene expression monitoring is conveniently used to test candidate modulators (e.g., protein, nucleic acid or small molecule). After the candidate agent has been added and the cells allowed to incubate for a period, the sample containing a target sequence to be analyzed is, e.g., added to a biochip. If required, the target sequence is prepared using known techniques. For example, a sample is treated to lyse the cells, using known lysis buffers, electroporation, etc., with purification and/or amplification such as PCR performed as appropriate. For example, an in vitro transcription with labels covalently attached to the nucleotides is performed. Generally, the nudeic acids are labeled with biotin-FITC or PE, or with cy3 or cy5. The target sequence can be labeled with, e.g., a fluorescent, a chemiluminescent, a chemical, or a radioactive signal, to provide a means of detecting the target sequence's specific binding to a probe. The label also can be an enzyme, such as alkaline phosphatase or horseradish peroxidase, which when provided with an appropriate substrate produces a product that is detected. Alternatively, the label is a labeled compound or small molecule, such as an enzyme inhibitor, that binds but is not catalyzed or altered by the enzyme. The label also can be a moiety or compound, such as, an epitope tag or biotin which specifically binds to streptavidin. For the example of biotin, the streptavidin is labeled as described above, thereby, providing a detectable signal for the bound target sequence. Unbound labeled streptavidin is typically removed prior to analysis. As will be appreciated by those in the art, these assays can be direct hybridization assays or can comprise "sandwich assays", which indude the use of multiple probes, as is generally outlined in U.S. Patent Nos. 5, 681,702; 5,597,909; 5,545,730; 5,594,117; 5,591,584; 5,571,670; 5,580,731; 5,571,670; 5,591,584; 5,624,802; 5,635,352; 5,594,118; 5,359,100; 5,124, 246; and 5,681,697. In this embodiment, in general, the target nudeic acid is prepared as outlined above, and then added to the biochip comprising a plurality of nucleic acid probes, under conditions that allow the formation of a hybridization complex. A variety of hybridization conditions are used in the present invention, including high, moderate and low stringency conditions as outlined above. The assays are generally run under stringency conditions which allow formation of the label probe hybridization complex only in the presence of target. Stringency can be controlled by altering a step parameter that is a thermodynamic variable, including, but not limited to, temperature, formamide concentration, salt concentration, chaotropic salt concentration pH, organic solvent concentration, etc. These parameters may also be used to control non-specific binding, as is generally outlined in U.S. Patent No. 5,681,697. Thus, it can be desirable to perform certain steps at higher stringency conditions to reduce non-specific binding. The reactions outlined herein can be accomplished in a variety of ways. Components of the reaction can be added simultaneously, or sequentially, in different orders, with preferred embodiments outined below. In addition, the reaction may include a variety of other reagents. These include salts, buffers, neutral proteins, e.g. albumin, detergents, etc. which can be used to facilitate optimal hybridization and detection, and/or reduce nonspecific or background interactions. Reagents that otherwise improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc., may also be used as appropriate, depending on the sample preparation methods and purity of the target. The assay data are analyzed to determine the expression levels of individual genes, and changes in expression levels as between states, forming a gene expression profile. Biological Activity-related Assays The invention provides methods identify or screen for a compound that modulates the activity of a cancer-related gene or protein of the invention. The methods comprise adding a test compound, as defined above, to a cell comprising a 77 cancer protein of the invention. The cells contain a recombinant nucleic acid that encodes a cancer protein of the invention. In another embodiment, a library of candidate agents is tested on a plurality of cells. In one aspect, the assays are evaluated in the presence or absence or previous or subsequent exposure of physiological signals, e.g. hormones, antibodies, peptides, antigens, cytokines, growth factors, action potentials, pharmacological agents including chemotherapeutics, radiation, carcinogenics, or other cells (i.e., cell-cell contacts). In another example, the determinations are made at different stages of the cell cycle process. In this way, compounds that modulate genes or proteins of the invention are identified. Compounds with pharmacological activity are able to enhance or interfere with the activity of the cancer protein of the invention. Once identified, similar structures are evaluated to identify critical structural features of the compound. In one embodiment, a method of modulating ( e.g., inhibiting) cancer cell division is provided; the method comprises administration of a cancer modulator. In another embodiment, a method of modulating ( e.g., inhibiting) cancer is provided; the method comprises administration of a cancer modulator. In a further embodiment, methods of treating cells or individuals with cancer are provided; the method comprises administration of a cancer modulator. In one embodiment, a method for modulating the status of a cell that expresses a gene of the invention is provided. As used herein status comprises such art-accepted parameters such as growth, proliferation, survival, function, apoptosis, senescence, location, enzymatic activity, signal transduction, etc. of a cell. In one embodiment, a cancer inhibitor'is an antibody as discussed above. In another embodiment, the cancer inhibitor is an antisense molecule. A variety of cell growth, proliferation, and metastasis assays are known to those of skill in the art, as described herein. High Throughput Screening to Identify Modulators The assays to identify suitable modulators are amenable to high throughput screening. Preferred assays thus detect enhancement or inhibition of cancer gene transcription, inhibition or enhancement of polypeptide expression, and inhibition or enhancement of polypeptide activity. In one embodiment, modulators evaluated in high throughput screening methods are proteins, often naturally occurring proteins or fragments of naturally occurring proteins. Thus, e.g., cellular extracts containing proteins, or'random or directed digests of proteinaceous cellular extracts, are used. In this way, libraries of proteins are made for screening in the methods of the invention. Particularly preferred in this embodiment are libraries of bacterial, fungal, viral, and mammalian proteins, with the latter being preferred, and human proteins being especially preferred. Particularly useful test compound will be directed to the class of proteins to which the target belongs, e.g., substrates for enzymes, or ligands and receptors. Use of Soft Agar Growth and Colony Formation to Identify and Characterize Modulators Normal cells require a solid substrate to attach and grow. When cells are transformed, they lose this phenotype and grow detached from the substrate. For example, transformed cells can grow in stirred suspension culture or suspended in semi-solid media, such as semi-solid or soft agar. The transformed cells, when transfected with tumor suppressor genes, can regenerate normal phenotype and once again require a solid substrate to attach to and grow. Soft agar growth or colony formation in assays are used to identify modulators of cancer sequences, which when expressed in host cells, inhibit abnormal cellular proliferation and transformation. A modulator reduces or eliminates the host cells' ability to grow suspended in solid or semisolid media, such as agar. Techniques for soft agar growth or colony formation in suspension assays are described in Freshney, Culture of Animal Cells a Manual of Basic Technique (3rd ed., 1994). See also, the methods section of Garkavtsev et al. (1996), supra. Evaluation of Contact Inhibition and Growth Density Limitation to Identify and Characterize Modulators Normal cells typically grow in a flat and organized patten in cell culture until they touch other cels. When the cells touch one another, they are contact inhibited and stop growing. Transformed cells, however, are not contact inhibited and 7R continue to grow to high densities in disorganized foci. Thus, transformed cells grow to a higher saturation density than corresponding normal cells. This is detected morphologically by the formation of a disoriented monolayer of cells or cells in foci. Alternatively, labeling index with ( 3 H)-thymidine at saturation density is used to measure density limitation of growth, similarly an MTT or Alamar blue assay will reveal proliferation capacity of cells and the the ability of modulators to affect same. See Freshney (1994), supra. Transformed cells, when transfected with tumor suppressor genes, can regenerate a normal phenotype and become contact inhibited and would grow to a lower density. In this assay, labeling index with 3 H)-thymidine at saturation density is a preferred method of measuring density limitation of growth. Transformed host cells are transfected with a cancer-associated sequence and are grown for 24 hours at saturation density in non-limiting medium conditions. The percentage of cells labeling with ( 3 H)-thymidine is determined by incorporated cpm. Contact independent growth is used to identify modulators of cancer sequences, which had led to abnormal cellular proliferation and transformation. A modulator reduces or eliminates contact independent growth, and retums the cells to a normal phenotype. Evaluation of Growth Factor or Serum Dependence to Identify and Characterize Modulators Transformed cells have lower serum dependence than their normal counterparts (see, e.g., Temin, J. Nati. Cancer Inst. 37:167-175 (1966); Eagle et al., J. Exp. Med 131:836-879 (1970)); Freshney, supra. This is in part due to release of various growth factors by the transformed cells. The degree of growth factor or serum dependence of transformed host cells can be compared with that of control. For example, growth factor or serum dependence of a cell is monitored in methods to identify and characterize compounds that modulate cancer-associated sequences of the invention. Use of Tumor-specific Marker Levels to Identify and Characterize Modulators Tumor cells release an increased amount of certain factors (hereinafter "tumor specific markers") than their normal counterparts. For example, plasminogen activator (PA) is released from human glioma at a higher level than from normal brain cells (see, e.g., Gullino, Angiogenesis, Tumor Vascularization, and Potential Interference with Tumor Growth, in Biological Responses in Cancer, pp. 178-184 (Mihich (ed.) 1985)). Similarly, Tumor Angiogenesis Factor (TAF) is released at a higher level in tumor cells than their normal counterparts. See, e.g., Folkman, Angiogenesis and Cancer, Sem Cancer Biol. (1992)), while bFGF is released from endothelial tumors (Ensoli, B et al). Various techniques which measure the release of these factors are described in Freshney (1994), supra. Also, see, Unkless et al., J. Biol. Chem. 249:4295-4305 (1974); Strickland & Beers, J. Biol. Chem. 251:5694-5702 (1976); Whur et al., Br. J. Cancer 42:305 312 (1980); Gullino, Angiogenesis, Tumor Vascularization, and Potential Interference with Tumor Growth, in Biological Responses in Cancer, pp. 178-184 (Mihich (ed.) 1985); Freshney, Anticancer Res. 5:111-130 (1985). For example, tumor specific marker levels are monitored in methods to identify and characterize compounds that modulate cancer-associated sequences of the invention. Invasiveness into Matrigel to Identify and Characterize Modulators The degree of invasiveness into Matrigel or an extracellular matrix constituent can be used as an assay to identify and characterize compounds that modulate cancer associated sequences. Tumor cells exhibit a positive correlation between malignancy and invasiveness of cells into Matrigel or some other extracellular matrix constituent. In this assay, tumorigenic cells are typically used as host cells. Expression of a tumor suppressor gene in these host cells would decrease invasiveness of the host cells. Techniques described in Cancer Res. 1999; 59:6010; Freshney (1994), supra, can be used. Briefly, the level of invasion of host cells is measured by using filters coated with Matrigel or some other extracellular matrix constituent. Penetration into the gel, or through to the distal side of the filter, is rated as invasiveness, and rated histologically by number of cells and distance moved, or by prelabeling the cells with M1 and counting the radioactivity on the distal side of the filter or bottom of the dish. See, e.g., Freshney (1984), supra. 79 Evaluation of Tumor Growth In Vivo to Identify and Characterize Modulators Effects of cancer-associated sequences on cell growth are tested in transgenic or immune-suppressed organisms. Transgenic organisms are prepared in a variety of art-accepted ways. For example, knock-out transgenic organisms, e.g., mammals such as mice, are made, in which a cancer gene is disrupted or in which a cancer gene is inserted. Knock-out transgenic mice are made by insertion of a marker gene or other heterologous gene into the endogenous cancer gene site in the mouse genome via homologous recombination. Such mice can also be made by substituting the endogenous cancer gene with a mutated version of the cancer gene, or by mutating the endogenous cancer gene, e.g., by exposure to carcinogens. To prepare transgenic chimeric animals, e.g., mice, a DNA construct is introduced into the nuclei of embryonic stem cells. Cells containing the newly engineered genetic lesion are injected into a host mouse embryo, which is re implanted into a recipient female. Some of these embryos develop into chimeric mice that possess germ cells some of which are derived from the mutant cell line. Therefore, by breeding the chimeric mice it is possible to obtain a new line of mice containing the introduced genetic lesion (see, e.g., Capecchi et al., Science 244:1288 (1989)). Chimeric mice can be derived according to US Patent 6,365,797, issued 2 April 2002; US Patent 6,107,540 issued 22 August 2000; Hogan et al., Manipulating the Mouse Embryo: A laboratory Manual, Cold Spring Harbor Laboratory (1988) and Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, Robertson, ed., IRL Press, Washington, D.C., (1987). Alternatively, various immune-suppressed or immune-deficient host animals can be used. For example, a genetically athymic 'nude" mouse (see, e.g., Giovanella et al., J. Nat. Cancer Inst. 52:921 (1974)), a SCID mouse, a thymectomized mouse, or an irradiated mouse (see, e.g., Bradley et al., Br. J. Cancer 38:263 (1978); Selby et al., Br. J. Cancer 41:52 (1980)) can be used as a host. Transplantable tumor cells (typically about 106 cells) injected into isogenic hosts produce invasive tumors in a high proportion of cases, while normal cells of similar origin will not. In hosts which developed invasive tumors, cells expressing cancer-associated sequences are injected subcutaneously or orthotopically. Mice are then separated into groups, including control groups and treated experimental groups) e.g. treated with a modulator). After a suitable length of time, preferably 4-8 weeks, tumor growth is measured (e.g., byvolume or by its two largest dimensions, or weight) and compared to the control. Tumors that have statistically significant reduction (using, e.g., Students T test) are said to have inhibited growth. In Vitro Assays to Identify and Characterize Modulators Assays to identify compounds with modulating activity can be performed in vitro. For example, a cancer polypeptide is first contacted with a potential modulator and incubated for a suitable amount of time, e.g., from 0.5 to 48 hours. In one embodiment, the cancer polypeptide levels are determined in vitro by measuring the level of protein or mRNA. The level of protein is measured using immunoassays such as Westem blotting, ELISA and the like with an antibody that selectively binds to the cancer polypeptide or a fragment thereof. For measurement of mRNA, amplification, e.g., using PCR, LCR, or hybridization assays, e. g., Northern hybridization, RNAse protection, dot blotting, are preferred. The level of protein or mRNA is detected using directly or indirectly labeled detection agents, e.g., fluorescently or radioactively labeled nudeic acids, radioactively or enzymatically labeled antibodies, and the like, as described herein. Alternatively, a reporter gene system can be devised using a cancer protein promoter operably linked to a reporter gene such as luciferase, green fluorescent protein, CAT, or P-gal. The reporter construct is typically transfected into a cell. After treatment with a potential modulator, the amount of reporter gene transcription, translation, or activity is measured according to standard techniques known to those of skill in the art (Davis GF, supra; Gonzalez, J. & Negulescu, P. Curr. Opin. Biotechnol. 1998: 9:624). Ra As outlined above, in vitro screens are done on individual genes and gene products. That is, having identified a particular differentially expressed gene as important in a particular state, screening of modulators of the expression of the gene or the gene product itself is performed. In one embodiment, screening for modulators of expression of specific gene(s) is performed. Typically, the expression of only one or a few genes is evaluated. In another embodiment, screens are designed to first find compounds that bind to differentially expressed proteins. These compounds are then evaluated for the ability to modulate differentially expressed activity. Moreover, once initial candidate compounds are identified, variants can be further screened to better evaluate structure activity relationships. Binding Assays to Identify and Characterize Modulators In binding assays in accordance with the invention, a purified or isolated gene product of the invention is generally used. For example, antibodies are generated to a protein of the invention, and immunoassays are run to determine the amount and/or location of protein. Alternatively, cells comprising the cancer proteins are used in the assays. Thus, the methods comprise combining a cancer protein of the invention and a candidate compound such as a ligand, and determining the binding of the compound to the cancer protein of the invention. Preferred embodiments utilize the human cancer protein; animal models of human disease of can also be developed and used. Also, other analogous mammalian proteins also can be used as appreciated by those of skill in the art. Moreover, in some embodiments variant or derivative cancer proteins are used. Generally, the cancer protein of the invention, or the ligand, is non-diffusibly bound to an insoluble support. The support can, e.g., be one having isolated sample receiving areas (a microtiter plate, an array, etc.). The insoluble supports can be made of any composition to which the compositions can be bound, is readily separated from soluble material, and is otherwise compatible with the overall method of screening. The surface of such supports can be solid or porous and of any convenient shape. Examples of suitable insoluble supports include microtiter plates, arrays, membranes and beads. These are typically made of glass, plastic (e.g., polystyrene), polysaccharide, nylon, nitrocellulose, or Teflon m, etc. Microtiter plates and arrays are especially convenient because a large number of assays can be carried out simultaneously, using small amounts of reagents and samples. The particular manner of binding of the composition to the support is not crucial so long as it is compatible with the reagents and overall methods of the invention, maintains the activity of the composition and is nondiffusable. Preferred methods of binding include the use of antibodies which do not sterically block either the ligand binding site or activation sequence when attaching the protein to the support, direct binding to "sticky" or ionic supports, chemical crosslinking, the synthesis of the protein or agent on the surface, etc. Following binding of the protein or ligand/binding agent to the support, excess unbound material is removed by washing. The sample receiving areas may then be blocked through incubation with bovine serum albumin (BSA), casein or other innocuous protein or other moiety. Once a cancer protein of the invention is bound to the support, and a test compound is added to the assay. Alternatively, the candidate binding agent is bound to the support and the cancer protein of the invention is then added. Binding agents include specific antibodies, non-natural binding agents identified in screens of chemical libraries, peptide analogs, etc. Of particular interest are assays to identify agents that have a low toxicity for human cells. A wide variety of assays can be used for this purpose, including proliferation assays, cAMP assays, labeled in vitro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, functional assays (phosphorylation assays, etc.) and the like. 81 A determination of binding of the test compound (ligand, binding agent, modulator, etc.) to a cancer protein of the invention can be done in a number of ways. The test compound can be labeled, and binding determined directly, e.g., by attaching all or a portion of the cancer protein of the invention to a solid support, adding a labeled candidate compound (e.g., a fluorescent label), washing off excess reagent, and determining whether the label is present on the solid support. Various blocking and washing steps can be utilized as appropriate. In certain embodiments, only one of the components is labeled, e.g., a protein of the invention or ligands labeled. Alternatively, more than one component is labeled with different labels, e.g., 1125, for the proteins and a fluorophor for the compound. Proximity reagents, e.g., quenching or energy transfer reagents are also useful. Competitive Binding to Identify and Characterize Modulators In one embodiment, the binding of the "test compound" is determined by competitive binding assay with a 'competitor." The competitor is a binding moiety that binds to the target molecule (e.g., a cancer protein of the invention). Competitors include compounds such as antibodies, peptides, binding partners, ligands, etc. Under certain circumstances, the competitive binding between the test compound and the competitor displaces the test compound. In one embodiment, the test compound is labeled. Either the test compound, the competitor, or both, is added to the protein for a time sufficient to allow binding. Incubations are performed at a temperature that facilitates optimal activity, typically between four and 40*C. Incubation periods are typically optimized, e.g., to facilitate rapid high throughput screening; typically between zero and one hour will be sufficient. Excess reagent is generally removed or washed away. The second component is then added, and the presence or absence of the labeled component is followed, to indicate binding. In one embodiment, the competitor is added first, followed by the test compound. Displacement of the competitor is an indication that the test compound is binding to the cancer protein and thus is capable of binding to, and potentially modulating, the activity of the cancer protein. In this embodiment, either component can be labeled. Thus, e.g., if the competitor is labeled, the presence of label in the post-test compound wash solution indicates displacement by the test compound. Alternatively, if the test compound is labeled, the presence of the label on the support indicates displacement. In an alternative embodiment, the test compound is added first, with incubation and washing, followed by the competitor. The absence of binding by the competitor indicates that the test compound binds to the cancer protein with higher affinity than the competitor. Thus, if the test compound is labeled, the presence of the label on the support, coupled with a lack of competitor binding, indicates that the test compound binds to and thus potentially modulates the cancer protein of the invention. Accordingly, the competitive binding methods comprise differential screening to identity agents that are capable of modulating the activity of the cancer proteins of the invention. In this embodiment, the methods comprise combining a cancer protein and a competitor in a first sample. A second sample comprises a test compound, the cancer protein, and a competitor. The binding of the competitor is determined for both samples, and a change, or difference in binding between the two samples indicates the presence of an agent capable of binding to the cancer protein and potentially modulating its activity. That is, if the binding of the competitor is different in the second sample relative to the first sample, the agent is capable of binding to the cancer protein. Alternatively, differential screening is used to identify drug candidates that bind to the native cancer protein, but cannot bind to modified cancer proteins. For example the structure of the cancer protein is modeled and used in rational drug design to synthesize agents that interact with that site, agents which generally do not bind to site-modified proteins. Moreover, such drug candidates that affect the activity of a native cancer protein are also identified by screening drugs for the ability to either enhance or reduce the activity of such proteins. 82 Positive controls and negative controls can be used in the assays. Preferably control and test samples are performed in at least triplicate to obtain statistically significant results. Incubation of all samples occurs for a time sufficient to allow for the binding of the agent to the protein. Following incubation, samples are washed free of non-specifically bound material and the amount of bound, generally labeled agent determined. For example, where a radiolabel is employed, the samples can be counted in a scintillation counter to determine the amount of bound compound. A variety of other reagents can be included in the screening assays. These include reagents like salts, neutral proteins, e.g. albumin, detergents, etc. which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Also reagents that otherwise improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc., can be used. The mixture of components is added ir an order that provides for the requisite binding. Use of Polynucleotides to Down-regulate or Inhibit a Protein of the Invention. Polynucleotide modulators of cancer can be introduced into a cell containing the target nucleotide sequence by formation of a conjugate with a ligand-binding molecule, as described in WO 91/04753. Suitable ligand-binding molecules include, but are not limited to, cell surface receptors, growth factors, other cytokines, or other ligands that bind to cell surface receptors. Preferably, conjugation of the ligand binding molecule does not substantially interfere with the ability of the ligand binding molecule to bind to its corresponding molecule or receptor, or block entry of the sense or antisense oligonudeolide or its conjugated version into the cell. Alternatively, a polynudeotide modulator of cancer can be introduced into a cell containing the target nucleic acid sequence, e.g., by formation of a polynudeotide-lipid complex, as described in WO 90/10448. It is understood that the use of antisense molecules or knock out and knock in models may also be used in screening assays as discussed above, in addition to methods of treatment. Inhibitory and Antisense Nucleotides In certain embodiments, the activity of a cancer-associated protein is down-regulated, or entirely inhibited, by the use of antisense polynucleotide or inhibitory small nuclear RNA (snRNA), i.e., a nucleic acid complementary to, and which can preferably hybridize specifically to, a coding mRNA nucleic acid sequence, e.g., a cancer protein of the invention, mRNA, or a subsequence thereof. Binding of the antisense polynucleotide to the mRNA reduces the translation and/or stability of the mRNA. In the context of this invention, antisense polynudeotides can comprise naturally occurring nudeotides, or synthetic species formed from naturally occurring subunits or their close homologs. Antisense polynucleotides may also have altered sugar moieties or inter-sugar linkages. Exemplary among these are the phosphorothioate and other sulfur containing species which are known for use in the art. Analogs are comprised by this invention so long as they function effectively to hybridize with nucleotides of the invention. See, e.g., Isis Pharmaceuticals, Carlsbad, CA: Sequitor, Inc., Natick, MA. Such antisense polynucleotides can readily be synthesized using recombinant means, or can be synthesized in vitro. Equipment for such synthesis is sold by several vendors, including Applied Biosystems. The preparation of other oligonudeotides such as phosphorothioates and alkylated derivatives is also well known to those of skill in the art. Antisense molecules as used herein include antisense or sense oligonucleotides. Sense oligonudeotides can, e.g., be employed to block transcription by binding to the anti-sense strand. The antisense and sense oligonuceotide comprise a single stranded nucleic acid sequence (either RNA or DNA) capable of binding to target mRNA (sense) or DNA (antisense) sequences for cancer molecules. Antisense or sense oligonudeotides, according to the present invention, comprise a fragment generally at least about 12 nudeotides, preferably from about 12 to 30 nucleotides. The ability to derive 83 an antisense or a sense oligonudeotide, based upon a cDNA sequence encoding a given protein is described in, e.g., Stein &Cohen (Cancer Res. 48:2659 (1988 and van der Krol et at. (BioTechniques 6:958 (1988)). Ribozymes In addition to antisense polynudeotides, ribozymes can be used to target and inhibit transcription of cancer associated nucleotide sequences. A ribozyme is an RNA molecule that catalytically cleaves other RNA molecules. Different kinds of ribozymes have been described, including group I ribozymes, hammerhead ribozymes, hairpin ribozymes, RNase P, and axhead ribozymes (see, e.g., Castanotto et al., Adv. in Pharmacology 25: 289-317 (1994) for a general review of the properties of different ribozymes). The general features of hairpin ribozymes are described, e.g., in Hampel et al., Nucl. Acids Res. 18:299-304 (1990); European Patent Publication No. 0360257; U.S. Patent No. 5,254,678. Methods of preparing are well known to those of skill in the art (see, e.g., WO 94/26877; Ojwang et al., Proc. Natb. Acad. Sci. USA 90:6340-6344 (1993); Yamada et al., Human Gene Therapy 1:39-45 (1994); Leavitt et al., Proc. Nat. Acad Sci. USA 92:699- 703 (1995); Leavitt et al., Human Gene Therapy 5: 1151-120 (1994); and Yamada et al., Virology 205: 121-126 (1994)). Use of Modulators in Phenolypic Screening In one embodiment, a test compound is administered to a population of cancer cells, which have an associated cancer expression profile. By "administration" or "contacting" herein is meant that the modulator is added to the cells in such a manner as to allow the modulator to act upon the cell, whether by uptake and intracellular action, or by action at the cell surface. In some embodiments, a nucleic acid encoding a proteinaceous agent (i.e., a peptide) is put into a viral construct such as an adenoviral or retroviral construct, and added to the cell, such that expression of the peptide agent is accomplished, e.g., PCT US97/01019. Regulatable gene therapy systems can also be used. Once the modulator has been administered to the cells, the cells are washed if desired and are allowed to incubate under preferably physiological conditions for some period. The cells are then harvested and a new gene expression profile is generated. Thus, e.g., cancer tissue is screened for agents that modulate, e.g., induce or suppress, the cancer phenotype. A change in at least one gene, preferably many, of the expression profile indicates that the agent has an effect on cancer activity. Similarly, altering a biological function or a signaling pathway is indicative of modulator activity. By defining such a signature for the cancer phenotype, screens for new drugs that alter the phenotype are devised. With this approach, the drug target need not be known and need not be represented in the original gene/protein expression screening platform, nor does the level of transcript for the target protein need to change. The modulator inhibiting function will serve as a surrogate marker As outlined above, screens are done to assess genes or gene products. That is, having identified a particular differentially expressed gene as important in a particular state, screening of modulators of either the expression of the gene or the gene product itself is performed. Use of Modulators to Affect Peptides of the Invention Measurements of cancer polypeptide activity, or of the cancer phenotype are performed using a variety of assays. For example, the effects of modulators upon the function of a cancer polypeptide(s) are measured by examining parameters described above. A physiological change that affects activity is used to assess the influence of a test compound on the polypeptides of this invention. When the functional outcomes are determined using intact cells or animals, a variety of effects can be assesses such as, in the case of a cancer associated with solid tumors, tumor growth, tumor metastasis, neovascularization, hormone release, transcriptional changes to both known and uncharacterized genetic markers (e.g., by Northern blots), changes in cell metabolism such as cell growth or pH changes, and changes in intracellular second messengers such as cGNIP. R4 Methods of Identifying Characterizing Cancer-associated Sequences Expression of various gene sequences is correlated with cancer. Accordingly, disorders based on mutant or variant cancer genes are determined. In one embodiment, the invention provides methods for identifying cells containing variant cancer genes, e.g., determining the presence of, all or part, the sequence of at least one endogenous cancer gene in a cell. This is accomplished using any number of sequencing techniques. The invention comprises methods of identifying the cancer genotype of an individual, e.g., determining all or part of the sequence of at least one gene of the invention in the individual. This is generally done in at least one tissue of the individual, e.g., a tissue set forth in Table I, and may include the evaluation of a number of tissues or different samples of the same tissue. The method may indude comparing the sequence of the sequenced gene to a known cancer gene, i.e., a wild-type gene to determine the presence of family members, homologies, mutations or variants. The sequence of all or part of the gene can then be compared to the sequence of a known cancer gene to determine if any differences exist. This is done using any number of known homology programs, such as BLAST, Bestfit, etc. The presence of a difference in the sequence between the cancer gene of the patient and the known cancer gene correlates with a disease state or a propensity for a disease state, as outlined herein. In a preferred embodiment, the cancer genes are used as probes to determine the number of copies of the cancer gene in the genome. The cancer genes are used as probes to determine the chromosomal localization of the cancer genes. Information such as chromosomal localization finds use in providing a diagnosis or prognosis in particular when chromosomal abnormalities such as translocations, and the like are identified in the cancer gene locus. XIV.) Kits/Articles of Manufacture For use in the diagnostic and therapeutic applications described herein, kits are also within the scope of the invention. Such kits can comprise a carrier, package or container that is compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used in the method. For example, the container(s) can comprise a probe that is or can be detectably labeled.- Such probe can be an antibody or polynucleotide specific for a Figure 2-related protein or a Figure 2 gene or message, respectively. Where the method utilizes nucleic acid hybridization to detect the target nucleic acid, the kit can also have containers containing nucleotide(s) for amplification of the target nucleic acid sequence and/or a container comprising a reporter-means, such as a biotin-binding protein, such as avidin or streptavidin, bound to a reporter molecule, such as an enzymatic, florescent, or radioisotope label. The kit can include all or part of the amino acid sequences in Figure 2 or Figure 3 or analogs thereof, or a nucleic acid molecules that encodes such amino acid sequences. The kit of the invention will typically comprise the container described above and one or more other containers comprising materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes; carrier, package, container, vial and/or tube labels listing contents and/or instructions for use, and package inserts with instructions for use. A label can be present on the container to indicate that the composition is used for a specific therapy or non-therapeutic application, such as a diagnostic or laboratory application, and can also indicate directions for either in vivo or in vffm use, such as those described herein. Directions and or other information can also be included on an insert(s) or label(s) which is included with or on the kit. The terms "kit" and "artide of manufacture" can be used as synonyms. In another embodiment of the invention, an article(s) of manufacture containing compositions, such as amino acid sequence(s), small molecule(s), nudeic acid sequence(s), and/or antibody(s), e.g., materials useful for the diagnosis, prognosis, prophylaxis and/or treatment of neoplasias of tissues such as those set forth in Table I is provided. The article of 85 manufacture typically comprises at least one container and at least one label. Suitable containers include, for example, bottles, vials, syringes, and test tubes. The containers can be formed from a variety of materials such as glass or plastic. The container can hold amino acid sequence(s), small molecule(s), nucleic acid sequence(s), and/or antibody(s), in one embodiment the container holds a polynucleotide for use in examining the mRNA expression profile of a cell,. together with reagents used for this purpose. The container can altematively hold a composition which is effective for treating, diagnosis, prognosing or prophylaxing a condition and can have a sterile access port (for example the container can be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). The active agents in the composition can be an antibody capable of specifically binding 98P4B6 and modulating the function of 98P4B6. The label can be on or associated with the container. A label a can be on a container when letters, numbers or other characters forming the label are molded or etched into the container itself; a label can be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package insert. The label can indicate that the composition is used for diagnosing, treating, prophylaxing or prognosing a condition, such as a neoplasia of a tissue set forth in Table 1. The article of manufacture can further comprise a second container comprising a pharmaceutically-acceptable buffer, such as phosphate-buffered saline, Ringers solution and/ordextrose solution. It'can further include other materials desirable from a commercial and user standpoint, including other buffers, diluents, filters, stirrers, needles, syringes, and/or package inserts with indications and/or instructions for use. EXAMPLES: Various aspects of the invention are further described and illustrated by way of the several examples that follow, none of which are intended to limit the scope of the invention. Example 1: SSH-Generated Isolation of cDNA Fragment of the 98P486 Gene To isolate genes that are over-expressed in prostate cancer we used the Suppression Subtractive Hybridization (SSH) procedure using cONA derived from prostate tissues. The 98P4B6 SSH cDNA sequence was derived from normal prostate minus LAPC-4AD prostate xenograft cDNAs. The 98P4B6 cDNA was identified as highly expressed in prostate cancer. Materials and Methods Human Tissues: The patient cancer and normal tissues were purchased from different sources such as the NDRI (Philadelphia, PA). mRNA for some normal tissues were purchased from Clontech, Palo Alto, CA. RNA Isolation: Tissues were homogenized in Trizol reagent (Life Technologies, Gibco BRL) using 10 ml/ g tissue isolate total RNA. Poly A RNA was purified from total RNA using Qiagen's Oligotex mRNA Mini and Midi kits. Total and mRNA were quantified by spectrophotometric analysis (O.D. 260/280 nm) and analyzed by gel electrophoresis. Oliqonucleotides: The following HPLC purified oligonucleotides were used. DPNCDN (cDNA synthesis primer): 5'TTTTGATCAAGCT 3 o3' (SEQ ID NO: 101) Adaptor 1: 5'CTAATACGACTCACTATAGGGCTCGAGCGGCCGCCCGGGCAG3'(SEQ ID NO: 102) R6 3'GGCCCGTCCTAG5' (SEQ ID NO: 103) Adaptor 2: 5'GTAATACGACTCACTATAGGGCAGCGTGGTCGCGGCCGAG3' (SEQ ID NO: 104) 3'CGGCTCCTAG5' (SEQ ID NO: 105) PCR prmer 1: 5'CTAATACGACTCACTATAGGGC3' (SEQ ID NO: 106) Nested primer (NP)1: 5TCGAGCGGCCGCCCGGGCAGGA3' (SEQ ID NO: 107) Nested primer (NP)2: 5'AGCGTGGTCGCGGCCGAGGA3' (SEQ ID NO: 108) Suppression Subtractive Hybridization: Suppression Subtractive Hybridization (SSH) was used to identify cDNAs corresponding to genes that may be differentially expressed in prostate cancer. The SSH reaction utilized cDNA from prostate cancer xenograft and normal tissues. The gene 98P486 sequence was derived from normal prostate Ussue minus prostate cancer xenograft LAPC4AD cDNA subtraction. The SSH DNA sequence (Figure 1) was identified. The cDNA derived from LAPC-4AD was used as the source of the "driver" cDNA, while the cDNA from normal prostate was used as the source of the 'tester" cDNA. Double stranded cDNAs corresponding to tester and driver cDNAs were synthesized from 2 pg of poly(A)+ RNA isolated from the relevant tissue, as described above;using CLONTECH's PCR-Select cDNA Subtraction Kit and I ng of oligonucleotide DPNCDN as primer. First- and second-strand synthesis were carried out as described in the Kit's user manual protocol (CLONTECH Protocol No. PT1117-1, Catalog No. K1804-1). The resulting cDNA was digested with Dpn il for 3 hrs at 370C. Digested cDNA was extracted with phenol/chloroform (1:1) and ethanol precipitated. Driver cDNA was generated by combining in a 1:1 ratio Dpn 11 digested cDNA from the relevant tissue source (see above) with digested cDNAs derived from normal tissue. Tester cDNA was generated by diluting 1 p1 of Dpn 11 digested cDNA from the relevant tissue source (see above) (400 ng) in 5 pd of water. The diluted cDNA (2 pd, 160 ng) was then ligated to 2 pd of Adaptor 1 and Adaptor 2 (10 pM), in separate ligation reactions, in a total volume of 10 d at 160C overnight, using 400 u of T4 DNA ligase (CLONTECH). Ligation was terminated with 1 p of 0.2 M EDTA and heating at 72oC for 5 min. The first hybridization was performed by adding 1.5 pd (600 ng) of driver cDNA to each of two tubes containing 1.5 p1(20 ng) Adaptor 1- and Adaptor 2- ligated tester cDNA. In a final volume of 4 pd, the samples were overlaid with mineral oil, denatured in an MJ Research thermal cycler at 980C for 1.5 minutes, and then were allowed to hybridize for 8 hrs at 68C. The two hybridizations were then mixed together with an additional 1 pl of fresh denatured driver cDNA and were allowed to hybridize overnight at 680C. The second hybridization was then diluted in 200 pd of 20 mM Hepes, pH 8.3, 50 mM NaCl, 0.2 mM EDTA, heated at 700C for 7 min. and stored at -20oC. PCR Amplification, Cloning and Sequencing of Gene Framents Generated from SSH: To amplify gene fragments resulting from SSH reactions, two PCR amplifications were performed. In the primary PCR reaction 1 p of the diluted final hybridization mix was added to 1 p of PCR primer 1 (10 pM), 0.5 pI dNTP mix (10 pM), 2.5 p 10 x reaction buffer (CLONTECH) and 0.5 p 50 x Advantage cDNA polymerase Mix (CLONTECH) in a final volume of 25 pd. PCR 1 was conducted using the following conditions: 750C for 5 min., 940C for 25 sec., then 27 cycles of 94oC for 10 sec, 660C for 30 sec, 72CC for 1.5 min. Five separate primary PCR reactions were performed for each experiment. The products were pooled and diluted 1:10 with water. For the secondary PCR reaction, 1 p1 from the pooled and diluted primary PCR reaction was added to the 87 same reaction mix as used for PCR 1, except that primers NP1 and NP2 (10 pM) were used instead of PCR primer 1. PCR 2 was performed using 10-12 cycles of 940C for 10 sec, 680C for 30 sec, and 720C for 1.5 minutes. The PCR products were analyzed using 2% agarose gel electrophoresis. The PCR products were inserted into pCR2.1 using the T/A vector cloning kit (Invitrogen). Transformed E coli were subjected to blue/white and ampicillin selection. White colonies were picked and arrayed into 96 well plates and were grown in liquid culture overnight. To identify inserts, PCR amplification was performed on 1 ul of bacterial culture using the conditions of PCRI and NP1 and NP2 as primers. PCR products were analyzed using 2% agarose gel electrophoresis. Bacterial ones were stored in 20% glycerol in a 96 well format. Plasmid DNA was prepared, sequenced, and subjected to nudeic acid homology searches of the GenBank, dBest, and NCI-CGAP databases. RT-PCR Expression Analysis: First strand cDNAs can be generated from 1 pg of mRNA with oligo (dT)1 2-18 priming using the Gibco-BRL Superscript Preampificatiop system. The manufacturer's protocol was used which included an incubation for 50 min at 420C with reverse transcriptase followed by RNAse H treatment at 370C for 20 min. After completing the reaction, the volume can be increased to 200 pl with water prior to normalization. First strand cDNAs frt?- 16 different normal human tissues can be obtained from Clontech. Normalization of the first strand cDNAs from multiple tissues was performed by using the primers 5'atatcgccgegctcgtcgtcgacaa3' (SEQ ID NO: 109) and 5'agccacacgcagctcattgtagaagg 3' (SEQ ID NO: 110) to amplify P-actin. First strand cDNA (5 pl) were amplified in a total volume of 50 p containing 0.4 pM primers, 0.2 pM each dNTPs, IXPCR buffer (Clontech, 10 mM Tris-HCL, 1.5 mM MgC12, 50 mM KCI, pH8.3) and 1X Klentaq DNA polymerase (Clontech). Five p1 of the PCR reaction can be removed at 18, 20, and 22 cycles and used for agarose gel electrophoresis. PCR was performed using an MJ Research thermal cyder under the following conditions: Initial denaturation can be at 940C for 15 sec, followed by a 18, 20, and 22 cycles of 940C for 15, 650C for 2 min, 720C for 5 sec. A final extension at 720C was carried out for 2 min. After agarose gel electrophoresis, the band intensities of the 283 bp p-actin bands from multiple tissues were compared by visual inspection. Dilution factors for the first strand cDNAs were calculated to result in equal p-actin band intensities in all tissues after 22 cycles of PCR. Three rounds of normalization can be required to achieve equal band intensities in all tissues after 22 cycles of PCR. To determine expression levels of the 98P4B6 gene, 5 p1 of normalized first strand cDNA were analyzed by PCR using 26, and 30 cycles of amplification. Semi-quantitative expression analysis can be achieved by comparing the PCR products at cycle numbers that give light band intensities. The primers used for RT-PCR were designed using the 98P4B6 SSH sequence and are listed below: 98P4B6.1 5'- GACTGAGCTGGAACTGGAAMTTTGT -3'(SEQ ID NO: 111) 98P4B6.2 5'- TTGAGGAGACTTCATCTCACTGG -3'(SEQID NO: 112) Example 2: Isolation of Full Length 98P486 Encoding cDNA The 98P4B6 SSH cDNA sequence was derived from a substraction consisting of normal prostate minus prostate cancer xenograft. The SSH cDNA sequence (Figure 1) was designated 98P486. The 98P4B6 SSH DNA sequence of 183 bp is shown in Figure 1. Full-ength 98P4B6 v.1 (clone GTD3) of 2453 bp was cloned from prostate cDNA library, revealing an ORF of 454 amino acids (Figure 2 and Figure 3). 98P486 v.6 was also cloned from normal prostate library. Other variants of 98P4B6 were also identified and these are listed in Figures 2 and 3.

98P4B6 v.2, v.3, v.4, v.5, v.6, v.7 and v.8 are splice variants of 98P4B6 v.1. 98P4B6 v.9 through v.19 are SNP variants and differ from v.1 by one amino acid. 98P4B6 v.20 through v.24 are SNP variants of v.7. 98P4B6 v.25 through v.38 are SNP variants of v.8. Though these SNP variants were shown separately, they could also 5 occur in any combinations and in any transcript variants. Example 3: Chromosomal Mapping of 98P4B6 Chromosomal localization can implicate genes in disease pathogenesis. Several chromosome mapping approaches are available including fluorescent in situ 10 hybridization (FISH), human/hamster radiation hybrid (RH) panels (Walter et al., 1994; Nature Genetics 7:22; Research Genetics, Huntsville Al), human-rodent somatic cell hybrid panels such as is available from the Cornell Institute (Camden, New Jersey), and genomic viewers utilizing BLAST homologies to sequenced and mapped genomic clones (NCBI, Bethesda, Maryland). 15 98P4B6 maps to chromosome 7q21 using 98P4B6 sequence and the NCBI BLAST tool: located on the World Wide Web at .ncbi.nlm.nih.gov/genome/seq/page.cgi?F=HsBlast.html&&ORG=Hs). Example 4: Expression Analysis of 98P4B6 20 Expression analysis by RT-PCR demonstrated that 98P4B6 is strongly expressed in prostate cancer patient specimens. First strand cDNA was generated from normal stomach, normal brain, normal heart, normal liver, normal skeletal muscle, normal testis, normal prostate, normal bladder, normal kidney, normal colon, normal lung, normal pancreas, and a pool of cancer specimens from prostate cancer patients, 25 bladder cancer patients, kidney cancer patients, colon cancer patients, lung cancer patients, pancreas cancer patients, and a pool of 2 patient prostate metastasis to lymph node. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers directed to 98P4B6 v.1, v.13, or/and v.14 (A), or directed specifically to the splice variants 98P4B6 v.6 and v.8 (B), was performed at 26 and 30 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Results show strong expression of 98P4B6 and its splice variants v.6 and v.8 in normal prostate and in prostate cancer. Expression was also detected in bladder cancer, kidney cancer, colon cancer, lung cancer, pancreas cancer, breast cancer, cancer metastasis as well as in the prostate 35 cancer metastasis to lymph node specimens, compared to all normal tissues tested. As noted below, e.g., in Example 6, as 98P4B6 v.1 is in expressed in cancer tissues such as 89 those listed in Table 1, the other protein-encoding 98P4B6 variants are expressed in these tissues as well; this principle is corroborated by data (not shown) for the proteins herein designated 98P4B6 v.6 or v.8 is found, e.g., in prostate, lung, ovary, bladder, breast, colon, kidney and pancreas, cancers, as well as in the literature (Porkka et al., 5 Lab Invest, 2002 and Korkmaz et al., JBC, 2002) where the protein 98P4B6 v.8 is identified in normal prostate and prostate cancer. When the genomic region to which a gene maps is modulated in a particular cancer, the alternative transcripts or splice variants of the gene are modulated as well. Disclosed herein is that 98P4B6 has a particular expression profile related to cancer. 10 Alternative transcripts and splice variants of 98P4B6 are also involved in cancers in the same or additional tissues, thus serving as tumor-associated markers/antigens. Expression of 98P4B6 v.1, v.13, and/or v.14 was detected in prostate, lung, ovary, bladder, cervix, uterus and pancreas cancer patient specimens. .First strand cDNA was prepared from a panel of patient cancer specimens. Normalization was 15 performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 98P4B6, was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Expression was recorded as absent, low, medium or strong. Results show expression of 98P4B6 in the majority of all patient cancer specimens tested. 20 98P4B6 is expressed in stomach cancer patient specimens. (A) RNA was extracted from normal stomach (N) and from 10 different stomach cancer patient specimens (T). Northern blot with 10 pg of total RNA/lane was probed with 98P4B6 sequence. Results show strong expression of 98P4B6 in the stomach tumor tissues and lower expression in normal stomach. The lower panel represents ethidium bromide 25 staining of the blot showing quality of the RNA samples. (B) Expression of 98P4B6 was assayed in a panel of human stomach cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 98P4B6 was detected in 7 out of 8 stomach tumors but not in the matched normal tissues. 30 Example 5: Transcript Variants of 98P4B6 Transcript variants are variants of mature mRNA from the same gene which arise by alternative transcription or alternative splicing. Alternative transcripts are transcripts from the same gene but start transcription at different points. Splice variants are mRNA variants spliced differently from the same transcript. In eukaryotes, when a 35 multi-exon gene is transcribed from genomic DNA, the initial RNA is spliced to produce functional mRNA, which has only exons and is used for translation into an 90 amino acid sequence. Accordingly, a given gene can have zero to many alternative transcripts and each transcript can have zero to many splice variants. Each transcript variant has a unique exon makeup, and can have different coding and/or non-coding (5' or 3' end) portions, from the original transcript. Transcript variants can code for similar 5 or different proteins with the same or a similar function or can encode proteins with different functions, and can be expressed in the same tissue at the same time or in different tissues at the same time or in the same tissue at different times or in different tissues at different times. Proteins encoded by transcript variants can have similar or different cellular or extracellular localizations, e.g., secreted versus intracellular. 10 Transcript variants are identified by a variety of art-accepted methods. For example, alternative transcripts and splice variants are identified by full-length cloning experiment, or by use of full-length transcript and EST sequences. First, all human ESTs were grouped into clusters which show direct or indirect identity with each other. Second, ESTs in the same cluster were further grouped into sub-clusters and assembled 15 into a consensus sequence. The original gene sequence is compared to the consensus sequence(s) or other full-length sequences. Each consensus sequence is a potential splice variant for that gene. Even when a variant is identified that is not a full-length clone, that portion of the variant is very useful for antigen generation and for further cloning of the full-length splice variant, using techniques known in the art. 20 Moreover, computer programs are available in the art that identify transcript variants based on genomic sequences. Genomic-based transcript variant identification programs include FgenesH (A. Salamov and V. Solovyev, "Ab initio gene finding in Drosophila genomic DNA," Genome Research. 2000 April; 10(4):516-22); Grail (URL compbio.oml.gov/Grail-bin/EmptyGraitForm) and GenScan (URL 25 genes.mit.edu/GENSCAN.html). For a general discussion of splice variant identification protocols see., e.g., Southan, C., A genomic perspective on human proteases, FEBS Lett. 2001 Jun 8; 498(2-3):214-8; de Souza, S.J., et al., Identification of human chromosome 22 transcribed sequences with ORF expressed sequence tags, Proc. Natl Acad Sci U S A. 2000 Nov 7; 97(23):12690-3. 30 To further confirm the parameters of a transcript variant, a variety of techniques are available in the art, such as full-length cloning, proteomic validation, PCR-based validation, and 5' RACE validation, etc. (see e.g., Proteomic Validation: Brennan, S.O., et al., Albumin banks peninsula: a new termination variant characterized by electrospray mass spectrometry, Biochem Biophys Acta. 1999 Aug 17;1433(1-2):321 35 6; Ferranti P, et al., Differential splicing of pre-messenger RNA produces multiple forms of mature caprine alpha(sl)-casein, Eur J Biochem.1997 Oct 1;249(l):1-7. For 91 PCR-based Validation: Wellmann S, et al., Specific reverse transcription-PCR quantification of vascular endothelial growth factor (VEGF) splice variants by LightCycler technology, Clin Chem. 2001 Apr;47(4):654-60; Jia, H.P., et al., Discovery of new human beta-defensins using a genomics-based approach, Gene. 2001 5 Jan 24; 263(1-2):211-8. For PCR-based and 5' RACE Validation: Brigle, K.E., et al., Organization of the murine reduced folate carrier gene and identification of variant splice forms, Biochem Biophys Acta. 1997 Aug 7; 1353(2):191-8). It is known in the art that genomic regions are modulated in cancers. Recently, Porkka et al. (2002) reported that transcript variants of STEAP2 were expressed and 10 were found in both normal and malignant prostate tissue (Porkka, K.P., et al. Cloning and characterization of a novel six-transmembrane protein STEAP2, expressed in normal and malignant prostate. Laboratory Investigation 2002 Nov; 82(11):1573 1582). Another group of scientists also reported that transcript -variants of STEAP2 (98P4B6 v.6 herein) also were expressed significantly higher in prostate cancer than 15 normal prostate (Korkmaz, K.S., et al. Molecular cloning and characterization of STAMP 1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer. The Journal of Biological Chemistry. 2002 Sept. 277(39):36689 36696.). When the genomic region to which a gene maps is modulated in a particular cancer, the alternative transcripts or splice variants of the gene are modulated as well. 20 Disclosed herein is that 98P4B6 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 98P4B6 are also involved in cancers in the same or additional tissues, thus serving as tumor-associated markers/antigens. Using the full-length gene and EST sequences, seven transcript variants were identified, designated as 98P4B6 v.2, v.3, v.4, v.5, v.6, v.7 and v.8. The boundaries of 25 exons in the original transcript, 98P4B6 v.1 were shown in Table LI. The first 22 bases of v.1 were not in the nearby 5' region of v.1 on the current assembly of the human genome. Compared with 98P4B6 v.1, variant v.2 was a single exon transcript whose 3' portion was the same as the last exon of v.1. The first two exons of v.3 were in intron 1 of v.1. Variants v.4, v.5, and v.6 spliced out 224-334 in the first exon of v.l. In 30 addition, v.5 spliced out exon 5 while v.6 spliced out exon 6 but extended exon 5 of v.1. Variant v.7 used alternative transcription start and different 3' exons. Variant v.8 extended 5' end and kept the whole intron 5 of v.1. Theoretically, each different combination of exons in spatial order, e.g. exons 2 and 3, is a potential splice variant. Tables LII through LV are set forth on a variant-by-variant basis. Tables LII(a) 35 - (g) show the nucleotide sequence of the transcript variant. Tables LIII (a) - (g) show the alignment of the transcript variant with the nucleic acid sequence of 98P4B6 v.1. 92 Tables LIV(a) - (g) lay out the amino acid translation of the transcript variant for the identified reading frame orientation. Tables LV(a) - (g) display alignments of the amino acid sequence encoded by the splice variant with that of 98P4B6 v.1. Additionally, single nucleotide polymorphisms (SNP) are noted in the alignment. 5 Example 6: Single Nucleotide Polymorphisms of 98P4B6 A Single Nucleotide Polymorphism (SNP) is a single base pair variation in a nucleotide sequence at a specific location. At any given point of the genome, there are four possible nucleotide base pairs: A/T, C/G, G/C and T/A. Genotype refers to the 10 specific base pair sequence of one or more locations in the genome of an individual. Haplotype refers to the base pair sequence of more than one location on the same DNA molecule (or the same chromosome in higher organisms), often in the context of one gene or in the context of several tightly linked genes. SNP that occurs on a cDNA is called cSNP. This cSNP may change amino acids of the protein encoded by the gene 15 and thus change the functions of the protein. Some SNP cause inherited diseases; others contribute to quantitative variations in phenotype and reactions to environmental factors including diet and drugs among individuals. Therefore, SNP and/or combinations of alleles (called haplotypes) have many applications, including diagnosis of inherited diseases, determination of drug reactions and dosage, identification of 20 genes responsible for diseases, and analysis of the genetic relationship between individuals (P. Nowotny, J. M. Kwon and A. M. Goate, "SNP analysis to dissect human traits," Curr. Opin. Neurobiol. 2001 Oct; 11(5):637-641; M. Pirmohamed and B. K. Park, "Genetic susceptibility to adverse drug reactions," Trends Pharmacol. Sci. 2001 Jun; 22(6):298-305; J. H. Riley, C. J. Allan, E. Lai and A. Roses, "The use of single 25 nucleotide polymorphisms in the isolation of common disease genes," Pharmacogenomics. 2000 Feb; 1(l):39-47; R. Judson, J. C. Stephens and A. Windemuth, "The predictive power of haplotypes in clinical response," Pharmacogenomics. 2000 Feb; 1(1): 15-26). SNP are identified by a variety of art-accepted methods (P. Bean, "The 30 promising voyage of SNP target discovery," Am. Clin. Lab. 2001 Oct-Nov; 20(9):18 20; K. M. Weiss, "In search of human variation," Genome Res. 1998 Jul; 8(7):691-697; M. M. She, "Enabling large-state pharmacogenetic studies by high-throughput mutation detection and genotyping technologies," Clin. Chem. 2001 Feb; 47(2):164-172). For example, SNP can be identified by sequencing DNA fragments that show 35 polymorphism by gel-based methods such as restriction fragment length polymorphism (RFLP) and denaturing gradient gel electrophoresis (DGGE). They can also be 92A discovered by direct sequencing of DNA samples pooled from different individuals or by comparing sequences from different DNA samples. With the rapid accumulation of sequence data in public and private databases, one can discover SNP by comparing sequences using computer programs (Z. Gu, L. Hillier and P. Y. Kwok, "Single 5 nucleotide polymorphism hunting in cyberspace," Hum. Mutat. 1998; 12(4):221-225). SNP can be verified and genotype or haplotype of an individual can be determined by a variety of methods including direct sequencing and high throughput microarrays (P. Y. Kwok, "Methods for genotyping single nucleotide polymorphisms," Annu. Rev. Genomics Hum. Genet. 2001; 2:235-258; M. Kokoris, K. Dix, K. Moynihan, J. Mathis, 10 B. Erwin, P. Grass, B. Hines and A. Duesterhoeft, "High-throughput SNP genotyping with the Masscode system," Mol. Diagn. 2000 Dec; 5(4):329-340). Using the methods described above, eleven SNP were identified in the original transcript, 98P4B6 v.1, at positions 46 (A/G), 179 (C/T), 180 (A/G), 269 (A/G), 404 (G/T), 985 (C/T), 1170 (T/C), 1497 (A/G), 1746 (T/G), 2046 (T/G) and 2103 (T/C). 15 The transcripts or proteins with alternative allele were designated as variant 98P4B6 v.9 through v.19. These alleles of the SNP can occur in different combinations (haplotypes) and in any one of the transcript variants (such as 98P4B6 v.5) that contains the site of the SNP. In addition, there were SNP in other transcript variants in regions not shared with v.1. For example, there were fourteen SNP in the fifth intron of 20 v.1, which was part of transcript variants v.2, v.6 and v.8. These SNP are listed as following (numbers relative v.8): 1760 (G/A), 1818 (G/T), 1870 (C/T), 2612 (T/C), 2926 (T/A), 4241 (T/A), 4337 (A/G), 4338 (A/C), 4501 (A/G), 4506 (C/T), 5434 (C/A), 5434 (C/G), 5434 (C/T) and 5589 (C/A). The SNP in the unique regions of transcript variant v.7 are as follows: 1956 (A/C), 1987 (T/A), 2010 (G/C), 2010 (G/T) 25 and 2059 (G/A) (numbers correspond to nucleotide sequence of v.7). Example 7: Production of Recombinant 98P4B6 in Prokaryotic Systems To express recombinant 98P4B6 and 98P4B6 variants in prokaryotic cells, the full or partial length 98P4B6 and 98P4B6 variant cDNA sequences are cloned into any 30 one of a variety of expression vectors known in the art. One or more of the following regions of 98P4B6 variants are expressed: the full length sequence presented in Figures 2 and 3, or any 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 contiguous amino acids from 98P4B6, variants, or analogs thereof. A. In vitro transcription and translation constructs: 35 pCRII: To generate 98P4B6 sense and anti-sense RNA probes for RNA in situ investigations, pCRII constructs (Invitrogen, Carlsbad CA) are generated encoding 92B either all or fragments of the 98P4B6 cDNA. The pCRII vector has Sp6 and T7 promoters flanking the insert to drive the transcription of 98P4B6 RNA for use as probes in RNA in situ hybridization experiments. These probes are used to analyze the cell and tissue expression of 98P4B6 at the RNA level. Transcribed 98P4B6 RNA 5 representing the cDNA amino acid coding region of the 98P4B6 gene is used in in vitro translation systems such as the TnTTm Coupled Reticulolysate System (Promega, Corp., Madison, WI) to synthesize 98P4B6 protein. 92C B. Bacterial Constructs: pGEX Constructs: To generate recombinant 98P4B6 proteins in bacteria that are fused to the Glutathione S transferase (GST) protein, all or paids of the 98P4B6 cDNA protein coding sequence are cloned into the pGEX family of GST-fusion vectors (Amersham Pharmacia Biotech, Piscataway, NJ). These constructs allow controlled expression of recombinant 98P4B6 protein sequences with GST fused at the amino-terminus and a six histidine epitope (6X His) at the carboxyl-terminus. The GST and 6X His tags permit purification of the recombinant fusion protein from induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-GST and anti-His antibodies. The 6X His tag is generated by adding 6 histidine codons to the cloning primer at the 3 end, e.g., of the open reading frame (ORF). A proteolytic cleavage site, such as the PreScissionTM recognition site in pGEX-6P-1, may be employed such that it permits deavage of the GST tag from 98P486-related protein. The ampicillin resistance gene and pBR322 origin permits selection and maintenance of the pGEX plasmids in E. coli. A glutathione-S-transferase (GST) fusion protein encompassing amino acids 2-204 of the STEAP-2 protein sequence was generated in the pGEX vector. The recombinant GST-STEAP-2 fusion protein was purified from induced bacteria by glutathione-sepaharose affinity chromatography and used as immunogen for generation of a polyclonal antibody. pMAL Constructs: To generate, in bacteria, recombinant 98P4B6 proteins that are fused to maltose-binding protein (MBP), all or parts of the 98P4B6 cDNA protein coding sequence are fused to the MBP gene by cloning into the pMAL-c2X and pMAL-p2X vectors (New England Biolabs, Beverly, MA). These constructs allow controlled expression of recombinant 98P4B6 protein sequences with MBP fused at the amino-terminus and a 6X His epitope tag at the carboxyl terminus. The MBP and 6X His tags permit purification of the recombinant protein from induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-MBP and anti-His antibodies. The 6X His epitope tag is generated by adding 6 histidine codons to the 3' cloning primer. A Factor Xa recognition site permits cleavage of the pMAL tag from 98P4B6. The pMAL-c2X and pMAL-p2X vectors are optimized to express the recombinant protein in the cytoplasm or periplasm respectively. Periplasm expression enhances folding of proteins with disulfide bonds. PET Constructs: To express 98P4B6 in bacterial cells, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pET family of vectors (Novagen, Madison, WI). These vectors allow tightly controlled expression of recombinant 98P4B6 protein in bacteria with and without fusion to proteins that enhance solubility, such as NusA and thioredoxin (Trx), and epitope tags, such as 6X His and S-Tag I that aid purification and detection of the recombinant protein. For example, constructs are made utilizing pET NusA fusion system 43.1 such that regions of the 98P4B6 protein are expressed as amino-terminal fusions to NusA. C. Yeast Constructs: pESC Constructs: To express 98P4B6 in the yeast species Saccharomyces cerevisiae for generation of recombinant protein and functional studies, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pESC family of vectors each of which contain 1 of 4 selectable markers, HIS3, TRP1, LEU2, and URA3 (Stratagene, La Jolla, CA). These vectors allow controlled expression from the same plasmid of up to 2 different genes or cloned sequences containing either Flag1" or Myc epitope tags in the same yeast cell. This system is useful to confirm potein-protein interactions of 98P4B6. In addition, expression in yeast yields similar post-translational modifications, such as glycosylations and phosphorylations, that are found when expressed in eukaryotic cells. pESP Constructs: To express 98P4B6 in the yeast species Saccharomyces pombe, all or parts of the 98P486 cDNA protein coding sequence are cloned into the pESP family of vectors. These vectors allow controlled high level of expression of a 98P4B6 protein sequence that is fused at either the amino terminus or at the carboxyl terminus to GST which aids purification of the recombinant protein. A FlagTmepitope tag allows detection of the recombinant protein with anti- FlagTM antibody. 93 Example 8: Production of Recombinant 98P4B6 in Higher Eukaryotic Systems A. Mammalian Constructs: To express recombinant 98P4B6 in eukaryotic cells, the full or partial length 98P4B6 cDNA sequences can be cloned into any one of a variety of expression vectors 5 known in the art. One or more of the following regions of 98P4B6 are expressed in these constructs, amino acids I to 255, or any 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 contiguous amino acids from 98P4B6 v.1 through v.11; amino acids I to 1266, or any 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 contiguous amino acids 10 from 98P4B6 v.12 and v.13, variants, or analogs thereof. The constructs can be transfected into any one of a wide variety of mammalian cells such as 293T cells. Transfected 293T cell lysates can be probed with the anti 98P4B6 polyclonal serum, described herein. pcDNA4/HisMax Constructs: To express 98P4B6 in mammalian cells, a 15 98P4B6 ORF, or portions thereof, of 98P4B6 are cloned into pcDNA4/HisMax Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter and the SP16 translational enhancer. The recombinant protein has Xpressm and six histidine (6X His) epitopes fused to the amino-terminus. The pcDNA4/HisMax vector also contains the bovine growth hormone (BGH) 20 polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Zeocin resistance gene allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and ColE 1 origin permits selection and maintenance of the plasmid in E. coil. 25 pcDNA3.1/MycHis Constructs: To express 98P4B6 in mammalian cells, a 98P4B6 ORF, or portions thereof, of 98P4B6 with a consensus Kozak translation initiation site was cloned into pcDNA3.1/MycHis Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the myc epitope and 6X His epitope fused to the carboxyl 30 terminus. The pcDNA3.1/MycHis vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability, along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Neomycin resistance gene can be used, as it allows for selection of mammalian cells expressing the protein and the 35 ampicillin resistance gene and ColEl origin permits selection and maintenance of the plasmid in E. coli. 94 pcDNA3.1/GFP Construct: To express 98P4B6 in mammalian cells and to allow detection of the recombinant proteins using fluorescence, the 98P4B6 ORF sequence was codon optimized according to Mirzabekov et al. (1999), and was cloned into pcDNA3..1/GFP vector to generate 98P4B6.GFP.pcDNA3.1 construct. Protein 5 expression was driven from the cytomegalovirus (CMV) promoter. The recombinant protein had the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-invasive, in vivo detection and cell biology studies. The pcDNA3.1/GFP vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA 10 stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Neomycin resistance gene allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColE 1 origin permits selection and maintenance of the plasmid in E. coli. Transfection of 98P4B6.GFP.pcDNA3.1 into 293T cells was performed. 293T 15 cells were transfected with 98P4B6.GFP.pcDNA3.1/mychis construct clone A12 or clone B12. STEAPl.GFP vector was used as a positive control. And as a negative control an empty vector was used. Forty hours later, cell lysates were collected. Samples were run on an SDS-PAGE acrylamide- gel, blotted and stained with either anti-GFP antibody, anti-98P4B6 antibody generated against amino acids 198-389, or 20 anti-98P4B6 antibody generated against amino acids 153-165. The blot was developed using the ECL chemiluminescence kit and visualized by autoradiography. Strong expression of the fusion protein was detected. Strong expression of the fusion protein was also detected by flow cytometry and fluorescent microscopy, resulting in strong expression of the fusion protein by western blot analysis, flow cytometry and 25 fluorescent microscopy. Additional constructs with an amino-terminal GFP fusion are made in pcDNA3. 1/NT-GFP-TOPO spanning the entire length of a 98P4B6 protein. PAPtag: A 98P4B6 ORF, or portions thereof, is cloned into pAPtag-5 (GenHunter Corp. Nashville, TN). This construct generates an alkaline phosphatase 30 fusion at the carboxyl-terminus of a 98P4B6 protein while fusing the IgGK 94A signal sequence to the amino-terminus. Constructs are also generated in which alkaline phosphatase with an amino-terminal IgGK signal sequence is fused to the amino-terminus of a 98P486 protein. The resulting recombinant 98P486 proteins are optimized for secretion into the media of transfected mammalian cells and can be used to identify proteins such as ligands or receptors that interact with 98P486 proteins. Protein expression is driven from the CMV promoter and the recombinant proteins also contain myc and 6X His epitopes fused at the carboxyl-terminus that facilitates detection and purification. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the recombinant protein and the ampicillin resistance gene permits selection of the plasmid in E. coli. pTaq5: A 98P4B6 ORF, or portions thereof, is cloned into pTag-5. This vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generates 98P4B6 protein with an amino-terminal IgGK signal sequence and myc and 6X His epitope tags at the carboxyl-terminus that facilitate detection and affinity purification. The resulting recombinant 98P4B6 protein is optimized for secretion into the media of transfected mammalian cells, and is used as immunogen or igand to identify proteins such as ligands or receptors that interact with the 98P4B6 proteins. Protein expression is driven from the CMV promoter. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the protein, and the ampicillin resistance gene permits selection of the plasmid in E. coli. PsecFc: A 98P4B6 ORF, or portions thereof, is also cloned into psecFc. The psecFc vector was assembled by cloning the human immunoglobulin GI (IgG) Fc (hinge, CH2, CH3 regions) into pSecTag2 (Invitrogen, Califomia). This construct generates an IgGi Fc fusion at the carboxyl-terminus of the 98P4B6 proteins, while fusing the IgGK signal sequence to N-terminus. 98P4B6 fusions utilizing the murine IgG1 Fc region are also used. The resulting recombinant 98P4B6 proteins are optimized for secretion into the media of transfected mammalian cells, and can be used as immunogens or to identify proteins such as ligands or receptors that interact with 98P4B6 protein. Protein expression is driven from the CMV promoter. The hygromycin resistance gene present in the vector allows for selection of mammalian cells that express the recombinant protein, and the ampicillin resistance gene permits selection of the plasmid in E. coli. pSRa Constructs: To generate mammalian cell lines that express 98P4B6 constitutively, 98P4B6 ORF, or portions thereof, of 98P4B6 were cloned into pSRL constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRz constructs into the 293T-10A1 packaging line or co-transfection of pSRct and a helper plasmid (containing deleted packaging sequences) into the 293 cells, respectively. The retrovirus is used to infect a variety of mammalian cell lines, resulting in the integration of the cloned gene, 98P4B6, into the host cell-lines. Protein expression is driven from a long terminal repeat (LTR). The Neomycin resistance gene present in the vector allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColEl origin permit selection and maintenance of the plasmid in E. coli. The retroviral vectors can thereafter be used for infection and generation of various cell lines using, for example, PC3, NIH 3T3, TsuPr1, 293 or rat-I cells. Additional pSRct constructs are made that fuse an epitope tag such as the FLAGTM tag to the carboxyl-terminus of 98P4B6 sequences to allow detection using anti-Flag antibodies. For example, the FLAGIM sequence 5' gat tac aag gat gac gac gat aag 3' (SEQ ID NO: 113) is added to cloning primer at the 3' end of the ORF. Additional pSRa constructs are made to produce both amino-terminal and carboxyl-terminal GFP and myc/6X His fusion proteins of the full-length 98P4B6 proteins. Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 98P4B6. High virus titer leading to high level expression of 98P4B6 is achieved in viral delivery systems such as adenoviral vectors and herpes amplicon vectors. A 98P416 coding sequences or fragments thereof are amplified by PCR and subcloned into the AdEasy shuttle vector (Stratagene). Recombination and virus packaging are performed according to the manufacturer's instructions to generate adenoviral vectors. Altematively, 98P486 coding sequences or fragments thereof are cloned into 95 the HSV-1 vector (Imgenex) to generate herpes viral vectors. The viral vectors are thereafter used for infection of various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. Regulated Expression Systems: To control expression of 98P4B6 in 5 mammalian cells, coding sequences of 98P4B6, or portions thereof, are cloned into regulated mammalian expression systems such as the T-Rex System (Invitrogen), the GeneSwitch System (Invitrogen) and the tightly-regulated Ecdysone System (Sratagene). These systems allow the study of the temporal and concentration dependent effects of recombinant 98P4B6. These vectors are thereafter used to control 10 expression of 98P4B6 in various cell lines such as PC3, NIH 3T3, 293 or rat-I cells. B. Baculovirus Expression Systems To generate recombinant 98P4B6 proteins in a baculovirus expression system, 98P486 ORF, or portions thereof, are cloned into the baculovirus transfer vector pBlueBac 4.5 (Invitrogen), which provides a His-tag at the N-terminus. Specifically, 15 pBlueBac-98P4B6 is co-transfected with helper plasmid pBac-N-Blue (Invitrogen) into SF9 (Spodoptera frugiperda) insect cells to generate recombinant baculovirus (see Invitrogen instruction manual for details). Baculovirus is then collected from cell supernatant and purified by plaque assay. Recombinant 98P4B6 protein is then generated by infection of HighFive insect 20 cells (Invitrogen) with purified baculovirus. Recombinant 98P4B6 protein can be detected using anti-98P4B6 or anti-His-tag antibody. 98P4B6 protein can be purified and used in various cell-based assays or as immunogen to generate polyclonal and monoclonal antibodies specific for 98P4B6. 25 Example 9: Antigenicity Profiles and Secondary Structure Five amino acid profiles of 98P4B6 variants 1, 2, 5-7, were generated by accessing the ProtScale website located on the World Wide Web at .expasy.ch/cgi bin/protscale.pl) on the ExPasy molecular biology server. These profiles: Hydrophilicity, (Hopp T.P., Woods K.R., 1981. Proc. Natl. 30 Acad. Sci. U.S.A. 78:3824-3828); Hydropathicity, (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132); Percentage Accessible Residues (Janin J., 1979 Nature 277:491-492); Average Flexibility, (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept. Protein Res. 32:242-255); Beta-turn (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294); and optionally others available in the art, such as on the 35 ProtScale website, were used to identify antigenic regions of each of the 98P4B6 variant proteins. Each of the above amino acid profiles of 98P4B6 variants were 96 generated using the following ProtScale parameters for analysis: 1) A window size of 9; 2) 100% weight of the window edges compared to the window center; and, 3) amino acid profile values normalized to lie between 0 and 1. Hydrophilicity, Hydropathicity and Percentage Accessible Residues profiles 5 were used to determine stretches of hydrophilic amino acids (i.e., values greater than 0.5 on the Hydrophilicity and Percentage Accessible Residues profile, and values less than 0.5 on the Hydropathicity profile). Such regions are likely to be exposed to the aqueous environment, be present on the surface of the protein, and thus available for immune recognition, such as by antibodies. 10 Average Flexibility and Beta-turn profiles determine stretches of amino acids (i.e., values greater than 0.5 on the Beta-turn profile and the Average Flexibility profile) that are not constrained in secondary structures such as beta sheets and alpha helices. Such regions are also more likely to be exposed on the protein and thus accessible to immune recognition, such as by antibodies. 15 Antigenic sequences of the 98P4B6 variant proteins are used to prepare immunogens, either peptides or nucleic acids that encode them, to generate therapeutic and diagnostic anti-98P4B6 antibodies. The immunogen can be any 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50 or more than 50 contiguous amino acids, or the corresponding nucleic acids that encode them, from 20 the 98P4B6 protein variants 1, 2, 5-7 listed in Figures 2 and 3. In particular, peptide immunogens of the invention can comprise, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profiles 98P4B6 v.1, v.2, v.5, v.6 and v.7; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole 25 number increment that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile 98P4B6 v.1, v.2, v.5, v.6 and v.7; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profiles 98P4B6 v.1, v.2, v.5, v.6 and v.7; a peptide region of at least 5 amino acids of 30 Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profiles 98P4B6 v.1, v.2, v.5, v.6 and v.7; and, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile 98P4B6 v.1, v.2, v.5, v.6 and v.7. Peptide 35 immunogens of the invention can also comprise nucleic acids that encode any of the forgoing. 97 All immunogens of the invention, peptide or nucleic acid, can be embodied in human unit dose form, or comprised by a composition that includes a pharmaceutical excipient compatible with human physiology. The secondary structure of 98P4B6 protein variants 1, 2, 5-7, namely the 5 predicted presence and location of alpha helices, extended strands, and random coils, is predicted from the primary amino acid sequence using the HNN - Hierarchical Neural Network method (Guermeur, 1997, http://pbil.ibcp.fr/cgi bin/npsaautomat.pl?page=npsann.html), accessed from the ExPasy molecular biology server (located on the World Wide Web at :expasy.ch/tools/). The analysis 10 indicates that 98P4B6 variant 1 is composed of 54.41% alpha helix, 12.33% extended strand, and 33.26% random coil. Variant 2 is composed of 17.78% alpha helix, 6.67% extended strand, and 75.56% random coil. Variant 5 is composed of 51.55% alpha helix, 13.13% extended strand, and 35.32% random coil. Variant 6 is composed of 54.49% alpha helix, 11.84% extended strand, and 33.67% random coil. Variant 7 is 15 composed of 48.26% alpha helix, 15.28% extended strand, and 36.46% random coil. Analysis for the potential presence of transmembrane domains in the 98P4B6 variant proteins was carried out using a variety of transmembrane prediction algorithms accessed from the ExPasy molecular biology server (located on the World Wide Web at .expasy.ch/tools/). The results of analysis of variant 1 identified the presence and 20 location of 6 transmembrane domains using the TMpred program and 5 transmembrane domains using the TMHMM program. The results of analysis of variant 2 indicated the presence and location of 1 transmembrane domains using the TMpred program and no transmembrane domains using the TMHMM program. The results of analysis of variant 5 indicated the presence and location of 6 transmembrane domains using the 25 TMpred program and 4 transmembrane domains using the TMHMM program. The results of analysis of variant 6 indicated the presence and location of 6 transmembrane domains using the TMpred program and 6 transmembrane domains using the TMHMM program. The results of analysis of variant 7 indicated the presence and location of 6 transmembrane domains using the TMpred program and 4 transmembrane domains 30 using the TMHMM program. The results of each program, namely the amino acids encoding the transmembrane domains are summarized in Table VI. Example 10: Generation of 98P4B6 Polyclonal Antibodies Polyclonal antibodies can be raised in a mammal, for example, by one or more 35 injections of an immunizing agent and, if desired, an adjuvant. Typically, the immunizing agent and/or adjuvant will be injected in the mammal by multiple 98 subcutaneous or intraperitoneal injections. In addition to immunizing with a full length 98P4B6 protein variant, computer algorithms are employed in design of immunogens that, based on amino acid sequence analysis contain characteristics of being antigenic and available for recognition by the immune system of the immunized host (see 5 Example 9 entitled "Antigenicity Profiles and Secondary Structure"). Such regions would be predicted to be hydrophilic, flexible, in beta-turn conformations, and be exposed on the surface of the protein. For example, recombinant bacterial fusion proteins or peptides containing hydrophilic, flexible, beta-turn regions of 98P4B6 protein variants are used as antigens 10 to generate polyclonal antibodies in New Zealand White rabbits or monoclonal antibodies as described in Example 11. For example, in 98P4B6 variant 1, such regions include, but are not limited to, amino acids 153-165, amino acids 240-260, and amino acids 345-358. In sequence specific for variant 2, such regions include, but are not limited to, amino acids 26-38. In sequence specific for variant 5, such regions include, 15 but are not limited to, amino acids 400-410. In sequence specific for variant 6, such regions include, but are not limited to, amino acids 455-490. In sequence specific for variant 7, such regions include, but are not limited to, amino acids 451-465 and amino acids 472-498. It is useful to conjugate the immunizing agent to a protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic 20 proteins include, but are not limited to, keyhole limpet hemocyanin (KLH), serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. In one embodiment, a peptide encoding amino acids 153-165 of 98P4B6 variant 1 was conjugated to KLH and used to immunize a rabbit. Alternatively the immunizing agent may include all or portions of the 98P4B6 variant proteins, analogs or fusion proteins thereof. For 25 example, the 98P4B6 variant 1 amino acid sequence can be fused using recombinant DNA techniques to any one of a variety of fusion protein partners that are well known in the art, such as glutathione-S-transferase (GST) and HIS tagged fusion proteins. In another embodiment, amino acids 2-204 of 98P4B6 variant 1 was fused to GST using recombinant techniques and the pGEX expression vector, expressed, purified and used 30 to immunize a rabbit. Such fusion proteins are purified from induced bacteria using the appropriate affinity matrix. Other recombinant bacterial fusion proteins that may be employed include maltose binding protein, LacZ, thioredoxin, NusA, or an immunoglobulin constant region (see the section entitled "Production of 98P4B6 in Prokaryotic Systems" and 35 Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et 99 al. eds., 1995; Linsley, P.S., Brady, W., Urnes, M., Grosmaire, L., Damle, N., and Ledbetter, L. (1991) J. Exp. Med. 174, 561-566). In addition to bacterial derived fusion proteins, mammalian expressed protein antigens are also used. These antigens are expressed from mammalian expression 5 vectors such as the Tag5 and Fc-fusion vectors (see the section entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems"), and retain post-translational modifications such as glycosylations found in native protein. In one embodiment, amino acids 324-359 of variant 1, encoding an extracellular loop between transmembrane domains, is cloned into the Tag5 mammalian secretion vector. The 10 recombinant protein is purified by metal chelate chromatography from tissue culture supernatants of 293T cells stably expressing the recombinant vector. The purified Tag5 98P4B6 protein is then used as immunogen. During the immunization protocol, it is useful to mix or emulsify the antigen in adjuvants that enhance the immune response of the host animal. Examples of adjuvants 15 include, but are not limited to, complete Freund's adjuvant (CFA) and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). In a typical protocol, rabbits are initially immunized subcutaneously with up to 200 pg, typically 100-200 ptg, of fusion protein or peptide conjugated to KLH mixed in complete Freund's adjuvant (CFA). Rabbits are then injected subcutaneously every 20 two weeks with up to 200 pg, typically 100-200 pg, of the immunogen in incomplete Freund's adjuvant (IFA). Test bleeds are taken approximately 7-10 days following each immunization and used to monitor the titer of the antiserum by ELISA. To test reactivity and specificity of immune serum, such as the rabbit serum derived from immunization with the Tag5 -98P4B6 variant 1 protein, the full-length 25 98P4B6 variant 1 cDNA is cloned into pCDNA 3.1 myc-his expression vector (Invitrogen, see the Example entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems"). After transfection of the constructs into 293T cells, cell lysates are probed with the anti-98P4B6 serum and with anti-His antibody (Santa Cruz Biotechnologies, Santa Cruz, CA) to determine specific reactivity to denatured 98P4B6 30 protein using the Western blot technique. 98P4B6 variant 1 protein expressed in 293T was detected with polyclonal antibodies raised to a GST-fusion protein and peptide. In addition, the immune serum is tested by fluorescence microscopy, flow cytometry and immunoprecipitation against 293T and other recombinant 98P4B6-expressing cells to determine specific recognition of native protein. Western blot, immunoprecipitation, 35 fluorescent microscopy, and flow cytometric techniques using cells that endogenously 100 express 98P4B6 are also carried out to test reactivity and specificity. Anti-serum from rabbits immunized with 98P4B6 variant fusion proteins, such as GST and MBP fusion proteins, are purified by depletion of antibodies reactive to the fusion partner sequence by passage over an affinity column containing the fusion 5 partner either alone or in the context of an irrelevant fusion protein. For example, antiserum derived from a GST-98P4B6 variant 1 fusion protein was first purified by passage over a column of GST protein covalently coupled to AffiGel matrix (BioRad, Hercules, Calif.). The antiserum is then affinity purified by passage over a column composed of a MBP-98P4B6 fusion protein covalently coupled to Affigel matrix. The 10 serum is then further purified by protein G affinity chromatography to isolate the IgG fraction. Sera from other His-tagged antigens and peptide immunized rabbits as well as fusion partner depleted sera are affinity purified by passage over a column matrix composed of the original protein immunogen or free peptide. 15 Example 11: Generation of 98P4B6 Monoclonal Antibodies (mAbs) In one embodiment, therapeutic mAbs to 98P4B6 variants comprise those that react with epitopes specific for each variant protein or specific to sequences in common between the variants that would disrupt or modulate the biological function of the 98P4B6 variants, for example those that would disrupt the interaction with ligands and 20 binding partners. Immunogens for generation of such mAbs include those designed to encode or contain the entire 98P4B6 protein variant sequence, regions of the 98P4B6 protein variants predicted to be antigenic from computer analysis of the amino acid sequence (see, e.g., Example 9 entitled "Antigenicity Profiles and Secondary Structure"). Immunogens include peptides, recombinant bacterial proteins, and 25 mammalian expressed Tag 5 proteins and human and murine IgG FC fusion proteins. In addition, cells engineered to express high levels of a respective 98P4B6 variant, such as 293T-98P4B6 variant 1 or 300.19-98P4B6 variant 1 murine Pre-B cells, are used to immunize mice. To generate mAbs to a 98P4B6 variant, mice are first immunized 30 intraperitoneally (IP) with, typically, 10-50 jig of protein immunogen or 10' 98P4B6 expressing cells mixed in complete Freund's adjuvant. Mice are then subsequently immunized IP every 2-4 weeks with, typically, 10-50 pig of protein immunogen or 107 cells mixed in incomplete Freund's adjuvant. Alternatively, MPL-TDM adjuvant is used in immunizations. In addition to the above protein and cell-based immunization 35 strategies, a DNA-based immunization protocol is employed in which a mammalian expression vector encoding a 98P4B6 variant sequence is used to immunize mice by I OOA direct injection of the plasmid DNA. For example, amino acids 324-359 is cloned into the Tag5 mammalian secretion vector and the recombinant vector is used as immunogen. In another example the same amino acids are cloned into an Fc-fusion secretion vector in which the 98P4B6 variant 1 sequence is fused at the amino-terminus 5 to an IgK leader sequence and at the carboxyl-terminus to the coding sequence of the human or murine IgG Fc region. This recombinant vector is then used as immunogen. The plasmid immunization protocols are used in combination with purified proteins expressed from the same vector and with cells expressing the respective 98P4B6 variant. 10 During the immunization protocol, test bleeds are taken 7-10 days following an injection to monitor titer and specificity of the immune response. Once appropriate reactivity and specificity is obtained as determined by ELISA, Western blotting, immunoprecipitation, fluorescence microscopy, and flow cytometric analyses, fusion and hybridoma generation is then carried out with established procedures well known 15 in the art (see, e.g., Harlow and Lane, 1988). In one embodiment for generating 98P4B6 monoclonal antibodies, a Tag5 98P4B6 variant 1 antigen encoding amino acids 324-359, is expressed and purified from stably transfected 293T cells. Balb C mice are initially immunized intraperitoneally with 25 pg of the Tag5-98P4B6 variant I protein mixed in complete 20 Freund's adjuvant. Mice are subsequently immunized every two weeks with 25 jg of the antigen mixed in incomplete Freund's adjuvant for a total of three immunizations. ELISA using the Tag5 antigen determines the titer of serum from immunized mice. Reactivity and specificity of serum to full length 98P4B6 variant 1 protein is monitored by Western blotting, immunoprecipitation and flow cytometry using 293T cells 25 transfected with an expression vector encoding the 98P4B6 variant 1 cDNA (see e.g., the Example entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems"). Other recombinant 98P4B6 variant 1-expressing cells or cells endogenously expressing 98P4B6 variant 1 are also used. Mice showing the strongest reactivity are rested and given a final injection of Tag5 antigen in PBS and then sacrificed four days later. The 30 spleens of the sacrificed mice are harvested and fused to SPO/2 myeloma cells using standard procedures (Harlow and Lane, 1988). Supernatants from HAT selected growth wells are screened by ELISA, Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometry to identify 98P4B6 specific antibody-producing clones. 35 To generate monoclonal antibodies that are specific for each 98P4B6 variant protein, immunogens are designed to encode sequences unique for each variant. In one 1 00R embodiment, a Tag5 antigen encoding the full sequence of 98P4B6 variant 2 (AA 1-45) is produced, purified and used as immunogen to derive monoclonal antibodies specific to 98P4B6 variant 2. In another embodiment, an antigenic peptide composed of amino acids 400-410 of 98P4B6 variant 5 is coupled to KLH and used as immunogen. In 5 another embodiment, a GST fusion protein encoding amino acids 455-490 of 98P4B6 of variant 6 is used as immunogen to derive variant 6 specific monoclonal antibodies. In another embodiment, a peptide composed of amino acids 472-498 of variant 7 is coupled to KLH and used as immunogen to generate variant 7 specific monoclonal antibodies. Hybridoma supernatants are then screened on the respective antigen and 10 then further screened on cells expressing the specific variant and cross-screened on cells expressing the other variants to derive variant-specific monoclonal antibodies. The binding affinity of a 98P4B6 variant monoclonal antibody is determined using standard technologies. Affinity measurements quantify the strength of antibody to epitope binding and are used to help define which 98P4B6 variant monoclonal 15 antibodies preferred for diagnostic or therapeutic use, as appreciated by one of skill in the art. The BlAcore system (Uppsala, Sweden) is a preferred method for determining binding affinity. The BlAcore system uses surface plasmon resonance (SPR, Welford K. 1991, Opt. Quant. Elect. 23:1; Morton and Myszka, 1998, Methods in Enzymology 295:268) to monitor biomolecular interactions in real time. BlAcore analysis 20 conveniently generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. Example 12: HLA Class I and Class II Binding Assays HLA class I and class II binding assays using purified HLA molecules are 25 performed in accordance with disclosed protocols (e.g., PCT publications WO 94/20127 and WO 94/03205; Sidney et al., Current Protocols in Immunology. 18.3.1 (1998); Sidney, et al., J. Immunol. 154:247 (1995); Sette, et al., Mol. Immunol 31:813 (1994)). Briefly, purified MHC molecules (5 to 500 nM) are incubated with various unlabeled peptide inhibitors and 1-10 nM 1 2 5 1-radiolabeled probe peptides 30 1 00C as described. Following incubation, MHC-peptide complexes are separated from free peptide by gel filtration and the fraction of peptide bound is determined. Typically, in preliminary experiments, each MHC preparation is titered in the presence of fixed amounts of radiolabeled peptides to determine the concentration of HLA molecules necessary to bind 10-20% of the total radioactivity. All subsequent inhibition and direct binding assays are performed using these HLA concentrations. Since under these conditions [labell<[HLAI and ICso>[HLA], the measured lCso values are reasonable approximations of the true Ko values. Peptide inhibitors are typically tested at concentrations ranging from 120 pg/ml to 1.2 ng/ml, and are tested in two to four completely independent experiments. To allow comparison of the data obtained in different experiments, a relative binding figure is calculated for each peptide by dividing the ICso of a positive control for inhibition by the ICso for each tested peptide (typically unlabeled versions of the radiolabeled probe peptide). For database purposes, and inter-experiment comparisons, relative binding values are compiled. These values can subsequently be converted back into ICso nM values by dividing the ICso nM of the positive controls for inhibition by the relative binding of the peptide of interest. This method of data compilation is accurate and consistent for comparing peptides that have been tested on different days, or with different lots of purified MHC. Binding assays as outlined above may be used to analyze HLA supermotif and/or HLA motif-bearing peptides (see Table IV). Example 13: Identification of HLA Supermotif- and Motif-Bearing CTL Candidate Epitopes HLA vaccine compositions of the invention can include multiple epitopes. The multiple epitopes can comprise multiple HLA supermotifs or motifs to achieve broad population coverage. This example illustrates the identification and confirmation of supermotif- and motif-bearing epitopes for the inclusion in such a vaccine composition. Calculation of population coverage is performed using the strategy described below. Computer searches and algorithms for identification of supermotif and/or motif-bearing epitopes The searches performed to identify the motif-bearing peptide sequences in the Example entitled 'Antigenicity Profiles" and Tables Vill-XXI and XXII-XLIX employ the protein sequence data from the gene product of 98P4B6 set forth in Figures 2 and 3, the specific search peptides used to generate the tables are listed in Table VII. Computer searches for epitopes bearing HLA Class I or Class I supermotifs or motifs are performed as follows. All translated 98P4B6 protein sequences are analyzed using a text string search software program to identify potential peptide sequences containing appropriate HLA binding motifs; such programs are readily produced in accordance with information in the art in view of known motif/supermotif disclosures. Furthermore, such calculations can be made mentally. Identified A2-, A3-, and DR-supermotif sequences are scored using polynomial algorithms to predict their capacity to bind to specific HLA-Class I or Class 11 molecules. These polynomial algorithms account for the impact of different amino acids at different positions, and are essentially based on the premise that the overall affinity (or AG) of peptide-HLA molecule interactions can be approximated as a linear polynomial'function of the type: 'AG" = a1; x a2i x a3i...... x an; where aW is a coefficient which represents the effect of the presence of a given amino acid () at a given position (i) along the sequence of a peptide of n amino acids. The crucial assumption of this method is that the effects at each position are essentially independent of each other (i.e., independent binding of individual side-chains). When residue j occurs at position i in the peptide, it is assumed to contribute a constant amount ji to the free energy of binding of the peptide irrespective of the sequence of the rest of the peptide. The method of derivation of specific algorithm coefficients has been described in Gulukota et al., J. MoL Biol. 267:1258-126, 1997; (see also Sidney et at., Human Immunol. 45:79-93, 1996; and Southwood ef al., J. Immuno. 160:3363 3373, 1998). Briefly, for all i positions, anchor and non-anchor alike, the geometric mean of the average relative binding 101 (ARB) of all peptides carrying j is calculated relative to the remainder of the group, and used as the estimate of j. For Class il peptides, if multiple alignments are possible, only the highest scoring alignment is utilized, following an iterative procedure. To calculate an algorithm score of a given peptide in a test set, the ARB values corresponding to the sequence of the peptide are multiplied. If this product exceeds a chosen threshold, the peptide is predicted to bind. Appropriate thresholds are chosen as a function of the degree of stringency of prediction desired. Selection of HLA-A2 supertype cross-reactive peptides Protein sequences from 98P4B6 are scanned utilizing motif identification software, to identify 8-, 9- 10- and 1 1-mer sequences containing the HLA-A2-supermotif main anchor specificity. Typically, these sequences are then scored using the protocol described above and the peptides corresponding to the positive-scoring sequences are synthesized and tested for their capacity to'bind purified HLA-A*0201 molecules in vitro (HLA-A*0201 is considered a prototype A2 supertype molecule). These peptides are then tested for the capacity to bind to additional A2-supertype molecules (A*0202, A*0203, A*0206, and A'6802). Peptides that bind to at least three of the live A2-supertype alleles tested are typically deemed A2 supertype cross-reactive binders. Preferred peptides bind at an affinity equal to or less than 500 nM to thre- or more HLA A2 supertype molecules. Selection of HLA-A3 supermotif-bearing epitopes The 98P4B6 protein sequence(s) scanned above is also examined for the presence of peptides with the HLA-A3 supermotif primary anchors. Peptides corresponding to the HLA A3 supermotif-bearing sequences are then synthesized and tested for binding to HLA-A*0301 and HLA-A*1101 molecules, the molecules encoded by the two most prevalent A3 supertype alleles. The peptides that bind at least one of the two alleles with binding affinities of 500 nM, often 200 nM, are then tested for binding cross-reactivity to the other common A3-supertype alleles (e.g., A*3101, A*3301, and A*6801) to identify those that can bind at least three of the live HLA-A3-supertype molecules tested. Selection of HLA-87 supermotif bearing epitopes The 98P4B6 protein(s) scanned above is also analyzed for the presence of 8-, 9- 10-, or 11 -mer peptides with the HLA-87-supermotif. Corresponding peptides are synthesized and tested for binding to HLA-B*0702, the molecule encoded by the most common B7-supertype allele (i.e., the prototype B7 supertype allele). Peptides binding B*0702 with ICso of 5500 nM are identified using standard methods. These peptides are then tested for binding to other common B7-supertype molecules (e.g., B*3501, B*5101, B*5301, and B*5401). Peptides capable of binding to three or more of the five B7 supertype alleles tested are thereby identified. Selection of Al and A24 motif-bearing epitopes To further increase population coverage, HLA-A1 and -A24 epitopes can also be incorporated into vaccine compositions. An analysis of the 98P4B6 protein can also be performed to identify HLA-Al- and A24-motif-containing sequences. High affinity and/or cross-reactive binding epitopes that bear other motif and/or supermotifs are identified using analogous methodology. Example 14: Confirmation of Immunogenicity Cross-reactive candidate CTL A2-supermotif-bearing peptides that are identified as described herein are selected to confirm in vitro immunogenicity. Confirmation is performed using the following methodology' 1 fl Target Cell Lines for Cellular Screening: The .221A2.1 cell line, produced by transferring the HLA-A2.1 gene into the HLA-A, -B, -C null mutant human B lymphoblastoid cell line 721.221, is used as the peptide-loaded target to measure activity of HLA-A2.1-restricted CTL. This cell fine is grown in RPMI-1640 medium supplemented with antibiotics, sodium pyruvate, nonessential amino acids and 10% (v/v) heat inactivated FCS. Cells that express an antigen of interest, or transfectants comprising the gene encoding the antigen of interest, can be used as target cells to confirm the ability of peptide-specific CTLs to recognize endogenous antigen. Primary CTL Induction Cultures: Generation of Dendritic Cells (DC): PBMCs are thawed in RPMI with 30 pg/ml DNAse, washed twice and resuspended in complete medium (RPMI-1640 plus 5% AB human serum, non-essential amino acids, sodium pyruvate, L glutamine and penicillin/streptomycin). The monocytes are purified by plating 10 x 106 PBMC/weII in a 6-well plate. After 2 hours at 37*C, the non-adherent cells are removed by gently shaking the plates and aspirating the supernatants. The wells are washed a total of three times with 3 ml RPMI to remove most of the non-adherent and loosely adherent cells. Three ml of -complete medium containing 50 ng!ml of GM-CSF and 1,000 Ulml of IL-4 are then added to each well. TNFa is added to the DCs on day 6 at 75 ng/ml and the cells are used for CTL induction cultures on day 7. Induction of CTL with DC and Peptide: CD8+ T-cells are isolated by positive selection with Dynal immunomagnetic beads (Dynabeads@ M-4S0) and the detacha-bead@ reagent. Typically about 200-250x106 PBMC are processed to obtain 24x10 6 CD8* T-ces (enough for a 48-well plate culture). Briefly, the PBMCs are thawed in RPMI with 30pg/ml DNAse, washed once with PBS containing 1% human AB serum and resuspended in PBS/1% AB serum at a concentration of 2Ox10 6 cells/ml. The magnetic beads are washed 3 times with PBS/AB serum, added to the cells (140pi beads/20x1O6 cells) and incubated for 1 hour at 4 0 C with continuous mixing. The beads and cells are washed 4x with PBSIAB serum to remove the nonadherent cells and resuspended at 100x106 cells/mi (based on the original cell number) in PBS/AB serum containing 1OOpI/mi detacha-bead@ reagent and 30 pg/mI DNAse. The mixture is incubated for I hour at room temperature with continuous mixing. The beads are washed again with PBS/AB/DNAse to collect the CD8+ T-cells. The DC are collected and centrifuged at 1300 rpm for 5-7 minutes, washed once with PBS with 1% BSA, counted and pulsed with 40pg/ml of peptide at a cell concentration of 1-2x1 06/ml in the presence of 3pg/ml S2- microglobulin for 4 hours at 20*C. The DC are then irradiated (4,200 rads), washed 1 time with medium and counted again. Setting up induction cultures: 0.25 ml cytokine-generated DC (at 1x10 5 cells/ml) are co-cultured with 0.25ml of CD8+ T-cells (at 2x10 6 cell/m) in each well of a 48-well plate in the presence of 10 ng/ml of IL-7. Recombinant human IL-10 is added the next day at a final concentration of 10 ng/ml and rhuman IL-2 is added 48 hours later at 10 IU/mI. Restimulation of the induction cultures with peptide-pulsed adherent cells: Seven and fourteen days after the primary induction, the cells are restimulated with peptide-pulsed adherent cells. The PBMCs are thawed and washed twice with RPMI and DNAse. The cells are resuspended at 5x1 06 cells/ml and irradiated at -4200 rads. The PBMCs are plated at 2x10 6 in 0.5 ml complete medium per well and incubated for 2 hours at 37 0 C. The plates are washed twice with RPMI by tapping the plate gently to remove the nonadherent cells and the adherent cells pulsed with 10pg/ml of peptide in the presence of 3 pg/ml B2 microglobulin in 0.25ml RPMI/5%AB per well for 2 hours at 37 0 C. Peptide solution from each well is aspirated and the wells are washed once with RPMI. Most of the media is aspirated from the induction cultures (CD8+ cells) and brought to 0.5 ml with fresh media. The cells are then transferred to the wells containing the peptide-pulsed adherent cells. Twenty four hours later recombinant human IL-10 is added at a final concentration of 10 ng/ml and recombinant human IL2 is added the next day and again 2-3 days later at 501U/ml (Tsai et al., Crtical Reviews in immunology 18(1-2):65-75, 1998). Seven days later, the cultures are assayed for CTL activity in a 5 'Cr release assay. In some experiments the cultures are assayed for peptide-specific recognition in the in situ IFNy ELISA at the time of the second 103 restimulation followed by assay of endogenous recognition 7 days later. After expansion, activity is measured in both assays for a side-by-side comparison. Measurement of CTL lytic activity by 5 1 Cr release. Seven days after the second restimulation, cytotoxicity is determined in a standard (5 hr) 51Cr release assay by assaying individual wells at a single E:T. Peptide-pulsed targets are prepared by incubating the cells with 1OpgIml peptide overnight at 37 0 C. Adherent target cells are removed from culture flasks with trypsin-EDTA. Target cells are labeled with 200pCi of 51 Cr sodium chromate (Dupont Wilmington, DE) for 1 hour at 37 0 C. Labeled target cells are resuspended at 106 per mi and diluted 1:10 with K562 cells at a concentration of 3.3x10 6 /ml (an NK-sensitive erythroblastoma cell fine used to reduce non specific lysis). Target cells (100 pl) and effectors (100pl) are plated in 96 well round-bottom plates and incubated for 5 hours at 37 0 C. At that time, 100 pl of supernatant are collected from each well and percent lysis is determined according to the formula: [(cpm of the test sample- cpm of the spontaneous 5'Cr release sample)/(cpm of the maximal 5 1 Cr release sample cpm of the spontaneous 5t Cr release sample)] x 100. Maximum and spontaneous release are determined by incubating the labeled targets with 1% Triton X-100 and media alone, respectively. A positive culture is defined as one in which the specific lysis (sample- background) is 10% or higher in the case of individual wells and is 15% or more at the two highest E:T ratios when expanded cultures are assayed. In situ Measurement of Human IFNy Production as an Indicator of Peptide-specific and Endogenous Recognition Immulon 2 plates are coated with mouse anti-human IFNy monoclonal antibody (4 pg/ml 0.1M NaHCO3, pH8.2) overnight at 4*C. The plates are washed with Ca 2 , Mg 2 +-free PBSIO.05% Tween 20 and blocked with PBS/10% FCS for two hours, after which the CTLs (100 pilwell) and targets (100 pl/well) are added to each well, leaving empty wells for the standards and blanks (which received media only). The target cells, either peptide-pulsed or endogenous targets, are used at a concentration of 1x10 6 cellsiml. The plates are incubated for 48 hours at 37*C with 5% C02. Recombinant human IFN-gamma is added to the standard wells starting at 400 pg or 1200pg/100 microliter/well and the plate incubated for two hours at 37'C. The plates are washed and 100 pl of biotinylated mouse anti-human IFN gamma monoclonal antibody (2 microgram/mI in PBS/3%FCS/0.05% Tween 20) are added and incubated for 2 hours at room temperature. After washing again, 100 microliter HRP-streptavidin (1:4000) are added and the plates incubated for one hour at room temperature. The plates are then washed 6x with wash buffer, 100 microliter/well developing solution (TMB 1:1) are added, and the plates allowed to develop for 5-15 minutes. The reaction is stopped with 50 microliter/well 1 M H3P04 and read at OD450. A culture is considered positive if it measured at least 50 pg of IFN-gammalwell above background and is twice the background level of expression. CTL Expansion. Those cultures that demonstrate specific lytic activity against peptide-pulsed targets and/or tumor targets are expanded over a two week period with anti-CD3. Briefly, 5x104 C08+ cells are added to a T25 flask containing the following: 1x106 irradiated (4,200 rad) PBMC (autologous or allogeneic) per ml, 2x10 5 irradiated (8,000 rad) EBV- transformed cells per mi, and OKT3 (anti-CD3) at 30ng per ml in RPMI-1640 containing 10% (v/v) human AB serum, non-essential amino acids, sodium pyruvate, 25pM 2-mercaptoethanol, L-glutamine and penicigin/streptomycin. Recombinant human IL2 is added 24 hours later at a final concentration of 2001U/mi and every three days thereafter with fresh media at 501U/ml. The cells are split if the cel concentration exceeds 1x106/ml and the cultures are assayed between days 13 and 15 at E:T ratios of 30, 10, 3 and 1:1 in the 51 Cr release assay or at 1x106/m in the in situ IFNy assay using the same targets as before the expansion. Cultures are expanded in the absence of anti-CD3+ as follows. Those cultures that demonstrate specific lytic activity against peptide and endogenous targets are selected and 5x10 4 CD8+ cells are added to a T25 flask containing the 1 fl4 following: 1x10 6 autologous PBMC per ml which have been peptide-pulsed with 10 pg/mI peptide for two hours at 37'C and irradiated (4,200 rad); 2x10 5 irradiated (8,000 rad) EBV-transformed cells per ml RPMI-1640 containing 10%(v/v) human AB serum, non-essential AA, sodium pyruvate, 25mM 2-ME, L-glutamine and gentamicin. Immunogenicity of A2 supermotif-bearing peptides A2-supermotif cross-reactive binding peptides are tested in the cellular assay for the ability to induce peptide specific CTL in normal individuals. In this analysis, a peptide is typically considered to be an epitope if it induces peptide specific CTIs in at least individuals, and preferably, also recognizes the endogenously expressed peptide. Immunogenicity can also be confirmed using PBMCs isolated from patients bearing a tumor that expresses 98P4B6. Briefly, PBMCs are isolated from patients, re-stimulated with peptide-pulsed monocytes and assayed for the ability to recognize peptide-pulsed target cells as well as transfected cells endogenously expressing the antigen. Evaluation of A'03/A1 1 immunogenicity HLA-A3 supermotif-bearing cross-reactive binding peptides are also evaluated for immunogenicity using methodology analogous for that used to evaluate the immunogenicity of the HLA-A2 supermotif peptides. Evaluation of B7 immunogenicit . Immunogenicity screening of the 87-supertype cross-reactive binding peptides identified as set forth herein are confirmed in a manner analogous to the confirmation of A2-and A3-supermotif-bearing peptides. Peptides bearing other supermotifs/motifs, e.g., HLA-Al, HLA-A24 etc. are also confirmed using similar methodology Example 15: Implementation of the Extended Supermotif to Improve the Binding Capacity of Native Epitopes by Creating Analogs HLA motifs and supermotifs (comprising primary and/or secondary residues) are useful in the identification and preparation of highly cross-reactive native peptides, as demonstrated herein. Moreover, the definition of HLA motifs and supermotifs also allows one to engineer highly cross-reactive epitopes by identifying residues within a native peptide sequence which can be analoged to confer upon the peptide certain characteristics, e.g. greater cross-reactivity within the group of HLA molecules that comprise a supertype, and/or greater binding affinity for some or all of those HLA molecules. Examples of analoging peptides to exhibit modulated binding affinity are set forth in this example. Analoging at Primary Anchor Residues Peptide engineering strategies are implemented to further increase the cross-reactivity of the epitopes. For example, the main anchors of A2-supermotif-bearing peptides are altered, for example, to introduce a preferred L, I, V, or M at position 2, and I or V at the C-terminus. To analyze the cross-reactivity of the analog peptides, each engineered analog is initially tested for binding to the prototype A2 supertype allele A*0201, then, if A'0201 binding capacity is maintained, for A2-supertype cross-reactivity. Alternatively, a peptide is confirmed as binding one or all supertype members and then analoged to modulate binding affinity to any one (or more) of the supertype members to add population coverage. The selection of analogs for immunogenicity in a cellular screening analysis is typically further restricted by the capacity of the parent wild type (WT) peptide to bind at least weakly, i.e., bind at an ICso of 5000nM or less, to three of more A2 supertype alleles. The rationale for this requirement is that the WT peptides must be present endogenously in sufficient quantity to be biologically relevant. Analoged peptides have been shown to have increased immunogenicity and cross reactivity by T cells specific for the parent epitope (see, e.g., Parkhurst el at., J. Immunol. 157:2539,1996; and Pogue et al., Proc. Nati. Acad. Sci. USA 92:8166, 1995). 105 In the cellular screening of these peptide analogs, it is important to confirm that analog-specific CTLs are also able to recognize the wild-type peptide and, when possible, target cells that endogenously express the epitope. Analoging of HLA-A3 and B7-supermotif-bearing eptides Analogs of HLA-A3 supermotif-bearing epitopes are generated using strategies similar to those employed in analoging HLA-A2 supermotif-bearing peptides. For example, peptides binding to 3/5 of the A3-supertype molecules are engineered at primary anchor residues to possess a preferred residue (V, S, M, or A) at position 2. The analog peptides are then tested for the ability to bind A*03 and A*1 1 (prototype A3 supertype alleles). Those peptides that demonstrate 500 nM binding capacity are then confirmed as having A3-supertype cross-reactivity. Similarly to the A2- and A3- motif bearing peptides, peptides binding 3 or more B7-supertype alleles can be improved, where possible, to achieve increased cross-reactive binding or greater binding affinity or binding half life. B7 supermotif-bearing peptides are, for example, engineered to possess a preferred residue (V, I, L, or F) at the C-teminal primary anchor position, as demonstrated by Sidney;et al. (J. Immunol. 157:3480-3490, 1996). Analoging at primary anchor residues of other motif and/or supermotif-bearing epitopes is performed in a like manner. The analog peptides are then be confirmed for immunogenicity, typically in a cellular screening assay. Again, it is generally important to demonstrate that analog-specific CTLs are also able to recognize the wild-type peptide and, when possible, targets that endogenously express the epitope. Analoging at Secondary Anchor Residues Moreover, HLA supermotifs are of value in engineering highly cross-reactive peptides and/or peptides that bind HLA molecules with increased affinity by identifying particular residues at secondary anchor positions that are associated with such properties. For example, the binding capacity of a 87 supermotif-bearing peptide with an F residue at position 1 is analyzed. The peptide is then analoged to, for example, substitute L for F at position 1. The analoged peptide is evaluated for increased binding affinity, binding half life and/or increased cross-reactivity. Such a procedure identifies analoged peptides with enhanced properties. Engineered analogs with sufficiently improved binding capacity or cross-reactivity can also be tested for immunogenicity in HLA-87-transgenic mice, following for example, IFA immunization or lipopeptide immunization. Analoged peptides are additionally tested for the ability to stimulate a recall response using PBMC from patients with 98P486 expressing tumors. Other analoging strategies Another form of peptide analoging, unrelated to anchor positions, involves the substitution of a cysteine with a amino butyric acid. Due to its chemical nature, cysteine has the propensity to form disulfide bridges and sufficiently alter the peptide structurally so as to reduce binding capacity. Substitution of a-amino butyric acid for cysteine not only alleviates this problem, but has been shown to improve binding and crossbinding capabilities in some instances (see, e.g., the review by Sette ef al., In: Persistent Viral Infections, Eds. R. Ahmed and I. Chen, John Wiley & Sons, England, 1999). Thus, by the use of single amino acid substitutions, the binding properties and/or cross-reactivity of peptide ligands for HLA supertype molecules can be modulated. Example 16: Identification and confirmation of 98P486-derived sequences with HLA-DR binding motifs Peptide epitopes bearing an HLA class Il supermotif or motif are identified and confirmed as outlined below using methodology similar to that described for HLA Class I peptides. 106 Selection of HLA-DR-supermotif-bearing epitopes. To identify 98P4B6-derved, HLA class 11 HTL epitopes, a 98P4B6 antigen is analyzed for the presence of sequences bearing an HLA-DR-motif or supermotif. Specifically, 15-mer sequences are selected comprising a DR supermotif, comprising a 9-mer core, and three-residue N- and C-terminal flanking regions (15 amino acids total). Protocols for predicting peptide binding to DR molecules have been developed (Southwood ef al., J. Immune. 160:3363-3373, 1998). These protocols, specific for individual DR molecules, allow the scoring, and ranking, of 9-mer core regions. Each protocol not only scores peptide sequences for the presence of DR-supermotif primary anchors (i.e., at position 1 and position 6) within a 9-mer core, but additionally evaluates sequences for the presence of secondary anchors. Using allele-specific selection tables (see, e.g., Southwood et al., ibid.), it has been found that these protocols efficiency select peptide sequences with a high probability of binding a particular DR molecule. Additionally, it has been found that performing these protocols in tandem, specifically those for DRI, DR4w4, and DR7, can efficiently select DR cross-reactive peptides. The 98P4B6-derived peptides identified above are tested for their binding capacity for various common HLA-DR molecules. All peptides are initially tested for binding to the DR molecules in the primary panel: DR1, DR4w4, and DR7. Peptides binding at least two of these three DR molecules are then tested for binding to DR2w2 p 1, DR2w2 p2, DR6w19, and DR9 molecules in secondary assays. Finally, peptides binding at least two of the four secondary panel DR molecules, and thus cumulatively at least four of seven different DR molecules, are screened for binding to DR4w1 5, DR5w1 1, and DR8w2 molecules in tertiary assays. Peptides binding at least seven of the ten DR molecules comprising the primary, secondary, and tertiary screening assays are considered cross-reactive DR binders. 98P4B6-derived peptides found to bind common HLA-DR alleles are of particular interest. Selection of DR3 motif peptides Because HLA-DR3 is an allele that is prevalent in Caucasian, Black, and Hispanic populations, DR3 binding capacity is a relevant criterion in the selection of HTL epitopes. Thus, peptides shown to be candidates may also be assayed for their DR3 binding capacity. However, in view of the binding specificity of the DR3 motif, peptides binding only to DR3 can also be considered as candidates for inclusion in a vaccine formulation. To efficiently identify peptides that bind DR3, target 98P4B6 antigens are analyzed for sequences carrying one of the two DR3-specific binding motifs reported by Geluk et al. (J. Immunol. 152:5742-5748, 1994). The corresponding peptides are then synthesized and confirmed as having the ability to bind DR3 with an affinity of 1pM or better, i.e., less than 1 pM. Peptides are found that meet this binding criterion and qualify as HLA class 11 high affinity binders. DR3 binding epitopes identified in this manner are included in vaccine compositions with DR supermotif-bearing peptide epitopes. Similarly to the case of HLA class I motif-bearing peptides, the class il motif-bearing peptides are analoged to improve affinity or cross-reactivity. For example, aspartic acid at position 4 of the 9-mer core sequence is an optimal residue for DR3 binding, and substitution for that residue often improves DR 3 binding. Example 17: Immunogenicity of 98P4B6-derived HTL epitopes This example determines immunogenic DR supermotif- and DR3 motif-bearing epitopes among those identified using the methodology set forth herein. Immunogenicity of HTL epitopes are confirmed in a manner analogous to the determination of immunogenicity of CTL epitopes, by assessing the ability to stimulate HTL responses and/or by using appropriate transgenic mouse models. Immunogenicity is determined by screening for 1.) in vitro primary induction using normal PBMC or 2.) recall responses from patients who have 98P4B6-expressing tumors. 107 Example 18: Calculation of phenotypic frequencies of HLA-supertypes in various ethnic back-grounds to determine breadth of population coverage This example illustrates the assessment of the breadth of population coverage of a vaccine composition comprised of multiple epitopes comprising multiple supermotifs and/or motifs. In order to analyze population coverage, gene frequencies of HLA alleles are determined. Gene frequencies for each HLA allele are calculated from antigen or allele frequencies utilizing the binomial distribution formulae gf=1-(SQRT(1 af)) (see, e.g., Sidney et al., Human Immunol. 45:79-93, 1996). To obtain overall phenotypic frequencies, cumulative gene frequencies are calculated, and the cumulative antigen frequencies derived by the use of the inverseformula [af=1-(1-Cgf). Where frequency data is not available at the level of DNA typing, correspondence to the serologically defined antigen frequencies is assumed. To obtain total potential supertype population coverage no linkage disequilibrium is assumed, and only alleles confirmed to belong to each of the supertypes are included (minimal estimates). Estimates of total potential coverage achieved by inter-loci combinations are made by adding to the A coverage the proportion of the non-A covered population that could be expected to be covered by the B alleles considered (e.g., total=A+B*(l-A)). Confirmed members of the A3-like supertype are A3, Al1, A31, A*3301, and A*6801. Although the A3-like supertype may also include A34, A66, and A*7401, these alleles were not included in overall frequency calculations. Likewise, confirmed members of the A2-fike supertype family are A*0201, A*0202, A*0203, A*0204, A*0205, A*0206, A*0207, A*6802, and A*6901. Finally, the B7-like supertype-confirmed alleles are: 87, B*3501-03, 851, 8*5301, 85401, B*5501-2, B*5601, 8*6701, and 8*7801 (potentially also B*1401, B*3504-06, B*4201, and B*5602). Population coverage achieved by combining the A2-, A3- and B7-supertypes is approximately 86% in live major ethnic groups. Coverage may be extended by including peptides bearing the Al and A24 motifs. On average, Al is present in 12% and A24 in 29% of the population across five different major ethnic groups (Caucasian, North American Black, Chinese, Japanese, and Hispanic). Together, these alleles are represented with an average frequency of 39% in these same ethnic populations. The total coverage across the major ethnicities when Al and A24 are combined with the coverage of the A2-, A3- and B7-supertype alleles is >95%, see, e.g., Table IV (G). An analogous approach can be used to estimate population coverage achieved with combinations of class Il motif-bearing epitopes. Immunogenicity studies in humans (e.g., Bertoni et al., J. Clin. Invest. 100:503, 1997; Doolan el al., Immunity 7:97, 1997; and Threlkeld et al., J. Immunol. 159:1648, 1997) have shown that highly cross-eactive binding peptides are almost always recognized as epitopes. The use of highly cross-reactive binding peptides is an important selection criterion in identifying candidate epitopes for inclusion in a vaccine that is immunogenic in a diverse population. With a sufficient number of epitopes (as disclosed herein and from the art), an average population coverage is predicted to be greater than 95% in each of five major ethnic populations. The game theory Monte Carlo simulation analysis, which is known in the art (see e.g., Osborne, M.J. and Rubinstein, A. 'A course in game theory" MIT Press, 1994), can be used to estimate what percentage of the individuals in a population comprised of the Caucasian, North American Black, Japanese, Chinese, and Hispanic ethnic groups would recognize the vaccine epitopes described herein. A preferred percentage is 90%. A more preferred percentage is 95%. Example 19: CTL Recognition Of Endogenously Processed Antigens After Priming This example confirms that CTL induced by native or analoged peptide epitopes identified and selected as described herein recognize endogenously synthesized, i.e., native antigens. Effector cells isolated from transgenic mice that are immunized with peptide epitopes, for example HLA-A2 supermotif-bearing epitopes, are re-stimulated in vitro using peptide-coated stimulator cells. Six days later, effector cells are 1 R assayed for cytotoxicity and the cell lines that contain peptide-specific cytotoxic activity are further re-stimulated. An additional six days later, these cel lines are tested for cytotoxic activity on 51 Cr labeled Jurkat-A2.1/Kb target cels in the absence or presence of peptide, and also tested on 51 Cr labeled target cells bearing the endogenously synthesized antigen, i.e. cells that are stably transfected with 98P4B6 expression vectors. The results demonstrate that CTL lines obtained from animals primed with peptide epitope recognize endogenously synthesized 98P486 antigen. The choice of transgenic mouse model to be used for such an analysis depends upon the epitope(s) that are being evaluated. In addition to HLA-A*0201/Kb transgenic mice, several other transgenic mouse models including mice with human Al1, which may also be used to evaluate A3 epitopes, and 87 alleles have been characterized and others (e.g., transgenic mice for HLA-Al and A24) are being developed. HLA-DR1 and HLA DR3 mouse models have also been developed, which may be used to evaluate HTL epitopes. Example 20: Activity Of CTL-HTL Conjugated Epitopes In Transgenic Mice This example illustrates the induction of CTLs and HTLs in transgenic mice, by use of a 98P486-derived CTL and HTL peptide vaccine compositions. The vaccine composition used herein comprise peptides to be administered to a patient with a 98P4B6-expressing tumor. The peptide composition can comprise multiple CTL and/or HTL epitopes. The epitopes are identified using methodology as described herein. This example also illustrates that enhanced immunogenicity can be achieved by inclusion of one or more HTL epitopes in a CTL vaccine composition; such a peptide composition can comprise an HTL epitope conjugated to a CTL epitope. The CTL epitope can be one that binds to multiple HLA family members at an affinity of 500 nM or less, or analogs of that epitope. The peptides may be lipidated, if desired. Immunization procedures: Immunization of transgenic mice is performed as described (Alexander et al., J. Immunol. 159:4753-4761, 1997). For example, A2/Kb mice, which are transgenic for the human HLA A2.1 allele and are used to confirm the immunogenicity of HLA-A*0201 motif- or HLA-A2 supermotif-bearing epitopes, and are primed subcutaneously (base of the tail) with a 0.1 ml of peptide in Incomplete Freund's Adjuvant, or if the peptide composition is a lipidated CTUHTL conjugate, in DMSO/saline, or if the peptide composition is a polypeptide, in PBS or Incomplete Freund's Adjuvant. Seven days after priming, splenocytes obtained from these animals are restimulated with syngenic irradiated LPS activated lymphoblasts coated with peptide. Cell lines: Target cells for peptide-specific cytotoxicity assays are Jurkat cells transfected with the HLA-A2.1I/Kb chimeric gene (e.g., Vitiello et al., J. Exp. Med. 173:1007, 1991) In vitro CTL activation: One week after priming, spleen cels (30x1 06 cells/flask) are co-cultured at 370C with syngeneic, irradiated (3000 rads), peptide coated lymphoblasts (10x10 6 cells/flask) in 10 ml of culture medium/T25 flask. After six days, effector cells are harvested and assayed for cytotoxic activity. Assay for cytotoxic activity: Target cells (1.0 to 1.5x106) are incubated at 37*C in the presence of 200 pl of 51 Cr. After 60 minutes, cells are washed three times and resuspended in R10 medium. Peptide is added where required at a concentration of I pg/ml. For the assay, 104 5 1 Cr-labeled target cells are added to different concentrations of effector cells (final volume of 200 pl) in U-bottom 96-well plates. After a six hour incubation period at 37*C, a 0.1 ml aliquot of supernatant is removed from each well and radioactivity is determined in a Micromedic automatic gamma counter. The percent specific lysis is determined by the formula: percent specific release = 100 x (experimental release - spontaneous release)/(maximum release - spontaneous release). To facilitate comparison between separate CTL assays run under the same conditions, % 5 1 Cr release data is expressed as lytic units/10 6 cells. One lytic unit is arbitrarily defined as the number of effector cells required to achieve 30% lysis of 10,000 target ceNs in a six hour 5 1Cr release assay. To obtain specific lytic units/106, the lytic units/1 06 obtained in the absence of peptide is subtracted from the lytic units/106 obtained in the presence of peptide. For example, if 30% 51 Cr release is obtained at the effector (E): target (T) ratio of 50:1 (i.e., 5x10 5 effector cells for 10,000 109 targets) in the absence of peptide and 5:1 (i.e., 5x10 4 effector celts for 10,000 targets) in the presence of peptide, the specific lytic units would be: [(1/50,000H1/500,000)] x 106 = 18 LU. The results are analyzed to assess the magnitude of the CTL responses of animals injected with the immunogenic CTUHTL conjugate vaccine preparation and are compared to the magnitude of the CTL response achieved using, for example, CTL epitopes as outlined above in the Example entitled "Confirmation of Immunogenicity. Analyses similar to this may be performed to confirm the immunogenicity of peptide conjugates containing multiple CTL epitopes and/or multiple HTL epitopes. In accordance with these procedures, it is found that a CTL response is induced, and concomitantly that an HTL response is induced upon administration of such compositions. Example 21: Selection of CTL and HTL epitopes for inclusion in a 98P4B6-specific vaccine. This example ilustrates a procedure for selecting peptide epitopes for vaccine compositions of the invention. The peptides in the.composition can be in the form of a nucleic acid sequence, either single or one or more sequences (i.e., minigene) that encodes peptide(s), or can be single and/or polyepitopic peptides. The following principles are utilized when selecting a plurality of epitopes for inclusion in a vaccine composition. Each of the following principles is balanced in order to make the selection. Epitopes are selected which, upon administration, mimic immune responses that are correlated with 98P4B6 clearance. The number of epitopes used depends on observations of patients who spontaneously clear 98P4B6. For example, if it has been observed that patients who spontaneously clear 98P4B6-expressing cells generate an immune response to at least three (3) epitopes from 98P486 antigen, then at least three epitopes should be included for HLA class 1. A similar rationale is used to determine HLA class 11 epitopes. Epitopes are often selected that have a binding affinity of an ICso of 500 nM or less for an HLA class I molecule, or for class lI, an ICso of 1000 nM or less; or HLA Class I peptides with high binding scores from the BIMAS web site, at URL bimas.dcrt.nih.gov/. In order to achieve broad coverage of the vaccine through out a diverse population, sufficient supermotif bearing peptides, or a sufficient array of allele-specific motif bearing peptides, are selected to give broad population coverage. In one embodiment, epitopes are selected to provide at least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known in the art, can be employed to assess breadth, or redundancy, of population coverage. When creating polyepitopic compositions, or a minigene that encodes same, it is typically desirable to generate the smallest peptide possible that encompasses the epitopes of interest. The principles employed are similar, if not the same, as those employed when selecting a peptide comprising nested epitopes. For example, a protein sequence for the vaccine composition is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. Epitopes may be nested or overlapping (i.e., frame shifted relative to one another). For example, with ovedapping epitopes, two 9-mer epitopes and one 10-mer epitope can be present in a 10 amino acid peptide. Each epitope can be exposed and bound by an HLA molecule upon administration of such a peptide. A multi-epitopic, peptide can be generated synthetically, recombinantly, or via cleavage from the native source. Altematively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reactivity and/or binding affinity properties of the polyepitopic peptide. Such a vaccine composition is administered for therapeutic or prophylactic purposes. This embodiment provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune response-inducing vaccine compositions. Additionally such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup that is presently unknown. Furthermore, this embodiment (absent the creating of any analogs) directs the immune response to multiple peptide sequences that are actually present in 98P486, thus avoiding the 110 need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing nucleic acid vaccine compositions. Related to this embodiment, computer programs can be derived in accordance with principles in the art, which identify in a target sequence, the greatest number of epitopes per sequence length. A vaccine composition comprised of selected peptides, when administered, is safe, efficacious, and elicits an immune response similar in magnitude to an immune response that controls or dears cells that bear or overexpress 98P4B6. Example 22: Construction of "Minigene" Multi-Epitope DNA Plasmids This example discusses the construction of a minigene expression plasmid. Minigene plasmids may, of course, contain various configurations of B cell, CTL and/or HTL epitopes or epitope analogs as described herein. A minigene expression plasmid typically includes multiple CTL and HTL peptide epitopes. In the present example, HLA-A2, -A3, -87 supemotif-bearing peptide epitopes and HLA-A1 and -A24 motif-bearing peptide epitopes are used in conjunction with DR supermotif-bearing epitopes and/or DR3 epitopes. HLA class I supermotif or motif-bearing peptide epitopes derived 98P486, are selected such that multiple supermotifs/motifs are represented to ensure broad population coverage. Similarly, HLA class I epitopes are selected from 98P4B6 to provide broad population coverage, i.e. both HLA DR-1 -4-7 supermotif-bearing epitopes and HLA DR-3 motif-bearing epitopes are selected for inclusion in the minigene construct. The selected CTL-and HTL epitopes are then incorporated into a minigene for expression in an expression vector. Such a construct may additionally include sequences that direct the HTL epitopes to the endoplasmic reticulum. For example, the Ii protein may be fused to one or more HTL epitopes as described in the art, wherein the CLIP sequence of the Ii protein is removed and replaced with an HLA dass Il epitope sequence so that HLA dass I epitope is directed to the endoplasmic reticulum, where the epitope binds to an HLA class Il molecules. This example illustrates the methods to be used for construction of a minigene-bearing expression plasmid. Other expression vectors that may be used for minigene compositions are available and known to those of skill in the art. The minigene DNA plasmid of this example contains a consensus Kozak sequence and a consensus murine kappa Ig-light chain signal sequence followed by CTL and/or HTL epitopes selected in accordance with principles disclosed herein. The sequence encodes an open reading frame fused to the Myc and His antibody epitope tag coded for by the pcDNA 3.1 Myc-His vector. Overlapping oligonucleotides that can, for example, average about 70 nucleotides in length with 15 nudeotide ovedaps, are synthesized and HPLC-purified. The oligonudeotides encode the selected peptide epitopes as well as appropriate linker nucleotides, Kozak sequence, and signal sequence. The final multiepitope minigene is assembled by extending the overlapping oligonucleotides in three sets of reactions using PCR. A Perkin/FJmer 9600 PCR machine is used and a total of 30 cycles are performed using the following conditions: 95*C for 15 sec, annealing temperature (5* below the lowest calculated Tm of each primer pair) for 30 sec, and 72*C for 1 min. For example, a minigene is prepared as follows: For a first PCR reaction, 5 pg of each of two oligonucleotides are annealed and extended: In an example using eight oligonudeotides, i.e., four pairs of primers, oligonudeotides 1+2, 3+4, 5+6, and 7+8 are combined in 100 pl reactions containing Pfu polymerase buffer (1x= 10 mM KCL, 10 mM (NH4)2SO4, 20 mM Tris-chloride, pH 8.75, 2 mM MgSO4, 0.1% Triton X-100, 100 pg/mI BSA), 0.25 mM each dNTP, and 2.5 U of Pfu polymerase. The full-length dimer products are gel-purified, and two reactions containing the product of 1+2 and 3+4, and the product of 5+6 and 7+8 are mixed, annealed, and extended for 10 cycles. Half of the two reactions are then mixed, and 5 cycles of annealing and extension carried out before flanking primers are added to amplify the full length product. The full length product is gel-purified and cloned into pCR-blunt (Invitrogen) and individual clones are screened by sequencing. Example 23: The Plasmid Construct and the Degree to Which It Induces Immunogenicity. 111 The degree to which a plasmid construct, for example a plasmid constructed in accordance with the previous Example, is able to induce immunogenicity is confirmed in vitro by determining epitope presentation by APC following transduction or transfection of the APC with an epitope-expressing nucleic acid construct. Such a study determines "antigenicity" and allows the use of human APC. The assay determines the ability of the epitope to be presented by the APC in a context that is recognized by a T cell by quantifying the density of epitope-HLA class I complexes on the cell surface. Quantitation can be performed by directly measuring the amount of peptide eluted from the APC (see, e.g., Sijts et a., J. Immunol. 156:683-692, 1996; Demotz et al., Nature 342:682-684, 1989); or the number of peptide-HLA class I complexes can be estimated by measuring the amount of lysis or lymphokine release induced by diseased or transfected target cells, and then determining the concentration of peptide necessary to obtain equivalent levels of lysis or lymphokine release (see, e.g., Kageyama et a!., J. Immunol. 154:567-576, 1995). Alternatively, immunogenicity is confirmed through in vivo injections into mice and subsequent in vitro assessment of CTL and HTL activity, which are analyzed using cytotoxicity and proliferation assays, respectively, as detailed e.g., in Alexander et al., Immunity 1:751-761, 1994. For example, to confirm the capacity of a DNA minigene construct containing at least one HLA-A2 supermotif peptide to induce CTLs in vivo, HLA-A2.1/Kb transgenic mice, for example, are immunized intramuscularly with 100 pg of naked cDNA. As a means of comparing the level of CTLs induced by cDNA immunization, a control group of animals is also immunized with an actual peptide composition that comprises multiple epitopes synthesized as a single polypeptide as they would be encoded by the minigene. Splenocytes from immunized animals are stimulated twice with each of the respective compositions (peptide epitopes encoded in the minigene or the polyepitopic peptide), then assayed for peptide-specific cytotoxic activity in a 5'Cr release assay. The results indicate the magnitude of the CTL response directed against the A2-restricted epitope, thus indicating the in vivo immunogenicity of the minigene vaccine and polyepitopic vaccine. It is, therefore, found that the minigene elicits immune responses directed toward the HLA-A2 supermotif peptide epitopes as does the polyepitopic peptide vaccine. A similar analysis is also performed using other HLA-A3 and HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 and HLA-B7 motif or supermotif epitopes, whereby it is also found that the minigene elicits appropriate immune responses directed toward the provided epitopes. To confirm the capacity of a class 11 epitope-encoding minigene to induce HTLs in vivo, DR transgenic mice, or for those epitopes that cross react with the appropriate mouse MHC molecule, I-Ab-restricted mice, for example, are immunized intramuscularly with 100 gg of plasmid DNA As a means of comparing the level of HTLs induced by DNA immunization, a group of control animals is also immunized with an actual peptide composition emulsified in complete Freund's adjuvant. CD4+ T cefls, i.e. HTLs, are purified from splenocytes of immunized animals and stimulated with each of the respective compositions (peptides encoded in the minigene). The HTL response is measured using a 3 H-thymidine incorporation proliferation assay, (see, e.g., Alexander et a. Immunity 1:751-761, 1994). The results indicate the magnitude of the HTL response, thus demonstrating the in vivo immunogenicity of the minigene. DNA minigenes, constructed as described in the previous Example, can also be confirmed as a vaccine in combination with a boosting agent using a prime boost protocol. The boosting agent can consist of recombinant protein (e.g., Bamett et al., Aids Res. and Human Retroviruses 14, Supplement 3:S299-S309, 1998) or recombinant vaccinia, for example, expressing a minigene or DNA encoding the complete protein of interest (see, e.g., Hanke et al., Vaccine 16:439 445, 1998; Sedegah et a., Proc. Nall. Acad. Sci USA 95:7648-53, 1998; Hanke and McMichael, Immunol. Letters 66:177 181, 1999; and Robinson et al., Nature Med. 5:526-34, 1999). For example, the efficacy of the DNA minigene used in a prime boost protocol is initially evaluated in transgenic mice. In this example, A2.1/Kb transgenic mice are immunized IM with 100 pg of a DNA minigene encoding the 117 immunogenic peptides including at least one HLA-A2 supermotif-bearing peptide. After an incubation period (ranging from 3 9 weeks), the mice are boosted IP with 107 pfulmouse of a recombinant vaccinia virus expressing the same sequence encoded by the DNA minigene. Control mice are immunized with 100 pg of DNA or recombinant vaccinia without the minigene sequence, or with DNA encoding the minigene, but without the vaccinia boost. After an additional incubation period of two weeks, splenocytes from the mice are immediately assayed for peptide-specific activity in an ELISPOT assay. Additionally, splenocytes are stimulated in vitro with the A2-restricted peptide epitopes encoded in the minigene and recombinant vaccinia, then assayed for peptide-specific activity in an alpha, beta and/or gamma IFN ELISA. It is found that the minigene utilized in a prime-boost protocol elicits greater immune responses toward the HLA-A2 supermotif peptides than with DNA alone. Such an analysis can also be performed using HLA-A1 1 or HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 or HLA-B7 motif or supermotif epitopes. The use of prime boost protocols in humans is described below in the Example entitled'Induction of CTL Responses Using a Prime Boost Protocol." Example 24: Peptide Compositions for Prophylactic Uses Vaccine compositions of the present invention can be used to prevent 98P4B6 expression in persons who are at risk for tumors that bear this antigen. For example, a polyepitopic peptide epitope composition (or a nucleic acid comprising the same) containing multiple CTL and HTL epitopes such as those selected in the above Examples, which are also selected to target greater than 80% of the population, is administered to individuals at risk for a 98P4B6-associated tumor. For example, a peptide-based composition is provided as a single polypeptide that encompasses multiple epitopes. The vaccine is typically administered in a physiological solution that comprises an adjuvant, such as Incomplete Freunds Adjuvant. The dose of peptide for the initial immunization is from about 1 to about 50,000 pg, generally 100-5,000 pg, for a 70 kg patient. The initial administration of vaccine is followed by booster dosages at 4 weeks followed by evaluation of the magnitude of the immune response in the patient, by techniques that determine the presence of epitope-specific CTL populations in a PBMC sample. Additional booster doses are administered as required. The composition is found to be both safe and efficacious as a prophylaxis against 98P4B6-associated disease. Alternatively, a composition typically comprising transfecting agents is used for the administration of a nucleic acid based vaccine in accordance with methodologies known in the art and disclosed herein. Example 25: Polyepitopic Vaccine Compositions Derived from Native 98P486 Sequences A native 98P4B6 polyprotein sequence is analyzed, preferably using computer algorithms defined for each class I and/or class I supermotif or motif, to identify 'relatively short" regions of the polyprotein that comprise multiple epitopes. The "relatively short" regions are preferably less in length than an entire native antigen. This relatively short sequence that contains multiple distinct or overlapping, 'nested' epitopes can be used to generate a minigene construct. The construct is engineered to express the peptide, which corresponds to the native protein sequence. The 'relatively short" peptide is generally less than 250 amino acids in length, often less than 100 amino acids in length, preferably less than 75 amino acids in length, and more preferably less than 50 amino acids in length. The protein sequence of the vaccine composition is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. As noted herein, epitope motifs may be nested or overlapping (i.e., frame shifted relative to one another). For example, with overlapping epitopes, two 9-mer epitopes and one 10-mer epitope can be present in a 10 amino acid peptide. Such a vaccine composition is administered for therapeutic or prophylactic purposes. The vaccine composition will include, for example, multiple CTL epitopes from 98P4B6 antigen and at least one HTL epitope. This polyepitopic native sequence is administered either as a peptide or as a nucleic acid sequence which 113 encodes the peptide. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reactivity and/or binding affinity properties of the polyepitopic peptide. The embodiment of this example provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune response-inducing vaccine compositions. Additionally, such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup(s) that is presently unknown. Furthermore, this embodiment (excluding an analoged embodiment) directs the immune response to multiple peptide sequences that are actually present in native 98P4B6, thus avoiding the need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing peptide or nucleic acid vaccine compositions. Related to this embodiment, computer programs are available in the art which can be used to identify in a target sequence, the greatest number of epitopes per sequence length. Example 26: Polvepitopic Vaccine Compositions from Multiple Antigens The 98P486 peptide epitopes of the present invention are used in conjunction with epitopes from other target tumor-associated antigens, to create a vaccine composition that is useful for the prevention or treatment of cancer that expresses 98P4B6 and such other antigens. For example, a vaccine composition can be provided as a single polypeptide that incorporates multiple epitopes from 98P4B6 as well as tumor-associated antigens that are often expressed with a target cancer associated with 98P4B6 expression, or can be administered as a composition comprising a cocktail of one or more discrete epitopes. Alternatively, the vaccine can be administered as a minigene construct or as dendritic cells which have been loaded with the peptide epitopes in vitro. Example 27: Use of peptides to evaluate an immune response Peptides of the invention may be used to analyze an immune response for the presence of specific antibodies, CTL or HTL directed to 98P4B6. Such an analysis can be performed in a manner described by Ogg e1 at., Science 279:2103-2106, 1998. In this Example, peptides in accordance with the invention are used as a reagent for diagnostic or prognostic purposes, not as an immunogen. In this example highly sensitive human leukocyte antigen tetrameric complexes ("tetramers") are used for a cross sectional analysis of, for example, 98P4B6 HLA-A*0201-specific CTL frequencies from HLA A*0201-positive individuals at different stages of disease or following immunization comprising a 98P4B6 peptide containing an A*0201 motif. Tetrameric complexes are synthesized as described (Musey ef at., N. Engl. J. Med. 337:1267,1997). Briefly, purified HLA heavy chain (A*0201 in this example) and p2-microglobulin are synthesized by means of a prokaryotic expression system. The heavy chain is modified by deletion of the transmembrane-cytosolic tail and COOH-terminal addition of a sequence containing a BirA enzymatic biotinylation site. The heavy chain, p2-microglobulin, and peptide are refolded by dilution. The 45-kD refolded product is isolated by fast protein liquid chromatography and then biotinylated by BirA in the presence of biotin (Sigma, St Louis, Missouri), adenosine 5' triphosphate and magnesium. Streptavidin-phycoerythrin conjugate is added in a 1:4 molar ratio, and the tetrameric product is concentrated to 1 mg/ml. The resulting product is referred to as letramer phycoerythrin. For the analysis of patient blood samples, approximately one million PBMCs are centrifuged at 300g for 5 minutes and resuspended in 50 pl of cold phosphate-buffered saline. Tri-color analysis is performed with the tetramer-phycoerythrin, along with anti-CD8-Tricolor, and anti-CD38. The PBMCs are incubated with tetramer and antibodies on ice for 30 to 60 min and then washed twice before formaldehyde fixation. Gates are applied to contain >99.98% of control samples. Controls for the tetramers include both A*0201-negative individuals and A*0201-positive non-diseased donors. The percentage of cells stained with the tetramer is then determined by flow cytometry. The results indicate the number of cells in the PBMC sample that contain epitope-restricted CTLs, thereby readily indicating the extent of immune response to the 98P486 epitope, and thus the status of exposure to 98P486, or exposure to a vaccine that elicits a protective or therapeutic response. -Example 28: Use of Peptide Epitopes to Evaluate Recall Responses The peptide epitopes of the invention are used as reagents to evaluate T cell responses, such as acute or recall responses, in patients. Such an analysis may be performed on patients who have recovered from 98P4B6-associated disease or who have been vaccinated with a 98P4B6 vaccine. For example, the class I restricted CTL response of persons who have been vaccinated may be analyzed. The vaccine may be any 98P4B6 vaccine. PBMC are collected from vaccinated individuals and HLA typed. Appropriate peptide epitopes of the invention that, optimally, bear supermotifs to provide cross-reactivity with multiple HLA supertype family members, are then used for analysis of samples derived from individuals who bear that HLA type. PBMC from vaccinated individuals are separated on Ficoll-Histopaque density gradients (Sigma Chemical Co., St. Louis, MO), washed three times in HBSS (GIBCO Laboratories), resuspended in RPMI-1640 (GIBCO Laboratories) supplemented with L-glutamine (2mM), penicillin (50U/ml), streptomycin (50 pg/m), and Hepes (10mM) containing 10% heat-inactivated human AB serum (complete RPMI) and plated using microculture formats. A synthetic peptide comprising an epitope of the invention is added at 10 pg/mI to each well and HBV core 128-140 epitope is added at 1 pg/mI to each well as a source of T cell help during the first week of stimulation. In the microculture format, 4 x 105 PBMC are stimulated with peptide in 8 replicate cultures in 96-well round bottom plate in 100 p1/well of complete RPMI. On days 3 and 10, 100 pi of complete RPMI and 20 U/ml final concentration of rlL-2 are added to each well. On day 7 the cultures are transferred into a 96-well flat-bottom plate and restimulated with peptide, rlL-2 and 105 irradiated (3,000 rad) autologous feeder cells. The cultures are tested for cytotoxic activity on day 14. A positive CTL response requires two or more of the eight replicate cultures to display greater than 10% specific 5 'Cr release, based on comparison with non-diseased control subjects as previously described (Rehermann, et a., Nature Med. 2:1104,1108,1996; Rehermann eta., J. Clin. Invest. 97:1655-1665, 1996; and Rehermann et al. J. Clin. Invest. 98:1432 1440,1996). Target cell lines are autologous and allogeneic EBV-transformed B-LCL that are either purchased from the American Society for Histocompatibility and Immunogenetics (ASHI, Boston, MA) or established from the pool of patients as described (Guilhot, et al. J. Virol. 66:2670-2678, 1992). Cytotoxicity assays are performed in the following manner. Target cells consist of either allogeneic HLA-matched or autologous EBV-transformed B lymphoblastoid cell line that are incubated overnight with the synthetic peptide epitope of the invention at 10 pM, and labeled with 100 pCi of 5 'Cr (Amersham Corp., Arington Heights, IL) for 1 hour after which they are washed four times with HBSS. Cytolytic activity is determined in a standard 4-h, split well 5 'Cr release assay using U-bottomed 96 well plates containing 3,000 targets/well. Stimulated PBMC are tested at effector/target (EIT) ratios of 20-50:1 on day 14. Percent cytotoxicity is determined from the formula: 100 x [(experimental release-spontaneous release)/maximum release spontaneous release)]. Maximum release is determined by lysis of targets by detergent (2% Triton X-100; Sigma Chemical Co., St Louis, MO). Spontaneous release is <25% of maximum release for a experiments. The results of such an analysis indicate the extent to which HLA-restricted CTL populations have been stimulated by previous exposure to 98P486 or a 98P486 vaccine. 115 Similarly, Class Il restricted HTL responses may also be analyzed. Purified PBMC are cultured in a 96-well flat bottom plate at a density of 1.5x10 5 cellstwell and are stimulated with 10 pg/ml synthetic peptide of the invention, whole 98P4B6 antigen, or PHA Cells are routinely plated in replicates of 4-6 wells for each condition. After seven days of culture, the medium is removed and replaced with fresh medium containing 1OU/mI IL-2. Two days later, 1 pCi 3 H-thymidine is added to each well and incubation is continued for an additional 18 hours. Cellular DNA is then harvested on glass fiber mats and analyzed for 3 H-thymidine incorporation. Antigen-specific T cell proliferation is calculated as the ratio of 3

H

thymidine incorporation in the presence of antigen divided by the 3 H-thymidine incorporation in the absence of antigen. Example 29: Induction Of Specific CTL Response In Humans A human clinical trial for an immunogenic composition comprising CTL and HTL epitopes of the invention is set up as an IND Phase I, dose escalation study and carried out as a randomized, double-blind, placebo-controlled trial- Such a trial is designe(l, for example, as follows: A total of about 27 individuals are enrolled and divided into 3 groups: Group 1 1 subjects are injected with placebo and 6 subjects are injected with 5 pg of peptide composition; Group II: 3 subjects are injected with placebo and 6 subjects are injected with 50 pg peptide composition; Group Il: 3 subjects are injected with placebo and 6 subjects are injected with 500 pg of peptide composition. After 4 weeks following the first injection, all subjects receive a booster inoculation at the same dosage. The endpoints measured in this study relate to the safety and tolerability of the peptide composition as well as its immunogenicity. Cellular immune responses to the peptide composition are an index of the intrinsic activity of this the peptide composition, and can therefore be viewed as a measure of biological efficacy. The following summarize the clinical and laboratory data that relate to safety and efficacy endpoints. Safety: The incidence of adverse events is monitored in the placebo and drug treatment group and assessed in terms of degree and reversibility. Evaluation of Vaccine Efficacy: For evaluation of vaccine efficacy, subjects are bled before and after injection. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient centrifugation, aliquoted in freezing media and stored frozen. Samples are assayed for CTL and HTL activity. The vaccine is found to be both safe and efficacious. Example 30: Phase I Trials In Patients Expressinq 98P4B6 Phase |1 trials are performed to study the effect of administering the CTL-HTL peptide compositions to patients having cancer that expresses 98P486. The main objectives of the trial are to determine an effective dose and regimen for inducing CTLs in cancer patients that express 98P486, to establish the safety of inducing a CTL and HTL response in these patients, and to see to what extent activation of CTLs improves the clinical picture of these patients, as manifested, e.g., by the reduction and/or shrinking of lesions. Such a study is designed, for example, as follows: The studies are performed in multiple centers. The trial design is an open-label, uncontrolled, dose escalation protocol wherein the peptide composition is administered as a single dose followed six weeks later by a single booster shot of the same dose. The dosages are 50, 500 and 5,000 micrograms per injection. Drug-associated adverse effects (severity and reversibility) are recorded. There are three patient groupings. The first group is injected with 50 micrograms of the peptide composition and the second and third groups with 500 and 5,000 micrograms of peptide composition, respectively. The patients within each group range in age from 21-65 and represent diverse ethnic backgrounds. AH of them have a tumor that expresses 98P4B6. 116 Clinical manifestations or antigen-specific T-cell responses are monitored to assess the effects of administering the peptide compositions. The vaccine composition is found to be both safe and efficacious in the treatment of 98P4B6 associated disease. Example 31: Induction of CTL Responses Usinq a Prime Boost Protocol A prime boost protocol similar in its underlying principle to that used to confirm the efficacy of a DNA vaccine in transgenic mice, such as described above in the Example entitled 'The Plasmid Construct and the Degree to Which It Induces Immunogenicity," can also be used for the administration of the vaccine to humans. Such a vaccine regimen can include an initial administration of, for example, naked DNA followed by a boost using recombinant virus encoding the vaccine, or recombinant protein/polypeptide or a peptide mixture administered in an adjuvant For example, the initial immunization may be performed using an expression vector, such as that constructed in the Example entitled "Construction of "Minigene" Multi-Epitope DNA Plasmids" in the form of naked nucleic acid administered IM (or SC or ID) in the amounts of 0.5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 pg) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose is then administered. The booster can be recombinant fowtpox virus administered at a dose of 5-107 to 5x10 9 pfu. An alternative recombinant virus, such as an MVA, canarypox, adenovirus, or adeno-associated virus, can also be used for the booster, or the polyepitopic protein or a mixture of the peptides can be administered. For evaluation of vaccine efficacy, patient blood samples are obtained before immunization as well as at intervals following administration of the initial vaccine and booster doses of the vaccine. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient centrifugation, aliquoted in freezing media-and stored frozen. Samples are assayed for CTL and HTL activity. Analysis of the results indicates that a magnitude of response sufficient to achieve a therapeutic or protective immunity against 98P4B6 is generated. Example 32: Administration of Vaccine Compositions Using Dendritic Cells (DC) Vaccines comprising peptide epitopes of the invention can be administered using APCs, or "professional' APCs such as DC. In this example, peptide-pulsed DC are administered to a patient to stimulate a CTL response in vivo. In this method, dendritic cells are isolated, expanded, and pulsed with a vaccine comprising peptide CTL and HTL epitopes of the invention. The dendritic cells are infused back into the patient to elicit CTL and HTL responses in vivo. The induced CTL and HTL then destroy or facilitate destruction, respectively, of the target cells that bear the 98P4B6 protein from which the epitopes in the vaccine are derived. For example, a cocktail of epitope-comprising peptides is administered ex vivo to PBMC, or isolated DC therefrom. A pharmaceutical to facilitate harvesting of DC can be used, such as Progenipoieinm (Monsanto, St. Louis, MO) or GM CSF/IL-4. After pulsing the DC with peptides, and prior to reinfusion into patients, the DC are washed to remove unbound peptides. As appreciated clinically, and readily determined by one of skill based on clinical outcomes, the number of DC reinfused into the patient can vary (see, e.g., Nature Med. 4:328,1998; Nature Med. 2:52,1996 and Prostate 32:272, 1997). Although 2-50 x 106 DC per patient are typically administered, larger number of DC, such as 107 or 108 can also be provided. Such cell populations typically contain between 50-90% DC. In some embodiments, peptide-loaded PBMC are.injected into patients without purification of the DC. For example, PBMC generated after treatment with an agent such as Progenipoietin m are injected into patients without 117 purification of the DC. The total number of PBMC that are administered often ranges from 108 to 10'0. Generally, the cell doses injected into patients is based on the percentage of DC in the blood of each patient, as determined, for example, by immunofluorescence analysis with specific anti-DC antibodies. Thus, for example, if ProgenipoetinTm mobilizes 2% DC in the peripheral blood of a given patient, and that patient is to receive 5 x 106 DC, then the patient will be injected with a total of 2.5 x 108 peptide-loaded PBMC. The percent DC mobilized by an agent such as ProgenipoietinT' is typically estimated to be between 2-10%, but can vary as appreciated by one of skill in the art. Ex vivo activation of CTUHTL responses Alternatively, ex vivo CTL or HTL responses to 98P4B6 antigens can be induced by incubating, in tissue culture, the patient's, or genetically compatible, CTL or HTL precursor cells together with a source of APC, such as DC, and immunogenic peptides. After an appropriate incubation time (typically about 7-28 days), in which the precursor cells are activated and expanded into effector cells, the cels are infused into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cells, i.e., tumor cells. Example 33: An Altemat' a Method of Identifying and Confirminq Motif-Bearing Peptides Another method of identifying and confirming motif-bearing peptides is to elute them from cells bearing defined MHC molecules. For example, EBV transformed B cell lines used for tissue typing have been extensively characterized to determine which HLA molecules they express. In certain cases these cells express only a single type of HLA molecule. These cells can be transfected with nudeic acids that express the antigen of interest, e.g. 98P4B6. Peptides produced by endogenous antigen processing of peptides produced as a result of transfection will then bind to HLA molecules within the cell and be transported and displayed on the cell's surface. Peptides are then eluted from the HLA molecules by exposure to mild acid conditions and their amino acid sequence determined, e.g., by mass spectral analysis (e.g., Kubo et at, J. Immunol. 152:3913, 1994). Because the majority of peptides that bind a particular HLA molecule are motif-bearing, this is an alternative modality for obtaining the motif-bearing peptides correlated with the particular HLA molecule expressed on the cell. Alternatively, cell lines that do not express endogenous HLA molecules can be transfected with an expression construct encoding a single HLA allele. These cells can then be used as described, i.e., they can then be transfected with nudeic acids that encode 98P4B6 to isolate peptides corresponding to 98P4B6 that have been presented on the cell surface. Peptides obtained from such an analysis will bear motif(s) that correspond to binding to the single HLA allele that is expressed in the cell. As appreciated by one in the art, one can perform a similar analysis on a cell bearing more than one HLA allele and subsequently determine peptides specific for each HLA allele expressed. Moreover, one of skill would also recognize that means other than transfection, such as loading with a protein antigen, can be used to provide a source of antigen to the cell. Example 34: Complementary Polynucleotides Sequences complementary to the 98P4B6-encoding sequences, or any parts thereof, are used to detect, decrease, or inhibit expression of naturally occurring 98P4B6. Although use of oligonucleotides comprising from about 15 to 30 base pairs is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonuceotides are designed using, e.g., OLIGO 4.06 software (National Biosciences) and the coding sequence of 98P4B6. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5' sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent nbosomal binding to a 98P4B6-encoding transcript. 110 Example 35: Purification of Naturally-occurring or Recombinant 98P4B6 Usinq 98P486-Specific Antibodies Naturally occurring or recombinant 98P4B6 is substantially purified by immunoaffinily chromatography using antibodies specific for 98P486. An immunoaffinity column is constructed by covalently coupling anti-98P4B6 antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer's instructions. Media containing 98P4B6 are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of 98P486 (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/98P486 binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate ion), and GCR.P is collected. Example 36: Identification of Molecules Which Interact with 98P4B6 98P4B6, or biologically active fragments thereof, are labeled with 121 1 Bolton-Hunter reagent. (See, e.g., Bolton et aL (1973) Biochem. J. 133:529.) Candidate molecules previously arrayed in the wells of a multi-well plate are incubated with the labeled 98P4B6, washed, and any wells with labeled 98P486 complex are assayed. Data obtained using different concentrations of 98P486 are used to calculate values for the number, affinity, and association of 98P4B6 with the candidate molecules. Example 37: In Vivo Assay for 98P4B6 Tumor Growth Promotion The effect of the 98P4B6 protein on tumor cell growth is evaluated in vivo by gene overexpression in tumor-bearing mice. For example, prostate (PC3), lung (A427), stomach, ovarian (PA1) and uterus cell lines are engineered to express 98P4B6. SCID mice are injected subcutaneously on each flank with 1 x 106 of PC3, A427, PA1, or NIH-3T3 cells containing tkNeo empty vector or 98P486. At least two strategies may be used: (1) Constitutive 98P4B6 expression under regulation of a promoter such as a constitutive promoter obtained from the genomes of viruses such as polyomavirus, fowlpox virus (UK 2,211,504 published 5 July 1989), adenovirus (such as Adenovirus 2), bovine papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis-B virus, and Simian Virus 40 (SV40), or from heterologous mammalian promoters, e.g., the actin promoter or an immunoglobulin promoter, provided such promoters are compatible with the host cell systems, and (2) Regulated expression under control of an inducible vector system, such as ecdysone, tet, etc., provided such promoters are compatible with the host cell systems. Tumor volume is then monitored at the appearance of palpable tumors and followed over time to determine if 98P4B6-expressing cells grow at a faster rate and whether tumors produced by 98P4B6-expressing cells demonstrate characteristics of altered aggressiveness (e.g. enhanced metastasis, vascularization, reduced responsiveness to chemotherapeutic drugs). Additionally, mice can be implanted with 1 x 105 of the same cells orthotopically to determine if 98P4B6 has an effect on local growth in the prostate or on the ability of the cells to metastasize, specifically to lungs, lymph nodes, and bone marrow. The assay is also useful to determine the 98P4B6 inhibitory effect of candidate therapeutic compositions, such as for example, 98P4B6 intrabodies, 98P4B6 antisense molecules and ribozymes. Example 38: 98P4B6 Monoclonal Antibody-mediated Inhibition of Tumors In Vivo. The significant expression of 98P4B6 in prostate, lung, stomach, ovary, and uterus cancer tissues, its restrictive expression in normal tissues, together with its expected cell surface expression makes 98P486 an excellent target for antibody therapy. Simflarly, 98P4B6 is a target for T-cell based immunotherapy. Thus, the therapeutic efficacy of anti 119 98P486 mAbs in human prostate cancer xenograft mouse models is evaluated by using androgen-independent LAPC-4 and LAPC-9 xenografts (Craft, N., et al., Cancer Res, 1999. 59(19): p. 5030-6) and the androgen independent recombinant cell line PC3-98P4B6 (see, e.g., Kaighn, M.E., et al., Invest Urol, 1979. 17(1): p. 16-23). Similar approaches using patient derived xenografts or xenograft cell lines are used for cancers listed in Table 1. Antibody efficacy on tumor growth and metastasis formation is studied, e.g., in a mouse orthotopic prostate cancer xenograft models and mouse lung, uterus, or stomach xenograft models. The antibodies can be unconjugated, as discussed in this Example, or can be conjugated to a therapeutic modality, as appreciated in the art. Anti-98P4B6 mAbs inhibit formation of both the androgen-dependent LAPC-9 and androgen-independent PC3-98P486 tumor xenografts. Anti-98P4B6 mAbs also retard the growth of established orthotopic tumors and prolonged survival of tumor-bearing mice. These results indicate the utility of anti-98P4B6 mAbs in the treatment of local and advanced stages of cancer. (See, e.g., (Saffran, D., et al., PNAS 10:1073-1078 or URL located on the World Wide Web at .pnas.org/cgidoi/10.1073/pnas.051624698). Administration of the anti-98P4B6 mAbs can lead to retardation of established odihotopic tumor growth and inhibition of metastasis to distant sites, resulting in a significant prolongation in the survival of tumor-bearing mice. These studies indicate that 98P4B6 is an attractive target for immunotherapy and demonstrate the therapeutic potential of anti 98P4B6 mAbs for the treatment of local and metastatic cancer. This example demonstrates that unconjugated 98P4B6 monoclonal antibodies are effective to inhibit the growth of human prostate tumor xenografts, as well as lung, uterus, or stomach xenograft grown in SCID mice; accordingly a combination of such efficacious monoclonal antibodies is also effective. Tumor inhibition using multiple unconjugated 98P4B6 mAbs Materials and Methods 98P4B6 Monoclonal Antibodies: Monoclonal antibodies are raised against 98P486 as described in Example 11 entitled 'Generation of 98P486 Monoclonal Antibodies (mAbs)." The antibodies are characterized by ELISA, Western blot, FACS, and immunoprecipitation for their capacity to bind 98P4B6. Epitope mapping data for the anti-98P486 mAbs, as determined by ELISA and Western analysis, recognize epitopes on the 98P486 protein. Immunohistochemical analysis of cancer tissues and cells with these antibodies is performed. The monoclonal antibodies are purified from ascites or hybridoma tissue culture supernatants by Protein-G Sephamose chromatography, dialyzed against PBS, filter sterilized, and stored at -20 0 C. Protein determinations are performed by a Bradford assay (Bio-Rad, Hercules, CA). A therapeutic monoclonal antibody or a cocktail comprising a mixture of individual monoclonal antibodies is prepared and used for the treatment of mice receiving subcutaneous or orthotopic injections of LAPC-9 tumor xenografts. Cancer Xenografts and Cell Lines The LAPC-9 xenograft, which expresses a wild-type androgen receptor and produces prostate-specific antigen (PSA), is passaged in 6- to 8-week-old male ICR-severe combined immunodeficient (SCID) mice (Taconic Farms) by s.c. trocar implant (Craft, N., et at., supra). The prostate (PC3), lung (A427), ovarian (PA1) carcinoma cell lines (American Type Culture Collection) are maintained in RPMI or DMEM supplemented with L-glutamine and 10% FBS. PC3-98P4B6, A427-98P4B6, PA1-98P486 and 3T3-98P4B6 cell populations are generated by retroviral gene transfer as described in Hubert, R.S., et al., STEAP: a prostate-specific cell-surface antigen highly expressed in human prostate tumors. Proc Natl Acad Sci U S A, 1999. 96(25): p. 14523-8. Anti-98P4B6 staining is detected by using an FITC conjugated goat anti-mouse antibody (Southern Biotechnology Associates) followed by analysis on a Coulter Epics-XL f low cytometer.

Xenograft Mouse Models. Subcutaneous (s.c.) tumors are generated by injection of 1 x 10 6 LAPC-9, PC3, PC3-98P4B6, A427, A427 98P4B6, PA1, PA1-98P4B6, 3T3 or 3T3-98P4B6 cells mixed at a 1:1 dilution with Matrigel (Collaborative Research) in the right flank of male SCID mice. To test antibody efficacy on tumor formation, i.p. antibody injections are started on the same day as tumor-cell injections. As a control, mice are injected with either purified mouse IgG (ICN) or PBS; or a purified monoclonal antibody that recognizes an irrelevant antigen not expressed in human cells. In preliminary studies, no difference is found between mouse igG or PBS on tumor growth. Tumor sizes are determined by vernier caliper measurements, and the tumor volume is calculated as length x width x height. Mice with s.c. tumors greater than 1.5 cm in diameter are sacrificed. PSA levels are determined by using a PSA ELISA kit (Anogen, Mississauga,-Ontario). Circulating levels of anti-98P4B6 mAbs are determined by a capture ELISA kit (Bethyl Laboratories, Montgomery, TX). (See, e.g., (Saffran, D., et al., PNAS 10:1073-1078 or URL located on the World Wide Web at .pnas.org/cgi/ doi/1O.1O73/pnas.051624698) Orthotopic injections are performed under anesthesia by using ketaminelxylazine. For prostate orthotopic studies, an incision is made through the abdominal muscles to expose the bladder and seminal vesicles, which then are delivered through the incision to expose the dorsal prostate. LAPC-9 or PC3 cells (5 x 105) mixed with Matrigel are injected into each dorsal lobe in a 10-pl volume. To monitor tumor growth, mice are bled on a weekly basis for determination of PSA levels. The mice are segregated into groups for the appropriate treatments, with anti-98P4B6 or control mAbs being injected i.p. Anti-98P4B6 mAbs Inhibit Growth of 98P4B6-Expressing Xeno-graft-Cancer Tumors The effect of anti-98P4B6 mAbs on tumor formation is tested by using LAPC-9 and PC3-98P4B6 orthotopic models. As compared with the s.c. tumor model, the orthotopic model, which requires injection of tumor cells directly in the mouse prostate, lung, or ovary, respectively, results in a local tumor growth, development of metastasis in distal sites, deterioration of mouse health, and subsequent death (Saffran, D., et al., PNAS supra; Fu, X, et al., Int J Cancer, 1992. 52(6): p. 987-90; Kubcta, T., J Cell Biochem, 1994. 56(1): p. 4-8). The features make the orthotopic model more representative of human disease progression and allowed us to follow the therapeutic effect of mAbs en clinically relevant end points. Accordingly, tumor cells are injected into the mouse prostate, lung, or ovary, and 2 days later, the mice are segregated into two groups and treated with either: a) 200 -500pg, of anti-98P4B6 Ab, or b) PBS three times per week for two to live weeks. A major advantage of the orthotopic cancer model is the ability to study the development of metastases. Formation of metastasis in mice bearing established orthotopic tumors is studies by IHC analysis on lung sections using an antibody against a prostate-specific cell-surface protein STEAP expressed at high levels in LAPC-9 xenografts (Hubert, R.S., et al., Proc Nail Acad Sci U S A, 1999. 96(25): p. 14523-8). Mice bearing established orthotopic LAPC-9 or PC3-98P4B6 tumors are administered 10OOpg injections of either anti-98P4B6 mAb or PBS over a 4-week period. Mice in both groups are allowed to establish a high tumor burden (PSA levels greater than 300 ng/mi for IAPC-9), to ensure a high frequency of metastasis formation in mouse lungs. Mice then are killed and their prostate and lungs are analyzed for the presence of tumor cells by IHC analysis. These studies demonstrate a broad anti-tumor efficacy of anti-98P4B6 antibodies on initiation and progression of prostate cancer in xenograft mouse models. Anti-98P4B6 antibodies inhibit tumor formation of both androgen-dependent and androgen-ndependent tumors as well as retarding the growth of already established tumors and prolong the survival of treated mice. Moreover, anti-98P4B6 mAbs demonstrate a dramatic inhibitory effect on the spread of local prostate tumor to distal sites, even in the presence of a large tumor burden. Thus, anti-98P4B6 mAbs are efficacious on major clinically relevant end points (tumor growth), prolongation of survival, and health. 121 Example 39: Therapeutic and Diagnostic use of Anti-98P4B6 Antibodies in Humans. Anti-98P486 monoclonal antibodies are safely and effectively used for diagnostic, prophylactic, prognostic and/or therapeutic purposes in humans. Western blot and immunohistochemical analysis of cancer tissues and cancer xenografts with anti-98P4B6 mAb show strong extensive staining in carcinoma but significantly lower or undetectable levels in normal tissues. Detection of 98P4B6 in carcinoma and in metastatic disease demonstrates the usefulness of the mAb as a diagnostic and/or prognostic indicator. Anti-98P486 antibodies are therefore used in diagnostic applications such as immunohistochemistry of kidney biopsy specimens to detect cancer from suspect patients. As determined by flow cytometry, anti-98P4B6 mAb specifically binds to carcinoma cells. Thus, anti-98P4B6 antibodies are used in diagnostic whole body imaging applications, such as radioimmunoscintigraphy and radioimmunotherapy, (see, e.g., Potamianos S., et. al. Anticancer Res 20(2A):925-948 (2000)) for the detection of localized and metastatic cancers that exhibit expression of 98P4B6. Shedding or release of an extraceular domain of 98P486 into the extracellular milieu, such as that seen for alkaline phosphodiesterase 810 (Meerson, N. R., Hepatology 27:563-568 (1998)), allows diagnostic detection of 98P4B6 by anti-98P4B6 antibodies in serum and/or urine samples from suspect patients. Anti-98P4B6 antibodies that specifically bind 98P4B6 are used in therapeutic applications for the treatment of cancers that express 98P4B6. Anti-98P4B6 antibodies are used as an unconjugated modality and as conjugated form in which the antibodies are attached to one of various therapeutic or imaging modalities well known in the art, such as a prodrugs, enzymes or radioisotopes. In preclinical studies, unconjugated and conjugated anti-98P4B6 antibodies are tested for efficacy of tumor prevention and growth inhibition in the SCID mouse cancer xenograft models, e.g., kidney cancer models AGS-K3 and AGS-K6, (see, e.g., the Example entitled "98P4B6 Monoclonal Antibody-mediated Inhibition of Bladder and Lung Tumors in Vivo"). Either conjugated and unconjugated anti-98P4B6 antibodies are used as a therapeutic modality in human clinical trials either alone or in combination with other treatments as described in following Examples. Example 40: Human Clinical Trials for the Treatment and Diagnosis of Human Carcinomas through use of Human Anti-98P4B6 Antibodies In vivo Antibodies are used in accordance with the present invention which recognize an epitope on 98P4B6, and are used in the treatment of certain tumors such as those listed in Table 1. Based upon a number of factors, including 98P4B6 expression levels, tumors such as those listed in Table I are presently preferred indications. In connection with each of these indications, three clinical approaches are successfully pursued. 1.) Adjunctive therapy- In adjunctive therapy, patients are treated with anti-98P486 antibodies in combination with a chemotherapeutic or antineoplastic agent and/or radiation therapy. Primary cancer targets, such as those listed in Table I, are treated under standard protocols by the addition anti-98P4B6 antibodies to standard first and second line therapy. Protocol designs address effectiveness as assessed by reduction in tumor mass as well as the ability to reduce usual doses of standard chemotherapy. These dosage reductions allow additional and/or prolonged therapy by reducing dose-related toxicity of the chemotherapeutic agent. Anti-98P486 antibodies are utilized in several adjunctive clinical trials in combination with the chemotherapeutic or antineoplastic agents adramycin (advanced prostrate carcinoma), cisplatin (advanced head and neck and lung carcinomas), taxol (breast cancer), and doxorubicin (precinical). II.) Monotherapy: In connection with the use of the anti-98P4B6 antibodies in monotherapy of tumors, the antibodies are administered to patients without a chemotherapeutic or antineoplastic agent. In one embodiment, monotherapy is conducted clinically in end stage cancer patients with extensive metastatic disease. Patients show some disease stabilization. Trials demonstrate an effect in refractory patients with cancerous tumors. 122 ll.) Imaging Agent Through binding a radionuclide (e.g., iodine or yttrium (1131, Y90) to anti-98P486 antibodies, the radiolabeled antibodies are utilized as a diagnostic and/or imaging agent. In such a role, the labeled antibodies localize to both solid tumors, as well as, metastatic lesions of cells expressing 98P4B6. In connection with the use of the anti-98P486 antibodies as imaging agents, the antibodies are used as an adjunct to surgical treatment of solid tumors, as both a pre-surgical screen as well as a post-operative follow-up to determine what tumor remains and/or returns. In one embodiment a (M in)-98P4B6 antibody is used as an imaging agent in a Phase I human clinical trial in patients having a carcinoma that expresses 98P4B6 (by analogy see, e.g., Divgi et a. J. Natl. Cancer Inst. 83:97-104 (1991)). Patients are followed with standard anterior and posterior gamma camera. The results indicate that primary lesions and metastatic lesions are identified Dose and Route of Administration As appreciated by those of ordinary skill in the art, dosing considerations can be determined through comparison with the analogous products that are in the clinic. Thus, anti-98P4B6 antibodies can be administered with doses in the range of 5 to 400 mg/m 2, with the lower doses used, e.g., in connection with safety studies. The affinity of anti-98P486 antibodies relative to the affinity of a known antibody for its target is one parameter used by those of skill in the art for determining analogous dose regimens. Further, anti-98P4B6 antibodies that are fully human antibodies, as compared to the chimeric antibody, have slower clearance; accordingly, dosing in patients with such fully human anti-98P4B6 antibodies can be lower, perhaps in the range of 50 to 300 mg/m 2 , and still remain efficacious. Dosing in mg/m 2 , as opposed to the conventional measurement of dose in mg/kg, is a measurement based on surface area and is a convenient dosing measurement that is designed to include patients of all sizes from infants to adults. Three distinct delivery approaches are useful for delivery of anti-98P4B6 antibodies. Conventional intravenous delivery is one standard delivery technique for many tumors. However, in connection with tumors in the peritoneal cavity, such as tumors of the ovaries, biliary duct, other ducts, and the like, intraperitoneal administration may prove favorable for obtaining high dose of antibody at the tumor and to also minimize antibody clearance. In a similar manner, certain solid tumors possess vasculature that is appropriate for regional perfusion. Regional perfusion allows for a high dose of antibody at the site of a tumor and minimizes short term clearance of the antibody. Clinical Development Plan (CDP) Overview: The CDP follows and develops treatments of anti-98P486 antibodies in connection with adjunctive therapy, monotherapy, and as an imaging agent. Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trails are open label comparing standard chemotherapy with standard therapy plus anti-98P486 antibodies. As will be appreciated, one criteria that can be utilized in connection with enrollment of patients is 98P4B6 expression levels in their tumors as determined by biopsy. As with any protein or antibody infusion-based therapeutic, safety concerns are related primarily to (i) cytokine release syndrome, i.e., hypotension, fever, shaking, chills; (ii) the development of an immunogenic response to the material (i.e., development of human antibodies by the patient to the antibody therapeutic, or HAHA response); and, (iii) toxicity to normal cells that express 98P486. Standard tests and follow-up are utilized to monitor each of these safety concerns. Anti 98P4B6 antibodies are found to be safe upon human administration. Example 41: Human Clinical Trial Adjunctive Therapy with Human Anti-98P4B6 Antibody and Chemotherapeutic Agent A phase I human clinical trial is initiated to assess the safety of six intravenous doses of a human anti-98P4B6 antibody in connection with the treatment of a solid tumor, e.g., a cancer of a tissue listed in Table 1. In the study, the safety 123 of single doses of anti-98P4B6 antibodies when utilized as an adjunctive therapy to an antineoplastic or chemotherapeutic agent as defined herein, such as, without limitation: cisplatin, topotecan, doxorubicin, adriamycin, taxol, or the like, is assessed. The trial design includes delivery of six single doses of an anti-98P4B6 antibody with dosage of 5 antibody escalating from approximately about 25 mg/m 2 to about 275 mg/m 2 over the course of the treatment in accordance with the following schedule: Day 0 Day 7 Day 14 Day 21 Day 28 Day 35 10 mAb Dose 25 75 125 175 225 275 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 Chemotherapy + + + + + + (standard dose) 15 Patients are closely followed for one-week following each administration of antibody and chemotherapy. In particular, patients are assessed for the safety concerns mentioned above: (i) cytokine release syndrome, i.e., hypotension, fever, shaking, chills; (ii) the development of an immunogenic response to the material (i.e., development of human antibodies by the patient to the human antibody therapeutic, or 20 HAHA response); and, (iii) toxicity to normal cells that express 98P4B6. Standard tests and follow-up are utilized to monitor each of these safety concerns. Patients are also assessed for clinical outcome, and particularly reduction in tumor mass as evidenced by MRI or other imaging. The anti-98P4B6 antibodies are demonstrated to be safe and efficacious, Phase 25 II trials confirm the efficacy and refine optimum dosing. Example 42: Human Clinical Trial: Monotherapy with Human Anti-98P4B6 Antibody Anti-98P4B6 antibodies are safe in connection with the above-discussed 30 adjunctive trial, a Phase II human clinical trial confirms the efficacy and optimum dosing for monotherapy. Such trial is accomplished, and entails the same safety and outcome analyses, to the above-described adjunctive trial with the exception being that patients do not receive chemotherapy concurrently with the receipt of doses of anti 98P4B6 antibodies. 35 124 Example 43: Human Clinical Trial: Diagnostic Imaging with Anti-98P4B6 Antibody Once again, as the adjunctive therapy discussed above is safe within the safety criteria discussed above, a human clinical trial is conducted concerning the use of anti 5 98P4B6 antibodies as a diagnostic imaging agent. The protocol is designed in a substantially similar manner to those described in the art, such as in Divgi et al. J. Natl. Cancer Inst 83:97-104 (1991). The antibodies are found to be both safe and efficacious when used as a diagnostic modality. 10 Example 44: Homology Comparison of 98P4B6 to Known Sequences The 98P4B6 gene is homologous to a cloned and sequenced gene, namely human STAMP1 (gi 15418732) (Korkmaz, KS et al, J. Biol. Chem. 2002, 277:36689), showing 99% identity and 99% homology to that gene (figure 4). The 98P4B6 protein also shows 99% identity and 99% homology to another human six transmembrane 15 epithelial antigen of prostate 2 (gi 23308593) (Walker, M.G et al. Genome Res. 1999, 9:1198; Porkka, K.P., Helenius, M.A. and Visakorpi, T, Lab. Invest. 2002, 82:1513). The closest mouse homolog to 98P4B6 is six transmembrane epithelial antigen of prostate 2 (gi 28501136), with 97% identity and 99% homology. We have identified several variants of the 98P4B6 protein, including 4 splice variants and 3 SNPs. The 20 98P4B6 v.1 protein consists of 454 amino acids, with calculated molecular weight of 52kDa, and pl of 8.7. It is a 6 transmembrane protein that can localize to the cell surface or possibly to the endoplasmic reticulum (Table VI). Several 98P4B6 variants, including v.1, v.5-8, v.13, v.14, v.21, v.25 share similar features, such protein motifs with functional significance, as well as structural commonalities such as multiple 25 transmembrane domains. The 98P4B6 v.2 is a short protein with no known motifs. Motif analysis revealed the presence of several known motifs, including oxido reductase, homocysteine hydrolase and dudulin motifs. Variant v.7 and SNPs of this variant also carry an Ets motif, often associated with transcriptional activity. Several oxidoreductases have been identified in mammalian cells, including the 30 NADH/quinone oxidoreductase. This protein associate with the cell membrane and function as a proton/Na+ pump, which regulates the protein degradation of the tumor suppressor p 53 , and protects mammalian cells from oxidative stress, cytotoxicity, and mutages (Asher G, et al, Proc Natl Acad Sci U.S.A. 2002, 99:13125; Jaiswal AK, Arch Biochem Biophys 2000, 375:62 Yano T, Mol Aspects Med 2002, 23:345). 35 Homocysteine hydrolase is an enzyme known to catalyze the breakdown of S adenosylhomocysteine to homocysteine and adenosine, ultimately regulating trans 125 methylation, thereby regulating protein expression, cell cycle and proliferation (Turner MA et al. Cell Biochem Biophys 2000; 33:101; Zhang et al, J Biol Chem. 2001; 276:35867 ) This information indicates that 98P4B6 plays a role in the cell growth of 5 mammalian cells, regulate gene transcription and transport of electrons and small molecules. Accordingly, when 98P4B6 functions as a regulator of cell growth, tumor formation, or as a modulator of transcription involved in activating genes associated with inflammation, tumorigenesis, or proliferation, 98P4B6 is used for therapeutic, diagnostic, prognostic and/or preventative purposes. In addition, when a molecule, 10 such as a variant or polymorphism of 98P486 is expressed in cancerous tissues, it is used for therapeutic, diagnostic, prognostic and/or preventative purposes. Example 45: Phenotypic Effects of STEAP-2 Expression Experiments regarding the expression of STEAP-2 protein having the amino 15 acid sequence shown in Figure 2 and encoded by a cDNA insert in a plasmid deposited with the American Type Culture Collection on 02-July-1999 and assigned as ATCC Accession No. PTA-3 11. As deduced from the coding sequence, the open reading frame encodes 454 amino acids with 6 transmembrane domains. The expression of STEAP-2 in normal tissues is predominantly restricted to the prostate. STEAP-2 is 20 expressed in several cancerous tissues. In patient-derived prostate, colon, and lung cancer specimens; and multiple cancer cell lines, including prostate, colon, Ewing's sarcoma, lung, kidney, pancreas and testis. By ISH, STEAP-2 expression appears to be primarily limited to ductal epithelial cells. The data set forth in the present patent application provide an expression profile 25 of the STEAP-2 protein that is predominantly specific for the prostate among normal tissues, for certain types of prostate tumors as well as other tumors. This evidence is based on detecting messenger RNA using Northern blotting. In keeping with standard practice in this industry, Northern blots are routinely used to assess gene expression, as it does not require the time consuming process of synthesizing the relevant protein, 30 raising antibodies, assuring the specificity of the antibodies, required for Western blotting of proteins and the histological examination of tissues. Northern blotting offers a credible and efficient method of assessing RNA expression and expression levels. This Example demonstrates that STEAP-2 protein is, indeed, produced. In 35 summary, the experiments show that PC-3 cells and 3T3 cells which were modified to contain an expression system for STEAP-2 showed enhanced levels of tyrosine 126 phosphorylation in general, and of phosphorylation of ERK protein in particular. The data also show that PC-3 cells that contain an expression system for STEAP-2 showed modified calcium flux, a modified response to paclitaxel, and a general inhibition of drug-induced apoptosis. These are effects exhibited at the protein level, thus these data 5 alone are probative that the STEAP-2 protein exists. Furthermore, although such phenotypic effects are protein-mediated, further evidence indicates that the STEAP-2 protein itself is the mediator of the effects. This evidence is obtained by utilizing a modified STEAP-2 protein. An expression system is stably introduced into PC3 and 3T3 cells which allows the expression of a modified 10 form of STEAP-2, designated STEAP-2CFI, where "Fl" stands for flag. STEAP-2CFI is a STEAP-2 protein having a peptide extension, i.e., a Flag epitope that alters the physical conformation of this protein. The Flag epitope is a string 8 amino acids, often introduced at either the amino or carboxy termini of protein as a means of identifying and following a recombinant protein in engineered cells (Slootstra JW et al, Mol Divers 15 1997, 2:156). In most cases, the introduction of the Flag epitope at either termini of a protein has little effect on the natural function and location of that protein (Molloy SS et al, EMBO J 1994, 13:18). However, this is dependent on the characteristics of the protein being Flag tagged. Recent studies have shown that a Flag tag affects the function and conformation of select proteins such as the CLN3 protein (see, e.g., 20 Haskell RE, et al. Mol Genet Metab 1999, 66:253). As with CLN3, introducing a Flag epitope tag to the C-terminus of STEAP-2 alters the physical conformation and properties of this protein. Altering the STEAP-2 protein with the C-Flag epitope resulted in a significant decrease in the effects otherwise observed, including phosphorylation of ERK and resistance to drug-induced cell death. The data indicate 25 that it is the STEAP-2 protein that mediated these phenotypic effects. Finally, in vitro translation studies using rabbit reticulocyte lysate, showed that the STEAP-2 protein is translated and exhibits the expected molecular weight. PC-3 and 3T3 cells, respectively, were modified to contain the retroviral expression system pSR encoding proteins, including STEAP-1, STEAP-2 and STEAP 30 2CFI, respectively. Gene-specific protein expression was driven from a long terminal repeat (LTR), and the Neomycin resistance gene was used for selection of mammalian cells that stably express the protein. PC-3 and 3T3 cells were transduced with the retrovirus, selected in the presence of G418 and cultured under conditions which permit expression of the STEAP-2 coding sequence. The cells were grown overnight in low 35 concentrations of FBS (0.5-1% FBS) and were then stimulated with 10% FBS. The cells were lysed in RIPA buffer and quantitated for protein concentration. Whole cell 17 lysates were separated by SDS-PAGE and analyzed by Western blotting using anti phospho-ERK (Cell Signaling Inc.) or anti-phosphotyrosine (UBI) antibodies. When compared to untransformed PC-3 cells, cells modified to contain STEAP-2 contain enhanced amounts of phosphorylated tyrosine. Similar results from an analogous 5 experiment on 3T3 cells are shown on page 3. In this latter experiment, the STEAP 2CFI expression system was also transfected into 3T3 cells, which cells were used as a control. The enhanced phosphorylation found in the presence of native STEAP-2 was significantly reduced when the conformation of the protein was altered. These results thus show conclusively that the STEAP-2 protein was produced and mediated the 10 above-described phenotypic effects. Similar results were obtained, both in PC-3 and 3T3 cells where phosphorylation of ERK, specifically, is detected. The protocol is similar to that set forth in paragraph 5 above, except that rather than probing the gels with antibodies specific for phosphotyrosine the gels were probed both the anti-ERK and anti-phospho 15 ERK antibodies. In the presence of 10% FBS, both PC-3 cells and 3T3 cells modified to express STEAP-2 showed phosphorylation of ERK which was not detectable in cells transformed to contain STEAP-2CFI. In contrast to control PC-3 cells which exhibit no background ERK phosphorylation, control 3T3-neo cells show low levels of endogenous ERK phosphorylation. Treatment with 10% FBS enhanced 20 phosphorylation of ERK protein in cells expressing STEAP-2 relative to 3T3-neo cells, while no increase in ERK phosphorylation was observed in 3T3 cells expressing modified STEAP-2, i.e. STEAP-2CFI. Other effects on cellular metabolism in cells modified to contain a STEAP-2 expression system were also observed. When cells with and without expression 25 systems for STEAP-2 were measured for calcium flux in the presence of LPA, calcium flux was enhanced in the STEAP-2 containing cells. Using FACS analysis and commercially available indicators (Molecular Probes), parental cells and cells expressing STEAP-2 were compared for their ability to transport calcium. PC3-neo and PC3-STEAP-2 cells were loaded with calcium responsive indicators Fluo4 and 30 Fura red, incubated in the presence or absence of calcium and LPA, and analyzed by flow cytometry. PC3 cells expressing a known calcium transporter, PC3-83P3H3 pCaT were used as positive control (Biochem Biophys Res Commun. 2001, 282:729). STEAP-2 mediates calcium flux in response to LPA, and the magnitude of calcium flux is comparable to that produced by a known calcium channel. 35 In addition, STEAP-2 expressing PC3 cells demonstrated increased sensitivity to agatoxin, a calcium channel blocker as compared to PC3-neo cells. These results 127A indicate that STEAP-2 expression renders PC3 cells sensitive to treatment with the Ca++ channel inhibitors. Information derived from the above experiments provides a mechanism by which cancer cells are regulated. This is particularly relevant in the case of calcium, as calcium channel inhibitors have been reported to induce the death of 5 certain cancer cells, including prostate cancer cell lines (see, e.g., Batra S, Popper LD, Hartley-Asp B. Prostate. 1991, 19:299). Cells transfected with a STEAP-2 expression system have enhanced ability to survive exposure to paclitaxel. In order to determine the effect of STEAP-2 on survival, PC3 cells lacking or expressing STEAP-2 were treated with chemotherapeutic 10 agents currently used in the clinic. Effect of treatment was evaluated by measuring cell proliferation using the Alamare blue assay. While only 5.2% of PC3-neo cells were able to metabolize Alalmare Blue and proliferate in the presence of 5 RM paclitaxel, 44.8% of PC3-STEAP-2 cells survived under the same conditions. These results indicate that expression of STEAP-2 imparts resistance to paclitaxel. These findings 15 have significant in vivo implications, as they indicate that STEAP-2 provides a growth advantage for prostate tumor cells in patients treated with common therapeutic agents. PC3 cells expressing or lacking STEAP-2 were treated with paclitaxel for 60 hours, and assayed for apoptosis using annexin V conjugated to FITC and propidium iodide staining. In apoptotic cells, the membrane phospholipid phosphatidylserine (PS) 20 is translocated from the inner to the outer leaflet of the membrane, thereby exposing PS to the external cellular environment. PS is recognized by and binds to annexin V, providing scientists with a reliable means of identifying cells undergoing programmed cell death. Staining with propidium iodide identifies dead cells. Expression of STEAP-2 inhibits paclitaxel-mediated apoptosis by 45% relative to paclitaxel-treated 25 PC3-neo cells. The protective effect of STEAP-2 is inhibited when STEAP-2 is modified by the presence of Flag at its C-terminus. The publicly available literature contains several examples of prostate and other cancers that exhibit similar phenotypic characteristics as those observed in PC3 cells that express STEAP-2. In particular, clinical studies have reported transient tumor 30 regression and/or only partial responses in patients treated with paclitaxel. For instance, only around 50% of prostate cancer patients entered, in a single agent clinical trial of paclitaxel showed reduced PSA levels when treated with doses of paclitaxel that induced grade 3 and grade 4 toxicity; a much higher level of response would have been expected based on this dose level, thus this data indicates the development of paclitaxel 35 resistance in prostate cancer patients (Beer TM et al, Ann Oncol 2001, 12:1273). A similar phenomenon of reduced responsiveness and progressive tumor recurrence was 127B observed in other studies (see, e.g., Obasaju C, and Hudes GR. Hematol Oncol Clin North Am 2001, 15:525). In addition, inhibition of calcium flux in cells that endogenously express STEAP-2, such as LNCaP cells, induces their cell death (Skryma R et al, J Physiol. 2000, 527:71). 5 Thus, STEAP-2 protein is produced not only in the cells tested, but also in unmodified tumor cells or unmodified prostate cells where the presence of mRNA has been shown. The Northern blot data in the specification clearly show that the messenger RNA encoding STEAP-2 is produced in certain prostate and tumor cells. The 3T3 and PC-3 cells, which are themselves tumor cell lines, are clearly able to 10 translate the messenger RNA into protein. Because it has been shown that there is no barrier to translation of the message in cells similar to those tumor and prostate cells in which the mRNA has been shown to be produced, it can properly be concluded that the protein itself can be detected in the unmodified tumor or prostate cells, given the fact that it is shown that mRNA is produced. This conclusion is also supported by the 15 patterns of phenotypic changes seen in cells specifically modified to express STEAP-2, these changes comport with changes seen in 127C cancer cells. Based on the above data, it is scientifically concluded that cells and tissues which produce mRNA encoding STEAP-2 also produce the protein itself. Example 46: Identification and Confirmation of Potential Signal Transduction Pathways Many mammalian proteins have been reported to interact with signaling molecules and to participate in regulating signaling pathways (J Neurochem. 2001; 76:217-223. Using immunoprecipitation and Western blotting techniques, proteins are identified that associate with 98P4B6 and mediate signaling events. Several pathways known to play a role in cancer biology can be regulated by 98P4B6, including phospholipid pathways such as P13K, AKT, etc, adhesion and migration pathways, including FAK, Rho, Rac-1, etc, as well as mitogenic/survival cascades such as ERK, p38, etc (Cell Growth Differ. 2000,11:279; J Biol Chem. 1999, 274:801; Oncogene. 2000,19:3003, J. Cell Biol. 1997,138:913.). To confirm that 98P4B6 directly or indirectly activates known signal transduction pathways in cells, luciferase (luc) based transcriptional reporter assays are carried out in cells expressing individual genes. These transcriptional reporters contain consensus-binding sites for known transcription factors that lie downstream of well-characterized signal transduction pathways. The reporters and examples of these associated transcription factors, signal transduction pathways, and~ activation stimuli are listed below. 1. NFkB-luc, NFkB/Rel; Ik-kinase/SAPK; growth/apoptosis/stress 2. SRE-luc, SRFfTCF/ELK1; MAPKISAPK; growth/differentiation 3. AP-1-luc, FOS/JUN; MAPK/SAPK/PKC; growth/apoptosis/stress 4. ARE-tuc, androgen receptor; steroids/MAPK; growth/differentiation/apoptosis 5. p53-luc, p53; SAPK; growth/differentiation/apoptosis 6. CRE-luc, CREB/ATF2; PKAlp38; growth/apoptosis/stress Gene-mediated effects can be assayed in cells showing mRNA expression. Luciferase reporter plasmids can be introduced by lpid-mediated transfection (TFX-50, Promega). Luciferase activity, an indicator of relative transcriptional activity, is measured by incubation of cell extracts with luciferin substrate and luminescence of the reaction is monitored in a luminometer. Signaling pathways activated by 98P4B6 are mapped and used for the identification and validation of therapeutic targets. When 98P4B6 is involved in cell signaling, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 47: 98P4B6 Functions as a Proton or small molecule transporter Sequence and homology analysis of 98P4B6 indicate that the 98P486 may function as a transporter. To confirm that STEAP-1 functions as an ion channel, FAGS analysis and fluorescent microscopy techniques are used (Gergely L, et al., Clin Diagn Lab Immunol. 1997; 4:70; Skryma R, et al., J Physiol. 2000, 527:71). Using FACS analysis and commercially available indicators (Molecular Probes), parental cells and cells expressing 98P486 are compared for their ability to transport electrons, sodium, calcium; as well as other small molecules in cancer and normal cell lines. For example, PC3 and PC3 98P4B6 cells were loaded with calcium responsive indicators Fluo4 and Fura red, incubated in the presence or absence of calcium and lipophosphatidic acid (LPA), and analyzed by flow cytometry. Ion flux represents an important mechanism by which cancer cells are regulated. This is particularly true in the case of calcium, as calcium channel inhibitors have been 117R reported to induce the death of certain cancer cells, including prostate cancer cell lines (Batra S, Popper LD, Hartley-Asp B. Prostate. 1991, 19: 299). Similar studies are conducted using sodium, potassium, pH, etc indicators. Due to its homology to an oxidoreductase, 98P486 can participate in imparting drug resistance by mobilizing and transporting small molecules. The effect of 98P486 on small molecule transport is investigated using a modified MDR assay. Control and 98P4B6 expressing cells are loaded with a fluorescent small molecule such as calcein AM. Extrusion of calcein from the cell is measured by examining the supematants for fluorescent compound. MDR-like activity is confirmed using MDR inhibitors. When 98P486 functions as a transporter, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 48: Involvement in Tumor Progression The 98P4B6 gene can contribute to the growth of cancer cells. The role of 98P4B6 in tumor growth is confirmed in a variety of primary and transfected cell lines including prostate as well as NIH 3T3 cells engineered to stably express 98P4B6. Parental cells lacking 98P4B6 and cells expressing 98P4B6 are evaluated for cell growth using a well-documented proliferation assay (Fraser SP, Grimes JA, Djamgoz MB. Prostate. 2000;44:61, Johnson DE, Ochieng J, Evans SL. Anticancer Drugs. 1996, 7:288). To confirm the role of 98P4B6 in the transformation process, its effect in colony forming assays is investigated. Parental NIH-3T3 cells lacking 98P4B6 are compared to NIH-3T3 cells expressing 98P4B86, using a soft agar assay under stringent and more permissive conditions (Song Z. et al. Cancer Res. 2000;60:6730). To confirm the role of 98P4B6 in invasion and metastasis of cancer cells, a well-established assay is used, e.g., a Transwell Insert System assay (Becton Dickinson) (Cancer Res. 1999; 59:6010). Control cells, including prostate and fibroblast cell lines lacking 98P4B6 are compared to cells expressing 98P4B6. Cells are loaded with the fluorescent dye, calcein, and plated in the top well of the Transwell insert coated with a basement membrane analog. Invasion is determined by fluorescence of cells in the lower chamber relative to the fluorescence of the entire cell population. 98P486 can also play a role in cell cycle and apoptosis. Parental cells and cells expressing 98P4B6 are compared for differences in cell cycle regulation using a well-established BrdU assay (Abdel-Malek ZA. J Cell Physiol. 1988,136:247). In short, cells are grown under both optimal (full serum) and limiting (low serum) conditions are labeled with BrdU and stained with anti-BrdU Ab and propidium iodide. Cells are analyzed for entry into the G1, S, and G2M phases of the cell cycle. Alternatively, the effect of stress on apoptosis is evaluated in control parental cells and cells expressing 98P486, including normal and tumor prostate cells. Engineered and parental cells are treated with various chemotherapeutic agents, such as etoposide, flutamide, etc, and protein synthesis inhibitors, such as cycloheximide. Cells are stained with annexin V FITC and cell death is measured by FACS analysis. The modulation of cell death by 98P4B6 can play a critical role in regulating tumor progression and tumor load. When 98P4B6 plays a role in cell growth, transformation, invasion or apoptosis, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 49: Involvement in Angioqenesis Angiogenesis or new capilary blood vessel formation is necessary for tumor growth (Hanahan D, Folkman J. Cell. 1996, 86:353; Folkman J. Endocrinology. 1998 139:441). Based on the effect of phsophodieseterase inhibitors on endothelal cells, 98P486 plays a role in angiogenesis (DeFouw L et al, Microvasc Res 2001, 62:263). Several assays have been developed to measure angiogenesis in vitro and in vivo, such as the tissue culture assays endothelial cell tube 129 formation and endothelial cell proliferation. Using these assays as well as in vitro neo-vascularization, the role of 98P4B6 in angiogenesis, enhancement or inhibition, is confirmed. For example, endothelial cells engineered to express 98P4B6 are evaluated using tube formation and proliferation assays. The effect of 98P4B6 is also confirmed in animal models in vivo. For example, cells either expressing or lacking 98P4B6 are implanted subcutaneously in immunocompromised mice. Endothelial cell migration and angiogenesis are evaluated 5-15 days later using immunohistochemistry techniques. 98P4B6 affects angiogenesis, and it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 50: Requlation of Transcription The localization of 98P486 and its similarity to hydrolases as well as its Ets motif (v.7) indicate that 98P486 is effectively used as a modulator of the transcriptional regulation of eukaryotic genes. Regulation of gene expression is confirmed, e.g., by studying gene expression in cells expressing or lacking 98P486. For this purpose, two types of experiments are performed. In the first set of experiments, RNA from parental and 98P4B6-expressing cells are extracted and hybridized to commercially available gene arrays (Clontech) (Smid-Koopman E et al. Br J Cancer. 2000. 83:246). Resting cells as well as cells treated with FBS or androgen are compared. Differentially expressed genes are identified in accordance with procedures known in the art. The differentially expressed genes are then mapped to biological pathways (Chen K et al. Thyroid. 2001. 11:41.). In the second set of experiments, specific transcriptional pathway activation is evaluated using commercially available (Stratagene) luciferase reporter constructs including: NFkB-luc, SREduc, ELK1-luc, ARE-luc, p534uc, and CRE-luc. These transcriptional reporters contain consensus binding sites for known transcription factors that lie downstream of well characterized signal transduction pathways, and represent a good tool to ascertain pathway activation and screen for positive and negative modulators of pathway activation. Thus, 98P486 plays a role in gene regulation. When 98P486 is involved in gene regulation, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 51: Protein - Protein Association Several 6TM proteins have been shown to interact with other proteins, thereby regulating signal transduction, gene transcription, transformation, and cell adhesion. Using immunoprecipitation techniques as well as two yeast hybrid systems, proteins are identified that associate with 98P4B6. Immunoprecipitates from cells expressing 98P4B6 and cells lacking 98P486 are compared for specific protein-protein associations. Studies are performed to confirm the extent of association of 98P4B6 with effector molecules, such as nuclear proteins, transcription factors, kinases, phsophates etc. Studies comparing 98P486 positive and 98P4B6 negative cells as well as studies comparing unstimulated/resting cells and cells treated with epithelial cell activators, such as cytokines, growth factors, androgen and anti-integrin Ab reveal unique interactions. In addition, protein-protein interactions are confirmed using two yeast hybrid methodology (Curr Opin Chem Biol. 1999, 3:64). A vector carrying a library of proteins fused to the activation domain of a transcription factor is introduced into yeast expressing a 98P4B6-DNA-binding domain fusion protein and a reporter construct. Protein-protein interaction is detected by colorimetric reporter activity. Specific association with effector molecules and transcription factors directs one of skill to the mode of action of 98P4B6, and thus identifies therapeutic, prognostic, preventative and/or diagnostic targets for cancer. This and similar assays are also used to identify and screen for small molecules that interact with 98P4B6. 1 2 Thus it is found that 98P4B6 associates with proteins and small molecules. Accordingly, 98P486and these proteins and small molecules are used for diagnostic, prognostic, preventative and/or therapeutic purposes. Throughout this application, various website data content, publications, patent applications and patents are referenced. (Websites are referenced by their Uniform Resource Locator, or URL, addresses on the World Wide Web.) The disclosures of each of these references are hereby incorporated by reference herein in their entireties. The present invention is not to be limited in scope by the embodiments disclosed herein, which are intended as single ilustrations of individual aspects of the invention, and any that are functionally equivalent are within the scope of the invention. Various modifications to the models and methods of the invention, in addition to those described herein, will become apparent to those skilled in the art from the foregoing description and teachings, and are similarly intended to fall within the scope of the invention. Such modifications or other embodiments can be practiced without departing from the true scope and spirit of the invention. 131 TABLES: TABLE I: Tissues that Express 98P486: a. Malignant Tissues a Bladder b. Breast c. Cervix d. Colon e. Kidney f. Lung g. Ovary h. Pancreas i. Prostate j. Stomach k. Uterus TABLE II: Amino Acid Abbreviations SINGLE LETTER THREE LETTER FULL NAME F Phe phenylalanine L Leu leucine S Ser seine Y Tyr tyrosine C Cys cysteine W Trp tryptophan P Pro proline H His histidine a Gin glutamine R Arg arginine lie isoleucine M Met methionine T Thr threonine N Asn asparagine K LYs lysine V Val valine A Ala alanine D Asp aspartic acid E GIu glutamic acid G Gly glycine TABLE III: Amino Acid Substitution Matrix Adapted from the GCG Software 9.0 BLOSUM62 amino acid substitution matrix (block substitution matrix). The higher the value, the more likely a substitution is found in related, natural proteins. (See world wide web URL ikp.unibe.ch/manual/blosum62.htnIl) A C D E F G H I K L M N P Q R S T V W Y. 4 0 -2 -1 -2 0 -2 -1 -1 -1 -1 -2 -1 -1 -1 1 0 0 -3 -2 A 9 -3 -4 -2 -3 -3 -1 -3 -1 -1 -3 -3 -3 -3 -1 -1 -1 -2 -2 C 6 2 -3 -1 -1 -3 -1 -4 -3 1 -1 0 -2 0 -1 -3 -4 -3 D 5 -3 -2 0 -3 1 -3 -2 0 -1 2 0 0 -1 -2 '-3 -2 E 6 -3 -1 0 -3 0 0 -3 -4 -3 -3 -2 -2 -1 1 3 F 6 -2 -4 -2 -4 -3 0 -2 -2 -2 0 -2 -3 -2 -3 G 8 -3 -1 -3 -2 1 -2 0 0 -1 -2 -3 -2 2 H 4 -3 2 1 -3 -3 -3 -3 -2 -1 3 -3 -1 I 5 -2 -1 0 -1 1 2 0 -1 -2 -3 -2 K 4 2 -3 -3 -2 -2 -2 -1 1 -2 -1 L 5 -2 -2 0 -1 -1 -1 1 -1 -1 M 6 -2 0 0 1 0 -3 -4 -2 N 7 -1 -2 -1 -1 -2 -4 -3 P 5 1 0 -1 -2 -2 -1 Q 5 -1 -1 -3 -3 -2 R 4 1 -2 -3 -2 S 5 0 -2 -2 T 4 -3 -1 V 11 2 W 7 Y 133 TABLE IV: HLA Class lli Motifs/Supermotifs TABLE IV (A): HLA Class I SupermotifsMotifs SUPERMOTIF POSITION POSITION POSITION 2 (Primary Anchor) 3 (Primary Anchor) C Terminus (Primary Anchor) Al TILVMS FWY A2 LIVMATQ IVMATL A3 VSMATLI RK A24 YFWVLMT FlYWLM B7 P VILFMWYA B27 RHK FYLWMVA B44 ED FWYLIMVA B58 ATS FWYLIVMA 862 QLIVMP FWYMIVLA MOTIFS Al TSM Y Al DEAS Y A2.1 LMVQIAT VLMAT A3 LMVISATFCGD KYRHFA All VTMLISAGNCDF KRYH A24 YFWM FLIW A*3101 MVTALS RK A*3301 MVALFIST RK A*6801 AVTMSLI RK B*0702 P LMFWYAIV B*3501 P LMFWYIVA 851 P LIVFWYAM B*5301 P IMFWYALV B*5401 P ATIVLMFWY Bolded residues are preferred, italicized residues are less preferred: A peptide is considered motif-bearing if it has primary anchors at each primary anchor position for a motif or supermotif as specified in the above table. TABLE IV (B): HLA Class Il Supermotif 1 6 9 W, F, Y, V,., L A, V, 1, L, P, C, S, T A, V, 1, L, C, S, T, M, Y TABLE IV (C): HLA Class II Motifs MOTIFS 1 a nchor 1 2 3 4 5 1* anchor 6 7 8 9 DR4 preferred FMYLIVW M T I VSTCPALIM MH MH deleterious W R WDE DR1 preferred MFLIVWY PAMO VMATSPUC M AVM deleterious C CH FD CWD GDE D DR7 preferred MFLIVWY M W A IVMSACTPL M IV deleterious C G GRD N G DR3 MOTIFS 1* anchor 1 2 3 ' *anchor 4 5 1* anchor 6 Motif a preferred LIVMFY D Motif b preferred LIVMFAY DNQEST KRH DR Supermotif MFLIVWY VMSTACPL Italicized residues indicate less preferred or "tolerated" residues TABLE IV (D): HLA Class I Supermotifs POSITION: 1 2 3 4 5 6 7 8 C-tenninus

SUPER

MOTIFS A1 1*0 Anchor I* Anchor TIL VMS FWY A2 1* Anchor 1* Anchor LIVMA TO LIVMAT A3 Preferred 10 Anchor YFW YFW YFW P 1* Anchor VSMATL (4/5) (3/5) (4/5) (4/5) RK deleterious DE (3/5); DE P (5/5) (4/5) A24 1 Anchor I* Anchor YFWIVLMT FIYW LM B7 Preferred FWY (5/5) 1* Anchor FWY FWY 1 *Anchor UVM (3/5) P (4/5) (3/5) VILFMWYA deleterious DE (3/5); DE G QN DE P(5/5); (3/5) (4/5) (4/5) (4/5) G(4/5); A(3/5); QN(3/5) B27 10 Anchor 1*Anchor RHK FYLWMIVA B44 1* Anchor 1 0 Anchor ED FWYLIMVA B58 1* Anchor I* Anchor ATS FWYLIVMA 862 1* Anchor 1- Anchor QUVMP FWYMIVLA Italicized residues indicate less preferred or "tolerated* residues 135 TABLE IV (E): HLA Class I Motifs POSITION 1 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW 1*Anchor DEA YFW P DEQN YFW 1*Anchor 9-mer STM Y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCUVM 1*Anchor GSTC ASTC LIVM DE 1*Anchor 9-mer DEAS Y deleterious A RHKDEPYFW DE PQN RHK PG GP Al preferred YFW 1*Anchor DEAQN A YFWQN PASTC GDE P l'Anchor 10- STM y mer deleterious GP RHKGLIVM DE RHK QNA RHKYFW RHK A Al preferred YFW STCLIVM 1*Anchor A YFW PG G YFW 1*Anchor 10- DEAS Y mer cl..rious RHK RHKDEPYFW P G PRHK QN A2.1 preferred YFW 1*Anchor YFW STC YFW A P 1*Anchor 9-mer LMIVQAT VUMAT deleterious DEP DERKH RKH DERKH POSITION:l 2 3 4 5 6 7 8 9 C Teninus A2.1 preferred AYFW 1*Anchor LVIM G G FYWL 1*Anchor 10- LMIVQAT VIM- - VLUMAT mer deleterious DEP DE RKHA P RKH DERK RKH H A3 preferred RHK 1*Anchor YFW PRHKYF A YFW P 1*Anchor LMVISATFCGD W KYRHFA deleterious DEP DE Al1 preferred A 1*Anchor YFW YFW A YFW YFW P 1* Anchor VTLMISAGNCD KRYH F deleterious DEP A G A24 preferred YFWRHK 1*Anchor STC YFW YFW 1*Anchor 9-mer YFWM FLIW deleterious DEG DE G ONP DERH G AQN K A24 Preferred 1*Anchor P YFWP P 1*Anchor 10- YFWM FUW mer Deleterious GDE ON RHK DE A QN DEA A310 Preferred RHK 1*Anchor YFW P YFW YFW AP 1*Anchor 1 MVTALIS RK Deleterious DEP DE ADE DE DE DE A330 Preferred l'Anchor YFW AYFW 1*Anchor 1 MVALF/ST RK Deleterious GP DE A680 Preferred YFWSTC 1*Anchor YFWUV YFW P 1 Anchor 1 AVTMSLI M RK deleterious GP DEG RHK A 8070 Preferred RHKFWY 1*Anchor RHK RHK RHK RHK PA 1*Anchor 2 P LMFWYA1 V deleterious DEQNP DEP DE DE GDE QN DE 136 POSMON1 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW 1*Anchor DEA YFW P DEQN YFW l'Anchor 9-mer STM y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCLIVM 1*Anchor GSTC ASTC LIVM DE l'Anchor 9-mer DEAS y deleterious A RHKDEPYFW DE PQN RHK PG GP B350 Preferred FWYLIVM 1*Anchor FWY FWY lAnchor 1 P LMFWYIV deleterious AGP G G B51 Preferred LIVMFWY 1*Anchor FWY STC FWY G FWY 1*Anchor P LIVFWYA M deleterious AGPDER DE G DEQN GDE HKSTC B530 preferred LIVMFWY 1*Anchor FWY STC FWY LIVMFW FY l'Anchor 1 P Y IMFWYAL deleterious AGPON G RHKQN DE B540 preferred FWY *Anchor FWYLIVM LIVM ALIVM FWYA l'Anchor 1 P P ATIVLMF deleterious GPQNDE GDESTC RHKDE DE QNDGE DE 137 TABLE IV (F): ummary of HLA-supertypes verall phenotypic frequencies of HLA-supertypes in different ethnic populations Specificity Phenotypic frequency p osition 2 -Terminu Caucasian N.A. BI apanes hine ispani verage 7 AILMVF 3.2 5.1 7.1 3.0 9.3 9.5 3 ILMVST K 7.5 2.1 5.8 2.7 3.1 .2 ILMVT ILMVT 5.8 9.0 2.4 5.9 3.0 2.2 4 F (WIVL I (YWLM) 3.9 8.9 8.6 0.1 :3 0.0 (D) WYLIMVA 43.0 1.2 42.9 9.1 9.0 37.0 1 I(LVMS) _VY 47.1 16.1 21.8 4.7 6.3 5.2 27 K CYL (WMI) 28.4 26.1 13.3 13.9 5.3 3.4 2 (IVMP) :VY (MIV) 12.6 4.8 36.5 5.4 1.1 8.1 TS FWY_(LV) 10.0 25.1 1.6 .0 .9 10.3 TABLE IV (G): Calculated population coverage afforded by different HLA-supertype combinations HLA-supertypes Phenotypic frequency aucasian 4.A Blacks Japanese inese ispanic verage .0 16.1 87.5 8.4 6.3 6.2 A2, A3 and B7 9.5 )8.1 100.0 , 9.5 9.4 .3 , A3, B7, A24, B44 9.9 99.6 100.0 9.8 9.9 9.8 d A A3, B7, A24, , Al, B27, B62, nd B 58 1 1 otifs indicate the residues defining supertype specificites. The motifs incorporate residues determined on the basis of ublished data to be recognized by multiple alleles within the supertype. Residues within brackets are additional residues iso predicted to be tolerated by multiple alleges within the supertype. Table V: Frequently Occurring Motifs ame Description ?otential Function Nucleic acid-binding protein functions as ranscription factor, nuclear location A-C2H-12 34% _ Zinc finger, C2H2 type probable Cytochrome b(N- membrane bound oxidase, generate ytochroebN 68% ierminal)/b6/petB superoxide Jomnains are one hundred amino acids ong and include a conserved Ig 19% Immunoglobulin domain ntradomain disulfide bond. landemn repeats of about 40 residues, ach containing a Trp-Asp motif. :unction in signal transduction and 40 18% WD domain, G-beta repea rotein interaction may function in targeting signaling PDZ 23% PDZ domain molecules to sub-membranous sites iRR 28% Leucine Rich Repeat short sequence motifs involved in orotein-protein interactions nserved catalytic core common to th serne/threonine and tyrosine rotein kinases containing an ATP Pkinase 23% Protein kinase domain inning site and a catalytic site 138 Ieclkstrin homology involved in ntracellular signaling or as constituents H 16% PH domain f the cytoskeleton 0-40 amino-acid long found in the xtracellular domain of membrane GF 34% _ GF-like domain bound proteins or in secreted proteins everse transcriptase (RNA-dependent DNA Rvt 49% lymerase) 2ytoplasmic protein, associates integral k 5% k repeat embrane proteins to the cytoskeleton NADH- embrane associated. Involved in Ubiquinone/plastoquinone roton translocation across the xie 12% 'complex 1), various chains embrane :alcium-binding domain, consists of a12 Efhad 24 EF and esidue loop flanked on both sides by a F hand 12 residue alpha-helical domain Retroviral aspartyl Aspartyl or acid proteases, centered on p 79% rotease catalytic aspartyl residue extracellular structural proteins involved n formation of connective tissue. The Collagen triple helix repeat sequence consists of the G-X-Y and the collagen 2% 20 copies) polypeptide chains forms a triple helix. ocated in the extracellular ligand inding region of receptors and is about 00 amino acid residues long with two airs of cysteines involved in disulfide n3 0% ibronectin type IlIl domain bonds even hydrophobic transmembrane regions, with the N-terminus located / transmembrane receptor xtracellularly while the C-terminus is tm_1 19% 'rhodopsin family) :ytoplasmic. Signal through G proteins Table VI: Motifs and Post-translational Modifications of 98P486 CAMP- and cGMP-dependent protein kinase phosphorylation site. 176 - 179 RKET (SEQ ID NO: 114) Protein kinase C phosphorylation site. 235 - 237 SVK Casein kinase I phosphorylation site. 9 - 12 SATD (SEQ ID NO: 115) 50 - 53 TVME (SEQ ID NO: 116) 130-133 SCTD (SEQ ID NO: 117) 172 - 175 SPEE (SEQ ID NO: 118) N-myristoylation site. 14 - 19 GLSIST (SEQ ID NO: 119) G-protein coupled receptors family 1 signature. 52 - 68 MESSVLLAMAFDRFVAV (SEQ ID NO: 120) Table VII: Search Peptides v.1 aal-454 (SEQ ID NO: 121) 9-mers, 10-mers and 15-mers MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 139 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD v.2 aal-45 (SEQ ID NO: 122) A 9-mers, 10-mers, 15-mers SGSPGLQALSL SLSSGFTPFS CLSLPSSWDY RCPPPCPADF FLYF v.5, (one aa diff at 211 and different c-terminal) Part A 9-mers: aa203-219 NLPLRLFTFWRGPVVVA (SEO ID NO: 123) 10-mers: aa202-220 ENLPLRLFTFWRGPVVVAI (SEQ ID NO: 124) 15-mers: aa197-225 SAREIENLPLRLFTFWRGPVVVAISLATF (SEQ ID NO: 125) Part B 9-mers: aa388-419 WREFSFIQIFCSFADTQTELELEFVFLLTLLL (SEQ ID NO: 126) 10-mers: aa387-419 NWREFSFIQI FCSFADTQTELELEFVFLLTLLL (SEQ ID NO: 127) 15-mers: aa382-419 VSNALNWREFSFIQI FCSFADTQT ELELEFVFLLTLLL (SEQ ID NO: 128) v.6, (different from our original in 445-490) 9-mers; aa447-490 (SEQ ID NO: 129) VLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM 10-mers: aa446-490 (SEQ ID NO: 130) LVLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM 15-mers: aa441-490 (SEQ ID NO: 131) NFVLALVLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM v.7, (deleting our original 340-394, 392-576 is different) Part A 9-mers: aa334-350 FLNMAYQQSTLGYVALL (SEQ ID NO: 132) 10-mers: aa333-351 LFLNMAYQQSTLGYVALLI (SEQ ID NO: 133) iS-mers: aa328-355 RSERYLFLNMAYQQSTLGYVALLISTFHV (SEQ ID NO: 134) Part B 9-mers: aa384-576 (SEQ ID NO: 135) PSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKI PPLSTPPPPA MWTEEAGATAEAQESGI RNKSSSSSQI PVVGVVTEDDEAQDSI DPPESPDRALKAANSWRNPV 140 LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLGEFLGSGTWMKLETIILSKLTQEQKSKHCMF SLISGS 10-mers: aa383-576 (SEQ ID NO: 136) LPSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKIPPLSTPPPPA MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDSIDPPESPDRALKAANSWRNPV LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLG EFLGSGTWMK LETIILSKLT QEQKSKHCMF SLISGS 15-mers: aa378-576 (SEQ ID NO: 137) VLALVLPSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKI PPLSTPPPPA MWTEEAGATAEAQESGIRNKSSSSSQI PVVGVVTEDDEAQDSIDPPESPDRALKAANSWRNPV LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLG EFLGSGTWMK LETIILSKLT QEQKSKHCMF SLISGS v.8, SNP variant of v.6, one aa different at 475 9-mers: aa466-482 KSQFLEEGMGGTIPHVS (SEQIDNO: 138) 10-mers: aa465-483 EKSQFLEEGMGGTIPHVSP (SEQIDNO: 139) 15-mers: aa460-489 IKKGWEKSQFLEEGMGGTIPHVSPERVTV (SEQ ID NO: 140) V13 9-mers: aa9-25 SPKSLSETFLPNGINGI (SEQIDNO: 141) 10-mers: aa8-26 GSPKSLSETFLPNGINGIK (SEQID NO: 142) 15-mers: aa3-31 SISMMGSPKSLSETFLPNGINGIKDARKV (SEQ ID NO: 143) v.14 9-mers: aa203-219 NLPLRLFTFWRGPVVVA (SEQID NO: 144) 10-mers: aa202-220 ENLPLRLFTFWRGPVVVAI (SEQID NO: 145) 15-mers: aa197-225 SAREIENLPLRLFTFWRGPVVVAISLATF (SEQ ID NO: 146) V. 21 9-mers 557-572 SKLTQEQKTKHICMFSLI (SEQ ID NO: 147) 10-mers 556-573 LSKLTQEQKTKHCMFSLIS (SEQ ID NO: 148) 15-mers 551-576 LETIILSKLTQEQKTKHCMFSLISGS (SEQID NO: 149) V. 25 9-mers aa 447-463 ILFLPCISQKLKRIKKG (SEQIDNO: 150) 10-mers aa 446-464 IILFLPCISQKLKRIKKGW (SEQ ID NO: 151) 141 15-mers aa440-468 VILGKIILFLPCISQKLKRIKKGWEKSQF (SEQ ID NO: 152) Tables Vill - XXI: 1TableVIII-VI-HL11A-A1.gmers- TableV1lt.V1.HLA.AI..gmers. at-~.IIL.Iges Table 1ill-V1-HLA-A1-9mers-ers 98P4B6 98P466 98P4B66 Each peptide is a portion of SEQ 10 Each peptde is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 speciied, the length of peptide is9 amino acds, and the end position for amino acids, and the end position for amino acids, and the end position for each peptide is the start position plus each peptide is the start position plus ach peptide is the start position plus eighL ___ eih ____ _I eight Start ubsequence]| Score Start Subseuenc o re StartS ______ 443 I ILDLLOLCR 25.000 EEEYYRFYT 0.225 432 FVLALVLPS 0.050 129|_ NAEYLASLF jf9.000 J 388][ WREFSFlQS 0.225 12 SLSETCLPN 0.05 294I WLETWLQCR || 9.000 198 AREIENLPL 0.225 106 HLLVGKILI 0.050 F113]| LIDVSNNMR 5.000 57 VIGSRNPKF 0200 311 VAY 0.050 1200 | EIENLPLRL |56| IGSRNPK .0.25 2691 LVYLAGLLA 0050 244.] QSDFYKIPI 3.750217 AISLATF VAISLAT I405 |ISTFHVLIY | 3.750 3 SlSMMGSPK 0.200 I-11 LSETCLPNG If 2.700 417T I RAFEEETYR If .2O] 166 J1 YICSNN10A if0.050 12211 LSLATFFFLY IF 2.500 j 436 LVLPSIVIL 0.200 258 TIPlVAlTI 0.050 126311 AITLLSLW j 3771 TSIPS H 0.150 8 LPNGING5K 00.050 276 LAAAYQLYY || 2.500 [158 IPKDASRQW 0.125 ] 435 ALVLPSIVI 0.050 419| FEEEYYRFY ||LWDLRHLLV 2500.125 2 IKDARKVV 0.050 [155| QLGPKDASR || 2.000 |Y 1 0.125 J 73 WDVTHHED 0.050 66I ASEFFPHVV 1.350 222 LATFFFLYS 0.050 _272 I LAGLLAAAY || 0J ENLPLRLFT 084 1 INIPIDI 0.050 35I| VIGSGDFAK || 1.000 |RYLFLNMAY 0367[ SlG1I I 0.050 17811 VIELARQLN 0.900 SGDFAKSLT 0.12 TIRLIRCGY 0.050 3561[ RIEMYISFG |5 306[ GLLSFFFAM 0.050 418 i AFEEEYYRF || 0.900 | 406] STFHVUYG 261]1 IVAITLLSL 1170.050 319 YSLCLPMRR ||VAISLATFF 0.75 0i-0 20 1 NLPLRLFTL[ 43 KSLTIRLIR |0.750 _ 67 ICSNNIQAR 327][ RSERYLFLN 4_0.675_j 0 YVALLISTF TableVlI.V24ILAAI.9mers. 427 11 YTPPNFVLA [23.51 V|HPYAR 9i_ _ _ _ 304 | QLGLLSFFF |381 | 0100] Each peptide is a portion of SEQ ID 257| KTLPIVAIT |INGIKARK .100 NO: 5; each start position is specified, the length of peptide is 9 135 Ii SLFPDSLIV II0501 2.. iGNIDARIF 010 amino acids, and the end position 223 | ATFFFLYSF || 0.500 | 81 QLYYGTKYR 0.100 1 for each peptide is the start position 5J LLAAAYQLY LJ J 22 CLPMRRSER .100 psg 3 ALNWREFSF ||0500 [ 1 -A : I 0.100 StartI Subs Score 1219 AISLATFFF I 0.500 1 1 0.100 23 ] 116 TCLPNGING 0.50 WKR 33 CPPPCPADF JI0.500 [901 FVAIHREHY 110500 1 41 NIENSWNEE 3[ PCPADFFLY 0.250 871 NIlFVAHR .251 PIEVNKTL .090 LSLSLSSGF 0.150 '249][ KIPIEIVNK 0.400 1 LSFFFAMVH 37 CPADFFLYF -137]| FPDSLIVKG 0.250 195 LSSAREIEN 1 0.075 1 ( 189 I1 PIDLGSLSS 31 0.250 [11161 FVSNNMRINQ IO oi 24 11StPSSWDYR l .0 [2-47I RNQQSDFYK][ 0.52801 YQIXYGTKY 0.757~ 1211SSGTFI 0.100] 1351 1 EEEVWRIEM 1 0.225 . ? 2 ISLATFFFL I 0.07-5. 14 FTPFSC 0075 [349 | WNEEEVWRI 11 0225 1 1753 RQQVIELAR 0 GLQALSISL F 0.0507 [25 11 YPSNAEYL 1 0225 1 127 71 ESAYA f 05I1 QALSLSLSS If 0.050 143 TableVill-V2-HLA-A-9mers- 4 LRLFTFWRG 0.00I TableVlll-VHLA-AI9mers 98P486 11] 1 0.000 98P4B6 I Each peptide is a portion of SEQ ID FWRGPVWA 1 (.000 Each peptide is a portion of SEQ ID NO. 5; each start position is _______________0._00 NO: 13; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 amino adds, and the end Position amino acids, and the end position or each peptide is the start position TableVIl-V58-HLAAI-9mers- r each peptide is the start position plus eight. 98P4B6 plus eight SartI Subsequence [ Score | Each peptide is a portion of SEQ ID Start I Subsequence S[or 13| LSSGFTPFS 0.030 NO: 5; each start position is 2 LPSIVILGK ~~] GSPGLQALS][ j~ specified, the length of peptide is 9 4 fTPYPR ~ amino acids, and the end position [201 FSCLSLPSS | 0.030 | or each peptide is the start position r1 HVSP 0200 __ SGSPGLOAL 1 0.025 plus eight _ 13 LFLPCISRK IF____ 32-|| RCPPPCPAD |f 0.020 | Start o 16 PCIS I 050-1 1 35 PPCPADFFL ||1 F21 E4 VLPSIVILG 11 0.050 371 SPGLQALSL 0.013 F17 E 2.250 _ LPCISRKLK 10.0 2111 SCLSLPSSW i 0.010 F ] E EF 1.800] iE~ IVILGKIIL . 8 || ALSLSLSSG || 0.010 F-1 [ 35 1 LEEGGGTI 0 10 r SLSSSGF | 0.00 | W][ Q E 074 GTIPH 0.025 I 11 || LSLSSGFTP || 0.007 | -4 S0381 GIGG0 25 | LPSSWDYRC I 0.005 | 0.050 1 KIILFLPCI 020 I 16 || GFTPFSCLS I 0.005 | -13 E 031 If KSQFEEGI 0.015 1 28 SWDYRCPPP I 0.005 1 18 E 04611 VSPERVTVM 0015I 31 1 YRCPPPCPA I 0.005 1 iz1 T 03771 EGIGGTIPH I 15-1 SGFTPFSCL I 0.003 107 0.010 471 SIVILGKIII 0.010 34-|| PPPCPADFF _ _0.003 |- IFOSFA f 0010 1SRK iF 5-1i 6 11LQALSLSLS I 0.002 | RE QF-.00 1 11 IILFLPCIS 110.010] 22 CLSLPSSWD I 051 I 1I 0_ SRKLKR.I0KK01 19 || PFSCLSLPS I 0.000 15 E 0.003 7 ILGKIILFL 0.5| 18 TPFSCLSLP | 0.000 |KKWEKSQF 4 PGLQALSLS || 0.000 1 ISRKLKRIK 27 |SSWDYRCPP[ 0.000 1 ADTOTELEL F0.0037 33 QFLEEGIGG .00 26 1 PSSWDYRCP |f 0.000 3 11 EFSFIQFC 10.003 4 F ]PHVSPERD I 29 WDYRCPPPC 00 I -55-52-1 1 GKIILFLPC|000 30 D | IRFTFN d I 139I IGGTIPHVS .003 ____________ -231 r7FLL ] .0 811 GWEKSQFL E Fo0002q 2 | FTFWL] 0.001 [ PSIVILGKI 1 0.002 91 IFCSFADTQ || 0.001 32] SQFLEEGIG J 0002 TabTeVa-V5A-HLAVAi-9mers- -H23 L - KRIKKGWEK 98P4B6 17 CIS Each peptide is a portion of SEQ ID TableVIIV6.HLA-AI-9mers- 0 1 GGTIPHVSP 0001 NO: 11; each start position is I 98P4B6 30 [j EKSQFLEEG 5F 0sit1 specified, the length of peptide is 91 Ech peptide is a portion of SEQ ID 7 11KGWEKSQFL [o -55 amino acids, and the end position for NO: 13; each start position is GIL ach peptide is the start position plus specified, the length of peptide is 9 eight. amino acids, and the end position RIKKGWEKS 1 0.000 Str Sb un e Ibrfo each peptide is the start position 21] KRIKKGW _____ 7i N RoSr plus eight. T] Fmw oStartf Subsuence l Score11 PHVPRT 1 0 21 | EEVLT 20 ||RL r 0000 ~i PLRLFTFWR 1 .0.005 F 1 ILFLIR 0.20 20 IKKG 5 ]) RLFTFWRGP I 0.001 VILGKIILF .05 WEKSQ r i TFWRGPV 11 0.001 __29_2 __ _ F |.005 144 TableV1ll-V6-HLA-A1.9mers- Each peptide is a portion of SEQ ID TableVlll.V7C-HLA-A1.9mers 98P486 NO: 15; each start position is 98P416 Each peptide Is a portion of SEQ ID specified, the length of peptide is 9 Each peptide is a portion of SEQ ID NO: 13; each start position is amino acds, and the end position NO: 15: each start position is specified, the length of peptide is 9 for each peptide is the start position specified, the length of peptide is 9 amino acids, and the end position plus eight. amino acds, and the end position for each peptide is the start ition S ce for each peptide is the start position plus eight. 167 KLETIILSK J90000] plus eight. Start | Subsequence ||Score] 5 WTEEAGATA 45W Start Subsquence I Score F227|| LKRIKKGWE || 0.00 |77 SS~PV] f [j~j]LKIKGWE[~I]iTI LASPAAAWK [4.000 ( fSSQP j0.030 f69 I AQESGIRNK LI[OCI 125 JrNGVGPLWEF 1[ 0.025] TableVll.V7A-HLA-A1-9mers- F PIEWOQORK 6 ATAEAQESG 0025 98P4136 =_6J TAEAQESGI 1f0.900 1 37 LPIEWQQDR [0.025] Each peptide is a portion of SEQ ID 9 1 SVEVLASPA 0.900 92 EDD NO- 15; each start position is 1 ASGTLSLAF 169 ETIILSKLT 0.025 specified, the length of peptide is 9 [E560 amino acids, and the end position II F1 s611 TEQS 0.2 for each peptide Is the start position plus eight. 5 LLVV 0.1121 PSOA F022 Start Subsequence Score KCLGANILR PESPRALK. I5 |1 LSETFLPNG j 2.7 90 VEDDEAQD 0EVASPA 0.020 _ 4 1 SLSETFLPN [0QIPWG 0020 7i ETFLPNGIN 2 LSEIVLPIE VILDL 8 || TFLPNGING 151 12 0.020 | FLPNGING | 0.010 | [1561 LGEFLGSGT I Q RKIPPL 015 3 || KSLSETFLP || 07____ KLTQEQKSK 10.200 1 1-7! ESGIRNKSS 10.015 1 | SPKSLSETF 0159T FLGSGTWMK 0.0.230 96 11 AODSIDPPE j 6| SETFLPNG |0.001 177 TQEQKSKHC F 14[ ASPM 10015 211 PKSLSETFL | .000 | 128 GPLWEFL SQIPWGW IIFY01j - 11451 GTLSLAFTS 1~I 3T91_ KSQMASGTL 10.0151 TableVIII.V75.-A-A1-9mers- 52 TPPPPAMWT [2 RJLSFTSWS ii 0.015 98P4B6 GVGPLWEFL [ L R S L .0131 Each peptde is a portion of SEQID 35 lVLPIEWQQ ID.10 r-1 S01 NO: 15; each start position is I IDPPESPDR U -o575 162 SGTWMKLET specified, the length of peptide is 91601 LGSGTWMKL amino acids, and the end position F-jj SSSSSQIFV 1 E for each peptide is the start position plus eight. 14 WLEFG - 71 LJ S Start Subsequence || Score] | ii]w Lup< ][.0] [88 GWvEDDEA L57| AYQQSTLGY ||0.125] 1 22 CLGANILRG 0.050] 1t4 2][ MSGTLS 0 9 || STLGYVALL ||68 I.5EAQESGRN O5 GATAEAQES 0fj |o 83 OSTLGYVAL || 0.030]CMFSLISG TNGV [ 1). [i11 FLNMAYQQS ||0,010 [7 1 DLSVEVLAS I I4|61 KIPPLSTPP][0j-] 4 I MAYQSTLG F5 10.1 170 ][001 [-62][ EAGATAEAQ 0.010 3:| NMAYQQSTL |F|R] F2 SIVISV I F 109]1 ALKMNSWR 0.0050] L QQSTLGYVA 0.003 GA 148 SLAFSWSL 0.1 r2| LNMAYQQST 001 QAASGTLSL F [121 AANSWRNPV H[..003 -6 ||YQQSTLGYV ||3 HTNGVGPLW [ 1 LAFTSWSLG r 0010] ---1311 GISEIVIPI IlO-0-50 34.i EIVIPIEWO .010io 1309 LWEFLLRLL 1(0045 116 1- WRNPVLPHT ]~h 173E LSKLTQEQK iaoof SEQGID T lspecif the IW ln h f i i 9 0 3 1 ][ 0 1 M84681][ SSQIPWGV 0 .J-3 SLGEFLGSG 10[0107] 145 TableVill-V7C-HLA-AI-9mers- TablelX-VI-HLAA1lmers. TabletX.V1-HLA.Al-mers. 98P4B6 I 98P46I 98P416 ach peptide is a portion of SEQ ID Each peptide is a portio of SEQ ID Each peptide is a portion of SEQ 1D NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is specfed, the length of peptide is amino acids, and the end position 10 amino acids, and the end 10 amino acids, and the end for each peptide is the start position position for each peptide is the stat position for each peptide is the sta plus eight. position plus-nine. position plus nine Start- I Subsequence [i Score | Subsequence Score 11201| VLPHTNGVG ||0.010 [7 KTLPIVAITL 1.250 TNIIFVAIHR 1 0.125 181 i KSKHCMFSL |0.008 271 YLAGLLAAAY 1.000] 3 vGVIGSGDF 113 1 ANSWRNPVL || o0oos] r-ii GVIG GDFAK 11000] 23511 VIIP F[ oJioo] 67 ] AEAQESGIR ||.005] 3211 LCLPMRRSER 31 1.000 14101 VYGWKRAF ]F-10 185 CMFSUSGS F10.05] 1181 AREIENLPLR 0112 R ILIDVSNNMR |00.100] 144-1 SGTLSLAFT |T 1111 VSNNMRIN.Y 00 0750 166 YICSNNQAR ____ 93 1 DDEAQDSID I10005] 32711 RSERYLFLNM 1 0.675 1 16 IITCLP 60|| TEEAGATAE || ] _ SGDFAKSLTI 1 0.625 0 05217 P AISLATFF 1 . 8 || LSVEVLASP ||003 i38741 NALNWREFSF 00 155 OLGPKDASRO 10..000 183 1 KHCMF 0218 I VAISLATFFI5 | 0. 003441NIENSNEEE 0;00 F25 | ANILRGGLS |0.003 127411 GUAAAYQLY 1 0.500 1 DSLIVKGFN 165 1 WMKLETIll 0 81 H DALTKTNIIF 0.003500 I 4051 IS1TFHVLlYG 0075 101 1| DPPESPDRA 10.003 | 32211 CLPMRRSERY 00366 MSLGLLSLLA 0.075 15| SPAAAWKCL 173. 00DVTHEDA 3Ii| KSLSETCLPN 3|075] ________________232 jVRDVIH-PYAR 31 0.500 34]1 ASLFPDSLIV7 II 075 1 TablelX-V1.HLA-A1-10mers- 1 442 I VILDLLQLCR F-431 K&TIRLIRC 07 98P486 125 YPESNAEYLA 0.450 30311 KQLGLLSFFF ][75] Each peptide is a portion of SEQ ID __ 2_9 ____F11__ 07 NO: 3; each start position is Rll SLGLF 0.07 specified, the length of peptide is GINGIKOARK 1 0.400 GS0 10 amino acids, and the end F 2I ESISMMGSPK 1 0.300 1 LLVGKILIDV IF 0.0W position for each peptide is the start -661 ASEFFPHWD 060 =SRNPKFASEF position plus nine. r4719 FEEEYYRFYT 10.22 I 12691I LVYLAGLLM ] [Strt[ Subsequence -o[ Score357o NEEEVWRIEM 23i1 LALVIPSIVI 0 178[ VIELARQLNF 4 [ 3j LATFFFLYSF || 4520. 0 0071 TIGYVALLIS7][0.050 [4431 r[2500 [561 WIGSRNPKF 10.200 41 GIMSLGLL 294 | WLETWLQCRK 0 2811 QLYYGTKYRR 0.200 401 VALLISTFHV 1.0.050 r135 SLFPDSLIVK al[ HWIGSRNPK 10200] 147 NWSAWALQ 2001 EIENLPLRLF I 278 AAYQLYYGTK 0.200 189 PIDLGSLSSA 9.00050 356[ RIEMYISFGI |I 4.500 [417 RAFEEEYYRF 30 ] 24 ITLLSIVYLA 0.050 2201[ ISLATFFFLY I 3.750 | [ WVAISLATF 102001 SFFFAMVH I0 I 391[ FSFIQSTLGY f 2 [ YKIPIEIVNK 310.200 310 FFFAMVHVAY .7500 [76]| VTHHEIDALTK7F2500 F 7j7 VAYSLCLPMR |1|20 201 FTLWRGP2.0V005|0 F404 I. LISTFHVLIY I 2.500 | 7 CLPNGINGIK 0.200 1194 SLSSAREIEN II o-o5o I 1262 VAITLLSLVY 2.500 2401 ARNQQSDFYK r275]| LLAAAYQLYY ||200 r37711 TSIPSVSNAL 2 |.150 29811 WLQCRQLL7 [113]| UDVSNNMRI II 2.50I 382I VSNALNWREF 1.150 44011 SIVILDLLQL 12500050 351 EEEVWRIEMY || 2.250 [ ENLPLRLFTL 1 0.125 1 22 SLATFFFLYS 0 | 418]i AFEEEYYRFY II - 1 01 LWDLRHLLVG 436 1 LPSIVILD 0050 |123|| NQYPESNAEY 1ERYLFLNMAY ||11.50ST0FHv|YGW |13 LSETCLPNGI |.350 | 1 ETCLPNGING 0 37 FPDSLIVKGF 1.250 3 STGYVALL 125 PPNF~vA 1Jj.50n j ] LTIRLRCGY7 1012 5] 9P486 146 Each peptide is a portion of SEQ ID Star Subsequence Score specified, the length of peptide is 10 NO: 5; each start position is = ENLPLRLFTF 1 1250] amino acids, and the end position for specified, the length of peptide is 8 G FTFWRP .V50 ach peptide is the start position plu 10 amino acids, and the end nine. position for each peptide is the start 3 LPLRLFTFWR 0.0131 stt Sub uence Score position plus nine. F NLPLRLFTFW 0.010 42 GTIPHVSPER 15000 Start Subsequence 6 [ RLFTFWRGPS or VeSIVILGK 1.00 32 RCPPPCPADF F2.000 _ | GGTI 10900 23 LSLPSSWDYR 1.5001 Lt47 PLRLFTFWRG 0.0001 LVP-1G 7so [3511 PPCPADFFLY ][ 0.6-25 I 1 [FWRGPVWVAI j*0.000 ] i.1 11 ILLPISRL r 0.500 [i22| CLSLPSSWDY ||5 1 LRLFTFWRGP .0001 IVILGKIILF 0.50 __33 i CPPPCPADFF 0.250 ILFLPCISRK 11 [ LSISSGFTPF 0.150FLPCISRKLK 0.200 F8 |1 ALSLSLSSGF | 0.10 LE Ii ASLSLSSG [9j~g]16 ][ LPCISRKLKR I~~ 13 |[ LSSGFTPFSC 1 0.075 1 IVSPERV1VM 2 | GSPGLQALSL|| 0.075 98P46 7 1 VILGKIILFL 0.050 F28 ||S(DYRCPPPC ||0.050 Eah|-5 ________________ Eachpeptide is a portion of SEQ I10] SI VLGKI IL 10.050] 1 SGSPGLQALS NO: 11; each start position is 18[ CISRKLKRIK 0.020 36 PCPADFFLYF 0| specified, the length of peptide is 1 SRKLKRIKK -0.015] 16 GFTPFSCLSL i 0.025 10 amino ads, and the end E___ 12 | SLSSGFTPFS | 0.020 position r each peptide is the sta 32 I Q FLEEGIG 1 F- -E _ poitio plus nine. 39 11 GIGGt-TIPHVS .1__ 24 |SLPSSWDYRC |F| 020u Fs:LLSW 00_____ r 431 rIPH'ISPERV 0-0:10 t] [20I F__________ I [18) QTELELEFVF 1112.500 11~ KIILFLPCIS oo] 9I 1 SSSGFTPFC 0015j [201 ELELEFVFLL 4.00] 331 SQFLEEGIGG ~T 18 TPFSCLSLPS 0.01351 - 2 I fE 1 4500] 38 IEGIGGTIPH 0005 7 QALSLSLSSG | 14 FADTQTELEL 500 14 LFLPCISRKL 5 GLQALSLSLS 0.010 DTTELELEF 1.250 36 LEEGGGTIP 0.005 6 LQALSLSLSS || .07 WREFSFIQIF 10450]1 37f EEGIGGIPH 10-| SLSLSSGFTP 0.005 | 577] FSFIQIFSF 0 3 LPSVILGKI 0.003 15| SGFTPFSCLS ||0.003 |21 CSFADTQEL 44 PHVSPERV - PGLkQALSLS 0:003_|FSFD 9 .0 r-4 PGLQALSLSL 0001 31-] YRCPPPCPAD | 0.001 -4 EFSFIQIFCS 0003 17 PCISRKLKRI [AL[ RCPPPAD0.011 jEFVFLLTLLL ii 0.003 ]10 j[GKIILFLPCI 0.001T r21 SCLSLPSSWD || ql 0.001 SC271PSSWRPP 0.00 1~] f ~ REF.SFIQIFC F 0003-1 26[ IKKGWEKSF I ~] SSDYRCPP JF6-- 17[TTLL 1002 34] QFLEEGIGGT 0.0 25J.PSSWDYRCP 0.0 005 i FCSFADTQT 31-] EKSFLEEGI 0 F-6 PSSWD)YRCPP7 0.000 E:NI 971 TELELEFVFL o27] KKGWEKSQFL 000 I719I FSCLSPSSI -0 000] fl SFIQIFCSFA 0-00~1 -.- 8[ 11GKIIL-FLP I 00 I DYRCPPPPA 0000 |o 0.001 40 11 IGGTIPHVSP 0.001 29iWDYRCPPPCP || 0.000| 29 YCPPP 0000 1 LEFVFLLTLL II0.001 ~ 4i1l1 GGTIPHVSPE 10.000 TabletX-V5A-HLA-Al-10mers f 7 98P4B6 15 ADT ELLE 002571 RIKKGWEKSQ Each peptide is a portion of SEQ ID 13IJ SFADTQTELE F45-] PHVSPERVTV II 000 NO: 11; each start position is 1 21 RK(RIKKGW 0000 specified, the length of peptide is 10 TablelX-V6-HLA-Al0mors2 amino acids, and the end position for 981416 each peptide is the start position plus Each peptide is a portion of SEQ ID F3 - I WEKS 15 00 nine. NO: 13; ea ch srt position is 147 TablelX-V6-HLA-A1-10mers- Each peptide is a portion of SEQ 10 TablelX-V7C-HLAAI-10mers. 98P486 NO: 15: each start position is 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 13; each start position is amino aids, and the end position for NO: 15; each start position is spepeified, the length of peptide is 10 specified, the length of peptide is 10 each peptide is the start positionfl Pus specified, the length of peptide is 10 amino aids, and the end position for nine. amino acids, and the end position for each peptide is the start position plus Fsi~n1[ S Scor e ach peptide is the start position plus nine. 1 00 PDR 100000- nine. tarti Subseuence Score TAEAQESGIR 1 9.0 stbequence _ Score F-22 KLKRIKKGWE | 0.000 .106][ SPDRALKAAN 0.025 _________________ [Tr11 LWEFLLRLK7 F4.500 I 411DDEAQDSIDP 10.0221 TablelX-V7A-HLA-Al-10mers- [91] VTEDDEAQDS 2 F 12 ][ EVLASPAWA 00 98P4B6 RiF][ s v PA 1 1 iii IVILDLSVEV II 0.020 Each peptide Is a portion of SEQ 1D STPPPPAMWT IS. NO- 15; eaach start position is 1.0 I L[KLTPPQ 020 specified, the length of peptide is Ell KLELSKL 10 10 amino acids, and the end F1ijKEILK 0901MWNV .2 position each peptide is the start 10311 PPESPDRAU E7GIRNKS 110015 position plus nine. 17 GTS 1 Start i Subsequence | Score 143 GTLS F0.5001 5 AS P LI [61 LSETFLPNGI7 1.350. LI-43-1 VASGTMA j I 1401 ASAAWKI7 L5Y0NT Il5 11-1VAPAWK]O40 F47 K-ASTS1.1 10 I FLPNGING K 7 I LSTPPPPAMW | 0.20 1 LSVEVLASPA1 811 ETFLPNGING |I 0.1251 4 | KSLSETFLPN -1 0.075WEEAGATAE IF ()-5 82 SSQIPWGW 0.015 s SSE FLPNG 1 5 5 E0~z. LGEFLGSGTW 1 1.2 551 WSLGEFLGSG 0.015 5 iSLSETFLPNG | 0.020 1 7| GSPKSLSETF r _69711 EAQESG 1050.015020 1 [105 0.15 N 9 _- 1 1 AQDSIDPPES 0.50 F NGI1 0 0.il 7l~ STF LPNG NG If 0005 [i AQ0E SG IRNKS J10WT3 124 1HTNGVGPLWE ][0.013 7TJ SETFLPNGIN |3 0.0011 PLWEFLLRL ][ 0013 2 J[ SPKSISETFL 0| - 170 I ETIILSKLTQ f 51 GOLSEIVIPI 0.013 3 1 PKSLSETFLP I 0.000E Ij rKLETL -~~ 12811 VGPLWEFLLR IlOK~ 1- [11145 Hf SGTL SLAFTS 11 0.013 TableX-V78-HLA-A1-10mers- 3771 VLPIEWOOR 10.100 I 1851 HCMFSLISGS 0.010 98P4B6 I]I LASPAAAWKC .0 F149 SLAFTSWSLG 0010 Each peptide is a portion of SEQ ID _6L]l TEEAGATAEA GATAEAQESG ].aoo NO' 15; each start position is E1 KAANSWRNP 001 specified, the length of peptide 1621 GSGTWMKLE QSGTLSLA 0.010 amino acids, and the end position for 7 KSSSSSQIPV] 25 GANILRGGLS ][ 001 ach peptide is the start position plus 160 FLGSGTWMKL 0.050 - 159 EFLGSGTWMK 0 nine. SStarti Subsequence i Score |[ KCLG ILRG ][ fl 23 CLGANILRGG 5 I MAYQQSTLGY | 2.500 1 67 MKLETIILSK R 0.109 RALKMNSWR 110.010 10--[ STLGYVALLI 0.I25 38][ LPIEW F 0.050] 176 KLTQEQKSKH 0.010 9 i QSTLGYVALL I8 1 80 0.030 35 IEPIEWQQ .0010] 2 FLNMAYQQST || 0.010 | SS SIP W 0 175 __ _0.010 4 I NMAYQQSTLG 0.005 8311 SClPWGV [T81 AAAWKCLGAN 0.010 7]| YQQSTLGYVA | 0.003 r 1]4471 ASGTLSLAFT 30.030 11 P0.010 8 [_QSTLGYVAL || 0.003 |0.0301 M IMI 1 3 i LNMAYQQSTL | 0.003] 1-41 GTLSLAFTSW 0.025 172 IILSKLTQEQ jI 6 |AYQQSTLGYV 0.001 | 667 1 ATAEAQESGI 102 1 SLGEFLGSGT 0.010 1 LFLNMAYQQS 0.001 L15 H FTSWSLGEFL 00 120 [PVLPHThGVG 0.010 12 I NGVGPLWEF 11 .0257 147 1 TLSLAFTSWS If0.010 TableIX-V7C-HLA-AI-10mers- 9 j TEDOEAQDSI 0.025 8 GWTEDDEAQ 0.010 98P466 17 TQEQKSKHC f0.025 11531 SWSLGEFLG -.D 2N 1 WKCLGANILR sii PSLDLSV.0 i .te l TablelX-V7C-HILA-A-10mers. TableXVI-HLA.A0201.gmers. TableXi.HLA-A0201-9mers 98P4B6 98P4B6 9BP486 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide isa portion of SEQ ID NO: 15; each start position is NO. 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for amio acds, and the end position for ach peptide is the start position plus ach peptide is the start position plus ach peptide is the start position plus nine. eight. eight. [s~tr][ Subsequence ][ score] Start IfSubsequence ]jsoef Start IfSubsequence IfScore Ih141 | SQAASGTLSL [. 0072 L AAA 52.561 166 YICSNNIQA 3142 |150 | LAFTSWSLGE 0.005 TLLSLVYLA 1 43531 EVWRIEMYI i. 17][ PAAAWKCLGA ][0.005 | 43[ VLALVLPSI 1140.7921 1221 SLATFFFLY 1121 ii[IDPPESPDRA ]o 42][VLDLLQLC 1140518] F37871 sIPSVSSNA 2.937 [151[ AFTSWSLGEF 1 10.0051 11 ILIOVSNNM 34.627 1641 QWICSNNI 2.921 r117] WRNPVLPHTN 00.0053 YISFGIMSL I F42 | WOQDRKIPPL ] 403][ LLISTFHVL 0.00 396[ STLGYVALL 1j04I| PESPDRAL(A 0.003 369 GLLSLLAVT I 1434] LALVLPSIV 12411 LGANILRGGL 1003] | CLPNGINGI 1123995 [ LGLLSFFF. 2377] 119 If NPVLPHTNGV 108 LVGKILIDV 002307953 L|LAGLLA 2.365] 118 RNPVLPHTNG ||L GSGDFAKSL0.003 11021| DPPESPDRAL 110.003 25751 TPIVArfL ]12 3 MSLGLLSLL .017 15311 TPPPPAMWTE If 0.003] |FIPIDL 2T.362 267][ LSLVYLGL SLPSIVILDLS 0003 11 AMVHVAYSL 15.428 242 NQQSDFYKI 410 If VLIYGWKRA Fin5] 7] V1LRL 153 TableX-Vi-HLA-A0201-9mers- 141 1 LIVKGFNW [16224][ TFFFLYSFV 11.474 98P4B6 98P4B6 i 305J LGLFFE[234 3491 WNEEEvwRi ]J 1418 Each peptide is a portion of SEQ ID 4 1 SLTIRLIRC [ 421128][ SNAEYLASL 1 NO: 3; each start position is 4 LPI 0i specified, the length of peptide is 9 4 L F_1 61 _ _J HLLVGKILI 1.312 amino acids, and the end position for I TLGYVAIJI ][ 1 [ TLPIVAIT 1.264 each peptide is the start position plus 386 1 LNWREFSFI ][ 10.042 [303 11IQGLSFE 11 eight J -0f ELARQN [ 9.898 [ 428 TPPNFVLAL 111.2191 Start ubsequence 25 j IVN GVIGSGDFA 1|S.172 227 FLYSFVRDV .61LISTFHVU F[21611 VVVAISLAT 1.108 -~ ~ LITH 5 1 IEMYISFGI 1140] 31-4-11 MVHVAYSLC7 11.108] 402 ALLISTFHV 1492.58 IVILDLLQL 7309 LSLLAvrsi 0.985 307J| LLSFFFAMV 853.681 - IVAITLLSL 7.309 VAHREHYT 0968 30611 GLLSFFFAM 2769.74809 FTL KTNIIFVA1 01 100 i SLWDLRHLL 726.962 368 LGLLSAV UW 133 LASLFPDSL I10.9 1 333 FLNMAYQQV 479.9097 SLGLLSLLA 114.968 1 4251 RFYTPPNFV 140 i LVKGFNV |ALLGPKDA F4968 250 IPIEIVNKT 043..7840 20 I46][ FNWVSAWAL I 41 1 F49 1 LIRCGYHWV 0] 6 I 203 NLPLRLFTL 284.974REFSFIQ 4.686 LTKTNIIFV 727 210JL TWRGPWV j236685] 65][ FASEFFPHV 11131.539 435 J[ALVLPSIVI 132 YLASL i~i SFDLI lFil 1871 FIPIDLGSL 11-4.040 1 -427 I1 YTPPNFVLA r0603 I 135 1| SLFPDSLIV |105.510 1 274 JL GLLAAAYQL If 790411 374[ LAVTSIPSV 3.777 1 17171 NIQARQQVI 1.588 393 ifFQTLY 262[ VAITLLSLV If3771 29 L PIVAITLL _I J .55 48 i RLIRCGYHV 1169.552| f29 LQCRKOLGL 3.682 I 381 LPSVILDL UF5 I IMSLGLLSL || 60.325| [ NMAYQQVHA-1135881 278 MYQLYYGT I- f sifSM GSKS 7 IL] FPPWLETWL 1 521 1701NIQR V [04541 5 i S-MMGSPKSL || 57.085 | ELA S6331- YLFLNMAYQ f 209m 1 eI ALNWREFSF] 1ach Vp Vs A WALrtL of 3E1 149 ableX-V2-HLA-A0201-9mers- NO 11; each start position is C ~98P4B6spcfetelntofppiei9 - AA21mr. Each peptide is a portion of SEQ ID amino acids, and the end position 98P416 NO: 5; each start position is for each peptide is the start position Each peptide is a portion of SEQ ID specified, the length of peptide is 9 Peght. NO: 13; each start position is amino acids, and the end position [F~ IIt a 7iSusequence] Score specified, the length of peptide is 9 for each peptide Is the starl position FTFWRGPW amino acids, and the end position lus eight for each peptide is the start position ____a~ril [ubseuenc F I N f _] 9941 pplus eight. Start Su unc 9 FRPV (0141 SatISbeuneI cr 5[GLUAlSLSL |2-1362|unc L i 21.362] 5 f RLFTFWGP Start IGiIF 149.9 10 || §IL jEF 7 271 LPLRLFTFW || ILCW FL 5.392350 17 1 FTPFSCLSL 1.365 | - 2[ KIIFL ] 15 I SGFTPFSCL | 0.980 |] PLRLFTFWR 0003 4382 1 SGSPGLQAL ||0.211 ] LRLFTFWRG 1.01 3 I I|IPR 119. 14 1(01881 T FWRGPWVA 11[O.OM 14T CISRK7LI 113j 8 W LLSLSG 10.171]1 1RLR 14 SLS FTC 0.142 34 FLEEGIGT 2 3T ~ C ](WQAL ..13 5 IOLKIIL -]130 F _2 9 W D Y R C P P P C il 0 . 0 _ _ _ _ _ _ _ _ _ _ F 4 1 1 S M L K I 5-0 8 8 1 35 ]PPC-PADFFL ][ 0.098] TableX-VS-HLA.A0201-9mers- 31 IPHVSPERV f07I 221CLSLPSSWD 0.08 hp~T ir4I I I[ VLPSIVILG I .9 ~ rCAFFY ~] Each peptide is a portion of SEQ ID) 46 1 VSPERVTVM F 0.2 131 NO: 11; each start position is - SLPSSWDYR I~ ~ specified, the length of peptide is 9 25 31 LPSSWDYRC [~~] amino acids, and the end position [ 0 6 1 LQALSLSLS IF-0-0370 for each peptide is the start position 31 KSQFLEEGI r0.1177 2371 LSLPSSWDY- [- plus eight. -- 12 ILFLPCISR 1 0094 _Start]( Subsequence || Score | 113-[_ 7SG F _j| FTFWGPV | .74 2071 FSCLSLPSS I 0.005 1 20|1 LELEFVFLL (|43.025 9.9 GKIILFLPC 1001 1QALSLSLSS 0.004 6|1 FIQTSFA 7 [.07 KLKRIKKGW 6LSLSSGFTP f 1 FVFLLLLL | . 11 LEEGIGGTI 0003 2 W 003| LEFVFLLTL | 22.835 421 TIPHVSPER 1 00027 37 1 SYRCPPA 8 0003- 1 QIFCSFADT f 0 321 SQFLEEGIG 837 YRPPCA ALLLS-|-.7 12ll LSLSLSSGF T1 1[iLNiI 1.72 720I RKLKRIKKG 2111j SCLSLPSSW I0.002 I :.17 QTELELEFrV I 33I LQFEGG f00 21I ~stspj ~o 10 I1 FCSFADTQT _jI 0224 1 FL GTISP II 0.000 -2. GSPGLQALS .0.11 FSFIQIF3CS9 PSMLGKI 0.000 Z CLL5FV 2110.052T 21LSIIG 33 CPPPCPADF I 0.000 2 16 W 121 SFADTTEL 26] KKGWEKSQF F 16 PCPADFFLY ][ 0.000 1 18 11 TELELEFVF 110.052 1 --- 11 IGGTIPHVS ] .0 32 H RCPPPCPAD. AD6 fTQTEEE FI 0314 1 RIKKGWEXS 10 S LSSLEL 0 15 LPCISRKLK W 6 LQALSLS ] 003 231 PPPCPADFF 0.023 2 REFSFIQIF F0131 LFLPCISRK ]0.0 3 | IQFCSFAD LS SGTF | .4001 GGTIPHVSP 20-1 || SCLSLPS || 0.005FFLTLI-- 7 i QLSLSLSSP || 0.004 ) 3 _0W _ 311 EFLLTLL 11 0 1 WEKSQFLEE ](.00000 26 7 1 PSSWDYRCP | 0.003 EFSFIQI 0.001 hE] LGKIILFLP I 301 DYRCPPPCP 0.003 [23 K 15007 21 -|S P CSADTQSTEW 00.000 I EGIGGTIPH S 0I 21||3GSP L 00 FADTQTELE 0000 31 EKSQFEG 0.000 TabeX-V5A-HLA-A0201-9mers 5 SFIQIFCSF | .0.000 I ERV0T I0I! .00 S 98P4 9 IFCSFADTQ 0 3 EGTIP E ch is a portion of0 0 15 DTQTELELE 0 1 P S I 0.000 26 PSSWDYRCP 0..00 Ta1e-5B-L-0219es TableX-V6-HLA-A0201-9mers- TableX-VTC-A0201.9mers. TableX-V7C-AD201.Smers. 98P486 I98P4B6 J9PB 98P4B64B Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Eachpeptide is a portion of SEQ ID NO: 13; each start position is NC, 15; each start position is NO: 15; each start position Is specified, the length of peptide is9 specified, the length of peptide Is9 specified, the length of peptide is 9 amino adds, and the end position amino acids, and the end position amino acds, and the end position for each peptide is the start position for each peptide is the start position or each peptide is the start position plus eight. I plus eight. p___ __ lus eighti itat Subseq uence Il Score SItar Subsequenceu Score [ 22 | LKRIKKGWE || 0.000 14 VILDSVEV [ 246.631 _11 EVLASPAAA 0.121 251| IKKGWEKSQ 50 1148 SLAFTS 160.218 49EPLSTPPPPA .00.109 1 ||ISRKLKRIK ||0.000 1 18 ]fIRLRKJ .0 19[ PLWEFLLRL r13.8 1782 grSK I 0.097 28 |f GWEKSOFLE |0.000 31 GLSEIVLPI 1 98.381 1591 wTEEAGAtA J 0.083 19 SRKLKRIKK | [| EAGA 0.29.780 ji AAAWKCLGA 0069 2 ULLV I9.563 147~j LSLAFTSWS 0.064 TabIeX-V7A-HLA-A0201-9mers- [126I GVGPLWEFL 18564 98P4B6 f M 1 ILOLSVEVL J6.712 35]IVLPIEWQQ 0062 Each peptide is a portion of SEQ ID 1521 TSWStGEFL 1 3.119 29 j RGGLSEIVL 0.057 NO: 15; each start position is 27 ILRGGLSEI 3.100 113 ANSWRNPVL 0057 specified, the length of peptide is 9 amino acids, and the end position 42 1 QQDRKIPPL 1.993 20 WKCLGAJIL 0056 for each peptide is the start position 168 LETIILSKL ]I 124 [so][ LSIPPPPAM D.055 plus eight.F125-O02 _________ 11711 VGPLWEFLL 1 .375 FTg] KLTQEQKSK r02 Start Subsequence || Score 11621 SGTWMKLET 0.049 F9 ||FLPNGINGl |110.379 l6 GTMLI L J LPNI 11.39 [ F851 SSQIPWVGV Jr1.044 [61LDLSV LA J___ [41| SLSETFLPN |F 0.581 F][ WMKLETIIL 1.018 VLPIEWQQD 0.043 6 || SETFLPNG 0.203 112 AANSWRNPV 0.966 3 KSLSETFLP 0.007 SQIPWG 0.864 TQEQKSKC 0032 2 LKLSETFL ||0.004 2]J~ : [KLEF El~~ 134] LLRLLKSQA 10.642 [h1 PRLA [03 5 ||LSETFLPNG |n 0005 7 Li8 LSTFLPNIG JroO441~J SOTISLAFT- ] 0.615 [1711r IILSKLTQE 10030 8 ]j TFLPNGING || 0.000 T 1FL JJS 0.3 iJrWQRIP 021 7 |ETFLPNGIN M 113.000LRSQ [2 1EFPNI f0.000 39 1[ IEWQQDRK 105721 [91 SVEVLASPA I5 1_ SPKSLSETF | 00.000.514 1821 SKHCMFSL1 10.028 U19!] PVLPHTNGV I0.495 1721 ILSKLTQEQ 0.025I TableX-V7B-HLA-A0201.9mers. 98P4B6 -8I Each peptide is a portion of SEQ ID F fSSOlPw 0.454 1 NO- 15; each start position is 79 ___________ .0 specified, the length of peptide is9 83 QIPWGVVT 0420 76 NKSSSSSQI 0014 amino acids, and the end position 1601 LGSGTWMKL 0L DLSVEVLAS 0.0_13__ or each peptide is the start position F 5 I5 SLGEFLGSG:1 0.347 LAFTSWSLG 0.011 plus eight. -S[ Srt II rlEfl QAASGT__ 0.297_ 0.0_1_1 Sart || Subsequence || Score 136I RLLKSOMS 0,276 [104[ ESPORALKA 0010 6 .| YQOSTLGYV ||53.345 [31| NMAYQQSTL 1i15.428 1 P 06 [ T0EG 009 ___ STGYVLL f 225I J ASPAAAWKC 1 02 43 fl[1251 NGVGPLWEF I 08 9 || STLGYVALL |- SPAAAWKCL [69I ETIILSKLT 2.5 I || FLNMAYQQS 70514 F--1LIYQS .0 181) KSKHCMF St.L 0.228 ] 167 1f KLETIIILSK If0.008 2 || LNMAYQQST I|_0_306 1 88][ GWTEDDEA r0213] 261 NILRGGLSEjoO8 F8-1 QSTLGYVAL ||0.209 E a][ ~ ~ ~ - OS1YA jj029 ) LGANILIRG 0.1i71 [140 IISQAASGTLS 008 r ]J QQSLGYVAL 0.207 __4 ____ U11] VEVLASPM J 0.164 [6111 EEAGATAEA[' ] SMAYO-STLG 006 S [AYQQSTLGY 0 00 14 2][ MS SLA Jr0.159 -7J TQEQKSKH 0f .oo07 -I _______ - E[TLSLAFTSW 1 0.42 4GI KIPPLSTPP 10.007 TLAS-PAAW 01F120 VLPHTNGVG 15s TableX-V7C-A0201-9mers. TableXl-VI-HLA.A0201.lomers. 98P486 I 98P4B6 I8P4BI Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide Is 10 amino adds, and the end position amino acids, and the end position for amino acids, and the end posibon for for each peptide is the start position each peptide is the start position plus ach peptide is the start position plus plus eight. nine, nine. [ S ub uen e 7e Start 1S qence IFScore Start 11 Subsequence Score [166 I MKLETjILSjjjHj0. ] . 266 1 LLSLVYLAGL | L83.527 MKLE7L K.LPIVAIT .30.8420 156 || LGEFLGSGT 1| 0.005 403 1 WSTFHVI 3 231 11 FVRDVIHPYA 3 158] EFLGSGTWM IF0.00 l 402 1 ALLISTFHVL j161T573] 314 FMVHVAYSLCL 17 [13111 WEFLLRLLK | 0.005 365 1 IMSLGLLSLL :]60.325] 3031 KQLGLLSFF 3. [101| DPPESPDRA [401 SLIVKGFNW.T05i 221 SLATFFFLYS Jf2959 I [89 1 VVTEDDEAQ 02581 TLPIVAITLL 49.134 1441 KGFNVVSAWA 231-0 [1371 LLKSQAASG || 11 1LAIVtPSIV _I48.478 28611 TKYRRFP.PWL004 1351j LRLLKSQAA 48 ] RLIRCGYHVV 147 i1 N.0SAWAL0L4| 110811 RALKAANSW IF 0.004 ] 37011 LLSLLAVsi l146792] 19911 REIENLPLRL 11703 -1s LRGG55If 10.003 2101 TLWRGPWVA 1 8 441 1 IVIWLLLC I1.700 110911 ALKANSWR 0.0032 AITLLSLVYL1137.157 1 389 U REFSFISTL 13 18 | AAWKCLGAN |[0.003] 43211 FWALVLPSI 1 2261 FFLYSFVRDV [437] 91 1 TEDDEAQDS IF 002 40111 VALLISTFHV 0.03502422 | GIKDARKVTV 1164]11 TWMKLETII H 0.002 | 07I R1FTLWRGPV 33.455 1 IEN.PLRLFT 13 3 I IVILDLSVE |1 0.002 2 FLYSFVRDVl 1 8 393 1 FIQSTLGYVA 12_88] 65 ATAEAQESG If 0.02 1 221 ATFFLYSFV F947 64 KFASEFFPHV0.0022| 65jFSFFPH 1128.385 1 i1 WALQILGPKDA 11.174 F3_61 G1MSLGLS 124.997 1 345 IENSWEV I1.12! 261 1IVAITLLSLV 1-~I 299 1 LOORKOGI 1,01-1 435 II ALVIL 1014 1 16311 RQWICSNNI 111.058 TableXI-V1-HLA-A0201-10mers. PNF 110 98P486 F179 I IELAR 16.141 1 2641 ITILSVLA 0.998 Each peptide is a portion of SEQ ID YTPPNFLAL 111.9291 [0.975I NO: 3; each start position is_____ __ ______ 0.972 specified, the length of peptide is 10 S FLIWV l18.846 [.966 amino acids, and the end position for 1 43] KSLTIRURC7 0 each peptide is the start position plus 3 1 LGLLSFFFAM 1 323 11 LPMRRSERYL 0.965 nine. - 172 IQARQQVIEL 8469 F4[274[ YRFYTPPNFVJI0.904 [Start] Subsequence IScjr] 249 KIPIE VSNcKTore 82 I 1 IGSGDFASL 01 100 DLRHLLV [366.85 183 L RQLNFIPIDL 03SLGL 7I 0877 F-' oF ~ -- 1 95~ REHYTSLWDL 11.614] SMSKSL. I0.877 306 I SFFii1 [440 SIVILDLLQL GL 6.56 IFFFAM MVAYQVHANI r. 7 82 1 LXNIF 8731 1 209 FTLWRGPV I F 3-9 [W] DSUVGV r 0_31_ 82 ALINIIF 8[833 LSFFFAMVHV1-6- 11 E0 304][ QLGLLSFFFA |301.110 [51 VIGSRNPKFA F387 r L06T _37_3 || LLAVTSIPSV 0271.948| E 271.9481 419 FEEEYYRFYT 5.579 F I-7 ASIFPDSLIVI 0.689 1107 394 IQSTLGYVA 5 121 [ RINQYLVKND 0271 132 | YLASLFPDSL 182973| I 1 LVYLAGLLAA [5.439 1 EIVNKTLPIV [ 0.676 219 AISLATFFFL 178032 D ] AMVHVAYSLC 0[5I382 98][ YTSLW r 0.__28 367 SLGLSIVJ I59 70) 385 If__tLLAVFl1 3 1312 11 FAMVHVAYSL 1[ 5.050 19] IGYVALLIsT :16091 385 ALNWIREFSI1 109.2 0 LYALA 14985]1_jTLP .8 298 I WLQCRKQLGL [98.267| I[ H 4.96 3 1 [TLGINGI 0 ___ VLPSIVLDL H83.527 9 fAHEYS 4636i TGVLI 056 1 1231QQSDFYKIPI 14.337 1361REMYISFGI 0.3j 152 TableXl-V1-HLA-A0201-10mers- TableYJ-V2-HLA.A0201 -l0mers1 TableXi.V5B.HLA.A0201-lomers 98P4B6 98P416 98P488 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Eac peptide is a portion of SEQ ID NO: 3; each start position is NO, 5; each start position is NO: 11; each start position is specified, the length of peptide is 10 Specified, the length of peptideis specified, the length of peptide is amino acids, and the end position for 10 amino acids, and the end 10 amino acids, and the end each peptide is the start position plus position for each peptide is the start position for each peptide is the start nine. position plus nin position plus nine. [Start Sub ence Score S [Start Subsequence S 202 ENLPLRLFTL 0.516 36 PCPADFFLYF 0.000 20 ELELEFVFLL 5.198 99(| TSLWDLRHLL 0.516 WDYRCPPPCP 0. 1 2.440 273 || AGLLAAAYQL || 0.516 28 SWDYRCPPPC 0.000 3 REFSFIQIFC 1.966 332 || LFLNMAYQQV | 0.456 r-w [ PPCPADFFLY 1 0.000 22 ELEFVFLLTL 0896 25~ LPSSWDYRCP 00014 IfFADTQTELEL]054 31 ][YRCPPPCPAD If00012 JCSFATQTEL 110.516 ' 30] DYRCPPPCPA If .000 6 fSFIQIFCSFA 0.7 TableXI-V2-HLA-A0201-l0mers 1000 7 FQFCSFAD 0.055 98P416 j 6_]l PSSWDYRCP 5 FSFIQIFCSF Each pepbde is a portion of SEQ ID 9 QIFCSFADTQ 0 014 NO: 5; each start position is 1 FCSFADTQT 0009 specified, the length of peptide is 2 [ EFVFLLTLLL 0001 10 amino acids, and the end TableXl.V5AHLA-A201.- mer 1 - ________ position for each peptide is the start 98P4B6 ___posiflon plus nine. Each peptide is a portion of SEQ ID 1i. I FCSFADTQTE ] .0 Start IfSubsequence Sc[re NO: 11; each start position is 18[ QTELELEFVF If0.000 24 IfSLPSSWDYRC 4.W~j specified, the length of peptide is 10 16] OT 1 OTELELEF 0.000I 12 SLSSGFTPFS _ .557 amino acids, and the end position for [157 EFSFIQIFCS -00o00J 22~ ___________ ef~ 1 ach peptide is' the start position plus 15ii ADTQTELELE 0.000__ __13__ LSSGFTPFSC 0.320 SAT EL 0.01 L14 SS L V0.266 RLFTFWRGPV 91 L F 0.2196.741 SGLALSLSLS 0.171NLPRLFTFW 10.77 TableX-V6.HLAA02010mers 2 GSPGLQALSL ][0139 L i 3_11_________0.07_1_____4B 3 4 PPPCPADFFL I 0 0.0341 Each peptide is a portion of SEQ 1D L 10 I 'S SL G 0 3 NO: 13; each start position is 10 SSLSGFP I .081 9 TFWVRGPWVA If0.027 specified, the length of peptidle is [ S5 ENLPLRF 10 amino acids, and the end | 1 GFTPFSCLSL | 0.006 PLRLFTFWRG 0 position for each peptide is the sta [..1611 LCALSLSLSS L 0.0113 10I FW-VRGPWVAI -00-! position plus n. 4I PGLALSLSL 110.0111 5-- 1r -RF G 10 Str Sbeqec Score 7 FQALSLSLSSG 0.009 7 VILGKIILFL 337191 15i. SGFTPFSCLS M~007 Twx.s.HAA~Iimr~ Iif TIPHVSPERV I .8 I LSLSSGFTPF 9860.002 3, SPGLQALSLS 1.001 27 S1 C 00Each peptide is a portion of SEQ IDS 23If LSLPSSWDYR If 0.003 j NO: 11; each start position is 27 KKGWEKSQFL 0.571 ..20... I FSCLSLPSSW II 0.002 I specified, the length of peptide is 8 ILGKIILFLP 0.338 17 FTPFSCLSLP 0.002 10 amino acids, and the end 13 ILFLPCISRK 0.216 position for each peptide is the start 1 KIILFLPCI 0.127 21~ SCLSLPSSWD position plus nine. Subs VLPSIVILG 0.094 1-8 L TPFSLSLPS 0.2 S WDYRPPP l|--b- 0.000-r-Sor 33 [ 0,00117 TQTELELEFV 179.213 380.35|PC DFY|0078. 31 SPGLQALSLS 00 19 V T2EFVFL L W || 0.0 FLPCISRKLK00___ 3 RCPPC0 211 LELEFVFLLT | P 7.100 0 KGWE if SGSPGLQALS lag]1 E I2 6 VLPSIVILGK | 0.058 | 153 TableXl-V6-HLA-A0201-10mers- TableXI-VA-HLA.A0201.10mers- TableXi*V7C-HLA-A201-l0mers 98P4B6 98P46I 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 13; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 10 amino acids, and the end 10 amino acids, and the end amino acids, and the end position for position for each peptide is the start position for each peptide is the start ach peptide is the start position plus position plus nine. position us nine, nine. Start|| Subsequence | Score I start [euence Stret Subsequence Score I LPSIVILGKI 0.035 | SETF NG 2.670 5. \nVILSVEVL 35.002 33 i SQFLEEGIGG if 0.028 1 9 11006 |6j SLGEFLGSGT 30553 F6 | IVILGKIlLF || 0.025 M SPKSLSETFL7F 027 27 NILRGGLSEI 12.208 34 || QFLEEGGGT || 0.023 1 E N 0 168 KLETIILSKL 11.006 114 H LFLPCISRKL I 0.019 |] LSETFNG 07 GVGPLWEFLL104 11|| KllFLPCIS | 0.015 10 FLPNGINGIK 0IVILDLSVEV 1.3461 46| HVSPERVTVM || 81 ETFLPNGING EFLLRLL 1.0314 121| IILFLPCISR || 0.013 1 1 GSPKSLSETF 0 o14871 LSLAFTSWSL L6.57i | 44 || .IPHVSPERVT || 0.007 | SETFLPNGIN I0 58 0 AMWTEAGAT 5.807 39 I GIGGTIPHVS 0.4 PKSLSETFLP || ooo0j 129 GPLWEFLLRL F9]| LGKIILFLPC 0.004 211 FTSWSLGEFL 11678 | 17 I PCISRKLKRI 0.003 | TableX BHLA-A02011mes 112 KAANSWRNPV 221 KLKRIKKGWE I 0.001 98P486 ILDLSEVLA 3378 I45 | PHVSPERVTV Each peptide isa portion of SEQ ID 1GTLSL 12.166 | 30 || WEKSQFLEEG j 0.0011 NO: 15 each start position is specified, the length of peptide is 118l ELSTM] 6 4|11 PSMLGKII 10.001 10 amino acids, and the end 28 ILRG 1.805 31 | EKSQFLEEGI 0 position for each peptide is the start 78 KSSSSS1 | 21 11 RKLKRIKKGW | position plus nine. 147 TLSLAFTSWS 557 141 | GGTIPHVSPE O 0.000 Sue c] 19 MWKCLGANI 03 F42 | GTIPHVSPER F Q481 )1 SqSQIPWGV || .00 | 18 -CISRKLKRIK ||0.000 | jQj GVAL 3. 11411 LASPAAAWKC 0880 |401 IGGTIPHVSP I0 F 7][ YQQSTLGYVA 0.950 F-13571 LLRLLKS.0AA |0.642 E 6i PUISKLKR | 0.000LNMAYQ 126 NGVGPLWEFL 639 |37 1 EEGIGGTIPH || 10 I STLGYVAL0.0053601 ASGTLST 1 0.61 S32I KSQFLEEGIG I 0.000 | 9 OSILGYVALL 0 ATAEAQESGI ]F 0594 1 |25 J RIKKGWEKSQ | 0.000 4 NMAYOOSTLG 0.05431 GGLSEIVLP 0 24 KRIKKGWEKS 0.00 |Y[ STLGYV 16 52 Si r p F5RJ 23| LKRIKKGWEK I0.000 5 MAYQSTIGY][ooooj .][ G1WMKLET 10 36 LEEGIGGTIP I 0000][m 1 177[ LTQE(KSKHC I041 19 ISRKLKRIKK 0.000 119 NPVLPHTNGV][ 0.454 |26 i IKKGWEKSQF I 0.000 |138 LLKSQAASGT 0443 | SRKLKRIKKG I 0.000 [ c GWEKSQFLEE Each peptide is a portion of SEQ ID 7 ][ OKSKHCMFSL71 0396 NO: 15; each start position is 83 SQIPWGVVT IF 0.310 1 A-HLA-A0201me specified, the length of peptide is 10 137 RLU(SASG 0276 91P406 amino acids, and the end position for acis KLTEQKSKH I poionfreach peptide is the start psto l Each peptide is a portion of SEQ ID aine LET1ILSKLT IF 0246] NO: 15; each start position is in specified, the length of peptide is Start Subs;uence oW 0 10 amino acids, and the endA601 LSVEVLASPA 0.226 sition for each peptide is the start 42 WQQDRKIPPL 11 If VEVLASPAAA position plus nine. __________84.55______ I 0.163 1 Start S ||ubs SuenLe FLP | 12 142 SPSSTAASGTLSLALSE 1 1 GS 5LSi | .0 TableXI-V7C-HLA-A0201-10mers ableX V7C.HLA.AO201-10mers. I TableXI-VI-HLA-A3-mers. 98P486 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Ecpeptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 3; each start position is specfied, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide isg amino acids, and the end position for amio acids, and he end position for amino acids, and the end position ach peptide is the start position plus ach peptide is the start position plus for each peptide is the start position nine. nine. pluseight rSt-iart Subsequence Str ]js ec Score I .. ta'! I1 Subsequence Score]-i]~~uneI 131 HVIASPAWK10.13 1 19 RAU<AANSWR1 004]1 10011 SLWDLRHU. 3.000 11491 SLAFTSWSLG 0.2] 97J AQDSIDPPES 10-0031 F2iLII GING3IKDAR f2.700 I 1I1 | AANSWRNPVL ]A ] QQDRKIPPLS 0.003 .14032 1 50 || PLSTPPPPAM |0.109 [145 SGTLSLAFTS 0.0033 265 TLLSLVYLA 2-700 163 | SGTWMKLETI || 0.077 [49[ PPLSTPPPPA 0.003 [43-1 AVuPSIVI 2.700 1122]| LPHTNGVGPL 1l0i07 8 DLSVEVLASP .0 |203 NLPLFI 2.700 1 32 | |1 GLSEIVLPIE_ 0058 [7 RNKSSSSSQI 0.002 [205j PLRLFTLW ][ 2400 I132I WEFLLRLS 00574 PESPDRALKA 0.002 [311 82][1 SSQIPWVGW I05] 291 LRGGLSEIVL If 0.002 j [258 If TLPIAT 1T00 162 || GSGTWMKLET 0.0493 SIVILDLSVE 00 [ QNFIPID 1800] 23 || CLGANILRGG 12 EVLAS 0.0020 339741 TLGYVA 1 178]| TQEQKSKHCM | 0.032 34 SEIVLPIEWQ 0365]1 IMSLGLLSL 24]| LGANILRGGL I 0.031 140 KSQAAS rLS [0.002 11 730 LLSFFFAMV 1.800 _10 I SVEVLASPAAJ 0028 87] NIIFVAIHR [i8[ VGVVTED[JEA[ 0.027 1 TableXIl-Vi-HLAA3.9mers- 110-61! HLLVGKILI I(1.0 F | VLPIEWQQDR 98P4B6||0. 121 I VLPHTNGVGP | 0.025 Each peptide is a portion of SEQ ID t91 DLGSLSSAR 1-200 [i 1 ]- T SLEG][ (:531 NO: 3; each start position is 11 F153 || TSWSLGEFLG |27 0.023PW 111specified, the length of pepide is ~ .] TWGW 1 .0 105 || ESPDRALKAA] amino acids, and the end position |4 .2IVKGFNV r 166 1 WMKLETilLS] 0.020 for each peptide is the start position CLPNGINGI] 0.900 110 | ALKAANSWRN [ 0.020] p|us eight. 231 FVRDVIHPY 0.900 182 || KSKHCMFSLI 0Start Subseuence S.06 [ RLIRCGYHV 0.900 22 | KCLGANILRG | 0.014SLATFFFLY 108.0001 0 ALLISTFHV 36 || IVLPIEWQQD 0.014227 FLYSFVRDV F | 1 IILSKLTQEQ 0.013] WLEWLQCR 417 RAFEEEYYR 173 || ILSKLTQEQK 0.02 J IQLYYGTYR ]1003 ATLLSWV 0 2 IfLPSIVILDLSV L10 J 249 KIPIEIVNK 5 SMMGSPKSL f 15-5 WSLGEFLGSG r7~5] 1031I DLRHLLVGK If9.000 I [6 iGLLA~I .7 [115I NSWRNPVLPH I0.009] 27411 GLLAAAYQL ][8.100 396 IfSTLGY VAILL 0. 608 90 VVTEDDEAQD || 93 ILDLLQLCR[ -102 || DPPESPDRAL_ 0.009 | [3 ATFFFLYSF 6.750 125 || TNGVGPLWEF 3i 0.008 [6.000] 1 381 1 S4NLNWR ]j 0.600I 146 I GTLSLAFTSW I| 0.007 |LGPKDASR 6.000 46 j TIRURCGY " 0.600 47 1| KIPPLSTPPP || 038.50 |f E 6219 AISLATFFF ]l6-6I 139 | LKSQAASGTL ||0.007 [ VIGSGDFA 6.000 2 1 YQLYYGTKY 0.540 61 It TEEAGATAEA | 0.006 | HVLIYGWKR 5 101[|| IDPPESPDRA .006IGSRNPK 45002 F577i PAMWTFEEAGA ||1-1 0.006YS |7 LGLA .5 ~~~~~~ 13 3jVYFII ~112][ ILIDVSNNM 71 __ 59_I| MWTEEAGATA .82 ALTKTNIIF || 400] KTNIIFVAI 0.405 171| TIllSKLTQE -[55- 322 ClPMRRSER 11.00 1 FVAIHREY7 0.005_ 84][ QIPWGWTE || 0.05 |i 367][ SGLSILA ] 165[ TWMKLETIIL 11.0 Q5 1 '135 1 iiFPD] 11V _LDVSNNMR I 040 155 TableXIl-VI-HLA-A3-9mers- NO: 5; each start position is Sence Score 98P4B6 specified, the length of peptide is 9 - NLPLRLFTF 9.000 Each peptide is a portion of SEQ ID amino acids, and the end p 3 PLRLF-FWR 3.600 NO: 3; each stt sion i for each peptide is the start position specified, the length of peptide is 9 plus eight F7 FTFWRGPW 1 0.050 amino acids, and the end position Start Subsequence So 5 RLFTFWRGP 0.03D for each peptide is the start position 12 [ SF-J-pJ 0 2 LPLRLFTFW 0.009 plus eight. 2 II T.] 9 FWRGPWVA 0.001 Strt Subsequence || Score | 308 TFWRGPV Jt 0.01 148| WSAWALQL || CPADFFLYF LL 11. LRLFTFWRG 175| ROQVIELAR 23f -LPSSWY 0.135 LFTFWRGPV iffi o [217| VVAISLATF 0.300 | 17 FTPFSSL 0.060 [1641 OVYICSNNI 36 PCPADFFLY 0.036 Table0.I3-0-0-9mers [400 | YVALUSTF 0.300 8 ALSLSLSSG 0.030 98P4B6 143)| KSLTIRLIR |F 0.270] Each peptide Is a portion of SEQ 0 441 I IVILDLLQL || 0.270 |F 0.030 NO: 11; each start position is -268 11 -SLLSFAG00 specified, the length of peptide is 11 f 1SLVYLAG0L...2770 CPPPCPAOF 1f 0.0301 amidno acids, and the end position 180 I25 LPSSWDYRC 1 0.018 reach peptide is the start position 3_53i| EVWRIEMYI 1 0.270 jT 1f LSL GF 0 pluseigh _ 358 EMYISFGIM |0.270 SGFTPFSCL I 0.013 Start t Subsequence ISor [276 1 LAAAYQLYY |F 0.240 [3f| SPGL 0.012 [24][ FVFLLTLLL J[6] 46 LVLP5IVIL | .0 [~~][ _VPM I0.203 14 19 HPCAF f .0 I ELELEFVFL If0.540] [3351| NMAYQQVHA 10.200] 14 SSGFTPFSC N 0003 [21]1 ELEFVFLLT 157 | VIGSRNPKF 0 21f SCLSLPSSW 0 .2003 | 269[ LVYLAGLLA | 0.200f C F 1 00371 QIFCSFADT IF0..1250 333I FLNMAYQQV 1 0.2o0 [ LQAS S 02 REFSFIQlFo135 1261 IVAITLLSL | 0.180 FT~- ffTPSLSLP 0.002 F2. ]j LELEFVFLL ][ *--j579 1225| FFFLYSFVR I I.180 |71 SSWDYRCPP 10 122][ LEFVFLLTL 360 [ YISFGIMSL IF 0.180 F SGSPGLQAL U0.001 161 FQIFCSFA ]['-0-60 1437 I[ VLPSMLD I 0.180 | QALSLSLSS 0.1 1 1 TELELEFVF 1404| LISTFHVLI | 0.180 [DYRCpppC 1-ooii 1 lT 1[ QTELELEFV 1242| NQQSDFYKI 1 F137[ LSSGFTPFS 0.1 62iF SFIQIFCSF (257 I KTLPIVAIT jF 0.152 2 GSPGLQALS F 0.00 FSFIQIFCS ][ 0005 SYLFLNIAYQ F 5 GFTPFSCLS 0.001 WREFSFIQI 11 |0.15 410 | VLIYGWKRA || 0.150 |F 1 ___. i34.f1 LSLSSGFTP I ooo 14 ADTQTELEL || GGG A 188| LPNGINGIK || 0.135 | [i][LPGIGK t .1532 IfRCPPPCPAD 0.00 F-5]10 FCSFADTQT ][0.001 _107|1 LLVGKILID | h .13520 F 1 2411 RNQQSDFYK I 0.120 |01_ 14051 ISTFHVLY 0.120 132 YLASLFPDS 0.1PGL2ALSLS f - 51 DTQTELELEIf .ooo] [I I _______it0.2030 1DYRCPPPCP 0.00 Fo 23' EFVFLLTLL I 000 4281 TPPNFVLAL | 0.108 [ I S j O 13 FADTQTELE I0000 1153| ALOLGPKDA I 0.100 |6 PSS YRCP 108| LVGKILIDV |0.090 |] IFCSADT] 378 ISIPSVSNAL t 0.090 F141 | LIVKGFNVV . .090 TaeIl-V2-HLA-A3-9mers--mers IflLIVIGFNVVq: 0.090ti i aprto of SEQ ID 1TabteXJIl-V64LA-A3-9mers.j ____________NO: S1; each start position is 98P4B6 TableX]i-V2-HLAA3-9mers. specified, the length of peptide Is 9 Each peptide is a portion of SEQ ID 98P4B6 ~~~~amino acids, and the end position N:1;ec tr oiini ~ach peptide isa portion of SEQ~] or each peptide is the start position s the length of peptide is 9 plus eight amino acids, and the n bo n 156 for each peptide is the start position ableXII-V7C-HLA-A39mers. plus eight. 9SP486 Start | Subsequence abeXIV7A-|LA|A3.mers. Each peptide is a portion of SEQ I 1 12 || ILFLPCISR 60.000 984 NO: 15; each start position is _ || ILGKIILFL I 2.700 | Start [Ibsence specified, the length or peptide is 9 S VILGKILF Each peptide isa pon of SEQ ID amino acids, and the end position E-LE VLGKIL IF-3-07NO: 15; each start poW is for each peptide is the start position 10 I KILFLPCI 1.215 lengthofpeptdeis 2 || LPSIVILGK I0900 amino ads, and the end position Start Subsence Score 42 ! TIPHVSPER |for each peptide is the start position 1 ALKAANSWR 1 4.0 21 || KLKRIKKGW h 0.4500 [ 2 1KKRIKKGW II 0.4701 F 9E1FLPNGINGI 148 j1 SLAFTSWSL 11 1800 SKRIKKGWEK 0. ILDLSVEVL 1800 __5 _ VILGKIlL__ - _ SP 27[ LRGSEI -I. -1 1LP~tVILG Jr 0.180 165 WMKLETIIL II _38 GIGGTIPHV j[0.135 [128 GPLWE F I -1s LPCISRKLK ] I 0~|1 K 5[ AMWTEEAGA 11.000 14 I FLPCISRKL || 0.090 | 163 13 |LFLPCISRK ||1 S L -1 1.0 i StAFTSW 0.0.600 2!.. I ________ 181 TFLPNGING I0.000 I ~LJLK1 .0 34 I FLEEGIGGT | 0.068 23 PSETLR(0 17j' CISRKLKRI || 0.045 | 217[ N 4 i SIVILGKIl TableXlI.WB-HLA-A3-9mers- 1 CLASGS If 0.300 19 | SRKLKRIKK | 0.040 98P46 1___. 45 iHVSPERVTV ||0.030| 451 HVSPERVTV If 0030] Each peptideisa portion of SEQ ID ii1LSPMK 100] 41 1 GTIPHVSPE || 0.020 NO: 15; each start position is PIEWQQDR107 2.0KGWEKSQFL L0014_ specified, the length of peptide is 9 [2671 GVGPLWEFL 0.270 16E I PCISRKLKR 11 0.012 amino acds, and the end position r If PIEWQQDRK 0 18 ISRKLRI for each peptide Is the start position f-1347 IILLRLU(SQA 1 0.200] 18 ISRKLKRI _0.0101 _ ___ usegt 31 KSQFLEEGI IF 009 Sta Ssenc e F I LKLTQEQK 19-100] 26 I KKGWEKSQF || 0.0061 G EDDEA .0 1131 ||LFLPCISNMAYQSL 00 61 AQESGIRNK F-9_ E0527 r1 FLNMAY r-771 DLSVEVLAS 0072] r461 VSPERVTVM 110.005] - 7FQQSTLGyVA J[ 0 I [|ISIVILSV [.060] 24 || RIKKGWEKS || 0.004 ' . 1361 RLU<SQAAS 0 060 PERIf oo ~ 1 AYQQSTLGY ]I 0.0--___ _ _ __ 43 ||_IPHVSPERV 0.002| [8[ QSGYVAL 0.003 1 22 1 CLGANILRG 35 ILEEGIGGTI 0.001_ 6 Q 0.003 5 SLGEF 32 ISQFLEEGIG 0.001 4 MA_____Jr 155 SLGEFLGSG 29 WEKSQFLEE 0.000 181 KSKHCMFSL .041 3 PSIVILGKI 0.000 | 37 EGIGGTIPH 0.0 91PLTPP .3 I 37J[ 0.000 [ ~~TableXH-V7C-HLA-A3-9mners. 9J LTPPAJ .3 28 GWEKSQFLE 0.000 98P4B6 VILDLSVEV J 350 8 LGKIILFLP 0EachpepiideisaportionofSEotD GTLSLAFTS 0027 F33[ QFLEEGIGG 0.000 |NO: 15; each start position is 4271 QQDRKIPPL 1 GGTIPHVSP || 0.000 specfied, the length of peptide is 9 F-2371 HTNGVGPLW JI 022-1 L9amino adds, and the end position 39 IGIHSA0001 for each peptide is the start position [1 1 STPPPPAMW 0.2 ~25 JrIKKGWEKSQ Jr0.000 Iplus eig ht. [ 133 ]1 FLLRLLKSQ J 0.0221 ~30 JrEKSQFLEEG 000 [Start I Subse uencej Score 1 F357[ IVLPIEWQQ Jr .020 20 | RKLKRIKKG I 0.000 1 KLEIILSK 270.001 36][ VIPlEWOOD 0 36 EEGIGGTIP 159 0.0FLGSGTWMK 60.000 F|2 ILSKLTQEQ P 0.020 r-22 1 LKRIKKGWE 7 00001 KLTQEQ ASGTLS 0020 4-1 P ERVT JTbe11 G--L A- A39 m SVEVLASPAers 1129 11 PLWEFIIRL LL450KIfWSQAASG7 .2 157 TableXIl-V7C-HLA-A3-9mers- TableXii.V7C.HLA.A3.gmersI TableXlI-VI-HLA-A3-10-9$P46 98P4B6 I 96P4B6 Each peptide is a portion of SEQ 1 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ 15 NO: 3; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is specified, the length of peptide is9 specified, the length of peptide is 9 10 amino acids, and the end amino acids, and the end position amino acids, and the end position position for each peptide is the sta or each peptide is the start position for each peptide is the start position position plus nine. plus eight. plus eigh - rtj[ Subsequence Score Start I Subsequence iStart Sco rence[soreI *i~[ SiWDuRLLV ] 8 . I SQIPWGW 1 0.018 FS l 2 I76i1 V|Ti1E ]j 000 L17 I EQKSKHCMF 0.018 | 160 31 I 0.002] 3701I LLSLLAVTS 1 59| WTEEAGATA 1 0.015 | 15 SWRNPVLPH 0.002 3YLASLFFDSL j 1.800 83 || QIPWGVVT 3 05VLIEW ji 002 1011 QLGLLSFFFA |1.5.800] 1 152_I TSWSLGEFL 0.015 |9 SSSSQIPW Ii .3851 ALNWREFSFI 1780] 176]i LTQEOKSKH 1 0.015 |0.002 1435jf ALWPSIVIL 1.35 73I GIRNKSSSS 1-0.0121 --657[ ATAEAQESG 0303f[ KQLGLLSFFF 1.215 141| QAASGTLSL 1 0.0121 64][ GATAEAQES jj0jof 3071 LLSFFFAMVH 1200 46 | KIPPLSTPP iRGGLSEIVL 0001 VILDLLQLCR 00.200 1113 EVLASPAAA 0.009 111 WZNPVL a29811 WLQCRKQLGL 1' 200 103 PESPDRALK | 009 SQSGTLS 100 i IDPPESPDR 1 0.006 |4101 VLIYGWKRAF j 0900 112 AANSWRNPV || 001 SLIVKGFNW 1 0900 170. TilLSKLTQ I 0.006] TablYll-V1-HL-A3-1098P4B6 1 20 -- L G 0 120 VLPHTNGVG || 0.006 Each peptide is a portion of SEQ ID 25 1 TIPIVAITL 0 ~ j AEAESGI11 NO~. 3; each start position is 66specified, the length of peptide is. 2311 NQYPESNAEY 26 NILRGGLSE ]| 0.006 1 10 amino acids, and the end :278 1 AAYQLYYGTIF 9-00-1 1127 1 VGPLWEFLL II 0005 position for each peptide is the s 36 IMSLGLLSL I 24 I GANILRGGL | 0005 |itio plus nine. 142||ASGTLSLA |0.005 start Subseuence Soe1 ISATfFFLY 1 81 SSQIPWGV |35|1SLFPDSLIVK .0450.000 52 _ 0521 OLYGTKYRR 60.|| TPAM || . |.2 3L IVILDLSVE [ 0.005 3331 FLNMAYQQVH .60 171 | IILSKLTQE || r 2 I 1 24.OO0] 28 SLVYLAGLLA 0 00600 119 || PVLPHTNGV 1[|___ 2941 WLE1WLQCRK20 3241 PMRRSERYLF 1 0600 99 SIDPPESPD 10005 241 GLLAAAYLY 118.000 821 ALTKTNIIFV 1 000 168 i LETIILSKL || I 1 CLPNGINGIK 9.000 367 SLGLLSLLAV 17 | AAAWKCLGA | .|04 211 GINGIKDARK 2031 NLPLRLFTLW _0.60 67 i AEAQESGIR =3061GLLSFFFAMV R10 1661 YICSNNIQAR 10600 108 R -1 0.003 1 2711 YLAGLLAAAY 6.0000 21A|SLATFFF_ 0540J 15 SPAAAWKCL || 0.003 | 1121ILIDVSNNMR 6 14o -W 86 1 WGVVTEDD 1 0.003 |ILOLLOCRY 6. 0 147 SAWALQL I D.45 177 i TQEQKSKHC ||0.003] 227 FLYSFVRDVI 4.5(M 56 1 WIGSRNPIT ] 14 l ASPAAAWiC . 0.2100 TLWRGPVVVA 4.50 4171 RAFEEEYRF 10.4 8931 VVTEDDEAQ 0.003 i] RRSERY If 451 LTIRLIRCGY 000450] 1543i WSLGEFLGS || 1 HI GSRPK 3000 2.00 |________ 139 KSQAASGTL 0.003 402 ALLISTFHVL 2.700 1781 IELARQLNF 15731 GEFLGSGTW r 2611 SLVYLAG3 2.700 041LPRuTLWR 50 o LSTPPPPAM 1002 1 LUSTFHV [2 3581 EMYISFGIMS 10.002_j 34 i EIVLPIEWQ F 0 4371 VLPSIVI0.0 02_700 2_ J85I PW VE 10.02 4041 LSTFHLI-Y 1i 2.400] .1MVAYLL 061 8 SPGVVTED|| 0.002 4 RLIRCGYW 0300 158 TableXII-VI-HLA-A3-10-98P4BJ position pus nin TabfeXIIlV5A-HLAA3-Iomers. Each peptide is a portion of SEQ ID S Sbqn Score 9BP486 NO: 3; each start position is 22 CLSLPSSWDY 12.00 Each peptide is a portion of SEQ JD specified, the length of peptide is 8 ALSISLSSGF 2.000 NO: 11; each start position is 10 amino acids, and the end specified, the length of peptide isl1 position for each peptide is the start 24 SLPSSWDYRC 1.800 amino acids, and the end position fo ___ iin plus nine. L5 31 GLQALSLSLS] 0I .180 acli peptide is the start position plus Start] Subsequence [12 [iISLSSGFTPFS 10.120 nine.____ 317 VAYSLCLPMR 0.300_- _____I ie 317 E______________0.300 10I SLSLSSGFTP II 0.060 F:Sar_ Subsequence ][Score] 331 YLFLNMAYQQ [ 0300 35 PPCPADFFLY 0.054 8 FTFWRGPWV 0050 31311 AMVHVAYSLC 11 TPF _ 4 PCRLFTFWRG 0018 3~5 u~rsisv [ ~ I Ust-sswy~ [~~l il ENLPLRLFTF 0.012~ 373 ILLAVTSIPSV .3002 SPSWY .4 LVYLAGLLAA 0.300 33 CPPPCPADFF -0. [4]9 TFWRGPWVA 0.005 440 11 SIVILDLLQL 0.270PCPADFFLYF 0.036 22 11 LATFFFLYSF ][0.270 [32I RCPPPCPADF 003~ 7 II - FTFWRGPW II 0.00 154t41LGP KDASR ][0.270 21 GSPGLQALSL 0027 - L 0.000_____ 85Jj KTNIIFVAIH If0.270 141 SSGF-TPFSCL j .1 .356 1 RIEMYISFGI 10270] [6 GFTPFSCLSL 1005 4061 STFHVLIYGW 1_022 13 ILSSGFTPFSC If0.005 396J STLGYVAJI F.203 J TPFSCLSLPS 0.0 432 FVLAL-VLPSI 6f023 T ) LQALSLSLSS If0.002] 2171 VVAISLATFF jI0.200 [~~[PPPCPADFFLj 002 43 VLALVLPSIV 30.200 j17 ][FTPFSCLSLP 01002 [TableXIlV-V56.HLA-A3-10mers 3911 FSFIQSTLGY- J~io 20 IfFSCLSLPSSW I 0001 98P4B6 3691 GLLSLLAVTS 0180SPGLQALSLS Each peptide is a portion of SEQ i 2241 TFFFLYSFVR [0.180] 15 IfSGFTPFSCLS ][~ INO: 11; each start position is 4~9 1 LIRCGYHVVI ][0.180 J 27 jSSWDEYRCPPP 0.001 specified, the length of peptide is 103 DLHLLVKI [ 0.62 21f SCSLPSWD f ____10 amino acids, and the end 131 KIUDVSNNM 2 position for each peptide is the st .11_1__________ IF ____35 [7 I QALSLSLSG]Z .00 7_ poslton plus nine. 12491 KIPIEIVNKT 0.135 )LSLSLSSGFT 0.000 1 Start IFSub 1264 I ITLLSLVYLA ||WDYRCPPPC 0.000 1 F207 1 ELELEFVFLL 114.860 L SMMGSPKSLS 0135 PGLQALSLSL 0.000 22 ELEFVFLLTL 113 ~ _ ILIVNMI101] 29 IfWDYRCPPPCP I000 j18 ITELEvFI0.0 262 1 VAITLLSLVY 11.2] 30 IfDYRCPPPCPA 0.0 I I 5 IfFSFIQIFCSF I .2 372 suAVrslPS1012j [Tj[ SGSPGLQALs 0000O I 11I DTQTELELEF II0.060 3971 TGYVALLS D 0 T[ -YRCPPPCPAD -. 0 F9--] QIFCSFADTQ 0.030. 1571I GPKDASRQWY ME 0106~I PSSWDYRC.PI 0.000 F12-] CSFADTOTELf 0.01qj5 172 1, IQARQVE FO. 0108 5I LPSSWDYRC 0.00 8 IQIFCSFADT 310.013 2431 OQSDFYKIPI I1W hI iF[PSLLSS- .01 123 11LEFVFLLTLL 10.013 3473 NSWNEEEVWR If010]117 TQTELELEFV 10.0131 39 31GDFAKSLTIR 0.0OA90] TableYJIllV5A.HLA.A3-l0mers- 19 TELELEFVFL 31 .012I 218_1 VAISLATFFF 11 0.090 ]98P4136 [1 ATTLLI.1 384 1 NALNRFFI 0.090 Each peptide is a portion of SEQ ID [2J WREFSFIQIF ] .0 28 ~ GKYRFPWIIo~-o NO: 11: each start position is 2-5 ____________ 1100- specified, the length of peptide is 10 [T[ REFSFIQIFC I amino acids, and the end postio Io 7] LELEFVFLLT ][ 0.006 TableXIII-V'2HLAA3l0mes ach peptide is the start position plus 7] FIQIFCSFAD[ ] 9846fnine. If NWREFSFIQI0. 5 Each peptide is a portion of SEQ ID FSt1art Susqec 11S]cr SFIQIFCSFA 0.1 specified, the length of pepide is ] RLFTFW 10j~ NL.r.RFTF 0.600, [n th edII -jFCSFADTQTE 0.000 1sition for each peptide is the start [ LPLRLFTFW .4 '59 TableXIll-V5B-HLA-A3-10mers- TabfeXIIl.V6-HLA-A3.lomers- amino acids, and the end position for 98P486 98P4BG ach peptide is the start position plu Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID nine. NO: 11; each start position is NO: 13; each start position is trB Subsequence Score specified, the length of peptide is specified, the length of peptide is 10 F II MAYQQSTLGY 10.400 10 amino acids, and the end amino acids, and the end position for I W position for each peptide is the start each peptide is the tart posito plus position plus nine, nine. 0_________ 0.203 ~ cr]Subsq uen e __9 19 1 QSTLGYVALL .0 2 7~ Start i usqece || Score | sr7 ec ~oe 110 |1 IFCSFADTQT I0000]E 0.000 1411 |MAYQQSThG 0.20 1| EFSFIIFCS | 0.000 1 [37 EEGIGGTIPH ][ 0 I 7 1 YQQSTLGYVA 1 0.01 1511 ADTOTELELE] 30 WEKSOFLEEG III-9i 871 QQSTLGYVAL.T000| 13 || SFADTOTELE 10.21 21 RKLKRIKKGW 3 1 LNMAYQQSTL 0.002 - 4- j 1j PSIVILGKII 0.000 = 1~~ AYQQSTLGYV 0.000 TableXIll'V6-HLA-A3-10mers- 38 EGIGGTPHV 000000 LFLNMAYQQS 98P4B6 [ 14 LFLPCISRKL 10.000 Each peptide is a portion of SEQ ID 4 GGTIPHVSPE 0.000 TableXIll-MCHLA-A-l0mers NO- 13; each start position is _ _ _ _ _ _ specified, the length of peptide is 10 KRIKKGWEKS Ec 0000 i amnino adids, and the end position for I~ ] EKSQFLEEGI 0 0.0 NO Each each isa portion fsEQI each peptide is the start position plus -4-4][ IPHVSPE-RvT110.00! spNO:ed t5; eh tar positidn is 1 nine. [1 I amino acids, and the end position for e3T][ KSOFL II .000 ach peptide is the start position plu F-1311 n I nFLPCISR ][15-0 i][ LEEGIGGTIP ]l-05! : nine. I Star7 VLPSLGK F]45][ PHVSP||V V starij Subsequence I Score 2= ||SAAW VLP2VLG.|00.00 [ 15|| FLPCISRKLK ||10.000|i [[ IGGTIPVSP I0.u0i I I SP K 120.0001 F42 1 GTIPHVSPER ][2.025 1 20 11 SRKLXRIKKG]II000 -W- 'R 11.0001 12 |1 IILFLPCISR || 1.800 [6 |I IVILGKIILF || 0.900 TablejllVfAHLAA3-10ges 168 KLETIILSIL 14.5 F7 || VILGKIILFL || 0608] 98P4B6 127 GVGPLWEFL 0 1 35 || FLEEGIGGTI 0405 Each peptide is a portion of SEQ 160 FLGSGTWMKL 19 71 ISRKLKRIKK ||5 2 NO: 15; each start position is 100 SDPPESPDR 1 18 CISRKLKRIK 110.20 I specified, the length of peptide is i~fKTEKK .0 8 ISRVLKIL 0.0] 10 amino acids, and the end LPJEQK 0.40 SIVIGKIII - portion for each peptide is the st GTWMKLETI r045 0 -87 1 ILGKL 0.135 position plus nine. O_ IS 0 1 46 | HVSPERVTVM ]( 069] J Start I Subsequence 1 Scr 134 FLLRLLKSQA 1 61 LPCISRKLKR 0LPNGINGIK 1 90= ILDLSVEVLA 0.300 23 i LKRIKKGWEK ||o-oeof I51 SLSETFLPNG 0.135 28 ILRGGLSEIV 0.300 il| LVLPSIVILG 1 0.041 |KSLSET = 1 VILDLSVEW 0.270 1 39 i GIGGTIPHVS | 2 iSKSLSETFL 0 121 GPLWEFLLRL 0.227 43 1 TIPHVSPERV ||0.020 6 LSETFLPNGI [1671 MKLETIILSK 0.203 F-22 || KLKRIKKGWE 1ki8 ETFLPNGI.G 018 32 GISEIVIPIE 0.20 11 KILFLPCIS ||0.018 141 KSLSETFLPN 5] 135 LLRLLKSQM 0.200 1011 GKiILFLPCI | 0.012 9 1 TFLPNGINGI 10.0061 SLGEFLGSGT 33 | SQFLEEGIGG ||0.006 | SETFLPNGIN 00 5 -tI.AMWTEEAGAT 150 131| LPSIVILGKI I 0.004 1311 PSLSETFLP 0.0w 14611 GTLSLAFTSW 1 3 26 || IKKGWEKSQF |0.003 |271 NILRGGLSEI 13 251 RIKKGWEKSQ i 0.003 1 166 1 WMKLETIILS 27 || KKGWEKSQFL i 0.002 | TabeXll-V7-HLA-A3-s 147-11 TLSLAFTSWS 0120 28 || KGWEKSOFLE ||10.001 |98P466 1 LLKSQMS0 Each peptide is a portion of SEQ ID P E R8 17 PCISRKLKHR0.001 NO: 15; each start position is 13 SLLAR 06 = 1 ___________________ 70 1 specifiede, the length of peptide is 10 1 166 TableXill-V7C.HLA.A3-10mers. Tabejll.WcNI-AAM er0 TableXIV-VI-HLA-A1O1-9mers. 98P486 98P416 98P4B6 Each peptide isa portion of SEQ 1D Ea Peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15: each start position is NO: 15; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specifed, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position ach peptide is the start position plus e is the start position plus reach peptide is the start position nine. nine. plus eight Start || Subsequence || Score tart S Subsequence Score 110j ALKAANSWRN 0.678_ KSSSSSQIPV 0ub06 u2n9 ScoreNK -2 I 109 31RALKAANSWVR 1__ [i00 1](2 LPHTNGVGPL F 005 I 35 ]jVGGFK11.200 1 66j[ ATAEAQESG 0.045 3][ SID 0 I 1751 RQQV 115~. NSWRNPVLPH If04 I~~ IVLPIEWQQD 11000 1os F417 I RAFEEEYYR If- 0480 1.59EFLGSGTWMKI9.4 [23[ CLGANILRGG [0.005] F 131 SISMMGSPK 10.4001 131 if LWEFLLRLLK J[ 0.040 171 TlLSKLTQE [11oo00 279 AYQLYYGTK 0400 141 SQAASGTLSL ][i 3 I I F152 ifFTSWSLGEFL I0.030 r22 KCLGANILRG I.00 381 SVSNALNWR I .0 50 JLPLSTPPPPAM 003035 EIVLPIEWQQ INQQSDFYK 060 137 jRLLKSQA-ASG &f 030 1119 IfNPVLPHTNGV 1f 0.003] 282 IfLYYGTKYRR f0.320 4.I IVIU)LSVEV J003 [162 11GSGTWMKLET 11 0.003] 225fFFFLYSFVIR7][ 0.240 19F I AAWKCLGANI ][ 0.030 142 T Q GLSL s f 0003] [21 1 GINGIKOAR 1[ 0.240j 125 || TNGVGPLWEF || 0.027 1GPLWE 0003 F-[3] GYM WIGSR 0.240 42 1 WQQDRKIPPL 110.027 90 WTEODEAQD 0003 87 NIFVAlHR FI-82-F KSKHCMFSLI 1f0.027 172 If ILSKLTQEQ 11 0.003 1 f18 IfLPNGINGIK ][0.2-00] [31 1 GGLSEIVLPI If0.024 [181-1 ]KSHCFS 0 00037 F443 ILDLLQLCR 110.160 1281 GPWELLR110.249 J[LSVEVLSPA 11 0.02 ) [103 ][DLRHLLVGK if0.120 | I52f| STPPPPAMWT [ 0.022 51 I LSWPPPAMW F0247 GVGSGDFA 0.090 .103 I PPESPDRALK I 0.0200002 322 CLPMRRSER 10 SVEVLASPAA LPIEW I||.002] 113[ .02SN0[ 8 149i SLAFTSWSLG 02 H VTEDDEAQDS .02.002 1 [155]QLGPKDASR0.080 121[ i VLPHTNGVGP 1 0.020 TWMKLET1IL AYSLCLPMR 0.080 112 iKAANSWRNPV 0.018 [11 IfKMSWRVI 0.08 2Jf LRGGLSEIVL [0.002I [269][ LVYLAGLLA ]o00 1751 SKLTQEQKSK 1 0 FAQESGIRNKS 281 QLYYGTKYR JFO_.1__ 148i LSLAFTSWSL 0.013 [32 1[ WEFLLRLLKS ]00021 j9J WETWLQCR If 0.080 12~ EVASPA AAV If0.1343j Q1QDRKIPPLS 1 0.002 1 97J H SLWLR If-00801 8IfDLSVEVLASP f0.013 92 ][ TEDDEAQDSI 31 0.002 1295 If1WLCK .6 1 69 1 EAQESGIRNK 7 0.013[ SSSSSQPW _0 0002] 441 I ViLDILL If 0 | 74 || GIRNKSSSSS I 0.012 60 .054 1 67 1 TAEAQESGIR If 0.012 153 EFLG I 0.002 199 REIENLPLR 83 __LSQPWGWT _ 0010 15 I ASPAAAwKCL f F-22 INGIKDARK ' 89 IGVVrEDDEAQlr[ 0.009 FI1481 IWSAWALQL I 01)40] 47 || KIPPLSTPPP || 0.009 |0040 |14 || LASPAAAWKC || 0.009 9BP4B6 I 10871 LVGKILIV 04 158 IGEFLGSGTWM If 0.009 Each peptide is a portion of SEQ ID [-22371 A F 040 21 WKCLGANILR [0.8N:0 3; each start position is specified, the length of peptide is 9 1 261 IVATLLSL 177ZL I ____________ If 0.007 amino acids, and the end position r 1677 ICSNNIQAR I.040 179 1f QEQKSKHCNIF][ 0.f06 or each peptde is the start position 164 lu QVYICSNNI 1 0040J [i.iI MSWNVL[0.006 plu 43h -- I KSLTIRLIR If 0.036 FI8-4IF QPVVGVVTE FS 0.006Subsequence_ I2 RDSHPYAR 178 -1 TQEOKSKHCM [56 48GR K 3.00 RLRCGYHV IF036 .LAFTSWSLGE 0.006 409 R 1.200 161 TableXIV-V1-HLA-A1101-9mers- TableXIV-VI.HLA.A1101.9mers- TabeXlV-V2-HLA.AI lI-Smers. 98P4B6 98P486 98P486 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ 1D Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 3; each start position is NO: 5; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino adds, and the end position amino acids, and the end position or each peptide is the start position for each peptide is the start position or each peptide is the start position plus eight. plus eight. plus eight. Start Subsequence T Score Start Subsequence [ScrS ubsequenceI Score 330 RYLFLNMAY L0F03LY 0.012 1 LJFC I 0000 408i FHVLIYGWK 1030 427 jIYTPPNFVI.A If0.010 125 ILSWYCjooo 851| KTNIIFVA ||0.030 285 GTKYRRFPP ][ 0] LSLSLSSGF I OoO 436 I LVLPSIVIL 280 YQLYYGTKY |F 0.093 1 SGSPGLQAL |.30.000 303 I KQLGLLSFF || 0.027 397 TGYVALLI 0.008 31 IYRCPPPCPA 0.000 353 || EVWRIEMYI || 0.024 7 SLGLLSLLA 34 1 PPPCPADFF 0f000 191 I DLGSLSSAR jj_0.024 166 YICSNNIQA 0.008 30 1 DYRCPPPCP .00 254 iV .IVNKTLPIV 0.020 | 258 I TLPIVA 00 liiLSLSSGFTP 0.00 90 AFHREHYI 0.020 317 VAYSLCLPM 0.008 1471 SSGFTPFSC 0000 151 AWALQLGPK | |100 SLWDLRHLL II .008 211 GSPGLQALS[ 8 LYIiiFV 00210 TLWRGPVVV 0.008 19 PFSCLSLPS 00 98 | YTSLWDLRH | 0.020 IMSLGLLSL H 0.008 2971 WDYRCPPPCI0.000 231 |1 FVRDVIHPY | 0.02063 ATi±SLW f[..08 7 1 SSWDYRCPP 110.000 r400| YVALLISTF [ 0.020 | YISFGIMSL I1371 LSSGFTPFs F -0.00 217 1 VVAISLATF | 0.020 20[ FSCLSLPSS 402 1 ALLISTFHV 0 TableXIV-V2.HLA.AIO1.9mers- 28 1 SWDYRCPPP |.10.000 [64 | KFASEFFPH |f 0018] 98P416 4 1 PGLQASLS IF 0000 [140| SLIVKGFNV | 0.018 Each peptide is a portion of SEQ ID 2 1 PSSWDYRCP 0 214 1 GPVVVAISL || 0.018] NO: 5; each start position is _______________ spcified, the length of peptide is 9 135 SLFPDSLIV || 0.016 | amino acds, and the end position ableXiV-VS .HLA-A1 101-9mer [ 205| PLRLFTLWR || 6 for each peptide is the start position 9BP4B6 [ 209 FTLWRGPVV 0.015 plus eight Each peptide is a portion of SEQ ID 264 ITLLSLVYL ||Startl Subsequence NO: 11; each start position is 396 f SLGYALL 1 00 1 f 2 ~ LPSWDYR]f osospecified, the length of peptide Is 9 396 ||STLGYVALL || 0.015 |4 SPSDR 1.8 1__________0.02 amino acids, and the end position f 319 || YSLCLPMRR |I [0.0 12S -57 oreachpeptideisthestartposition 3941| IQSTLGYVA ||17I .01 0.00 1 plus eght _ 30 I KVTVGVIGS ||1 Li3[ SPGLQALS0I0 1 2-0] Str Subseuence f score F270 1 VYLAGLLAA I 0.012J12 SLSSGFTPF f0.004PLRLFTFWR ][ 024 -203 | NLPLRLFTL I 0.012r CPAFFLYF FTFW F 0020 F425 [ RFYTPPNFV ||0.012 1 21 SCLSLPSSW 10.003 i j NPIRIFIF 0.012 F242 | NQQSDFYKI I 0.012 | CPPPCPADF 0.002 1 TFWRGPVVV 0. 287|'KYRRFPPWL |0.001 LPLRLFTFW 0.01 _435_E ALVLPSIVI I 0.012 |QALIS6S11f 0.0011 LFTFWRGPV If0.002 265 TLLSVYLA If0.012 1 16 GFTPFSCLS 0 1 RLFTFWRGP 2 LQCRKOLGL || 0.012 F-321 RCPPPCPAD If0.001 1 9I( FWRGPWVA] 313 AMVHVAYSL 6 0.0124 [ 30LR FWRG 11 0 40 DFAKSLTIR 5 0012PPCPADFFL 10001 -106| HLLVGKILI || 0.012] QALSSISS TableXl -V ILA-AII.9mer1 I 42671 FYTPPNFVL I 0012I SLSLSSGFT )[ o.o 9OP4B6 385' ALNWREFSF I 0.012] 15 SGFTPFSCLEach peptide is a portion of SEQ ID NN: 11; each start position is sp specified, the length of pepide is 9 QLGLLSFFF 10.012] i ASLSL.SSG 10.000 1 amino acids, and the end position 162 for each peptide is the start position] TableXfV-V64ILA.A1OI.9rners- abteXV-VTA.HILA-AI IO11-9mers. plus eight. I__ 98P486 I9PB Start Subsequence IfScore J Each peptide is a portion of SEQ ID Each peptidle is a portion of SEQ ID 24|| FVFLLTLLL 0.080 NO: 13; each start position is NO: 15: each start position is 16 | TOTELELEF 0.012specified, the length of peptide is9 sp , e length of peptide is 9 amino acids, and the end position amino acids, and the end position 17 || QTELELEFV F 0.010 f each peptide is the start position for each peptide is the start position E FLIQFCSFA [ 0 0 plus eight plus eht. 2 ~ REFSFIQiF i01rt I Suseue ce Start Subsequence Score L ] SFQlFCSF 0.003J [21 I KLKRIKKGW 0.006 1 PKSLSETF 0.002 7 iiQFCSFAD 0.003 11 GTIPIVSPE 4 SLSETFLPN 0.001 18 | TELELEFVF || 0.003 F SIVILGKII 0 ETFLPNGIN 0.001 20 LELEFVFLL 8 0003 1 ISRKLKRIK 8 . 22 || LEFVFLLTL | KRI 1 0.002 ETFLPNGI 0.001 12 }|SFADTQTEL ||_0.002 | 4 IPHVSPERV 3 KSLSETFLP E19 L 1 ELELEFVFL ][. | 32 SFLEEGIG 2 0KSLSETFL f00 K 1 2 EFVFLLTLL ] oi]241 RIIQGWEKS 11.O011 5]L LSETFLPNG__][W565 8 1 F01010 0.001 114 1f ADTQTELEL ][ 10 1 11 VLPSIVILG I011] ableXV-V7B-HLA-A1 101 -9mers 1 EWREFSFIQI ][-26o (71 I KKGWKQ]0.1 98P43 F1 5 1 DTQTELELE F[000]111 II iLFLPI IFO- T j] Each peptidle is a portion of SEQ ID S EL LT 00NO: 15; each start position is 21 ELEFVFT [0.000 F3-31 QFLEEGI 0.0 peiid the length of peptide is9 | 9f IFCSFADTQ || _ 3 I I OFLE [ 1 amino acds, and the end position |1J|| FADTQTELE || 0.000 |LEEGIGOTI1 for each peptide is the start position 10 | FCSFADTQT 0.000]14 F PCISRK 0000] pus eight. -4][ FSFIQIFCS 034|1 FLEEGIGGT 0.000 ]St u e e | 3 ||EFSFlQlFC |[ 0.000VSPERVTM 9 0 STGYVAII 0.015 11~ 9SATT I~ ]E1 GKIILFLPC If r-5]F~i] QQSTLGYVA I .1 |1 ||CSFADTQTE ||0.00011 ______________ i~it GEKSFLE][0)0 1 A QQSTLGY 110 TableXIV-V6-HLA-A1101.9mers. 1 EGIGGTIPH 0.000 6 H9)JYV 0.006 98P4B6 29 WEKSQFLEE f 0000 F3fNMAYQQSTL 0.004 Each peptide is a portion of SEQ ID [T 41 MAYQQSTLG 0.000 NO: 13; each start position is 8 GGTIP specified, the length of peptide is 9 40 _________ 1 F_7________P_._-0 amino acids, and the end position ] 0.000 8 I SILGYVAL for each peptide is the start position 3 PSLGI 0.000 2 NMAYOST [2plus eight.U(RIKKGWE I Start I Subsequence || Sco9r| IGGTIPHVS 0 abieXlV.V7C.HLA.A1OI.9mers 2 || LPSIVILGK | 0.400 |] EEGIGGTIP 0.000 98P416 12 IfILFLPCISR 17032072 KGES 000 Each peptidle is a portion of SEQ ID 13 LFLPCISRK 0.I _____ __ NO: 15; each start position is .1.1 J[FO[30 I1 EKSQFLEEG I 0.000 specified, the length of peptidle is 9 L LJLKRIKKGWEK I0180 I amino ads, and the end position 15 IfLPCISRKLK If 0.100 1 - reach peptidle is the start position 42 ilTIPHVSPER 110.080! ebteXIV7AHLA11O19mes- - plus eight. 5 IVLGKIIL JF.0760 98P46 Subseuence Score 19 IfSRKLKRIKK I0.01 Each peptidle is a portion of SEQ ID r167I KLETIILSK J2400 45 IfHVSPERVTV If0.020 NO: 15; each start position is 159. 11 FLGSGTflNMK-l 0.800] 10 KIILFLPCI specified, the length of peptidle is 9 -175 I1 KLTQEQKSK 110.600 1 ________Ifamino adds, and the end position 21 11 KCLGANILR 0.360 I 6.§..I PCISRKLKR If002 for each peptide is the start position ____________ 6 IfVILGKIILF I .1 plus eight.18GLW L 0.360 F38 IfGIGG11PHV If01 trt [1 ubeence Sco re 1131 WEFLLRLLK 0.240 7 f ILGKiiLFL f= I8 FLPNGING j1 LASPAAAWK 0.) 200] 163 ableXlV-V7C-HLA-A1101-9mers- ableXlV-V7C-HLA.AI ioI9mers ableXIV-V7C-HLA-Ai 10-9mers. 98P48698P4B6 98P486 Each peptide is a portion of SEQ ID Each pepbde is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 9 ead specfied thelenth o pepide s 9 specified the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position or each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. plus eight. plus eight. Start]| Subsquence [ta|t | Subsequence Score ore tart subsequence [score 88 GVVTEDDEA |0.090 86 1 GWTEDD 00021 172 ILSKLTOEQ 109 ALKAANWR .00SGTLSLA 0.002 1 115 SWRNPVPH ]d.0000 69|| AQESGIRNK || 0.060] 112] ANS 0.002 1 99 1 SIDPPESPD 0.000 1 163 || GTWMKLE1 || 0.060 181 KSKCMFSL 1 0.0 I LAFTSWSLG 110.000 37 I LPIEWQQDR | 0.060 136 RLLKSQAAS 1 0.002 113)[ ANSWRNPVL70 126 || GVGPLWEFL | 0.060 179 EQKSKHCMF 155 1 SLGEFLGSG 0.000 [38 |1 PIEWQQDRK | 0.040 1 31 11_ SlLPj~02194I PLWEFLLRL 11 0.002] 1I20)1j VLPHTNGVG 0.0 1I73E 0. LS0T2Q 0~~i 170 11 TIILSKT 0.00 78T SSSSSQuPV 0. 9 | SVEVLASPA I 0.020 73 I GIRNKSSSS 1 I [1457| GTLSLAFTS IF 0.013] 29 RGGLSEIVL 0 TableXV-V HLAAI 101.1 Omer 2 1 SIVILDLSV IF 0.012] 46 Il KIPPLSTPP 0.001 98P4B6 67 |1 AEAQESGIR | 0.012 1 WQQRKIPP 0.001 Each peptide is a portion of SEQ ID 151 i FTSWSLGEF 0.010 NILRGGLSE NO: 3; each start position is ____________ ____________ specified, the length of peptide is 10 I LTQEQKSKH 0.010] 10 1 SPDRAU(AA 0amino acids, and the end position for 51 I STPPPPAMW 10 6-51 ATAEAQESG 0.001] ach peptide is the start position plus 59 || WTEEAGATA 0.010 1571 SPAMWKCL 00 1 nine. 123 1 HTNGVGPLW vEDDEAQD I Subsequence [ || 1f EVLASPAAA 0.009 1 EFLGSGTM.001 )Ir GVGSGDFAK J1 27.00 82 || SQIPVVGVV 0.009 1 VEVLASPAA 10.001] 5 F |\W1GSRNPK JF 3.000 108 I RALKAANSW 0.009 -2271 CLGANILRG 0176] VHHEDAUK 2 57I AMWTEEAGA |0.008 18511 CMFSLISGS 0 1135 SFPDSUW 111.600 | _165_1| WMKLETIll 0.008 HCMFSLISG 0001] 21 GINGIKDARK1 1I-48 1 SLAFTSWSL | 0.008 127-11 VGPLEFLL .001 I II W Jo 0.400 4 I VILDLSVEV | 01.390 06 .1 1 278 MYOYYGTK [1031 PESPDRALK | 0.006 1251 NGVGP[WE o ] 150 j SAWALQLGPK If0.400 I [ 42 QQDRKIPPL 1 .] 6411 GATAEAQES o.oo| 1|7 cLPNGiNGiK If 0.006 [241 GANILRGGL 140 SASGTLS 28111 QLYYGTKYRR|1|06 35 | IVLPIEWQQ |70.006171 IILSILTQE 0.001] 144211 VILDLLQLCR 0.240 5 ILDLSVEVL 0.004 9 AQDS f.240 -134 | LLRLLKSQA |00 16871 LETIILSKL .0011 1 1 11 0.0 100| IDPPESPDR |7| 154 LQLGPKDASR [141 QAASGTLSL |101 DPESPD0R04 3R 27 I ILRGGLSEI 0 44 TWMKLETII 10000 00.40 L|FTLWR 14611 TLSLAFTSW 0.004 PLSTPPPPA 0.000 112 ILIDVSNNMR 10.120 [~~~~__If~~~I Fisw 2-80 F fAAKLGNo71] YQLYYGT1(YR]009 1-2 |1 VLASPAAAW | 0.0-04 781AVKLA [ 17 || AAAWKCLGA ]14311 ASGTLSLAF o0.004 257 KTLPIVAITL I 0090 157 |7 GEFLGSGTW |15071 AFTSWSLGE o-00o0 3 I- KQLGLLSFFF 00811 [1 3I IVILDLSVE 0.003] 36 F VLPIEWOQ) 10.000] 1 166 11 YICSNNIQAR 0080 F1-197I PVLPHFNGV 0.O003 83- IfQIWVV .ooo0- I 69 LWLAGLLMA F0080 89 I VVEDDEAQ | 0.002 1 LGSGTWMK o.ooo 317-I1 VAYSLCIPMR 0.080 TAEATESGI a0.002 52 1 TPPPPAw 0r 2 ARNQQSDFYK 164 TableXV-VI-HLA-A101-10mers- TableXV-VI-HLA-AI101-10mers- Start- Subs uence Score 98P486 I 98P486 16 GFTPFSCLSL 0.012 Each peptide isa portion of SEQ ID Each peptide is a portion of SEQ ID 22 CLSLPSSWDY 0.008 NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 amino acds, and the end position for amino acids, and the end position for 32 RCPPP _ 0.0 ach peptide is the start position plus adi peptide is the start position plus 8 ALSLSLSSGF 0.004 nine. nrne. -- CPPPCPADFF 0.002 Start Subseuenc Score Start Subseuence scored 6 LOAStSLSS 0.001 [ 321 |LCLPMRRSER || 45 LTIRLIRCGY 00 GSPGLALSL . 01 F-147 NVVSAWALQL 1 0.060 209 FTLWRGPVVV ][57 GLALSLSLS .001 183 RQLNFIPIDL |409 VLIYGWKRA 0.015 LSLSSGFTP 0.001 364 || GIMSLGLLSL | 0.048 1 408 FHVUYGWKR YRCPPPCPA 0001 406 4 _STFHVLIYGW 0040 [ QQSDFYKIPI 0012 17 FTPFSCLSLP 0001 254]|| IVNKTLPIVA | 0.040 F4-407 SIVILDLLQL [314 | MVHVAYSLCL |200401 __ DA ViV 24 S [ 316 |HVAYSLCLPM ||34 FQ30[ PPCPADFFLY0.040 [ 356| RIEMYISFGI | 0.036 | -145-1 GFNWSAWAL [ 134IPPPCPADFFL 0.001 I 425 RFYTPPNFVL ] 0.036 | S036 PCPADFFLYF 0.000 102 I WDLRHLLVGK || 0.030 | 172 II IQAROOVEL .012 12 SLSGFTPFS 0000 248 YKIPIEIVNK - 0.030J21 RINQYPESNA ]j .012 11 LSLSSGFTPF Jr 0.000 S367 if IGSRNPKF ]f~5 2 QP~'AY1 .1 21 SCLSLPSSWD I1.00 2851| GTKYRRFPPW I 0.030 165 VYICSNNIQA0 7 QALSLSLSSG 110.000 :216 || VWVAISLATF || 1.070 LLVGKILIDV 30 IT SLS 0.00 83 || LTKTNIIFVA 1 0.030 L-2i.9[ FFL 1 0.012 FYI FSCLSLPSSW 1O0.00 85 || KTNIIFVAIH || 0.030 268 SLW LA F 01 1 - SSGFPFSCL 0.000 1396| STLGYVALLI 0.030 | VTSIPSVSNA 10-10 4 PGLQALSISL 0.000 432| FVLALVLPSI 10.030 [2| ESISMMGSPK 10.091 13 LSSGTPFSC 0.000 [ ]264| ITLLSLVYLA I 0.030 | 4-701 VASTFHV 0.009 163| RQVYCSNNI 02] 214][ GPVWAISLA I 0.009 27[SSWDYRCPPPJJ 0000] 416 KRAFEEEYYR 0.024 F-2178 VAISLATFFF F 0009 15 SGFT _86j| TNIIFVAIHR i3 0024 |NALNREFSF 0.009 0. 39 GDFAKSLTIR I 0024 67 SLGLLSLLAV 10.008 [31YRCPPPCPA7DF 0000] 417 RAFEEEYYRF i 0.024 LLSFFFAMVH 0.008 19 PFSCLSLPSS 207 | RLFTLWRGPV I0.024 1 I 437][ VLPSMLDL I 25 ILPSSWDYRCP 0.000 I 217] j|VVAISLATFF If 0 2 7] FLYSFVRDVI 10008 28 SWDYRCPPPC [00 [223 || ATFFFLYSFV 42[ ASLTIRUR 0008] SPGLQALS ( 400 | YVALLISTFH 1 0.020 JJI I LIDVSNNMRI IF S] 261 IVAITLLSLV ||O* 1 2.02 | TLWRGPVA 0.008 [32 | TVGVIGSGDF I 0.020 | 178 VIELARQNF 0.00 TableXV-VAHLAAI1011.l0mers 142]| IVKGFNWSA I 0.020! | 2981 0 98P416 231| FVRDVIHPYA |4|041 USTFHVLIY 1.00 Eachpepideisaportion ofSEQ 73 VVDVTHHEDA |ATKTNIIFV 0o008 NO: 11; each start position is 340 specified, the length of peptide is 10 ii.'amino acids, and the end position for ]42L7 TableXV-2VHLA-AIIOI10mers- ach peptide is the start position plu 399 ||GYVALLISTF ||f 98P486.01 1 || KILIDVSNNM || 0.018 EachpeptideisaportionofSEQl Stare 2741LAAQL f01 NO: 5; each start position is Str I0ubeqene 0i 274| GLLAAAYQLY ||0.018 3 R 0.8 specified, the length of peptide is 10 RLIRCGYHW f0018 I10 amino acids, and the end foRLFTFWRGPV 306 GLLSFFFAWV If po018sjition for each peptide is the start po FTFWRGPVplus 100 11SLWDLRHLLV 11 0.016 positon lus nine FTLWRGPGPVWVA|| 165 TableXV.V5-HLA.A11IOI1-lomers1 [TableXV-V6.HLA.Al11-10mers- I TableXV 64LAA-AI lO-l1rnors 98P88 [98p488 98134136 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO- 11; each start position is N0 13; each start position is NO: 13; each stan position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position for each peptide is the start position plus ach peptide is the start position plus ach peptide is the start position plus nine. I nine. nine. I Start][ Subsequence |ScoreI Start 11 Subsequence [Subsequence Score 2 || NLPLRLFTRFW 0.00 VSPER H10.900 44 IPHVSPERVT ]0..04 L_7 LFTFWRGPVV j 00022 VLPSIVILGK 40 f IGGTIPVSP T ENLPLRLFTF [0.001j 1 31 ILFLPCISRK 0.800 4if PSIVILOKII FO000] 10 | FWRGPVVVAI || .000 1211 IILFLPCISR 110.240 1 11 SRKLKRIKKG =[0 4 || PLRLFTFWRG 110.000 | [15 -f FLPCISRKLK FO 200 5 | LRLFTFWRGP F 6.000 |1 LPCISRKLKR Tabe161 IVILGKIILF .060 TableXV-VTA1HLA-AIIO 10mers-98P4416 TableXV-VSB-HLA-AI 101- F1 9 1 ISRKLKRIKK 1]0.040]ler9PB 10mers-98acho 1871 CISRKLKRIK 7 5 Each pePide is a portion of SEQ ID Each peptide is a portion of SEQ 1D NO: 15; each start position is NO: 11!,-each-start position is F-37 ___________ ii0.040_ secfied, the length of peptide Is specified, the length of peptide is 4671 HVSPERV1VM]FI 0020 10 amino acids, and the end 10 amino acids, and the end 5 [ SIVILGKIIL 0.012 position for each peptide is the start position for each peptide is the start I VILGKIILFL position plus nine. 19 1 LVLP j0 ____ I I Subsequence 11 Scor I Sub uence 35 FLEEGIGGTc I1 1 10 1 FLPNGINGIK 10.400 18][ QTELELEFVF 0.030 TIPVSPERV F TFLPNGINGI F0003 167[ DTQTELELEF 0.006 SQFLEEGIGG 0.002 2 SPKSLSEFL 0.002 177|| TQTELELEFV ||1 ___ LPSIVILGKI 0.002 ETFLPGING 0001 14 FADTQTELEL | 0.004 | KIIIFIPCIS F 002 [ r201[ ELELEFVFLL 1 39 GIGGTIP.0VS 0401 r[571 SLSETFLPNG 0.___ F6 | SFIQIFCSFA | 8]1 ILGKIILFLP .0 36] LtETFL ][o5007 I 22]|| ELEFVFLLTL |0.002 2 I KLKRIKKGWE 00 F47I KSLSETFLPN IF 0000 F-24 || EFVFLLTLLL | 0.002 ISETFLPNGIN [ F || FIQIFCSFAD 0.001 25 RIKKGWEKSQ 03 |23 LEFVFLLTLL 0.001 2 F-8]| IQIFCSFADT o0.001 | 21 KKKGW 1 1 TableXVV7-AIIO1-l0mers 29 | TELELEFVFL 0.001 9 | QIFCSFADTQ || 0.001 28 KGWEKSQFLE 000 Each peptide ipon SEQ ID ___1____________ 37 11EEGIGGTIPlI JI07000 NO. 15; each start position is 3 I REFSFIQIFC || 0.001 14 LFLPCISRKL 0.000 specified, the length of peptide Is 10 F__1 | NWREFSFIQI 0.000QFLEEGIGGT amino acids, and the end position for 1 CSFADTQTEL| 0.000 2 IKKGWEKSQF 0000 ach peptide is the start position plus M_________________ ____________ nine. 5 | FSF1QIFCSF 1 17 PCiSRKLKRI 0.000 13 || SFADTQTELEII 0.000 1 2 11 GWEKSOFLEE 0.000 2 | WREFSFIQIF | 0.000 24 KRIKKGWEKS 00 7 | SLGYVA 0.030 11 FCSFADTQTE 0.000 - |GIGGTIPHV 0 71 YOQSTLGY 0.012 _10 IIFCSFADTQT ][I0.000 41GGTIPHVSPE 0.000 4]1 EFSFIQIFCS |F-0.000 [32]1 KSQFLEEGG 0.00 00 21 LELEFVFLLT 36 LEEGIGGTIP 0.000 LNAYQQST 151AT TEI 0.000 I3 3F EKSQFLEEGI_ 0,000 2] FLNPAAYQOST 10.000] 301WEKSQFLEEG 10.00 NMAQQfL VT I ~ J 49, 0 1LFLNMAYQQS Ii (700] 166 TableXV-V7B-A1101-10mers- TableX MCA1110mers. TableXV-AI0OI-l0mers. 98P4B6 98P416 98P486 Ecpetd sapronoSEID EhpeteisaotinoSE DEach peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acds, and the end position r mo acids, and the end position for amino acids, and the end position for ach peptide is the start position plus peptide is the start position plu ach pepbde is the start position plus nine. nine, __ nine. [tr ie c Ijj] tat[Subsequence 11 [coe 5 ][r Subsequence Score 9 QSTLGYVALL || 0.000 27 NILRGGLSEI 0[ AQESGIRNKS .00 ______________ 781 TQEQKSKH-CM J.006 0.001SKOFS Ioo TableXV-V7C.A1101-10mers- 1 2 WQQDRKIPPL ]F0 006 1 IILSKLTQEQ 0.001 98P486 6 IF0.004 148 1 LSLAFTSWSL 0.001 Each peptide is a portion of SEQ ID wLsQA NO: 15; each start position is r r specified, th length of peptide is 10 143 AMSGTLSLAF 0004 25 GAILRGGLS _i W~t amino acids, and the end position for 19 AMWKCLGANI 00 F-97 AQDSIDPPES ]F ch peptide is the start position plus ILRGGLSEIV ]j0004 _43=1 QORKIPPIS:]F0-T Nine. r. 151 GEFLGSGTWM 1100O041 92 IITEDDEAQDSI (0.001 (Start P nescorel 36 M.PIEWQQD D. =0 61I FTEEGATAEA 1000 [1-73| ILSKLTOEQK FO .400 119 NPVLPHTNGV 0.03 171 IEQKSKICMF 0.001 13 || VLASPAAAWK ] 0 124 HTNGVGPLWE 0.402 077 LTQEQKSKHC 38: | LPEWQQDRK 0.30 1131 MNSWRNPVL 0.02 147 TLSLAFTSWS 0 109 1 RALKAANSWR ||0.180N I 127 || GVGPLWEFLL ]j 0.185[17[PAAWCLGA 0.0 159|| EFLGSGTWMK 0.180 1 901 VVTEDDEAQD I U(SQMSGT [ 100I SIDPPESPDR ||0.080| --1- 0002 29 LRGGLSEIVL 137| VLPIEWQQDR 1] 87 WGVEDDE 0.002 (537 TPPPPAMW 0.0000 F1-67 | MKLETIlLSK |0.06750] -7E I 16 MKETIL~t(]k99] 151j AFTSWSLGEF 1(00 14J[SPPMAWKC 10.000 16 |GTWMKLETi 110.060 31 GGLSEVL 02000 146 iGTLSLAFTSW 1 0045 131 |[ LWEFLLRLLK 1 0.0401 22 KCLGANILRG 0002 185 HCMFSLISGS 1 ||7 TAEAQESGIR 1 0.0401 -11 GIRNKSSSSS FO0.01 [5771 PAMWEA 0 ]4 IVILDLSVEV 10.030 47 KIPPLSTPPP ]F001 SLAFTSWSLG 1000 F 103]| PPESPDRALK 10.020| 3 _GLSEIVLPIE 110129 SVLELAP 10.01 767[_ RNKSSSSSI 10.001 M56] SLGEFLGSGT 10.0070 LE 0.018 KSSSSSQIPV 0.001 175 SKLTQEQKSK 10.015 60 WEEAGATAE F -0"7 TableXVI-VI-HLA-A24-9mers 176 || KLTQEQKSKH ||0.012| [-F]1 VTEDD 0.001 98P4B6 Vhi(SAST 10.012 (F8371 SQIWVVI-WT 01 . ahpetd I orinofiQI 168 ||[KLETIILSKL 1 1 7 [ ETII0 NO: 3; each start position is ATAEAQESGI specified, the length of pepde is hF -6 ITEQS I JF_ 1 ii I VEVLASPAAA JI001 amino acids, and the end position 15 || FTSWSLGEFL |60.0101 11 TWME foreachpepfideisthe start position 12 || EVLASPAAAW H 0.009| TNGGPLWF 1 plus eight. 89 I GVVTEDDEAQ 10.009 110 ALKAANSWRN 0.00 Start Subsequence Score (1 LGSGTWMKL 11008 1 16 1100 WMLFIS1 28 77 KYRRFPPWL14000 160 WMLT]L FLSGWML|0.08 21 1 WKCLGANILR 10.008 I NSWRNPVLPH 110.0 42 FYTPPNFVL 128 |F VGPLWEFLLR | S.008 _j 00 331 150]LAFiS]E(Pg 5If VILDLSVEVL 110Oo6J 5 AMWTEAA j-' 000 283][ YYGTKYRRF 1100.000 1- 12 ][ KMANSWRNPV (0.006 3 SIVILDLSVE II 0 I 28[LSVDI 70.000 74[- EAQESRN 0.- 39 18 IKKCFSII __ FSFIQS~T 8.0 NO: 31; ah.ta0poitoni ____________ _110.006 j171 TILLSLTQA 0.004 Lnj 20.000 167 TableXVI-V1-HLA-A24-9ers- TableXV-VI-HLA-A24-9mers jV-V LA-A24-9mers 98P486 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptideis a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3: each start position is NO; 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide Is the start position plus eight. ____plus eight. plus eight Start Subsequence JjScore j Start JrSubs ] coe [Sta rt[ Susqe c oe 418 _AFEEEYYRF I 18.000 128 iSNAEYLASL 4.800 3LLAVTSI 1 1.50 330 RYLFLNMAY If 18.000j 41 IfFAKSLTJR 1r 4.0353 1[ EVWRIEMYI Jj .40 378][ SIPSVSNAL 3710.080 | GSGDFAKSL 14.800 [397 TIGYVALLI .400 1 QYPESNAEY 9900 1 QARQQVEL 4.400 433[ VLAvLPSI j1.40 399 I GYVALLIST 9.000 300 QCRKQLGLL 4000 186 NFIPIDLGS 1.260 171QV1ELARQL 184] 75[ -DVTHHEDAL 4.00 - 1641 QVYICSNNI 11.200 1841i QLNFIPIDL [95 iSTGYVAL 4.000 18074 ELARONFI L1.200 258 || TLPVAITL [ 4 299 LQCRKQLGL 4000 425||T 313 AMVHVAYSL 5.403 LALFPDSL 14.0001 386 LNWREFSF 214 I GPVVAISL | 8.400 365 IMSLGLLSL 4000 246 || DFYKIPIEI [ 7.700 | 48 WSAWALQL 4.000 2701 | VYLAGUA 360|. YISFGIMSL 50TabeXVV2-HLAA24mers1 359 |I MYISFGIMS || 7.0 IVATLLSL 98P46 268]| SLVYLAGLL |7.200 196 SSAREIENL EachpeptideisaporionofSEQID ___ IfFPLTI NO: 5; each start position is 291_________ a129 NAEYLASLF 3.600 specified, the length of peptide is 366 i MSLGLLSLL 72 2 [78 VS 3.600 amino acids, and the end position 220 ISLATFFFL 7200 for each peptide is the start position 403_I LLISTFHVL | 7200VGVIGS 303 KQLGLLSFF 40 7.200] YVALLISTF F -400 Start Subsequence score 436 f LVLPSIVIL [3041 QLGLLSFFF 5 L GLQALSLSL 7.2 2 || EIENLPLRL || 7.200 383 SNALNREF -17L[ FIKSCLSL 6 61 || RNPKFASEF || 6.600 1 57 IVIGSRNPKF 2.200 1 1 SGSPGLQAL 115760 428 I TPPNFVLAL 6.000 223 ATFFFLYSF -T1 SGTPFSL 274 I1 GLLAAAYQL |0 o] 41 11 LIYGW0RAF0 0 3 125 1 YPESNAEYL 6.000219 AISLATFFF 2f 1 ][ CPPPCPADF3.600 363 || FGIMSLGLL |1 00 I 62-1 NPKFASEFF 1 2 -9( LSLSLSSGF I -26411 ITLLSLVYL_ _6000 _ 821 NIIF 2.000 -711 CPF F 27 F3961I STIGYVALL 11 6.000 F 23911 YARNQQSDF j-- 12 SSGTF[A0 297 1 TWLOCRKQL ][6000] 21711 WAJSLATF 2.00 16 GFTPFSCLS 6.0000| 259 || LPIVAITLL 6 242 NQQSDFYKI ||98 30 DYRCPPPCP JF 0 5 || SMMGSPKSL I8 6.000 |DALTKTNII ] ADFFL 04 203 ||NLPLRLFTL I 6.000 | 171 CLPNGINGI I 34 PPPCFADFF H[.0 441 | IVILDLLQL || 6.000 1 3491 WNEEEVWRI 1.0 23 LSLISSWDY J[ 0.180 187 FPIDLGSL I 6.000_j NIQARQQVI 1821 GSPGLALS 0 146 || FNVSAWAL I 6.000 1 SCLSLPSSW .18o 267 I LSLVYLAGL || 6.000 105 RHLLVGKIL 7 QALSISISS 110.180 | 99| TSLWDLRHL If 6.010 SSGFTPFSC F -0.100 100I LDLIIL1761 I12I ILIDVSNNM 1.52 r Z1SLSLSSGFT 0.100o 43 fSLDLL _j55 -6v'sv sooJ ij LQALSLSLS] i 485I KTNIIVID I 5.00 F-37 1011 LVGKIIn1 1.500 1 25 LPSSWDYRC 0.100 247 11 FYKIPIEIV 5.000 ASLFPDSLI 1.500 1 13 LS PSS]0.0 4231 [ YYRFYTPPN[R231EVKLI 1 0 FCSPSji TabeVI16A 4 e TableXVI-V2-HLA-A24-9mers. TableX V5B-ILA.A24-mers_ TableVIV.HLA.A24.9mers. 98P486 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 5; each start position is NO: 11; each start position is NO: 13; each start position is specified, the length of peptide is 9 specified, the length of peptide is9 specified, the length of peptide is 9 amino acids, and the end position aioadadteedpsto mn cdadteedpsto for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. plus eight. -plus eight. [Start][ Subsequence if Scorert iubsequence IFScore Start 11 Subseuence I Score |19 PFSCLSLPS i 0.060 M2 SFADTQTEL r26.400 126 [KKGWEKSOF 0.400 |32 || RCPPPCPAD I 0.036 F-57 SFIQIFCSF 25.200 1 21 1 KLKRIKKGW 0.280 [367| PCPADFFLY 10018ELELEFVFL 7.200 1311 PSIVILGKI 0.231 24 || SLPSSWDYR i2 0015FVFLLTLLL j14.800 124 RIKKGWEKS 0220 ET-] PGLQALSLS ] 0.015 ) 16 1 TOTELELEF 13.168 1 10 F 1-1I LSLSSGFTP Ii =.1 21 LELEFVFLL 31 0.720 F34J1 FLEGIGGT M K9I9. F27 |1 SSWDYRCPP || 0.012 r__37 EFSFIQIFC 11 IILFLPCIS 31 YRCPPPCPA 0.012 2 REFSIQIF GGTIPHVS |18 | TPFSCLSLP I 0.010 11411 ADTQTELEL ][C [ HVSPERVTV I 01 |29 | WDYRCPPPC || 0.010 EFVF 0432 1 38 11 GIGGTIPHV 0.100 r_8 |F ALSLSLSSG 1 0.010 r22 -1 LEFVFLLTL I1 040 1[ IPIV 0.100 28 j SWDYRCPPP ||2111 ELEFVFLLT 1 3331 QFLEEGIGG 0.001900 [22 || CLSLPSSWD I1 0180 r1 31 LFLPCISRK f 26 | PSSWDYRCPF 0.Ooi 671 FIOIFCSFA 0.150 ||42 J1 TIP.VSPER 0.023] - 1 QTELELEFV f 9 [ 71 GKIILFLPC jr0.022] TableXVI-V5A-HLA-A24-9mers- 8 11 QIFCSFADT 11 07 LL][ V.PSIVILG 98P4B6 W FCSFADTQT 01 1 GTIPHVSPE 0.0183 Each peptide is a portion of SEQ ID FSFIQIFCS 0.100 28 GWEKSQFLE 0.015 NO: 11; each start position is specified, the length of peptide is 9 F-971 IFCSF r003771 EGIGGTIPH 0.015 amino acids, and the end position [ 2 1 [ h[IV[LGK]0.014 for each peptide is the start position 15 DTQTELELE 0 15 3 8 plus eight. CSFADTQTE 0.1 81 ISRKU(RIK 127 IStart| Subsequence I Score FADIOTELE 0. 1 1 32 SOFLEEGIG 0.010 | 1 I NLPLRLFTF || 3.000 407 GGTIPHVSP F0_0_170 | 87i TFWRGPWV ||0500 TableXVI-0.-50A-A24-9mers- 1 LPCISRKLK F-6 | LFTFWRGPV | 0.500 98P4B6 ILFLPCISR 2 |~ LPLRLFTFW ]Eachpeptideisaportion of SED I 23 If KRIKKGWEK 0.216 -7 | FTFWRGPVV NO: 13; each start position is0.10 specified, the length of tide is 9 I~iI FWR PVV A 0 0 amino acids, and the end position r-176 1 I PCISRI<UR II .0 5 | RLFTFWRGP I 0.020 for each peptide is the start position 44 VERVT 0 4 | LRLFTFWRG |F0.00 plus eight. 0.002 3 1 PLRLFTFWR || [.01uence I S [9 E000 27 KrFKOFL 11520 FI-0-11 EKSOFLEEG C 00 TableXVl-V5BHLA-A24-9mers- 1 FLPCISRKL If 9.240 F227FLKRIKKGWE 0.001 98P486 [-5[ IVILGIIL If 6.000 I 25 If IKKGWEKSQ Each peptide is a portion of SEQ ID IG7L M E F EGGGTIP NO: 11; each start position is r_7 SFEG .0 specified, the length of peptide is 9 1 amino acids, and the end position [J.-0i[ KIILFLPCI 11 TableXVV-5V-HLA-A2-9mers or each peptide is the start position 98P4 VILGKIILF If 3.000 B6_ _ lus eight. [7[ SIVILGKII Rf 1.800 1 Each peptide I a portion of SEQ ID F - Subse uence lS -core 1 7[ CISRKLKRI jf .o NO: 15; each start position is EFVFLLTLL 36.000 specified, the length of p i 9 amino acids, and the end 169o , fo1ahppid6stesar9 oiin for each peptide is the start position TL- A24-10mers- TableXVIVC-HLA-A24-l0mers. plus eight 4136 98P486 Sta rt Subsequence Score Each peptide is a portion of SEQ ID Each peptide Is a portion of SEQ ID 1 || SPKSLSETF [ 2.400 NO: 15; each start position is NO: 15; each start position is specified, the length of pepide is 9 specified, the length of peptide is 9 [11 IIFLPGIGI (1.00amino acids, and the end position amino adds, and the end position 4[1 SLSETFLPN || 0.144 | for each peptide is the start position or each peptide is the stat position 6 || SETFLPNGI || 0.144 plus eiht 3 plus eight 7 || ETFLPNGIN || 0.100 1Sta uJ[cjIScore i Score 811 TFLPNGING (0.090 [j|T SPAAAWKCL 14000] 8811 GVVTEDDEA 0. F2 |1 PKSLSETFL ||GTLSL II4.000 14]jIASPAAAWKC I 0 .16 1 3 || KSLSETFLP [057 ILDLSVEVL T-4300 25 1 ANILRGGLS [050.00 5 || LSETFLPNG ||01is 165 WMKLETIIL 72)1 SGIRNKSSS 0.150 ____________- -113 [fANSWRNPVL- -1- 4.0011i EVLASPAMA 0.150 Tabl1XVI-V7B-HLA-A24-mers-58 EFLGSGTWM 381 ip GV Ro o1 98P4B6 125f NGVGPLWEF 3300 177 TQEQKSKHC Each peptide is a portion of SE 10 143EASGTLS 1 147 LSLAFTSWS 0.150 NO- 15; each start position is - A specified, the length of peptide is 9 15171 FTSWSLGEF 64 G * 0.132 amino acids, and the end position 179 EQKSKHCMF 2.000 134 LLRLLKSQA 31 0.120 or each peptide is the start position 164 TWMKLETII 11.800 I11TLSLAFTSW I *-i'A plus GISEIVIPI FT68 ri-8J CMFSLISGS eIight Start |I Subsequence ||Score 66 TAEAQESGI 1 1.5 1821 SKHCMFSLI 0.1 5 || AYQQSTLGY | 7.5001 1 10 1 A8 j MWE F[0120 F-97| STLGYVALL ||6.000 [ ILRGGLSEI 97 EDD ODS 1 8 QSTLGYVAL GTWMKLETI I IEWQQDRKI 4.000 F3 1 NMAYQQSTL l. 4.000 I67F1_00I F3 3 fNMYQTL 4 132 IfEFLLRLLK-S- II 0825] 1I62 I1 SGTWMKLET 0.110i S1 |1 FLNMAYQQS | 0.1801 1 LETIILSKL 0616] 17 AAAW 0.100 2T|1 LNMAYQQST 0.180 | 10 PPESPDRAL 100]1 ssss ][5i6* 6 || YQQSTLGYV | 0.150 _ L1407] SQMSGTLS 3 F I QQSTLGYVA ||129 PLWEFLLR 1 0.480 76 NKSSSSSQI 4 | MAYQQSTiG 0.010] | 20 WKCLGANIL 142 MSGSLA 0.100 ~ 036 ] 105 1f SPDRALKAA IF0.1-00 TableXVI-WC-HLA-A24-10mers- RNPVLPHTN 0.360 AmwFEEA f oi0o 98P4B36 9846J I136 IfRLU(SOAAS If0.300 1I44]! SGTLSLAFT 1I0.1001 Each peptide is a portion of SEQ I 8 IF 0 -- 75 [ 1 NO: 15; each start position is specified, the length of peptide is 9 4 VILDLSVEV F 0Sw 1 amino acids, and the end position 2 HTNGVGPLW SSSSSQIPV 1f 0.100 for each peptide is the start position 83 QIPWGWT 0.210 F 2)1 VtAS 0.100 plus eight -104 ESPDRALKA 0.198 1 7371 GIRNKSSSS ][ 0.00] Start I Subsequence || S 51 S ____ 171 ESGIRNKSS 0.10 139 I KSQAASGTL ||12.000| 145 =GLSLAFTS 178 QEQKSKHCM][ 0.075 29 || RGGLSEIVL || 8.0 181 1 RGSEIVL C IMFS 8 0 14 WSLGEFLGS If0.180 FI-501 AFTSWSLGE 11.501 1810 KSKHCMFSL I 11 KIPPLSTPP8.000 10I LWEFLLRLL | 7.200 9 j SVEVLASPA 7.20 0i T6I KLETIIL 0. _4 127 i VGPLWEFLL | 6.000 | 5 WTEEAGATA 0.180 122 ] PHTNGVGPL 100401 fli~J VPLWFLL 1~.ao a15 LGEFLGSGT 21)KCGNL if03 126 i GVGPLWEFL 1 5.760 | 152 TSWSLGEFL 4.800 | 52 TP MWT 1 0.180 [116]1WRNPVLPHT 152 31 TWL L 1f 4.00] 112 AANSWRNPV 1f 0.180 F3571I IVLPIEWQQ II 0025]1 160 i LGSGTWMKL | 4 [8 LSVEVLASP 148 SLAFTSWSL || SIVILDLSV 10.180 1771 KSSSQlP IF 0.024] 42 - QDRKIPPL if 4.001 169 ETI ILSKLT 110.-1801 191 PVPHTNGV fooI 170 TabIeXVI-V7C-HLA-A24-10mers- TableXVII-VI-HLA.A24-0mers. 98P4B6 981416 9SP486 Each peptide is a portion of SEQ ID Each Peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position amino acds, and the end position for o acids, and the end position for for each peptide is the start position each peptide is the start position plus peptide is the start position plus plus eight nine nine. Start Subse uence Start Subsequence Scorere NO: 3; eache start positionncs 124 LPIEWQQAERL0.22 j2671 LSLVYLAGLL |3.7.200 000_______ 3.0 1 PS VILDIS || 0.021 1 FYTPPNFVLA 1 410 _____ 3.000 6 DLSVEVA 0021 402 ALLISTFVAISLATF 3.000 32 SEIVLPIE f 0.01 1 F GYHWIGSRN f 7.000 LYYGKYRR ||100.0000 183 | KHCMFSLIS 10000 247] FYKIPIEIVN 1 7.000 2.000 1 8F GIMSLGLLSL|I 6000 NPIENDLPLRF 30 30000 1 IVI.HLAA24-lomers. r 17[ ESNAEYLASL 6.000 81 ALTKTNIIF 3.000 98P486 | 614 .F 60000 1280 |E A I 880 Each peptide is a portion of SEQ ID ||WLQCRKQLGL SGMLL ||0 20.000__ Z800 NO: 3; each start position is If |PDSLIVXGF 6.000 specified, the length of peptide is 10 ___[IMGPS -~11I IIVNMI amino acids, and the end position for [ 273 ]( AGLLAAAYQL 116.000 21 [WILATFF _11 2.400 ch peptide Is the start position plus [323 I1 LPMRRSERYL 11 6.000 6I CPGIG [26 1 nine. RQLNA NDLL 6.000||1 377 || TS _SV NA ||_ 12.09 | R E NM Srt JSubse uence]Score 435~ AL VLI VI f600 L LSETCLPNGI IF2-160 [359 ] QYPS NAEL 36 . 0 440 -1 SIVILDLLQL I 6.000 1 396 1 STLGYV A I I2 1 0 131 || NEYLD || 0.800 |j 0 TLPIVAITLL |.FVLALVLPSI 00100 437438 |LPSIVILDL||.0 5.600 354 -IM 282| LYYGTKYRRF 11100.000 422 EYYRFYTPPN 22 . LATFFFLYSF I [-17 I YYRFYTPPNF 1100.0001 219 AISLATFFFL 4321 TVGVIGSGDF I r-~I 201RPWLErW' .40 1o 417 IRAEEYYRF If4.800 385 11 NM ESIIT 427I RFYTPPNFVL 41 365 IMSLGLLSLL 4.800 [iF 1-67 NFIPIDLGSL I 36.00 19711 SAREIENLPL If.4.80 0 348 IIWNEEEVWRI 1.8001 s 145 GF7NWSAWAL 11 30.000 1 72f IQARbeVIEL 4A400me REIENLPLRL rs- 728 52-7F KTPDFASTIL JJ 2 K 356J RIEMYISFGI IF42700 1431LLISTFH VIIf150 2h 36 ppIGSGDFAKSL ID4.000 330 RYLFLNMAYQ 11500I r362N SFGIMSLGLL:98 YTSLWDLRHL 40 4341 1.500 F2137]1 RGPVVVAISL I[0 ] 132 ftYLASLFPDSL If4J0211 LW RG PV-WA [F-4-0i F1831 RQLNFIPIDL II1 65800 1296 J1 EWQRiKQL 336 4.000 V HMiwu - I i~T IF3 TSIPSVSNA7 Jf 79] 267 11 |LSLVYLAGLL ]| 4.00 7I2 FYSFVRDVI [5407 F-13-1426 |YALD FYTPP0NFL || 7.20 M KI EY SFDS 08.195 0 LSSAREIENL || 4.001 DLRHLLVGKI.[ 2477 ||EVNT YI PIN| .0 314 f MVHVAYSLCL .000 238 PYARNQQSDF 1 263 IfALSVYL 4.0600 ||RNPKFAS-V2-HLA-A24EF-F16 270 IVYLAGL 2.000 || LQCRKQLGLL | 4.000 1 3 fVLPSIVILDL 92840] ~ j'I AIHREHYTSL ][ ~Each peptide is a portion of SEQ ID 3-127 T[ FAMHVAYSLJ[48400 || ISFGIMSLGL NO: 5; each start position is [ If AYQLYYGT2Y 0 A A specified, the length of peptide is 165 VYICSNNIQA 7.5003 9 SPKSLSETCL I 4.000 amino acids, and the end 11 QOIELAR1 47 | 395 QSTLGYVALL || 4.000 sition for each peptide is the sta 435 LAVP7.2S007 V L ___ 0Jp_ 172I ENPRFLI25- 8 I||TLGYVAL || 4.000 _plus nine. 202 L_____ 7.2001 2Tf42 RN SDFYKI || 3.960 Start Subsuence Score 2_1 || AISLATFFFL ||..805 9 IF TSLWDLRLIf ~ 417 || RQVYICSNN | .600 16 GFTPFSCLSLI 24. 427 YTNF 382 7.20 1 97VSNAL ||32 S ERCPPPCPADF 7.200 303f KQLGLLSFFF ][7.20 [3 2 GPGLQALSL | 6K || 171 1TableXVI.V24ILA-A24-0mers- Star I Subse uence IfScore 1 [ach peptide is the start position plus] .98P4B6 I i.I ENLPLRLFTF If360 [nine. Each peptide is a portion of SEQ ID: 10 FWRGPVWVAI If~ 1~ ~ iSubsequence I cr NO: 5; each start position is 7 55.440 specified, the length of peptide is 10 amino acids, and the end r9-171 TFWRGP 05 7 VILGKIILFL 8.400 position for each peptide is the start 2 NLPRLFTFW I SIVILGKIIL II6.000 position plus nine. 6 1 IVLGKIILF 3.00 Start |i Subsequence || Score [ FTFWRGPV ][ .10 35 JEFLEEGIGGTI 1 |30| DYRCPPPCPAI 3 LPSLGKI 1.540 14 I SSGFTPFSCL | 4.800 |027 j KKGWEKSQFL 0960 1i1 LSLSSGFTPF | 30PLR0 TFWRG 0.01 34 QFEEGIGGT 10900 |33 I CPPPCPADFFj 3.6- 46 HVSPERVTVM |30.600 |8 || ALSLSLSSGF | r 2.4700 TabloXVII.V5B4ILA-A2410mem- 11 1 KIILFLPCIS ]10.360j | 4| PGLOALSLSL ||0.720| 98P4B6 1 26 IKKGWEKSQF Ii 0200J 34II PPPCPADFFL 0.600~ Each peptide is a portion ofSEQ ID) 4I PSI VLGKII ][ 0.180]1 [36.[ PCPADFFLYF ][030NO: 11; each start position is F-8-I EGIGGTIPHV 1][.150 r~- I LSLSLSSGFT ]( 0150 ,pecified. the length of peptide isPCSKRI]0151 610 amino acds, and the end 5 2 Q I [-1 position for each peptide is the start .. 120 TIPHVSPERV I 24 I SLPSSWDYRC 1 0.150 position plus nn. - 107J GKIILFLPCI J10.i1o50 15 | SGSPGLQALS F] 0.144 ore] __9 __________ .4 13 LSSTPFSC 120 E TLLL 136.000 0.140 20 1[ FSCLSLPSSW ]F010] I_21 ELEFVFLLTL F-0o]3-1][J EKSQFLEEGI I T ~ F78 TPFSCLSLPS 110101 2071 ELELEFVFLL 6.000 [-T][ IPHVSPERVTr 0 0 1 1 SGFTPFSCLS 0.01I CSFADTTEL 4.400 F-21 RKLKRIKKGW IF 0.042] 3i1 S PPSCPAFS 0.04 FADTELEL 4400 F24][ KRIKKGWEKS 0.03 [28 SWDYRCPPPC 1 0.100 1 DTQTELELEF [3.6 LEEGIG 1131 LSSGFTPFSC 1f 0.100 [_18IF QTELELEFVF [ 3.600! 42 GiPVS-PER 1002 3I SPGLQALSLS 1 0.1001 [..5L1 FSFIQIFCSF 1 3.3601 11 1 UV.jf S~IVIG J00 F22 TCLSIWSSWDY 1f 0.10 I -CE NWREFSFIQI 1440 I 281 [ GWEKS1J[ 0.024] 119 IPFSCLSLPSS If11. 19 JfTELELEFVFL 0.86 f I 2-I VLPSIVILGK I 0.021 1 23 LSLPSSWDYR 0.018 6 1 0150 1 25 1RI0ES70 7 IfQLSLSLSSG If0.15I 4 J FFIIC I 0.sw 22 ]jKLKRIKKGWE 0r .02o0 T FRPFSCLSLP 15IFCSFADTQT I SQFLEE 0.020 21 JrSCLSLPSSWD Jr0.015] [23 J[ LEFVFLLTLL If0.480]1] IILFLPCISR I 35j PPCPADFFLY F[014-2 J1 WREFSFIQIF 10.360 1 1 IfFLPCISRKLKJri] ~T~ SWDRCPPP [ 0.012] 8 J[ IQIFCSFADT f0.180 38 IfILGKIILFLP _l O)1 S25 3LPS YRP30.1][ TQTELELEFV f 0.120-7 JPSD C 18 L fCSK(IKJ .1 10][ SLSLSSGFTP 10.01 F1-33 SFADTQTELE 0.060 16I-F LPCISR(LKR Jif-Tj 31L 1 YRCPPPCPAD r0.001 I 1[LELEFVFLLT 0.030 1 1[19 1f ISRKLKRIKJ( 110.011 L29WDYRCPPPCP L 3 REFSFIQIFC 0.028 33 SQFLEEGIGG PiSSWDYRCPP 7ii FIQIFCSFAD 0.015 41 GGTIPHVSPE1] -- 11II CSFDTQE 012 F[40 I GGTIPHVSP 1[.010 9 11QIFCSFADTQ 1001] 1 ILFLPCISRK 1000 TableXVil-YSA-HLA-A24-10mers- AYQTELELE 0 0001 136 1 EEGIGGTIP 98P4B6 4 - 1(0.002 Each peptide is a portion of SEQ ID r NO- 11; each start position is 9bP86 specified, the length of peptide is 10 [-30 WEKSQFLEEG 0 mino acids, and the end position for Each peptide is a portion of SEQ ID 23 LKRIKKGWE 0 0 ach peptide is the start position plus N 13; each start position is amino acids, and the end position for 172 TableXVl-V7A-HLA-A24-10mers- TableXVll-V7C-HLAA24-0mers- ableXVlf-VTC.ILA.A24.l0mers. 98P4B6 981416 1 F 98P416 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide Is a portion of SEQ ID NO: 15; each start position is NO 15; each start position is NO 15; each start position is specfied, the length of peptide is specified, the length of peptide is 10 specified, the length of peptide is 10 10 amino acids, and the end amino acids, and the end position for amino acids, and the end position for position for each peptide is the start ach peptide is the start position plus ach peptide is the start position plus position plus nine. nine nine. Start Subs uence Score Start fSubsequence || Scoreatt[Subsequence Score 9 TFLPNGINGI 10.800 | l1261 NGVGPLWEFL 7052]F STPPPPAMWT -2 | SPKSLSETFL | 4.000] 1102 PE R 7.200[ LTO|QKSKIC [ 0.180 1|| GSPKSLSETF| 3.600 Ll AANSWRNPVL 6.00 [134][ FLLKSQA 1 0.180 6 || LSETFLPNGI 2.160129 GPLWEFLLRL 6.000 i CMFSLISGS 0.180 S4 | KSLSETFLPN | 0.360 148 LSAFTS 6000 I 146 ] GTLSLAFTSW 18 10 || FLPNGINGIK ||02 DE][ASPA WKCL IF-0] 3 [ PIEWQQDRKI .10.165 5 |5 SLSETFLPNG 0.0125 TWMKLETIIL 6.000 8 VTEDDEA 0.165 L I|| SETFLPNGIN__||0_0 241_ LGANILRGGL 4.800 SVEVLASPM ]1o.150 8 ETFLPNGING || 20 A73 SGIRNKSSSS 0.010 3 PKSLSETFLP |I | ] [27 GGPLWEFLI 4.800] 2511 GANILRGGLS 0.0000 - lV[FTSWSL GEFL 14.800 [ 1 5711 LGEFLGSGT [t 0150 TableXVIlI-V7.A24-10mers- F 160[ FLGSGTWMKL 4.400 1211 EVLASPAAAW 0.150 98P486 122][ V 1 4.000 1756 SLGEFLGSGT Each peptide is a portion of SEQ ID Fli41IF SQAASGTLSL 4.000 LI -II1JLPSIVILDLS 0.140 NO: 15; each start position is specified, the length of peptide is SE 10 amino acids, and the end 143 AMSGTLSLAF 1 2.400 r (116 0.140 position for each peptide is the start 125 QQDRKIPPLS ii0.140 position plus nine F-31 I GGL SEIVI I 2.100 7 [& Jr, A]TEAE IF 01 32- I [siartI Subsequence-ll Score -761 RNKSSSSSQI12-000] [ LA KC 132 611 AYQQSTLGYV i 7.500 2 NILRGGLsi 0 14 LS<LTQEQKS 0.132 3 H LNMAYQQSTL || 6000I 1[2 8 |QQSTLGYVAL || 4.000 19 MWKCLGANI 1200 92 TDSI |1 2 9 iF QSTLGYVALL |1400| 0 |K[ ATAEAQESGI 4.001 0|RLLKsQM 120 110 | STLGYVALLI | 2.100 F 63 SGIWMKLETI 1.000 1 01 SPDRALKMN 0120] 1 || LFLNMAYQQS 178 TQEQKSKHCM | 00590] MTEEAGATA 7 | YQQSTLGYVA ||.1 13011 PLWELLRLL 0576J F283[ ILRGGLSE.V180 | 1 2 I FLNMAYQQST I LRGGLS 0.1I8|54 SWSLGEFLGS 1[ 0.120 5 || MAYQQSTLGY || 0.100 [j18 11 QKSKHCMFSL 0.400 1145][ SGTLSLAFTS 31 0.120] I4 I| NMAYQQSTLG || 0010 1 Q -0I GSTWMKLET 179 If QEQKSKHCMF 1 0.300 1 r97][ AQDSIDPPES jo1] TableXVil-V7C-HLA-A24-1_0mers- Q] 14 TLSLAFTSWS] 98P4B6 F-7071 AQESGIRNKS 10277 1 80 EQKS(HCMFS I Each peptide is a portion of SEQ ID NO: 15; each start position is __7E_ specified, the length of peptide is 10 112 31 KAANSWRNPV 0.240 1142 IQ SGTLSLA amino acids, and the end position for F][ VTEDDEAQDS 0.216 1 18 AAAWKCLGAN each peptide is the start position plus I L A 0 3 QA Sube9unc LSELAP 0.210 J F311 ALKASWRNG _____ nine. [ 8[ SSQIPWGVV 0200 1A 168 KLETIILSKL 118.4-801KSSQP14R GTLA 1010 15[1 AFTSWSLGEF 11.01 0ILDLSVEV 10198] 1740 GIRNKSSS0SS0 15Th5 [1 ~ If AF SWSLE F 33i~o 1W 1 SEIV PIE W .9 81 SSSQIP WVGV ] .100 [ ~ ~ ~ ~ ~j~f jfVLLVV I. 3 [13 NPVLPHTNGV 1 .8 16 WMKLETIILS 1.0] [~TWQDRIPL [L~.] [is] EPDALM 0.1801 1 72 ESGIRNKSSS ]l P* 173 TableXVI.WCHLA.A24.IIOrners- TableXV11IMVIHLA.B7.gmers. Table)MI.I4LA.B7.9mer 90P488 84B 98P4B6 Eachpeptide is aportion of SEOID 1 Each peptide is aportion of SEQ 10 Each peptides a portion of SEO 10 N0r 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position forl amino acids, and the end position amino acids, and the end position chpeptide is the start position plus for each peptide is the start position for each peptide is the start position nine. ____plus eight. ___ plus eight. ____ [I S ubseuence I Score 1 Start]Subsequence] Score] stRa7rt[ Subseqec IScorei -58. 11 AMWEEAGAT f000I 220][ ISLATFFFL ]F 4.000] [ 32-8 IISERYLFLNM 31ODOo 1133 If EFLLRLLK-SQIf 0.090 1 187 IfFPDLGSL JI40] I306 IIGLLSFFFAM ][ Iooo 19!EFLGSGTWMK 10285 V GINAEYLASL 14000] L-2Zd MYQLYYGT ][0.900] [iifGEFLGSGTWM 0.0501 363] FGIMSLGLL i 4.000 ALITH 0.600 f50 ifPLSTPPPPAM F-06] 274]7 GLLAMAYQL If400] I297 1 TWLQCRKQL 10.600] 47 IfKIPPLSTPPP r 0.035 [ I IMSLGLLSL If400J I262 IfVAITLLSV1 0.800 F-22 K CLGANILRG 31.030] 61 MSLGI.LSLL F 239]I YARNQQSOF 0."60 118-11 RNPVLPHTNG 0. 030] 184 IIQLNFIPIDL If4.000 44][ LALVLPSIEA [09 11 RAJ(AANSWR ii0.0-30] 9-3 1HREHYS I1.016] FASEFFPIIV 0.600 [37 RW(XSQAASG 310.030] 32 PMRRSERYL If4.000 161]1 ASRQVY1CS I 96 EAQDSIDPPE 0.025] 3-9511 OSIYA0I400 i YTPFLi~ 172j IILSKLTQEQ 1'0.024]1 267j LSLVYLAGL F-&00I37411 LAvTsipsvIf00 268 L[ SLVYLAGLL If4.000 I 3141 MVAYSLC 0[.500 ITableXV11l.V -HLA-B7-9mers. 6 fYSGIS 1-5 341 GVIGSGDFA 050 I98P4B6 19 I f PA SAREJENL If4.00] f 161 VWAISLAT_ 0.500 Each peptide is a portion of SEQ ID IIS F-69 31spvsL [VsooJ [Y 1 LAGLIA ]1 o.500 NO: 3: each start position Is 25MTTPVIL 1400J I270I PANO] specified, the length of peptide is 9 25 LCRKQLL 4.[ 0 37 HYSLAVTQS I 0.400] amino acids, and the end position 299 ____ ___ _____LG ___37___] _____S1040 for each peptide is the start position F- 991TLDRH [T 8571 KTN1IFVAI ]f 0.400] ____ - .9~L 403][LLISTFHVL Jf4.000] 30I EISFIQSTh t0.0 Strt1 Subsequence Scor 37 I 0 GSGDFAKSL ][ '.00O1 J 1439-11 PSVLDLL 30.400] 173.I QAROOVIEL If100 203] NLPLRLFTL I4.01311TIGYVALLl 1[ 0.4001 214 If GPVAISL 80-000 F 264] ITLLSLVYL If4.000 F 143011 PNFVLALVL J[-0-0o1 259 f L IVIL F800] [36[ STLGYVALL If4001 362 IfSFGIMSLGL If O-407 [28 i TPPNFVLAL.r 80-DOO [2787[ KRRFPPWL 114.0001 r21 71 ARQV 110400 F-378 LPSIVILDL' II4-0- 80.000]l -040 __2___F__WE OOj 317][ VAYSLCLPM IfT Fl 19311 GSLSSAREI JI -. 40] 300f QCRK(LGLL ifr[j S LEC f2003861J LNWREFSFI 104] 125i YPESAEYAl 24.00[05 IPIEIVNKT If2-04i- ] LLRLFTLW i: 177W] QVELARQL ]j20.oo 353] EVREMYl I2.0[429] PPNFVLALV 11 .40 1483 WSAWALQL ]ooo49fICGH f200 18][IPIDL GSLJS -04-001 261f IV~nusL .00 [164_I QVYICSNNI 112.00 01 379]1 IPSVSNALN 11 .40 E75] LVHEA 132000 1 ASLFPDSU fi' o 1 62] NFASEFFII55 [AALI IILDI.LL 3120.00 i [F51 ALVuLPVV1 1_012] RRSERYI.FL I~W I436 lfLVLPSIVIL rf 20.00 075 EIENIPRL 11-1.200_rIT [ Hi %/I VAlVLPSI 4F1 FAKSLTIRL * 81 DALTKTN11 1.200 [253jl EIVNKTLPI 10.400 313[ ANVHVAYSL 2.000 32 1 LPMRRSERY I.2F [1063-1HLGI .0 F133][ LASLFPDSL 31200 18-1 LVGKILIDV 11 1.____________ I 5]1 SMMGSPKSL 31120001 F35871f EMYJSFGIM L1I.i If TableXVIl.-V2-IILA-B7-9mers. i F27][ DARKVTVGV3 6000W 112jj I DSN 1.000 98P4B6 I 100~ 1I SLWDLRHLL Hf 6.10 I TLPiriIV1.0Eahppiesa portion of SEQ IDJ I ~§ NWAWL314001 23 fFRDIP I N:5eAMhstr position is I 174 specified, the length of peptide is 9 Start Subsequence core plus eight. amino acids, and the end position fLFW 00 Start Subsequence for each peptide is the start position RP jj Ii GI plus eight. Str |Subsequence Score [3 | SPGLQALSL 8 LFTFWRGPV 00 0430 PHVSPERV 0000 35 I PPCPADFFL 8000 ILGKIILFL _15 _1_SGFTPFSCL _ [ii NLPLRLFTF 0.020 IL SGSPGLQAL 4.00 [311 PLRLFTFWR 0.010O 45 HVSPERV1V I1.500 __400_0_P! 0010 J 46 VSPERVTVM 1.000 17-i FTPFSCLSL J4000 5 i GLQALSLSL 4.00 0 - .3___ 04 J25 LPSSWDYRC 1 2.000] 4 SIVILGKII .0.400 37 ICPADFFLYF 0.400 el3 5H..IL 1 ClSRKLKRl 0.400 33 CPPPCPADF 98P486 KIILFLPCI 0.4 33 CPPCAD IEach peptide is a portion of SEQ ID15b.0 8 _TPFSCLSLP ]FO.JL0O0 NO 11; each start position is 20jRKK 0 F107] SLSLSSGFT if 0.100 specified, the length of peptide is 9 I38 GIGGTIPHV i0.200 [14 [_ SSGFTPFSC 0[100 anino acids, and the end position 2 L.. IILGK 0.2W 7~ ALLSLS ~u~ each peptide is the start position 18 jIISRKLKRIK If0.100 [7 iQALSLSLSS:] ||u 0.060 34 i PPPCPADFF || .u0se 60ore S0 8 |f ALSLSLSSG 24 FVFLLTLLL 20.3 0FLPCIS 0.030 23|| LSLPSSWDY || 0.020 | 14 AD I__ ] ]__ _ 0. 12= | SLSSGFTPF ||1 19 ELEL 111.200 F IG9V1 0.020 21 I SCLSLPSSW || LEFVL 1.200 F-67 VILGKIILF [02 6 |LQALSLSLS ||0.020 | 24 RKKGW 0.020 13 LSSGFTPFS ||23[ EFVFLLTLL .400 j-21][ GW .020 _ | GSPGLQALS j 0.020 | 22 [ LEFVFLLTL 04 --- I 20~~] ~ J LELEFVFUL .40 F40 [T GIPCIS 0.015 9T i LSLSLSSGF 0.020 |0 FCSFADTOT 0.100 j LE2 11 0.012 20 || FSCLSLPSS 0.020 | 871 QFCSF 0.100 EQIGGTI 0.010 [3232 RCPPPCPAD 0.015 | [ ] FtQIFC. 37 2 IGW 1 0.010 22 || CLSLPSSWD | 0.015 |7 QTELELEFv 02 LKIIF I00 3_1 j YRCPPPCPA 21 ELEFVFLLT 0.10.030 ____ 30 | DYRCPPPCP 1 0.015 |032 SOFLEEGIG 0 [27_ SSWDYRCPP || I TQTELELEF 0.020 141 GTIPHVSPE 0.010 29 i WDYRCPPPC |1 | WREFSF10 n . 1 1 VLPSIVILG if00010 24 SLPSSWDYR ||010 11 CSFADTQTE 0.10.010 IPE 1Li| LSLSSGFTP ||010 3] EFSFIQIFC 0.010 KGWEKSQF .010 36 PCPADFFLY 7 IQIFCSFAD 06 SK(K J(]F 0.002 16 GFTPFSCLS || 0.002 511 DTQTELELE 0 SR VT r 4 PGLQALSLS | 1.I FAD.OTELE 0.00.009 02 I EG T f0.01 26 PSSWDYRCP |6 0.00 I2-8 I1 SWDYRCPPP | 1.00 20 WKLEE |1 9 PFSCLSLPS ||TELELEFVF 29 F TbeVl-V$A.HLAB7-9mes = Ljf ICSFADTQ 0.001 ___ 25 KGWEKSQ ]I OMT 98P4B6 jalXllV-LAB-res- [F-307 EKSQFLEEG 0. 1001] Each peptide is a portion of SEQ ID ITeV-6 3 I FLEEGIGG NO: 11; each start position is F-23 I1 KRIKKGWEK 0.001 specified, the length of peptide is 9 Each peptide is a portion of SEQ ID0 amino acids, and the end position NO: 13; each start position is F1 _CS K for each peptide is the start position specified, the length of peptie is 9 L2i GWEKSQFLE 01. 000 plus nht amino ads, and the end position for each peptide is the start position 175 TableXVIIl-V7A-HLA-B7-9mers- TableXVIII-V7C.HLA.57.9mers. [ae M-7ILA-87.9ners 98P486 !8P411 9BP4136_I_________________I Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specfied, the length of peptide is 9 specified, the length of peptide is 9 specie, the length of peptide is 9 amino acids, and the end position ano acds, and the end position amino acds, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. ___ _ __ _____ plus eight. [Start || Subsequence I Sce St Subsequence Score Subsequence $[or i9 | FLPNGINGI || 0.400 148 SLAFTSWSL Fl-2i[ LPHTNGVGP 1f0.200 1] |SPKSLSETF || 0.400 1 871 KSKHCMFSL 4 187 ][ C AN 110.180 | 6||SETFLPNGI 1 0.040] 29 1 RGGLSEIVL 4000 F g][ E S 0.i | 2 || PKSLSETFL ||0.040] 1 FKSQA 164 | 7 ETFLPNGIN |0.030 27 [ ILRGGLSEI 4.000 1 AWKCLGANI | 4 || SLSETFLPN | 0.020 |WMKLETIIL 4.001 LWEFLLRLL 0.120 31| KSLSETFLP || 0.0101 15211] GEFL 4.000 1 104 ESPDRALKA 0.100 |5 I LSETFLPNG 160 LGSGWMKL 1.0 EFLGSGTW||.00 8 TFLPNGING .001102 PPESPDRAL 13.600 -1|627ISGTWMKLET h 0.100 5~ 1 TPPPPA-MWTrj 3.00 I169 11 ETIILSKLT Fl0 TableXVll-WB-HLA-B7-9mers- 112 [ AANSWRNPV 2.700I VVTIfQ0.WGW 98P4B6 101 FDPPESPDRA 2.000 1 QEQKSKHCM .100 Each peptide is a portion of SEQ ID 750[ LSTPPPPAM 1 NO: 15; each start position is 144_________-_1-5-_ specified, the length of peptide is 9 -i[ ILDLSVEVL 1.200 111 PVLP F0100I amino acids, and the end position 42 QQDRK1PPL 111.200 3 14371 ASGTLSLAF 0 for each peptide is the start position 134 LLRLLKSQA F 000] 64 If GATAEAQES 110.060 plus eight. 142 AASGTLSLA 0[00 687II EAESGIRN 0.060 S Subseuence LS1coreK FStart Su ue c [Sore -17' AAAWKCLGA ][ 0900 25 I1 ANILRGGLS II0060 I | 971 STLGYVALL | 4.000 1[5 11 S10tisw IF -W | j8]| QSTLGYVAL ][4.000 j1] EVLASPAAA 5 0 -35 IVL 90Wi | 3 i NMAYQQSTL || 4.000 |]GvvTEDDEA 0500 86 VVGITjD0 F-27||LNMAYQQST || 0.300 | Usuvi-Pl If 000 3 IVILDLSVE | 6 1 YQQSTLGYV ][02|002 WKCLGANIL I1 "400] VVTEDDEAQ 020500 7 |' QQSTLGYVA 0.100 168 LETIILSKL 0.400 122 PHNGVGPL0 14 |1 MAYQQSTLG || 0.030 |GTWMKLETI 0400 -76-] NKSSSSSQI 0.040 I[ FLNMAYQQS || 0.020 1 129 PL EFLLRL 0 182 SKH .040 5 | AYQQSTLGY || 0 66 TAEAQESG 1 0.360 39 iEwQQDRKi 0.040 81 SSQIPVVGV 10300 121 VLASPAMAW 0.00 TableXVIl-V7C-HLA-B7-9mers- 57 A If 0.300 62"] EAGATAEAQ 0.030 98P4B6*--I Each peptide is a portion of SEQ ID 11 II PVLHNG 0.300 1 I NG01)30 I NO: 15; each start position is 1_3F specified, the length of peptide is 984 IPVVGvvE 0.200 1 19 ALKANSWR 030 amino acids, and the end position 79 SSSSQIP 02 6 T IAGATAEAQE 0.030 for each peptide is the start position 55 PPIf 0.200 957 IDPP 030 plus eight. -[-Q | Start|| Subsequence I Score I 82 149 65 ATSWSLG 0.030 1 |-] SPAAAWKCL ||80.000 78 | 0.200 149 KAANSWR 03 | 126 || GVGPLWEFL ] 20.000 GI[020S STPPPPAMW 0.030 SGANILRGGL LDLS HCMFSLISG SI ANSWRNPVL 12000 0.200 WEEAGATA .3 | 141 || QAASGTLSL ||2.00 14 I47AGTS 12.0 ~ L IPPLTPP If 0.200]j 156 1f LGEFLGSGT0.3 f17fVGLELLIN 28 1GPLWEFLLR 110[ 0 IN77 1~ TQEQKSKHC 0.030 176 TableXVIll-V7C-HLA-87-9mers- TableXXVI.HLAB7.l0mers. TableXIXVI-HA-BY-10mers. 98P4B6 __ _ __ _ _ 98P486 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ 1D Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is specified, the length of peptide is amino acids, and the end position 10 amino acids, and the end 10 amino acds, and the end for each peptide is the start position position for each peptide is the sta position for each peptide is the start plus eiqht. position plus nine, position pus nine. Start ISubsequence IfSoeI Startj Subsequence I Score I Starti Subsequence IfScore 140 | SQAASGTLS | 0.020 195 LSSAREIENL 4.000 2551 0.600 48 || PPLSTPPPP |0.020 2571 KLPIVA 0600 71 || ESGIRNKSS 0.020 TSIPSVSNAL 4000 125 YPESNAEYLA 30600 123 || HTNGVGPLW 266 LLSLVYLAGL 314.000) 1571 GPKDASRW 0.600 72. SGIRNKSSS 202 ENLPLRLFTL 4.000 227 FLYSFVRDVI 179 EQKSKHCMF |10.020 LASLFPDSL 4.000 821 ALTKTNIIFV 0.600 185 CMFSLISGS | 0.020 24251 RFYTPPNFVL f 0.600 54 PPPAMWTEE I1 QQVIELARQL 4.000 651 FASEFFPHW 0.000 147 || F SWS I 0.020 | 4271 YTPPNFVLAL 4.000 1341 ASLFPDSDIV 1Ii00] 28 LRGGLSEIV 394 IQSTLGYVAL 4 2231 ATFFFLYSFV 0.600 2131% RGPVVVAISL 4.000 269 1LWLAGLLAA Ifo o TableXIX-V1-HLA-B7-10mers- 3651 IMSLGLLSLL 1421 lVKGF 0.500 90P486 49 1 LIRCGYHWI 75 1 DVTHHEDALT1 0.5W Each peptide is a portion of SEQ ID 4281 TPPNFVLALV 4411 IVILDLOIC NO: 3; each start position is 1031 DLRHU.VGKJ 4000 J 409HVUYGwKRA Ej_____ specified, the length of peptide is 10 amino acids, and the end 36 1__110_ __2541 _______ __0_50 position for each peptide is the sta rLtRHL 4.000 1 90 1 FVAIHREHYf jr 0.500] position plus nine. 298 WLQCRKQLGL f 400 375 AVTSIPSVSN I 0.450 Start|| Subsequence | Score RRS ERYLFL LRL 0.400 323 I LPMRRSERYL ||240.000| 3611 ISFGIMSLGL I[ WDL 0,400 197 SAREIENLPL 120.000 2581 TLPIVAITLL IF4000 139 IPSVSANW 438 I LPSIVILDLL ||80.000 172 IQARQQVIEL 4.000 259 LPIVA S I 0.400 9 I SPKSLSETCL 80.000 1271 ESNAEYLASL 4.000 211 LWRGPVWAI IF 0.40 250 || IPIEIVNKTL J 80.000 440 SIVILDLLQL 1631 RQVYICSNNI 11 0.0! 312MVH VAYSL I 36000 |RONFIPIDI I4000! 145 GFNWSAWAL 04-0I 147 || NWSAWALQL ] 20.000] 267 SLVYLLL I 'T5I 1861 NPIDGSL F6-67 314*W{VHV AYSLCL |20000 VLPSIVILDL I[ 4.000 [88 1 IPIDLGSLSS ].0 364 GIMSLGLLSL 1112.000 | 3 QSTLGYVALL LLSLLAVTSI 04 263 I AITLLSLVYL 2 173 QARQQVIELA 219 I AISLATFFFL 1 12.000 43 FVjAjyLPSj fT0001 [161 TCLPNGINGI [ 402 ALLISTFHVL || 12.000 |4(fP ESNAEYL 0 1435 ALVLPSIVIL | | I iALVLPSIVI 31 7 1 NNIAR2VI 0040010 273| AGLLAAAYQL ||i[] 1 .800 12F24.3 | QSDFYKIPI 4 H ISMMGSPKSL 1112.000 j ALNWREFS [ 92 AlHREHYTSL 152.000 6 MAYQQVHANI 1.200 VDVTHHEDAL 1 0.400 277| DARKVTVGVI i 12.0001 | &RM 181 _ LARLNFIPI _)12.000 KILIDVSNNM 1429 HPPNFVLALVL I 8000 26 IVATL% 1.~uiv] ~ TableXIX.V2-A-B3710mers 296 ETWLQCRKQL 0 6000 LGSFFFAM I .00 98P4B6 99] TSLWDLRHLL 276000 AYQLYY GT f 000 Each peptide is a portion of SEQ ID NO:_3N 5; each start position is SN specified, the length of peptide is ___________I 1 01 12391 Y QQSDFY 11 0. 1 U 10 amino acids, and the end 177 position for each peptide is Start[ Subsequence Score] Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID" 34 i PPPCPADFFL 8.000 | NO: 11; each start position is NO: 13; each start position is 14 || SSGFTPFSCL specified, the length of pepde is specified, the length of peptide is 10 210 amino acids, and the end amino acids, and the end position for ___ GSGLQLS II4.00] position for each peptide is the start each peptide is the start position plus 33 || CPPPCPADFF 0.600position plus nine nine. 18 TPFSLSLPS Start fence [Scor.4 00 S e c[ 16 || GFTPFSCLSL F| 0.400 8 FTFWRGPVWJ 0200 3 LPSMLGKI ][ DO 31 SPGLQALSLS || 0.400 3LPLRLFTFWR 46 5.000 [h4l PGLQALSLSL 0.400NLPLRLFTFW 5 SIVILGKIIL 4.000 25 LPSSWDYRCP 0.200 1f LFTFWRGPW 0020 7 FLGKIILFL 4[0001 [30 DYRCPPPCPA] f010Ij ENPLLFTF I0.2 (44] IPHVSPERVT ]300 24 SLPSSWDYRC ][0.100 9 TFWRGPVVA 14 LFLPCISRKL ]0o.100 13i LSSGFTPFSC 0.100 4 PLRLFTFWRG 0.010 J 27][ KKGWEKSQFL 0.400 9ZJ LSLSLSSGFT:] 5 1 1100011 16 -] LPCISRKLXR 7110.200 8 LSLSLSSGF '1 0,0607 4 TIPHVSPERV 11 0..060l E35 PPCPADFFLY | Tabe 5B-HLA7mers 38 EGIGGTIPHV 0.200 F7-1 QALSLSLSSG |I 003098P416 F jj ISRKLKRIKK (0150] 1 15 SGFTPFSCLS | Each peptide is a portion of SEQ 1. 02 0] FLEEGIGGTI 1020] 22R.02 NO: 11; each start position is CLS || 0.00 | ~ CSLPSWD If0.00 I specified, the length or pepide is [.L I LGILLC I( ~*~5 1 ||] LSLSSGFTPF || 0.020 10 amino acids, and the end E6 IVILGKIILF J 0.100 6 | LQALSLSLSS ] 0.020 position fr each peptide is the start II LVLPSIVILG 110050 32|| RCPPPCPADF 0posion plus . 02100 GKIILFLPCI 110.040 F1 SGSPGLQALS |10.020a e e Score - T] PSIVILGKII 0.040 20 I FSCLSLPSSW |0.020 12 CSFADTQTEL 12 || SLSSGFTPFS |14 FADITELEL T 3600] 177 PCISRKLKRI 0.040 5| GLQALSSLS 0.02020 ELELEFVFLL PCIS 0.0 21 || SCLSLPSSWD || 0.015 | ' 2 j ELEFVFLLTL F G V [ 10 SLSLSSGFTP || F231 LEFVFLLTLL 0.115 01| FLPCISRKLK 0F.010 | J7 FTPFSCLSLP JL0010 JW .40 40 IGGTIPHVSP H 0.015 SS2-I WDYRCPPP 11 0.010- 19] TELEEFL 0.400] 12 IILFLPCISR Hf 0.1 LSLPSSWDYR || AIA 24 I 34 QFLEEGIGG0.010 | 28] SWDYRCPPPC || 0.003 1 EE V 0 ] VLPSMLGK 0 36 PCPADFFLYF |f-00-2-18 IQIFCSFADT 0.0020 ] SQFLEEGIGG ][0.010 26| PSSWDYRCPP 0| FSFIQIFCSF 110.020 25] RIKKGWEKSQ .010 31| YRCPPPCPAD || 0.002 16 DTQTELELEF 1 0.0201 [32 j[ KSQFLEEGlG ][ 0010I 29 WDYRCPPPCP |10 FCSFADTQT 0.0 2 13 j[ILFLPCISRK 19 | PFSCLSLPSS | 0000 | ]F _ 2 KLKRIKKGWE 0.010 M 16 1 SFIQIFCSFA ]I0.010 1 8 ] ILGKIILFLP JrIFO1 TableXX-V5A-HLA-B7-10mers. 3 - II 0.010 41][ GGTIPHVSPE I I 98P486 9 QlFCSFADTQ [7178 CISRKLKRIK .010 Each peptide is a portion of SEQ ID 7 FIQIFCSFAD 28 KGWEKSQFLE 0.010 NO: 11; each start position is 11 FCSFADTOTE 0010 42 GTIPHVSPER II 1 I specified, the length of peptide is 10 amino acids, and the end 18 QTELELEFVF 0006 23 LKRIKKG K position for each peptide is the start [ is QTLELE .003 45 PHVSPERVTV 0.003 sition lus nine. 4 EFSFIQIFCS i 0.002 [-2L1KR JI 002 Start Subs Suence FQTELE 1 FWRGPVVVAI IiZ00 10 1ab 0.400 2e XI-VSF 071 s0.002] 6] _RLFTFWRGPV 01 .300SRLRKGI001 17R TableXIX-V6HLA-87-10mers- TableXX.V7C-HLA-B7-10mers. 98P4B6 Table-V7CILAB7.10mers- 981416 ach peptide is a portion of SEQ ID 98P486 Each peptide is a portion of SEQ ID NO- 13; each start position is Each peptide isa portion of SEQ ID NO: 15; each start position is specified, the length of peptide is 10 Na 15; each start position is specified, the length of peptide is 10 amino acids, and the end position for specified, the length of peptide is 10 amino acids, and the end position for ach peptide is the start position plus amino acids, arnd the end position for each peptide is the start position plus nine. aac peptide is the start position plus nine. start ]Subsequence I Score nine. Sa I Subsequence Score 37 EEGIGGTIPH H 0.001 StatS[ sence0Score 178 H[TQEQKSKHCM 0.300 30 WEKSQFLEEG 0.001 F f 0 ]PPESDRAL 1 67 P 29 GVVEKSQFLEE || O.O] 122 LPHTNGVGPL 0.0.000 F L ipwGvvTED 0.200 36 LEEGIGGTIP || 129.01 GPLWEFLLRL 00.001 [i82 SSQIPWG [. - - Lr][M - SWF NPVL I XOO 48[ JIPPLSTPPPP ][0.20 TableXIX-V7A-HLA-87-10mers- GVGPLWEFLL I 20000! [55 ]pppAM F0200] 98P486 ASPAAAWKCL 112.000 1 KSSSSSQIPV 0 Each peptide is a portion of SEQ ID 241 LGANILRGGL W SSSSSQIPW [ 0200 NO:15; each start position is 152 FTSWSLGEFL 4 74 GIRNKSSSSS specified, the length of peptide Is RKPPL I sO TPPPPMWTE ][ __ 10 amino acids, and the end _ _ _ 38 ______ _____ _1_0.2 position for each peptide is the start 160 FLGSGTWMKL 4000 position plus ninVILDLSVEVL 140001 18 AAAWKCLGAN 180 Start H Subsequence | Score | 126] NGVGPLWEFL 1 4.000 1 143 AASGTLSLAF 0.180 2 | SPKSLSETFL 1 I41 SQAASGTLSI 4.000 I 5 PLSTPPPPAM[ 0.150 6I| LSETFLPNGI [ 1191 NPVLPHTNGV 1 4.000.1 |10 S P 9 3 TFLPNGINGI IF 0.040 | 148 1 LSLAFTSWSL 1 4.000 1 FTH STppppAMWT 3 0.50 1 3 GSPKSLSETF 19 0.020 |WKCLGANI 04411 QRKIPPLST 0.50 4 || KSLSETFLPN || 0.020 28 ILRGGLSEIV J-2.0055 - - 12 E 01 1 10]| FLPNGINGIK 10.010 16811 K|ETIIISKI 1T0I 106 SPoRuX.A J i 5 || SLSETFLPNG 1 0.010 | -20 -] AWKGANIL 171200 I 158 GEFLGSGTWM 0.100 8 | ETFLPNGING || 16511 TMKLETIIL 1..01 056 S GT 0.100 7| SETFLPNGIN 0.003 [F1 ATAEAQ 162 GSGTWMKLET 110 :3 |PKSLSETFLP I 0.000 | 411 IVILDLSVEV ]f .0j 887rIVGWTEDDEA F- -351 LLRLLKSQMA 1o000 134 11FLLRLLKSQA ]I0100] TableXIX-V78-HLA-B7-10mers- r-112 I KAANSWRNPV 0.90 138 LLKSQAASGT 98P486 98P49 I 1647 I GTMLTI O40 1177 ILTQEQKSKHC 3 .0 Each peptide is a portion of SEQ ID I LKSAASGTL 0 0.40] 1 SQPWGVVT NO- 15: each start position is 1 1 8311 04 0.0 I specified, the length of peptide is 10 amino acids, and the end position for 76 H RNKSSSSSQI 10.400 116 11SWRNPVLPHT -- 0.0 ach peptide is the start position plus 29 0.400 1___1 LSVEVLASPA 0.100 nine. 1 LPSVILDLS 0.400 3 577 PAMWTEEAGA1 0.0901 Start Subsequence ]Score 130 PIWFLRI 1 0400 iLNMAYOQSTL ||12.000- TJ[LNAY L 120001 F 27[ NILRGGLSEI -rOO 0-4-0 1 ALKAANSWRN I .6 8 | QQSTLGYVAL 4011 GGLSEIVPI 2 0 ] GANILRGGLS4.000 9 || QSTLGYVALL 4.00063 SGTWMKLETIT.400 64 AGAAEAQES ~F07 STLGYVALUI 11 0.400! 1 F82 1KSKHCMFSLI 1 40] 36 1IVLPIEWQQD 0.050 7][ YQQSTLGYVA 10.100! F--4 ASGT-JAy 1 0.300 1) [87 WVGWTEDDE 0.050o r- -1TrNAYOQQsiST il 2 I FIMAYOSTII491011 PPLSTPPPPA 1 090 ' -"' VVTEDDEAQD 10.050 I 6 If AYQQSTLGYV I 0.060 8 SSQIPWGV 10.300 1 GVVTEDDEAQ 5 I MAYQQSTLGY 1 1 AASGTLSLA 150 LAFTSWSLGE 4 || NMAYQQSTLG || 0.010 14 LASPAAAWKC 11 0 1 _12 TNGVGPLWEF . E pe pFNMAp _ _ WTEEAGAT of SEQ0 1 spciie,_helegt1 o 03td isW10 amn 1c79 n h n psto o TableXiX-V7C-HLA-B7-10mers- TabteXX-V1-HLA.53501.Smers- 98P4B6 98P4B6 I9PB 843 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ 1 NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position amino acids, and the end position each peptide is the start position plus for each peptide is the start position for each peptide is the start position nine. plus eight plus eight Start Subsequence || Score | S If S 3 SatSubse uence 96 EAQDSIDPPE | 0.030 196 1 SSAREIENL 750]65 FASEFFPHV 11.200 63 ]| EAGATAEAQE | 0.030 911 SPKSLSETC 6.000 365 IMSLGLLSL IFooo0 26 ANILRGGLSE I 030 |VAYS 84 Q FIPIDL IT.D 15111 LSTPPPPAMW | 0.030] 2 LAAAYLYY |.0] [35 ALNWREFSF 10 169 R EAQESGIRNK I 0.030 1 272 1 LAG 16.000 148 WsAWALQt -1.0001 17 ] PAAAWKCLGA 11 0.030 | 125I YPESNAEYL 116000 1 274 GLLAAAYQL 1.000 1 165 GATAEAQESG 0030 46 TIRLIRCGY 144 KGFNSAW 1.000 116 ANSWRNPVLP || 0.0301 146 FNWSAWAL i.000 6 |1 ILDLSVEVLA IF 0030 395 QTLGYVAL F]383 SNANWREF II.oo 703| AQESGIRNKS | 3 MSLGIISLL r5300] L j QLGLLSFFF].027 147[|| TLSLAFTSWS H 0.020 1 220 5A00 1 ro] 16311 FGIMSLGLL 11.0001 146]| GTLSLAFTSW || 0.020 125011 IPIEIVNKT 40217 VWAISLATF 11.000 -1401 1 KSQMSGTLS 0 112 j ILIOVSNNM r- 007 1 57 IIVIGSRNPKF y 1.000 180 || EQKSKHCMFS 1W . 188 IIPIDLGSLS 14000] 1 31311 AMVHVAYSL I_ 1.00 56[|| PPAMWTEEAG | 0.020 347 NSWNEEEVW 1370 1411 1 LYGWKRAF 1 1.000 145 || SGTLSLAFTS | 0.020 13|3 LASLFPDSL 13000] 137811 SIPSVSNAL 1.TD] 72 ESGIRNKSSS I 0.020 300 CRKOLGLL 3.000 264 j ITLLSLVYL I.5' --2181 VAISLAIFF 13.0001 J i75i1 DVTHHEDAL I 1.000] TabteXX-V14LA-83501-9mers- 177 QVIELARQL 1 436 1 LVLPSIVIL 98P486 303 1 KQLGLLSFF 128000 F I TKTNIIF 11.000 Each peptide is a portion of SEQ ID LSLLAVTSI 2.000 403 1 LLISTFHVL 1 NO: 3; each start position is 12 specified, the length of peptide is 9 amino acids, and the end position 275 LLAAAYQLY T-2000 40011 YVALLISTF for each peptide is the start position 61 RNPKFASEF 1 2000] F258 ILPIVAITI 'I-1.000] plus eight 100 SLWDLRHLL 2 siwiwu. 1.00 Start|| Subsequence ] Score] HPYARNQQS 2.O 5 SMMGSPKSL 1.000 62 I60 ,000 379 IPSVSNALN 2.000 223 ATFFFLYSF 6f 0.000 323| LPMRRSERY 4000 NMRINQY 33 VGVIGSGDF I 157 || GPKDASRQV 12400 306 _ ______.0003____ 259| LPIVAITLL 1120.000| _1 ASL MI 2.000 261 YVAI± 1 428I TPPNFVLAI 20.00000 [ 87'I TPP FVLL 20.0001 I221 11SLATFFFLY 2.00 r'55'] [5 YISFGIMSLIfio] 291 | FPPWLETWL |I 193 GSLSSARI 1100 219 AISLATFFF 20.000 438| LPSIVILDL 263 AITLLSLVY 02.000] 203 00 NLPLRLFTL f 1.00 214| GPVVVAISL |20.000 1 12E 2 NAEYLASLF I 231 || FVRDVlHPY | 12.0001 37I GSGDFAKSL |0 1 ,3581 EMYISFGIM 112.] 12 ESNAEYLAS 457|| ISTFHVLIY 10.000| 271 DARKVTVGV 1.800 [3861 LNWREFSFI 0.600 204|| LPLRLFTLW |10.0 0 IVILLQL .T5'] 4ij 239 [| YARNQQSDF 9000 161 ASRQVYICS I .5 416 RAFEEEYY I41| FAKSLTIRL || F GSRNPK F ][5.00 328 SERYLFLNM .600 173 QARQQVIEL |OO |71 FIPIDLGSL 9. | KYRRFPPWL E 51~i TSWD..H ___]IF ATK'I [.024F GIKDARKVT 10.6001 180 ___________________NO: 11; each start position is Each peptide is a portion of SEO ID TableXX-V2-HLA-B3501-9mers- specified, the length of peptide is 9 NO: 13; each start position is 98P4B6 amino acids, and the end position specified, the length of peptide is 9 Each peptide is a portion of SEQ ID or each peptide is the start position amino acds, and the end position NO: 5; each start position is Plus eight or each peptide is the start position specified, the length of peptide is 9 Start [~bjeuence JI score plus eight. amino acids, and the end position LPLRLFTFW Start Subsequence Score for each peptide is the start position I LPL - 46 VSPERVTVM II plus eight. [.E] 1.000 S 4 Star Subs uence Score] FWWRGPW 0.200 27 _________ 40 7 || CPADFFLYF | 40.000 33 || CPPPCPADF | 20.000 LFTFWRGPV 0 KSFLEEGI 3 i SPGLQALSL RLFTFWRGP 21 KLKRIKKGW 3000 F23 | LSLPSSWDY 8 |oooo] _ _0.0 14 FLPCISRKL 1.000 9j LSLSLSSGF |5.000 |3 PLRL VILGKIILF 1.000 L-4 LRLFTFWRG 0.00 51 IVILGKIIL .0 35 PPPFFL || 2.00 PPPCPADFF [ ]1 ILGKIILFL 2.000000 345 Hf LPSSDC IDF ___0 TableXX-V5B-HLA-B3501-9mers. 107I tLFPII 0.800 F251 LPSSWDYRC ||2.000 |846-2-1-IKWK .0 15 SGFTPFSCL T| 1.000KGEK 00 I_ 571 _______ F-,_0_ 07 Each peptide is a porton of SEQ 15 17 IICISRKL<RI IFO0400] I SGSPGLOAL |F|!90I NO: 11; each start position is 4 SIVLGKII I _12 H SLSSGFTPF I specified, the length of peptide is 9 45 10f3000 S5 7f GLQALSLSL || 1.000 amino acds, and the end position 1771 FTPFSCLSL ||1{A0j for each peptide is the start position 2 KKGWEKSQF 1 0 plus eight. -2 IfLPSIVILGK IFO--0 20 || FSCLSLPSS | 0.500 | i tar I Subsequence 15 LPCISRKLI I Fo 2 GSPGLQALS I TTELELEF 2.0001 13 LSSGFTPFS 0.001IS3 IGTII)0.0 73[SGTF 1f00 24 H FVFLLTLLL 0f 1.0001 3I PSI VILGKI If 14][ SSGFTPFSC || 4 FSFIQIFCS = 1 ISRKF(RI -507 21J I SCLSLPSSW 0.500 ELELEFVFL I 7 1|201 SFADTQTEL I| 0.300 ] 1 IILFLCIS I.100 36 i PCPADFFLY [.| W TELELE.3VF 0 r-187| TPFSCLSLP || 0.20 0 18 6~~ TPSCLSLP 20020 11I LELEFVFLL If0.200 1 r-81 LGKIILFLP IF 03 0 LQALSLSLS |0.100 | REFSFI 0.200 1321 SOFLEEGIG 10.015 10 || SLSLSSGFT ||. EFFLLI 0.100 1 5 LEIGT [| 27 || SSWDYRCPP 0.100 | 2 0 -00 3 EGGT 1.1 -- 10-1f FCSFADTQT ]f'o67 101 3711 EGIGGTIPH I[O 01 1 ||LLSFP 0.050 | 4 1 lCFDTI-.- F32 | RCPPPPAD || 0.00 |F GTIPHVSPE F -oi5 8 ||CALSLSLSSG 0010 | EFVFLLTLL 0. 401 GGTIPHVSP 0 22 || CLSLPSSWD 0.010 6 FIQFCSFA 1 ] 1 F ILPSIVILG 0.010 29 g ~SWDP 0.010 14T~ ADTQTELEL 1 0.100I F79 1 GKIILFLPC r TO -1 2E WDYRCPPPC 0 SFIQIFCSF 00 121 ILFLPCISR IF 0 24 || SLPSSWDYR || 0.010 1T17 OTELELEFY r1421 TIPHVSPER 0-10 F 31 || YRCPPPCPA I 0010 I CSFADTQTE 033 QFLEEGIGGf 0.003 ____1 21PLASSI ai ~ -I ELEFVFLLT If 0.030 1 F29 11 WEKSQ FO 0003 4_ 1 a AL L 0.010 -1 16 _G C 0.010 1 1 DTQTELELE 11 0.01 1 r-2K5ES I01 30 DYRCPPPCP ) 0.003 ___ ______ ~ .F 1 IQIFCSFAD ][0.010 i-I 7 SRKLKRIKK 1f 0.003 19 ||PFSCLSLPS || 0.001- | 28 9 F C P S 0 0 H EFSFIQIFC 0.010 S D R |RKLKRIKKG 281 WYRLP 13 11 FADTQTELE 0[.009 1-2311 IKGE If- 0 0 I fIFCSFADTQ- If00 r144 If PHVSPERvTI 565 TableXX-V5A-HLA-83501-9mers- F_113 If LFLPCISRK 0.001 1 Eah id 1i5aonofSE6 I TableXX-W6HLA-B33501 -9mers- 30 IIEKSQFLEEG If '--il forj~ eahpetde is th starto position I 98P486 I 116 11 PCI SRKLKR 1f1W51 181 TableXX-V6-HLA-B3501-9mers- specified, the length of peptide is 9 TableXX-V7C-HLA-B3501.9meas 98P486 amino acids, and the end position _ _ _ _ _ _ Each peptid ispid as porio ofar SEsitiD ]Each peptide is a portion of SEQ 1D oeahplud s thetatpsio Each peptide is a portion of SEQ ID NO: 13 each start position is NO: 15; each start position is specified, the length of peptide is 9 Start Subseence [ or: specified, the length of peptide is 9 amino acids, and the end position 181 KSKHCMFSL amino acds, and the end posit for each peptide is the start position So each peptide is the start position plus eight. F plus eight. Str j|Sbequec || Score |nc star. Subse uence [~wre I i. i SQAASGTL 10.0001 Start J SuSqe c oe 36 | EEGIGGTIP ||0.001 |S M70 42 ] QQDRKIPPL 28 GWEKSQFLE TSWSLGEFL 5.000 ___ ___ __ II ASTSLF 5.000 7~ AAAWKlCLGA 0.0 TableXX-V7A-HLA-B3501-9mers- 1 4.50 1421 ]MSGTLSLA 0 98P486 | 101 FDPPESPD] 4.000 128][ GPLWEFLLR Each peptide is a portion of SEQ iD F I EQKSKHCMF ID3.000 1 1 ]MWKCLGAN N:5each start position is F17_F-0 NO: 15; *ahsatpoiini 24 IfGANILRGGL 5 .00I ILDLSVEVL II 0.300]1 specified, the length of peptide is 9 I141f QMSGTLSL 136 RLU(SQMS 0.20 amino acids, and the end position LKAANSW 38S00 or each peptide is the start position F82 QPVGV plus eight. 29 2.00 47 1PPLSTPP rt lr SubsequenceIf Score1 52 1 TPPPPAMwI IF2.000 5 0.200 SPKSLSETF | - 27 LRGGLSE 9 ||FLPNGINGI || 0.400o |.0 _ _ _ F L t G I G F 40 0 ] .i I 1 S S S I V ] 1 0 ]1 2 9 If P L W E F L L R L 0 . 0 4 || SLSETFLPN || 0.200 | 3l] KSLSETFLP | 0.150 ii13i ANSWRNPVL 117 RNPVLPHTN 704 ETFLPNGIN .1 2 SLSV 0.200 6 SETFLPNGI 1601 LGSGTWMKL 1.000. |I EFLGSGTWM 0.200 I5 |j LSETFLPNG 2 0.0151 VGPWI [ 1 2 j1 PKSLSETFL | 0.010 79 I SSSSOIPW 10 - 8 IPVVG ]VT 81] TFLPNGING || 0.001 1 SLAFTSWSL 1 571 AWTEEAGA _________-151 FTWLE 1[ 1.000 17311 L~LQ7K]-.5 TableXX-VB-HL[0A-133501-9mers- I7 j 98P4B6 81 SSOW Pf ] GWTEDDEA 0 Each peptide is a portion of SEQ ID 31 GLSEtVLPI 0.800 19H ______ 0.2 NO: 15; each start position is 154 WSLGEFLGS FO0750 - I specified, the length of peptide is 9 '102 - DSIDPPESP 0.100 amino acids, and the end position 1451 GTLSLAFTS 0.100 for each peptide is the start position 112 AANA WRNPV I[ 83 QIPVVT 0.100 I plus eight. 105 SPDRALK -8 LSW.ASF -0100 Start || Subsequence || Score 6 EAQESGIRN I 00 18SKL 0.100 18 11 QSTLGYVAL I 5.000 7171 STPPPPAWW 0.50 1 |ISKLE1.0 9 || STLGYVALL | 1.000 147 LSLATSWS j F W 3 I| NMAYQQSTL 11.000 146 TLSLAFTSW o-soo] 1611 S LO 010 6 YQQSTLGYV ||12 VLASPAAAW 0..20 01 |V LS J100 F5-|| AYQQTLGY ||0.200 | :: Isf YQSTGY1 _020 71 ESGIRNKSS Ifoo]72I SGIRNKSSS 0.0 7 I QQSTLGYVA || 0.100 123 TNGVGPLW I SGTLSLAFT 0.100 1 || FLNMAYQQS 14 ASP.0AWKC0 140 SQ SGTLS 271 LNMAYQQST |1 64 GATAEA1ES 0450] 7 KSSSSSQIP 0100 4 || MAYQQSTLG |6 0.030GTWMKLETI 185 CMFSLISGS 0.100 _____________37 1~~ PIEWOQOR R2040] __ WKCLGANIL 0.1005 TableXX-V7C-HLA-83501-9mers- 4 jI V1LDLSVEV j 0.400] 95 EAQDSIDPP I1 0.0601 98P4B6 6( TAEAQESGI ][ 0.60 ;11 KANRN I I 006 Eforach pepe is portionofSEQ I LLRLLKSQA iti NO: 15; each start position is -r S uRNKSSSSSQ 182 TableXX-V7C-HLA-B3501-9mers- TableXXI-VI.HLAB3501.lomers- TableXXI VI-HLA-83501-10mes. 98P4B6 1 98P4B6 I 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide isa portion of SEQ ID NO: 15: each start position is NO: 3; each start position is NO 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position amino acds, and the end position fo amino acds, and the end position for for each peptide is the start position ach peptide is the start position plu ach peptide is the start position plus plus eight nine, ____ nine. sital su ~tce's Start I Subsequence ][Score [St7r Subs uence IfScore Start fSbsqee Score 59|| WTEEAGATA | 0.060 127 ESNAEYLASL 5[000 49 LIRCGYI 1.200 1 | PSMLDLS ||4 ISMMGSPKSL .0434 LALVLPS 1200 80 SSSQIPWG || 0050 1 F 382-1 VSNALNWREF LASLFPDSLI ] .20 157 LGEFLGSGTW jL0050_ 37 15][GELSGW 105] 771TSIPSVSNAL ][~ 243 GIKDARKVV, [1.200 33 SEIVIPIEW 0[.os 1 04281 TPPNFLAV 4.000o [-241][ RNQQSDFYKI 1.20 161|| GSGTWMKLE ||0o50] 188 IPIDLGSLSS 32 TVGVIGSGDF I.OO _114_J| NSWRNPVLP 0.050 KILIDVSNNM .. 76 1 NKSSSSSQI 0.040 181 LARQLNFIPI 3.600 273[ AGLLAAAYQL r11.000 1641| TWMKLETII 00407 36 IGSGDFAKSL 1821| SKHCMFSLI | 10040 FAKTIR 1 F391 iiIEWQQDRKI ] 0040 [384 NALNWREFSF _03.000 4 0] IGSRNPKF I11.000 5 MWTEEAGAT 0.030 312 FAMVHVAYSL 3.000 1 1.000 89 |WTEDDEAQ 0.030 222 LATFFFLYSF 30 o296 JETWLQCRKQL lII 000 - [111DATKTNIIF IJ3 4-3]1 KSLTIRLIRC 11 1000 TableXXI-V1-HLA-B3501-10mers- 218 VAJSLATFFF 3.000 2 ENLPLRLFTL ji-ooo 98P486 322 CIPMRRSERY 1 14711 NWSAWALQL Each peptideis a portion of SEQ ID 2 PPNF 2000 F217 VWAISLATFF 1 NO- 3; each start position is 1 specifed, the length of peptide is 10 amino acids, and the end position for 61 I RNPKFASEFF 2.000 132 YLASLFPDSL each peptide Is the start position plus 257 KTLPIVAITL 34 GJMSLGLLSL 1.000 nine. 1259jjLPIVAITLLS 200 1386571 IMSLGLL [19.00 [Start Subseuence Score F l A 1.... I I RCG I F 250o0 92 AIHREHYTSL IFTRDooo 157 || GPKDASRQVY 1240.000| 275 LAAAYQLYY 2.0 ] 314 MVHVAYSLCL .000 9 SPKSLSETCL i 60.000 274 GLLAAAYQLY 2410 |VYGWKRAF 1.000 [ 250 IPIEIVNKTL I 40.000 303 KQLGLLSFF - 299 LL 197| SAREIENLPL j 27.0001 128 SNAEYLASIF 2.000 394 IQSTLGYVAL 1.0o0 323_jl LPMRRSERYL | 20.0001 123 NQYPESNAEY -01 KSLSETCLPN 1.000 438|| LPSIVLDLL 15Ol 305 LGLLSFFFAM 02630 AITLLSLL 1 2391| YARNQQSDFY 1118.0001 404 USTFHVY 112000] [1 1 1.000 4171| RAFEEEYYRF 118.0001 213 RGPVAISL 219 AIS.ATFFFL 1.000 379 IPSVSNALNW 110.0001 271 |YAGUAAAY 2000 298 WLQCRKLGL 11.000 116 If VSNNMRINQY TO 10.000 1831 RQLNFIPIDL 2000 3 [ GSGDFAKSLT 0..000 391 || FSFIQSTLGY || 1.GP00 | 4021 AUISTFHVL -220|| ISLATFFFLY |100 1 [ ASLFPDSLIV 28 TLPIVAI S195 || LSSAREIENL 1|i| 440 S7l.0 10 [4270 Y1 [1371 FPDSUVKGF || 60 | 0 0327 | RSERYLFLNM || 139.000IVKG NV| F 2672 | VATLLSLVY || 6000 1611 ASRQICSN 4371 VPSIVILL .00 361 ISFGIMSLGL || 5.000 | 85 T KRHLLGK 2h6 - 395 O STLGYVALL ||5.000 | 0 LHLVK .0 35 T MAYQQVHANbX - TableX51VZ-HLAmB3501esmers ____ t L 1500 2 j VNKTLPIVAI 98P4B6 971 SW H fa] [ad peptide is thea staron of SEQ ID 183 NO: 5; each start position is Start Subsequnce Score amino adds, and the end position for specified, the length of peptide is 1 ENLPLRLFTF 1.000 ach peptide is the start position plus 10 amino acids, and the end nine. position for each peptide is the start W Start Subsequence Score ___________plus___ .I6 RLFTFWRGPV IFO.400] _______ Start Subsequenice IIScore]8I FTP WRGP VVV 1f0.200] F31 LPSIVILGKI 3[ 8.900 J33 CPPPCPADFF 20.000LRLFTFWR 0200 35 PPCPADFFLY || 6.000 10 FWRGPA j[0.1201 T HVSPERVTVM 14 SSGFTPFSCL 5.000 7 LFTFWRGPW 1[.020 11 LSLSSGFTPF 5.000 9 f TFWRGP.0VA0 01 r flF VILGKIILFL 1.00 2 GSPGLQALSL 5.000 4 PLRLFTFWRG I L[ SMLGKIIL 1-000 20 FSCLSLPSSW 2500 5 RLFTFWRGP 00 F-97 IKKGWEKSQF 0450 34 PPPCPADFFL 2000 F- LGKIILFLPC -'*SPGLQALSLS 1-2_.0700 TableXXJ.V5-~L A3501-lomers- 35 ][FLEEGIGGTI 1020 22- 9P46 r43 ]TIPHVSPERV C P0200L W ~T RCPPCADFj ___ Each E peptide is a portion of SEQ 10 1 i] KIILFLPCIS 10.200 I_4 32 || RCPPPCPADF | 2.000 0 |MP U TPSCSLS] -NO: 11; each start position is 27 II KKGWEKSQFL 0.200 18 TPFSCLSLPS |2.000 |3 " Specified, the length of peptide is - 38MoGGTIH .0 8 ALSLSLSSGF ||0 ] 10 amino acids, and t end 9 || LSLSLSSGFT 0.50 position for each peptide is the str0 D13 || LSSGFTPFSC 0.500 |siion nine. 25 11 LPSSWDYRCP I Score 0.150 4 I PGLQALSLSL --i ISRKLKRIKK .1 | [ 15 I SGFTPFSCLS || 0.100 | 5 FSFIOIFCSF 5.000 J39 GJGGTIPHVS 27 SSWDYRCPPP || F 1-671JDTQTELELEF 0.1 00 141 LFL CSRKL 110.1001 16 | GFTPFSCLSL ||_4_ FATELEL 1.900 (2131 RKLIRIKKGW 0.100_| :6 - LOQALSLSLSS |I 1 T7 0.600] I 3 RIKKGWEKSb.1i00 1 SGSPGLQALS |-227 ELEFVFLLTL [ 022 ] KLKRIKKGWE .01060 I 24 IJSLPSSWDYRCI0100 J QTELELEFVF 1 0.300 GKIILFLPCI 0.04 I36 11 PCPADFFLYF FI010 [0if-7 ELELEFVFLL I[ 0300]D ~ [KWKSFEI 00 519 GLQALSLSLS || 0.10[ |E1E77 PIS rLKRI ir 12 || SLSSGFTPFS 0100 NWREF 0 ___ [LSPSWY j [ ] IQIFCSFADT 0.10 24h5 1__ KRIKKGWEKS f0.020 23 || LSLPSSWDYR || .5 |1 LEFVFLLTLL F]347 QFLEEGIGGT 17 |1 QALSLSLSSG ||0.630- r--1 F 307 DYRCPPPCPA _0.030_ 24 EFVFLLTLLL 0.100 33 11 SQFL.EEG 0 17][1 2TFCLL j0.12WREFSFIQIF 0f .0M0 1 F13[ Ij.LFLPClSRK j0.010] 17 ||FTPFSCLSLP ||001 SLSLSSFTP ]-3io 3]REFSFIQIFC IFl-81] CISRKIYRIK 10.010] 10 1 SLSLSSGFTP 1 0.01 |.....8 ___If SCSPSD1 21][LELEFVFLLTf] 8I 1.[ ILGKIILFLP 000 21 SCLSLPSSWD ||D0O M6fSWDRP~ 0005] FCSFADTQTE I0.1] 2]FT~ VLPSVLGK 0.1 26 || PSSWDYRCPP || .005 | 2 SWDYRCPPPC 1-5] [FCSFAOTQT 10010 F-40 71 IGGTIPSP 0.0103 7 LRCPPCPJL0.001 1 FLPCISRKLK 0.010 I19 i1 PFSCLSLPSS IFO00 1__ 4]I EFSF QIFCS 0.10 1FI GG1PHVSPE0.1 31 5YRCPPPCPAD r[oa 97] QFCSFADTQ 1 0.010 1F1 1 LVLPSIVILG 0.0 F-6I SFIQIFCSFA 0.010 r14-21 GTIPHVSPER [00710 _____________ 13IfSFADTQTELE 0.002 12 1 IILFLPCISR 110010 ableXXI-V5A-HLA-B3501-10mers- ADTTElElE 0002 PHVSPERVTV 0003] 98P486 SRKLKRIKKG 0.003 Each peptide is a portion of SEQ ID L 30 1 WEKSQFLEEG 0.003 NO- 11; each start position is TableXXI-HLA.B3501.lomers.] 1 23 I U<RIKKGWEK 00 specified, the length of peptide is 10 98P416 ] -3771 EEGIGGTPH 0 amino acids, and the end position for Each peptide is a portion of SEQ ID ach peptide is the start position plus NO 13; each start position i GWEQLEE 11 0.00 nine, I specified, the length o peptide is 10 21 r 1S T abIeX-VCXHLAXB35-1-Amers- 10aboX-V7CHLAB3501-1-mers Tabl, 9-V7A-HLA350 Omers- 98P46 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ 1 [ NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is amino acids, and the end position for amino acids, and the end position for 10 amino acids, and the end each peptide is the start position plus each peptide is the start position plus positon for each peptide is the start nine. nine. position plus nine. Subseuence Subseuence Score] |Start[ Subsequence i Score] LWEFLLRLLK Sco DDEAQDSIDP 0.022 2 SPKSLSETFL VTEDDEAQDS 12 E 1 | GSPKSLSETF i 5.000 F-107 SVEVLASPAA 1 ] 4 H IVILDLSVEV 0.020 4 i KSLSETFLPN 1.0001 sTPPPP~ywr | 1-5 17[ ILSKLTQEQ 6 || LSETFLPNGI J 0.600 6 6 1 ILDLSVEVLA [1.000 7 KIPPLSTPPP 02 9 i TFLPNGINGI 10.040] I168 KLETLS J o._6 oJ 7113 |0.020 _5| SLSETFLPNG || I 103 ] PPESPDRALK 0.9 72 ESGIRNKSSS 10 || FLPNGIN lK i 0.010 | fly][ LPNINIK f 0101 Ii~TJ~GVGPLWEFLL 0.5g] 43[ QQDRKIPPLSJf01 7 || SETFLPNGIN 1 .i01 I143 I MSGTLSLAF ]15 1 ASPAAAWKCL [0015 8 || ETFLPNGING | 0.010 | 1 V.ASPAAAWK F 1-4 0[ KSQMSGTLS I 3J| PKSLSETFLP 0.00| | 5171 LSTPPPPAMW [ 9 F LSVEVLASPA 0.015 1-6011j WTEEAGATAE ][o2282~T SSQIPVVGV 110,015 abe)U- --1-A135 1r F157 11 LGEFLGSGTW] 1r0.2 1 5 [iss] WSGFLSG][q 1 0.015 ableXX-VBHLA-B35 s EAQESGIRNK ESPDRALKAA 01-.10 98P46 __ _________ _ Each peptide is a portion of SEQ ID [01 [..] LS 15o NO: 15; each start position is [7011 AQE 1 [ 4? 1 HTNGVGPLWE I specified, the length of peptide is 10 [i178I1 TOEQKSHCM ]j 0.35] 1 29J[ GPLWEFLLRL 0.13 amino acids, and the end position for 5i70-11 ETIILSKLTQ I F[171 -- GGLSEIVLPI F03 each peptide is the start position plus 128 I VGPLWEFLLR 11 0.125 145 H SGTLSLAFTS J 0013 nine. __3_7_11 ______________ Start I Subsequence || Score |ID 100 r 1 [[ F51| MAYQOSTLGY | 6.00 LASPAAWKC] SLAFTSWSLG .01 9 | QSTLGYVALL |F5.000 F61 0AQESG __ 3 IF LNMAYOOSTL 1.00 39 PIEWQQDRKI I 012-1 MNSWRNPV][ 0.010 8 || QQSTLGYVALIJr j0-J (162 11 SGTWMKLET |F1|42-1 QAASGT10SLA0] F 10 STLGYVALLI 0 KSSSSSIPV J GANILRGGLS 010 7 | YQQSTLGYVA 159 EFLGS 2 |FLNMAYQQST || 0.10 [|22 KCLGANILRG 0 0G 6 || AYQOSTLGYV || 0.020 167 MKLETISK II 0050 ] RALAAS-W|R IF0010 4 4 | NMAYQQSTLG I 0.010 | ] I EWQQRK1 0.0[ [ KLTQEQKSKH 1 || LFLNMAYQQS |1i| 80 I pwG f-3571 E.VLPIEWQQF.01I0| F79 I SSSSQI PW F0001751]. SKLTQEQKSK 0.1I JTableXXl-V7C4iLA-B3501-10mers- 8 SQIPWGVVT 1 0 11 AAAWKCLGAN 0.010 98P486 F144 ASGTLSLAFT 136 IAE = 0.010 Each peptide is a portion of SEQ ID 1 81 S0 F-E 0010] NO: 15; each start position is [ 1ILS L 0 specified, the length of peptide is 10 F 1 E E 1 0 1 F 0 SLGEFLGSGT 0.010I amino acids, and the end position for _-66 ___T I each peptide is the start position plus 152 E 02 LPHTG 0.1 nine. F125 TNGVGPLWEF 0.025 147 TLs S Start Subsequence Score | 92 TEODEAQOSI 0.025 F GvvrEDDEA0.00 100i SDPPESPDR ||100.000 | -177 LTEQKSKHC 0025 153 1 TSWSLGEFLG 000 67 TAEAQESGIR 1 9.000 1 21 WKCLGANILR 0.025 1 2 IPSI VILDLSV o.oos 3 LSEIVLPIEW 16750 1 106 SPDRAAAN bl0.025 141 e -SQX 7SGCASL 185 TableXXI-VTC-HLA-83501-10mers- Table Vll.V13-HLA.A1.9mers. [51 QEQKTKHCM 98P486 98P4B6 Each peptide is a portion o SEQ ID Each peptide is a portion of SEQ ID Table VlllV-HLA-Ai-gmers NO: 15; each start position is NO: 27; each stat position is 9BP466 specified, the length of peptide is 10 specified, the length of peptide i EQ amino acids, and the end position for amino acds, and the end position Nach sa portion I each peptide1isethe start position plu each peptide is the start position plus for each peptide is the start position specified, the length of peptide is 91 nine. pu ih ____ nin. -pluseigh -,amino acids, and the end position Start I Subsequence If S Srt Subseuence for each peptic is the start position 150 || LAFTSWSLGE | 0.005ETFLPNGIN F[ 025 lusiht 17 PAAAWKCLGA || 0.005 | 10i] IDPPESPDRA 1 1 FLPNGIN 0.010 2 LFLPCISQK 151 If AFTSWSLGEF IF 0.005 Z[.. 117 1 WRNPVLPHTN || 0 | SPKSLSETF 1 0 PCISQUR 0.050 42 ]J WQQDRKIPPL |f 0.003STLNI f001 _ PCSKK Ifoo 104 I PESPDRALKA IF 0.003 1 PKSLSETFL 11 F70 - ISQKIJRIK 110.030 24 || LGANILRGGL || 0.003 |8-1 sQKLRIKK -55 119 i NPVLPHTNGV | 0.003 Table VlI-V14-B1A-A1- I FLPCIS 0.010 118 i RNPVLPHTNG 9mers-98P4B6 M I CISQ. |R [0010 102 || DPPESPDRAL |Each peptde is a portion of SEQ ID QKLKRIKKG 53 H TPPPPAMWTE - NO: 29; each start position is _____ If ____________ II!specified, the length of peptideis 9 _____________ 1 | LPSIVILDLS || 0.003 1 amino acds, and the end position Table IX.VB.HLA.Al10mers. eac peptide is the start position 9894P6 Table VIII-V8LAAl-gmers. plus eight Each peptide is a portion of SEQ ID 98P4B6 IStaril Subsequence NO: 17; each start position is Each peptide is a portion of SEQ ID I I NLPLRLFTF 11 0. j specified, the length of peptide is NO: ~ ~ ~ ~ ~ i 17; eahsatpsto i -7 IWG 10 amino acids, and the end NO: 7; achstat psiton s 7II TFWGPV i~____ I position for each peptide is the star specified, the length of peptide is 9 3 PLRLFrFWR 3[ O Ipsition pus nine. amino adds, and the end position for each peptide is the start position 1 plus eight. 6 I LFTFWRGPVJ 0.00 F Jj GGI 1 0.900 Start Subs uence [ _Sco 471 LRL G KSQFLEM If 0.15 4 i FLEEGMGGT 2 1 .0 LPLRLFFw 15.55 3 SQFLEEGMGG 0007 5s 31 LEEGMGGTI 0.045 9 |JFWRGPVVVA M r [EGMGGTIPHV 0005 1 || KSQFLEEGM 0.015 TFWRGPVVV . M G IPHVS 0.005 71 i EGMGGTIPH | 0.01 3 6 3f LEEGMGGTIP II D 83| GMGGTIPHV ||l0.010 |VilIV21-HLA-AI-9mers- 711 EEGMGG11PII 0.003 9 i MGGTIPHVS 0.003 98P4B6 3 31 QFLEEGMGG || Each peptide is a portion of SEQ ID 1 1 EGGT|PH 000 NO: 43; each start position is ll GTPVPI .0 2 SQFLEEGMG ]specified, the length of peptide is 9 1 EKSQFLEEGM 0.001 6 J EEGMGGTIP 0.000amino acids and the end position reach peptide is the start position Table IX-V1-HLA-AI-l0mers Table Vill-V13-HLA-A1-Smers- plus eight. 98P486 98P4B6 Statl Subsequence I Score Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 2 KLTQEQKTK 1 0200 NO: 27; each start position is NO: 27; each start position is 4 0.1351 speiffed, the length of peptide is specified, the length of peptide is 9 31LTQEQKTKH j 0.025__ 10 amiuno acids, and the end amino acds, and the end position 8 K F-0--0-13-1 position for each peptide Is the start for each peptide is the start position 6 'I _ 0.01 position plus nine. plus eight. Subs uence Score Start I Subsequence i Score 9 TKHCMFSLI 6 11 LSETFLPNGI 1.350 5 LSETFLPNG 2 1 SKLTQEQKT 01 FLPNGINGIK 0.200 I4 SLSETFLPN 0.050 7 QKTKHCMFS jj00 ETFLPNGING 0.125 186 98P486 EKKHCMFS 0.001 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 6 QKTKHCMF 0 0011 NO: 17; each start position is NO: 27; each start position is 80 specfied, the length of peptide is 9 specified, the length of peptide is 0 amino acids, and the end position for 10 amino acids, and the end ach peptide Is the start Position p position for each peptide is the start eight. pstnplsnine. Table lX-V254ILA-AI-l0mers. Start[ Subsequence Scrj sta t SLSequence][ Lo 98P486 I iT KSLSETFLPN f ~ Each peptide Is a portion of SEQ ID 9 TFPG.~ 1 d iFLN 1.8 SI SLS~~rFLPNG ][OA)20] NO: 51; each start position is== SETLN [0.1] specified, the length of peptide is 6M , EFPNII .0 I ~ SPKLSEF ] 005 110 amino acids, and the end 3 fKSLSETFLP I00] I91TFLPNGINGIJ 0.005 position for each peptide is the start 2~j PKSLSETFL 0.004 7 SETFLPNGIN [ 0.001 Position Plus nine. 51 FNG 0.00 2 SPKSLSETFL | 0.000_ubeqen e 8 I 0.000 3 PKSLSETFLP 0 CISQKLKRIK 0.200 ETFLNGIN 10.000 - - ~4-I FLPCISQKU( 020[ PSSTF] .0 _________r__ [2[ ILFLPCISQK I JjSLEF1 0.00000 Table IX-V14-HLA-AI-10mers- ISQKLKRIKK 0.150 98P486Table X.V14A0201-ners-98P46 Eacp pti is oLPCISQriKR ]o 0.125 c p Each peptide is a portion or SEQ ID [T1 IILFLPCS EI000I O 9 ach pefd sa position Qis NO: 29; each start position is [3 2 ed, tel t ofipis specified, the length of peptide is 10 amino acids, and the end [61 PCISQKLKR1 001 amino acds, and the end position for poitonfo echpptdeisth -ar R IKKG ach peptide is the start position plus position for each peptide is the start 9 QLRKGt ih cr position plus nine. _I I QKLKRIKKGW r 0 -ubeigne[ [Star| Subsequence | Score I Sa 6.7q1 I I1 ENLPLRLFTF 6.74 1. F8 1 FTFWRGPVVV | 0.050 |XV8-A0201-9mers.98p486 = NLPLRLFTF 0.994 [ LPLRLFTFWR | Each peptide is a poon of SEQ ID [ TFWRGPWV -2 1 NLPLRLFTFW W NO: 17; each start position is I . -61R~~R~v .1 specified, the length of peptide is 9 [ii2i11LinLLw R-- 0.032] 6 | RLFTFWRGPV amino acids, and the end position [6 . LFTFWRGPV I 0or each peptide is the start position [ 47 | PLRLFTFWRG 0.000 s eight. |[10 | FWRGPVVVAJ || 0.000 |ence _-471 LRLFTFWRG 1 .0 [5 1 LRLFTFWRGP 00] GMGGTIPHV [115.534 FWGPWA 0.000 9 TFWRGPVVA 0. ] FLEEGMGGT TI KSQFLEEM 0 Table X-V21XA0201-mer 98P4B13 Table IX-V2I4LA.AI-l0mers.- 2 IfSQFLEE~GG 0.004] 84 E c Eahepp seisaapportontofiSEQoID ___________5 JEL NO: 43; each start position is Eachpeptide is aportion of SEQ ID 131 QFLE-EGMGG If001specified, the length of peptide is 9 NO: 43; each start position is j IMGIHSfW5 amino acids, and the end position specified, the length of peptide is for each peptide is the start position 10 amino acids, and the end 1 ____ rFai plus eight. position for each peptide is the start F6-I] EEGMGGTIP r e I position Score nif ._ Subse8uence J S oiie Subs9mers98P46S 05 F5 | TOEQKTKHCM [|135 Each peptide is a Portion of SEQ ID _ QEQKTHCM 4 |Jr LTQEQKTKHC ||NO: 17; each start position Is TQEQKTK 0.052 3 EKLTQEQKTH specified, t length of peptide is 9_1 SKLTQEQKT I 08 3 | SKLTQEQKTK amio acds, and the end position for 4 TQEQKTKHC 0032 2.C 3 SKLTQEOKTK ||00007 KTKHCMFSLI ~ ~ ~~Ech peptide is tea position p EQ KHMSLID 02 1aTKHCMFSLIS [ Irt Subsuence Score 7 |CSQLRK 1.0 187FPCSKKi .0 Table X-V21-A020O-9mers- NO: 27; each start position is EQKTKHCMFS 0.001 98P4B6spcfetelntofppieI E TKC7] Each peptide is a portion of SEQ ID 10 amino acids, and the end NO: 43; each start position is position for each peptide is the start 8 QKTKHCMFSL 0.00 specified, the length of peptide is 9 position plus nine. amino acids, and the end position Start Subsequence Score Table X-V-HLAA0201-l0mers. or each peptide is the start position 5 1 SLSETFLPN 98P46 p us eIht Each peptide isa portion of SEQ I S Subsquence S 97.]TFLPNGINGI 0.062 NO: 51; each start position is E__ _ _ _ _ _ _ _ 11_2_ 0 0_ _ 2 __. Ii S P K S L S E T F L s p e c ifie d , th e le n g th o f p e p tid e is amino KSLSEtFLPN 10 amino acids, and the end t a e es 6 LSETFLPNGI position for each peptide is the sta 98P4 6 10ght FLPNGINGIK sition p nine Start Subsequence |SScor Each peptide is a portion of SEQ IDI 2' 1 L j Start Sub _ec 0.216 NO: 51; each start position is 9 1 GSPKSLSETF .1 3 ILFLPCISQK 1[ 0.216 specified, thb length of peptide is 9 SEFPNI 3.O L41FLPCI-SQKL- ][F 09.9 amino acids, and the end position 3 KLEFL Do 7FPIOLK1 .6 3 1 FLPCSESQKL ||98267o for each peptide is the start posi..n... IILFLPCISQ |[0.094 plus eight 0.00XV4 AA2OII1 t I s PCISQKLKRI 0003 Start Subs. u en ce [ Tae 98--413 s-F 71 S(OLKRIKI(G ] w 3 i FLPCISQK 98.2600046_________ 81 _________ Each peptide is a portion of SEQ ID .1 BE QKLKRIKKGW] 0 6 I CISQKLKRI [3i NO: 29; each start position is M I CISQKLKRIK q 0.000 ..I ILFLPCISQ [I ] specified, the length of peptide is 8 [ ISQKLKRII [W 9 O KLKRIKKG 0.001 1 10 amino acids, and the end 5--i 10 ~ ][ 0.000 4 I LPCISQKLK 0.000] position for each peptide is the start ________ 5i LPCISQK 0 position plus nine. M E____________Subse~uence IF Score Tb SQKLKRIKK 0.000] 61 RLFTFWRGPV Table X-mVe-HLArA3-9mers 7 9 ISQKLKRIK 8PF4B 6P4 5 CSKK TWG VVEach peptide is a portion of SEQ ID S 2 1 NLPLRLFTFW II 0779] NO: 17; each start position is 3 LPLRLFTFWR 0.074 specified, the length of peptide is 9 10 XVTA0.034 amino acids, and the end position p T ion for8HLA-AT201G10mers-o each peptide is the start position 8Pos plus nine.A R 0.027 plus eight. Each peptide is a portion of SEQ ID ij NPRFFf 021 Sat Sb ec cr r Subs2 Sence I useun NO: 17; each start position is FE PLEGFTFWRGMGGT2|| specified, the length of peptide is 10 FWRGPVAI 00 P -1 1EG G0 31 47 SOLEG1 0.0288 10 amino acids, and the end 1 0 Position for each peptide is the start 71-ILLTWGP- ~ ]__ SOLEM I .0 position plus nine. 0 |SQFLEEGM 2 ||KSQFLEEGMGM 0.0001 Start X-Sub - SuncA ers- Table X-V21-HLA-A0201-mers 5] LEEGMGGTI 5 J[ FE7GG98 .637 0.. 8 1 EGMGGTIPIIV 0.290] Each peptide Is a portion of SEQ ID i.. GGTP I00 NO: 43; each start position is - 1 IFLEEGMGG ( 0.000 --- ][ SOFILEEGIIGG I0.028 1 specified, the length of peptide is 9 1 MGGTIPHVS ] 4 ][QFLEEGMGGT 0.023] 10 amino acids, and the end r ft EEGMGGTIP I 0000 9 GMGGTIPHVS position for each peplide is the start 1 ][ EKSQFLEEGM ][ position plus nine. Table XII.V13-HLAA3..mers 2 EStart|| Subsequence] Score | KSQFLEEGG9 || TFLPGIKTKHC 0.06 9843 77 10 1MGGT1PHVSP 4=11 TQEQKTCM 00213 Each peptide is a portion of SEQ ID 7E EEGMGGTIPH 3___ K.L[LTQEQ<TKH .2 NO: 27; each start position is 6 EGGTP[~] -I LQQTH 0001 specified. the length of peptide is,9 o rKLSET 0.010 |an ids the position Table X-V13-HLA-A0201-0mers. 9 11~ KTKH-CMFSU ]0.003 I frec pseigi hetar osto 6 || LSE0TFLPNT || 0.002 Subse uence Score Each peptide is a portion of SEQ IDS E TFLI | 188 Table XiI-V13-HLA-A3-9mers- 9 TKHCMFSLI 0.002 1 able Xf 3LAA3lmers. 98P486 5 QEQKTKHCM 0.001 WPM Each peptide is a portion of SEQ ID 1 . Each peptide is a portion of SEQ ID NO: 27; each start position is specified, the length of peptide is 9 L 7 QTKCMF .000 NO: 27; eh a psti is amino acids, and the end position for each peptide is the start position Table XII-V25-HLA.A3-9mersI position for each peptide is the sta plus eight. 98P4B6 p Start[ Subsequence ScoreJ Each peptide is a portion of SEQ ID Start Subsequence 9 _FLPNGINGI NO: 51;each start position is 10 [LPNGINGIK 4 SLSETFLPN se the length of peptide is9 [T 0.180_P511_L_ _ 0 1 0 amino acids, and the end position 6 S F 0.020 for each peptide Is the start position I] GSPKSLSETF__ _ _ _ _ I_ _ lsegLj S K L E F 006 6 ||SETFLPNGI l 0.002 Plsegt| PKLUL 006 3_j KSLSETFLP 0.001 S Score 6 LSETFLPNGI 0.00 7 ETFLPNGIN 0.001 8 SQKLKRIKK ETFLPNGING 110] 5 SETFLPNG 0. 00QKL 03 K ETFLPN 1 0.003] 8 T FLPNGIG 0.000 1 taPC II 0.300 _ LPNGINGI F[ 0021 |2i PKSLSETFL | 00 11 LPCISQK.0K 1I0.100 7I1 GlJ .00O 2 31LFLPCISQK 31006 3 11 PKSLSTffLP 0.0 63 CISQKLKRI ~ i Table XJI-V14-HLA-A3-9mers TaleXI-V4B6AA.9es 5 ]~PCISQKLKR 31002Table XIII-V14-HLA-A3-0mers 98P46 ISQKLKRIK 0109W1 Each peptide is a portion of SEQ ID T ;QKL NO: 29; each start position is specified, the length of peptide is 9 0iin ais. and the end position Table XIII-V8-HLA3.es 10smpe cifi d ,an the legho edei ~~~0amino acids, and the end psto for each peptide is the start position 98P46 position for each peptide is the st plus eight. Each peptide is a portion of SEQ ID position plus nine. [Starti Subsequence |[ ore NO: 17; each start position cr I c or 1 I NLPLRLFTF [|| 00 specified, the length of peptide is 9.00 RLFTFWRGPV 0900 3 | PLRLFTFWR 10 amino acids, and the end position for each peptide is the startl . NLPLFWI 0O600 7 1 FTFWRGPV | 0.050] positionplusnine. - 1 LPLRLFTFWR 5 | RLFTFWRGP I 0.030 | 2 || LPLRLFTFW [| 0.009SP SFWRGPVVA [ GMGGTF 0.01 8- I9 TFWRGPVV I|| 0.0051| T][ LRLFTFWRG 0.000 |10 FWRGP A 00 6 | LFTFWRGPV| 0.000 | EGMGGTI 007 LFTFWRGPW 0.000 4 [ FLEMGGT 0.00 51LRLFTFWRGP 0.0 Table XII-V21-HLA-A3-9ners- 6 LEEGMG 0a Vs 98P4B6 2 ESQFLEEGM 3 0.000 1 98P4B6 J Each peptide is a portion of SEQ ID F 10 i FLMG G F 00 Ec p4td i NO: 43; each start position is E H _1 _i n specified, the length of peptide is 9 NO: 43; each start position is amino acids, and the end position T 1 specified, the length of peptide is for each peptide is the start position 10 amino acids, and te end plus ight.98P4B6 i position for each peptide is the start plus eight. 5i~aI] Subseuence Scr Each peptide is a portion of SEQ ID psition pus nine. S tar||NO: 27; each start position is Start Subsequence S specified, the length of peptide 30 . 0KLT0EQKTKH 8 | KTKHCMFSL 10 amino adds, and the endj F-6- Er=KCM 0.1 psbon for each peptide is the star 9j 31 KTCMFSLI I ~ 0 6 LTEQKTKHCMF 0.018 position plus nine. L 1 SKLTQE ][ 015] 31 LTQEQKTKH | 0.01 rt Subsuence S 4 LTEQIrKI-Ic0] 5 || QEQKTKHCM | .0.00 1 1|SKTE8T9 .0 | .6 lus eight Each peptide is a portion of SEQ ID 5 1 TQQKTKHCM 00 Start Subs jn Score NO: 51; each start position is 8|e000 specified, the length of peptide is 9 L LF 0.00 1 1 FN G - amino ads, and the end position I~~~~~~~~~ jjjj[1C F J[ f.011jSKLST I002I or each peptide is the start position 1 LSKLTQEQKT f T 4 IiiI SLSETFLPN II0.001 _plus eight. |110 I TKHCMFSLIS | 0.0007 ETFLPNGIN Start Subsequence Score 8is TFLPNGIN-G] 8 0.0 _ SKLKRIKI( 1.200 Table-Xill-V25-HLA-A3-10mers- 6 SETFLPN F0.001] 2 LPCISQK f0300 98P4B6 ]E 98463 KSLSETFLP 0.000 4 LCISQKLK 10.1001 Each peptide is a portion of SEQ ID I NO: 51; each start position is IT 0 specified, the length of peptide sSETFLPNG 0.0 3 FLPCISQKL 10 amino acids, and the end ISQKLKRlK 0.002 position for each peptide is the start Tabl XiV.V14-HLA-AIIOI. 6 CISQKKRI 0002 position plus nine. 9mers.98P4B6 1 ILFLPCISQ R1. 0 q2 [Starti Subsequence || Score Each peptide is a portion of SEQ ID 9 OLKRIKKG 0000] | 2 I ILFLPCISQK 150.000 NO: 29; each start position is | 4 FLPCISQKLK specified, the length of peptide is 9 8I ISQKLRIKK ai and the end position ..k ________ Jfor each peptide is the start position Table XV-S-LA-AI-i0mers | 7 ||CISQKLKRIK |plus eight. 98P46 5 I LPCISQKLKR || 0.080W ] | artI Subsequence] Score Each peptide is a portion of SEQ ID | I LFLPCIQI 91 3 PLRLFTFWR If 024 NO: 17; each start position is L -1 specified, the length of peptide is | 3 || LFLPCISQKL 0.002 |10 amino acids and the end |6I PCISQKLKRI ||1 .0 NLPLRLFTF 01 sitinforeach peptide isthestart 9II[ SQKLKRIKKG r 8 TFWRGPVVV 0 position plus nine. 10 I OKLKRIKKGW || 0.000 |] LPLRLFTFW Sa 0 Subseuence Score __-_______ -6 ][ LFTFWRGPV ]o.Oo2 5IIFE -EGMGGTI 0.004 Table XRV-VT-HLA-AT I101-9mers-FWRGP 0.000 SFLE 98P486 91 FWRGPWVA 000 M GMGGTIPHVS 0.001 Each peptide is a portion of SEQ ID I J LRLFWRG I 0 M7 EEGG 0000 NO: 17; each start position is I ___0 specified, the length of peptide is 9 8 EGMGG 0.057 amino acids, and the end position Table XiV.V21-HLAAI 101 T for each peptide is the start position 9mers-98P486 2 KSQFLEEGMG 0000] plusei. Each peptide is a portion of SEQ D g]h LEEGMGGTIP 0.000 Start| NO: 43; each start position is ]] EKSQFLEEGM 0 8 GMGGTIPHV | specfied, the length of peptide is 9 MG amino acids, and the end position 110 GJPVP .0 4 IFLEEGMGGT 0f r each peptide is the start position 1 KSQFLEEGM [1 0.003 phus eight Table XV-VI 3-HIA-AI 1-1 Diers 2 SQFLEEGMG [ P 98P4B6 5 ILEEGMGGTl_ 0.001] M KLTQEQKTK ach peptide is a portion of SEQ ID 7 71 EGMGGTIPH | 0.000 | ] TMFSL 7 0 NO: 27; each start position is f-3 1 QFEEGGG 0000LTQEKTK-]EO010specified, the length of peptide is SQFLEEGMGG 0000 amin acids, and the end 9 1 MGGTIPHVS 0.000 | 6] EQKTKHCMF 02sition for each peptide is the start 6 1 EEGMGGTIP || QEQKTKHCM ][ 0- position p.sdee. -47 -- I [TQEQKTKHC ][OD] Fst~ai11 Subsequen~ce IIScore Table XIV-V13-HLA-A1101- 1 . TKHCMFSU j M I FLPNGINGII 0 9mers-98P4B6 F 7]FQKTKHCMFS )ooo I TFLPNGING17110003 Each peptide is a portion of SEQlD T E 9 1 LSETFL 0002 NO: 27; each start position is slI ETFLPNGING specified, the length of peptide is 9 Table amino acids, and the end position XiV25.HLA-A11. II GSPKSLSETF 7! 9ELPGIN 0.001 6or each peptide is the start posiSonLPG loan 6 SETFLPNG ii Susqcoe Each peptide is a portion of SEQ 1D 4 Fi YS iiPq T I 2 - NQ 29; each start position is 2 [ALCIQ~ 0.0 specifi.ed, the length of peptide is59 7~~ | SETFLNGIN ||0.000 PKSLSETFLP 11 0.000 | for each peptide is the start Position 5 11 ] IS_______ 0.080 plus eight. Table XV-VI4-HLA-A1 1-10mers- 1 [ ISQKLKRIKK 0.040 Start Subseuence $core 98P4B6 11 C KLKRIK 0.040 Lk1 NLPLRLFTF 3.000 Each peptide is a portion of SEQ ID 3 LFLPCISQKL 0 003 8 TFWRGPVVV 0.500 NO: 29; each start position is 1 IILFLPCISQ 0.001 LFTFWRGPV 0.500 specified, the length of peptide is * SQLKRKKG oDoo 2LPLiYTFW r 26 10 amino acids, and the end 10 QKLK 7 0 _ ___ ___ 0.1 position for each peptide is the start - CISQF NVR0 position plus nine. Stt subsequenceRLFTFWRGP 0.020 SLPLRL FFWR S1F8 00 6 RLFTFWRGPV 0.024 |981486 1 0.001 FTFWRGPVVV 0020 EachpeptideisaportionofSEQID L. NO: 17; each start position is_____________ 9_ TFWRGPVVVA t0.004 1 specified, the length of peptide is 9 Table XVI-V21-HLAA24-9mers.. 2 ]NLPLRITFW [0.004 amino acids, and the end position 98P416 7 LFTFWRGPVV for each peptide is the start position Each pepde is a portion of SEQ ID 1P fELLR~FJ~ plus eight. ___ NO.- 43; each start position is 1 | NLPLRLFTF ||0.001 |etdei 10S bsuence 1 Score specified, the length of 10 1 PRFWRGWII(001] KSQFLEEGM IF Ti807 amino acids, and the end position 0.00 lii LEGGG 1 .10 for each peptide is the start position 4 |1 PLRLFTFWRG ||4]1 0.000 | 5 |RLFTFWRGP|S plus eight. TaIX -VILA IIO LEGMGGTISI 0.140 SatIubsequence II core e...m ers.9 11111 0_____~ .140- 8[ KKHCMFSL ~.0 Table XV-V21-HLA-A11-10mers- - G G 98P4B6 8 MFGTIPHV [T6EQKTKHCMF 2.000 Each peptide is a portion of SEQ ID 3 1 OFLEEGMGG j 0.090 [ 4 TQEQKTKHC 0.150 NO: 43; each start position is 7]1 EGMGGTIPH 0 TKHCMFSLI 0.120 specified, the length of peptide is 2 11 SOFLEEGMG 5 QE** I rT'7 10 amino acids, and the end - --- nQ., E07 position for each peptide is the start L-- 1 E KLTQEQKTK position plus nine. 1 QKT Start|| Subsequence || Score Table XVI-V3-HLA-A24-9mers- 3 1 " -9iKTKHCMFSLI ||~W 0.030 |I 2| SKLTQEQKTK Each peptide is a portion of SEQ -I rK NO: 27; each start position is______________ 31 KLTQEQKTKH I 0.012 specified, the length of peptide is 9 ble XVl.25-HLAA24-9mers 5 I TQEQKTKHCM 0.006 amino acids, and the end position 98P 8 I QKTKHCMFSL or each peptide is the start position Each peptide is a portion of SEQ ID 6 ~ ~ ~ t IfQOTHCF.__ plus eight.- NO: 51; each start position is 6 TQEQKTKHCMF | 0.001 Start Subsequi specified, the length opeptide is9 4 LTQEQKTKHC 1 S EF 4 amio acids, and the end position 7 QKKHMS 0009 17 1 FPLIN 1f -400 for each peptide is the start Position 10 1TKHCMFSLIS 0.000 9 }ooj I __ useigt I 1F[ LSKLTQEQKT || SLSETFLPN .144 Startl Subsequence [. Sc00e ____ - j~~11 SETFLPNGI U- 1441 Jj LCSK 1im~ _______________7 ETFLPNGIN ___0__ Table XV-V25-HLA-A11-10mers- -I' 0 9 6 CISQKLKRI 98P486 - TFL 2 LFLPCISQK 0.090 Each peptide is a portion of SEQ ID E ISQKLKRIK 0.018 NO: 51; each start position is 3 KSLSETFLP 0.030 1 [ SQKLKRIKK 0.011 specified, the length of peptide is P5 LSETFLP 1 0.010 10 amino acids, and the end 1 ILF- 1111 position for each peptide is the start 4 LPCISQKLK 0.010 I position plus nine. Table XVI.Y14-HLA-A24-9mers- 9 _______________ 98P46|9SQKLKRIKKK.04 191 Table XVI-V25-HLA-A24-9mers- Each peptide is a portion of SEQ ID 7 CISQKLKRIK 0.012 98P4B6INO29eahsatpstois9 1SKKIK 0.1 Each peptide is a portion of SEQ ID specified, the length of peptide is _____________10_ mno 29achdsstanth iind is57 9 SQKLKRKG .011 NO- 51; each start position is specified, the length of peptide is 9 position for each peptide is the start amino acids, and the end position I position plus nin for each peptide is the start position Start I Subsequence Score Table XVIII-V8-HLA-87-9mers1 plus eight. 1 ENLPLRLFTF 3.600 98P46 str] Subsequence [1 ScoreIf FWRGPVVA[ 1.400 Each peptide is a portion of SEQ ID PCISQKLKR 0.02T LFTFWRGPW NO: 17; each start position is ep specified, the length of peptide is 9 1097 TFWRGPWVA I amino acids, and the end position s ItVio HLA-A24-mers- for NLRLFTFW [02 each peptide is the start position -- 4B 1 6 J RLFTFWRGPV III 0.20 I__ plus eight. E a c h p e p t id e is a p o r tio n o f S E Q ID8 Ii S a t 1 S b e u n e [ i i NO: 17; each start position Isne. specified, the length of peptide is 1.80 LPLRLFTFWR r 0.015 1 1 KSQFLEEGM 1 1.000 10 amino acids, and the end 5 f TFWRGF 1 8 GMGGTIPHV 11 0.200 position for each peptide is the start PLRLFTFWRG 0.001 7 EGMGGTIPHVS |.1 position plus || 4 11 FLEEGMGGT 0.030 10r S Table XVII-V21-HLAA24-mersG GT9P HVMGGSHVS |.10.020 3 | FLEEGMGGID5800] 98|4|6 5.00 LEEGMGGTI 1 j.4 FFLEEGMGGT 110900 Each peptide is a portion of SEQ ID 2 F SQFLEEGMG If0010 O8 : EGMGGTIPHV I NO: 43; each start position is I GGTIP F0.001 9 f GMGGTIPHVS specified, the length of peptide is = 1 _ _ _ _ _ 10 am in o acid s, an d th e e n d L .. J L -2 KSQFLEEGM 1 0.030 position for each peptide is the start position plus nine. Table XVIII-V3.LA-B7-9mers Star MGGTIPHVSP I 0.10 I Subsequence S|cSe 9rP4e6 93 SQFLEEGMGG F _0010 9 11 KTKHCMFSLI I2.400 Each peptide is a portion of SEQ ID 1 6 f LEEGMGGT1P I .02 1 5 _TQEQKTKHCM jj ____0 NO: 27; each start position is 2 EEGMGGTIPH 8 specified, the length of peptide is _______________6 IfQEQK11(HCMF If0.300 f or each peptide Is the start position TabMe XVIV13.HLA.A241lOmers.] 4 ][ TEIK THC If0.180 j plus eight.- 98P4N36 [| 2.160|1 Each peptide isa portion of SEQ ID] [ I EQKT S j Start If 0c400 NO: 27; each start position isi __________ IL 0_100_ -1 ________I__ 4-0 specified, the length of peptide is I 3 ][KLTQEQKTKH 1 002 1 SPKSLSETF I00 10 amino acids, and the end o0[ TKHCMFSLIS ] -i H SETFLPNGI I00.0401 position for each peptide Is the st0 SKLTEQKTK .010 2 PKSL 00 8 position plus nine. 0.00 ETFLPNGIN Start Subsequence7 Score Table XV-4 AHLA.A-2A2-41mers.0 m SLSEFLPN r-97 T FL PN G IN GI I110.8 00 19813486 J KSLSETFLP I .1 3 SPKSLSE .00 ] Each peptide is a portion of SEQ 1D LSETLPNG 0.003 NO: 51; each start position is -TFLPNGING 0.001 6 LSETFLPNG .1 6 specified, the length of peptide is -471 KSLSETFLPN ~10 amino acids, and the end oF1 FLPNGINGIK FO0021 position for each peptide is the start 571 SLSETFLPNG 0.012 Start nie. S.5 9|F G |ETFLPNGIN 0 Score 3_____________ j 66.528l Table XVIII4V4-HLA.B379ners 6 || R LWRPV || 0.1 98P4B6 f 3!PKSLETFL 0.00 I ~ 10 QKLKRIKKGW ][~ ] Each peptide is a portion of SEQ IDI 3 1 07 NO: 29; each start position is Table XVII-V HLA-A24-0mrs. LPCISQLK] specified, the length of pepX2de -sV9 98P461 amino acids, and the end position o fo ec Q er each peptide is the start poiio9ls, ie plus eight. 98P4B6 7 LFTFWRGPWV 0.020 S Subsequence Score Each peptide is a portion of SEQ ID 1 ENLPLRLFTF 0.20 2 |1 LPLRLFTFW 0.400NO: 17; each start position is FWRGPVA 0.015 FTFWRGPW ~~~~~ specified, the length of peptide is PLLTWGI0011 7'M FFRGVV| 0.200 14 PRFFR .1 7 _____ I 10 amino acids, and the end _9 ||FWVRGPVVVA ||0.150 LL-FRP 0 FWRPVVAI .5 position for each peptide is the star ji~~iLLFFRPI 0.001 6 LFTFWRGPV i 0.030 _ position plus nine -8 J TFWRGPVVV 0.020 start Subsquence Score Table XIX-V21HLAB7-l0mers. 1 |NLPLRLFTF | .020 (8] EGMGGTIPHV 9OP486 3 | PLRLFTFWR I 0.010 5 FLEEGMGGII 0.120 Each peptide is a portion of SEQID -5 _ 0.010 Li] EKSOLEEGM 0.100 NO: 43; each start position Is (ji...I F 1WG Ef_______I specified, the length of peptide is _4_ || LRLFTFWRG .DI 9.001PHV If RLTFRG .01 ~ F GGTPH1] 02 10 arnino acids, and the end -10 1 MGGTIPHVSP I015position for each peptide is thestr Table QFLEEGMGGT 0.010 position lus nine .98P4B6 SQFLEEGMGG If 010 ubsequence I Each peptide is a portion of SEQ ID S EEGMG 0 0 KTKHCMFSU II 0400] NO: 43; each start positions 8 QKThHCMFSL .400 specified, the length of pepfide is 9 - iTEKK M f00 amino acids, and the end position LEEGMGGTIP 5 0.000 I ______ for each peptide is the start position I LSKLTQEQKT 0:100 plus eight. Table XIX-V13-HLA67-10mers- 4 LTQEQKTKHC 0.100 Start Subsequence I Score 9OP486 7 EQKTKCMFS 110.020 8 |KTKHCMFSL || 4.000 Each peptide is a portion of SEQ ID 3 KLTQEQKTKH 0.010 5 I QEQKTKHCM j NO: 27; each start position 0.0 I TKHCMFSLIS .00 specified, the length of peptide is 04 0 If THCMFLI I 0.00 110 amino acids, and the end IM-1 EQ<KCF .0 4 TOEQKTKHC 0.030 SLQEKK: l f7 IfTQEQ~KHCIf 0030]sition for each peptide is the star 0001 K~QEK I 6 I EQKTKHCMF 0.020 position pus nine. 3 I LTOEQKTKH ] 0.010 1 I u I Score TbX-25HLA-B740mers I I SKLTQEQKT || 0.0101 I SPKSLSETFL I80.000 98P486 2 I KLTQEQ 0.010_ LSETFLPNGI ][0.12 Each peptide is a portion of SEQ ID 7 || QKTKHCMFS I 0.002 | 9 0 TFLPNGINGI ][ 0 NO: 51;each start position is - __________ -specified, the length of peptide is r 17 1 GSPKSLSETF iF0.020 10 amino acids, and the end Table XVIII-V25-HLA-B7-9mers. 47 1 KSLSETFLPN 10. position for each peptide is the start 98P4B6 0 position plus nine. Each peptide is a portion of SEQ ID r I[ SLSETFLPNG If 1 [gi S [o NO: 51; each start position is specified, the length of peptide is 9 5 LPCISQKL 0.20 amino acids, and the end position SETFLPNGIN .0I[ for each peptide is the start position P K SLSETFLP 10 .000 j l... PCISQKLKRI plus eight. ISQKLKRIKK Start Subsequence [ Table XIXSVc4-oLArB7.e mers. IILFIPOISO 0.015 3 FLPCISQKLI I 98P4B6 II CISQKLKRIK|| 4.0.00 6 CISQKLKRI || 0.400 1 Each peptide is a portion of SEQ ID I FLPCISQKLK _1k.010 4 | LPCISQKLK If|| 7 NO: 29; each start position is M SKLKRIKKo 8 i SQKLKRIKK specified, the length of peptide 1I position for each peptide is the 1ta0 7 || ISQKLKRIK | 0.010 sition lus nine. 9 QKLKRIKKG ||ar001 SubsaqueSub Score TlX lLA-B3501-9mers 2 LFLPCISOK 0 1 FWRGPVVVAI 0.40 98P46 I ISK0 6 RLFFWRGPV 0.300 ach peptide is a portion of SEQ ID NNO: 17; each start position is 3 specified, the lth of peptide is 9 if_ _ Table If LPLRL 200 amino acids, and the end position 2 NLPLRLFTFW or each peptide is the start 193 plus eight. | Each peptide is a portion of SEQ 10 7 EEGMGGTIPH [ .j0f Start Subsequence Score NO 43; each start position is LEEGMGGTJP 0.00 I 1_ _ _ _ _ _ _ _ _ _ _20.000 specified, the length of peptide is 9 1 KSQLEEGM JJ ~amino acids, and the end position 8 GMGGTIPHV 0200 for each peptide Is the start position Table XOi*VI 3-|HLA-6351 Omers 9 || MGGTIPHVS | 0.100 plus eight 98P 4 S[r Sbsequence score ach peptide isaportion of SEQ ID 2 SQFLEEGMG 0015 NO: 27; each start position is f-2-1 S LEEG:G 8 1KTKCMFS 6-000Specified, the length of peptide is 5 I LEEGMGGTI [ 0.012 | 6 EQKTKHCMF 10 amino acids, and the end 7 | EGMGGTIPH 5 QEQKTKHCM 0.200 position for each peptide is the start T Q(FLE-EGMGG .0 9 jt TKHCMFSU 1 0.040 - position plus nine___ 6 || EEGMGGTIP | 0.001 2 KLTQEQKTK Start Subseuence -4__ TQEQKTKJC 0.3 2 SPKSSETFL f0.0 Table XX-V13ILA.B3501-9mers- 3 LTQEQKTKH 0 1 GSPKSLSETF - 98P486 7 QTKHCMFS 0.010 4 IKSLSEWLPN 1.000 Each peptide is a portion of SEQ ID| SKLTQEQKT 0010 _±I l LSETFLPNGI_ 0600 NO: 27; each start position is -9 INGINGI 0.040 specified, the length of peptide a amino acids, and the end position Table XX-V25-lLA-83501-9me 5 SLSETFLPNG 0.020 or each peptide is the start position 10 plus eight Each peptide is a portion of SEQ ID 71 SETFLPNGi 0.010 Start I Subsequence score NO: 51; each start position is ETFLPNGING SPKSLSETF - ~specified, the length of peptide is 9 ~ PSSTL 1 |I SPKSLSETF |60.000 3 KLEFL .0 II _________ ][6.oooamino acids, and the end position 9 9I FLPNGINGI for each peptide is the start position 4 |f SLSETFLPN 0.200 plus eight Table X V14-HLA-B35-10ers 3 | KSLSETFLP || 0.150 | Start Subseuence Sre 98P4B6 F77 1 ETFLPNGIN 0.100 31 FLPCISQKL IT ____ EachpeptideisaportionofSEolD 6 ~ ~ ~ _ If STLNI]0006 ICSK RI i' ___ NO: 27; each start position is __________ 0.005 LP6: CISQKLK specified, the length of peptide is 5 |1 LSETFLPNG || M I LPCISQK__ 0.200 10 amino acds, and the end r2_j| PKSLSETFL 5[ 5-o7 7 ISQKLKRik position for each peptide is the s0.01 8 || TFLPNGING ||0.001 | 8J1 SQ KRIKK -0 03 sitlon lus nine. 1-il ILFLPCISQ Start I Subsecluence ]Score Table XX-V14-HLA.B3501.9mers. RIKKG 0.001 F ENLRLFTF 1.00 98P4B6 2 Q2 Each peptide is a portion of SEQ ID = PCISQKLKR 6 0 RLFTFWRGP 0 0 NO: 29; each start position is T WRGPVW specified, the length of peptide is 9 amino acids, and the end position 1 for each peptide is the start position 98P4B6 j.0j[ FWRGPVWAI0 plus eight. Each peptide is a portion of SEQ ID LFTFWRGPW 0 Start I Subsequence I Score NO. 17; each start position is "'7' f 1] specified, the length of peptide is 9 FRPVA 001_ F2 j LPLRLFTFWV 10.000 4 1LTWGi .0 M E10 amino acids, and the end 'I I17 | NLPLRLFTF 111.0001 position for each peptide is the sta 5 LRLFTFWRGP 0.001 -77 | FTFWRGPVV || 0.200 position plus nine. 9|11 FWRGPVVA i.0.030 i Table XXI-V21-HLA-35-l mers r.6 |11 LFTFWRGPV ir1 FLEEGMGGTI 00..2200| 51I RLFTFWRGP 028 EGMGG11PHVDM E Each peptide isaportion of SEQ ID 8 |L TFWRGPVVV I 0.020 1 |EKSQFLEEGM 11 0200_ NO: 43; each start position is __________I sp00ecifiEEed, the length of peptide is 3 |I PLRLFTFWR I0.003 2 |S.I L 11 0. 10 amino acids, and the end 4 | LRLFTFWRG I 0.001 1 9 GMGGTIPHVS 0100 position for each peptide is the sta ______________M_ I QFLEEGMGGT ii 0.020= position plus nine. _ Table XX-V21-HLA-B3501-9mr sGMGG 0.05 S Subsuence Score II98P46 10 11 MGGTIPHVSP oI .0101 KTKH-CMFSU 2.400 194 L-SKLTQE0K(f] 1.500 [Table XXI-V25-IfLA-B335-10mers. 8T1 ISOKLKRIKK f0.050 -5 TQEQKTKHCM ][0.600 I.98P4136 10 ]jQKU(RIKKGW ][0.050 ir EQKTKJ-CMFS f0.300 Each peptide is a portion of SEQ ID 6 JJPCISQKLKRI if0. 0 A[LTQEOWTKHC 0.200__ NO: 51; each start position is9 QKRKG 03 nlnspecified, the length of peptide is QURKGI .3 6 ][QEQKTKHCMFJ]010 10 amino acids, and the end 4j FLPCISQKLK 0. 010I 8 rf QKTKHCMFSL If0.100 position for each peptide is the star 7 IICISOKLKRIK II0.010 3f KLTQEQKTKH I ___ position plus nine. 21 ILFLPCISQK J I! 1 If TKCMFSLIS Start SuIbisencI cr IFPIQ I -2 ]r SKLTQEQKTK .025 LPCISQKLKR 0.200 -- ______ ~LFLPCISKL 0.0 195 Tables XXII - XLIX: labIeXXH-VI-HLA-AI- position is speed, the TableXXII-V-HLA-AI 9mers-98P4B6 length of peptide is 9 amino 9mers-98P 6 Each peptide is a portion of acids, and the end position Each peptide is a portion of SEQ ID NO: 3; each start for each peptide is the start SEQ ID NO: 13; each start position is specified, the length sition us eih position is specified, the of peptide is 9 amino acids, Pos 123456789 score length of peptide is 9 amino and the end position for each 23 LSLPSSWDY 23 acds, and the end position peptide is the start position 3 PCPADFFLY 2 for each peptide is the start plus eight. 17 _FSCLSL 13 position plus eih Pos 123456789 ore 28 SWDYRCPPP I Pos 125456789 score 158 KDASRQVY 27 VILGIILF 8 419 EEYYRFY 7 TableXXII-V5A-HLA-Al- 1 PCISRKLKR 8 405 STFHVLIY 6 9mers-98P4B6 ILGKIILFL 7 221 LATFFFLY 23 Each peptide is a portion of 37 EGIGGTTPH 7 263 _TLLSLVY 3 SEQ ID NO: 11; each start 46 VSPERVTM 7 392 EIQSTLGY 3 position is specified, the length 3 PSIVIGKI 6 76 AAAYQLYY 22 of peptide is 9 amino acids, 5 IVILGKIIL 80 QLYYGIKY Iand the end position for each I [LPCJSR 6 244 S~DFYKIP1 19ppte stetatoiio 101 WDLRHLLV 18 hi TableXXII-V7A-HLA 189 IDLGSLSS 18 123456789 score AI-9mers-98P4B6 198 IENLPL 18 Eachpeptideisaportio 31 _ VIHPY 18 SEQIDNO15;eachstart 40 ARNQQSDFY 18 position is specified, the 275 LAAAYQLY 18 TablcXXH-V5B-HLA- length of peptide is 9 amino 311 FAMVHVAY 18 A1-9mers-98P 6 acids, and the end position 90 AJHREHY 17 Each peptide is a portion of for each peptide is the start 117 _NMRINY 17 SEQIDNO:11;eachstart sition plus ei h. 327 SERYLELN 17 position is specified, the Pos 123456789 score 388 _ FSFIQS 17 length of peptide is 9 amino 5 LSETFLPNG 14 427 PNFVLA 17 acids. and the end position SLSETFLPN 1 443 ILDLLQLCR 17 for each peptide Is the start 8 LNGING 9 444 IDLLQLCRY 17 position plus eih L______ 8 46 -I RCGY 16 Pj 123456789 score 66 SEFFPHVV 16 21 ELEFVFLLT 24 124 YPESNAEY 16 1 WREFSfIQI 17 TableXXII-V7B-HLA-AI 200 EIENLPLRL 16 1 QTELELEFV 16 9mers-98P4B6 330 YLFLNMAY 1613 FADTQTLE 15 Each peptide is a portion of 35 V RIM 191 ELELEFVFL 14 SEQ ID NO: 15; each start 352 LEVWRIEMY 16 position is specified, the 272 LAGLLAAAY 15 23 MRRERYTablexxH-v6-HLA-AI - length of peptide is 9 amino 323 LPMRRSERY 15 9mers-98P4B6 acids, and the end positions 351 EEEVWRIEM 15 Each peptide is a portion of each peptide is the start 415 - EEEY 15 SEQ ID NO: 13; each start sition Ius ei hi 416 KAEEEYY 15 16 EEY ~position is specified, the Posl 123456789 Iscore 13 LSETCLPNG 14 length of peptide is9 amino 5 AY STLGY 22 38 qDFAKSLT 14 acids, and the end position 9 SILGYVALL 13. 98 LWDLRH 14 178 IELARQLN 14 for each peptide is the start 178 __________ 14 position plus eight. ITableXXI-V7-HLA-AI 406 STFHVLIYG 14 Pos 123456789 score 9mers-98P4B6 94 HYTSLW 13 34 FLEEGIGGT 14 Each peptide is a portion of 135 LFPDSLIV 13 28 GWEKSQELE 12 SEQ ID NO: 15; each start 137 PDSLIVKG 3 35 LEEGIGTI 12 position is specified, the length 251 IEIVNKTL 13 29 WEKS FLEE 11 of peptide is 9 amino acids, 396 SILGYVALL 13 41 GTIPHVSPE 11 and the end position for each I VP IVILG peptide is the start position TabIeXXHI-V2-HLA-AI- 9 GKIILFLPC use h 9mers-98P4B6 19 SRxtIKK 9 Pos 123456789 score Each peptide is a portion of 2 LPSIVILGK 8 59 1 SEQ ID NO: 3; each start sito use t TableXXII-V7C-H LA-A I- acids, and he end position sition plus eight 9mers-98P4B6 for each peptide is the start Pos 123456789 score Each peptide is a portion of t le . PCISQKLKR 10 SEQ 1D NO: 15; each start Pos 123456789 score 8 SQK]KtJK 9 position is specified, the length 4 FLEEGMGGT 14 1 ILFLPCISQ 6 of peptide is 9 amino acids, 5 LEEGMGGTI 12 2LELPCISOK 4 and the end position for each 7 EGMGGTjpH 7 3 FLPCIS0KL 4 peptide is the start position 7 ISOKLKRIK lus ei hL. Pos 123456789 score TabeXXal-VI3-HLA 90 VIEDDEAQD 17 AI-9mers-98P4B6 TabteXXM-VI-HLA 99 SIDPPESPD 17 Each peptide is a portion of A02014mers-98p6 167 KLETIILSK 17 SEQ ID NO:27; each start Each peptide is a portion of 32 LSEIVLPIE 16 position is specified, the SEQ ID NO: 3; each start 51 STPPPAMW 14 length of peptide is 9 amino position is specified, the length 154 WSLGEFLGS 14 acids, and the end position of peptide is 9 amino acids, and 5 ILDLSVEVL 13 for each peptide is the start the end position for each 69 AQESGINK 13 sition plus eight. peptide is the start position Plus 9 SEVLASPA 12 Pos 123456789 score 38 PIEWQQDRk 12 5 L nENG 14 Pos 12345679 score 60 TEEAGATAE 12 4 SLSETFLPN 12 365 IMSLGLLSL 2 66 ESGI 12 8 TFLPNGING 9 71 YLAGLAAA 28 93 DDEAQD ID 12 7 ETFLPNGIN 8 433 VLALVLPSI 28 104 ESPDRALKA 12 6 227 FLYSFVR v 2 105 SPDRALKAA 12 360 YISFGIMSL 27 123 HINGVGPLW 12 TableXXII-V14-HLA-A1- 39 STLGYVALL 27 130 LWEFLLRLL 12 9mers-98B6 17 CLPNG 146 2 96 AQDSIDPPE 11 Each peptide is a portion of 100 SLWDLRHLL 2 102 PPESPDRAL 11, SE ID NO: 29; each start 12 128 GPLWEFLLR I| sition is specified, the ngth 22 143 ASGTLSLAF I- of peptide is 9 amino acids, 402 A1LRLFH 2 15 LELGGT -and the end position for each 432 LLPSIFV 26 156 LGEFLGSGT I1 461LS L 2 42 DRK _PL 1 peptide is the start position 128 SNAEYLASL 25 78 SSSSSQIPV 10 pluseiht 140 SLVKGFNV 25 82 SQIPVVGVV 10 s 123456789 score 187 iiPID SL 25 91 TEDDEAQDS 10 7 91FWRGP 9 21 TLWRGPVVV 25 92 EDDEAQDSI 10 I ) H 261 WVIL[SL 25 115 SWRNPVLPH 10 403 LLISTFHVL 25 176 LIQEQKSKH 10 TableXXl-V21-HLA-AI- 5 SMMGSPKSL 2 177 TEKSKHC 109mers-98P4B6 21 NILRGGLSE 91 Each peptide is a portionof 264 TLLSLVYL 2 50 LSTPPPPAM 9 SEQ ID NO: 43; each start 27 LLAAAYQL 2 SO LSTPPPPAM ~~ position is specified, the 37LSFAV 2 79 SSSSQIPVV 9 length of peptide is 9 amino 369 GLLSLLAVT 2 131 WEFLLRLLK 9 acids. and the end position fo 48 RL[RCGYHV 23 2 SIVILDLSV 8 each peptide is the start 49 LIRCGXHVV 23 7 DLSVEVLAS 8 position plus eight 141 LIVKGFNVV 23 21 KCLDANILR 8 Pos 123456789 score 313 AMVHVAYSL 23 31 GLSEIVLPI 8_3 LQKTKH 1 374 LAV1SIPSV 23 81 SSQIPVVGV 8 TQEQKTKHC 10 393 FIQSTLGYV 23 124 TNGVGPLWE 8 1 SKLTQEQKT 441 IVILDLLQL 23 132 EFLLRLLKS 8 8 KTKHCMFSL 106 HLLVGKIl 22 141 _AASGTLSL 8 180 ELARQLNFI 22 162 SGTWMKLET 8 254 IVNKTLPIV 22 169 ETIILSKLT 8 TableXXI-V25-HLA- 258 TLPIVAITL 2 AI-99 Prs-98P4B6 262 VAITLLSLV 22 TableXXII-V8-HLA-A1- Each peptide is a portion of 265 TLSLVYLA 2 9mers-98P4B6 SEQ ID NO: 51; each start 267 eLac rGL 22 Each peptide is a portion of position Is specified, the 268 SLVYLAGLL 2 SEC ID) NO: 17; each start length of peptide is 9 amino 3331 FLMMAYQQV 22 position is specified, the acids, and the end position 378 SIPSVSNAL 2 length of peptide is 9 amino for each peptide is the start 404 LISTHVLI 21 197 TableXXBI-VI-H LA- TableXXIH-VI-HLA- TableXXIf-V2--HLA A0201-9mers-98P4B6 A0201-9mers-98P4B6 A0201-9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO- 3; each start SEQ ID NO 5; each start position is specified, the length position is specified, the length position is specified, the of peptide is 9 amino acids, and of peptide is 9 amino acids, and length of peptide is 9 amino the end position for each the end position for each acids, and the end position peptide is the start position plus peptide is the start position plus for each peptde is the start eight. eighL sition plus eigh Pos 123456789 score Pos 123456789 score Pos 123456789 score 435 ALVLPSIVI 21 50 IRCGYHVVI 15 1 SLSLSSGFF 1 107 LLVGKTLID 20 111 KILIDVSNN 15 3 SPOALSL 15 108 LVGKILIDV 20 211 LWRGPVVVA 15 12 SLSSGFTFF 14 112 ILIDVSNNM 20 217 VVAISLATF 15 15 sGFTPFSCL 1 173 QAROQVIEL 20 221 SLATF FLY 15 241SLPSSWDYR 12 184 QLNFIPIDL 20 247 FYKIPIEIV 15 368 LGLLSLLAV 20 249 KIPIEIVNK 15 TableXXlll-V5A-HLA 65 FASEFEPHV 19 251 PlEIVNKTL 15 A0201-9mers-98P4B6 83 LTKTNIIFV 19 25 NKTLPIVAI 151 Each peptide isa portion of 133 LASLFEDSL 19 - VYLAGLLAA 15 SEQIDNO11;eachstart 177 QVIEL_.RL 19 299 LQCRKQLGL position is specified, the legth 257 KTLPIVAIT 19 32 PMRRSERYL 5 ofpeptideis9aminoacids, 30 GLLSFFFAM 19 331 YLFLNMAYQ 15 andtheendpositionforeach 366 MSLGLLSLL 19 335 NMAYQQVHA 15 peptide is the staut position 434 LALVLPSIV 19 385 ALNWREFSF 15 plus eight. 27 DARKVTVGV 18 4 YVALLISTF 15 Pos 123456789 score 19 SSAREIENL 18 437 VLPSIVILD 15 7 F 17 209 FTLWRGPVV 18 23 NGTKDARKV 14 1 NLLRLFf 16 259 LPIVAITLL 18 37 GSGDFAKSL 14 8 TFWRGPVV 15 36 SLGLLSLLA 18 39 GDFAKSLTI 14 9 FWRGPVVA 14 371 LSLLAYTSI 18 42 AKSLTIRLI 14 5 RLFFWRGP 13 397 TLGYVALU 18 1 QVYICSNNI 14 3 PLRLFTFWR 1 41 FAKSLTIRL 17 16 YICSNNIQA 14 6 LFTFWRGPv 1 81 DALTKTNH 17 22 ISLATFFFL 14 85 KTN1IEVA 17 223 ATFFFLYSF 14 103 DLRHLLVGK 17 266 LLSLVYLAG 14A0201-9mrs-98P4B6 104 LRHILLVGKI 17 275 LLAAAY LY 14 EachpeptideIsaportionof 153 ALQLGPKDA 17 278 AAY LYYGT 14 SEQIDNO11;eachstart 155 QLGPKDASR 17 300 Q LGLL 14 position i specified, the 212 WRGPVVVAI 17 309 SFFFAMVHV 14 length of peptide is 9 amino 250 IPIEIVNKT 17 362 SFGIMSLGL 14 ads, and the end position 250 [PIEVNKT 17 373 ___TIS 4 for each peptide Is the start 253 EIVNKTLP1 17 373 LLAVTSIPS 14vsto lsegt 363 FGIMSLGLL 17 395 QSTLGYVAL 14 pos 1357 scoIt 37 LLSLLAVTS 17 411 LIYGWKRAF 14 2 LELEFVFLL 21 410 VLIYGWKPA 17 427 YTPPNEVLA 14 2 LEFVFLLTL 21 428 TPPNFVLAL 17 443 ILDLLQLCR 14 438 LPSIVILDL 17 1 2 LLTLLL 20 442 VILDLLQLC 17 TableXX1H-V2-HLA- ELELEEVFL 17 25 IKDARKVTV 16 A0201-9mers-98P4B6 12 68 EFFPHYVDV 16 Each peptide is a portion of 17 QTELELEFV 17 88 IIFVAIHRE 16 SEQ ID NO: 5; each start 8 QEFCSFADT 15 ______ 16posn 1 spedt6 FIQIFfSFA 14 93 IHREHYTSL 16 position is specified, the14 99 TSLWDLRHL 16 length of peptide is 9 amino23 EFVFLLTLL 11 132 YLASLEPDS 16 acids, and the end position 148 VVSAWALQL 16 for each peptide is the start 171 NIQARQQVI 16 position plus ei ht. 19 IDLGSLSSA 16 Pos 123456789 score 20 EIELPLRL 16 5 GLALSLSL 25 Each peptide is a portion OF 372 SLLAVSIP 1 6 18 SEQID NO: 13; each start I SLSETCLPN 1 5 8 ALSLSLSSG 18 psto sseiid h 441 SLT RC i 7 FSCLSL 17eifed,the 1 QR length of peptide is 9 amino TableXXI-V7C-HLA8 GMGGTIPHv 26 acids, and the end position for A0201-9mers-98P4B6 4 each peptide is the start Each peptide is a porton of' 13 - position plus eig SEQ ID NO: 15; each stat I__._ _ Pos 123456789 score position is specified, the length TableXIll-V 3-HLA 7 ILGKIILFL 27 of peptide is 9 amino acids, A0201-9mers-98P4B6 38 GIGGTIPHV 26 and the end position for each Each peptide is a portion of 1 KIILFLPCI 25 peptide is the start position SEQ ID NO: 27; each start 14 FLPCISRKL 23 plus eight. position is specified, the 34 FLEEGIGGT 23 Pos 123456789 score length of peptide is 9 amino 5 IVILGKHL 20 27 ILRGGLSEI 3 acids, and the end position 1 CISRKLKRI 20 4 VILDLSVEV 27 foreachPeptideisthestart 45 HVSPERVTV 20 5 ILDLSVEVL 2 pluseiL 4 SIVILGKII 18 31 GLSEIVLP1 2 score 6 VILGKIILF 18 129 PLWEFLLRL 26 1 ILFLPCISR 16 148 SLAFTSWSL 25 1 VLPSIVILG 15 2 SLVISV 24 2 KGWEKSQFL 15 141 QAASGILSL 23 TableXXUl-V144ILA 3 PSIVILGKI 13 155 SLGEFLGSG 21 A0201-9mers-98P4B6 35 LEEGIGGTI 13 163 GTWMKLETI 21 Each peptide is a poron of 41 GTIPHVSPE 13 81 SSQIPVVGV 2 SEQ ID NO: 29; each start 8 _2 SQ[PVVGVV 20 position Is specified, the length TableXXHlI-V7A-HLA- 119 PVLPHTNGV 19 of peptide is 9 amino acids, A0201-9mers-98P4B6 133 FLLRLLKSQ 19 and the end position for each Each peptide Is a portion of 165 WMKLETHL 19 peptide is the start position SEQ ID NO: 15; each start 24 GANILRGGL 18 - p eiht. position is specified, the 57 AMWTEEAGA 1 Pos 123456789 score length of peptide is 9 amino 112 AANSWRNPV 18 7 FTWRGPVV 17 acids, and the end position 126 GVGPLWEFL 18 1 NLPLRLFTF 16 for each peptide is the start 12 VLASPAAAW 8 TFWRGPVVV 15 Pionuse 79 SSSSQIPVV 17 9 FWRPVVVA 14 123456789 134 LLRLLKSQA 17 c e 13 1 JP G I 27 167 KLETHLSK 17 3 PLRLFTFWR 10 41SL~r7 LN 1 168 LETHILSKL 1716 LFTF IGPV 1 10 171 5SK TQE 17 TabeLTableA-I-V21-HLA TablcXXIH-V7B-HLA- A0201-9mers-98P4B6 A0201-9mers-98P4B6 42 AASGTL 16 Each peptide is a portion of Each peptide is a portion of 160 LGSGTWMKI 16 SEQ ID NO: 43; each start SEQ ID NO: 15; each start 1 position is specified, the position is specified, the 7 AAAWKCLA 1 length of peptide is 9 amino length of peptide is 9 amino 17-.WKLG 5 adds, and the end position acids, and the end position for 22 CLGANTLRG 15 for each peptide is the start each peptide is the start 26 NILRGGLSE 5 sition us e hi. sition us 'h 28 LRGGLSEIV IS Pos 123456789 score Pos 123456789 score 130 LWEFLLRLL 1 8 KTKHCMFSL 16 STLGYYALL 27 136 RLLKSQAAS 15 2 ! j QEQKTK 1I 3 NMAY STL 21 13 1 _ T K qKT 10 Y ST 16 159 FLGSGTWMK 15 3 LTQEQKTKH 10 8S~ G ~ 1 185 CMFSLISGS Is ~ 814 83 QIPVVQVVT - TableXX]HI-V7C-HLA- TableXXI-V25-LA A0201-9mers-98P4B6 Tab~eXXIII-VS-HLA- A219es9PB A0201-9mers-98P4B6A0201-9mers-98P4B6 EEach peptide is a portion of SEQ ID NO: 15; each start E ID e s rt SEQ ID NO: 51; each start position is specified, the length position is specified, the of peptide is 9 amino acids, position is specified, t length of peptide is 9 amino and the end position for each length of peptide is 9 amino acids, and the end position peptide is the start position acids, and the end position for each peptide is the start lus & h for each peptide is the start position S DN 2 eahta Pos 2345789sit e'~ h pos ition is eiid the position 123456789 score lng o123456789 score Pos 123456789 score 3FLPCISKL 23 199 I 61ISQKKRII201J~os]23467 Tab~eXXV-VI-HLA-A3 11IFPIQ1161 1 oeut~ud 9mers-98P4136 _____________________________Each peptide is a portion of TableXXIV-VI-HLA- TableXXIV-V21- SEQ ID NO: 3; each start A0203-9mers-98P4B36 HLA-A0203-9mers- position is specified, the length Pos 11234567891 score 98P4136 of peptide is 9 amino acids, NoResultsFound. Pa 13579 cr and the end position for each _____________NoResultsFound. peptide is the start position [TableXXIV-V2-HLA- _ ______plus eight. LA0203-9mers-98P4B36 TableXXIV-V25- Pos 123456789 score [Pos 11234567891 score H-LA-A0203-9mers- 411 LIYGWKRAF 19 [NoResultsFound. 98P4B6 436 LVILPSIVIL 19 __________Pos 11234567891 score 34 GVIGSGDFA 18 TableXXIV-V5A- NoResultsFound. 92 AIHREHYTS 18 HILA-AO203-9mers- _ _______140 SLIVGFN 18 98P4136 TableXXV-V1-HLA-A3- 191 DLQSLSSAR 18 Pos 11234567891 score 9mers-98P4B6 221 SLATFIFFILY 18 NoResultsFound. Each peptide is a portion of 43 ALVLPSTV 18 ____________SEQ ID NO: 3I each start 22 INGIKDARK 17_ TableXXIV-VSB- positi-!- specified, the length 49 L1RCGXYjVV 17 HLA-A0203-9mers- of peptide is 9 amino acids, 82 AL'YCrwNIF 17 98P4136 -and the end position for each Ii Inmsm I TiD-NN 1 Pos 11234567891 score peptide is the start posiion 112 -ILWVSNNiM 17 NoResultsFound. I _ plus eight. 135 SL[PDS-LJV 17 _________Posl 123456789 score 153 ALQLqPKDA 17 TableXXIV-V6-HLA- 103 DLRHLLVGK 27 164 QVYISNNI 171 A0203-9mers-98P4B6 56 VVIGSRNPK 26 203 NLPLRLFTL .17 Pos 1234567891 score 249 KIPIEIYNK 26 271 YLAGLLAAA 17 NoResultsFound. 3 SISMMGSPK 25 30 QLLLSFFF 17 ____L___ 55 QLQPKPASR 25 381 SVSNALNWR 17 TableXXIV-V7A- 2631 AJTLLSLVY 251 39 TLGYVALLI 17 HLA-A0203-9mers- 210 TLWRGPVVV 241 403 LLISHV 17 98P4136 48 RLIRCGYHV 23 i S2 FVLALS 1 Pos 1234567891 score 142 IVKGFNVVS 23 32 TVGVIGSGD 16 NoResultsFound. 217 VVAISLATF 23 107. ULVGKIILID 16 Tab~eXXIV-V7B-400 YVALLISTIF 2315 WLLIK 6 HalA-A020-Vmei- 177 QV1ELA1QL 22 171 NIQARQQVI 16 HL 8AP039B rs 2051 PLRLFTILWR 221 189 PIDLGSLSS- 16 Po 123468 scr 281 QLYYGTKYR 22 216 VVVAISLAT 16 Pasu3571sore 37 LLSjLLAVTS 22 219 AISLATIFFF 16 Neslson.441 IVILDLLQL 22 234 DVIIIYARN 16 Ta~XXVV7-35 VIGSGOFAK 21, 266 LLSLVYLAG 16 TbeXIV7-77 THHEDALTK 21 302 RKQGLF 1 HLA-A0203-9mers- 14 VAAQL 2 0 LLF 16 98P4B6 ___________11_02_LISFH 1 Pos 11234567891 score, 231 FRDVIjB' 211 12 SLSETCLPN 15 NoResultsFound. 26 VLGL !21 Gfl4GIKDAR 15 375 AVTSIPSVS 21 24 GEKDARKVY. 1S TableXXIV-V8-HLA- 385 AU'JWREFSF 21 30 KVTVGVIGS 15 A0203-9mers-98P4B6 274 GLLAAAYQL 20 121 RINQYFESN Is Pos 11234567891 score 322 CLPMRRSER 20 136 LFPDSLIVK 15 NoResultsFound. 40 HVIgK 20 179 EL N 15 4431 ILD-LL QLCR 20 268 SLVYLAGLL IS Tab~eXXIV-V 13- 46 TIRLIRCOY _19 35 RIEMYTSFG 15 HLA-A0203-9mers- 871 NUIVAIHR 15~ 367 SLLLLA 15 98P4136 90FVAIIR.EH 5_1 410 VLIYGWKRA 15 os 1234567891 score 258 TLEIVA1TL __19 43 VLALYLfsI 15 NoResultsFound. 261 IVAITILLSL __19 25 IKDAKV 14 275 LLAAYQLY 19 41SLTMRLRC 14 TableXXIV-V 14- 1_79 AYQLYGTK 19 57 VIGSRNPKF 14 HLA-A0203-9mers- 1369 GLISLLAVI' 19 61RNKSE 98P4136 1 3721 SLLAVTSIP ,19 1 6IILLVKTLIE 14 I700GKLI 1 TabIeXXV-VI-HLA-A3- Pos 123456789 score adds, and (he end position for 9mers-98P4B6 8 A S each peptde is the start Each peptide is a portion of 2 SLSSGEEPF 18 position plus eigh SEQ ID NO: 3; each start 5 GLQALSLSL 17 Pos 123456789 score position is specified, the length 22 CLULPWD 15 45 HVSPERVTV 22 of peptide is 9 amino acids, 24 SLPSSWDYR 15 23 KRIKKONEK 2 and the end position for each 10 SLSLSSGFr 13 12 ILFLPCISR 19 peptide is the start position 23 LSLPSSWDY 11 5 IVILOKIIiL 18 plus eight. 33 C 1 13 LFLPCISRK 18 Pos 123456789 score 3 SPGLOALSL 1 6 VILGKIILF 17 141 LIYKGFNVV 14 7_QLSLSLSS 9 21 KlKRKGW 17 180 ELAR LjNF1 14 18 ELRQNF 12 LSLSLSSGF 9_2 LP$IVLGK 151 20 RLFTLWRGP 14 -7 ILGKI1LFL 15 227 FLYSFVRDV 14 21 SCLSLSSW 9 KIILFLICI 15 235 VIHPYARNQ 14 37 FFLYF 18 ISRXLKRIK 15 241 RN QSDFYK 14 19 SRKxuuuKK 15 251 PIEIVNKTL 14 TabeXXV-V5A-HLA-A3- 24 RIKKOWEKS 15 272 LAGLLAAAY 14 9mers-98P4B6 3 FLEEGIGGT 14 29 WLETWLQCR 14 Each peptide is a portion of SIILGKII 13 303 KQLGLUFF 14 SEQIDNO:11;eachsW II ULFLC1S 307 LLSFFFAMV 14 position is specified, the length 20KKGWEKSQF 13 330 RYLFL AY 14 of peptide Is 9 amino acds, 42 TEPHYSPER 13 331 YLFLNMAYQ 14 and the end position for each 15 LPCISRKLK 12 340 QVHANIENS 14 peptide is the start position 16 PCISRKLKR 12 353 EVWRIEMYI 1 plus eight. -17 C1RKL 12 364 GIMSLGLLS 14 Pos 123456789 score 37 EGIGTIPH II 17 CLPNGINGI 13 1 NLPLRLfTF 21 1 VL!S1YLG 1 18 LPNGINGIC 13 3 PLRLFTFWR 19 4 PCISRKL 10 26 KDARKVTVG 13 5 RLF1TWRGP 14 43 KSLTIRLIR 13 8 TFWRGPVV 1 38 GIGGTWHV 10 5 HVYIGSRNP 13 9 FWRGPYYVA 13 7 FPHVVDVTH 13 TableXXV-V7A-HLA 10 SLWDLEHLL 13 TableXXV-V5B-HLA- A3-9mers-98P4B6 113 LLDVShNR 13 A3-9mers-98P4B6 Each peptide is a portion of 14 NVVSAWALQ 13 Each peptide is a portion of SEQ ID 00: 15; each start 158 PKDASRQVY 13 SEQ ID NO: 11. each start piion is specifed, the 18 QLNFIPIDL 13 position is specified, the length of peptide is 9 amino 2 EIDENLRL 13 length of peptde is 9 amino acds, and the end position 211 LWRGPVVVA 13 acids, and the end position for each peptide is the start 215 PVVVAISLA 13 for each peptide is the start position plus 253 EIVNKTLPI 13sition plus eig L 123456789 score 26 PIVAIILLS 13 Pos 123456789 score 4 SLSETFLPN 15 3 GLLSFFFAM 13 19 ELELEFVFL 15 _ FIYNGINGI 13 311 FFAMVHVAY 13 21 ELEFVFLLT 14 I SP1SLSETF 10 31 MVHVAYSLC 13 24 FVFLLTLLL 14 8 TFLPNGING 8 333 FLNMA V 13 8 QIECSFADT 13 3 YISFGIMSL 13 6 FIQIFCSFA 12 39 SF! STLGY 13 I8 TELELEFVF II TableXXV-V7B-HLA-A3 940 e f rHVL GWK 13 4B6 SICSF 10 9mers-98P46 1 9 13 Each peptide is a portion of D 2 REFSF!QIF 8 SEQ ID NO: 15; each start 1t6 TQ eELEF 8 position is specified, th TableXXV-V2-HLA-A3- 22 LEFVELLTL 7 length of peptide is 9 amino 9mers-98P4B6 adds, and the end position for Each peptide is a portion of each peptide is the start SEQ ID NO: 5; each start TablcXXV-V6-HLA-A3- ht____pls i~ position is specified, the 9mers-98P4B6 r123456789 score length of peptide is 9 amino Each peptide is a portion of AI NA~YS 13 adids, and the end posi t on SEQ ID NO: 13: each start 5 AQQILY 12 for each peptide is the start position is specified, the position plus eight. length of peptide is 9 amino 7 IOSTXYVA __ 201 TableXXV-V7B-HLA-A3- TableXXV-V7C-HLA-A3- TabeXXC-V]4-HLA-A3 9mers-98P4B6 9mers-98P4B6 9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion ot SEQ ID NO: 15; each start SEQ ID NO: 15; each start SEQ ID NO: 29; each start position is specified, the position is specified, the length position is specified, the length length of peptide is 9 amino of peptide is 9 amino acids, of peptide Is 9 amino adds, acids, and the end position for and the end position for each and the end position for each each peptide is the start peptide is t start position peptide is the start position sition lus eit. plus eigh pl.s eit. Pos 123456789 score Pos 123456789 score Pos 123456789 score 3 NMAY STL 8 3 VL-IEWOOD 14 GP 1 STLGYVALL 8 85 PVVGVVI'D 14 8 TFWRGPVVV 14 MAYQQSILG 12 PLWEFLLRL 14 9 FWEGPMVVA 13 146 TUSLATSW 14________ TableXXV-V7C-HLA-A3- 148 SLAFTSMWSL TableXXV-V2I-HLA-A3 9mers-98P4B6 25 ANLRGGLS 3 9mers-98P4B6 Each peptide is a portion of 82 SQIPVVGW 13 Each peptde is a portion of SEQ ID NO: 15; each start 12 GVGPLWEFL 3 SEQ ID NO: 43. each start position is specified, the length position is specified, the of peptide is 9 amino acids, TabeXX. -1-HLA-A3- length of peptide is9 amino and the end position for each 9mers-98P4B6 acids, and the end position peptide is the start position Each peptide is a portion of for each peptide is the start plus eight SEQ ID NO: 17; each start iton lus eight Pos 123456789 score position is specified, the Pos 123456789 score 167 KLETIILSK 28 length of peptide is 9 amino 21 E KTK 27 175 KLIJEQKSK 25 acds, and the end position for 109 ALKAANSWR 24 each peptide is the start TableXXV-V2S-HLA 3 IVILDLSVE 23 position plus eigh. A3-9mers-98P4B6 26 NILRGGLSE 23 Pos 123456789 score Each peptide isa portion of 159 FLGSGTWMK 23 4 FLEEOM(IGT 14 SEQ ID NO: 51; each start 27 ILRGGLSEI 22 5 LEEGMGGTI 10 oifion is specified, the 83 QIPVVGVVT 22 3 QFLEE9MGG length of peptide is 9 amino 13 LASPAAAWK 20 7 EGMGGTIPH 8 acids, and the end position 35IVP~EQQ 20 _6 EEQMGGITIP for each peptide is the start 35 1VLIEW 20 134 LLRLLKSQA 20 tion plus eight 136 RLLKSqAAS 20 TabeXXV-VI3-HLA- Pos 123456789 score 11 EVLASPAAA 19 A3-9mers-98P4B6 2 LFLPCSQK 21 137 LLKSQAASG 19 Each peptide is a portion of I IQLPCISQ 15 170 TAILSKLTQ 19 SEQ ID NO, 27;each start 8 S 15 12 VLASPAAAW 18 position is specified, the 38 PEW DRK 18 lengthofpeptideis9amino 4 LPC1SQ!LK 73 GIRNKSSSS 18 acids, and he end position 3 FQCIQKL 10 5 ILDLSVEVL 17 for each peptide is the start 5 PCISQKLKR tO 9 SVEVLASPA 17 positon plus eig t. 1 45 RKIPPLSTP 17 Pos 123456789 score TableXXVI-V1-HLA-A26 103 PESPDRALK 17 4 SLSETFLPN 15 9mers-98P 6 133 FLLRLLKSQ 1 9 FLPNG17GI 13 Each pepd6 is a portion of 171 IILSKLTQE 17 1 SPKSLSET 1 SEQ ID NO: 3; each start 2 SIVILDLSV 15 8 TFLPNGNG, 8 position is specified, the length 4 of peptide is 9 amino aVSds, 22 CLIJLRGVE 15 TableXXV-V14-HLA-A3- and the end position for each 22 CSTPP 15 9mers-98P4B6 peptide is the start position 46 .KEPPLSTPP 15 69 AQSIN 5Each peptide is aportion of - plus eight 69 A ESGIRN 15 9 IPEP SEQ ID NO:. 29; each start Pos 123456789 score[ 99 SIDPPESPD 15 Y 2 119 VLPTNG position is specified, the length 352 EEVWRIEMY 2 1191 PVLPHTNGV 15 120 VIPHTNGVG 15 of peptde is 9 amino acids. 75 DVTHHEDAL 28 131 WEFLLRLLK 15 and the end position for each 441 VILDLLQL 28 peptide is the start position 177 QVIELAKQL 26 155 SLGEFLGSG 15 plus eight 223 ATFFFLYSF 25 173 LSKLT E ____ 13LKTQEQK 15o 12456789 orel 231 FVRDVUHPY L 25 7 DLtSVE VLAS 14 ) 31DLSEVL I 141Ta LX VCL AA 4 YVAL3-STF 25 SEQ0NO:11 20 EIELPLRL2 202 TableXXVI-VI-HLA-A26- TableXXVT-Vt-HLA-A26- 123456789 score 9mers-98P4B6 9mers-98P4B6 Ijj PJjjj 1 Each peptide is a portion of Each peptide Is a portion of 13 SEQ ID NO 3; each start SEQ ID NO: 3; each start position is specified, the length position is specified, the length TableXXVI-VSB-HLA of peptide is 9 aminoacids, of peptide is 9 amino acids, A26-9mers-98P4B6 and the end position for each and the end position for each Each peptide is a portion of peptide is the start position peptide is the start position SEQ ID N0 11; each start plus eight. plus eight, position is specified, the Pos 123456789 score Pos 123456789 score length of peptide is9 amino 261 IVAITLLSL 24 5 VIGSRNPKF 14 acids, and the end position 217 VVAISLATF 23 83 LTKTN1FV 14 foreachpeptideisthestart 436 LVLPSIVIL 23 131 EYLASLFPD 14 ition plus eighI. 96 EHYTSLWDL 22 138 PDSLIVKGF 14 Pos 123456789 score 234 DVIHPYARN 22 18 ELARQLNF1 14 23 EFVFLLTLL 27 353 EVWRIEMYI 22 21 GPVVVAISL 14 2 FVFLLTLLL 24 390 EFSFIQSTL 22 218 VAISLATFF 14 15 DTQTELELE 20 39 STLGYVALL 21 2 IVNKTLPfV 14 1 ELELEFVFL 18 9 FVAIHREHY 20 30 RKQLGLLSF 1 22 LEFVFLLTL 18 148 VVSAW QL 20 33 KQLGLLSFF 14 2 REFSFIQ[F I 253 EIVNKTLPI 20 31 HVAYSLCLP 14 5 SFIQIFCSF 16 264 ITLLSLVYL 20 365 IMSLGLLSL 14 1 TQTELELEF 1 15 ETCLPNGIN 19 36 MSLGLLSLL 14 20 LELEFVFLL 14 68 EFFPHVVDV 19 43 PNFVLALVL 14 3 EFSFIQIFC 13 115 DVSNNMRIN 19 LDLLQLCRY 14 215 PVVVAISLA 19 TabeXXVI-v6-1{LA 296 ETWLQCRKQ 19 TableXXVI-V2-fLA- A26-9mers-98P4B6 31 VTVGV1GSG 18 A26-9mers-98P4B6 Each peptide is a portion of 187 FIPIDLGSL 18 Each peptideisaportionof SEQ ID NO: 13; each start 21 VVVAISLAT 18 SEQ ID NO: 5; each start position is specified, the 40 STFHVLIYG 18 position is specified, the length of peptide is 9 ammo 439 PSIVILDLL 18 length of peptide is 9 amino acids, and the end position for 2 ESISMMGSP 17 acids, and the end position each peptide is the start 45 LTIRLIRCG 17 for each peptide is the start ption lus ei . 4 TIRLIRCGY' 17 sition plus eight. Pos 1 3456789 score 108 LVGKILIDV 17Pos 123456789 score 263 AITLLSLVY 175 1.GKIIL 23 23 YISFGISL 17 1 SGSPGLQAL 18 6 VILOKIILE 18 360 YISFGIMSL 1715 363 FGlMSLGLL 17 15 SGFTPFSCL 14 41 GTIPIVSPE 18 3 KVTVGVIGS 16 3 SPGLQALSL 1 7 ILGKIILFL 15 1175 GLALSLSL 11 37 EGIGGTIPH 15 128 SNAEYLASL 16 3 PSIVLG 12 259 LPIVAITLL 16 18ITPFSCLSLP 11 3 _________ 1 355 WRIEMYISF 16 23 LSLPSSWDY I 10 KIILFLPCI 12 392 SFIQSTLGY 16 12 SLSSGFTPF 10 45 HVSPERVTV 12 405 ISTFHVLIY 16 36 PCPADFFLY 10 4 SIVILOII 11 432 FVLALVLPS 16 37 CPADFFLYF 10 1 FLPCISRKL I 32 TVGVIGSGD 15 33 CPPPCPADF 9 27 KGWEKSQFL 11 3 GVIGSGDFA 15 35 PPCPADFFL 9 36 EEGIGGTIP 11 72 HVVDVTHHE 15 0 DYRCPPPCP 8 147 NVVSAWALQ 15 3_ PPPCPADFF 8 A26-9mers-98P4B6 257 KTLPIVAIT 15 268 SLVYLAGLL 15TabeXXVI-V5A-HLA- Each peptide is a portion of 32ERLFNNA 15 A26-9mers-98P4B6 SEQ ID NO: 15; each start 32E peptide i o position is specified, the 340 OVHANIENS 151SEQchDpNO:i1; eaca trt length of peptide is 9 amino 375 AVTSIPSVS 151 sio Is spechstd, t acids, and the end position 378 SIPSVSNAL 15 lengtiof peid the for each peptide is the start 381 SVSNALNWR 15 angs of te isd ain sition lus eight. 42 TPPNFVLAL 15 aorseaandpehtendisotheion Pos 123456789 score 55 HVVIGSRNP 14 7 each 23 -position s eig henth TabLeXXVI5BHLA 56 VVIGSRVRPK 14 aci1 SPKSLSETF 12 203 TableXXVI-V7C-H LA- TableXXVI-V2 I-HLA TabteXXVI-V7B-HLA- A26-9mers-98P4B6 A26-9mers-98P4B6 A26-9mcrs-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 15; each start SEQ ID NO: 43; each start SEQ ID NO: 15; each start position is specified, the length position is specified, the position is specified, the of peptide is 9 amino acids, length of peptide is 9 amino length of peptide is 9 amino and the end position for each acids, and the end position for acids, and the end position for peptide is the start position each peptide is the start each peptide is the start plus eight. sition lus ei hi. sition us 'hi. Pos 123456789 score Pos 123456789 score Pos 123456789 score 65 ATAEA ESG 11 E KTKHCMF 20 STLGYVALL 21 71 ESGIRNKSS 11 8 KTKHCMFSL 17 5 AY STLGY 11 82 SQIPVVGVV 11 3 LTQEQKTKH 11 3 NMAY STL 10- 119 PVLPHTNGV 11 8 QSTLGYVAL - 10 141 QAASGTLSL 11 TableXXVI-V25-HLA 143 ASGTLSLAF II A26-9mers-98P4B6 TableX-XVI-V7C-HLA- 145 GTLSLAFTS II Each peptide is a portion of A26-9mers-98P4B6 158 EFLGSGTWM II SEQ ID NO: 51; each start Each peptide is a portion of 17 TRLSKLTQ 11 position is specified, the SEQ ID NO: 15; each start 171 ULSKLT(, I length of peptide is 9 amino position is specified, the length 1185 CMSLISGS I1 acids, and the end position of peptide is 9 amino acids, for each peptide is the start and the end position for each TabIeXXVI-V8-HLA- sition plus eighL peptide is the start position A26-9mers-98P4B6 Pos 123456789 score plus eight. Each peptide is a portion of 3 FLPCISQKL II Pos 123456789 score SEQ ID NO: 17; each start 6 CISOKLKRI 9 16 ETIILSKLT 23 position is specified, the 2 LFLPCISQK 7 EIVLPIEWQ 22 length of peptide is 9 amino 5 PCISQKLKR 7 II EVLASPAAA 21 acids, and the end position _ ILFLPCISQ 6 151 FTSWSLGEF 21 for each peptide is the start 9QKLKRIKKG 5 17 EQKSKHCMF 21 stion lus ei ht. 12 GVGPLWEFL 20 Pos 123456789 score TableXXVII-VI-HLA 3 IVILDLSVE 19 6 EEGMGGTIP 11 B0702-9mers-98P4B6 8 PVVGVVTED 18 7 EGMGGTIPH 11 Each peptide is a portion of 168 LETHLSKL 17 2 SQFLEEGMG 7 SEQ DNO: 3; each start 125 NGVGPLWEF 16 position is specified, the length 13 EFLLRLLKS 16 TabIeXXVI-V13-HLA- of peptide is 9 amino acids, 9 EAQDSIDPP 15 A26-9mcrs-98P4B6 and the end position for each 129 PLWEFLLRL 15 Each peptide is a portion of peptide is the start position DLSVEVLAS 14 SEQ ID NO: 27; each start lus eight. 35 IVLPIEWQQ 14 position is specified, the Pos 123456789 score 68 EAQESGlRN 14 length of peptide is 9 amino 428 TPPNFVLAL 24 88 GVVTEDDEA 14 acids, and the end position 438 LPSIVILDL 24 89 VVTEDDEAQ 14 for each peptide is the start 259 LPIVAITLL 21 9 DSIDPPESP 14 ition lus ei ht. 291 FPPWLETWL 21 12 PHTNGVGPL 14 Pos 123456789 score 125 YPESNAEYL 20 163 GTWMKLETI 14 123 214 GPVVAISL 20 9 SVEVLASPA 13 SPKSLSETFI 12 25 IPIEIVNKT 18 42 QQDRKIPPL 13 62 NPKFASEFF 17 92 EDDEAQDSI 13 TableXXVI-V14-HLA- 211 LWRGPVVVA 17 104 ESPDRALKA 13 A26-9mers-98P4B6 429 PPNFVLALV 17 130 LWEFLLRLL 13 Each peptide is a portion of 157 GPKDASRQV 16 2 SIVILDLSV 12 SEQ ID NO: 29; each start 32 RRSERYLFL 16 5 ILDLSVEVL 12 position Is specified, the 148 VVSAWALOL 15 59 WTEEAGATA 12 length of peptide is 9 amino 198 AREIENLPL 15 152 TSWSLGEFL 12 acids, and the end position 365 IMSLGLLSL 15 176 LTQEQKSKH 12 for each peptide is the start 426 FYTPPNFVL 15 8 LSVEVLASP I Iiti ht. 93 [HREHYTSL 14 45 RKIPPLSTP 11 Po 123456789 score 220 ISLATFFFL 14 51 STPPPPAMW 11 . 261 IVAITLLSL 14 62 EAGATAEAQ 11 FTFWRGP _ 13 287 KYRRFPPWL 14 204 TableXXVII-VI-HLA- TableXXVI-VI-HLA- Each peplideis a portion of B0702-9mers-98P4B6 B0702-9mcrs-98P4B6 SEQ ID N0 11. each start Each peptide is a portion of Each peptide is a portion of position is specified, the SEQ ID NO: 3; each start SEQ ID NO: 3; each start length of peptide is 9 amino position is specified, the length position is specified, the length acids and the end position of pepbde is 9 amino acids, of peptide is 9 amino acids, for each peptide is the start and the end position for each and the end position for each sition lus ei t. peptide is the start position peptide is the start position Pos 123456789 score P lus 128. plus eight 19 ELELEFVFL 5 ____ 147 Pos 123456789 score 1 ADT TELEL 14 37 IPSVSNALN 14 271 YLAGLLAAA 11 2 FVFLLTLLL 13 39 STLGYVALL 14 274 GLLAAAYQL 11 12 SFADTQTEL 12 5 SMMGSPKSL 13 292 PPWLETWLQ 11 22 LEFVFLLTL 12 1 PKSLSETCL 13 297 TWLQCRKQL 11 23 EFVFLLTLL 12 13 FPDSLIVKG 13 323 LPMRRSERY If 2 LELEFVFLL 11 17 QARQQVIEL 13 328 SERYLFLNM 11 21 ELEFVFLLT 10 2 EIENLPLRL 13 378 SIPSVSNAL 1- 10 FCSFADTQT 9 2 ITLLSLVYL 13 394 IQSnGYVA 11 8 QIFCSFAT 8 289 RRFPPWLET 13 425 RFYT 11 16 TQTELELEF 8 3 QCRKQLGLL 13 1 WREFSROI 7 315 VHVAYSLCL 13 TableXXVII-V2-HLA- 2 SFIQEF 7 362 SFGIMSLGL 13 B0702-9mers-98P4B6 5 SFIQIFCSF 7 3 EFSFIQSTL 13 Each peplide is a portion of 6 FIQEFCSFA 7 395 QSTLGYVAL 13 SEQ ID NO: 5; each start 17QTELELEFV 7 43 PNFVLALVL 13 position is specified, the 18 TELELEFVF 7 43 LVLPSIVIL 13 length of peptide is 9 amio 441 IVILDLLQL 13 acids, and the end position 18 LP3NGINGIK 12 for each peptide is the start TableXXVII-V6-ULA 27 DARKVTVGV 12 position plus eih B0702-9mers-98P4B6 IRCGYHVVI 12 Pos 123456789 score Each peptide is a portion of 7 FPHVVDVTH 12 3 SPO ALSL 23 SEQIDNO13;eachstart 105 RHLLVGKIL 12 35 PPCPADFFL 22 position is specified, the 128 SNAEYLASL 12 34 PPPCPADFF 20 length of peptide is 9 amino 133 LASLFPDSL 12 3 CPADFFLYF 20 acids, and the end position for 188 IPIDLGSLS 12 33 CPPPCPADF 18 each ppide is the start 20 ENLPLRLFT 12 1 SGSPGLQAL 141 position plus eigh. 204 LPLRLFTLW 12 15 SGFTPFSCL 14 Pos 123456789 score 212 WRGPVVVAI 12 5 GLQALSLSL 13 43 IPHVSPERV 17 219 AISLATFFF 12 17 FTPFSCLSL 12 7 ILGKIlFL 16 25 NKTLPIVAI 12 SWDYRC 12 LPSILGK 1 299 12CRKQLGL 12 1 SLSSGFrPF 11 27 KGWEKSQFL 12 313 AMVHVAYSL 12 31 YRCPPPCPA I1 45 HVSPERVTV 12 324 PMRRSERYL 12 51 II 360 YISFGIMSL 12 TableXXYII-V5A-HLA- 15 LPCISRKLK II 366 MSLGLLSLL 12 B0702-9mers-98P4B6 14 FLPCISRKL 10 403 LLISTFHVL 12 Eachpeptideisaportion of 38 GIGGTIPHV _I 435 ALVLPSIVI 1 SEQ ID NO.1; each start PfVSPERVr 1 25 ~-position is specified, the length 35 -LEEGIGGTI 9 251 GSDAKSL 1 of peptide is 9 amino acids, 4 VSPERVTVM 9 37 GSGDFAKSL andtheendpositionforeach 6 VIKLF 8 41 FAKSLTIRL __1I 68 EFKSHVVV - peptide is the start position FKFHFVLPCI 8 75 DVTHHEDAL 11 plus eight 7 CISRKLRI 8 85 KTNTIVAL 11 Pos 123456789 score __ WEKSQF 8 85 KTNHFVAI 119 FWRGPVVVA 17 96 EHYTSLWDL __11 100 SLWDLRHLL 11 2 LPLRLFTFW 13 TableXXVH-V7A-HLA 134 ASLFD LI 7 W 9 B0702-9mers-98P4B6 134 FW S I. __) 8 TFWRGPVV 9 ~ Each peptide is a portion of 146 FNVVSAWAL 1 61 LFTWRGPV

-

SEQ ID NO 15; each start 196 _________ _1 position is specified, the 37 HPYARNQQS 11 TabeXXVI-VB-ULA- length of peptide is 9 amino 253 EIVNKTLPI 11 [ 7-9mer98P4B1J acids, and the end position 267T LSLVYLAGLa X 205 for each peptde is the start TablcXXVI-V7C-HLA- peptide is the start position L sitonu e'ht. B0702-9mers-98P4B6 plus eight 123456789 score Each peptide is a portion of Pos 123456789 score PKS 16 SEQ ID NO: 15; each start 9 FWRGPVVVA 17 2 SLSETFL 14 position is specified, the length 2 LPLRLFTFW 13 of peptide is 9 amino acids, 7 FTFWRGPVV 9 TableXXVH-V7B-HLA- and the end position for each 8 TFWROPVVV 9 B0702-9mers-98P4B6 peptide is the start position 6 LFTFWRGPV 8 Each peptide is a portion of plus eight SEQ ID NO: 15; each start Pos 123456789 score TableXXVII-V21-HLA position is specified, the 142 AASGTLSLA 12 B0702-9mers-98P4B6 length of peptide is 9 amino 143 ASGTLSLAF 12 Each peptide is a portion of acids, and the end position for 152 TSWSLGEFL 12 SEQ ID NO: 43; each start each peptide is the start 17 AAAWKCLGA 11 position is specified, the length position plus eiht. 24 GANILRGGL 11 of peptide is 9 amino adds, Pos 123456789 score 27 [LRGGLSEI 11 and the end position for each STLGYVALL 14 44 DRKIPPLST 11 peptide is the start position 8 QSTIYVAL 13 53 PPPPAMWTE 11 plus eight. 3 MAY ST 11 125 NGVGPLWEF Ii Pos 123456789 score 7 QQSTLGYVA 10 ' 148 SLAFTSWSL t 8 KTKHCMFSL 11 2 LNMAYQQST 8 158 EFLGSGTWM 11 5 KTKHCM _ YQQSTLGYV 6 165 WMKLETIL 11 6 EQKTKHCMF 181 KSKHCMFSL 11 9 TKHCMFSLI TableXXVI-V7C-HLA- I SKLTQEQKT B0702-9mers-98P4B6 TableXXVI-V8-HLA Each peptide is a portion of B0702-9mers-98P4B6 TableXXVIH-V25-HLA SEQ ID NO: 15; each start Each peptide is a portion of B0702-9mers-98P4B6 position is specified, the length SEQ ID NO: 17; each start Each peptide is a portion of of peptide is 9 amino acids, position is specified, the SEQ ID NO, 51; each start and the end position for each length of peptide is 9 amino position is specified, the peptide is the start position adds, and the end position length of peptide is 9 amino plus eight. for each peptide is the start acids, and the end position Pos 123456789 score ition plus eight for each peptide is the start 102 PPESPDRAL 24 Pos 123456789 score portion plus eig ht. 15 SPAAAWKCL 22 8 GMGGTIPHV 10 Pos 123456789 score 52 TPPPPAMWT 20 5 LEEGMGGTI 9 3 FLPCISQKL 10 55 PPAMWTEEA 18 1 KSQFLEEGM 7 4 LPCISQKLK 1 105 SPDRALKAA 18 FLEEGMGGT 6 6 CISQKLKRJ 8 101 DPPESPDRA 16 EGMGGTIPH 6 1 ILFLPCISQ 113 ANSWRNPVL 16 EEGMGGTIP 4 5 ILDLSVEVL 14 TableXXVIII-VI-HLA 47 IPPLSTPPP 14 B08-9mers-98P4B6 84 IPVVGVVTE 14 TableXXVII-V13-HLA- Each peptie is a portion of 118 NPVLPHTNG 14 B0702-9mers-98P4B6 SEQ ID NO: 3; each start 141 QAASGTLSL 14 Each peptide is a portion of position is specified, the length 160 LGSGTWMKL 14 - SEQ ID NO: 27; each start of peptide is 9 amino acids, 29 RGGLSEIVL 13 position is specified, the and the end position for each 42 QQDRKIPPL 13 length of peptide is 9 amino peptide is the start position 49 PLSTPPPPA 13 acids, and the end position plus eight. 121 LPHTNGVGP 13 for each peptide is the start Pos 123456789 score 12 GVGPLWEFL 13 ition us ei ht 41 FAKSLTIRL 25 128 GPLWEFLLR 13 123456789 score 203 NLPLRLFTL 25 31 GLSEIVLPI 12 1 SPKSLSEF 16 62 NPKFASEFF 22 48 PPLSTPPP 12 24 PKSLSFL 1 173 QARQQVIEL 22 50 LSTPPPPAM 12 253 EWNKTLPI 22 54 PPPAMWTEE 12 TableXXVH-V14-HLA- 57 VIGSRNPKF 20 61 EEAGATAEA 12 B0702-9mers-98P4B6 81 DALTKTNII 20 81 SSQIPVVGV 12 Each peptide is a portion of 285 GTKYRRFPP 20 122 PHTNGVGPL 12 SEQ ID NO: 29; each start 299 LQCRKQLGL 20 12 PLWEFLLRL 12 position is specified, the length 326 RRSERYLFL --20 139 KSQAASGTL 12 of peptide is 9 amino acids, 385 ALNWREFSF -20 and the end position for each 206 TableXXVIM-VI-HLA- TabeXXVII-VI-HLA- Each peptide is portion B08-9mers-98P4B6 B08-9wers-98P4B6 SEQ 10 NO: 11: each start Each peptide is a portion of Each peptide is a portion of position is specified, the SEQ ID NO: 3; each start SEQ 10 NO: 3; each start length of peptide is 9 amino position is specified, the length position is specified, the length acids, and the end position of peptide is 9 amino acids, of pepbde is 9 amino acids, for each peptide is the start and the end position for each and the end position for each sitio lus ei ht peptide is the start position peptide Is the start position Pos 123456789 score plus eight. plus eight 1 NLPLRLFTF 21 Pos 123456789 score os 123456789 score 3 PLRLFTFWR 13 93 IHREHYTSL 19 142 IVKGFN S 131 1 SLIVKGFNV 1 14 FNVVSAWAL 13 268 SLVYLAGLL 19 196 SSAREIENL 13 TableXXIX-V5B-HLA 9 SPKSLSETC 18 205 PLRLFLwR 13 B08-9mcrs-98P4B6 28 ARKVTVGVI 18 26 FLLSLVYL 13 Each peptide is a portion of 100 SLWDLRHLL 18 304 QL GILFFF _ 13 SEQIDNO: 11;each start 171 NIQARQQVI 18 395 QSTLGYVAL 131 position is specified, the 21 GPVVVAISL _18 39 STIYVALL 13 length of pepbde is 9 amino 25 LPIVAITLL 18 39 TLGYVALLI 13 acids, and the end posito 428 TPPNFVLAL 18 435 ALVLPSIV 13 foreachpeplideisthestart 3 GDFAKSLTI 17 37 GSGDFAKSL 12 position plus ei L 1 10 LLVGKILID 17 SRNPKFASE 12 Pos 123456789 score 15 GPKDASRQV 17 9 EHYTSLWDL 12 19 ELELEFVFL 20 27 GLLAAAYQL 171 15 RHLLVGKIL 12 12 SFADTQTEL 13 291 FPPWLETWL 17 10 VGKILHVS 12 20 LELEFVFLL 13 378 SIPSVSNAL 17 177 QVIELARQL 12 23 EFVFLLTLL 12 438 LPSIVILDL 17 247 FYKIPIEIV 12 LLTLLL 12 24 GIKDARKVT 16 325 MRRSERYLF 12 4 ADTQTELEL '1 44 SLTIRLRC 16 62 SFGIMSLGL 121 22 LFVFLLTL 11 125 YPESNAEYL 16 365 MSLGLLSL 121 16 TQTELELEF 9 155 QLGPKDASR 16 39 EFSFIQSTL 12 18 QLNFIPIDL 16 4 GW EEE 12 2 EIENLPLRL 16 42 FTPPNFVL 12 TableXX(-V6-HA 237 HPYARNQQS 16 43 LVLPSIVL 12 23 YARNQQSDF 1644 VLLQ 12B8mes9P6 231 YLEINKTLD 16 4 IL,1 1 Each peptide is a portion of 251SEQ ID NO: 13 each start 258 TLPIVAITL 16 TabeXXVIII-V2-HLA- position is specified, the 283 YYGTKYRRF 16 B08-9mers-98P4B6 length of peptide is 9 ami 287 KYRRFPPWL 16 Each peptide is a portion of no 3 QCRKOLGLL 16 SEQ ID NO: 5; eh stat achppand the stf 324 PMRRSERYL 16 position is specified, the 403 LLISTFHVL 16 length of peptide is 9 amino position plus eigh. 133 LASLFPDSL 15 ads, and the endposition 1356789( sc23 159 KDASRQVYI 15 foreachpeptideisthestart 6 VILKII 22 17 IELARQLNF 15 position plus eight 61 KOWEKSQF 22 18 FIPIDLGSL 15P 123456789 score 322 CLPMRRSER 1517 CISRKLKRI 21 3 YSFGfMSL 15 5 GLQALSL 17 7 ILGKIILFL 18 I HLLVGKILI 14 35 PPCPADFFL 16 1 KLPCIKL 17 128 SNAEYLASL 14 12 SLSSGFTPF 14 2 LKIKKGW 17 180 ELAR LNFI 14 1 SGSPGLQAL 13 22 RIKKGWE 1 19 SAREIENLP 14 15 SGFTPFSCL 12 4 RIK GKS 1 245 SDFYKIPIE 14 33 CPPPCPADF 12 4 IVILOKO 13 298 CRKQLG 14 34 PPPCPADFF 12 25 IVILOKIII 1 323 LPMRRSERY 14 3 CPADFFLYF 12 25 VSPEKSQ 1 433 VLALVLPSI 14 17 FIPFSCLSL 1 46 VS PE T 12 5 SMMGSPKSL 13 28 SWDYRCPPP 1 23 KRIKKGWEK I1 17 CLPNGINGI 13 10 SLSLSSGF1 91 29 WEKSQFLEE 11 82 ALTKTNIJF 13 91 VAIHREHYT 13 TableXXLX-V7A-HL 103 DLRILLVK 13 08-9mers-98P4BJ6 SA 207 B08-9mers-98P4B6 TableXXIX-VS-HLA- for each peptide s thestar Each peptide is a portion of B08-9mers-98P4B6 sition lus eight. SEQ ID NO: 15; each start Each peptide is a portion of Pos 123456789 score position is specified, the SEQ ID NO: 17; each start 8 S KLKRIKK 23 length of peptide is 9 amino position is specified, the KLKRI 21 acids, and the end position length of peptide is 9 amino for each peptide is the start acids, and the end position sition lus e' 1. for each peptide is the start TableXXIX-V1-HLA Pos 123456789 score poition use hit. B510-9wers-98PB6 I SPKSLSETF 24 Possco Each peptide is a portion of 9 FLPNGINGI 14 GMGGT 9 SEQ ID NO: 3; each start 2 PKSLSETFL I Ition is *pefied, the length of peptide is 9 amino acids, TableXXIX-V7B-HLA- and the end position for each B08-9ners-98P4B6 TableXXIX-V13-HLA- peptide is the start position Each peptide is a portion of B08-9mers-98P4B6 plus eight. SEQ ID NO: 15: each start Each peptide is a portion of Pos 123456789 score position is specified, the SEQ ID NO: 27; each start 93 IHREHYTSL 23 length of peptide is 9 amino position is specified, the 9 EIYTSLWDL 21 acids, and the end position for length of peptide is 9 amino 105 RHLLVGKIL 20 each peptide is the start acids, and the end position 315 VHVAYSLCL 20 hisition us e' t for each peptide is the start 200 EIENLPLRL 15 Pos 123456789 score sition lus e' h 42 FYTTPNFVL 15 8 STLGYVAL 13 Pos 123456789 score 43 LVLPSIVLL 15 9STLGYVALL 13 1 SPKSLSETF 24 54 YHVViGSRN 1 3 NMAY STL 11 9 FLPNGINGI 14 2 TTISLVYL 14 1 FLNMAYQQS 7 PKSLSETFL 1 360 YISFGIMSL 14 TableXXIX-V7C-HLA- TableXXIX-V14-HLA- 365 QSLGYVAL 14 B08-9muers-98P4B6 B08-9mers-98P4B6 77 S 13 Each peptide is a portion of Each peptide is a portion of 99 TSLWDLR- 13 SEQ ID NO: 15; each start SEQ ID NO: 29; each start YSNAEYL 13 position is specified, the length position is specified, the of peptide is 9 amino acids, length of peptide is 9 amino 173 QARQQVEEL 13 and the end position for each acids, and the end position 177 VIELARL 13 peptide is the start position for each peptide is the start 26 PARN!Q 13 plus eight. siton lus e'hi 261 IVAITLLSL 13 Pos 123456789 score Pos 123456789 score 297 TWLQCRKQL 13 179 E KSKHCMF 28 1 NLPLRLFTF 21 390 EFSFIQSTL 13 42 DRKIPPL 21 3 PLRLFTFWR 13 428 TPPNFVLAL 13 73 GIRNKSSSS 21430 PNFVLALVL 13 165 WMKLETIIL 21 TableXXIX-V21-HLA- 5 GS KSL 12 27 ILRGGLSEI 20 B08-9mers-98P4B6 37 ___________ 811 KSKHCMFSL 20 Each peptide is a portion of 41 FAKSLTIIL 12 5 ILDLSVEVL 19 SEQ ID NO: 43; each start 71 _____ 1 15 SPAAAWKCL 19 position is specified, the 78 HIHEDALTKT 12 113 ANSWRNPVL 19 length of peptide is 9 amino 100 SLWDLRHLL 12 129 PLWEFLLRL 18 acids, and the end position for 128 SNAEYLASL 12 148 SLAFTSWSL 1 8 each peptide is the start 133 LASLFPDSL 12 102 PPESPDRAL 17 ition lus ei 1 109 ALKAANSWR 17 Pos 123456789 score 196 SSAREIENL 12 163 GTWMKLETI 17 E KTKHCMF 28 214 GPVVVAISL 12 19 AWKCLGANI 16 8 KTKHC 2 220 ISLATFFFL 31 GLSEIVLPI 16 4 TEKTKHC 11P VNKTL 12 137 LLKSAASG 16 258 TLPVAITL 12 241 GANLRGGL 15 TableXXLX-V25-HLA- 259 LPWATLL 12 24 IILK L 15 B08-9mers-98P4B6 287 KYRRFPPWL 12 171 WLSKCLTE 14 Each peptide is a portion of 324 PMRRSERYL 12 14 AAAWKCLGA 14 SEO ID NO: 51; each start 32 RRSERYLFL 12 141 QAASGTLSL 14 position is specified, the 3 9 S 12 134 LL.RL.LKS A 13 length of peptide is 9 amino 403 LLISTFHVL 12 ads, and the end position e438 LPSiILDL 12 208 TableXXIX-VI-HLA- TableXXIX-V5A-HLA- SEQ ID NO: 15; each start B1510-9mers-98P4B6 B1510-9mers-98P4B6 position is specified, the Each peptide is a portion of Each peptide is a portion of length of peptde is 9 amino SEQ ID NO- 3; each start SEQ ID NO: 11; each start acids, and the end position position is specified, the length position is specified, the length for each peptide is the start of peptide is 9 amino acids, of peptide is 9 amino acids, sition use ht. and the end position for each and the end position for each Pos 123456789 score peptide is the start position peptide is the start position 2 PKSLSEITL 1I us e ht-plus eight. plus eight. I__hs ih SPKSISETF 7 Pos 123456789 score Pos 123456789 score 441 IVILDLLQL 12 1 NLPLRLFTF 7 TableXXIX-V7B-HLA I PKSLSETCL II 8 TFWRGPVVV 7 B1510-9mers-98P4B6 75 DVTIHEDAL 11 9 FWRGPVVVA 7 Each peptide is a portion of 148 VSAW L 1 i1 7 FTFWRGPVV 3 SEQ ID NO: 15; each start 184 QLNFIPFDL 11 position is specified, the 198 AREIENLPL _ 11 length of peptide is 9 amino 201 ILPLRLF I I TableXXIX-V5B-H LA- acids, and the end position for 203 NLPLRLFTL 11 B1510-9mers-98P4B6 each peptide is the start '267 LSLVYLAGL II Each peptide is a portion of sition lus ei ht. 274 GLLAAAYQL II SEQ ID NO: 11; each start Pos 123456789 score 283 YYGTKYRRF 11 position is specified, the 8 STLYVAL 14 300 QCRKQLGLL II length of peptide is 9 amino 3 NMAY STL 12 341 VHANIENSW -I acids, and the end position 9 STLGYVALL 12 351 EEEVWRIEM I1 for each peptide is the start 366 MSLGLLSLL I position plus eight. 378 SIPSVSNAL 11 Pos 123456789 score TableXXIX-V7C-HLA 383 SNALNWREF 11 1 ELELEFVFL 14 B1510-9mers-98P4B6 411 LIYGWKRAF Im 1 SFADTqTEL 13 Each peptide is a portion of 439 PSIVILDLL 11 _ ADTQTELEL 12 SEQ ID NO: 15; each start 2 LELEFVFLL 12 position is specified, the length TableXXIX-V2-HLA- 22 LEFVFLLTL 12 of peptide is 9 amino acids, B 1510-9mers-98P4B6 23 EFVFLLTLL 11 and the end position for each Each peptide is a portion of 1 TELELEFVF 10 peptide is the start position SEQ ID NO: 5; each star 2 FVFLLTLLL 10 plus eight. position is specified, the TQTELELEF 9 Pos 12'456789 score length of peptide is 9 amino 2 REFSFIQIF 7 122 PHTNGVGPL 22 acids, and the end position 5 SF1QIFCSF 7 5 ILDLSVEVL 15 for each peptide is the start 102 PPESPDRAL 15 sition plus ei ht TableXXIX-V6-HLA- 113 ANSWRNPVL 14 Pos 123456789 score B1510-9mers-98P4B6 12 GVGPLWEFL 13 1 SGSPGLQAL 15 Each peptide is a portion of 129 PLWEFLLRL 13 3 PPCPADFFL 12 SEQ ID NO- 13; each start 130 LWEFLLRLL 13 5 GLQALSLSL I .t position is specified, the 24 GANILRGGL 12 1 SGFTPFSCL 11 length of peptide is 9 amino 29 RGGLSEIVL 12 3 SPGLQALSL 10 acids, and the end position for 42 QQDRKIPPL 12 1 FTPFSCLSL 10 each peptide is the start 5 LSTPPPPAM 12 33 CPPPCPADF 9 position plus eight 141 QAASGTLSL 12 1 SLSSGFTPF 8 Pos 123456789 score 160 LGSGTWMKL 12 3 CPADFFLYF 8 44 PHVSPERVT 15 15 SPAAAWKCL 11 3 PPPCPADFF 7 5 IVILGKUIL 14 20 WKCLGANIL II ILGKHLFL 14 139 KSQAASGTL 11 TableXXIX-VSA-HLA- 1 FLPCISRKL 12 148 SLAFTSWSL 11 B1510-9ners-98P4B6 27 KGWEKSQFL 11 152 TSWSLGEFL 11 Each peptide is a portion of 46 VSPERVTVM 10 181 KSKHCMFSL 11 SEQ ID NO: 11; each start 6 VILGKIILF - 8 127 VGPLWEFLL 10 position is specified, the length 26 KKGWEKS F 7 165 WMKLETIIL 10 of peptide is 9 amino acids, 45 HVSPERVTV 7 168 LETIILSKL 10 and the end position for each 183 KHCMFSLIS I peptide is the start position TableXXIX-V7A-HLA lus ei1ht. B1510-9mers-98P4B6 TableXXIX-V8-HLA Pos 12468 score Each peptide is a portion of B1510-9mers-98P4B6 209 Each peptide is a portion of SEQ ID NO: 51; each start TableXXX-VI-HLA SEQ ID NO: 17: each start position is specified, the B2705-9mers-98P4B6 position is specified, the length of peptide is 9 amino Each peptide is a portion of length of peptide is 9 amino acids, and the end position SEQ ID NO: 3; each sa acids, and the end position for each peptide is the start position is specified, the length for each peptide is the start p ion lus ei L of peptide is 9 amino acds, position plus eig Pos 123456789 score and the end position for each Pos 123456789 score KL 10 peptide is the start position I KSQFLEEGM 617 2 L KR4K 6 Iusei I - FLEEGMGGT 4 Pos 123456789 score 8 GMGGTIPHV 4 22 INGIKDARK I 5 LEEGMGGTI 3 TableXXX-VI-HLA- 39 GDFAKSLTI 1 7 EGMGGTIPH 3 B2705-9mers-98P4B6 40 DFAKSLTIR 1 9 MGGTIPHVS 3 Each peptide is a portion of 43 KSLTIRLTR 1 6 EEGMGGTIP 2 SEQ ID NC. 3; each start 5 VVIGSRNPK I position is specified, the length 1121 ILIDVSNNM 1 TableXXIX-V13-HLA- of peptide is 9 amino acds, 175 RQQVIELAR 1 Bl510-9mers-98P4B6 and the end position for each 177 QVIELA&QL I Each peptide is a portion of peptide is the start position 196 SSAREIENL 1 SEQ ID NO: 27; each start plus eight 20 LRLFTWRG I position is specified, the Pos 123456789 score 218 VAISLATFF 1 length of peptide is 9 amino 326 RRSERYLFL 26 225 FFFLYSPVR 1 acids, and the end position 424 YRFYTPPNF 26 233 RDV PYAR I for each peptide is the start 355 WRIEMYISF 25 313 AMVHVAYSL 1 siIon lus eight 198 AREIENLPL 24 319 YSLCLPMRR Pos 123456789 score 240 ARNQQSDFY 22 396 STLGYVALL 1 PKSLSETFL 11 325 vRRSERYLF 22 418 AFEEEYYRF I 1 SPKSLSETFI 7 47 IRLIRCGY- 21 443 ELDLLQLCR 1 _________50 IRCGYHVVI 21, 37 GSGDFAKSL I TableXXIX-V14-HLA- 104 LRHLLVGKI 21 82 ALTKTNIF 15 B1510-9mers-98P4B6 289 RRFPPWLET 21 87 NIIFVAIHR i5 Each peptide is a portion of 416 KRAFEEEYY 21 93 flRJYfL 15 SEQ ID NO: 29; each start 212 WRGPVVVAI 2 96 EHYTSLWDL 15 position is specified, the length 302 RKQLGLLSF 20 155 QLGPKDASR 15 of peptide is 9 amino acids, 417 RAFEEEYYR 20 173 QARQQVEEL 15 and the end position for each 28 ARKVTVGVI 19 295 LE7VLQCRK 15 peptide is the start position 6 RNPKFASEF 19 297 TWL CRK L 1 lus ei ht. 182 ARQLNFIPI 19 329 ERYLFLNMA 15 Pos 123456789 score 19 REIEMYLR 19 3 EFSFIQSTL 1 1 NLPLRLFTF 7 249 KIPIEIVNK 19 41 VALLISTFH 1 8 TFWRGPVVV 7 303 QLGLLSFF 19 409 HVLIYGWKR 15 9FWRGPVVVA 7 53 G _I 411 LIYGWKRAF 1 FTFWRGPVV 3 105 R14LLVGKL 1 438 LPSILDL 15 TableXXX-V2-HLA-179 IELARQLNF 18 SMMGSPKSL TB150eXI-21-4ILA 214, GPVVVAISL 18, 101 PKSLSETCL 14 BI510-9mers-98P4B6 Each peptide is a portion of 241 WQQSDFYK 18 18 LPNGINGIK 1 SEQ ID NO: 43; each startGLLAAAYQL 1 33 VGVIGSGDF 14 position is specified, the length 43 LVLPSIVIL 18 47 VIGSRNPKF 1 of peptide is 9 amino acids, 43 L -i 5 60 SRNPKF 1 and the end position for each 2.____16____ 1 peptide is the start position 174 ARQQVIELA 17 77 TIHEDALTK 1 us eihL 223 ATFFFLYSF 17 12 MRINQYPES 1 Pos 123456789 score 259 LPIVAITLL 17 128 SNAEYLASL 1 8 KTKHCMFSL 11 264 ITLLSLVYL 17 136 LFPDSLIVK E KTKHCM 8 330 RYLFLNMAY 17 146 FNVVSAWAL 1 E KTKHCMF 7 360 YISFGIMSL 17 162 SRQVYICSN 14 TQEQKTKHC 365 IMSLGLLSL 17 167 ICSNNIQAR 1 366 MSLGLLSLL 171 193 GSLSSAREI 14 TableXXIX-V25-HLA- 400 YVALLISTF 200 EIENLPLRL 14 B1510-9mers-98P4B6 430 PNFVLALVL 1 201 ENLPL R L F 14 Each opetide is a portion of 441 aiLDLLQL 1E 7 tiisLATF o 210 TableXXX-V I -HLA- TableXXX-VI-HLA- TableXXX-V2-HLA B2705-9mers-98P4B6 B2705-9mers-98P4B6 B2705-9mers-98P4B6 Each peptide is a portion of Eachpeptideisaportionof Eachpepeisaportionof SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 5; each start position is specified, the length position is specified, the length position is specified, the of peptide is 9 amino acids, of peptide is 9 amino acids, length of pepide is 9 ammo and the end position for each and the end position for each acids, and the end position peptide is the start position peptide is th start position for each peptide is the start plus eight. plus eight. *on plus eit Pos 123456789 score Pos 123456789 score Pos 123456789 score 258 TLPIVAITL 14 17 CLPNGINGI 12 PPPCPADFF 12 261 IVAITLLSL 14 7 FPHVVDVTH 12 35 PPCPADFFL 12 263 AITLLSLVY 14 711PHVVDVTHH 12 24 SLPSSWDYR 11 267 LSLVYLAGL 14 8 EDALTKI 12 37 CPADFFLYF if 28 YQLYYGTKY 14 8 TNIIFVAIH 12 2 GSPGLQALS 9 281 QLYYGTKYR 14 8 IFVAIIEH 12 3 C F 8 299 LQCRKQLGL 14 10 HLLVGKILI 12 301 CRKQLGLLS 14 114 IDVSNNMRJ 12 TableXXX-VSA-HLA 308 LSFFFAMVH 14 133 LASLFPDSL 12 B2705-9mers-98P4B6 318 AYSLCLPMR 14 13 ASLFPDSL 12 Eachpeplideisaportionof 363 FGIMSLGLL 14 164 QVYICSNN 12 SEQIDNO:I1;each start 392 SFI STLGY 14 18 QLNFIPIDL 12 position isspecifed, the 395 QSTLGYVAL 14 18 FIP[DLGSL 12 length of epde is 9 amino 426 FYTPPNFVL 14 205 PLRLFTLWR 12 acids, and the end position 439 PSIVILDLL 14 21 AISLATFF 12 f each peptide is the start 444 LDLLQLCRY 14 231 FVRDVLHY 12 siton lus & h.__ 35 VIGSGDFAK 13 232 VRDVIPYA 12 Pos 123456789 score 98 YTSLWDLRH 13 25 NKTLPIVAI 12 4 LRIFrFWRG 15 99 TSLWDLRHL 13 272 LAGLLAAAY 12 1 NLPLRLFT 13 103 DLRHLLVGK 13 288 YRRFPPWLE 12 3 PLRLFTFWR 11 113 LIDVSNNMR 13 317 VAYSLCLPM 12 5 RtFWRGP 7 117 SNNMRINQY 13 322 CLPMRRSER 12 124 QYPESNAEY 13 328 SERYLFLNM 12 TableXXX-V5B-HLA 129 NAEYLASLF 13 349 WNEEEVWRJ 12 B2705-9mers-98P4B6 138 PDSLIVKGF 13 352 EEVWRIEMY 12 Eachpeptdeisaportionof 148 VVSAWALQL 13 362 SFGIMSWL 12 SEQIDNO:11;eachstart 151 AWALQLGPK 13 381 SVSNALNWR 12 positon Is specified, the 191 DLGSLSSAR 13 383 SNALNWREF 12 lengthofpeptideis9amino 203 acids, and the end position 20 L1RFL 13 35ANWES 12for each peptide is the start 220 ISLATFFFL 13 TPPNFVLAL 12 position plus eighL 229 YSFVRDVIH 13 239 YARNQQSDF 13 TableXXX-V2-HLA- 2123456789 score 246 DFYKIPIEI 13 B2705-9mers-98P4B6 2 REFSFQI 20 251 PtEIVNKTL 13 Eachpeptideisaportionof 5 SFIQEFCSF 1 268 SLVYLAGLL 13 SEQ ID NO: 5; each start 22 LEFVFLLTL 16 279 AYQLYYGTK 13 position is specified, the 283 YYGTKYRRF 13 length of pep is 2 SFADTQTL 16 287 KYRRFPPWL 13 acids, and the end position 14 ADTQTEL 15 291 FPPWLETWL 13 foreachpepideisthestart TELEL 15 300 QCRKQLGLL 13 position plus eig I_1 304 QLGLLSFFF 13 Pos 123456789 s 23 EFVFLLTLL 15 306 GLLSFFFAM 13 5 GLQALSLSL 17 16 TQTELELEF 14 315 VHVAYSLCL 13 9 LSLSLSSGF 15 20 LELEFVFLL 14 337 AY VHAN1 13 15 SGFrPFSCL 15 1 13 348 SWNEEEVWR 13 1 SGSPGLOAL 14 371 LSLLAVTSI 13 3 4O L 1 b ers-96 378 SIPSVSNAL 13 12 SLSSGFTPF 1 Each peesa otn 388 WREFSFIQS 13 23 LSLPSSWDY 14 EQ id O a trt 403 LLISTFHVL 13 17 FTFSCLSL 13 O : 1s ech te 408 FHVLIYGWK 1331 YRCPPPCPA 1 13 i length of peptide is 9 amino 452Po 11 scox 27CPN1G11 acids, and the end position for plus eight. ' TableXXX-V7C-HLA each peptide is the start Pos 123456789 score B2705-9mers-98P4B6 position plus eight 21 KCLGANILR 18 Each peptide is a portion of Pos 123456789 score 29 RGGLSEIVL 18 SEQ ID NO. 15; each start 23 KRIKKGWEK 29 69 AQESGIRNK 18 position is specified, the length 19 SRKLKRIKK 25 167 KLETIILSK 18 of peptide is9 amino acids, 6 VILGKIILF 19 175 KLTQEQKSK 18 and the end position for each 13 LFLPCISRK 19 74 JINKSSSSS 17 peptide is the start position 5 IVILGK1L 18 125 NGVGPLWEF 17 - plus e'ght. ILGKIILFL 18 128 GPLWEFLLR 17 Pos 123456789 score i ILFLPCISR 18 107 DRALKAANS 16 1 TWMKLETH 11 1 PCISRKLKR 16 131 WEFLLRLLK 16 17 EQKSKHCMF 11 2 KKGWEKSOF 16 5 ILDLSVEVL 15 15 SPAAAWKCL 10 LPSIVILGK 15 20 WKCLGANTL 15 30 GGLSEIVLP 10 1 ISRKLKRIK 15 37 LPIEWQQDR 15 7 NKSSSSSQI 10 2 KGWEKSQFL 15 42 QQDRKIPPL 15 9 EDDEAQDSI 10 3 EGIGGTIPH 151 67 AEAQESGIR 15 75 RNKSSSSSQ 8 4 FLPCISRKL 14 I0 IDPPESPDR 15 85 PVVGVVTED 8 4 TIPHVSPER 14 12 GVGPLWEFL 15 145 GTLSLAFTS 8 129 PLWEFLLRL 15 171 IILSKLTQE 8 TableXXX-V7A-HLA- 135 LRLLKSOAA 1 5 185 CMFSLISGS 8 B2705-9mers-98P4B6 158 EFLGSGTWM 15 Each peptide is a portion of 160 LGSGTWMKL 15 TableXXX-VS-HLA SEQ ID NO- 15; each start 168 LETIILSKL 15 B2705-9mers-98P4B6 position is specified, the 24 GANILRGGL 14 Each peptide is a portion of length of peptide Is 9 amino 27 ILRGGLSEI 14 SEQ ID NO: 17; each start acids, and the end position 28 LRGGLSEIV 14 position is specified, the for each peptide is the start 38 PIEWQQDRK 14 length of peptide is 9 amino sition plus eight. 113 ANSWRNPVL 14 acids, and the end position Pos 123456789 score 116 RNPI-1T 14 for each peptide is the start 2 PKSLSETFL 14 sition lus el ht. 2 SPKSLSETF 14 14 QAASGTL 14 Pos 123456789 score 9 FLPNGINGI 12 AL EGMGGTIPH 13 __SETFLPNGI 8143 ASGTLSLAF 14 1G 11 I 8 173 LSKLTQEQK 14 51 KSFLEGM if 71 ETFLPNGIN 13 LASPAAAWK 13 5 LE MGGTI9 8 TFLPNGING 6 31 GLSEIVLPI 13 8 GMGGTPHV TableXXX-V7B-HLA- 44 DRKIPPLST 13 TableXXX-V13-HLA B2705-9mers-98P4B6 109 ALKAANSWR 13 B2705-9mers-98P4B6 Each peptide is a portion of 122 PHTNGVGPL 13 Each peptide Is a portion of SEQ ID NO: 15; each start 148 SLAFTSWSL 13 SEQ ID NO: 27; each start position is specified, the 151 FTSWSLGEF 13 position is specified, the length of peptide is 9 amino 159 FLGSGTWMK 13 length of peptide is 9 amino acids, and the end position for 165 WMKLETIIL 13 acids, and the end position each peptide is the start 176 LTQEQKSKH 13 for each peptide is the start position plus eight 181 KSKHCMFSL 13 sition plus eight. Pos] 123456789 score 39 IEW QQDRKI 12 Pos 123456789 score 91 STLGYVALL 16 102 PPESPDRAL 12 2 PKSLSETFL 14 3 NMAY T 14 103 PESPDRALK 12 1 SPKSLSETF 13 8 QSTLGYVAL 14 130 LWEFLLRLL 12 9 FLPNGINGI 12 5 AYQQSTLGY 13 136 RLLKSQAAS 12 6 SETFLPNGI 8 4 MAYQQSTLG 7 163 GTWMKLETI 12 ETFLPNGIN 6 178 QEQKSKHCM 12 8 TFLPNGING 6 TableXXX-V7C-HLA- 19 AWKCLGANI 11 B2705-9mers-98P4B6 45 RKIPPLSTP 11 TableXXX-V]4-HLA Each peptide is a portion of 50 LSTPPPPAM 11 B2705-9mers-98P4B6 SEQ ID NO:15; each start 108 RALKAANSW 11 Each peptide is a portion of position is specified, the length 115 SWRNPVLPH II SEQ ID NO: 29; each start of peptide is 9 amino adds, 127 VGPLWEFLL 11 position is specified, the and the end position for each 152 TSWSLGEFL 11 length of peptide is 9 amino peptide is the start position 157 GEFLGSGTW 11 acids, and the end position for each peptide is the start 212 position plus eight TabeXXXI-VI-HLA- TableXXXI-VI-HLA 132709-9mers-98P4B36 B2709-9niers-98P4B6 Pos 123456789 score 4 LRLFTFWRG 151 Each peptide is a portion of Each peptde is a portion of I NLPLRLFTF 13 SEQ ID NO, 3; each start SEQ ID NO 3; each start 3 PLRLFTFWR 11 position is specified the length position is specified, the length 5of pepbde is 9 amino acids, of peptide is 9 amino acids, ~I!~~~]iiJand the end position for each and the end position for each TbeX-2-L-pepfide is the start position peptide is the start position TableXXX-V2 I-H LA-_ lset _____ B2705-9mers-98P4B6 - plus eight. Eah etie sa orin fPosl 123456789 score Pos 1123456789 score Each peptide is a portion of182 ARQLNFIPI 19 365 ISLGLLSL 12 SEQ ID NO: 43; each strt35 WRMYF 966 SL LLL 1 position is specified, the length 3 WLLAAYQL 18 395 QSLGYVAL 12 of peptide is 9 amino acids, 289 RRFPPAYQL 18 3 LSTFIIVL 12 and the end position for each 105 RHLLVGKJ 16 406 KRAFEY 12 peptide is the start position 193 GSLSSRI 16 426 FYTPWV 12 plus eight. Posl 123456789 score 214 GPVVVAISL _ 5 428 TPPNFVLAL 12 2 KLTQEQKTK 18__41 IVIDLLQL 15 439 PSIVIL 12 3 LTQEQKTKH 14 37 GSGDFAKSI, 14 8 KTKiHCMFSL 13 39 GDFAKSL1' 14 TableOC-V2-HLA _I QEQKTKHCM 1_ 48 RRCGYHV 4 B2709-9mers-98P4B6 62 TLLSLVYL 14 Each pepde is a portion of ~ 1306 GLLSFFFAM 14 SEQ ID NO: 5;each start TableXXX-V25-HLA- 313 AMVHVAYSL 14 position is specified, the B2705-9mers-98P4B6 425 RFY'-rPNFV 14 length of peptide is 9 amino Each peptide is a portion of 430 PNFVLALVL 14 a and the end position SEQ ID NO: 51: each start 43 LVLPSIL 14 for each peptde is the start position is specified, the 47 IRLRCGYH 13 sition plus ei t. length of peptide is 9 amino 61 R KFASEF 13 Pos 123456789 score acids, and the end position 68 EFFPHVDV 13 5 GLQALSLSL 14 for each peptide is the start 99 TSLWDLRHL 13 3 SPGLQALSL 12 position plus ei t 135 SLFPDSLIV 13 15 SGFTPFSCL 12 Pos 123456789 score 148 VVSAWALQL 131 1 SGSPGLQAL 11 2 LFLPCISQK 18 177 QVIELARQL 13 9 LSLSLSSGF If 5 PCISQKLKR 16 179 IELARQLNF 13 17 FTRFSCLSL 1 7 ISQKLKRIK 15 206 LRLFTLWRG 13 31 YRCPPPCPA It 8 S KLKR1KK 15 220 ISJATFFFL 13 35 PPCPADFFL 11 3 FLPCISQKL 14 287 KYRRFPPWL 13 12 SLSSGFTPF 9 LPCISQKLK 13 297 TWL 6CISQKLKRI 12 3 RK QL 13 33 PPPCPADF 9 KLKRIKKG 9 396 STLGYVALL 13 3 CPADFFLYF 9 I ILFLPCISQ 8 41 FAKSLTIRL 12 32 PPPCPAD 6 185 KTNIIFVAI 12 TableXXXI-VI-HLA- 9 EHYTSLWDL 12 Table XI-VSA-HLA B2709-9mers-98P4B6 114 IDVSNNMRI 12 B2709-9mers-98P4B6 Each peptide is a portion of 120 MRIN YPES 12 Eachpepfideisaportionof SEQ ID NO: 3; each start 125 YPESNAEYL 12 SEQ ID NO: 11; each start position is specified, the length 146 FNVSAWAI 12 position is specified, the of peptide is 9 amino acids, 157 GPKDASRQV 12 length of peptide is 9 amino and the end position for each 1 acds, and the end position for peptide is the start position 2 KDASRL I1 each peptide is the start l0s .sition lus ei h plus eight 223 ATFFFLYSF 12 Pos 123456789 score Pos 123456789 score 227 FLYSFVRDV 121 3261 RRSERYLFL 25RFFW CJ 1 36RSRLL 25 232 VRDVIHYA 121 7 FTFWRGPVV 11 198 AREIENLPL 22 261 IVAITLLSL 12 LFFWRGPV 9 424 YRFYTPPNF 22 267 LSLVYLAGL 12 8TFWRGPVV 9 21 WRGPVVVAI 21 268 SLVYLAGLL 12 1 NLPLRLFTF 8 28 ARKVTVGVI 20 303 KQLGLLSFF 12 50 IRCGYHVVI 20 315 VHVAYSLCL 12 325 MRRSERYLF 20 317 VAYSLCLPM 12 104 LRHLLVK 19 3291 ERYLFLXX A 213 B2709-9mers-98P4B6 sition us e' hI. TableXXXI-V7C-HLA Each peptide is a portion of Pos 123456789 score B2709-9mers-98P4B6 SEQ ID NO: 11; each start 2 PKSLSETFL 10 Each peptide is a portion of position is specified, the 1 SPKSLSETF 9 SEQ ID NO: 15; each start length of peptide is 9 amino SETFLPNG1 9 position is specified, the length acids, and the end position 9 FLPNGINGI 8 of peptide is 9 amino adds, for each peptide is the start 3 KSLSETFLP 5 and the end position for each position plus e'ht- 8 TFLPNGING peptide is the start position Pos 123456789 score plus eight. I WREFSFIQI 19 TablcXXXI-V7B-HLA- Pos 123456789 score 2 REFSFIQIF 15 B2709-9mers-98P4B6 2 SIVILDLSV 10 14 ADTQTELEL 13 Each peptide is a portion of 15 SPAAAWKCL 10 20 LELEFVFLL 13 SEQ ID NO: 15; each start 19 AWKCLGANI 10 22 LEFVFLLTL 13 position Is specified, the 76 NKSSSSSQI 10 2 FVFLLTLLL 13 length of peptide is 9 amino 79 SSSSQIPVV 10 19 ELELEFVFL 11 acids, and the end position for 81 SSQIPVVGV 10 23 EFVFLLTLL 11 each peptide is the start 112 AANSWRNPV 10 5 SFIQ1FCSF 10 sition us ei ht. 127 VGPLWEFLL 10 12 SFADTOTEL 10 Pos 123456789 score 130 LWEFLLRLL 10 I TOTELELEF 10 STLGYVALL 13 143 ASGTLSLAF 10 18 TELELEFVF 10 8 STLGYVAL 1 148 SLAFTSWSL 10 3 NMAY STL_10 158 EFLGSGTWM 10 TableXXX-V6-HLA- 6 YQQSTLGYV 9 160 LOSGTWMKL 10 B2709-9mers-98P4B6 165 WMKLETIIL 10 Each peptide is a portion of TableXXXI-V7C-HLA- 27 ILRGGLSEI 9 SEQ ID NO: 13; each start B2709-9mers-98P4B6 39 IEWQQDRKI 9 position Is specified, the Each peptide is a portion of 78 SSSSSQIPV 9 length of peptide is 9 amino SEQ ID NO: 15; each start 125 NGVGPLWEF 9 acids, and the end position for position is specified, the length 179 EQKSKHCMF 9 each peptide is the start of peptide is 9 amino acids, 66 TAEAQESGI 8 position plus eiht. and the end position for each 92 EDDEAQDSI 8 Pos 123456789 score peptide is the start position 151 FTSWSLGEF 8 7 ILGKIILFL 13 plus eight. 16 TW E- 8 23 KRIKKGWEK 13 Pos 123456789 score 178 KSKHCM 8 5 [VILGKIIL 12 28 LRGGLSEIV 18 182 SKCMFSLI 8 10 KIILFLPCI 12 29 RGGLSEIVL 14 27 KGWEKSQFL 12 31 GLSEIVLPI 14 TableXXXI-V8-HLA 38 GIGGTIPHV 12 126 GVGPLWEFL 14 B2709-9mers-98P4B6 I FLPCISRKL 11 24 GANILRGGL 13J. Each peptide is a portion of 26 KKGWEKSQF 11 5 ILDLSVEVL 12 SEQ ID NO: 17; each start 3 PSIVILGKI 1 107 DRALKAANS 12 position is specified, the 6 VILGKIILF R0 113 ANSWRNPVL 12 length of peptide is 9 amino 19 SRKLERIKK 1 116 WRNPVLPHT 12 acids, and the end position 31 KSQFLEEGI 1 122 PHTNGVGPL 12 for each peptide is the start 43 IPHVSPERV 10 129 PLWEFLLRL 12 sition us ei ht. 45 HVSPERVTV 10 135 LRLLKSQAA 12 Pos 123456789 score 4 SIVILGK I 9 139 KS AASGTL 12 8 GMGGTIPHV 12 17 CISRKLKRI 9 141 QAASGTLSL 12 I KS FLEEGM 10 35 LEEGIGGTI 9 168 LETHLSKL 12 5 LEEGMGGTI 8 4 VSPERVTVM 9 181 KSKHCMFfSL 12 20 RKLKRIKKG 6 4 VILDLSVEV 11 TableXXXI-V13-HLA 41 GTIPHVSPE 6 20 WKCLGANIL II B2709-9mers-98P4B6 42 QQDRKIPPL 11 Each peptide Is a portion of TableXXXI-V7A-HLA- 44 DRKIPPLST 11 SEQ ID NO- 27; each start B2709-9mers-98P4B6 50 LSTPPPPAM II position is specified, the Each peptide is a portion of 74 IRKSSSSS 11 length of peptide is 9 amino SEQ ID NO: 15; each start 82 SQIPVVGVV 11 acids, and the end position position is specified, the 102 PPESPDRAL I1 for each peptide is the start length of peptide is 9 amino 119 PVLPHTNGV 11 'tio lus e . acids, and the end position 152 TSWSLGEFL 11 Po score for each peptide is the start 163 GTWMKLETI 11 ISEFL 1 0 7111 I SPKSLSETF 9 aeXXIV-L-Tbc XIV-HA SSETFLPNGIB4402-9mes-98P4B6 B4402-9mers-98P46 9 FLPNGINGI 8 Eachpeptideisaportionof Eachpeptideisaportiono 3i.STP 5 SEQ ID NO: 3; each start SEQ ID NO: 3; each start 8 TFLPNGjjjj4 POStionis specified, the length position is specified, the length of Peptide is 9 amino adds, of peptide is 9 amino acids, TableXXXI-V14-H LA- and the end position for each and the end position for each B2709-9mers-98P4B6 peptide is the start position peptide is the start position Each peptide is a portion of us ight -lus eighI SEQ ID NO: 29; each start Pos 123456789 score Pos 123456789 score position is specified, the 352EEVWRIEMY 2 10 RILLVGKIL 14 length of peptide is 9 amino 201 IENLPLRLF 24 148 VVSAWALQL 14 acids, and the end position for 179 23 198 _________ 1 each peptide is the start 1 SETCLPNGI 21 2 LPLRLFTLW 14 position plus eig 419 FEEEYYRFY 21 21 VAISLATF 14 Pos 123456789 score 357 TEMYISFGI 2 221 SLATFFFLY 14 - LRIr G 13 42 AKSLTIU 18 258 TLPIVAITL 14 7 FTFWRGPVV 11 436 LVLPSL 18 264 ITLLSLVYL 14 6 LFTFWRGPV 9 117 SNNMRINQY 17 272 LAGLLAAAY 14 TFWRGPVVV 9 144 KGFNVVSAW 17 303 KQLGLLSFF 14 1 NLPLRLFTF 8 259 LPIVArTL 17 313 AIVHVAYSL 14 5 RLFTFWRGP 6 441 IVILDLLQL 17 351 EEEVWRIEM 14 51 SM GSPKSL 16 355 -WRIEMYISF 14 TableXXXI-V21-HLA- 138 PDSLIVKGF 1 3 YISFGIMSL 14 B2709-9mers-98P4B6 _77 QVIELAQL 16 365 IMSLOLLSL 14 Each peptide is a portion of 199 REIENTJLR 16 3 MSLGLLSLL 14 SEQ ID NO: 43; each start 203 NLPLRLFTL 1 383 SNALNWREF 14 position is specified, the length 219 AISLATFFF 1 38 ALNWREFSF 14 of peptide is 9 amino acids, 223 ATFFFLYSF 16 395 QSTLGYVAL 14 and the end position for each 25 NKTLPIVAJ 16 411 LIYGWKRAF 1 peptide is the start position 263 AITLSLVY 16 42 FYTPPNFVL 14 plus e' ht. seht290 RFPPWLETW 16 435 ALVLPSlFVI 14 Pos 123456789 score 392 SFIQSTLGY 16 28 ARKVTVGVI 13 8 KTKHCMFSL 12 403 LLISTFHVL 16 4 TIRLICGY 13 5 E KTKHCM 8 428 TPPNFVLAL 16 9 TSiWDfRHL 13 6 E KTKHCMF 8 4 PSIVILDLL 16 12 PESNAEYLA 13 9 TKHCMFSL1 8 67 SEFFPHVD 15 12 NAEYLASLF 13 TableXXXI-V25-HLA-79 HEDALTKT 15 133 LASLFPDSL 13 B2709-9mers-98P4B6 1 SL FP 15 14 FNV S L 13 Each peptide is a portion of 132 A1 SEQ ID NO: 51; each start 1 QLNFIPI 15 158 PKDASRQVY 13 position is specified, the 196 SSAREIENL 15 18 ELARQLNFI 13 length of peptide is 9 amino 20 EIENLPLRL 15 18 QLNFEPIDL 13 acids, and the end position 212 WRGPVVVAI 15 24 ARNQQSDFY 13 for each peptide is the start 231 FVRDVIHPY 15 251 PIEIVNKTL 13 sition us ei ht. 252 IEIVNKTLP 15 253 EIVNKTLPI 13 Pos 123456789 score 297 TWLQCRKQL 15 268 SLVYLAGLL 13 3 FLPCIS KL 1363 FG1MSLLL 15 274 GLLAAAYQL 13 6 CIS KLKRI 9 378 SIPSVSNAL 15 28 TKYRRFPPW 13 2 LFLPCISQK 4 38 REFSFI ST 15 287 KYRRFPPWL 13 390 EFSFIQSTL 1 302 RKQLGLLSF 13 TableXXXJI-VI-HLA- 396 STLGYVALL 15 311 FFAMVHVAY 13 B4402-9mers-98P4B6 4 YVALLISTF 15 323 LPM!RRSERY 13 Each peptide is a portion of 421 EEYYRFYTP 15 32 RRSERYLFL 13 SEQ ID NO: 3; each start 43 PNFVLALVL 15 328 SERYLFLNM 13 position is specified, the length 438 LPSIVILDL 15 33 RYLFLNMAY 13 of peptide is 9 amino acids, 17 CLPNGINGI 14 341 VHANIENSW 13 and the end position for each AKSL 14 347 NSWNEEEVW 13 peptide is the start position 82 ALTTIIF 14 38 PSVSNALNW 13 Pus eight. 85 KTNHFVAI 14 40 TFHVLrYGW 13 PE12a3c4 peptie score 9p EoYTSLWDL 4 418 AFEEEYYRF 13 r 215 TableXXXII-V1-HLA- TableXXXII-V2-HLA- TableXXXII-V6-HLA B4402-9mers-98P4B6 B4402-9mers-98P4B6 B4402-9mers-98P4B6 Each pepide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 5; each start SEQ ID NO: 13; each start position is specified, the length position is specified, the position is specified, the of peptide is 9 amino acids, length of peptide is 9 amino length of peptide is 9 amino and the end position for each acids, and the end position acids, and the end position for peptide is the start position for each peptide is the start each peptide is the start plus eight. position plus ei ht. sition lus ei h. Pos 123456789 score Pos 123456789 score Pos 123456789 score 42 EEEYYRFYT 13 37 CPADFFLYF 13 VILGKIILF 17 42 YRFYTPPNF 13 17 FTPFSCLSL 12 5 IVILDKIIL 15. 44 LDLLQLCRY 13 3 PPPCPADFF 12 7 ILGKIILFL 15 10 PKSLSETCL 12 _ 51 GLQALSLSL 11 21 KLKRIKKGW 15 39 GDFAKSLTI 12 91 LSLSLSSGF I1 3 PSIVILGKI -14 41 FAKSLTIRL 12 1 KULFLPCI 14 57 VIO3SRNPKF 12 TableXXXII-V5A-HLA- 1 FLPCISRKL 14 61 RNPKFASEF 12 B4402-9mers-98P4B6 17 CISRKLKRI 13 75 DVTHHEDAL 12 Each peptide is a portion of 2 KKGWEKSQF 12 81 DALTKTNI 12 SEQ ID NO: 11; each start 29 WEKSOFLEE 12 94 HREHYTSLW 12 position is specified, the 3 EEGIGGTIP 12 125 YPESNAEYL 12 length of peptide is 9 amino 4 SIVILGKII 11 128 SNAEYLASL 12 acids, and the end position 27 KGWEKSQFL I I 173 QARQQVIEL 12 for each peptide is the start 18 FIPIDLGSL 12 p lusei t TableXXXII-V7A-HLA 21 GPVVVAISL 12 Pos 123456789 s B4402-9mers-98P4B6 217 VVAISLATF 12 1 NLPLRLFTF 16 Each peptide is a portion of 220 ISLATFFFL 12 2 LPLRLFTFW 13 SEQ ID NO: 15; each start .261 IVAITLLSL 12 position is specified, the 267 LSLVYLAGL 12 length of peptide is 9 amino 28 YQLYYGTKY 12 - bleXXXII-SB acids, and the end position 283 YYGTKYRRF 12 B4402-9mers-98P4B6 for each peptide is the start 299 LQCRKQLGL 12 Each peptide is a portion of sition plus eight. 300 RKLGLL 12SEQ ID NO: 11; each start Pos 123456789 Iscore 20 PMREY 12 position is specified, the 6~ S LPiii 21 32 PMRRSERYL 12 length of peptide is 9 amino 9 FLPNGINGI 14 2 325 MRRSERYLF 12 acids, and the end position 9 SPKSLSETF 12 3501 NEEEVWRIE 12 for each peptide is the start 2 PKSLSET 12 353 EVWRIEMYI 12 sition lus eight. str2 PKSLSETFL 12 362 SFGIMSLGL 12 Pos 123456789 scoreT 4 LISTFHVLI 12 REFSFIQ[F 25 TableXXXII-V7B-HLA 405 ISTFHVLIY 12 2 LEFVFLLTL 25 B4402-9mers-98P4B6 _2 LELFVFLL 25 Each peptide is a portion of TableXXXII-V2-HLA- 20 LELEFVFLL 23 SEQ ID NO: 15; each start B4402-9mers-98P4B6 18 TELELEFVF 22 position is specified, the Each peptide is a portion of 5 SFIQIFCSF 6 length of peptide is 9 amino SEQ ID NO: 5; each start 24 FVFLLTLLL 16 acids, and the end position for position is specified, the 19 ELELEFVFL 15 each peptide is the start length of peptide is 9 amino 14 ADTQTELEL 14 osition lus ei ht. acids, and the end position 23 EFVFLLTLL 14 Pos 123456789 score for each peptide is the start 12 SFADTQTEL 12 5 AY STLGY 15 sition plus eight. 9 STLGYVALL 15 Pos 123456789 score TableXXXHI-V6-HLA- 8 STLGYVAL 14 I SGSPGLQAL 18 B4402-9mers-98P4B6 - 3NMYQQSTL 12 15 SGFTPFSCL 15 Each peptide is a portion of 1_31_ 12 33 CPPPCPADF 15 .QD NO: 13; each start TableXXXII-V7C-HLA 3 SPG CALSL 14 position is specified, the B4402-9mers-98P4B6 23 LSLPSSWDY 14 length of peptide is 9 armino Each peptide is a portion of 2 SLSSGFTPF 13 acids, and the end position for SEQ ID NO: 15; each start 2 SCLSLPSW each peptide is the start position is specified, the length 21 SCLSLPSSW 13 sition -lus e h. of peptide is 9 amino acids, 3 PPCPADFFL 13 Pos 123456789 score and the end position for each 3 PCPADFFLY 13 35 LEEGIGGTI 21 peptide is the start position 216 plus eight. for each peptide is e start TableXXXIII-V I -HLA Pos 123456789 score sibon lus eight BSIOI-9mers-98P4B 33 SEIVLPIEW 26 Pos 123456789 score Each peptide is a portion of 15 GEFLGSGTW 24 6 SE G' 21 SEQ ID NO: 3; each start 168 LETllLSKL 239 ZG11 168 ~ ~ ~ ~ N LEILK 39FPGNGI position is specified, the length 39 1EWQQDRKI 2011 KLEF 2 39 IWQQDICJ 0 1 PKS T 12 of peptide is 9 amino acids, and 143 ASGTLSLAF 17 2 PKSLSETFL 1 the end position foreach 51 STPPPPAMW 16 peptide is the start position plus 70 QESGRNKS 16 TableXXI-V]4-HLA eight 103 PESPDRALK 16 B4402-9mers-98P4B6 Pos 123456789 score 113 ANSWRNPVL 16 Eachpeptideisaportionof 27 DARKVTVGV 131 WEFLLRLLK 16 SEQ ID NO: 29; each start 65 FASEFFPIv 23 42 DRKIPPL 15 position is specified, the 37 LAVSPSV 23 5 ILDLSVEVL 14 length of peptide is 9 amio 4 LALVLPSIV 23 61 EEAGATAEA 14 acsds, and the end position 438 LPSIVILDL 22 10 VEVLASPAA 13 for each peptide is the start 24 DFYKIPIEI 21 12 VLASPAAAW 13 sition useight 26 VAITLSLV 21 15 SPAAAWKCL 13 Pos 123456789 score 368 LGLLSLLAV 21 20 WKCLGANIL 13 NLPL 1 428 TPNFVLAL 21 29 RGGLSEIVL 13 2LLLXFi13 42 PPNFVLAIV 21 60 TEEAGATAE 13 23 NGIKDARKV 2 67 AEAQESGIR 13 BteXXI-V8HA 15 GPKDASRQV 20 91 TEDDEAQDS 13 peptidertionPof 21 GPVVVAJSL 20 102 PPESPDRAL 13 E ID e s trt of9 LPIVAITLL 20 108 RALKAANSW 13SEIDN:4,ehstr41FKLRL 9 108 RALAN 13 position is specified, the length 1 YPESNAEYL 19 125 NGVGPLWEF 13peptide Is9 amino acds, 13 L 19 126 GVGPLWEFL 13 and the end position for each 133 LARQQVEL 5 127 VGPLWEFLL 13 130 LWEFLLRLL 13 p s e itio 25 IPIEIVNKT 19 146 TLSLAFTSW 13 291 FPPWLETWL 19 60LSGW_ 13 !~9.6 78QIJIHCMF 50 IRCGYHVVI 18 160 LGSGTWMKL 228 LYSFVRDV 17 165 WMKLETIIL 13 3 Q 17 31 GLSEIVLPI 12 8KTKHCM fSLII 371 LSYLLAN 17 122 PHTNGVGPL 12 9____31___ 1 123 HTNGVGPLW 12 28 ARJVTVGVI 1 129 PLWEFLLRL 12TableXXXII-V25-HLA- 70 FPHVDTH 16 139 KSQAASGTL 12 B4402-9mers-984B6 141 QAASGTLSL 12 Eachpep aportionof 104 LRHLLVGI 16 151 FTSWSLGEF 12 SEQ ID NO: 51; each start 141 LIVKGFNVV 16 179 EQKSKHCMF 12 position is specified, the 16 DASRQVY1C 1 TableXXXII-V8-HLA- of peptide is 9 a 227 LF 16 TableXX)UI-V8-HLA- acids, and the end position 27FYFRV 1 B4402-9mers-98P4B6 for each peptde is the start 237 RPYARNQQS 16 Each peptide is a portion of _ sn lus ei 1. 31 VAYSLCLPM 16 SEQ ID NO: 17; each start Pos 123456789 score 52 COYHYVIGS i position is specified, the 3 FLPC 137 FPDSLIVKG 151 length of peptide is 9 amino C SKL 12 1 QVY]CSNNI I acids, and the end position 2 LFLPCISQK 871 NIQARQQVI 1 for each peptide is the start 91K RK 193 GSLSSARI 1 sition lus ei hL 210 TLWRGPVVV 1 Pos 123456789 score TableXXIIII-V1HL. 212 WRGPVVVAI 15 5 LEEGMGGTI 20 B5101-9mers-98p4B6 27 LAAAYQLYY 1 6 EEGMGGT[P 12 Each peptide is a portion of 349 WNEEEVWRI 1 SEQ ID NO: 3; each start 363 FGIMSLGLL 15 TableXXXII-VI3-HLA- position is specified, the length 397 TLGYvALLI 1 B4402-9mers-98P4B6 f peptide is 9 amino acids, and 425 RFYTPPNFV 15 Each peptide is a portion of the end position for each _8 LPNGINGfK 1 SEQ ID NO: 27; each start peptide is the start position plus 25 IKDARKVTV 1 position Is specified, the ei ht 114 IDVSNNR] 14 length of peptide is 9 amino PoS 123456789 score 152 W QLGPKD I acids, and the end position 81 DALTKTec 29 209 FLWRGPVV I 217 TableXXXIIH-VI-HLA- TableXXXHIII-V5A-HLA- TableXXXIII-V7A B5101-9mers-98P4B6 B5101-9mers-98P4B6 HLA-B5101-9mers Each peptide is a portion of Each peptide is a portion of 98P4B6 SEQ ID NO: 3; each start SEQ ID NO: 11; each start Each peptide is a portion of position is specified, the length position is specified, the length SEQ ID NO- 15; each start of peptide is 9 amino acids, and of peptide is 9 amino acids, position is specified, the the end position for each and the end position for each length of peptide is 9 amino peptide is the start position plus peptide is the start position acids, and the end position eight. lus e ht. for each peptide is the start Pos 123456789 score Pos 123456789 score 'tion lus ei h. 222 LATFFFLYS 14 4 LRLFTFWRG 7 Pos 123456789 score 242 NQQSDFYKI 14 9 FINGINGI 14 258 TLPIVAITL 14 TableXXXHIIU-V5B- I SPKSLSETF 12 278 AAY LYYGT 14 HLA-B5101-9mers- SETFLPNGI 12 379 IPSVSNALN 14 98P4B6 PKSLSETFL 38 LNWREFSFI 14 Each peptide is a portion of 398 LQYVALLIS 14 SEQ ID NO: 11; each start TableXXXI-V7B-HLA 401 VALLISTFH 14 position is specified, the B5101-9mers-98P4B6 4 LISTFHVU 14 length of peptide is 9 amino Each peptide is a portion of 433 VLALVLPSI 14 acids, and the end position SEQ ID NO: 15; each start 435 ALVLPSIVI 1 for each peptide is the start position is specified, the 'tion plus eig h I length of peptide is 9 amino TableXXXIII-V2-HLA- Pos 123456789 score acids, and the end position for B5101-9mers-98P4B6 2 LELEFVFLL 14 each peptide is the start Each peptide is a portion of 1 WREFSFIOI 13 position plus eight. SEQ ID NO: 5; each start 22 LEFVFLLTL 13 Pos 123456789 score position is specified, the 13 FADTQTELE 12 4 MAYQQSTLG 16 length of peptide is 9 amino 12 SFADTQTEL 9 6 Y STLGYV 12 acids, and the end position 17 QTELELEFV 9 9 STLGYVALL - 12 for each peptide is the start 2 FVFLLTLLL 9 3 NMAYQSTL 9 position plus ei ht. 14 ADTQTELEL 8 8 QSTLGYVAL 7 Pos 123456789 score 18 TELELEFVF 8 3 SPGLQALSL 18 19 ELELEFVFL 8 TableXXXH-V7C-HLA 35 PPCPADFFL 16 23 EFVFLLTLL 8 B5101-9mers-98P4B6 15 SGFTPFSCL 15 15 DTQTELELE 6 Each pepide is a portion of I SGSPGLQAL 13 SEQ ID NO: 15; each start 7 QALSILSS 13 TableXXXHI-V6-HLA- position is specified, the length 18 TPFSCLSLP 13 B5101-9mers-98P4B6 of peptide is 9 amino acids, 25 LPSSWDYRC 13 Each peptide is a portion of and the end position for each 37 CPADFFLYF 13 SEQ ID NO: 13; each start peptide is the start position 331 CPPPCPADF 12 position is specified, the plus eiht. 34 PPPCPADFF 12 length of peptide is 9 amino Pos 123456789 score 17 FrPFSCLSL 10 acids, and the end position for 6 TAEAQESGI 22 4 PGLQALSLS __9 each peptide is the start 101 DPPESPDRA 20 5 GLQALSLSL 8 position plus eiht 112 AANSWRNPV 19 Pos 123456789 score 15 SPAAAWKCL 18 TableXXXH-VSA-HL-A- 43 IPHVSPERV 23 160 LGSGTWMKL 18 B5101-9mers-98P4B6 2 LPSIVILGK 16 2 RGGLSEIVL 17 Each peptide is a portion of 27 KGWEKSQFL 16 84 IPVVGVVTE 17 SEQ ID NO: 11; each start 35 LEEGIGGTI 15 102 PPESPDRAL 17 position is specified, the length 15 LPCISRKLK 14 141 QAASGTLSL 17 of peptide is 9 amino acids, 17 CISRKLKRI 14 24 GANILRGGL 16 and the end position for each 3 PSIVILGKI 13 39 IEWQQDRKI 16 peptide is the start position 39 IGGTIPHVS 13 31 GLSEIVLPI 15 plus eight. 38 GIGGTIPHV 12 68 EAQESGIRN 15 Pos 123456789 score 4 SIVILGKII 11 82 SQIPVVGVV 15 2 LPLRLFrFW 16 7 ILGKHLFL 11 108 RALKAANSW 15 8 TFWRGPVVV 15 1 KILFLPCI 11 149 LAFTSWSLG 15 7 FTFWRGPVV 13 14 FLPCISRKL 11 163 GTWMKLETI 15 6 LFTFWRGPV 10 45 HVSPERVTV I11 5 ILDLSVEVL 14 9]FWRGPVVVA 8 27 ILRGGLSEI 14 218 TabIeXXXIIU-V7C-HLA-8 GMJIjlHV 12 6ISQL1IT 4 B5101-9mers-98P4B6 L G1V RLA2 3FS I44 10 Each peptide is a portion of L2G§GT H8 jHH 8j 7 SEQ ID NO: 15; each start position is specified, the length TableXXXII-V13- TableXXXIV-VI-HLA-A1. of peptide is 9 amino acids, HLA-B51O1-9mers- 1Omers-98P4B6 and the end position for each 98P416 Each peptide is a portion of SEQ peptide is the start position Each peptide is a portion of ID NO: 3; each start position is plus eight. SEQ ID NO: 27; each start specified, the length of peptide Pos 123456789 score position is specified, the is 10 amino acids, and the end 37 LPIEWQQDR 14 length of peptide is 9 amino position for each peptide is the 47 IPPLSTPPP 14 acids, and the end position start position plus nine. 48 PPLSTPPPP 14 for each peptide is the start Pos 1234567890 score 54 PPPAMWTEE 14 )sto lseat31EE)M Y 2 121 LPHTNGVGP 14 Pos 1234567 9 sore 391 351 26 127 VGPLWEFLL 149 LNIG 1448AFE i5V 2 128 GPLWEFLLR 14 1SPKSLSETF 12 443 ILDLLQLCRY 26 4 VILDLSVEV 13 SETF[PNGI 12 220 IaLATFEFLY 24 13 LASPAAAWK 13 21PKSLSETFL 8 262 VAITLLLVY 23 18 AAWKCLGAN 13 327 RSERYLFLNM 23 52 TPPPPAMWT 13 TableXXXIIi-V14-HLA- 45 LIMJRCGY 22 53 PPPPAMWTE 13 B5101-9mers-98P4B6 275 LLAAAQLYY 22 62 EAGATAEAQ 13 Each peptide is a portion of 4 USTFHVUY 22 95 EAQDSIDPP 13 SEQ ID NO: 29; each start 116 VSNNMRINQY 20 142 AASGTLSLA 13 positon is specified, the length 123 NQYPESNAEY 20 164 TWMKLETH 13 ofpeptideis9aminoacids, 27 YLAGLLAAAY 19 17 AAAWKCLGA 12 and the end position for each 279 AYQLYYQTKY 19 64 GATAEAOES 12 peptide is the start position 427 YPPNFVLAL 19 76 NKSSSSSQI 12 plus eight _38 18 79 SSSS0[PVV 12 PosJ 1 8 274 GLLAAAYQLY 18 92 EDDEAQDSI 12 2 106 LWDLR1LLVG 17 105 SPDRALKAA 12 7 TFWRGPVV 1 157 GPKDASROVY 17 I1 KAANSWRNP 121 178 VIELARL 17 118 NPVLPHTNG 12 23 SFVRVIHY 17 129 PLWEFLLRL 12 239 YA"WSDFY 17 182 SKiCMFSLI 12 _ __ 396 STLGYVALLI 17 16 PAAAWKCLG 11 6 AEFFPHVD 16 28 LRGGLSEIV 11 B5 e rx-mv21HL 89 WVAIREHY 16 56 PAMWTEEAG 11 B5101-9mis a p 16 81 SSQIPVVGV 11 I 12 NAEYLASLFP 16 119 PVLPHTNGV _1 position is specified, the31 168 LETIILSKL 11 322 CLPMRRSERY 16 19 AWKCLGANI 10 acds, and the end position 23 LGANILRGG 10 for each peptide is 41 G WREEE 15 30 GGLSEIVLP 10 sition pus ei . _1 ________ 151 55 PPAMWTEEA 10 Pos 123456789 score 415 WKRAFEEEYY 15 78 SSSSSQIPV 10 9 TKiCMFSLI 13 13 LSETCLNGI 1 113 ANSWRNPVL 10 3LT E KTKH 125 YPESNAEYLA 1 130 LWEFLLRLL 10 8 KTKHCMFSL 2 QaDFYKUPIE 14 ____________257 KTLPIVAITL 14 TableXXXIIII-V8-HLA- TableXXXII-V25-HLA- 7 VTHHEDALTK 13 B5101-9mers-98P4B6 BSIOI-9mcrs-98P4B6 198 ARE[ENLPLR 13 Each peptide is a portion of Each peptide is a portion of 3 M5LGLLSLLA 13 SEQ ID NO:17; each start SEQIDNO51;eachstart 42 E 13 position is specified, the position is specified, the 25 IKDARKVTVG 1 length of peptide is 9 amino length of peptide is 9 amino 135 SLFPDSLIVK 12 acids, and the end position adds, and the end position 13 FPDSLIVKGF 12 for each peptide is the start for each peptide is the starl 2 EIENLPLRLF 1 sition ls eiht. sition us e hi 221 SLATFFFLYS 1 Pos 123456789Sco Pos 123456789 score 251 PIEIVNKTLP 12 LEMGI I41 LPCISQK K 114 268 SLVYLAGLLA 1121 219 TableXXXIV-VI-H LA-Al- TableXXXIV-V7C-HLA S10mers-98P4B6 TableXXXIV-V6-HLA-Al- Al-l&s98P4B6 Each peptide is a portion of SEQ 10mers-98P4B6 Each peptide is a portion of SE ID NO: 3; each start position is Each peplide is a portion of ID NO 15; each start position Is specified, the length of peptide SEQ ID NO: 13; each start specified, the length of peptide is 10 amino acids, and the end position is specified, the length is 10 amino acids, and the end position for each peptide is the of peptide is 10 amino acids, position for each peptide Is the start ition lus nine. and the end position for each tart position plus nine. Pos 1234567890 score peptide is the start position plus Pos 1234567890 score 419 FEEEYYRFYT 12 nine. ILDLSVVLA 13 439 PSIVILDLLQ 12 Pos 1234567890 score 103 PPESIDRALK 13 2 GWEKSQELEE 19 124 HTNGVGPLWE 13 TableXXXIV-V2-HLA-Al- 35 FLEEGIGGTI 13 168 KLEfILSKL 13 10mers-98P4B6 3 LEIEGIGGTIP 12 1 SYEVLASPAA 12 Each peptide is a portion of I LVLPSIVILG 11 39 PIEWQQQRKI 12 SEQ ID NO: 5; each start 19 ISRKLKRIKK 11 43 QQDRKIEFLS 12 position is.specified, the length 42 GIIPHVSPER 10 52 STPPPPAMWT 12 of peptide is 10 amino acids, 9 LGKIILFLPC 9 1 PFSPDRALKA 12 and the end position for each 106 SPDRALKAAN 12 peptide is the start position TableXXXIV-V7A-HLA- 128 V PLWEfLLR 12 us nine. A I-I0mers-98P4B6 17 JI KLTQ 12 Pos 1234567890 score Each peptide is a portion of 97 A2DS1DPPES II 35 PECPADFFLY 24 SEQ ID NO: 15; each start 115 NSWRNPVLPH 11 22 CLSLPSSWDY 16 position is specified, the B SWSLGEELGS It 28 SWDYRCEPPC 12 length of peptide is 10 amino 2 PS1Vff.LSV 10 2 GSPG14ALSL I1I acids, and the end position for 61 TEEAGATAEA 10 each peptide is the start 67 TAEAQESGIR 10 TableXXXIV-V5A-HLA- sition lus nine. 92 ThDDEAQDS _ 10 Al-10mers-98P4B6 Pos 1234567890 score 93 E __ 10 Each peptide is a portion of LSETFLPNGI 14 157 LGEFLGSGTW 10 SEQ ID NO: 11; each start 4 KSLSETFLPN 131 position is specified, the length 8 ETFLPNGING I 11178 TQE K LET 10 of peptide Is 10 amino acids, and the end position for each TableXXXIV-V7B-HLA-LTPPPAMW 9 peptide is the start position plus Al-10mers-98P4B6 nine. Each peptide is a portion of Pos 1234567890 score SEQ ID NO: 15; each start TableXXXIV-V8-HLA 8 FIFWRGPVVV 8 position is specified, the length Al-l0mers-98P4B6 I ENLPLRLFTF 4 of peptide is 10 amino acids, 2 NLPLRLFTFW 4 and the end position for each Each peptide is a portion of 4 PLRLFTFWRG 4 peptide is the start position plus SEQ ID NCr 17; each start 10 FWRGPVVVAI 3 nine. position is specified, the length ________________ soreof peptide is 10 amino acids, Pos 1234567890 scored TableXXXIV-V5B-HLA- TLAY GY21 and the end position for each Al -I Omrs-9P4B6_ 1 peptide is the start position A-10mers-9846 STLGYVAL 17us nine. Each peptide is a portion of SEQ ID NO: 11; each start TableXXXIV-V7C-HLA- fLEEGMGGTI 13 position is specified, the length Al-10mers-98P4B6 of peptide is 10 amino acids, Each peptide is a portion of SEQ and the end position for each ID NO: 15; each start position is TableX1V-V3-HLA peptide is the start position specified, the length of peptide plus nine. is 10 amino acids, and the end pepties a8po n f Pos 1234567890 score position for each peptide is the E ID e s tart -14 FADTTELEL 17 start position plus nine. sQ i N2ech the 18 QIELELEFVF 17 Pos 1234567890 score posgtion pep ife the 22 ELEFVFLLTL 17 131 LWEFLLRLLK 19 lenth e Isi0oamio 20 ELELEFVFLL 14 33 LSEIVLPIEW 18 as and the str 16 DIQTELELEF 12 91 VTEDDEAQDS 17 each pl s ites 21 LELEFVELLT 11 6 WTEEAGATAE 16 t368 u s 2 WREFSFIOIF 10 100 SIDPPESPDR 16 6 LSETFLPNGI 14 5_ FSFIIEFCSF 8 70 AQESGIRNKS 14 4D NO- EF N 151ac3trtpstin1 124 EFVFLLTLLLIT 8 94 DDEAQDSIDP 1 141 220 TeFLIGING II TabeXXXV-VI-HLA- TabeXXXV-VI-HLA A0201-0mrs-98P4B6 A0201-m0mers-98P4B6 TableXXXIV-V14-HLA- Each peptide isa portion of SEQ Each peptide is a portion of SEQ Al-I Omers-98P4B6 ID NO: 3; each start position Is ID NO: 3; each start position is Each peptide is a portion of specified, the length of peptide is specified, the length of peptide is SEQ ID NO: 29; each start 10 amino acids, and the end 10 amino acds, and the end position is specified, the length position for each peptide is the position tor each peptide is the of peptide is 10 amino acids, start position plus nine, start position pius nine. and the end position for each Pos 1234567890 score Pos 1234567890 score peptide is the start position plus 364 GIMSL L 27 179 IELARQLNFI 17 nine. 132 YLASLEPDSL 26 202 ENLPLRLFTL 1 PosJ 1234567890 score 37 LLSLLAVTSI 26 25 IIEIVNKTL 17 8JFTFWRGPVVV 8 437 VLPSIMILDL 26 2 1TLLSLVYLA 17 1 ENLPLRLFTF 4 82 ALTKTIIFV 25 26 LVYLAGLLAA 17 2 NLPLRLETFW 10 SLWDLRHLLV 25 348 SWNEEEVWRI 17 4 PLRLFTFWRG j 4 14 SLIVKGFNVV 25 361 ISFGIMSWL 17 10oFrwlGhPVVyV~l 3 263 AIT1LSLVYL 25 369 GLLSLLAVTS 171 306 GLLSFEFAMV 2 401 VALLISTFHV 17 TableXXXIV-V21-HLA-Al- 402 ALLISTF1VL 25 2 KDARKVTVGV 10mers-98P4B6 440 SIVILI&!LQ 25 41 FAKSLTIRJ 1 Each peptide is a portion of TLPIVA 24 111 KILIDVSNNM 1 SEQ ID NO: 43; each start 365 IMSLGLLSLL 2 112 ILIDVSNNMR 1 position is specified, the length 403 LLISTFHVLI 24 127 ESNAEYLASL I of peptide is 10 amino acids, 427 YTPNVLAL 24 195 SSARIENL and the end position for each 24 GIKWAJCVTV 23 223 ATFFFLYSFV I peptide is the start position plus 48 R.LIRCGYHVV 23 22 FFLYSFVRDV 1 nine. __ 13 DLRHLLVGKI 23 268 SLVYLAGLLA 1 Pos 1234567890 score KTKHCMESLI 433 VLALVLPSIV 23 299 LQCRKQLGLL I 9 THW L 192 AJHREHYTSL 22 356 RIEMYISFGI 1 5T EQKTKHCM 10 260 PVAITLISL 22 362 SFGIMSLOLL I _I LSKLTQEQKT 6 261 IVAITLLSLV 2 377 TSIPSVSNAL 1 4 LTQEQKTKHC 6 298 WLQCRKQLGL 22 428 TPPNFVLAIV 16 E TKHCMFSLIS 6 432 FVL VLPSI 2 434 LALVLPSI 16 TabeXXXIV-V25-H07 RLFLWGPV 21 438 LPS LDLL TAb-1eXXXI-V25--lLA 210 TLWRGPVVVA 21 443 TILDL Q LC RY __6 Al l0mers-98P4B6__ Each peptide is a portion of 257 KTLPIVAITL 21 27 DARKVTVGVI 15 SEQ ID N9- 51; each start 385 ALNWREFSFI 21 3 IGSGDEAKSL 151 position is specified, the 49 LIRCGYHVVI 20 44 SLTIURCG 15 length of peptide is 10 amino 98 YTSLWDLRHL 20 47 IPLIRGYHV 15 acids, and the end position for 172 IQARQQVIEL 20 147 NVVSAWALQL 15 eadi peptide is the start 18 NFIPDLGSL 20 16 YICSN1AR 15 sition lus nine. 219 AISLATFFFL 20 18 PIDLGSLSSA 1I Pos 1234567890 score 227 FLYSFVRDVI 20 199 REIENLPLRL 15 8 IS KLKRIKK 1 249 KIPIEIVNKT 2 221 SLATFFFLYS 15 5 LE-CIS KLKR 8253 EIVNKTLPIV 20 25 VNKTLPIVAI IS 3 LELPCISQKL 6 12 SLSETCLPNG 19 273 AGLLAAAYQL 15 135 SLFPDSLIVK 19 275 LLAAAXQLYY 15 TableXXXV-VI-HLA- 142 IVKGFNVVSA 19 314 MVHVAYSLCL Is A0201-10mcrs-98P4B6 197 SAREIENLPL 19 33 NMAYQQVHAN I5 Each peptide is a portion of SEQ 209 FTLWRGPVVV 19 33 MAYQQYHANI 15 ID NO: 3; each start position is 211 LWRGPVVVAI 1 34 lENSWNEEEV 15 specified, the length of peptide is 271 YLAGLLAAAY 19 3 FQSTLGYVAL 15 10 amino acids, and the end 312 FAMVHVAYSL 19 395 QSTLGXVALL 15 position for each peptide is the 39 STLGYYALU _ 19 41 STFHVLIY 15 start position plus nine. 1 TCLPNGINGI 18 11 1IYGWKRAFE 15 Pos 1234567890 score 65 FASEFFPHVV 18 373 LLAVTSIPSV 31 6 SEFFPHVVDV 18 TabIeXXXV-V2-HLA 2 LLSLVLAGL 29LDVSNMRI 18 A0201-0mers-98P4B6 107 LLVGKILIDV 28 35 MYISFG1MSL Each peptide is a portion of 367 SLGLLSLLAV 28 3 F _ SEQ ID NO 5; each start 435 ALVLPStheL 28 of HLLVGK pLIeD 1 i s specify ied, the len th 221 of peptide is 10 amino acids, A0201-1Omers.98P4B6 Each peptide is a portion of SEQ and the end position for each Each peptide is a portion of ID NO: 15; each start position is peptide is the start position SEQ ID NO: 13; each start specified, the lnth of peptide Is -_ plus nine. position is specified, the length 10 amino acids, and the end Pos 1234567890 score of peptide is 10 amino acids, position for each peptide is the 2 GSPGLALSL 16 and the end position for each start position plus nine. 5 GLQALSLSLS 15 peptIde is the start position plus Pos 1234567890 score _6 GFTPFSCLSL 15 nine. 5 VILDLSV2VL 2 10 SLSLSSGFTP 14 Pos 1234567890 score 168 KLETHLSKL 26 8 ALSLSLSSGF 13 7 VILGKILFL 28 12 SLSSGFTPFS 13 35 FLEEGIGGTI 22 28 LLRGGLSEIV 24 24 SLPSSWDYRC 13 5 SC1J 20 130 PLWEFLLRLL 24 4 PGQALSLSL 12 14 LFLPCISRKL 18 1 FLGSGTWMKL 23 7 QALSLLSSG 12 43 TIPHVSPERV 18 IVILDLSVEV 22 1 SSGFTEFSCL i1 2 VLPSILGK 17 66 ATAQ7 GI 19 22 CLSLPSSWDY 10 13 ILFLPCISRK 17 81 SSSQIEVVGV 1 9 LSLSLSSGFT 3 LPSMLKI 1 156 SLEFLGSGT 19 17 FTPFSCLSLP 8 8 "KWLFLP 16 6 ILDLSVEVLA 18 6 ALSLSLSS 7 GKIILFLPCI 1 32 GSELPIE 18 34 PPPCPADFFL 7 38 EGIGGTLPHV 1 112 KAANSWRNPV 18 _I LVLPSIVILG 14 113 AANSWRNPVL 18 TableXXXV-VSA-HLA- 46 HVSPERVTVM 14 12 GPLWEFLLRL 18 A0201-10mers-98P4B6 12 ILLFLPCISR 13 8 DLSVEYLASP 1 Each peptide is a portion of 34 QFLEEGIGGT 13 19 AAWKCLGANI 17 SEQ ID NO: 11; each start 79 SSSSSQIVV 17 position is specified, the length TabICXXXY-V7A-HLA- 127 GVGPLWEFLL 1 of peptide is 10 amino acids, A0201-I0mers-98P4B6 134 FLLRLLKSQA 1 and the end position for each Each peptide is a portion of 135 LLRLLKSQAA 1 peptide is the start position plus SEQ 10 NO: 15; each start nine. Pos 1234567890 score the 31 GGLSIYLPI 1I ____1234567890 scor length of peptide is 10 amino 421 WQQDR.KIPPL 16 6 RLFTFWRGPV 21 acids, and the end position 58 AMWTEAGAT I 8 FTFWRGPVVV 18 each peptide is the start 1 FWRGPVVVAI 18 Position plus nine. 84 S. GVV 1 7 LFTFWRGPVV 11 Pos 1234567890 score 12 ThVGPL 10 I TFWRGPVVA 11 5 STh1 PNG 19 137 LPHTN AG I 2 NLPLRLFTFW 10 9 TFLPNGINGI 18 138 LLKSQAASG I 2 SPKSLSETFL 11 148 LSLAFTSWSL 16 TableXXXV-VSB-HLA- 6 LSETFLPNGI 1 13 VLASPAAAWK is A0201-10mers-98P4B6 10 FLPNGYNGIX 1 23 CLOANILRGG 15 Each peptide is a portion of SEQ ID NO: 11; each start TabeXXXV-V7B-HLA- 2 LG EFL - i position is specified, the length A0201-I0mers-98P4B6 163 SWMLETI 15 of peptide is 10 amino acids, Each peptide is a portion of 3 SIVIL E 14 and the end position for each SEQ ID NO: 15; each start 2 LRGOLSE 14 peptide is the start position position is specified, the length 29 PIEGQDRI 14 plus nine. of peptide is 10 amino acids, Pos 1234567890 score and the end position for each 121 VLPHTNGVGP 14 22 ELEFVFLLTL 22 peptide is the start position plus 139 LKSQAASGTL 1 20 ELELEFVFLL 20nine. 42 QAASGLSLA 14 1 FADTQTELEL 18 Pos 1234567890 score 164 GTWMXLETII 14 23 LEFVFLLTLL 17 1 STLGYVALL I 1 171 TLLSKLTQE 14 19 TELELEFVFL 16 2 FLNMAQQST 18 172 MKLLTQEQ 14 17 TQTELELEFV 15 6 AYQQSTLGYV 16 18 AAAWKCLGAN 13 12 CSFADTQTEL 13 3 LNMAYQQSTL 1 50 PLSTPPPPAM 13 QFCS[ADTQ 9 STWYVALL IS 100 SIDPPESPDR 13 21 LELEFYFLLT 1 8 QQSTLGYVAL 13 149 SLAFTSWSLG 13 1 NWREFSFIQI 41MAYQQSTLG 2 SIVLDLSV 12 7 FIQIFCSFADA 20 AWKCLGANL 12 Table)OXXV-V7C-LA- 47 KIPST 12 TableXXXV-V6-HLA- A0201-10mcrs-98P4B6 52 STPPPPAMWTP 12 222 TableXXXV-V7C-HLA- TableXXXVT-V2-HLA A0201-10mers-98P4B6 [q G VA II A0203-1tmers-98P4B6 Each peptide is a portion of SEQ Each peptide is a portion of ID NO: 15; each start position is SEQ ID NO: 5; each start specified, the length of peptide is TableXXXV-V21-HLA- position is specified, the length 10 amino acids, and the end A0201-10mens98P 6 of peptide is 10aminoacids, position for each peptide is the Each peptide Is a portion of and the end position for each start position plus nine. SEQ ID NO: 43; each start peptide is the start position Pos 1234567890 score position is specified, the length pus nine. 83 SQIPVVGVVT 12 of peptide is 10 amio acids, Pos 1234567890 score 102 DPPESPDRAL 12 and the end position for each 3 DYRCPPPCPA 10 119 NPVLPITNGV 12 peptide is the start position plus 31 YRGPPCPAD 9 12 NGVGPLWEFL 12 nn. I SGSPGL ALS 8 144 ASGTLSLAFT 12 Pos 1234567890 score 3 R-PPPCPADF 8 173 ILSKLTQEQK 12 31KT 1 176 KLTQEQKSKH 12 9 KTKHCMFSLI 1 TabICXXXVI-V5A-HLA 181 QKSKHCMFSL 12 8 QKTKHCMFSL I1 A0203-10mers-98P4B6 _I ESKLTQEQKT 7 Each pepide is a portion of LTQEQKTKHC SEQ ID NO: 1; each start TableXXXV-V8-HLA- 2 SKLTQEOKTK 5 position is specified, the length A020 1-0mers-98P4B6 of pepde is 10 amino acids, Each peptide is a portion of TableXXXV-V25-HLA- and the end position for each SEQ ID NO: 17; each start A0201-l0mers-98P4B6 peptide is the start position plus position is specified, the lth Each peptide is a portion of nine. of peptide is 10 amino acids, SEQ ID NO: 51; each start 1234567890 score and the end position for each position is specified, the 9TEWRGPYVA 10 peptide is the start position length of peptide is 10 amnino 10 FARGPYVyA4J9 jlus nine, acids, and the end position___________ Pos 1234567890 Iscore for each peptide is the start TableXXXVI-V5B-HLA 5 FLEEGMGGTI 22 position plus nine. A0203-I0mers-SIPB6 8 EGMGGTIPHV 15 Pos 1234567890 score Each peptide is a portion of 9 GMGGTIPHVS 12 31 LFLPCISQKL 18 SEQ ID NO: 11; each start -2 ILFLPCISQK 171 position is specified, the TablcXXXV-V13-H LA- I IILFLPCISQ 13 length of peptide is 10 amino A0201-10mers-98P4B6 4 FLPCISQKLK 10 acids, 6 the end position Each peptide is a portion of _6 PCISQKLKRI 10 for each peptide is the start SEQ ID NO: 27; each start __ CISQKLKRIK 8 sition lus nine. position is specified, the Pos 1235790Jsor length of peptide is 10 amino TableXXXVI-VI-HLA -_ acids, and the end position for A0203-0mers-98P4B6 each peptide is the start Each peptide Is a portion of SEQ psition plus nine. posiion~89 plsni ID NO: 3; each start position is ________ Posspecified, the lenh of peptide is TabeXXXVV6-HLA 51 SLSETELPNG 19 10 amino acds, and the end A0203-l0mers-98P4B6 9 TFLPNGINGI 18 position for each peptide is the Pos 1234562890 sore 2 SPKSLSETFL 11 start P ion us nn. NoResultsFound. LSETFLPNGI 11 Pos 1234567890 score 1 FLPNGINGIK 11 27 VYLAGLLAAA TableXXXVI-V7A 269 LVYLAGLLAA II19 HLA-A0203-l0mers TableXXXV-V14-HLA- I KGFNVV$AWA 18 98P4B6 A0201-10mers-98P4B6 271 YLAOLLAAAY j1 Pos 1234567890 score Each peptide is a portion of NoResulisFound. SEQ ID NO: 29; each start TableXXXVI-V2-HLA position is specified, the length A0203-10mers-98P4B6 of peptide is 10 amino acids, Each peptde is a portion of TableXXXVI-V7B-HLA and the end position for each SEQ ID NO: 5; each start A0203-l0mers-98P4B6 peptide is the start position plus position is specified, the length Each peptide is a portion of nine. of peptde is 10 amino a SEQ ID NO: 15; each start Pos 1234567890 score and the end position for each position is specified, the length RLFTFWRGPV 21 peptide is the start position of peptide is 10 amino acids, 8 FTFWRGPVVV 18 ne. and the end position for each 10 FWRGP VA 18 [ 1234567890 score peptide is the start position plus 223 nime. 10 amino acids, and the end TableXXXVII-V1-HIA-A3 Posl 1234567890 Iscore position for each peptide is the I Omers-98P4B6 -QSTLGY-VA 10start position plus nine Each peptide is a portion of SEQ 8o STLGYVAPos 1234567890 score ID NO 3 each start position is QSTLGYVALL 8 135 SLFPDSLIVK 28 fled, the length of peptide is 34l GV1GS(DjFAK 26 10 amino adds, and tie end TableXXXVI-V7C-HLA- 271 YLAGLLAAAY 26 position for each peptide is the A0203-10mers-98P4B6 48 RURCGYHVV 24 start position lus nin. Each peptide is a portion of SEQ 21 INGIKDARK 23 Pos 1234567890 score ID NO: 15; each start position is 216 VVVAISLATF 23 262 VAJTLLSLVY 1 specified, the length of peptide is 369 (3LSLLAVTS 23 263 ATLLaLVYL 1 10 amino acids, and the end 171 CLPNGING[K 22 265 TLSVYLAG I position for each peptide is the 55 HVYIGN 2SFFFAMV 16 start position plus nine. 27LL LYY 22 322 CLPMRRSERY 1 Pos 1234567890 score 278 AAYQL 22 3 ANTENSW 16 11 VEVLASPAAA 27 30 LLSFFF 367 SLGLLSLLAV 16 10 SYEVLASPAA 19 EAMV H 21 385 ALNWRFFSFI 16 105 ESPDRALKAA 19 1VKGFNVVSA 21 432 FVLALYLPS1 16 135 LLRLLKSQAA 19 1 QLGPKDASRQ 21 433 VLALVLPSfV 16 5 PAMWTEEAGA 18 2: '. i7LWRGPVVVA 21 44 SIVILDL L 1 59 MWTEEAQATA 18 76 -IEDALTK 2 4 !VMDLWLC 1 61 TEEAGATAEA 18 21 VVAISLATFF 2 32 TVGV1OGDF 15 12 EVLASPAAAW 17 248 YKJPIErvNK 2 1 SLWDLRHLLV 15 10 SPDRALKAAN 17 10 HLLVGKILID 15 13 LRLLKSQAAS 17 121 RINQYFESNA 15 2941WLETWL RK 20 153 ALOLGPKDAS 15 TableXXXVI-V8-HLA- 402 ALLISTFHVL 20 187 FIPIDLGSLS 15 A0203-10mers-98P4B6 21 ES1SMMGSPK 19 221 SLATFFFLYS 15 Pos 1234567890|score 4 LIRCqYHVVI 19 235 VWPYARNQQ 15 NoResultsFound. 5 W GSR PKF 19 25 KTLPIVATL 15 TbeXVVI102 WDLR-HLLVGK _9 2 60 PIVAITLISL 15 TableXXXVI-V3-1 SAALQL 1 320 LP RSE 15 HLA-A0203-10mers- 227 FLYSFVRDVI 1 372 SLLAVUEPS 15 98P4R6 269 LVYLAGLLAA 19 393 Fl STLGYVA 15 PosJ12345678901score 375 AVTSIPSVSN 19 436 LVLPSWILD 15 NoResultsFound. 4 I JQLCR _ 19 6 SRNPKFASEF 14 TabeXXXVI-V4-HLA- GjDAKVTV 18 88 IIFVAHREH 14 A0203-10mers-98P4B6 14 SLVKGFNVV 18 103 DRHLLVGKI 14 A003ImesL4B 33 FLIL{MAYQQVH 181 108 LVGKILIDVS 14 Pos 1234567890 score 410 VLIYGWKRAF 18 111 KILIDVSNNM 14 9TFWRGPVVVA 10 411 LlYGWI AE 18 132 YLASLFPDSL 14 10 FWRGPVVAI 435 ALVLPSIVL 18 15 SAWALQLGPK 14 442 VILD11LQLCR 18 171 MQARQQVIE 14, TableXXXVI-V21- 46 T(RLIRCGYH 17 18 ELARQLNHP 14 HLA-A0203-10mers- 92 AFREffML 17 189 PIDLGSLSSA 14 98P4B6 _ QVYICaNNIQ 17 19 IDLGSLSSAR 14 Pos11234567890|score 177 OWELAQLN 17 205 PLFTLWRG 14 NoResultsFound. 25 NKTLPIVA 17 215 PVVAISLAT 14 _Z_____ 61 WA1TIJSLV 17 231 FVRDVIIIPYA 14 TableXXXVI-V25- 268 SLVYLAGLLA 17 2 LL$LVY1AGL 14 HLA-A0203-10mers- 331 YLFLNMAYQQ 17 279 AY LYYGTKY 14 98P4B6 4 YVALLISTFH 17 31 HVAYSj LPM 14 Pos|1234567890 score 403 [LISTEHYLI 17 370 LLSLLAVTSI 14 NoResultsFound. 4 LISTFHVLIY 17 45 LTXRLMCGY 13 30 KVTVGVIGSG 16 751 DVTfHEDALT 13 TableXXXVH-VI-HLA-A3- 123 NQYPESNAEY 16 _2 A! ]EFL 13 10mers-98P4B6 141 LIVKGFNVS 16 128 SNAFYLASLF 13 Each peptide is a portion of SEQ 178 VIELAQLNF 16 154 LQLGPKASR 13 ID NO. 3; each start position is 20 RLFTLWRGPV 16 157 GPKDASRQVY 13 fSpecified, She length of peptide is Q 1 16 YI-CSNWQAR 13 1913 DLGSLSSARE 13 224 TableXXXVII-VI-HLA-A3- TabIeXXXVII-VSA-HLA 10mers-98P4B6 A3-10mers-98P4B6 TableXXXVII-V7A-HLK~ Each peptide is a portion of SEQ Each peptide is a portion of A3-1 Omers-98P4B6 ID NO: 3; each start position is SEQ ID NO: 11; each start Each peptide is a portion of specified, the length of peptide is position is specified, the length SEQ ID NO: 15; each start 10 amino acids, and the end of peptide is 10 amino acids, position is specified, the position for each peptide is the and the end position for each length of peptide is 10 amino start position plus nine. peptide is the start position plus acids, and the end position for Pos 1234567890 score nine. each peptide is the start 20 E!ENLPLRLF 13 Pos 1234567890 score lion lus nine. 2 LPLRLFTLWR 13 9 TFWRGUYVVA 11 Pos 1234567890 score 240 ARQQSDFYK 13 3 IPLRIFFWR 10 1 FLPNGINGIK 22 298 WLQCRK LGL 13 T FWRGPVVVAI 10 SL.SETEL 12 3 QLGLLSFFFA 13 8 FTFWRGPVVV 9 31 FFEAMVHVAY 13 LFTFWRPVV 7 TableXXXVII-V7B-HLA 314 MVHVAYSLCL 13 A3-10mers-98P4B6 321 LCPMRRSER 13 TableXXXVII-V5B-HLA- Each peptide is a portion of 329 ERYLFLIMAY 13 A3-10mers-98P4B6 SEO ID NO: 15; each start 353 EVM _EMYIS 13 Each peptide is a portion of position is specified, the length 364 G11SLGLLSL 13 SEQ ID NO: 11; each start of peptide is 10 amino adds, 373 LLAVTIPSV 13 position is specified, the and the end position for each 39 TLGYVALLIS 13 length of peptide is 10 amino peptide is the start position plus 399 GYVALLISTF 13 acids, and the end position for nine. 40 YWKRA 13 each peptide is the start Pos 1234567890 scome 437 VIPSIVTLDL 13 position plus nine. 5 MAY ILQQ GY 13 445 DLLQLCRYPD 13 Pos 1234567890 score 2 FLNMAYQQST 12 QIFCSFADT 17 10 STLGYyALLI 11 TableXXXVII-V2-HLA- 22 ELFVELLTL 17 3 LNMAYQQSTL 9 A3-10mers-98P4B6 1 QTELELEFVF 1 7 Y STLGYVA 7 Eachpeptide is a portion of 2 E LEFVFLL 11 8 QQSTLYVAL 7 SEQ ID NO: 5; each start I FJQIFCSFAD 10 1 LFLNMAYQQS 6 position is specified, the length IQIFCSFADT 8 9 QSTLGYVALL of peptide is 10 amino adds, and the end position for each TableXXXVII-V6-HLA- TableXXXVH-V7C-HLA peptide is the start position A3-10mers-98P4B6 A3-llmers-98P4B6 plus nine. Each peptide is a portion of Each peptide is a portion of SEQ Pos 1234567890 score SEQ ID NO: 13; each start ID NO: 15; each start position is 8 ALSLSLSSGF 21 position is specified, the length specified, the length of peptide is 1 SL0 LS FTP 19 of peptide is 10 amino acids, 10 amino acids, and the end 2 CLSLPSSWDY 17 and the end position for each position for each peptide is the 5 GLALSLSLS 15 peptide is the start position plus start position plus nine. 32 RCPPPCPADF 15 nine. Pos 1234567890 score 12 SLSSGFTPFS 11 Pos 1234567890 score 13 VLASPAAAWK 28 24 SLPSSWDYRC 11 13 ILFLPCISRK 26 173 ILSKLTEQK 25 GSPG[9ALSL 10 VLESI1ILGK 23 137 RLLKSQAASG 24 33 CPPPCEADFF 10 15 FLPCISRKLK 21 1 EVLASPAAAW 21 18 CISRKLKRJK 21 1 FLLRLLKSQA 21 TableXXXVII-VSA-HLA- 6 IVILGKIILF 20 IVILDLSVEV 20 A3-10mers-98P4B6 22 _U GWE 19 3 IVLPIEWQQD 20 Each peptide is a portion of 35 FLEEGIGGTI 19 12 PVLPHTNGVG 20 SEQ ID NO: 11; each start 12 IULFLNISR 18 17 KL EQKSKH 20 position is specified, the length 46 HVSPERTVM 18 83 SQIPVGVVT 18 of peptide is 10 amino acids, 23 LKRIKH WEK 17 8 QIEVVQVVTE 18 and the end position for each II KHLFLPCIS 16 15 SLGEFLGSGT 18 peptide is the start position plus 19 ISRKLKRIKK 16 167 MKLETIJLSK 18 nine. I LVLPSIVILG 15 3 SIVILDLSVE 17 Pos 1234567890 score 7 VILGKIILFL 15 ILDLSVEVLA 17 R TWRGPV 16 25 RIKKGWKSQ 15 28 ILRGGLSEIV 17 PLRLFTFWG 14 2 EKKGWEKSOF 15 7 G -NKSSSS 17 1 ENLPLRLFTF 13 3 GIGGTPHVS 15 VVEDDEAD 17 2 N1PLRLEFW 2 8 ILGKIILFLP 12 121 VLPHTNGVGP 17 225 TableXXXVII-V7C-HLA- SEQ ID NO: 29; each start TabICXXXVII-VI-HLA A3-l0mers-98P4B6 position is specified, the length A26- I mers-98P4B6 Each peptide is a portion of SEQ of peptide is 10 amino acids, Each peptide is a portion of SEQ ID NO: 15; each start position is and the end position for each ID NO: 3; each start position is specified, the length of peptide is peptide is the start position plus specified, th length of peptide is 10 amino acids, and the end nine. 10 amino acids, and the end position for each peptide is the Pos 1234567890 score position for each peptide is the start position plus nine. 6 RLFTFWRGPV 161 tart position plus nine. Pos 1234567890 score 4 PLRLFIFWRG 14 Pos 1234567890 score 138 LLKSQAASGT 17 1 ENLPLRLFTF 13 127 ESNAEYLASL 23 27 NILRGGLSEI 16 2 NLPLRLFTFW 12 427 YTPPNFVLAL 23 1 S1DPPESPDR 16 9 TFWRGPVVVA i 44 SWILDLLQL 23 110 ALKAANSWRN 16 3 LPLRLIFFWR 10 45 LTIRLIRCGY 22 168 KLETHLSKL 16 10 FWRGPVVVAI 0 34 DV PYARNQ 22 171 TIMIKLTQE 16 8 FTFWRQEVVV 9 253 EIVNKTLPIV 22 5 VILDLSVEVL 15 7 LFIFWRGPVV 7 260 P1VAITLLSL 22 8 DLSVEVLASP 15 329 ERYLFLNMAY 21 26 ANILRGGLSE 15 TableXXXVII-V21-HLA- 15 ETCLPNGING 20 37 VLPIEWQQDR 15 A3-10mers-98P4B6 32 TVGVGSGDF 20 135 LLRLLKSQAA 15 Each p_,e is a portion of 98 YTSLWDLRHL 20 14 TLSLAFTSWS 15 SEQ ID NO: 43; each start 353 EVWRIEMYIS 20 149 SLAFTSWSLG 15 position is specified, the length 159 EFLGSGTWMK 15 of peptide is 10 amino acids, 75 DVTHHEDALT 19 175 SKLTQEQKSK 15 and the end position for each 115 DVSNNMRINQ 19 38 LPIEWQQDRK 14 peptide is the start position plus 186 NFIPIDLGSL 19 47 KIEPLTPPP 14 nine. 230 SFYRDVIHPY 19 103 PPESPDRALK 14 Pos 1234567890 score 257 KTLPIVAITL 19 109 RALKAANSWR 14 8 314 MVHVAYSLCL 19 131 LWEFLLRLLK 14 21SKLTQEQ_ KY 17 131LWFL~RLK 14 ~ I~ 2 LA 364 GEMSLGLLSL 19 127 GVGPLWEFLL 13 404 LISTFHVLIy 19 143 AASGTLSLAF 13 TableXXXVII-V25-HLA- VVAISLATFF 18 A3-10mers-98P4B6 359 MYISFGESL 18 TableXXXVII-V8-HLA- Each peptide is a portion of 3 GYVALLISTF 18 A3-10mers-98P4B6 SEQ ID NO. 51; each start 4 IVDLLQLC 18 Each peptide is a portion of position is specified, the ESISMMGSPK 17 SEQ ID NO- 17; each start length of peptide is 10 amino 30 KVTVGVIGSG 17 position is specified, the length acids, and the end position 40 DFAKSLTIRL 17 of peptide is 10 amino acids, for each peptide is the start 81 DALTKIIF 17 and the end position for each sition lus nine, peptide is the start position Pos 1234567890 score 26 ATLLSLVYL 17 lus nine. 2 ILFLPCIS K 29 Pos 1234567890 score FLPCIS KLK 20177 QVIELQ1N 1 51FLEEGMGGTI 19 7 CIS KLKRIK 18 269 LVYLAGLLAA 16 1 ILFLPCISQ 14 TableXXXVU-VI3-HLA- 435 ALVLPSIVIL 16 A3-10mers-98P4B6 TabIeXXXVH1-VI-HLA- 436 LVLPSIVILD 16 Each pepide is a portion of A26-10mers-98P4B6 34 GVIGSGDFAK 15 SEQ ID NO: 27; each start Each peptide is a portion of SEQ 72 HVVDVTHHED 15 position Is specified, the ID NO: 3; each start position is 116 VSNNMRINQY 15 length of peptide is 10 amino specified, the length of peptide is 142 JVKGFNVSA 15 acids, and the end position for 10 amino acids, and the end 199 REIENLPLRL 15 each peptide is the start position for each peptide is the 25 IPIErVNTL 15 ition lus nine. start position plus nine. 261 [VAITLLSLV 15 Pos 1234567890 score Pos 1234567890 score 262 VAITLLSLVY 15 10 FLNGINGMK 22 216 VVVAISLATF 27 31 FFFAMVHVAY 15 5 SL rELPNG 12 29 ETWLCRKQL 27 377 TSIPSVSNAL 15 20 EIENLPLRLF 26 389 REFSFIQSTL 15 147 NVVSAWALQL 25 391 FSFJQSTLGY 15 Tab[eXXXV1-V14-HLA- 351 EEEVWRIEMY 25 32 FVLALVLPSI 15 A3-10mers-98P4B6 202 ENLPLRLFTL 24 31 VTVGVIGSGD 14 ac ptide is a *onof 5 VVIGSRNPKF 23 55 HVVIGSRNPK 14 89 IFVALHREHY 114 226 TableXXXVII-VI-HLA- TableXXXVrn9V2-Hjjj.3S EGIGUTIPHV 18 A26-10mers-98P4B6 A26-I0mers-98P4B6 VILGKLL 17 Each peptide is a portion of SEQ Each Peptide is a portion of IjyVP4PLG j6 ID NO: 3; each start position is SEQ 1D NO: 3; each start 15 specified, the length of peptide is position is specified, the length 13 10 amino acids, and the end of peptide is 10 amino acids, position for each peptide Is the and the end position for each TableXXXVIII-V7A start sition lus nine. peptide is the start position HLA-A2&IOmers-98P4B6 Pos 1234567890 score pus nine. Each peptide is a portion of 103 DLRHLLVGKI 14 Pos 1234567890 score SEQ ID NO: 15; each start 108 LVGKILIDVS 14 30 PPPCPA 8 position is specified, the 148 VVSAWALQLG 14 34 PPPCPADFFL 8 length of peptide is 10 amino 222 LATFFFLYSF 14 7 ALSLSLSS 7 adds. and the end position for 301 CRK LGLLSF 14 18 TPFSCLSLPS 7 each peptide is the start 352 EEVWRIEMYI 14 3 SPG ALSLS 6 sition us n 362 SFGIMSLGLL 14 Pos 1234567890 417 RAFEEEYYRF 14 TabeXXXVI..V5A-HLA. 8 ETFLPNG1NG 2 43 VLPSIVILDL 14 A 2 6-10mers-98P4B6 443 ILDLLQLCRY 14 Each peptide is a portion of TableXXXVIII-V7B-HLA. 27 DARKVTVGVI 13 SEQ ID NO: 11; each start A26-]Omcrs-98P4B6 7 VDVTHHEDAL 13 position is specified, thelength Each peptide is a portion of 9 AIHREHYTSL 13 ofpepbdeis10ammnoacids SEQIDNQ15,eachstart 13 FPDSLIVKGF 13 and the end position for each position is specified, the length 17 1 AR VIEL 13 peptideisthestartpositonplus ofpeptideis10aminoacids 17 VIELAR L 13 nine, and the end position for each 178 VIELAR LNF 13 Pos 1234567890 score peptide Is the start position plus 21 VAISLATFFF 13 1 ENLPLRLFTF 24 nine. 223 ATFFFLYSFV 138 FTFWRGP V 12 Pos 1234567890 Score 25 TLPIVAITLL 13_ 9 QS MALL 13 2 LQCRKQLGLL 13 TableXXXVIll.V5B-HRA 5 MAYQOSTLGY 11 30 RKQLGLLSFF 13 A26-J0mers-98P4B6 3 LNMAYQQSTL 1 358 EMYISFGIMS 13 Each peptide is a portion of STLGYVALLI 10 361 ISFGIMSLGL 13 SEQ ID NO: 11; each start 8 STLGYL 9 365 MSLLLSL position is specified, the length 365 IMSLGLLSLL 13pepide is 10 amino acids, 375 AVTSIPSVSN 13 aeX VII7CHA 375 VTSIPSVSNA 13 and the end position for each A26-0mers-98P4B6 375 VSTSSVNA 13 peptidle is mhe start position Each peptide is a porton of 395 4 STLGYVALL 13 his nine. SEQ ID NO 15; each start 41Pos 1234567890 score Posion is specified, the length TableXXXVI-V2-HA-16 DTQTELELEF 25 of peptide is 10 amino acids, A26-10mers-98P4B36 22 ELEFVFLLTL 24 and the end position for each Eah- petieisprtionP4of 24 EFVFLLTLLL 23 peptide is the start position plus Each peptide is a portion of20E LFV Lnie SEQ ID NO: 3; each start ELELEFVF 1 P 13 70 c position is specified, the length 23 LEFVF 1 17 1234567890 24 of peptide is 10 amino acids, and the end position for each 4 EFSFIQIFCS 1 12 EVLASPAAAW 21 peplide is the start position 5 FSFIQIFCSF 13 35 EWLIEWQQ 19 lus nine.WEFSFIIF 1 102 DPPESPDRA 19 Pos 1234567890 score 12 CSFADTQTE I 1 GVGPLWEFLL 19 17 FTPFSCLSLP 13 5 VILDLSVEVL 17 16 GFTPFSCLSL 12 TableXOOVIII-V6-HLA 152 FTSWSLGEFL 17 35 PPCPADFFLY II A26-0mers-98P4B6 69 EAQESGRNK 16 2 GSPGLQALSL 10 Eachpeptideisaportionof 105 ESPDRALKAA 16 4 PG LSEQ ID NO 13; each start 89 GVVTEDDEA 15 14 SSGFTPFSCL 10 position is specified, the length 133 EFLLRLLKSO 15 22 CLSLPSSWDY 10 of peptide is 10 amino acids, 151 AFTSWSLGEF 15 22 CLS LSSWY 10 and the end position for each 3 SIVIDLSVE -14 peptide is the start position pus 11 LSLSSGFTPF 9 45 DRKIPPLSTP 14 32 RCPPPCPADF 9 Pos 1234567890 score 33 CPPPCPADFF 9 ILGKIILF 27 9 VVTEDDD 14 36CPA LYFT 9 5 SIVLKIIL 18 227 TableXXXVIII-V7C-HLA- I 8|ETFLPNGING) 24| TableXXXIXVI-HLA A26-110mers-98P4B6 B0702-10mers-98P4B6 Each peptide is a portion of TableXXXVIII-V14-HLA- Each peptide is a portion of SEQ SEQ ID NO: 15; each start A26-10mers-98P4B6 ID NO: 3; each start position is position is specified, the length Each peplide is a portion of specified, the length of peptide is of peptide is 10 amino acids, SEQ ID NO: 29; each start 10 amino acids, and the end and the end position for each position is specified, the length position for each peptide is the peptide is the start position plus of peptide is 10 amino acids, start position plus nine. nine. and the end position for each Pos 1234567890 scorer Pos 1234567890 score peptide is the start position plus 323 LPMRRSERYL 21 99 DSIDPPESPD 14. nine. 137 FPDSLIVKGF 18 130 PLWEFLLRLL 14 Pos 1234567890 score 428 TPPNFVLALV 17 168 KLETIILSKL 14 1 ENLPLRLFTF 24 125 YPESNAEYLA 16 171 TULSKLTOE 14 81FTFWRGPVV 12 214 GPVVVAISLA 16 8 DLSVEVLASP 13 219 AISLATFFFL 16 42 WQQDRKIPPL 13 TableXXXVUI-V21-HLA- 394 IQSTLGYVAL 16 93 EDDEAQDSID 13 A26-I0mers-98P4B6 36 IGSGDFAKSL 15 122 LPHTNGVGPL 13 Each peptide is a portion of 197 SAREIENLPL 15 125 TNGVGPLWEF 13 SEQ ID NO- 43; each start 325 MRRSERYLFL 15 129 GPLWEFLLRL 13 position is specr'6, the length 361 ISFGIMSLGL 15 10 SVEVLASPAA 12 of peptide is 10 amino acids, 379 IPSVSNALNW 15 3 IVLPIEWQQD 12 and the end position for each 427 YTPPNFVLAL 15 72 ESGIRNKSSS 12 peptide is the start position plus 211 LWRGPVVVAI 14 95 DEAQDSIDPP 12 nine. 263 AITLLSLVYL 14 12 PVLPHTNGVG 12 Pos 1234567890 score 402 ALLISTFHVL 14 12 NGVGPLWEFL 12 4 LTQEQKTKHC 10 4351 ALVLPSIVIL 14 41 EWQODRKIPP I1 _ EQKTKHCMFS 10 40 DFAKSLTIRL 13 6 WTEEAGATAE - 1 8 QKTKHCMFSL 10 92 AJHREHYTSL 13 62 EEAGATAEAQ 11 6,E KTKHCMF 9 127 ESNAEYLASL 53 63 EAGATAEAQE 11 1 KTHCMFSLI 9 172 IQARQQVIEL 13 66 ATAEAQESGI 11 188 IPIDLGSLSS 13 96 EAQDSIDPPE _ 1TableXXXVIII-V25--ILA- 19 SAEEL 1 9 A SDPE 1A26-10mers-98P4B36 195 LSSAREIENL 13 141 SQAASGTLSL 11 199 REIENLPLRL 13 159 EFLGSGTWMK 11 Each peptide is portion of 204 LPLRLFTLWR 13 1180 EQKSKHCMFS -mSEQ ID NO: 51; each start ~ ______ 1 position is specified, the length 259 LPVAITLLS 13 of peptide is 10 amino acids, 260 PVAITLLSL 13 TableXXXVIll-V8-HLA- and the end position for each 266 LLSLVYLAGL 13 A26-10mers-98P4B6 peptide is he start position 29 RFPPWLETWL 13 Each peptide Is a portion of plus nine. 364 GIMSLGLLSL 13 SEQ ID NO: 17; each start Pos 1234567890 score 365 IMSLGLLSLL 13 position is specified, the length 2 1FLPCISK 10 4 ISMMGSPKSL 12 of peptide is 10 amino acids, 3 LFLPCISQKL 10 18 LPNGINGIKD 12 and the end position for each 6PCISKLKRI 9 70 FPHVVDVTHH 12 peptide is the start position plus PCIS 6 98 YTSLWDLRHL 12 nine. I IILFLPCISQ 6 98 YTSLWDLRHL 12 Pos 1234567890 score 9 SQKLKRIKKG 6 142 IVKGFNVVSA 12 8 EGMGGTIPHV 14 7 CISQKLKRIK 4 147 NVVSAWALQL 12 7 EEGMGGTIPH 11 157 GPKDASRQVY 12 1 EKSFLEEGM 10 202 ENLPLRLFTL 12 3 SQFLEEGMGG 6 TableXXXIX_VJ-HLA- 257 KTLPIVAITL 12 B0702-10mers-98P4B6 273 AGLLAAAYQL 12 TableXXXVIII-V13-HLA- Each peptide is a portion of SEQ 29 PPWLETWLQC 12 A26-I0mers-98P4B6 ID NO: 3; each start position is 29 ETWLQCRKQL 12 Each peptide is a portion of specified, the length of peptide is 298 WLQCRKQLGL 12 E D2ach statideis ort f 10 amino acids, and the end 314 MVHVAYSLCL 12 sQ is 2pech sta position for each peptide is the 377 TSIPSVSNAL 121 length of peptide is 10 amino start position plus nine. 395 QSTLGYVALL 12 acids, and the end position for Pos 1234567890 score 425 RFYTPPNFVL 12 each peptide is the start 429 PPNFVLALVL 23 437 VLPSIVILDL 12 position lus nine. 438 LPSIVILDLL 22 440 SIVILDLQL 12 Pos 1234567890 score 9 SPKSLSETCL 21 26 KDARKVTVGV 11 250 IPIEIVNKTL 21 27 DARKVTVGVI 11 228 TableXXXIX VI-HLA- TableXXXIX-VSA-HLA- TableXXXIX-V6-HLA B0702-10mers-98P4B6 B0702-1lmers-98P4B6 B0702-l0mers-98P4B6 Each peptide is a portion of SEQ nine. Each peptide is a portion of ID NO: 3; each start position is Pos 1234567890 score SEQ ID NO: 13; each start specified, the length of peptide is 1 FWRCPVVvAi 14 position is specified, the length 10 amino acids, and the end 3 LPLRLFTFWR II of peptide is 10 amino adds, position for each peptide is the 9 TFWRGPVVA 10 and the end position for each start position plus nine. RLFTFWRGPV 9 peptide is the start position plus Pos 1234567890 score 8FTFWRGPVVV 9 nine. 49 LIRCGYHVVI 11 1 ENLPLRIFTF 8 Pos 1234567890 score 62 NPKFASEFFP 11 LFTFWRGPVV 8 4 9 7 VDVTHHEDAL 11 95 REHYTSLWDL II TableXXXIX-V5B-HLA- TableXXXIX-V7A-LA 99 TSLWDLRHLL II B0702-0mers-98P4B6 B7O2-10mers98P4B6 132 YLASLFPDSL 11 Each peptide Is a portion of Each peptide is a portion of 145 GFNVVSAWAL 11 SEQ ID NO: 11; each start SEQ ID NO: 15; each start 183 RQLNFIPIDL 11 position is specified, the length position is specified, the 18 NFIPIDLGSL 11 of peptide is 10 amino acids, length of peptide is 10 amino 201 IENLPLRLFT I I and theend position for each acids, and the end position 213 RGPVVVAISL I I peptie is the start position for each peptide is the start 237 HPYARNQQSD 11 pius'nine. 252 IEIVNKTLPI I1 Pos 1234567890 score Jj2567890.cr 258 TLPIVAITLL 111 19 TELELEFVFL I j LEThL22 286 TKYRRFPPWL 11 2 EFVFLLTLLL 14 291 FPPWLETWLQ 11 1 FADTQTELEL 13 TableXXXIX-V7B-HLA 312 FAMVHVAYSL 11 22 ELEFVFLLTL 3 B0702-10mers-98P4B6 362 SFGIMSLGLL 11 12 CSFADTQTEL 12 Each peptide is a portion of 389 REFSFIQSTL 11 20 ELELEFVFLL 12 SEQ ID NO: 15; each start ___________23 LEFVFLLTLL I11 position is specified, the length TableXXXIX-V2-HLA- 1 NWREFSFIQI _ of peptide is 10 amino acids, B0702-10mers-98P4B6 8 IQfFCSFADT 9 and the end position for each Each peptide is a portion of 21 LELEFVFLLT 9 peptide is the start position plus SEQ ID NO: 5; each start 10 IFCSFADTQT _ 8 nine. position is specified, the length 16 DTQTELELEF 1234567890 score of peptide is 10 amino acids, _ FSFIQEFCSF ___1 LNMAYQSL 1 and the end position for each SFIQEFCSFA 7_ LGYVALL 12 peptide is the start position 171TQTELELEFV 7 ThGYVf 1t plus nine. 181QTELELEFVF 7 to sn GYV 8 Pos 1234567890 score 2 WREFSFIQ1F I QQSTLGYV 7 34 PPPCPADFFL 21 33 CPPPCPADFF 18 TabICX X-V6-HLA- TableXXXLXW7C-HLA 2 GSPGLQALSL 14 B0702-0mers-98P4B6 B07021 Omers-98P4B6 1 GFTPFSCLSL 13 Each peptide is a portion of Each peptide is a portion of SEQ 18 TPFSCLSLPS 13 SEQ ID NO: 13; each start D NO: 15; each start position is 4 PGLQALSLSL 12 position is specified, the length specified, the length of peptide is 14 SSGFrPFSCL 12 of peptide is 10 amino acds, 10 amino acids, and the end 25 LPSSWDYRCP 12 and the end position for each position for each peptide is the 35 PPCPADFFLY 12 peptde is the start position plus 3 SPGLQALSLS -11 nine. - Pos po34t789 scre 8 ALSLSLSSGF 10 Pos 1234567890 score 1 2 34567890 sco22 36 PCPADFFLYF 10 3 LPSTVILGKA 18 121 LPLW13FLLL 22 44 IPHVSPERVT 18 129 DPEDRL 21 7 VILGKHULL 151 10 PPSTPPPAL 21 TableXXXIX-V5A-HLA- 27 KKGWEKSQFL 13 4 PPAMWTEEA 18 B0702-10mers-98P4B6 16 LPCISRKLKR 12 11 NPPHTNOV 17 Each peptide is a portion of 46HVSPERVTVM 12 SEQ ID NO: 11; each start 14 LFLPCISRKL 41 position is specified, the length 5 SrV]LGKHL 1 1 AGTLS1A 15 of peptide is 10 amino acids, 38 EGIGGTIP{V 10 29 LRGGLSEIVL 14 and the end position for each 26 EKKGWEKSQF 9 A13 AAWKCL 13 peptide is the start position plus, 31 -EKSQFLEEGI I 48 IPSP PPPL 131 229 F 14 3 2PRLTWR9 TableXXXIX-V7C-H LA- B08-1 Omers-98P4B6 B0702-10mers-98P4B6 TableXXXIX-VI3-HLA- Pos 234567890 score Each peptide is a portion of SEQ B0702-10mers-98P4B6 NoResultsFound. ID NO: 15; each start position is Each peptide is a portion of specified, the length of peptide is SEQ ID NO: 27; each start TableXL-V2-HLA. 10 amino acids, and the end position is specified, the B08-1 mers-98P4B6 position for each peptide is the length of peptide is 10 amino Pos 1234567890 score start siton lus nine. acids, and the end position Pos 1234567890 score for each peptide is the start 85 IPVVGVVTED 13 sition pis nine. TableXL-V5A-HLA 10 SPDRALKAAN 13 P 108-I mers-98P4B6 12 NGVGPLWEFL 13 j2SPK L 22 Pos 12345678 152 FTSWSLGEFL 13 NoResultsFound. 165 TWMKLETIIL 13 Table)OLXIX-V14-HLA 181 QKSKHCMFSL 13 B0702-10mers-98P4136 TableXLV5B-HLA I LPSIVILDLS 12 Each peptie is a portion of B08-I Omers-98P4B6 5 VILDLSVEVL 12 SEQ ID NO: 29; each start Pos11234567890 score 1 SPAAAWKCLG 12 position is specified, the length NoesultsFound. 2 AWKCLGANIL 12 of peptide is 10 amino acids, 24 LGANILRGGL 12 and the end position f0 '"h TableXLV6-HLA 4 WQQDRKIPPL 12peptide is the stat position plus 54 PPPPAMWTEE 12 nine. Pos 234567890 score 5 PPAMWTEEAG 12 Pos 1234567890 score NoResultsFound. 103 PPESPDRALK 12 T FWRGPVVVAI 14 12 GVGPLWEFLL 12 3 LPLRLFTFWR 11 Table)-V7A-RLA 13 LKSQAASGTL 12 9 T'RGPVVVA 10 B08-I0mers-98P4B6 28 ILRGGLSEIV 11 61 RLFTFWRGPV 9 Pos 1234567890 score QDRKIPPLST I 1 8 FTFWRGPVV 9 NoResultsFound. 53 TPPPPAMWTE I I 1 ENLPLRLFF 8 81 SSSQIPVVGV 11 7 LFTFWRGPVV 8 TableXaV7B-HLA 104 PESPDRALKA II B08-10mers-98P 6 11 ASGTLSLAFT I 1 Pos 1234567890 score 148 LSLAFTSWSL 11 B0702-1Omers-98P4B6 NoResultsFound. 160 FLGSGTWiKLI I Each peptide is a portion of 168 I UDSKL 1_ SEQ ID NO: 43; each start TabKeLLKV7C-HLA 6 ILDLSVEVLA 10 poston is specified, the length B08-I0mers.98P4B6 17of peptide Is 10 amino acids, Pos234567890 score 19 AAWKCLGAN and the end position for each NoResultsFound. 19 AAWKCLGANT __ 1 peptide is the start position plus _________ 31 GGLSEIVLPI I nine. 38 LPIEWQQDR 10lX V8HA 38LWQRK I_ Pos 1234567890 score. B08-l1niers-98P4B6 50 PLSTPPPPAM 1 8 QKTKHMFSL 11 Pos1123456780 78 KSSSSSQ1PV 1 9 KTKHCMFSLI 8 NoResultsFound. 79 SSSSSQIPVV 10 QEQKHC 7 83 SQIPVVGVVT 10 LSKLTQEQKT 6 TabeXL-V13-HLA 112 KAANSWRNPV 10 _1TQEQKTKHCM 6 B08-l0mers-98P4B6 13 PLWEFLLRLL 1 Pos 1123456780 score TabTeXXXX-V25 -LA- NoResultsFoud. Tab7X02 IX-V8-HLA B0702-8Pmers-98P4B6 E0702-I Oers-98P46 Each pepide is a portion of TableXL-V14-fLA Each peptide is a portion of SEQ ID N0r 51; each start B08l10mers-98P4B6 SEQ ID NO: 17; each start Pos 12345678 position Is specified, the length posgtiof peie the of peptide is 10 amino acids. acids, and the end position for and the end position for each each peptide is the stat peptide is the start position plus sition his nine. b0 eXs-98P4B6 nine. 381mr9846 Pos 1234567890 score Ps 1234567890 score Pos~ 1235689 5cr LPcisQKLKR -i1 oeuiud 8 EGMGGTIPHV 11 3 LFLPCIS KL 11 1 EKS FLEEGM 9 PCIS KKJ1 6 TableXLV25-ILA FLEEGMGGT 6 B08-10mers-98P4B6 5. FLEEGMGGTI, 6 TabeXLI-V-HLA- Pos 1234567890 score 230 TableXL-V25-HLA- Pos|12345678901score B08-10mers-98P4B6 NoResultsFound. TableXLI-V21-HLA Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V25-HLA- Pos 12345678901 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V1-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TabieXLI-V25-HLA Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXL-V-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-VI -HLA Pos|1234567890|score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXL-V5A-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V5A-HLA-. Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V5B-HLA- Pos|1234567890|score B1510-10mers-98P4B6 NoResultsFound. TableXU-VSA-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V5B-HLA- Pos|1234567890|score B2705-10mers-98P4B6 NoResultsFound. TableXLl-V6-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TabteXLI-V5B-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V6-HLA- Pos|1234567890|score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V7A-HLA- Pos 1234567890 score BI510-10mers-98P4B6 NoResultsFound. TableXLI-V6-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V7A-HLA- Pos 11234567890 score B2705-10mers-98P4B6 NdResultsFound. TableXLI-V7B-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V7A-HLA Pos 1234567890 score B2709-10ners-98P4B6 NoResultsFound. TableXLI-V7B-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA- Pos|1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V7B-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V8-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA Pos|1234567890|score B2709-10mers-98P4B6 NoResultsFound. TableXLl-V8-HLA- Pos|1234567890|score B2705-1Oners-98P4B6 NoResultsFound. TableXLI-VI3-HLA- PosT1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V8-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXU-VI3-HLA- Pos 1234567890|score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V14-HLA- Pos|1234567890|score B1510-10mers-98P4B6 NoResultsFound. TableXLI-VI3-HLA Pos 1234567890 score B2709-1 Omers-98P4B6 NoResultsFound. TableXLI-V14-HLA- Pos 11234567890 score B2705-10imers-98P4B6 NoResultsFound. TableXLI-V21-HLA- Pos|1234567890 score BI510- 10mers-98P4B6 NoResultsFound. TableXLI-V14-HLA 231 B2709-10mers-98P4B6 TabIexLI-HLA-B4402- ableXLlV-V1-HLA-B4402. Pos 1234567890 score I mers-98P4B6 I Omers-98P6 NoResultsFound. Each peptide is a portion of SEQ Each peptide is a portion of sEQ _____________ID NO: 3; each start position is ID NO: 3; each start position is TableXLl-V21 -HLA- specified, tie length of peptide is specified, the length of peptide is B2709-I0mers-98P4B6 10 amino acids, and the end 10 amino acids. and the end Pos I1234567890Tsco0reI position for each peptide is the position for each peptide is the [ o~eltFo~jjj start Position plus nine start Position plus nine Pos 1234567890 score Pos 1234567890 Pscre TableXLI-V25-HLA- 255 VNKTLPIVAI 15 323 LPMRSERYL 13

B

2 709-10mers-98P4B6 258 TLPIVAITLL 15 32 PMRRSERYLF Pos 1234567890 score 279 AYQLYYGTKY 15 328 SERYLFLNMA 13 NoResultsFound. 310 FFFAMV14VAY 15 350 NEEEVWRJEM 13 329 ERYLFLNMAY 15 362 SFGLMSWGLL 13 394 IQSTLGYVAL _151 34 GIMSLGLLSL 13 TableXLIV-V I-HLA-B4402- 437 VLPSIVILDL 1 379 IPSVSNALNW 13 10mers-98P4B6 4 ISMMGSPKSL 14 38 NALNWREFSF 13 Each peptide is a portion of SEQ 92 AMHREHYWSL 14 395 QSTLGYVALL 13 ID NO: 3; each start position is 98 YTSLWDLRIL 14 403 LLISTFIVLI 13 specified, the length of peptide is 9 TSLWDLRHLL 429 PPNFVLALVL 13 10 amino acids, and the end _23 NQYPESNAEY 14 438 LPSVLDLL 13 position for each peptide is the 1 FPDSLIVKGF 14 443 ILDLLQLCRY 13 start position plus nine.147 NVVSAWALQL 14 38 SGDFAKSLTI 12 Pos 1234567890 score 183 RQLNFIPIDL 14 4 DFAKSLTIRL 12 199 REIENLPLR.L 251- 351 EEEVWRIEMY 25 195 LSSAREIENL 14 93 H-RE1LW 121 252 EEEVWRI 25 218 VAISLATFFF 14 105 RHLLVGKLI 121 252271 YLALLAAAY 14 12 QYPESNAEYL 12 389 REFSFI STIL 23 39 REFYSFI SL 23 290 RFPPWLETWL 14 178 VELARQLNF 121 95 REHYTSLWDL 21 346 ENSWNEEEVW 14 192 LGSLSSAREI 12 179 IELAR LNFI 21 361 ISFGIMSLGL 14 197 SAREIENLPL 12 352 EEVWREMYI 2365 IMSLGLLSLL 14 21 VVVASLATF 12 79 HEDALTKTNI 19 391 FSFI STLGY 1 260 PIVAILLSL 12 377 TSIPSVSNAL 19 396 STLGYVALLI 14 274 GLLAAAYQLY 12 186 NFIPIDLGSL 181 399 GYVAISTF 14 282 L GTKYRRF 12 202 ENLPLRLFTL 8 18 4 LISTFHVLIY 14 28 TK PPWL 12 25 KTLPIVAITL 18 418 AFEEEYYRFY 141 295 12 427 YTPPNFVLAL 18 420 EEEYYRFYTP 14 301 CRKQLGLLSF 12 435 ALVLPSIVIL 18 4 SIVILDLLL 14 302 RKQLGLLSFF 12 273 AGLLAAAY L 17 41 FAKSLTIRLT 13 312 FAMVHVAYSL 12 289 RRFPPWLETW 17 7 VDVHREDA _ 13 357 JEMYISEGIM 12 296 ETWL CRKOL 17 402 ALLISTFHVL 17 8 EDALTKI1 13 385 ALNWREFSFI 12 14 TCLPNGINGI 16 81 DALTKTNIIF 13 417 RAFEEEYYRF 12 11 VSNNMRIN Y 16 84 TKTNTFVAI 13 421 EEYYRFYP 12 200 EENLPLRLF 16 104 LRHLLVGKIL 13 45 RFYTPPNFVL 12 219 AISLATFFFL 16 127 ESNAEYLASL 13 231 SFVRDVIPY 16 128 SNAEYLASLF 13 TableLIV-V2-HLA 23 FVDVI1P ~143 VKGFNVVSAW 13 B4402-10mers-98P4116 250 IPIEIVNKTL 16 145 GFp/SAWA 13 Each peptide is a portion of 262 VAITLLSLVY 16 157 GPKDASRQVY 13 SEQ ID NO: 5; each start 263 AITLLSLVYL 16 17 NMQAR V1 13 position is specified, the length 359 MYISFGIMSL 16 17 1QARQ9VIEL 13 ofpeptdeis10aminoacids 40 STFHVLIYGW 16 1 VIELARQL 13 and the end position for each 41 VLIYGWKRAF 16 201 IENLPLRLFT 13 peptide is the start position 36 IGSGDFAKSL 15 211 LWRGPVVVAI 13 plus nine. 45 LTIRLIRCGY 15 213 RGPVVVAISL 13 Pos 1234567890 score 56 VVIGSRNPKF 15 22 ISLATFFFLY 13 8 ALSLSLSSGF 15 6 SRNPKFASEF 15 245 SDFYKIPIEI 13 32 RCPPPCPADF 15 6 SEFFPHVVDV 1 2 LLSLVYLAGL 33 CPPPCPADFF 15 12 PESNAEYLAS 15 26 LSLVYLAGLL 1 35fPPCPADFFLY I5 13 AEYLASLFPD 152 LQCRKQLGLL 13 2 GSPGLQALSL 1 203_NP1 FL 15 L10 KQLLLSF 13 1-16 GFTPFSCLSL 14 232 TableXLIV-V2-HLA- SEQ ID NO: 13; each start specie, the i ofpeptideis B4402-10mers-98P4B6 position is specified, the length 10 amino acids, and the end Each peptide is a portion of of pepbde is 10 amino acids, position for each peptide is the SEO ID NO: 5; each start and the end position for each _ start position plus nine. position is specified, the length peptide is the start position plus Pog 1234567890 score of peptide is 10 amino acids, nine. 92 3PPDAQDSI 20 and the end position for each Pos 1234567990 score 17 QEQKSKHCMF 20 peptide is the start position - VILGKIILF 19 143 AASGTLSLAF 18 plus nine. 7 VILGKHLFL 16 3 SEIVLPIEWQ 17 Pos 1234567890 score 14 LFLPCISRKL 16 1 PESPDRALKA 17 3 PCPADFFLYF 13 17 PCISRKLKJU 1 1 EVLASPAAAW 16 4 PGLQALSLSL 12 37 EEG1GGTIH 14 15 ASFAAAWKCL 16 11 LSLSSGFTPF 12 4 PSWLGKII 13 62 EEAGATAEAQ 16 1 SSGFTPFSCL 12 21 RKKRIKKGW 13 13 WEFLLRLLKS 16 2 FSCLSLPSSW 12 5 SPVILGKI[L 12 20 AWKCLGANIL 15 22 CLSLPSSWDY 12 10 GKIELFLPCI 12 5 VILDLSVEVL 14 3 PPPCPADFFL 11 26 IIKGWEKSQF 12 11 VEVLASPAAA 14 3 LPSIVILGKI 111 42 WQQDRMIPL 14 27 KKGWEKSQFL _ 11 51 LSTPPPPAMW 14 TableXLIV-V5A-HLA- 30 WEKSQFLEEG 11 68 AEAQESGIRN 14 B4402-10mers-98P4B6 Each peptide is a portion of 3 LEEGIGOTIP 11 102 DPPESPDRAL 14 SEQ ID NO: 11; each start 35 FLEEGIGGTI 113 AANSWRNPVL 14 position is specified, the length 38 EGIGGTEPI-1 9 127 GVGPLWEFLL 14 of peptide is 10 amino acids, 51 AFTSWSLGEF 14 and the end position for' each peptide is the start position plus TabICXLIV-V7A-HLA- 168 KLETITLSKL 14 petdei testr pstinplsB4402-I~ners-98P4B6 29 LRGGLSEIVL 13 Po n1346790 scr Each peptide is a portion of 40 IEWQQDRICIP 13 Pos 123456780 SEQ ID NO: 15; each start 95 DEAQDSIDPP 13 2 NLPLLF 14 position is specified, the 108 DRALKAANSW 13 NLPLRLFTFWlength of peplide is 10 amino 129 GPLWEFLLR 13 10 FWRGPVVVAI 13 acids, and the end position 13 PLWEFLLRL 13 TaICLI-5BHL-for each peptide Is the start 1411 SQAASGTLSL 131 TableXLIV-V5B-HLA-position plus nine. 158 GEFLGSGTWM 13 B4402-10mers-98P4B6 Pos 1234567890 score Each peptide is a portion of 9 TLPNGINGI 16 165 TWMKLr 13 SEQ ID NO: I1; each start I GSPKSLSETF 12 position is specified, the length 2 SPKSLSETFL 1 27 NILRGGL 12 of peptide is 10 amino acids, ETFLPNGI 11 and the end position for each 31 LSEIV.PIEW 12 peptide is the start position 122 LI-TNGVGPL 12 plus nine. 123 PHTNGVGPLW 12 Pos 1234567890 score B4402-IOmers-98P4B6 126 NGVGPLWEFL 12 23 LEFVFLLTLL 24 Each peptide is a portion of 139 LKSQAASGTL 12 19 TELELEFVFL 23 146 GTLSLAFTSW 12 20 ELELEFVFLL SE15NO 5 ac tr 22 EELEFVFLL 15 position i specified, the length 19 AAWKCLGANI I1 22of peptide is 10 amino acids, 31 GGLSEIVLPI 24 EFVFLLTLLL 15 and the end position for each 61 TEEAGATAEA 11 21 LELEFVFLLT 14 peptide is the start position plus 66 ATAEAQESGI 11 2 WREFSFIQIF 13 nine. 125 TNGVGPLWEF 11 3 REFSFIQIFC 13 Pj 1234567890 score 148 LSLAFTSWSL 11 5 FSFIQIFCSF 13 QQSTGYVAL I5 152 FTSWSLGEFL I1 14 FADTQTELEL 13 10 STLGYVALU 14 157 LGEFLGSGTW 11 I NWREFSFIQI 12 9 QSTLGYVALL 13 16 FLGSGTWMKL 11 12 CSFADTQTEL 12 3 LNMAYQQSTL 12 163 SGTWMLET I I 16 DTQTELELEF 12 12 181 KSKHCMfSL II 18 QTELELEFVF 12 182 KSKHCMFSLI TabeXaV-V7C-HLA- 39 W-LQDRA BT40-e s-V9PLA B4402-0mers-98P4B6 76 RNKSSSSSQI 9 B4402-10mers-98P4B6 Each peptide is a portion of SEQ 83 SIPVVGVVT 9 Ech pptdeiaportonpof IDNO: 15; each start positions 105 ESPDRALKAA 9 233 B4402- mm4rs-98P4B6 ers-9845Bscor6 TableXLIV-V8-HLA- Each pepide is a portion of B4402-10mers-98P4 6 SEQ ID NO: 51; each start Each peptide is a portion of position is specified, the length TableXLV-V14-HLA SEQ ID NO: 17; each start of peptide is 10 amino acids, B5101-l0mers-98P4B6 position Is specified, the length and the end position for each Pos 112345678901 score of peptide is 10 amino acids, peptide is the start position plus NoResultsFound. and the end position for each nine. peptide is the start position Pos 1234567890 score TableXLV-V2]-HLA us nine. 3 LFLPCISQKL 15 B5101-10mers-98P4B6 Pos 1234567890 score 6 PCISQKLKRI 14 Pos 1234567890 score EEGMGGTIPH 1410 QKLKRLKGW 13 NoResuitsFound. LEEGMGOTIP 1 9 SQKLKRkK 8 5 FLEEGMGGTI 9 4QK 7 TabeXLV-V25-HLA 8 EGMGGTIPHV 7 BS101-10mers-98P4B6 TabeXLV-VI-HL- Pos 1234567890 score TableXCLIV-V I3-HLA- [BS101- l0mers-98P4B6 NoResults~ound. B4402-10mers-98P4B6 Pos 1234567890 score Each peptide is a portion of NoResultsFound. TableXLVI-V1-HLA-DRBI-0101 SEQ ID NO: 27; each start _ _ _ _is-98P4B6 position is specified, the TableXLV-V2-HLA Each peptide is a portion of SEQ ID NO: length of peptide is 10 amino B5101-l0mers-98P4B6 3; each start position is specified, the acids, and the end position Los 12345678901score length of peptide is 15 amino acids, and for each peptide is the start NoResultsFound. the end position for each peptide is the sition lus nine. start position plus fourteen. Pos 1234567890 score TableXLV-V5 Pos 123456789012345 score 9 TFLPNGINGI 16 B5101-10mers-98P4B6 143jVKGFNVVSAWALQLG 3 I GSPKSLSETF 12 Pos 1234567890 score 266 LLSLVYLAGLLAAAY 33 2 SPKSLSETFL 11 NoResuftFound. 367 SLGLLSLLAVTSIPS 32 6 LSETFLPNGI 11 1 MESISMMGSPKSLSE 31 7 SETFLPNGBN 11 TabeXLV-V5B-11LA 13 AEYLASLFPDSLIVK 3 B5 101-I0zners-98P4136 30 KVTVGVIGSGDFAKS 29 TableXLIV-V14-HLA- Pos 1234567890 score 431 NFVLALVLPSPVLD 29 B4402-10mers-98P4B6 NoResultsFound. 206 LRLFTLWRGPVVVAJ 28 Each peptide is a portion of 215 PVVVAISLATFFFLY 28 SEQ ID NO: 29; each start TableXLV-V6-HLA- 370 LLSLLAVTSIPSVSN 28 position is specified, the length B5101-10mers-98P4B6 438 LPSIVTLDLLQLCRY 28 of peptide is 10 amino acids, 5678901score 101 LWDLRHLLVGKILID 27 and the end position for each NoResultsFound. 185 LNFIPIDLGSLSSAR 27 peptide is the start position plus 356 RIEMYISFGIMSLGL 27 nine. TableXLV-V7A-HLA- 360 YISFGIMSLGLLSLL 27 Pos .1234567890 score B5101-0mers-98P4B6 397 TLGYVALLISTFHVL 27 1 ENLPLRLFTF 18 Pos12345678901score 421 EEYYRFYTPPNFVLA 27 2 NLPLRLFTFW 14 N ultsFound. 1 FWRGPVVVAI1 3 102 WDLRHLLVGKLIDV 2 TableXLIV-V21-HLA-NQPESAELAS 2 B5101-10mers-98P4B6 129 VSWQYES PKYASL 26 TabieXLIV-V21I-HLA- Pos 11234567890 r 1 24 VSWALQLPKDASRK 26 B4402-10mers-98P4B6 ii 24 KIPIEIVNKTLPIVA 2 Each peptide is a portion of SEQ ID NO: 43; each start TableXLV-V7C-HLA- 25 NKTLPIVAITLLSLV 26 position is specified, the length B5101-10mer-98P4B6 261 IVAITLLSLVYLAGL 26 of peptide is 10 amino acids, Ji234567890se 29 WL RKQLGLLSFFF 2 and the end position for each 368 LGLLSLLAVTSIPSV 26 peptide is the start position plus 109 VGKIDVSNNMIN 25 nine. TabeXLV-V8-ILA- 13 FPDSLIVKGFNVSA 25 Pos 1234567890 score B5IO1-l0mers-98P4B6 145 GFNVSAWALQLGPK 25 E KTKHCMF 20 Pos 198 AREIENLPLRLFTLW 25 9 KTKHCMFSLI 11 NoResulFo22L2 8 QKTKHCMFSL 10 25 1 EIVNKTLPIVAITL 25 TaTeLI-V5-eIA-F V-V13HL- 264 ITLISLVYLAGLLAA 25 B440-10mers-98P4B6 302 RKQLGLLSFFFAMVH 25 2341 TabIeXLVI-V1-HLA-DRB1-00l- TableXLVI-VI-HLA-DRB1-0101- TabeXLVI- I-HLA-DRB1-0101 15mers-98P4B6 l5mers-98P4B6 1Smers-98P4B6 Eadh pepbde is a portion of SEQ I) NO: Each peptide is a portion of SEQ lIaO Each peptide is a portion of SEQ ID NO: 3, each start position is specified, the 3; each start position is specified, the 3; each start position is specified, the length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and the end position for each peptide is the the end position for each peptide is the the end position for each peptide is the start position plus fourteen. start position plus fourteen, start Position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 3 SFFFAMVHVAYSLCL 25 429 PPNFVLALVLPSIVI 2 90 FVAIHREHYTSLWDL 17 35 VWRIEMYISFGIMSL 25 45 LTIRLIRCYHVVIG 19 105 RHLLVGKILIDVSNN 17 362 SFGIMSLGLLSLLAV 25 80 EDALTKTIVAIH 19 119 NMRINQYPESNAEYL 17 36 IMSLGLLSLLAVTSI 25 95 REHYSLWDLRHLLV 19 138 PDSLIVKGFNVVSAW 17 51 RCGYHVVIGSRNPKF 24 135 SLFPDSLIVKGFNVV 19 140 SLIVKGFNVVSAWAL 17 98 YTSLWDLRHLLVGKJ 24 139 DSLIVKGFNVVSAWA 19 1511 AWALLGPKDASRQV 17 10 HLLVGKILIDVSNNM 24 224 TFFFLYSFVRDVIHP 19 154 LQLGPKDASRQVYIC 17 -15 SAW LGPKDASR 24 259 LPIVAITLLSLVYLA 19 17 QQVIELARQLNFIPI 17 18 LNFJPIDLGSLSSA 24 280 19 187 FIP[DLGSLSSAREI 17 205 PLRLFTLWRGPVVVA 24 281 QLYYGTYYRRFPWL 19 195 LSSAREIENLPLRLF 17 229 YSFVRDVIHPYARNQ 24 288 YRRFPPWLEMLOCR 19 217 VVAISLATFFFLYSF 17 269 LVYLAGLLAAAY LY 24 307 LLSFFFAMVHVAYSL 19 22 FFLYSFVRDVHYA 17 330 RYLFLNMAYQQVHAN 24 322 CLPMRRSERYLFLNM 19 232 VRDVIHPYARNQQSD 17 335 NMAYQQVHANIENSW 24 328 SERYLFLNMAYQQVH 19 251 P[EWNKTLPIVAjT 17 388 WREFSFIQSTLGYVA 24 357 lEMYISFG[MSLGLL 19 253 EIvn PIVAfML 17 391 FSFIQSTLGYVALLI 24 400 YVALLISTFHVLIYG 19 27 VYLAGLLAAAYQLYY 17 398 LGYVALLISTFHVLI 24 424 YRFYTPNFVLALVL 1 271 YLAGLLAAAYQLYYG 17 427 YTPPNFVLALVLPSI 24 7 MGSPKSLSETCLPNG 18 305 LGLLSFFFAMVHVAY 17 430 PNFVLALVLPSIVL 24 25 TKDARKVTVOVIGSG 18 31 HVAYSLCLPMRRSER 17 52 CGYHVVIGSRNPKFA 23 27 DARKVTVGVIGSGDF 18 317 VAYSLCLPMRRSERY 17 55 HVVIGSRNPKFASEF 23 39 GDFAKSLTIRLRCG 18 329 ERYLFLNMAYQQVHA 17 18 NFIPIDLGSLSSARE 23 47 IRLIRCGYHVVIGSR 18 361 ISFGIMSLGLLSLLA 17 214 GPVVVAISLATFFFL 23 62 NPKFASEFFPIVVDV 18 363 FGIMSLGLLSLLAVT 17 258 TLPFVAITLLSLVYL 23 129 NAEYLASLFPDSUV 18 389 REFSFIQSTLGYVAL 17 351 EEEVWRIEMYISFGI 23 163 RQVYICSNNIQARQQ 1 392 SF1 STLGYVALLIS 17 352 EEVWRIEMYISFGIM 23 167 ICSNNIQARQQVIEL 18 406 STFHVJJYGWKRAFE 17 127 ESNAEYLASLFPDSL 22 179 IELARQLNFEPIDLG 18 408 FHVLMWKRAFEEE 1 178 VIELAR LNFIPIDL 22 190 IDLGSLSSAREIENL 18 4361LVLPSIVILDLLQLC 17 18 PIDLGSLSSAREIEN 22 236 tHPYARNQQSDFYKI 18 2 ESISMMGSPKSLSET 16 211 LWRGPVVVAISLATF 22 267 LSLVYLAGLLAAAYQ 18 3 SISMMGSPKSLSErC 16 216 VVVAISLATFFFLYS 22 268 SLVYLAGLLAAAYQL 18 8 GSPKSLSETCLPNGI 16 255 VNKTLPIVAITLLSL 22 285 GTKYRRFPPWLETWL 18 11 KSLSETCLPNGINGI 16 301 CRKQLGLLSFFFAMV 22 296 ETWLQCRKQLGLLSF 18 16 TCLPNGINGHCDARK 16 312 FAMVHVAYSLCLPMR 22 299 LQCRQLGLLSFFFA 18 2 GIKDARXVTVGVIGS 1 35 MYISFGIMSLGLLSL 22 YLF 18 59 GSRNPKFASEFFPHV 1 364 GIMSLGLLSLLAVTS 22 38 PSVSNALNWREFSF J 1 67 SEFFPH1DVTEHED 1 395 QSTLGYVALLISTFH 22 383 SNALNWREFSFIQST 18 71 PHVDVTIIEDALTK 1 432 FVLALVLPSIVILDL 22 390 EFSFIQSTLGYVALL 18 103 DLRILLVGKJLIDVS W 435 ALVLPSIVILDLLQL 22 405 ISTFHVLIYGWKRAF 18 111 KIUDVSNNMRINQY 1 20 NGINGIKDARKVTVG 21 410 VLIYGWKRAFEEEYY 18 126 PESNAEYLASLFPDS 1 117 SNNMRJNQYPESNAE 21 423 YYRFYTPPNFVLALV 18 153_ALQ KDASRQVYI 1 161 ASRQVYICSNNIQAR 21 433 VLALVLPSIVILDLL 18 166 YICSNNIQARQQVIE 1 174 ARQQVIELARQLNFI 21 22 INGIKDARKVTVGVI 1 71 NIQARQQVIELARQL 1 277 AAAYQLYYGTKYRRF 21 29 RKVTVGVIGSGDFAK 1 175 RQQVIELAkQLNHP I 373 LLAVTSIPSVSNALN 21 33 VGVIGSGDFAKSLTI 17 182 ARQLNFIPIDLGSLS 1 399 GYVALLISTFHVLIY 21 34 GVIGSGDFAKSLT[R 1 200 EIENLPLRLFTLWRG 1 407 TFHVLIYGWKRAFEE 21 44 SLTfURCGY-II 1 208 LFLWRGPVVVAISL 1 31 VTVGVIGSGDFAKSL 20 46 TIRLIRCGYHVIGS 1 219 AISLATFFFLYSFVR 1 142 IVKGFNVVSAWALL 2 54 YYVIGSRNPKFASE 17 25 FFFLYSFVRDVPY I 209 FTLWRGPVVVAISLA 2 58 IGSRNPKFASEFFPH -17 63 ArLLSLVYLAGLLA 346 ENSWNEEEVWRIEMY 2 77 THZ0EDALTKTNIFV 1 265 TLLSLVYLAGLLAAA 1 385 ALNWR.EFSFIQSTLG 2 87 NUFVAIIIREHYFL 112941 wLETwuQcRKQLGLL 16 235 TableXLVI-VI-HLA-DRB1-0101- TabICXLVI-VSA-HLA-DRB1- TableXLVI-V6-HLA-DRB 1-0101 15mers-98P4B6 0101-1 mers-98P4B6 I Sners-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ IDNO: Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the 11: each stat position Is specified, the 13; each start position is specified, the length of peptide is 15 amino acids, and length of peptideis 15 amino acds, and length of peptide is 15 amino acids, and the end position for each peptide is the the end position for each peptide is the the end position for each peptide is the start position plus fourteen. start position plus fourteen. start ition pus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 304 QLGLLSFFFAMVHVA 16 1 PLRLFTFWRPVVVA 1 18 ILFLPCISRKLKRIK 15 308 L.SFFFAMVHVAYSLC 16 1 RLFFWRGPVVVAIS 13 25 SRKLKRIKKGWEKS 15 31 FFFAMVHVAYSLCLP 1 SARBIENLPLRLFTF 1 3 RIKKGWEKSFLEEG 14 314 MVHVAYSLCLPMRRS 16 7 NF V 1 43 EGIGGTlPHVSPERV 1 371 LSLLAVTSIPSVSNA 16 15 TFWRGPVVAISLAT I 3 IQSTLGYVALUSTF 16 TableXLVI-V7A-HLA-DRBI 401 VALLISTFHVLIYGW 16 TableXLVI-V5B-HLA-DRBI. 0101-15mers-98P4B6 42 EEEYYRFYTPPNFVL 16 0101-15mers-98P4B6 Each peptide is a portion of SEQ ID 428 TPPNFVLALVLPSIV 16 Each peptide is a portion of SEQ ID NO: 15; each start position is specified, 440 SIVILDLLQLCRYPD 16 NO: 11; each start position is specified, the length of pepbde is 15 amino acids, - the 'length of peptide Is 15 amino acids, and the end position for each pepfide is TableXLVI-V2-HLA-DRBI-O010- and the end position for each peptide is 1-' start position plus fourteen. 15mers-98P4B6 the start position plus foutn. Pos 123456789012345 score Each peptide is a portion of SEQ ID Pos 123456789012345 score 12 SETFLPNGINGIKDA 21 NO: 5; each start position is specified, 7 WREFSFIQIFCSFAD 25 5 MGSPKSLSETFLPNG 18 the length of peptide is 15 amino acids, 9 EFSFIFC ADTQ 24 1 SISMMGSPKSLSETF 16 and the end position for each peptide is 4 ALNWREFSFIQIFCS 20 4 MMGSPKSLSETFLPN 16 the start position plus fourteen. 2 SNALNWREFSFIQIF 18 __ GSPKSLSETFLPNGI 16 Pos 123456789012345 score 2 ADTQTELELEFVFLL 18 9 KSLSETFLPNGINGI 16 17 FTPFSCLSLPSSWDY 26 8 REFSFIQIFCSFADT 17 1 TFLPNGINGIKDARK 1 28 SWDYRCPPPCPADFF 26 1 FSFIQFCSFADTQT 17 2 ISMvGSPKSLSETFL 14 6 LQALSLSLSSGFTPF 25 22 TQTELELEFVFLLTL 17 15 FLPNGINGIKDARKV 13 8 ALSLSLSSGFTPFSC 25 23 QTELELEFVFLLTLL 17 1 SLSETFLPNGING[K 10 3 SPGLQALSLSLSSGF 2 12 FIQIFCSFADTQTEL 16 1 SLSLSSGFTPFSCLS 22 1 FCSFADTQTELELEF 16 TableXVI-V7B-HLA-DRB1-0101 1 SSGFTPFSCLSLPSS 19 1 CSFADTQTELELEFV 14 15mers-98P4B6 2 PSSWDYRCPPPCPAD 16 Each peptide is'a portion of SEQ ID NO: 31 YRCPPPCPADFFLYF 16 TableXLVI-V6-HLA-DRBI-O101- 15; each start position is specified, the 1 SGSPGLQALSLSLSS 15 I mers-98P4B6 length of peptide Is 15 amino acids, and PGLQALSLSLSSGFT 15 Each peptide is a portion of SEQ ID NO, the end position for each peptide is the 20 FSCLSLPSSWDYRCP 15 13; each start position is specified, the start position plus fourteen. 2 GSPGLQALSLSLSSG 14 length of peptide is 15 amino acids, and Pos 123456789012345 score 7 QALSLSLSSGFTPFS 14 the end position for each peptide is the 4 RYLFLNMAYQQSTLO 2 13 LSSGFTPFSCLSLPS 14 start position plus fourteen , 1 QSTLGYVALLISTFH 2 1 GFTPFSCLSLPSSWD 14 Pos 23456789012345 score 7 FLNMAYQQSTLGYVA 21 1. PFSCLSLPSSWDYRC 14 1 NFVLALVLPSIVILG 29 2 SERYLFLNMAYQQST 19 27 SSWDYRCPPPCPADF 14 8 LPSIVIKIILFLP 29 9 NMAYQQSTLGYVALL 18 30 DYRCPPPCPADFFLY 14 - GGTIHVSPEVTVM 28 3 ERYLFLNMAYQQSTL 1 17 1ILFLPCISRKLKRI 26 11 AYQQSTLGYVALLIS 17 TableXLVI-VSA-HLA-DRB- 11 IVILGKDLFLPCIS 2 1 MAYQQSTLGYVALLI 1 0101-15mers-98P4B6 38 SQFLEEGIGGTIPHV 24 13 QQSTLGYVALLISTF 1 Each peptide is a portion of SEQ ID NO- 9 QFLEEG[GGT[PHVS 24 _8 LNMAYQQSTLGYVAL 14 11; each start position is specified, the 7 VLPSIVILGKILFL 23 length of peptide is 15 amino acids, and I LGKIILFLPCISRKL 23 TableXLVI-V7C-HLA-DRB1-0101 the end position for each peptide is the 2 FVLALVLPSIVILGK 22 15mers-98P4B6 start Position plus fourteen. 42 EEGIGGTIPHVSPER 22 Each peptide is a portion of SEQ ID NO: Pos 123456789012345 score 13 ILGCIILFLPCISRK _1 15; each start position is specified, the I1 LRLFTFWRGPVVVAI 28 3 VLALVu'swuxncj 8 length of peptide is 15 amino acids, and 3 AREIENLPLRLFTFW 25 6 LVLpSILGKIILF 18 the end position for each peptide is the 16 FWRGPVVVAISLATF 22 9 PSIVILGKILFLYC 17 start position plus fourteen. 14 FTFWRGPVVVAISLA 2o 15 GKIILFCISRKLK 17 POT 123456789012345 Score 13 LFTFWRGPVVVAISL I8 I 5 1 PSwwLjw -1 23 AAAWKCLGANILRGG 3 5 EIENLPLRiLFTFWRG I I 19 SWVILGKIILFLPEi- 16 1681 SGTWMKlLETTLSKL 1 35 236 TableXLVI-V7C-HLA-DRBI-O1IJ- TabO0XLVI--HLA-DRB -0101- length of peptide is 15 amino acids, and 15mers-98P4B6 I zers-98P4B6 the end position for each peptide is the Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: start position plus fourteen. 15; each start position Is specified, the 17; each start position is specified, the Pos 123456789012345 score length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and 3 TIILSKLTQEQKTKH 18 the end position for each peptide is the the end position for each peptide is the 2 ETIILSKLTQEQKTK start position plus fourteen. start position plus fourteen. 7 SKLTQEQKTHCMFS 13 Pos 123456789012345 score Pos 123456789012345 score LSKLTQEQKTKHCW 11 138 EFLLRLLKSQAASGT 33 8 SQFLEEGMGGTEPHV 24 11 QEQKTKHCMFSLISG 11 13 DLSVEVLASPAAAWK 30 9 QFLEEGMGGTHVS 2 1 LEnILSKITQEQKT 1 5 DRKIPPLSTPPPPAM 3 1 EEGMGGTHVSPER 2 _ LTQEQKTKiCMFSLI 10 28 CLGANILRGGLSEIV 28 13 EGMGGTIPHVSPERV 1 10 TQEQKTKHCMFSLIS 9 62 PAMWTEEAGATAEAQ 27 7 KSQFLEEGMGGTIP'. 13 12 EQKTKHCWSLISGS 9 11 ESPDRALKAANSWRN 2 2 KKGWEKSQFLEEGMG 12 51 HSKLTQEQKTKHCM 8 124 NPVLPHTNGVGPLWE 26 - EKSQFLEEGMGGTIP 12 81 KLTQEQKTYHCMFSL 8 141 LRLLKSQAASGTLSL 25 8 SIVIDLSVEVLASP 21 TabICXLV-V13-HLA-DRB1 31 ANILRGGLSEIVLPI 24 0101-5mers-98P6 TableXLVI-V25-HLA-DRB1-0101 4 VLPIEWQQDRKIPPL 24 Each peptide is a portion of SEQ ID I mers-98P4B6 77 ESGIRNKSSSSSQIP 24 NO: 27; each start position is specified, Each peptide Is a portion of SEQ ID NO: 13 TNGVGPLWEFLLRLL 24 the length of peptide is 15 amino acids, 51; each start position is specified, the 137 WEFLLRLLKSQAASG 24 and the end position for each peptide is length of peptide is 15 amio acids, and 7 PSIVILDLSVEVLAS 23 start position plus furten. the end position for each peptide is the 1 LDLSVEVLASPAAAW 23 Pos 123456789012345 score _ start position plus fourteen. 15 SGTLSLAFTSWSLGE 23 12 SETFLPNCING[KDA 2 Pos 123456789012345 score 171 WMKLETIILSKLTQE 23 5MGPSSTLN 18 6IFLCQK R 2 3 ALVLPSIVILDLSVE 22 1 SISMMGSPKSLSETF 3 LGKIIIFLPCISQKL 23 53 IPPLSTPPPPAMWTE 22' MMGSPKSLSETFLPN 2 ILGKIILFLPCISQK 19 15 FTSWSLGEFLGSGTW 22 GSPKSLSETfLPNGI 4 GKIIFLPCISQKLK 17 8 QIPVVGVVTEDDEAQ 21 KSLSETFLPNGINGI 16 7 ILFLPCISQKLKRIK Is LPSVILDLSVEVLA 20 1 TFLPNGINGIKDARK 1 9 FLPCISQKLKRIKKG 15 58 TPPPPAMWTEEAGAT 2C 2 ISMMGSPKSLSETFL T4 14 SQKLKRIKGWEKSQ 15 97 TEDDEAQDSIDPPES 2 15 FLPNGINGDARKV 15 QKLKRIKKGWEKSQF13 10 DEAQDSIDPPESPDR 20 10 SLSETFLPNGNGIK 13 GPLWEFLLRLLKSQA 1 TabeXLV11-' ' -HLA-DRB 1-0301 F SLAFTSWSLGEFLGS _ I TabIeXLVI-V14-HLA-DRBI-010l I5mers-98P6 1 VLALVLPSIVILDLS 1 1mers-98P4B6 Each peptide is a portion of SEQ ID NO. 2 PAAAWKCLGANILRG 18 Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the PIEWQDRKIPPLST _18 29; each start position is specified, the length of peptide is 15 amino acids, and 122 WRNPVLPHTNGVGPL 18 length of peptide is 15 amino acids, and the end position for each peptide is the 135 PLWEFLLRLLKSQAA 18 the end position for each peptide is the starl ition phs fourteen. 14 LLRLLKSQAASGTLS 18 start position plus fourteen. Pos 123456789012345 score 148 AASGTLSLAFTSWSL 18 Pos 123456789012345 score 9 HYTSLWDLRHLLVGK 2 159 SWSLGEFLGSGTWMK 4 10 LRLFTFWRGPVVVA 28 L76 VIELARQLNFIPI 27 161 SLGEFLGSGTWMKLE 18 2 AREIENLPLRLFTFW 2 228 YSFVRDVIHPYARN 27 169 GTWMKLETIILSKLT 18 15 FWRGPVVVAISLATF 22 322 CLPMRRSERYLELNM 27 17 THLSKLTQEQKSKH 18 13 FTFWRGPVVVAISLA 54 YHVVIGSRNPKFASE 2 LVLPSIVILDLSVEV 17 12 LFTFWRGPVVVAJSL 18 296 MTLOCRKQLGLLSF 26 9 IVILDLSVEVLASPA 17 EIENLPLRLFTFWRG 16 408 FHVLIYGWKRAFEEE 2 3 GANILRGGLSEIVLP 171 PLRLFFWRGPVVVA 16 273 AGLLAAAYQLYYGTK 25 61 PPAMWTEEAGATAEA 17 11 RLFTFWRGPVVVAIS 1 439 PSIVILDLLQLCRYP 25 67 EEAGATAEAQESGIR 17 _1 SAEENLPLPLFFF 14 09 VGKIUDVSNNMRIN 2 9 GVVTEDDEAQDSIDP 17 ENLPLRLFTFWRGPV 1 288 YRRFPPWLETWLQCR 2 101 EAQDSIDPPESPDRA 17 41 TFWRGPVVVAISLAT 14 87 NIIFVAfHREyrL 23 107 DPPESPDRALKAANS 17 81 RIFTFWRGPVVV 12 43 YYRFyTPNFVLALV 23 133 VGPLWEFLLRLLKSQ 17 133 LASLFPDSUVKGFN 22 143 LLKSQAASGTLSLAF 17 185 LNFIPfDLGSLSSAR 22 162 LGEFLGSGTWMKLET 17 TableXLVI-V21-HLA-DRBI0I0i 261 IVArTLLSLVYLAGL 2 163 GEFLGSGTWMKLETI 17 5mers-98P 6 272 LAGLLAAAYQLYYGT 22 172 MKLETILSKLTQEQ 17 Each pepide is a portion of SEQ ID NO: 433 VLALVLPSIVILDLL 22 43; each start position is specified, the 145 GFNVSAWALQLGPK 21 237 TableXLVII-V I-HLA-DRB1-0301- TableXLVH-V1-HLA-DRB1-0301- TabkXLVII-V2-HLA-DR 1-0301 15mers-98P4B6 15mers-98P4B6 I mers-98P4B6 Each peptide Is a portion of SEQ ID NO: Each peptide is a portion of SEQ 1D NO: Each peptide is a portion of SEQ ID 3; each start position is specified, the 3; each start position is specified, the NO: 5; each start position Is specified, length of peptides 15 amino acids, and length of peptide is 15 amino acids, and the length of peptide is 15 amino acds, the end position for each peptide is the the end position for each peptide is the and the end position for each pepEde is start position plus fourteen. I start ition lus fourteen, the start position plus foutn. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 214 GPVVVAISLATFFFL 21 327 RSERYLFLNMAY V 17 1 SSGFTPFSCLSLPSS 2 269 LVYLAGLLAAAYQLY 21 338 YQQVHANIENSWNEE 17 2 fSCLSLPSSWDYRP 20 362 SFGIMSLGLLSLLAV 21 379 IPSVSNALNWREFSF 17 2 SLPSSWDYRCPPPCP 6 363 FGIMSLGLLSLLAVT 21 41 KRAFEEEYYRY-PP 17 2 GSPGLQALSLSLSSG 12 175 RQQVIELARQLNFIP 20 151 ETCLPNGINGIKDAR 161 3 SPGLQALSLSLSSGF 12 198 AREIENLPLRLFTLW 20 72 IVVDVThHEDALTKT 1 8 ALSLSLSSGFrPFSC 12 258 TLPIVAITLLSLVYL 20 7 HEDALTKTNHFVAI 1 LSLSLSSGFTPFSCL 12 264 ITLLSLVYLAGLLAA 20 88 IIFVAIRREHYTSLW 16 10 SLSLSSGFTPFSCLS F 376 VTSIPSVSNALNWRE 20 111 KILIDVSNNMRINQY 16 22 CLSLPSSWDYRCPP 11 400 YVALLISTFIIVLIYG 20 205 PLRLFTLWRGPVVVA 16 3 DYRCPPPCPADFFLY 10 435 ALVLPSIV!L-DLL L 201 248 YKIPIEIVNKTLPIV 16 31 YRCPPPCPADFFLYF 10 438 LPSIVILDLLOLCRY 20 279 AYQLYYGTKYRRFPP 1 12 SZ,-3FTPFSCLSLP 9 440 SIVDLL LCRYPD 20 342 HANIENSWNEEEVWR 16 17 FTPFSCLSLPSSwDY 9 30 KVTVGVIGSGDFAKS 19 382 VSNALNwREFSFIQS 16 53 GYHVVIGSRNPKFAS 19 413 YGWKRAFEEEYYRFY 16 110 GKILIDVSNNMRINQ 19 43 KSLTIRLIRCGYHV 15 TabeXLVI-V5A-HLA-DRI4J301. 130 AEYLASLFPDSLIVK 19 263 AITLLSLVYLAGLLA 1 5 l5mers-98P4B6 151 AWALQLGPKDASRQV 19 294 WLETWLQCRKQLGLL 13 Each peptde is a portion of SEQ ID NO: 215 PVVVAISLATFFFLY 19 321 LCLPMRRSERYLFLN 5 11; each start position is specified, the 217 VVAISLATFFFLYSF 19 367 SLGLLSLLAVTSJPS 5 length of peptide isi1 amino acds, and 256 NKTLPIVAITLLSLV 19 387 NWREFSFIQSTLGYV 15 the end position for each peptide is the 312 FAMVHVAYSLCLPMR 19 41 IYGWKRAFEEEYYRF 1 start position plus fourteen. 320 SLCLPMRRSERYLFL 19 73 VVDVTHHEDALTKTN 14 Pos 123456789012345 score 402 ALLISTFHVLIYGWK 19 104 LRHLLVGKILLDVSN 1 3 1[LPLLFTFW 2 3 SISMMGSPKSLSETC 18 23 IRPYARNQQSDFYKI 14 10 PLRLFTFWRGPVVA 1 22 INGIKDARKVTVGVI 18 26 LSLVYLAGLLAAAYQ 14 2 SAnIENLPLRLFrF 12 34 GVIGSGDFAKSLTIR 18 3 OLGLLSFFFAMVHVA 14 _ iENLPtRLFrAJRGP 1 90 FVAIHREHYTSLWDL 18 36 IMSLGLLSLLAVTSI 14 119 NMRINQYPESNAEYL 18 373 LLAVTSIPSVSNALN 14 51 EINLPLRLFTFWRG 11 139 DSLIVKGFNVVSAWA 18 401 VALLISTFHVLIYGW 14 13 LFTFWRGPVVVAISL 1 143 VKGFNVVSAWALQLG 18 434 LALVLPSrvILDLLQ - 14 4 9 162 SRQ ICSNNIQARQ 18 MESISMMGSPKSLsE 13 _ LRLFTFWRGPVVVAI 9 184 QLNFIPIDLSLSSA 18 ISMMGSPKSLSETCL 13 195 LSSAREIENLPLRLF 18 32 TVGV1GSGDFAKSLT 13 TabIeXLVII-VSB-HLA-DRI 233 RDVIHPYARNQQSDF 18 33 VGVIGSGDFAKSLTI 13 0301-15mers-98P4B6 308 LSFFFAMVHVAYSLC 18 101 LWDLRHLLVGKILJD 13 Each peptide is a portion of SEQ ID 331 YLFLNMAYQQVHANI 18 138 PDSLIVKGFNVSAW 13 NO 11; each start position is specified, 360 YISFGIMSLGLLSLL 18 164 QVY[CSNNIQARQQV 13 the length of peptdeIs 15 amino adds, 409 HVLIYGWKRAFEEEY 18 189 PIDLGSLSSAREIEN 13 and the end position for each peptide is 7 MGSPKSLSETCLPNG 17 201 IENLPLRIFTLWRGP 13 e start Position plus fourteen. 21 GINGIKDARKVTVGV 17 213 RGPVVVAISLATFFF Pos 123456789012345 score 38 SGDFAKSLTIRLIRC 17 26 LLSLVYLAGLLAAAY 13 113 LIDVSNNMRINQYPE 17 407 TFHVLIYGWKRAFEE 1 23QTLELEFSFLL I 20 121 RINQYPESNAEYLAS 17 1 155 QLGPKDASRQVYICS 17 TabIeXLVII-V2-HLA-DRI-0301. 1 FADTQTELELEFVFL 16 169 SNNIQARQQVIELAR 17, l5mrs-98P4B6 21 DTQTELELEFVFLLT 16 178 VIELARQLNFIPIDL 17 Each peptide is a portion of SEQ ID 17 CSF T TELELEFV 15 192 LGSLSSAREIENLPL 17 NO: 5; each start position is specified, 22 TQTELELEFVFLLTL 13 225 FFFLYSFVRDVIHPY 17 the length of peptide is 15 amino acds, 2 SNALNWREFSFIQJF 11 249 KIPIEIVNKTLPIVA 17 and the end position for each peptide is 1 FSFIQEFCSFADTQT 11 292 PPWLETWL)QCRKQLG 17 the start sition us fourteen. 3181 _AYSLCLPMRRSER 17 PosT 123456789012345 s-core I N 6 15ALSLSLSSGFPF 2 5iers-98P46 2-39 TableXLVIl-V13-HLA-DRI- 3 15mes-984B615mers-98P4B6 Each peptide is a Portion of SEQ ID t- Each peptide is a portion of SEQ ID NO: Ecpetdsap S ID 13; each f psti is speciPids, and 15; each start position isc NO: 27; each start position is Specid length of peptide is 15 amide is hie length of peptide is 15 amino acids, and Nhe eah f pepti is scieds the end position for each pepe the end position for each peptide is the the length ot peptide is 15 amino a s position0p2us score start sition lus fourteen and the end position for each peide is L SVL K LF P2Pos 123456789012345 the start sition lus oren cr h tr I s fourteen. 2 Pos 123456789012345 score 123456789012345 score 8 LPSIVILGKLFLP 22 93 VGVVTEDDEA DSID 29 Po13 ETF5LNINGIKDAR 16 3 VLALVLPSIVILGVL 22 13 TNGVGPLWEFLLRLL 26 SMMpGKSLSETFL 13 9 PSIVILGKILFLPC 21 7 PSIVILDLSVLAS 24 12 SETLPNGINGIKDA 13 1 SIVILGKIILFLPCI 2 1 VLALVLPSIVILDLS 22 2 SETFLP NGING 12 17 IILFLPCIS1 8 SPVALDLSVEVLAP 21 4 PKSPLS TP N 9 25 SRLLPCIS M S 18 133 VGPLWEFLLRLKS 21 t0 SLSETFLPNGINGIK 9 21 LPCSRKLKKK W 1 3 ALVLPSIVLDLVE 20 21 PCSRLKRKKW 17 163 GEFLGSGW MLT 2 TableXLVi-V14-HLA-DRI-0301 28 LKRIKGWEKS FLE 16 9 IVILDLSVEVLASPA 19 15mers-98P4B6 29 K GWEKS FLEE 13 13 RNPLPHTNGVG 19 Each peptide is a portion of SEQ ID NO: 4S LALV.LPCSI~l 13 137 WEFLLKSAS 9 29; each start position is specified, the 14 LGKIILFLPCISRKL 13 1 SLAFTSWSLGEFLGS 1 length of peptide is 15 amino acids, and 15 GKLFLPCIS 12 8 WLSEI SKLT E 18 the end position for each peptide is the I NFVLALV S ILG 12 38 LSEIVLP DRK 18 start ition lus fourteen. 5 LLSVIGH 2 179 LSKLT E KSKHCMF 18 Pos 123456789012345 score 37 KS FLEEIGGTH 42 EFVLPIEW DRKIP 17 2 AREIENLPLRLPTFW 2 ableXLVW AH DR1 I-0301 44 PIEW DRKIPPLST 9 PLRLFFWRGPVVVA 1 abeX -A-LA-D 9 IPVVGVVTEDDEA D1) to SAREIELLRLFTF 1 c e rtion of SEQ ID 17 TSKLT E KSKH1 5 IENLPLRLFWGP 12 Each peptide is a oton te SV-EVLASPAAWCL 15 7 N LLLTWGPVV 121 NO: 15; each start position is specified. KCLG ALRGGLSE 1 4 EENLPLRLFTFWRG 12 the length of peptide is 15 amino acids, 2 KC L. LIE 15 1 E LFRLHT'VAI to and the end position for each peptide is 3 NILRGGLSE LIE 5 12 LFTFWRGPVVV ISL 10 the start sion tus fourteen. 3 SEIVLPIEW DRKI 15 3 RE1ENLPLRLFTFW 9 thsa34567890123,45 score iti LKAANSWRNPVLPT 15 10 LRLFTFWRGjPVVVAI 9 I SISMMG- PKS 1 138 EFLLRLLK AASG 15 0LRF VRP" 9 5osGSPKS T LNG 1 175 ETIlLSKLT E KS TbIeXLVHV21HLADR 0 3 0 5 MGSPK 16 LALVLPSIVLDLSV 14 152ners-98P 4

B

6 2 ISMMvGSPKSLS ~1L 13hpptdi 1 21 3 ET L P N G I N G I K D A is a o tio n o f S E Q ID N O : 2 SEML GNG KA 13 TabeXLV-V8H LA-DRI0301- 43 ea t sition is specified. the 8 PKSLSETFLN 154IN 11mers-98P 4

B

6 length of peptide is 15 amino acids, and 4 GSPKSLSETF LPN Each peptide is a portion of SEQ ID NO: the end position for each peptide is the 4 S SE FLPN N K 8 17; each start position is specified, the start sition lus fourteen. length of peptide is 15 amino acids, and Pos 123456789012345 score L LADRI-0301- the end position for each peptide is the 6 LSKLT E KTKHCMF 18 nTableXL'i-_l-V7B- -PI start sition lus fourteen. 3 TRLSKLT E KTKH 16 Each peptide is a pon of SEQ ID NO: Pos 123456789125 2 ETLSKLT E KTK I5 Each start position is specified, the 7 KS FLEEGMGGIH 12 I L LSKLT 15; eachstartp o amn sa and a FLEEGMGGTIPHV 11 4 ULSKL E KTHC o length of peptide is 15 amin acids, an9 LEMGIV I the end position for each pepide is the 12 EEGMGGTIPHVSPER 0 5 I LSKLT E KTKHCM 9 tatiosition his fourteen. I IKKGWEKS FLEEGM 9 L E KTKH Pos 123456789012345 score 4 GWEKS FLEEGMGGT 7 9 T KTKCMFSLISG 9 5 LNMAY STLGy 8 5 WEKS FLEEGMGGTE 7KbeX y V2 - L DR 0 9 I RSERLF AY R 17TableXLVI-V25HLJADRl -030 1 ~~~ ~ ~ ~ IIS SiSL 41mers-98P

B

6 62 LFSTL GYVALUST 12 TableXLVV 3HLADR1 3 01 Each peptideis portion of SEQ ID NO 12 Y IT I E 5mers-98P4B6 51; each start position is specified, the 3 ERLFLNMAY ST I Each peptide is a portion of SEQ ID length of peptide is 15 amino acids, and SFLNMAy YVA 11 NO: 27; each start position is specified. the end position for each peptide Is the 7 FLNMA YQSTL YVA 11 the length of peptide is 15 amino acids, sa s us fourteen. 14 STLGYV ALLSTFH II and the end position for each peptide is Pos 1234567901345 score 14 STLGYVAL 10 the start osition lus fourteen. IILFLPCIS KLKRI 21 8 AY S Pos 123456789012345 score 8ILFLPCIS KLKRI M I SISMMGSPKSLS 18 7 S KLKRIKEKS 1 TableXLVf:V7:C: A-DR'1O 5 MGSPKSLETFLPNG 17 14 S KL 239 TableXLVIl-V 5-1LA-DR=030 F T 'ableXLVIII-V I-HLA-DR 1-0401- TableXLV11II 11DR 041 15Smers-98P4B6 I Sniers-98P4B6 I Smers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO:, Eachpeptide is a portion of SEQ 1D -N: 51; each star position is specified, the 3; each starl position is specified, the 3; each start position Is specified, the length of peptide is 15 amino acids, and length of peptide is 15 amino adds, and length of peptide is 15 amino acids, and the end positions eh p~eeis the the end posion rechpeptie isthe the end position for each pepe s te start Psition Plus fourteen. - start Position Dhis fourteen,. __ start psitin plus fourteen. Po-s 123456789012345 scoe Pos 123456789012345 sore Paos 123456789012345 score - UFCISQKLKRJIKKGW 17 86 TNUIFVAIHRERyT 20 142 WVKGFNVVSA' L 1 3 JGKI1LFLPC1SQKL 13 90 FVALHREHYTSLWDL 20 154 L LGPKDASRQ VC 18 4 GKIILFLPCISOKLK 13 101 LWD RHLLVG1CIJJ) 20 161 ASR VYICSNNI AR 18 51 KIILFLPCISOKLKR I11 106 HLLVGKILIVSNNM 2 168 CSNNIQAR. VIFLA 18 I I GKILIVSNMI 20 186 NFIP1DLGSL SSARE 18 TableXLVH-V1 HLADRI..j-001 III KILJDVSNNMRN Y 2 195 -LSSAREIENCPLRLpF 18 15mers-98P4B6 113 LIDVSNNMRINOYPL3 20 234 DVIHPYARNQQSDFY 18 Each peptide is a poriGo f SEQ ID NO: 130, AEYLASLFPDSUVK 2 248 YKIPIEIVNKTLPfV - 18 3; each stairtpostion is specified, the 133 LASLPPDSLIVKGFN 2( 257 KTLPIVA]TLLSLVY 18 length of peptide is 15 amnino acids, and 139 DSLIVKGFNVVSAWA 2 289 RRFPPWLETWLOCRC 18 the end position for each peptide is the 14 SLIVKGFNVVSAWAL -2 C3-39 OQVHANIENSWNEEE 18 stal ostio pusfouten.t45GFNVVSAWALOLGPK 2 3481 SW EEVWREMY1S 18 Pos 123456789012345 score _62' SRQVICS14NIAR0 20 359 M SFGIMSLGLL.SL 18 420 EEEYYRFYTPNFVL 28 176 QVIELAR_ LNFIPI 2N 34 GMLLSL S 1 98YSWDRLVGJ 2 185 LNFIPIDLGSLSSAR 2 34 NALNWREFSFIQSTL 18 109 VGKILIDVSNNMRIh1 26 189 PIDGSLSSAREIEN 2 387 NWREFSFIOSTLGYV_ 18 17 ~I1RLF 6192 LGSLSSAREIENUPL 2 399 GYVALUSTFHVUIY 18 205'PLRLFTLWRGPVVVA 261 217 VVAISLATFFFLYSF 20 432 FVLALVLPSIVIDL 18 213 RGPVVVAISLATFFF 261 219 AISLATFFFLYSFVR 2 66 ASEFFPHVVDVrIIJW 161 225 FFFLYSFVRDVmPY 26 233 RDVIHYARN(Q SDF 201 6 SEFFPHVVDVTHHED 16 22 YFRDIPYRQ 47 FYKIPIWNKTLPI 20 9 REHYTSLWDLRI{LLV 16 312 FAMVHAYSLCLPMJ( 2- 256 NKTLPIVArrLLSLV 201 12 IN YPESNAEYLASL -16 370 LLSLLAVTSIPSVSN 26 25-8 TLPIVAITLLSLVYL 201 12 NAEYLASLFPDSLIV 16 373 LLAVTSESVSNALN 26 61I IVAITLLSLVYLAGL 20 2 LRLFTLWRGPVVVAI 16 3i76 VrSIPSVSNALNWRE 26 26 ITLLSLVYLAGLLA 20 2 FT GVASA 1 38SDFKL~LC 2266 LLSLVYLAGLLAAAY 2 22 TFFF1LYSFVRDVU1P 16 51 RCGYHVVGSRPjKjF 22 267 LLVYLAGLLAYQ _2 22 FFLYSFVRDV11PYA 16 62 NPKFASEFFPHYVDV 22 2 73 ALAYLYYGTK 20 228 LYSFVP Dvu YARN 16 87 NIIFVA~iREHYTSL 22 T2 PPWLEWLQCRK LG 20 2i36 l-YARNQ SDFYKI 1 143 VKGFNVVSAWALQLG 22 302 RKQLGLLSFFFAMVH 20 245 _SDFYKIPIEIVNKTL I 163 QVYFEIcSNIQA 22 30 QLGLLSFFFAMVHVA 20 268 SLVYLAGLLAAAYQL I4 18 QNFPDLSSS 2331 YLFLNMAYQ VHANI 20 285 GTKYRRFppWLETWL 16 222 -LATFFFLYSFVRDVI 22 351 EEEVWRIEMYISFGI -2 288 YRRFPPWLETW QR 16 244 QSDFYKIPIEIVNKT 22 35 VWRIEMY1SFGIM4SL 2 308 LSFFFAMVHVAYSLC 16 307 LLSFFFAMVHiVAYSL 22 362 SFGIMSLGLLSLLAV 2 330 RYLFLNMAYQQVHAN% 14 30 SFAMHAYLL l 365 IMSLGLLSLLAVTSI 2 35 NMAYQQVIIANIENSW 161 328 SERYLFLNMAYQQVH 22 367 SLGLLSLLAVTSFPS- 20 352 EEVWRIEMY1SFGM 16 34 NWEEWJM 2368 -LGLLSLLAVTSIPSV ,20 360 YISFGIMSLGLLSLL 1 35 EM37IMLLL 2 IPSVSNALNWREFSF 20 390 EFSFIQSTLGYVALL 1 385 ALNWREFSFIQSTLO 22 _19 QSTLGYVALLISTFH- 201 397 TLGYVALLISTFHfVL 1 388 WREFSFIQSTLGYVA 22 398 LGYVALLISTFH-VLI 20 412 IYGWKR AFE---R- 1 405 ISTFHVLIYGWRKX4F 2 401 VALLISTFHVLIYGW 20 416 KRAFEEEYYRFYTrpP 16 423 YYRFYTPPNFVLALV 22 430 PN ALVLPSWVIL 20O 424 YRFYTrPPNFVLALVL 16 429, PPNFVL-ALVLPSIVI 22 431 NFVLALVLPSIID- -20 2i96 Efl;WEQCRQLGLLSF 15 I MSTSI~G~pSLE 2 ~ ALVLPWLLQ 20 3 SISMMGSPKSLSETC 14 15 ETCLPNGINGIKDAR 2..) 438 LPSIVILDLIQLCRY 201 ISMMGSPKSLSETCL 14 19 PNGINGKDARKVTV 20 440 SIVELDLLOLCRYPD 20 32 TVGVIGSGDFAXSLT 14 22 INGIKDARKVTVGVI 20 -12 SLSETCL.piNI 18 33 VGVIGSGDFAKSLT1 14 30 KVTVGVIGSGDFAKS 20 -21 GINGiKDARKvrvG -18 44 SLTIRLIRCGYHVVI 14 47 IRUIRCGYHVVIGSR 20 36 IGSGDFAKSLTMRT -18 46 TIRLfRCGYIIVVGS 14 53 GYHVV1GSRNPKFAS 20 76 VTHHEDALTKTNMW -18 -54 YlqcSRNPysASE 14 70 WHVVDVTIIWDAJLT, 97 HSLWDLRHLLVGK 1 '18 73 VDVTF.I-EAJLTKTN I14 711 PHVVDVHHEDALTK 2 240 TableXLVIH-VI-HLA-DR 1-0401- TableXLV111-V5A-H[A-DRB1- TableXLVlI-V6-HLA.DR 15mers-98P4B60401-1mrs-98P4B6 0401-1 ers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of S ac peptide is a portion of SEQ ID NO: 3; each start position is specified, the NO: 11; each start posibon is specified, 13; each start position is specified, the length of peptide is 15 amino acids, and the length of peptide is 15 amino acids, length of peptide is 15 amino acds, and the end position for each peptide is the and the end position for each peptide is the end position for each peptide is the start position plus fourteen. - start position plus fourteen. I _ start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 8 EDALTKTNIIFVAIH 14 28 SWDYRCPPPCPADFF 16 11 fVILGKIILFLPCIS 14 85 KTN VA EHY 1 LQALSLSLSSGFF 14 15 GKFLPCISRKLK 14 88 IIFVAIHREHYTSLW 14 2 FSCLSLPSSWtYRCP 14 6 KIILFLYCISRKLKR 14 117 SNNMRINOYPESNAE 14 PGLQALSLSLSSGFT 12 25 SRKLKRIKGWEKSO 14 11 NMRINYPESNAEYL 14 13 LSSGFTPFSCLSLPS 12 28 KKOWKSQFLE 1 151 AWALQLGPKDASRQV 14 1 GFTPFSCSLPSSWD 12 38 SQ EGIGGTPHV 14 178 VIELAROLNFIPIDL 14 19 PFSCLSLPSSWYRC 1 42 EEGIGGTIPHVSPER 1 182 ARQLNFIPIDLGSLS 14 24 SLPSSWDYRCPPPCP 12 6 LVLIiLGKIILF 12 187 FIPIDLGSLSSAREI 14 7 VLPSIVILGKILFL 12 198 AREIENLPLRLFTLW 14 TableXLVI-V5B-HLA-DRB1. 13 IGKIILFLPCISRK 12 203 NLPLRLFTLWRGPVV 14 0401-5mers-98P4B6 3 GWEKSQFLEEGIGGT 12 208 LF.TLWRGPVVVAISL 14 Each peptide is a portion of SEQ ID 43 EGIGGTIPHVSPERV 12 214 GPVVVAISLATFFFL 14 NO: 11; each start position is specified, 232 VRDVIHPYARNQQSD 4 the length of peptide is 15 amino acds, 249 KIPIEIVNKTLPIVA 14 and the end position for each peptide TableXLVUI-V7A-HLA-DRBI. 252 IEIVNKTLPIVArFL 14 t start Position plus fourteen. 0 4 01-15mers-98P4B6 259 LPIVAITLLSLVYLA 14 Pos 123456789012345 score Each peptide Isa portion of SEQ ID 263 AITLLSLVYLAGLLA 14 ALNWREFSFIQ[FCS 22 NO: 15; each start position is speciied, 26 LVYLAGLLAAAYOLY 14 7 WREFSFIQEFCSFAD 22 the length of peptide is 15 amino adds, 272 LAGLLAAAYQLYYGT 14 - EFSFIFCSFADTQ 22 and the end position for each ede I 305 LGLLSFFFAMVHVAY 1 13 IQLFCSF TQTELE 22 e star position us fo 311 FFAMVHVAYSLCLPM 14 10 FSF1 IFCSFADTQT 20 Pos 123456789012345 score 314 MVHVAYSLCLPMRRS 14 23 QTELELEFVFLLTLL 20 13 ETFLPNGINGEKDAR 2 318 AYSLCLPMRRSERYL 14 3 NLSF1QC 18 1 SLSETFLPNGING[K 18 322 CLPMRRSERYLFLNM 14 1 IFCSFADTQTELELE 18 12 SETFLPNGINGIKDA 16 329 ERYLFLNMAYQQVHA 14 16 FCSFADTQTELELEF 16 1_I S 14 333 FLNMAYQQVHANIEN 14 12 FIQICSFADTQTEL 14 2 ISMMGgPKSLSETFL 14 342 HANIENSWNEEEVWR 14 6 NREFSFIQFCSFA 12 5 MGSPKSLSETFLPNG 12 35 RIEMYISFGIMSLGL 14 1 QICSFADTQTELEL 12 7 SPKSISErFLPNGIN 12 363 FGIMSLGLLSLLAVT 14 20 ADTQTELELEFVFLL 12 1_ KSLS 12 371 LSLLAVTSIPSVSNA 14 22 TQTELELEFVFLLTL 12 391 FSFIQSTLGYVALLI 14 2 TELELFVLLTLLL 12 TableXL.HI-V7B-HlA-DR1.. 400 YVALLISTFHVLIYG 14 0401-15mers-98P4B6 402 ALLISTFHVLIYGWK 14 TabIeXLV1I-V6-HLA-DRl1 Each peptide is a portion of SEQ ID NO: 40 TFHVLIYGWKRAFEE 14 0401-I5mers-98P46 15; each start position is specified, the 409 HVLIYGWKRAFEEEY 14 Each peptide is a portion of SEQ ID NO length of peptide isi1 amino adds, and 433 VLALVLPSIVILDLL 14 13; each start position is specified, the the end position for each peptide is the 439 PSIVILDLLQLCRYP 1 4 length of peptide is 15 amino adds, and start posin plus fourteen. - the end position for each peptide is the Pos 123456789012345 score TableXLVIII-V5A-HLA-DRB31- start position plus fourteen. F YLFLNMAY STLGY 26 0401-15mers-98P4B6 Pos 123456789012345 score 2 SERYLFLNMAYQQST 22 Each peptide is a portion of SEQ ID -8 ILFLPCISRKLKIK 26 1 QSTLGYVALLISTFH 20 NO. 11; each start position is specified, 17 IILFLPCISRKLKRJ 22 4 RYLFLNMAYQQgML 16 the length of peptide is 15 amino acids, _L KSQFLEEGIGGT[PH 22 9 NMAY STLGYVALL 16 and the end position for each peptide is I NFVLALVLPSIVILG 2 3 ERYLFLNMAYQQSTL 14 the start position plus fourteen. 5 ALVLPSILGKIIL 20 7 FLNMAYQQSTLGYVA 14 PosI 123456789012345 score 8 LPSIVILGKIILFLP 20 1 RSERYLFLNMAYQQS 12 14 SSGFTPFSCLSLPSS 22 14 LGKIILFLPCISRKL 20 6 LFLNMAYQQSTLGYV 12 17 FTPFSCLSLPSSWDY 22 46 GGTIHVSPERVTVM 2 11 AYQQSTGYVALLIS 12 3 SPGLQALSLSLSSGF 20 FVLALVLPSIVLK 18 1 STLGYVALISTFHV 2 i SLSLSSGFTPFSCLS 2 22 PCISRKLKRIKGWE 18 2 GSPGL ALSLSLSSG 3 RIKGWEKSQFLEEG 18 18UI-V7C-HLA-DRB SLSSGFrPFS 18 3. VLALVLPSILOKI 14 4--15mers-985-B6 241 Each peptide is a portion of SEO ID NO: TableXLVIJV7C-HIAD"I- TabeXLV-V2I-HLA-D I 15; each start position is specified, the 04 Ol-l5mers-98P4B6 0401-15mers-98P4B6 length of peptide is 15 amino acids, and Each pepfie is a portion of SEQ 1D NO: Ea pide is a portion of SEQ ID NO: the end position for each peplide is the 15; each start position is specified, the 43; each start position is specified, the start position plus fourteen. length of peptide is 15 amino acids, and length of peptide isi1 amino acids, and Pos 123456789012345 score the end position for each peptide is the the end position for each peptide is the _34 GPLWEFLLRLLKSQA 28 start sition lus fourteen. start ition us fourteen. 168 SGTWMKLETIILSKL 28 Pos 123456789012345 core Pos 123456789012345 score 7 PSIVILDLSVEVLAS 26 179 LSKT E KSKHCMF 3 TIULSKI E KTK 2 13 DLSVEVLASPAAAWI 2- 2 ETISKIT EQKTK 15 1131DRALKAANSWRNPVL 26 TableXLVlI.V8HLADBI-401. 6 LSKLT EQKTKHCMF 14 13 EFLLRLLKSQAASGT 26 5mers-98P4B6 ILSK E KTKHCM 12 150 SGTLSLAFSWSLGE 26 Each peptide is a portion of SEQ ID N0 176 TILSKLTQEQKSKH 26 17; each start position is specified, the TableXLVll1-VZ5-HLA-DpI. 23 AAAWKCLGANILRGO 2 length of peptide is 15 amino acids, and 0401-5mers98P4B6 62 PAMWTEE-AGATAEA9 22 the end position for each peptide is the Each peptide is a portion of SEQ ID NO. 162 LGEFLGSGTWMKLET 22 start positon plus fourteen. 1 51; each stat position is specified, the 3 ALVLPSIVILDLSVE 20 Pos 123456789012345 score length of peptide is 15 amino acds, and 8 SILDLSVEVLASP 20 7 KSFLEEGMGGTIPH 22 the end position for each peptide is the 31 ANILRGGLSEIVLPI 20 83 SFLEEGMGGTIYHV 1 start Position Dlus fourteen. 40 EIVLPIEWQQDRKIP 20 EEGMGGTIPHVSPER 1 Pos 123456789012345 score 50 DRKIPPLSTPPPPAM 23 QFLEEGMGGT 12 7 ILFLPCISQKLKIK 26 61 PPAMWTEEAGATAEA 2 13 EGMGGTIPHVSPERV 6 IELFLPCISQKLKRU 22 89 QIPVVOVVTEDDEAQ 20 1 KKGWECSQFLEEGMG 1 3 LGKIILFLPCISQKL 2 92 VVGVVTEDDEAQDSI 20 4 3 GKIILFLPCISQKLK 20 i30TNVGLWFLRL 2 TableXLVIll.V134ijA.DRBI. I 11 CISQKLKRICKGWE 18 130 TNGVGPLWEFLLRLL 20 0 4 01-5mers-98P4B6 5 KI 4 1331 VGPLWEFLLRLLKSQ 201 137 WEFLLRLLKSQAASG 20 Each peptide Is a portion of SEQ ID 14 SQKLKRIKKGWEKSQ 14 159 SWSLGEFLGSGTWMK 20 NO: 27; each start position is specified, 2 LGKIIFLPCISQK 12 169 GTWMKLETHLSKLT 20 the length of peptide is 15 amino acds WKEIIS.TE -- and the end position for each peptide is lXI- I-L-R I-I1 1W71 ______________ _ 20 te start Poition pus fourteen. TbeLXV-L.nB.111 27 KCLGANILRGGLSEI 18 27KCGNIRGLE1 - 8 Pos 1123456789012345 score 15mers-98P4B6 74 VTEAQDUU4SSSSS 1 18 13 ETFLPNGINGIKE)AR -20 Each peptide is,a portion of SEQ ID NO: 95 TDEQSDP 1 14 KLKQASGLSA 8 10 SLSETFLPNGING[K 18 3; each start po'bition is specified, the 12 RLLKSQAAT SLE 1 12 SMrLPNGINGIKDA 1 length of peptide is 15 amino acds, and 151 GTLSLAFTSWSLGEF 18 - _ 44 PIEWQQDRKIPPLST 16 2 ISMMGSPKSLSETFL 1 I _ start position plus fourteen._ 119 ANSWRNPVLPHTNGV 1 - MGSPKSLSETFLPNO 12 Pos 123456789012345 Iscor 15 FTSWSLGEFLGSGTW 1 7 SPKSLSETFLPNGIN 12 249 K10IEVNKTLP1VA 27 7 7 _ _ _ _ _ _ _ _ _ 157 7 - 9 K S L S E T F L N G I N G I 12 3 0 8 L S F F F A M V H V A Y S L C 2 7 175 E LSKLTOEOKSK 151 229 YSFVRDVWYARNQ 26 17 ETLLSLQSK 14 TableXLVlI-V4-HLADRBI. 281 _QLYYGTKYRRffPWL 25 1 VLALVLPSIVILDLS 04ETWLQCRKQLGLLs 25 LPSIVILDLSVEVLA 14 Each peptide is a poron of SEQ ID NO: 87 NHFVAIHREHYTSL 24 9 IVILDLSVEVLASPA 1 4 29; each start position is specified, the 388 WREFSFQSTLGYVA 23 11 ILDLSVEVLASPAAA 14 length of peptide is 15 amino ads, and 39 SFFFAMVHVAYSLCL 22 1 VEVLASPAAAWKCLG 14 the end position for each peptide is the -3 SISMMGSPKSLSETC 21 3 GANILRGGLSEIVLP 14 start position plus fourteen 7 PHVVDVTHHEDALTK 21 35 RGGLSEIVLPIEWQQ 14 123456789012345 score 98 YTSLWDLRHLLVGKI 21 38 LSEIVLPIEWQQDRK 14 PLRLFTFWRGPVVVA 175 RQQVIEAQLNFIP 21 39 SEIVLPIEWQQDRKI 14 1 LRLFFWRGPVVVAI I 205 PLRLFTLWRGPVVVA 21 4 VLPIEWQQDRKIPPL 14 1 LFTFRGpVVVAISL 1 70 FpHVVDVTmIEDALT 20 53 IPPLSTPPPPAMWTE 14 13 FWRGPVVVAISLA 1 9 _____________ 2 87 SS-IPVVGVVTEDDE 14 2 97 IPVVGVVTEDDEAOD 14 2 NLPLRLFPW 1 151 AWALOLGPKDASRQV 20 9 ~ TG~ EDD AOD 14 NL LPL TFW GPV ~263 AITLLSLVYLAGLLA 20 93 VGVVTEDDEAQDSID 14 3 R 1 -MESISMMGSPKSLSE 19 103 QDSIDPPESPDRALK 14 ENLPLRLFTFWRGP 1 51 RCGYHVIGSRNPKF 19 123 RNPVLPHTNGVGPLW 14 1 TFWRGPVVVAJSLAT 1 10 HLLVGKILIDVSNNM 19 141 LRLLKSQAASGTLSL 14 15 FWRGPVVA1SLATF 1 1 QL IDLGSLS 19 163T GEFLGSGTWMKLETI 14 26 LLSLVYLAGLLAAAY 19 242 TableXLIX-Vl-HLA-DRB-I 101- TableXLLX-VI -HLA-DRBI-I 101 I Smers-9815 B6 Imers-98P4B6 TableXLIX-V5A-HLA-DRB I Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID N6 110l-I5mers-98P4B6 3; each start position is specified, the 3; each start position is specified, the Each peptide is a portion of SEQ ID NO: length of peptide is 15 ammo acids, and length of peptide is 15 amino acids, and 11; each start position is specified the the end position for each peptide is the the end position for each peptide is the length of peptide is 15 amino acids, and start position plus fourteen. start position plus fourteen, the end position for each peptide is the Pos 123456789012345 score Pos 123456789012345 score start position plus fourteen. 351 EEEVWRIEMYISFGI 19 89 IFVAiREHYTSLWD 4 Pos 123456789012345 score 395 QSTLGYVALLISTFH 19 113 LIDVSMRIN YPE 14 -13 LFTWRGPVVVAISL 17 424 YRFYTPPNFVLALVL 19 189 PIDLSLSSAREIEN 14 10 PLRLFFWRGPVVVA 15 67 SEFFPHVVDVTHHED 18 198 ARIENLLRLFTLW 14 15 TFWRGPVVVA1SLAT B 222 LATFFFLYSFVRDVI 18 203 NLPLRThWRGPVV 1 3 ARELENUILRLrF 14 302 RKQLGLLSFFFAMVH 18 212 WRGPVVVASLATFF 14 8 NLPLRLFTFWRGPVV 14 307 LLSFFFAMVHfVAYSL i8 33 RDVFHPYANQQSDF 14 1 LRLFTWGPVVVAI 13 367 SLGLLSLLAVTSIPS 18 261 IVAITLLSLVYLAGL 14 1FTFWRGPVVVAISLA 12 37 LLSLLAVTSIPSVSN 18 319 YSLCLPM ERYLF 14 1 FWRGPVVVAISLATF 9 2 ARKVTVGVIGSGDFA 17 34 SWNEEEVWRl'MYIS 14 4 REIENLPLRFTFWR 8 8 TNIIFVAIHREHYTS 17 373 LLAVTSPSVSNAN 14 99 TSLWDLRHLLVGKIL 17 381 SVSNAYWkEFSF1Q 14 134 ASLFPDSLIVKGFNV 17 407 TFHVUYGWKRAFEE 14 TabeXLIX-V5B-HLA-DRB 14 VKGFNVVSAWALQLG 17 409 VLIYGWKRAFEEEY 14 lI0l-15mers-98P4B6 22 FFFLYSFVRDVIHPY 17 43 PNFVLALVLPSIVIL 14 Each peptide Is a portion of SEQ ID 22 FFLYSFVRDVIHPYA 17 435 ALVLPSVILDLL L 14 NO: 11; each start position is 244 SDFYKIPIEIVNKT 17 3 KV GVIGSGDFAKS 13 specified, the length of peptide is 15 335 NMAY VHANIENSW 17 33 VGVIGSGDFAKSLTI 13 amino acds, and the end position for 3 YISFGIMSLGLLSLL 17 101 LWDLRHLLVGKELID 13 each peptide is the start position plus 405 ISTFHVLIYGWKRAF 17 139 DSLIVKGFNVVSAWA 13 12 NAEYLASLFPDSLrV I 146 FNVVSAWALQLGPKD 13 123456789012345 score 13 LFPDSLIVKGFNVVS 1 178 VIELARQLNFIPIDL 13 WREFSFIQIFCSFAD 22. 163 RQVYICSNNIQARQQ l 185 LNFIPIDLGSLSSAR 13 9 EFSFIQJFCSDTQ 2 18 QLNFIPIDLGSLSSA 16 206 LRLFTLWRGPVVVAI 13 1 FCSFADTQTELELEF 11 268 SLVYLAGLLAAAYQL 16 208 LFLWRGPVVVAISL 13 ALNWREFSFIQEFCS 10 27 AYQLYYGTKYRRFPP 16 223 LYSFVRDVIH 13 1 I D 28 LYYGTKYRRFPPWLE 16 252 IEIVNKTLPIVATL 13 TabeXUX-V6-HLA-DRBI 1101 328 SERYLFLNMAYQQVH 16 256 NKTLPIVAJTLLSLV 13 33 RYLFLNMAYQQVHAN 16 280 YQLYYGTKYRRFPPW 13 idertoofP IDN 385 ALNWREFSFIQSTLG 16 311 FFAMVHVAYSLCLPM 13 each tars potion of SEQ tNO 397 TLGYVALLISTFHVL 16 358 SFGIMSLGLLS 13 1eah t pstin is saecid, the 429 PPNFVLALVLPSIVI 16 364 IMSLGLLSLLAVTS 13 th of peiti 15 amo adds and 4 AKSLTIRLIRCGYHV 15 376 VIPSVSNALNWRE 1 stend position fo ptee 47 IRLIRCGYHVVIGSR 15 391 FSFIQSTLGYVALL1 1 123456s8fourteenscore 103 DLRHLLVGKILIDVS 15 431 NFVLALVLPSILD 8 LPSIAJKIRFLP 21 142 IVKGFNVVSAWALQL 15 18 ELFLPCISRKLKRIK 21 21 TLWRGPVVVAISLAT 15 TableXLIX-V2-HLA-DRBI-I 101- 25 SRKLKRIKKGWEKSQ 20 317 VAYSLCLPMRRSERY 15 Ismers-98P4B6 318 AYSLCLPMRRSERYL 15 Each peptide is a portion of SEQ ID I IGGTIPHVS 20 322 CLPMRRSERYLFLNM 15 NO: 5: each start position is si 2 LPCIS 19 401 VALLISTFHVLIYGW 15 the length of peptide is 15 amino acids, 21 PCISRLKRIKKGW 1 408 FHVLIYGWKRAFEEE 15 and the end position for each peptide is 5 PCISRKUC ILW 15 428 TPPNFVLALVLPSIV 15 the start position plus fourten. 4 G HVSP1LGK]I 14 19 PNGINGIKDARKVTV 14 Pos 123456789012345 so 4 GGVLLVSPEVV 14 22 INGIKDARKVTVGVI 14 17 FTPFSC[SLPSSWDY 2 4 LALVLPSIVILG 13 43 KSLTIRLIRCGYHVV 1 3 SPGLQALSLSLSSGF 19 LALVLPSV L 13 52 CGYHVVIGSRNPKFA 14 28 SWDYRCPPPCPADFF 1~ ~1 WGKIIFLPCISR 13 53 GYHVVIGSRNPKFAS 14 2 SLPSSWDYRCPPPCP 14 56 VVIGSRNPKFASEFF 14 5 GLQALSLSLSSGFTP 12 4 EEGIGGTPHVS 13 66 ASEFFPHVVDVTHHE 14 8 ALSLSLSSGFTPFSC 12 77 THHEDALTKTNIIFV 14 10 SLSLSSGFrPFSCLS 12 1 OKIELFLPCISRKcU 12 85 KTNUFVAIREHyT 14 1_4 SSGFFPFSCLSLPSS 12 17 IILFLPCISRXLKRI 12 2 PSWYRP--P - 321 KKGWEKSQFLEEGIG 1 Each peptdeisprtionoSD NO 3;ec 2ta4pstoni3 pciid h TableXLIX-V6-HLA-DRB 1-1 101- TableXLIX-V7C-HLA-DRB 1-1101 - Each peptide is a portion of SEQ ID 15mers-98P4B6 1 Imers-98P4B6 NO: 27; each start position is Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: specified, the length of peptide is 15 13; each start position is specified, the 15; each start position is specified, the amino acids, and the end position for length of peptide is 15 amino acids, and length of pepbde is 15 amino acids, and each peptide is the start position plus the end position for each peptide is the the end position for each peptide is the fourteen. start sition lus fourteen. start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score IISISMMGSPKSLSETF 21 37 KSQFLEEGIGGTIPH 10 43 LPIEWQQDRKIPPLS 15 8 PKSLSETFLPNGNG 12 _____________ 73_AEAQESGIR}JKSSSS [ 5 12 SETFLPNGINGI[KDA 10 TableXLIX-V7A-HLA-DRB1- 3 ALVLPSIVILDL 14 1101-15mers-98P4B6 27 KCLGANILRGGLSEI 14 TableXLIX-V I 4-HLA-DRB I-I101 Each peptide is a portion of SEQ ID 75 AQESGIRNKSSSSSQ 14 l5mers-98P4B6 NO: 15; each start position is 89 OIPVVGVVTEDDEA 1 specified, the length of peptide is 15 135 PLWEFLLRLLKSQAA 14 29; each start position is specified, the amino acids, and the end position for 173 KLETIILSKLTQEQK 14 length of peptide is 15 amino acids, and each peptide is the start position plus 4 LVLPSIVILDLSVEV 13 the end position for each peptide Is the fourteen. 6 LPSIVILDLSVEVLA 131 start position plus fourteen Pos 123456789012345 score 8 SIvLSVEVIASI 13 Pos 123456789012345 score I SISMMGSPKSLSETF 21 26 WKCLGANILRGGLSE 13 1 LFTFWRGPVVVAISL 17 8 PKSLSETFLPNGING 1 28 CLGANILRGGLSEIV 3 PLRLFTFWRGPVVA 15 I SETFLPNGINGIKDA 10 87 SSQIPVVGVVTEDDE _13 1 TFWRGPVVAISLAT I5 90 1pvvGvv-rEDDEAQD 13 21 ARIE RL~FFF 14 TableXLIX-V7B-HLA-DRBI-1 101- 123 RNPVLPHTNGVGPLW 13 NLPLRLFTFWRGPVV 14 15mers-98P4B6 13 TNGVGPLWEFLLRLL 13 1 LRLFTFWRGPVVVAI 13 Each peptide is a portion of SEQ ID NO: 152 TLSLAFTSWSLGEFL 73 13 FTFWRGPVVAISLA 12 15; each start position is specified, the 1 AFTSWSLGEFLGSGT 13 15 FWRGPVVVAISLATF 9 length of peptide is 15 amino acids, and 169 GTWMKLETHLSKIT 13 3 REIENLPLRLFrFWR 8 the end position for each peptide is the 1 WMKLET_________ 13 start psition plsfourteen. 17 KLT SLTE 3 start ___ _ -oito plsfute.1 VILDLSVEVLASPAA 121 TableXLIX-V21I-HLA-DRB 1- J0l Pos 123456789012345 score 1 - I l__________ RYLFLNMAYQQSTLG 22 12 is 1 ortoofP4 INO 14 QSTLGYVALUSTFH 1 39 SEIVLPIEWQQDRKI 1 each tdrs potion of hN SERYLFNMAYQST 16 58 TPPPPAMWTEEAGATI 12 4;ec tr oho sseiid h 2FLNMAYQSTGYV 16 74 EAQESGIRNKSSSSS 12 length of peptide is 15 amino acids, and 7 FLNMAYQQSTLGYVA 13 7 ESGIRNKSSSSSQIP 12 the end position for each peptide is the 9 NMAYQQSTLGYVALLDEADSIDPPESPDR 12 start sition s fourteen Ta~XLXV7-LADBI110- 110 ESPDRALKAANSWRN 12 Pos 1123456789012345 score TableXLIX-V7C-HLA-DRB I-1I101 - 6S. EKK T 1 15mers-98P4B6 119 ANSWRNPVLPHTNGV 12 6 LSKLT E KTKH 17 Each peptide is a portion of SEQ IDNO: 124 NPVLPHTNGVGPLWE 12 8 KLT E KT KH 1 15; each start position is specified, the 140 LLRLLKS AASGTLS 12 length of peptide is 15 amino acids, and 15 SGTLSLALTSWSLGE 12 9 the end position for each peptide is the 154 SLAFTSWSLGEFLGS 12 start position plus fourteen. 17 TIILSKLTQEQKSKH 2 1 5-HL-DB 1 Pos 123456789012345 score Each peptide is a portion of SEQ ID NO: 137 WEFLLRLLKSQAASG 26 TabeXLIX-V8-HLA-DRRI-I 101- 51; each start position is specified, the 134 GPLWEFLLRLLKS A 25 5mers-98P4B6 length of peptide is 15 amino acids. and PIEWQQDRKIPPLST 24 Each peptide is a portion of SEQ ID NO: the end position for each peptide is the 121 SWRNPVLPHTNGVGP 21 17; each start position is specified, the start position plus fourteen. 13 DLSVEVLASPAAAWK 19 length of peptide is 15 amino acids, and Pos 123456789012345 score 5 DRKIPPLSTPPPPAM 18 the end position for each peptide is the T SQKLKREKKGWEKSQ 2 621PAMWTEEAGATAEAQ 181 start psition plus fourteen. 10____KKRKGW 1 62 PAMWTEEAGATAEAQ 18 Pos 123456789012345 score I IPCISQKLKRIKKGW 16 138 EFLLRLLKSQAASGT 18 - _ 23 AAAWKCLGANILRGG 17 3 EGMGGTIPHVSPERV 20 3 PCISQKL 15 168 SGTWMKLETILSKL 17 9 FLEEGMGGTIPHVS 13 3 ILFLPCISQKL 3 12 EEGMGGTEPHVSPER 13 LLCIQLRK 1 179 LSKLTQEQKSKHCMF 17 4 KILFLPCISQKLK 12 157 FTSWSLGEFLGSGTW 16 WEKSQFLEEGMGGTt 12 BLLPCISQKLKRI I1 Y VILDLSVEVLASPA 15 2 KKGWEKSQFLEEGMG 10 8 LFLPCISQK RIK 9 11 ILDLSVEVLASPAAA 15 - KSQFLEEGMGGTH 10 19 LASPAAAWKCLGANI i5 TAbleXLIX-VJ3-HLA-DRBI 35 RGGLSEVLPHEQ 15 1101-5mers-98P4B6 244 Table L: Properties of 98P4B6 V.1 Bioinformatic URL Outcome Program ORF ORF finder Protein length 454 aa Transmembrane region TM Pred http://www.ch.cmbnet.org/ 6TM, aa 214-232, 261 286, 304-325, 359-379, 393-415,426-447, N term inside HMMTop httpJ/www.enzim.huTopmtop/ 6TM, aa215-232 261 279 306-325 360-379 396-415 428-447 N term out Sosui http://www.genome.adjp/SOSui/ 6TM, aa 206-228, 255 277, 304-325, 3S9-3 8 1, 393-415, 428-450 ThU-LMM http://www.cbs.dtu.dk/scrvice&-TMHMyM 6T1, aa 210-232, 262 284, 304-323, 360-382, 392-414,427-449 Signal Peptide Signal P http://www.cbs.dtu.dk/servicesSigaIP/ none pl p/MW tool http://wwv.expasy.ch/tootsj pi 8.74 Molecular weight p1/MW tool http//www.expasy.ch/tools/ 52.0 kD Localization PSORT http://psortnibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT 11 http://psort.nibb.acjp/ Endoplasmic reticulum 39%, plasma membrane 34% Motifs PHam http:/www.sanger.ac.ukPfan/ no known motifs Prints http:/www.biochem.ucl.aceuk/ pyidine nucleotide reductase ProDomn http://prodes.toulouse.ra.f Dudulin, oxidoreductase Blocks http://www.blocks.hcrc.org/ adenosyl-L ho/ rocysteint hydrolase V.2 Bioinfoxnnatic LJRL Outcome Program ORE ORE finder Protein length 45 a3 Transmesnbrane region 7M Pred httpi/www.ch.embnet.oigf I TM, aa 5-23, N-term inside HMMTop httpJ/www.enzim.huthmnntopl no TM Sosui http:/www.genome.ad.jp/SOSui/ souble protein ThIHMM http:/www.cbs.dtu.dlservicj'TMHM no TM Signal Peptide Signal P httpi/www cbs diu.dklservices/Signa)P/ none p1 p1/MW tool httpi/www expasy ch/tooWs p1 4.2 Molecular weight p1/MW tool http/www.cxpasy.chltools/ 4.84 kD Localization PSORT http/psort.nibb.acjp/ Ouside 37%, microbody 32% PSORT 11 http/psortnibb.ac.jp/ Extracellular 33%, nuclear 33% Motifs Pfam http://www.sanger.ac.uk/Pfaml no known motifs Prints http:/www.biochenm.ucl.ac.uk/ no known motifs Blocks httpJ/www.blocks.fficrcorg/ no known motifs V.5 BPoinformatic mRL Outcome Program ORE ORE finder 245 Protein length 419 aa Transmembrane region TM Pred http://www.ch.embnet.org/ 4TM, aa 214-232, 261 286, 304-325, 359-379 N-term inside HMMTop http://www.enzim.hu/hmmtop/ 4TM, aa 215-232, 259 278, 305-324,360-379 N-term outside Sosui http-//www.genome.ad.jp/SOSui/ 4TM, aa 209-231, 255. 277, 304-325,356-379 TMHMM http://www.cbs.dtu.dk/scrvicesfrMHMM 4TM, aa 210-232, 262 284, 304-323, 360-382 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignaIP/ none pf pL/MW tool http:/www.expasy.ch/tools/ pI 8.1 Molecular weight p1/MW tool http-//www.expasy.ch/tools/ 47.9 kD Localization PSORT http-/psort.nibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT 11 http://psort.nibb.ac.jp/ Endoplasmic reticulum 44%, plasma membrane 22% Motifs Pfam httpJ/www.sanger.ac.uk/Pfam/ no known motifs Prints httpJ/www.biochem.ucl.ac.uk/ no known motifs ProDom http://prodes.toulouse.inraf Dudulin, oxidoreductase Blocks http://www.blocks.fhcrc.org/ no known motifs V.6 Bioinformatic URL Outcome Program ORF ORF finder Protein length 490 an Transmembrane region TM Pred http://www.ch.embnet.org/ 6TM, an 214-232, 261 N 286, 304-325,359-379, 393-415,432-455 HMMTop httpJ/www.enzim.huihmtop/ TM, aa 140-158,214 232, 259-280, 305-323, 361-383, 396-413, 432 455, N -term out Sosui http/www.genome.ad.jp/SOSui/ 6TM, aa 206-228, 255 277, 304-325, 359-381, 393-415, 428-450 TMHMM http://www.cbs.du.dk/servicesrrMHMM 6TM, an 210-232,262 284, 304-323, 360-382, 392-414, 427-449 Signal Peptide Signal P htp/www.cbs.dtu.dk/services/SignaIP/ none p1 p1/MW tool httpi/www.cxpasy.ch/tools/ p 1 9.2 Molecular weight p1/MW tool httpf/www."pasy.cb/tools/ 55.9 kD Localization PSORT httpi/psort.nibb.acjpt Plasma membrane 60%/, golgi 40% PSORT 11 http:/psoii.nibb.ac.jp/ Endoplasmic reticulum 39%, plasma membrane 34% Motifs Pfam http/www.sanger.ac.uk/PfanV no known motifs Prints httpJ/www.biochen.uci.ac.uk/ pyridine nucleotide reductase ProDom http//prodes.toulouse-inraf Dudulin, oxidoreductase Blocks http:/www.blocks.ficre.org/ adenosyl-L, bomocysteine hydrolase 246 V.7 Bioinformatic URL Outcome Program ORF ORF finder Protein length 576 aa Transmembrane region TM Pred http://www.ch.embnet.org/ 6TM, aa 214-232, 262 280, 306-322, 331-360, 371-393, 525-544. N tern out HMMTop http://www.enzim.hu/hmmtop/ STM, aa 215-232, 261 279, 306-325, 342-359, 378-397 N -term out Sosui http://www.genome.ad.jp/SOSui/ 5 TM, aa 206-228, 255 277, 304-325, 339-360, 380-402 TMIHMM http://www.cbs.dtu.dk/scrvices IMHMM 4TM, aa 210-232, 262-284, 304-323, 343-360 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalP/ none PI pl/MW tool http://www.expasy.ch/tools/ p 1 8.5 Molecular weight p/M W tool http://www.expasy.ch/tools/ 64.5 kD Localization PSORT http://psortnibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT 11 http://psort.nibb.ac.jp/ Endoplasmic reticulum 44%, plasma membrane 22% Motifs Pfam http://www.sanger.ac.uk/Pfam/ no known motifs Prints http-J/www.biochem.ucl.ac.uk/ pyridine nucleotide reductase ProDom http://prodes.toulouse.inra.f Dudulin, oxidoreductase Blocks http://www.blocks.fhcrc.org/ Ets domain, adenosyl L-homocysteine hydrolase Table LL. Exon boundaries of transcript 98P4B6 v.1 Exon Number Start End Length 1 23 321 299 2 322 846 525 3 847 1374 528 4 1375 1539 165 5 1540 1687 148 6 1688 2453 766 Table Lil(a). Nucleotide sequence (partial, 5' open) of transcript variant 98P486 v.2 (SEQ ID NO: 153) agtggatccc ccgggctgca ggctctctct ctctctctct cttccgggtt cacgccattc 60 tcctgcctca gcctcccgag tagctqggac tacaggtgcc cgccaccatg cccggctgat 120 ttctttttgt atttttagta cagacggagt ttcaccgtgt tagccaggat ggtctcgatc 180 tcctgacctc gtgatccgcC cgccttggcc tccaaagtgc tgggattaca ggtgtgagct 240 accgcgcccg gcctattatc ttgtactttc taactgagcc ctctattttc tttattttaa 300 taatatttct ccccacttga gaatcacttg ttagttcttg gtaggaattc agttgggcaa 360 tgataacttt tatgggcaaa aacattctat tatagtgaac aaatgaaaat aacagcgtat 420 tttcaatatt ttcttattcc ttaaattcca ctcttttaac actatgctta accacttaat 480 gtgatgaaat attcctaaaa gttaaatgac tattaaagca tatattgttg catgtatata 540 ttaagtagcc gatactctaa ataaaaatac cactgttaca gataaatggg gcctttaaaa 600 atatgaaaaa caaacttgtg aaaatgtata aaagatgcat ctgttgtttc aaatggcact 660 atcttctttt cagtactaca aaaacagaat aattttgaag ttttagaata aatgtaatat 720 atttactata attctaaatg tttaaatgct tttctaaaaa tgcaaaacta tgatgtttag 780 ttgctttatt ttacctctat gtgattattt ttcttaattg ttatttttta taatcattat 840 247 ttttctgaac cattcttctg gcctcagaag taggactgaa ttctactatt gctaggtgtg 900 agaaagtggt ggtgagaacc ttagagcagt ggagatttgc tacctggtct gtgttttgag 960 aagtgcccct tagaaagtta aaagaatgta gaaaagatac tcagtcttaa tcctatgcaa 1020 aaaaaaaatc aagtaattgt tttcctatga ggaaaataac catgagctgt atcatgctac 1080 ttagctttta tgtaaatatt tcttatgtct cctctattaa gagtatttaa aatcatattt 1140 aaatatgaat ctattcatgc taacattatt tttcaaaaca tacatggaaa tttagcccag 1200 attgtctaca tataaggttt ttatttgaat tqtaaaatat ttaaaagtat gaataaaata 1260 tatttatagg tatttatcag agatgattat tttgtgctac atacaggtg gctaatgagc 1320 tctagtgtta aactacctga ttaatttctt ataaagcagc ataaccttgg cttgattaag 1380 gaattctact ttcaaaaatt aatctgataa tagtaacaag gtatattata cttcattac 1440 aatcaaatta tagaaattac ttgtgtaaaa gggcttcaag aatatatcca atttttaaat 1500 attttaatat atctcctatc tgataactta attcttctaa attaccactt gccattaagc 1560 tatttcataa taaattctgt acaqtttccc ccaaaaaaag agatttattt atgaaatatt 1620 taaagtttct aatgtggtat tttaaataaa gtatcataaa tgtaataagt aaatatttat 1680 ttaggaatac tgtgaacact gaactaatta ttcctgtgtc agtctatgaa atccctgttt 1740 tgaaataagt aaacagccta aaatgtgttg aaattatttt gtaaatccat gacttaaaac 1800 aagatacata catagtataa cacacctcac agtgttaaga tttatattgt qaaatgagac 1860 accctacctt caattgttca tcagtgggta aaacaaattc tgatgtacat tcaggacaaa 1920 tgattagccc taaatgaaac tgtaataatt tcagtggaaa ctcaatctgt ttttaccttt 1980 aaacagtgaa ttttacatga atgaatgggt tcttcacttt ttttttaqta tgagaaaatt 2040 atacagtgct taattttcag agattctttc catatgttac taaaaaatgt tttgttcagc 2100 ctaacatact gagttttttt taactttcta aattattgaa tttccatcat gcattcatcc 2160 aaaattaagg cagactgttt ggattcttcc agtccaga tgagctaaat taaatcacaa 2220 aagcagatgc ttttgtatga tctccaaatt gccaacttta aggaaatatt ctcttgaaat 2280 tgtctttaaa gatcttttgc agatttgcag atacccagac tgagctggaa ctggaatttg 2340 tcttcctatt gactctactt ctttaaaagcggctgccat tacattcctc agcgtcctt 2400 gcagttaggt gtacatgtga ctgagtgttg gccagtgaga tgaagtctcc tcaaaggaag 2460 gcagcatgtg tcctttttca tcccttcatc ttgctgctgg gattgtggat ataacaggag 2520 ccctggcagc tgtctccaga gqatcaaa c cacacccaaa gagtaaggca gattagagac 2580 cagaaagacc ttgactactt ccctacttcc actgcttttt cctgcattta agccattgta 2640 aatctgggtg tgttacatga agtgaaaatt aattctttct gcccttcagt tctttatcct 2700 gataccatti aacactgtct gaattaacta gactgcaata attctttctt ttgaaagctt 2760 ttaaaggata atgtgcaatt cacattaaaa ttgattttcc attgtcaatt agttatactc 2820 attttcctgc cttgatcttt cattagatat tttgtatctg cttggaatat attatttct 2880 ttttaactgt gtaattggta attactaaaa ctctgtaatc tccaaaatat tgctatcaaa 2940 ttacacacca tgttttctat cattctcata gatctgcctt ataaacattt aaataaaaag 3000 tactatttaa* tgatttaaaa aaaaaaaaaa aaaaaaaaaa a 3041 Table 1-111(a). Nucleotide sequence alignment of 98P486 v.1 (SEQ ID NO: 154) and 98P4136 v.2'(SEQ ID NO: 155) Score = 1429 bits (743), Expect = 0.0ldentities = 7501751 (99%), Gaps =11751 (0%) Strand = Plus / Pius V.: 1687 ga4ctttt6 V. 2: 2291 gacttcgttcgtccgctacgacgattttctt 2350 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagcttccttgcagttaggt 1806 V.2: 2351 gactctacttctttaaaagcggctgcccattacattcctcagcttccttgcagttaggt 2410 V.1: 1807 gtacatgtgactgaqtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgg 1866 V.2: 2411 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaagcagcatgtg 2470 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggaccctggcagc 1926 V.2: 2471 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagcctgcagc 2530 V.t: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagaacagaagacc 1986 Vt2: 2531 taggaca 2590 V.1: 1987 ttgactacttccctacttccactgctttt-cctcatttaagccattgtaaatcgggtg 2045 248 V.2: 2591 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 2650 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 i lil ||i ll i1111||||| 1|||||||i||111|1||||||11||1||||||||||11 |1111 V.2: 2651 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2710 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 V.2: 2711 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2770 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2225 V.2: 2771 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2830 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 V.2: 2831 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2890 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2345 IIl il I l l l il l lillillli li ~i~ l l l li l lI 11i1111111 i l i il i lllil l1ii ll V.2: 2891 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2950 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 l illlllllllillllllllllllllllllilllll fil 1 111 1 ill1i111l1 l i1111 11 11 i11 li ii 11l111 i| V.2: 2951 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 3010 V.1: 2406 tgatttaaaaaaaaaaaaaaaaaaaaaaaaa 2436 l|i|iiII||| iI|||| l l i| l| l iii V.2: 3011 tgatttaaaaaaaaaaaaaaaaaaaaaaaaa 3041 NOTE: THERE WAS A SINGLE NUCLEOTIDE INSERTION OF A SINGLE BASE AT 2620 OF V.2. Table LIV(a). Peptide sequences (partial) of protein coded by 98P486 v.2 (SEQ ID NO: 156) SGSPGLQALS LSLSSGFTPF SCLSLPSSWD YRCPPPCPAD FFLYF 45 Table LV(a). Amino acid sequence alignment of 98P4B6 v.1 and 98P4B6 v.2 -NO SIGNIFICANT HOMOLOGY Table Ui(b). Nucleotide sequence of transcript variant 98P4B6 v.3 (SEQ ID NO: 157) ttctgctata gagatggaac agtatatgga aagctcccaa gaaagtgaag agaggaaatt 60 ggaaaattgt gagtggacct tctgatactg ctcctccttg cgtggaaaag gggaaagaac 120 tgcatgcata ttattcagcg tcctatattc aaaggatatt cttggtgatc ttggaagtgt 180 ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg aaacttgttt 240 acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg tgattggaag 300 tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc atgtggtcat 360 aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag atgtcactca 420 tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca gagaacatta 480 tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg atgtgagcaa 540 taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt cattattccc 600 agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc agttaggacc 660 taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc gacaacaggt 720 tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct tatcatcagc 780 249 cagagagatt gaaaatttac ccctacgact Ctttactctc tggagagggc cagtggtggt 840 agctataagc ttggccacat tttttttcct ttattccttt gtcagaqatg tgattcatcc 900 atatgctaga aaccaacaga gtgactttta caaaattcct ataqagattg tgaataaaac 960 cttacctata gttgccatta Ctttqctctc cctagtatac cttqcaggtc ttctggcagc 1020 tgcttatcaa ctttattacq gcaccaagta taggaqattt ccaccttggt tggaaacctg 1080 gttacagtgt agaaaacagc ttggattact aaqttttttc ttcgctatgg tccatgttgc 1140 ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca acatggctta 1200 tcagcaggtt catgcaaata ttgaaaactc ttqgaatgag gaagaagttt ggagaattga 1260 aatgtatatc tcctttggca taatgagcct tggcttactt tccctcctgg cagtCacttc 1320 tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc agtctacact 1380 tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat ggaaacgagc 1440 ttttgaggaa gagtactaca gattttatac accaccaaac tttgttcttg ctcttgtttt 1500 gccctcaatt gtaattctgg atcttttgca gctttgcaga tacccagact qctqqaac 1560 tggaatttgt cttcctattg actctacttc tttaaaagog gctgcccatt acattcctca 1620 gctgtccttg cagttaggtg tacatqtgac tgagtgttqg ccagtgagat gaagtctcct 1680 caaaggaagg cagcatgtgt cctttttcat cccttcatct tgctgctggg attgtggata 1740 taacaggagc cctggcagct gtctccagag gatcaaagcc acacccaaag agtaagqcag 1800 attagagac.c agaaagacct tgactacttc cctacttcca ctgctttttc ctgcatttaa 1860 gccattgtaa atctgggtgt gttacatgaa gtgaaaatta attctttctg cccttcagtt 1920 ctttatcctg ataccattta acactgtctg aattaactag actgcaataa ttctttcttt 1980 t-aaagcttt taaaggataa tgtgcaattc acattaaaat tgattttcca ttgtcaatta 2040 gttatactca ttttcctgcc ttgatctttc attagatatt ttgtatctgc ttggaatata 2100 ttatcttctt tttaactgtg taattqgtaa ttactaaaac tctgtaatct ccaaaatatt 2160 gctatcaaat tacacaccat gttttctatc attctcatag atctgcctta taaacattta 2220 aataaaaagt actatttaat gatttaactt ctgttttgaa aaaaaaaaaa aaaaaaaaaa 2280 Table 1-111(b). Nucleotide sequence alignment of 98P4136 v.1 (SEQ ID NO: 158) and 98P4136 v.3 (SEQ ID NO: 159) Score = 4013 bits (2087), Expect =0.Oldentities =211612128 (99%), Gaps = 1/2128 (0%) Strand =Plus I Plus V.1: 320 aggatattcttgqtqatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 V.3: 153 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 212 V.1: 380 cct gtata39 V.3: 213 gccctaagagccttagtgaaacttgtttacctaatggcataaatgtatcagatgcaa 272 V.1: 440 ggaaggtcactgtaggtgtgattqgaagtggagattttgccaaatccttgccattcgac 499 V.3: 273 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 332 V-1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctagtttgcttctgctt 559 V.3: 333 ttattagatgcggctatatgtggtcataqgaagtagaaatccttcgtttgcttctgaat 392 V.1: 560 t619ccatga V.3: 393 tttctaggtgttatacagaagttaaaaaaaa 452 Vg1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 V.3: 453 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacgtctgattg 512 Vg1: 680 9gacaaag 250 V.3: 513 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 572 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 ||1 |||1 ||||||||||1 |||1 |11 ||||||||lf |||||i ||||||||||11 |1|1 ||1 V.3: 573 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 632 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 |||||||||||||||||||||||||||||||||||||||||||||1||||1|,|||1||1 V.3: 633 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 692 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 |||1 ||||1 |1 |1f |||1 |||||||||ff |||11 1|||ff11ff || fil| fil11||||1|| V.3: 693 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 752 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 V.3: 753 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 812 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 V.3: 813 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 872 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 V.3: 873 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 932 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 V.3: 933 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 992 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 V.3: 993 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1052 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 V.3: 1053 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1112 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 V.3: 1113 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1172 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 V.3: 1173 Egagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1232 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 V.3: 1233 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1292 251 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 1i1l111l11ll11111 lfill lli111ll t || 1|| 1|| 11|1||||| 1||||||||l|| V.3: 1293 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1352 V.1: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 111ll I IlI llifiilllllf f f lli i||||| lii|||1|||||||||||11 || V.3: 1353 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1412 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 V.3: 1413 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1472 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1699 Ilf II I lll ll I lill fIl lifil lill I|||I||||||||I|||||||I !|||| V.3: 1473 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1532 V.1- '700 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1759 V.3: 1533 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1592 V.1: 1760 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1819 V.3: 1593 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1652 V.1: 1820 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1879 lillf Ill ll 11lll 11l1l 1f1l 11111111|||||| 1l|||| h||1||||||11 |||| V.3: 1653 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1712 V.1: 1880 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1939 V.3: 1713 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1772 V.1: 1940 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1999 V.3: 1773 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1832 V.1: 2000 tacttccactgctttt-cctgcatttaagccattgtaaatctgggtgtgttacatgaagt 2058 V.3: 1833 tacttccactgctttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagt 1892 V.1: 2059 gaaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaa 2118 V.3: 1893 gaaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaa 1952 V.1: 2119 ttaactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcac 2178 V.3: 1953 ttaactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcac 2012 V.1: 2179 attaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcat 2238 V.3: 2013 attaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcat 2072 252 V.1: 2239 tagatattttgtatctgettggaatatattatcttctttttaactgtgtaattggtaatt 2298 li1111111l1ll1l1111l111lIII illiii||lii,,, l1111111111j11111111 V.3: 2073 tagatattttgtatctgcttggaatatattatettctttttaactgtgtaattggtaatt 2132 V.1: 2299 actaaaactetgtaatctccaaaatattgctatcaaattacacaccatgttttctatcat 2358 V.3: 2133 actaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcat 2192 V. 1: 2359 tctcatagatctgccttataaacatttaaataaaaagtactatttaatgatttaaaaaaa 2418 |I lllil i||||l||l lil lIl lI 11111 111||111. 11111111Ii ll I I| V.3: 2193 tctcatagatctgccttataaacatttaaataaaaagtactatttaatgatttaacttet 2252 V.1: 2419.aaaaaaaaaaaaaaaaaaaaaaaaaaaa 2446 11lllllli IiliiilI| Jllli V.3: 2253 gttttgaaaaaaaaaaaaaaaaaaaaaa 2280 NOTE: AN INSERTION OF A SINGLE BASE AT 1845 OF V.3 Table LV(b). Peptide sequences of protein coded by 98P4B6 v.3 (SEQ ID NO: 160) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ.VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD 454 Table LV(b). Amino acid sequence alignment of 98P4136 v.1 (SEQ ID NO: 161) and 98P4136 v.3 (PEQ ID NO: 162) Score = 910 bits (2351), Expect =O.Oldentities. 4541454 (100%), Positives =454/454 (100%) V.1: I MESISMMGSPKSLSETCLPNGINGIKD11J/TVGVIGSGDFAKSLTIRLIRCGYHIGS 60 MESISMMGSPKSLSETCLPNGINGIKDRKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.3: 1 MESISMMGSPKSLSETCLPNGINGIKDARKiJTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVDVTHHEDALTKTNIIFAIHREHYTSLWDLRLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNI IFVAI HREHYTSLWDLRHLLVGKI LIDVSNNM V.3: 61 RNKAEFHVVREATTIEVIRRTLDRLVKLDSN 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWAJLQLGPKDASRQVYICSNNIQARQQVI E V.3: 121 RINQYPESNAEYLASLFPDSLIVKGFNiJVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 FVRDVIHPYA 240 LARQLNFIPI1DLGSLSSAREI ENLPLRLFTLWRGPVVVAISLATFFFLYS FVRDVIIIPYA V.3: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVJVJ1AISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKI PIEIVNKTLPIVAITLLSLVYLAGLLMAYQLYYGTKYRFPPWLETWLQ V.3: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLAAYQLYYGTKYRRFPPWLETWLQ 300 V. 1: 301 CRKQLGLLsFFFAENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLLNAYQQVANI ENSWNEEEVWRT EMY V.3: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNAYQQVANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWRFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIGSTLGYVALLISTFHVLIYGWKRAFE 253 V. 3: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V..: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 EEYYRFYTPPNFVLALVLPSIVILDLLOLCRYPD V.3: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 Table Ul(c). Nucleotide sequence of transcript variant 98P4B6 v.4 (SEQ ID NO: 163) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc ggcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgcgcctc 120 cctccttcct tctcccctgg ctgttcgcga tccagcttgg gtaggcgggg aagcagctgg 180 agtgcgaccg ccacggcagc caccctgcaa ccgccagtcg gagagctaag ggcaagtcct 240 gaggttgggc ccaggagaaa gaaggcaagg agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc 480 atgtggtcat aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattr- agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactctc tggagagggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 ttctggcagc tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg 1260 tccatgttgc ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatgtatatc tcctttggca taatgagcct tggcttactt tccctcctgg 1440 cagtcacttc tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agtctacact tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat 1560 ggaaacgagc ttttgaggaa gagtactaca gattttatac accaccaaac tttgtticttg 1620 ctcttgtttt gccctcaatt gtaattctgg atcttttgca gctttgcaga tacccagact 1680 gagctggaac tggaatttgt cttcctattg actctacttc tttaaaagcg gctgcccatt 1740 acattcctca gctgtccttg cagttaggtg tacatgtgac tgagtgttgg ccagtgagat 1800 gaagtctcct caaaggaagg cagcatgtgt cctttttcat cccttcatct tgctgctggg 1860 attgtggata taacaggagc cctggcagct gtctccagag gatcaaagcc acacccaaag 1920 agtaaggcag attagagacc agaaagacct tgactacttc cctacttcca ctgcttttcc 1980 tgcatttaag ccattgtaaa tctgggtgtg ttacatgaag tgaaaattaa ttctttctgc 2040 ccttcagttc tttatcctga taccatttaa cactgtctga attaactaga ctgcaataat 2100 tctttctttt gaaagctttt aaaggataat gtgcaattca cattaaaatt gattttccat 2160 tgtcaattag ttatactcat tttcctgcct tgatctttca ttagatattt tgtatctgct 2220 tggaatatat .tatcttcttt ttaactgtgt aattggtaat tactaaaact ctgtaatctc 2280 caaaatattg ctatcaaatt acacaccatg ttttctatca ttctcataga tctgccttat 2340 aaacatttaa ataaaaagta ctatttaatg attt 2374 Table 1.111(c). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 164) and 98P486 v.4 (SEQ ID NO: 165) Score = 404 bits (210), Expect =e-1091denfities = 210/210 (100%) Strand =Plus / Plus V. 1: 1 ggacgcgtgggcggacgcgtggqttcctcgggccctcggcgccacaagctgtccgggcac 60 V. 4: 14 ggacgcgtgggcggacgcqtgggttcctcgggccctcggcgccacaagctgt 0 ccgggcac 73 V.1: 61 g 120 V.4: 74 gcgccacgggccgcaccgccgqgcccctctc 133 254 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 111i1l11111111l111l1111l11l1111||1||||||11| l|i|||||11|11111|1 V.4: 134 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 193 V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 lillill ill If ffll1ill1ll ill I lI V.4: 194 cggcagccaccctgcaaccgccagtcggag 223 Score = 4022 bits (2092), Expect = 0.Oldentities = 2092/2092 (100%) Strand = Plus / Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 V.4: 283 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 342 V.1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 -1|||||1||||11|||||||1||||1||||||||||11||||||1||1|||||ff111111 V.4: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 V.4: 403 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 V.4: 463 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 522 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgetctcacaaaaacaaatataa 619 V.4: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgetctcacaaaaacaaatataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 V.4: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 1111111111|11111|1|1|111111ff|1||1||||1||||11||1||1|||1|1|111 V-4: 643 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 |||||||||11111|||11|||1|||1||11|1|1||1||1111||f|1|||111|11 V.4: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 .V.4: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 V.4: 823 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 255 V.4: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 V.4: 943 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 V.4: 1003 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 |||||l|||||||||||||||1|||1||||1|1||||||||||11 l l 11||||||||||1| V.4: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 V.4: 1123 tagtataccttgcaggtcttctggcagctgctt- -aactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 l|t||||||||1||ll|l|l||||||||||||l||||||-lll|||||||||liIIl l || V.4: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaag gcag 1339 ||||||||||||||11||||1|1|||||||11||||1|||11|||||11|||11|111|| V.4: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 V.4: 1303 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1362 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 11|1||11|||11|1|| lii 11||1||11|11| |1 ||l | ||11 ||||||1 1 |11 |111 V.4: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 V.4: 1423 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1482 V.1: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 V.4: 1483 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1542 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 ||||i|l|||||liii lI||||11||||111|||||1||||11||1|1||1||||||||1|| V.4: 1543 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1602 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1699 |I|||||li l Illl lili lli111 li||i||||1|111|1||1||||||||11|| V.4: 1603 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1662 256 V.1: 1700 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1759 V.4: 1663 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1722 V.1: 1760 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1819 I!li ii l 11111ll l t l illl ill 11||||1||1|1||||||1||||11|||lii| V.4: 1723 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1782 V.1: 1820 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1879 V.4: 17,83 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1842 V.1: 1880 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1939 V.4: 1843 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1902 V.1: 1940 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1999 lilt lilllll111lllillii i lII l II||||||| l||| |||i||||1 |1 ||111|1 V.4: 1903 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1962 V.1: 2000 tacttccactgcttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagtg 2059 V.4: 1963 tacttccactgcttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagtg 2022 V.1: 2060 aaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtetgaat 2119 11l1il11l1|||1|I1111ll11l1l11l1l11|||||111|1||||11|||1|1|||1 V.4: 2023 aaaattaattctttctgcccttcagttctttatcctgataccatttaacactgttgaat 2082 V.1: 2120 taactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcaca 2179 V.4: 2083 taactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcaca 2142 V.1: 2180 ttaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcatt 2239 V.4: 2143 ttaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcatt 2202 V.1: 2240 agatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatta 2299 V.4: 2203 agatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatta 2262 V.1: 2300 ctaaaactctgtaatctccaaaatattgetatcaaattacacaccatgttttctatcatt 2359 lill111l1l111l1|||1||||1| |||||ll||l |1111 ||1! ||11 ||111 I*I1|||11 V.4: 2263 ctaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcatt 2322 V.1: 2360 ctcatagatctgccttataaacatttaaataaaaagtactatttaatgattt 2411 V.4: 2323 ctcatagatctgccttataaacatttaaataaaaagtactatttaatgattt 2374 Table LIV(c). Peptide sequences of protein coded by 98P4B6 v.4 (SEQ ID NO: 166) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 257 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD 454 Table LV(c). Amino acid sequence alignment of 98P486 v.1 (SEQ ID NO: 167) and 98P486 v.4 (SEQ ID NO: 168) Score = 910 bits (2351), Expect = 0.01dentities = 4541454 (100%), Positives = 454/454 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDEAKSLTIRLIRCGYHVVIGS V.4: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.4: 61 .RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGP: ..SRQVYICSNNIQARQQVIE V.4: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIN 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.4: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.4: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY V.4: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE V.4: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD V.4: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 Table Ul(d). Nucleotide sequence of transcript variant 98P486 v.5 (SEQ ID NO: 169) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc gcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgcgcctc 120 cctccttcct tctcccctgq ctqttcgcga tccagcttgg gtaggcgggg aagcaqctgg 180 agtgcgaccg ctacgqcagc caccctgcaa ccgccagtcg gagagctaag gqcaaqtcct 240 gaggttqggc ccaggagaaa gaaggcaagq agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatqatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaqa tgcggctatc 480 atgtggtcat agqaagtaqa aatcctaagt ttgcttctga attttttcct catgtqgtaq 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgaqq ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattccc agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatqcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaactt gcccgccagt tgaatttcat tcccattgac ttggqatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactttc tgqagaggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 258 ttctggcagc tgcttatcaa ctttattacg qcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc tggattact aagttttttc ttcgctatgq 1260 tccatgttgc ctacagcctc tgcttaccga tgaqaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatgtatatc tcctttggca taatagcct tggcttactt tccctcctqq 1440 cagtcacttc tatcccttcg gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agatcttttg cagctttgca gatacocaga ctgagctgga actggaattt gtcttcctat 1560 tgactctact tctttaaaag cggctgccca ttacattcct cagctgtcct tgcagttagg 1620 tgtacatgtg actgagtgtt ggccagtgag atgaagtctc ctcaaaggaa ggcagcatgt 1680 gtcctttttc atcccttcat cttgctcctq ggattgtgqa tataacaqqa gccctggcag 1740 ctgctccaga ggatcaaagc cacacccaaa gaqtaaqqca gattagagac caqaaagacc 1800 ttgactactt ccctacttcc actgcttttt cctgcattta agccattgta aatctgggtg 1860 tgttacatga agtgaaaatt aattctttct gcccttcagt tctttatcct gataccattt 1920 aacactgtct gaattaacta gactgcaata attctttctt ttgaaagctt ttaaaggata 1980 atgtgcaatt cacattaaaa ttgattttcc attgtcaatt agttatactc attttcctgc 2040 cttgatcttt cattagatat tttgtatctg cttggaatat attatctct ttttaactgt 2100 gtaattggta attactaaaa ctctgtaatc tccaaaatat tgctatcaaa ttacacacca 2160 tgttttcta t cattctcata gatctgcctt ataaacattt aaataaaaaq tactatttac 2220 caaaaaaaaa aaaaaaaaaa aaaaaaaaa 2249 Table 1.111(d). Nucleotide sequence alignment of 98P4B6 Y.1 (SEQ ID NO: 170) and 98P4B36 v.5 (SEQ ID NO: 171) Score = 398 bits (207), Expect =e- 1071denties =209/210 (99%) Strand =Plus / Plus V.t1: 1 60cc tggcaatgagccttggetac V. 5: 14 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccggcac 73 V.1: 61 tcgga 120 V.c5: 74 gtggc 133 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 V.5: 134 193cacct V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 V.5: 194 cggcagccaccctgcaaccgccagtcggag 223 Score 2334 bits (1214), Expect =0.0Identi~es = 1218/1220 (99%) Strand =Plus I Plus V.t1: 320 379cttggaa tatcattatcct V.5: 283 2tctatcaa V.1: 380 gccaggctggactttccatgaaagttaaaga 439 V.5: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcga 499 V.5: 403 ggaaggtcactgtaggtgtgattggaagtgagattttqccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgctttg 16 559 V.5: 463 522 259 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 V.5: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaastataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 tl i ll ||||||||| 1||||||||||||| 1|| 1|||||| 1 ! i l l till||| i|| ||lt V.5: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 V.5: 643 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 V.5: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 V.5: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 |ti||l||||||||IiitilI|||||||||ii||||t|1i11 ||ii||111|||||||1|| V.5: 823 gcaacaatattcaagcgcgacaacaggttattgaaettgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 ||l||1|11||1|||111||1||1||1|||1111|1|1| til 1|1|||||||1||||1|| V.5: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagettggccacattttttttccttt 1039 V.5: 943 ttactttctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 V.5: 1003 atteetttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 V.5: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 V.5: 1123 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 V.5: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagettggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 260 V.5: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 |||||||||||||||||||||||11|||||1||||||||||||||||||||1|||||||| V.5: 1303 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1362 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 li1llllllllllllillll11l11111liii 1111l1ll1l11li11l1li1l V.5: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 |111||1||||||||111|||1|tilt 11111|1|1| |||||||||||||||||1|1|| V.5: 1423 gcttactttccctcctggcagtcacttctatcccttcggtgagcaatgctttaaactgga 1482 V.1: 1520 gagaattcagttttattcag 1539 V.5: 1483 gagaattcagttttattcag 1502 Score 1375 bits (715), Expect = 0.Oldentities = 741/749 (98%), Gaps = 2/749 (0%) Strand = Plus / Plus V.1: 1687 gatettttgcagctttgcagatacccagactgagetggaactggaatttgtettcctatt 1746 V.5: 1502 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1561 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1806 V.5: 1562 gactctacttctttaaaagcggctgcccattacattcctcagctgtcttgcagttaggt 1621 V.1: 1807 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggscagcatgtg 1866 lilIll11l11l1l11111ll11l1111l111|111||||11|||1111|11||1||11 il V.5: 1622 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1681 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1926 V.5: 1682 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1741 V.1: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1986 V.5: 1742 tg-ctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1800 V.1: 1987 ttgactacttccctacttccactgctttt-cctgcatttaagccattgtaaatctgggtg 2045 V.5: 1801 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 1860 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 |||||111||1|1|| 1|1||||| 11| | I| liii| till |||| 1111111111111iiji V.5: 1861 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 1920 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 ||||||||||||1 ||||||||||||||||||||||||||1111,11|11 ii Ill jil I V.5: 1921 aacactgtctgaattaactagactgcaataattctttcttttgaaagctttaaaggata 1980 261 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctge 2225 ||||||||1 |1 I llI l 1I1 |I I i l |||||I l 1I l l 1111| Il lilii I V.5: 1981 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2040 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 11I||||||||il |||111 1 l1111111 |11lli||1 1 l1111111| 11| 1 V.5: 2041 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2100 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatattgetatcaaattacacacca 2345 ||||11||||||||||111l11 1111i I t|| |1|| | |1 ||||11 1 I I l~il11IlIl| V.5: 2101 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2160 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 V.5: 2161 tgttttctatcattetcatagatctgccttataaacatttaaataaaaagtactatttac 2220 V.1: 2406 tgatttaaaaaaaaaaaaaaaaaaaaaaa 2434 V.5: 2221 caaaaaaaaaaaaaaaaaaaaaaaaaaaa 2249 NOTE: A SNP AT 192 AND AT 1510, A DELETION AT 1742-1743, AND AN INSERTION OF SINGLE BASE AT 1830 OF V.5. Table UV(d). Peptide sequences of protein coded by 98P4B6 v.5 (SEQ ID NO: 172) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT FWRGPVVVAI SLATFPFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLKTWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQIFCSF ADTQTELELE FVFLLTLLL 419 Table LV(d). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 173) and 98P4B6 v.5 (SEQ ID NO: 174) Score = 788 bits (2036), Expect = 0.01dentities = 394/395 (99%), Positives = 394/395 (99%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKTVGVIGSGDFAKSLTIIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.5: 1 MESISMMGSPKSLSETCLPNGINGIKDAR(XTVGVIGSGDFAKSITIRLIRCGYUWVIGS 60 V. 1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIEIAIHRHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKPNII FVAIHREIIYTSLWDLRHLLVGKILIDVSNNM V.5: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVI E V.5: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWAQLGPKDASRQVYICSNNIQARQQVIE 180 V.V1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVAISLATFFFLYSFRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFT WRGPVVVAISLATFFFLYSFVRDVIHPYA V.5: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTFWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V. 1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYAGLLYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKI PIEIVNKTLPIVAITLLSLVYLAGLLAJ1JYQLYYGTKYRRFPPWLETWLQ V.5: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLJAGLLIJAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFA 360 CRKQLGLLSSFFFAMVHVAYSLCLPMRRSERYLFLNADYQQVHANIENSWNEEERIEMY 262 V.5: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ 395 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ V.5: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ 395 NOTE: A SNP CAUSED A SINGEL AMINO ACID DIFFERENCE AT 211. Table LII(e). Nucleotide sequence of transcript variant 98P486 v.6 (SEQ ID NO: 175) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc ggcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgcgcctc 120 cctccttcct tctcccctgg ctgttcgcga tccagcttgg gtaggcgggg aagcagctgg 180 agtgcgaccg ccacggcagc caccctgcaa ccgccagtcg gagagctaag ggcaagtcct 240 gaggttgggc ccaggagaaa gaaggcaagg agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc 480 atgtggtcat aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattccc agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactctc tggagagggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 ttctggcagc tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg 1260 tccatgttgc ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatgtatatc tcctttggca taatgagcct tggcttactt tbcctcctgg 1440 cagtcacttc tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agtctacact tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat 1560 ggaaacgagc ttttgaggaa gagtactaca gattttatac accaccaaac tttgttcttg 1620 ctcttgtttt gccctcaatt gtaattctgg gtaagattat tttattcctt ccatgtataa 1680 gccgaaagct aaaacgaatt aaaaaaggct gggaaaagag ccaatttctg gaagaaggta 1740 ttggaggaac aattcctcat gtctccccgg agagggtcac agtaatgtga tgataaatgg 1800 tgttcacagc tgccatataa agttctactc atgccattat ttttatgact tctacgttca 1860 gttacaagta tgctgtcaaa ttatcgtggg ttgaaacttg ttaaatgaga tttcaactga 1920 cttagtgata gagttttctt caagttaatt ttcacaaatg tcatgtttgc caatatgaat 1980 ttttctagtc aacatattat tgtaatttag gtatgttttg ttttgttttg cacaactgta 2040 accctgttgt tactttatat ttcataatca gacaaaaata cttacagtta ataatataga 2100 tataatgtta aaaacaattt gcaaaccagc agaattttaa gcttttaaaa taattcaatg 2160 gatatacatt tttttctgaa gattaagatt ttaattattc aacttaaaaa gtagaaatgc 2220 attattatac atttttttaa gaaaggacac gttatgttag catctaggta aggctgcatg 2280 atagcattcc tatatttctc tcataaaata ggatttgaag gatgaaatta attgtatgaa 2340 gcaatgtgat tatatgaaga gacacaaatt aaaaagacaa attaaacctg aaattatatt 2400 taaaatatat ttgagacatg aaatacatac tgataataca tacctcatga aagattttat 2460 tctttattgt gttacagagc agtttcattt tcatattaat atactgatca ggaagaggat 2520 tcagtaacat ttggcttcca aaactgctat ctctaatacg gtaccaatcc taggaactgt 2580 atactagttc ctacttagaa caaaagtatc aagtttgcac acaagtaatc tgccagctga 2640 cctttgtcgc accttaacca gtcaccactt gctatggtat aggattatac tgatgttctt 2700 tgagggattc tgatgtgcta ggcatggttc taagtacttt acttgtatta tcccatttaa 2760 tacttagaac aaccccgtga gataagtagt tattatcctc attttacaca tgagggaccg 2820 aaggatagaa aagttatttt tcaaaggtct tgcagttaat aaatggcaga gtgagcattc 2880 aagtccaggt agtcatattc cagaggccac ggttttaacc actaggctct agagctcccg 2940 ccgcgcccct atgcattatg ttcacaatgc caatctagat gcttcctctt ttgtataaag 3000 tcactgacat tctttagagt gggttgggtg catccaaaaa tgtataaaaa tattattata 3060 ataaacttat tactgcttgt agggtaattc acagttactt accctattct tgcttggaac 3120 atgagcctgg agacccatgg cagtccatat gcctccctat gcagtgaagg gccctagcag 3180 263 tgttaacaaa ttgctgagat cccacggagt ctttcaaaaa tctctgtaga gttagtcttc 3240 tccttttctc ttcctgagaa gttctcctgc ctgcataacc attcattagg gagtacttta 3300 caagcatgaa ggatattagg gtaagtggct aattataaat ctactctaga gacatataat 3360 catacagatt attcataaaa tttttcagtg ctgtccttcc acatttaatt gcattttgct 3420 caaactgtag aatgccctac attcccccca ccccaatttg ctatttcctt attaaaatag 3480 aaaattatag gcaagataca attatatgcg ttcctcttcc tgaaattata acatttctaa 3540 acttacccac gtagggacta ctgaatccaa ctgccaacaa taaaaagact tttatttagt 3600 agaggctacc tttcccccca gtgactcttt ttctacaact gccttgtcag tttggtaatt 3660 cacttatgat tttctaatgt tctcttggtg aattttatta tcttggaccc tctttttttt 3720 tttttttaaa gacagagtct tgctctgtca ccca 3754 Table Lill(e). Nucleotide sequence alignment of 98P486 v.1 (SEQ ID NO: 176) and 98P486 v.6 (SEQ ID NO: 177) Score = 404 bits (210), Expect = e-1091dentities = 210/210 (100%) Strand = Plus / Plus V.1: 1 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 60 11l1111l1111lfill 11111111111111lllliiilitllill llilllillI (ii V.6: 14 .ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 73 V.1: 61 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctc :ccttct 120 1||11fl l11111111111111111111 1 1111i|11lil ll li lii il|||||||| V.6: 74 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 133 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 lili lli li i Ifiiiifilliliilii liiill llllili ll ll1111111 V.6: 134 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 193 V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 iil li ll llii li11 iiiiii 111ll V.6: 194 cggcagccaccctgcaaccgccagtcggag 223 Score = 2630 bits (1368), Expect = 0.0ldentities = 1368/1368 (100%) Strand = Plus / Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 Il I 1111i11111111111111111il l 111llll1)illll 11111111111111 V.6: 283 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 342 V.1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 V.6: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 V.6: 403 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 1illill llillllllfilllillllflllllllluflfllllilfllljlllllf V.6: 463 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 522 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 111l11l ff111111111l1111 Ilfill 11111ll11l1liliilfilllii ll ill iil V.6: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 264 V.6: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 V.6: 643 tgggtaaaatectgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 |||||||||||||||||1||11|1|1111|ll1l1lliililililillilii111li V.6: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagettgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 1 lll lll lll1ll1ll11 1ilill 111 111 1 ll I l ll 1 til ii V.6: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 V.6: 823 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 liilll11ll11l1|||||11ll1l111l11111111ll111l1illilliilli11li V.6: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 V.6: 943 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 a ttcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgcttttaca 1099 V.6: 1003 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 ||||||1||111|||||||1||||1|1||||||||||||1|||||1||1||||||1|||1 V.6: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 V.6: 1123 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 V.6: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 V.6: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 ti li lll lt 11 li l llil lllllilliij lij Iljj||11|||1 ii lii||| V.6: 1303 agagatatttgtttetcaacatggettatcagcaggttcatgcaaatattgaaaactctt 1362 265 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 V.6: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgtttaaactgga 1519 V.6: 1423 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1482 V.1: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 V.6: 1483 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1542 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 g|| I111||| ||1111 ll It i llllillll 11 1 1 1 1 1 l iii i till,|||||| l||t|i||||||||| V.6: 1543 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1602 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctgg 1687 i i || |11|||||||||t|l||I| |t||l| |i til tilt|| 111|| i| V.6: 1603 caccaaactttgttcttgctcttgttttgccctcaattgtaattctgg 1650 Table LIV(e). Peptide sequences of protein coded by 98P4B6 v.6 (SEQ ID NO: 178) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLIAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGIGPTIP 480 HVSDPERVTVM 490 Table LV(e). Amino acid sequence alignment of 98154136 v.1 (SEQ ID NO: 179) and 98P4136 v.6 (SEQ ID NO: 180) Score =888 bits (2294), Expect = 0.Oldentities =444/444 (100%), Positives = 444/444 (100%) V. 1: 1 MESISMMGSPKSLSETCLPNGINGIKDAVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGS PKSLSETCLPNGINGI KDARKVTVGVIGSGDFAKSLTI RLI RCGYHVVIGS V. 6: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHIVIGS 60 V. 1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNI IFVAIHREHYTSLWDLRHLLVGKILI DVSNNM V.6: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIPAIIREHYTSLWDLRHLLVGKILIDVSNNM 120 V. 1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V. 6: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVAISLATFFFLYSF.VRDVIHPYA 240 LARQLNFI PDLGSLSSAREIENLPLRLTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V. 6: 181 LAIRQLN FIP IDLGS LS SARE IENL PLRLFTLWRG PVWAI SLAT FFFLYS FVRDV I HPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPqLETWLQ V. 6: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGL1JAJAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRQGLFFMHASCPRSRYFNAQVAINWEEWIM 360 CRKQLGLLSFFEAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 266 V.6: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE V.6: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 EEYYRFYTPPNFVLALVLPSIVIL V.6: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 Table 111(f). Nucleotide sequence of transcript variant 98P4B6 v.7 (SEQ ID NO: 181) ggagaaaatt tacagaaacc cagagccaaa ggtgctctca ggggatcccc tgaaacattc 60 aaagccattg cggccccaga agcttgggta ggcggggaag cagctggagt gcgaccgccg 120 cggcagccac cctgcaaccg ccagtcggag gtgcagtccg taggccctgg cccccgggtg 180 ggcccttggg gagtcggcgc cgctcccggg gagctgcaag gctcgcccct gcccggcgtg 240 gagggcgcgg ggggcgcgga ggatattctt ggtgatcttg gaagtgtccg tatcatggaa 300 tcaatctcta tgatgggaag ccctaagagc cttagtgaaa cttttttacc taatggcata 360 aatggtatca aagatgcaag gaaggtcact gtaggtqtga ttggaagtgg agattttgcc 420 aaatccttga ccattcgact tattagatgc ggctatcatg tggtcatagg aagtagaaat 480 cctaagtttg cttctgaatt ttttcctcat gtggtagatg tcactcatca tgaagatgct 540 ctcacaaaaa caaatataat atttgttgct atacacagag aacattatac ctccctgtgg 600 gacctgagac atctgcttgt gggtaaaatc ctgattgatg tgagcaataa catgaggata 660 aaccagtacc cagaatccaa tgctgaatat ttggcttcat tattcccaga ttctttgatt 720 gtcaaaggat ttaatgttgt ctcagcttgg gcacttcagt taggacctaa ggatgccagc 780 cggcaggttt atatatgcag caacaatatt caagcgcgac aacaggttat tgaacttgcc 840 cgccagttga atttcattcc cattgacttg ggatccttat catcagccag agagattgaa 900 aatttacccc tacgactctt tactctctgg agagggccag tggtggtagc tataagcttg 960 gccacatttt ttttccttta ttcctttgtc agagatgtga ttcatccata tgctagaaac 1020 caacagagtg acttttacaa aattcctata gagattgtga ataaaacctt acctatagtt 1080 gccattactt tgctctccct agtatacctc gcagqtcttc tggcagctgc ttatcaactt 1140 tattacggca ccaagtatag gagatttcca ccttggttgg aaacctggtt acagtgtaga 1200 aaacagcttg gattactaag ttttttcttc gctatggtcc atgttgccta cagcctctgc 1260 ttaccgatga gaaggtcaga gagatatttg tttctcaaca tggcttatca gcagtctaca 1320 cttggatatg tcgctctgct cataagtact ttccatgttt taatttatgg atggaapcga 1380 gcttttgagg aagagtacta cagattttat acaccaccaa actttgttct tgctcttgtt 1440 ttgccctcaa ttgtaattct ggatctgtct gtggaggttc tggcttcccc agctgctgcc 1500 tggaaatgct taggtgctaa tatcctgaga ggaggattgt cagagatagt actccccata 1560 gagtggcagc aggacaggaa gatcccccca ctctccaccc cgccgccacc ggccatgtgg 1620 acagaggaag ccggggcgac cgccgaggcc caggaatccg gcatcaggaa caagtctagc 1680 agttccagtc aaatcccggt ggttggggtg gtgacggagg acgatgaggc gcaggattcc 1740 attgatcccc cagagagccc tgatcgtgcc ttaaaagccg cgaattcctg gaggaaccct 1800 gtcctgcctc acactaatgg tgtggggcca ctgtgggaat tcctgttgag gcttctcaaa 1860 tctcaggctg cgtcaggaac cctgtctctt gcgttcacat cctggagcct tggagagttc 1920 cttgggagtg ggacatggat gaagctqgaa accataattc tcagcaaact aacacaggaa 1980 cagaaatcca aacactgcat gttctcactg ataagtggga gttgaacaat gagaacacat 2040 ggacacaggg aggggaacgt cacacaccag ggcctgtcgg gggtgggagg cctagcaatt 2100 cattagaatt acctgtgaag cttttaaaat gtaaggtttg gatggaatgc tcagacccta 2160 ccttagaccc aattaagccc aca'gctttga gg 2192 Table 1111(f). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 182) and 98P4B6 v.7 (SEQ ID NO: 183) Score = 2350 bits (1222), Expect = 0.0ldentities = 1230/1234 (99%) Strand = Plus / Plus V.1: 141 agcttgggtaggcggggaagcagetggagtgcgaccgccacggcagccaccctgcaaccg 200 11il11ll1l11ll111lil1111111l1l11l111ll11ll11l lliilIlilil lii V.7: 81 agcttgggtaggcggggaagcagctggagtgcgaccgccgcggcagccaccctgcaaccg 140 V.1: 201 ccagtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgc 260 V.7: 141 ccagtcggaggtgcagtccgtaggccctggcccccgggtgggccettggggagtcggcgc 200 267 V.1: 261 cgctcccgaggagctgcaaggctcgcccctgcccggcgtggagggcgcggggggcgcgga 320 1|11|1|| |1 ||1 ||1|11 |1 1|111 |||||||11 ||||||11 |||1|11 111|||| V.7: 201 cgctcccggggagctgcaaggctcgcccctgcccggcgtggagggcgcggggggcgcgga 260 V.1: 321 ggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaag 380 V.7: 261 ggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaag 320 V.1: 381 ccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaag 440 |11111|1||1||||111||1|| ||||1111111111l1111li11llililt||illi V.7: 321 ccctaagagccttagtgaaacttttttacctaatggcataaatggtatcaaagatgcaag 380 V.1: 441 gaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgact 500 'ii 1|1||111||111|1||11|1|1| 1|||11||11|||1|||11|||1|||111|11|1 V.7: 381 gaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgact 440 V.1: 501 tattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatt 560 V.7: 441 tattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatt 500 V.1: 561 ttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataat 620 V.7: 501 ttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataat 560 V.1: 621 atttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgt 680 V.7: 561 atttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgt 620 V.1: 681 gggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaa 740 till |||||||||||1|1|1||1|1|11|||11|||||11|11111||11111|||1||1 V.7: 621 gggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaa 680 V.1: 741 tgctgaatatttggettcattattcccagattctttgattgtcaaaggatttaatgttgt 800 1111||||| 1|1| t|||||li|1|1|| 1||| t|||||| 11111|||| i ||||||)||||||1111il V.7: 681 tgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgt 740 V.1: 801 ctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcag 860 V.7: 741 ctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcag 800 V.1: 861 caacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattcc 920 V.7: 801 caacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattcc 860 V.1: 921 cattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactctt 980 V.7: 861 cattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactctt 920 V.1: 981 tactctctggagagggccagtggtggtagctataagcttggccacattttttttccttta 1040 268 V.7: 921 tactctctggagagggccagtggtggtagctataagcttggccacattttttttccttta 980 V.1: 1041 ttcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaa 1100 1111il111i11lil111I1I1I111ill11 tllill l11 liii|||| 1111111111111111i V.7: 981 ttcctttgtcagagatgtgattcatccatatgetagaaaccaacagagtgacttttacaa 1040 V.1: 1101 aattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccct 1160 V.7: 1041 aattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccct 1100 V.1: 1161 agtataccttgcaggtettetggcagctgcttatcaactttattacggcaccaagtatag 1220 I 1|||1| ill l11 iil|i|i|||l|||||i|||||,||| ill|i||||||i|||||il V.7: 1101 agtatacctcgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatag 1160 V.1: 1221 gagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaag 1280 V.7: 1161 gagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaag 1220 V.1: 1281 ttttttcttegctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcaga 1340 V.7: 1221 ttttttcttcgctatggtccatgttgcctacagcctctgettaccgatgagaaggtcaga 1280 V.1: 1341 gagatatttgtttctcaacatggcttatcagcag 1374 V.7: 1281 gagatatttgtttctcaacatggcttatcagcag 1314 Score = 298 bits (155), Expect = 2e-771denties = 155/155 (100%) Strand = Plus / Plus V.1: 1537 cagtetacacttggatatgtcgctctgctcataagtactttccatgttttaatttatgga 1596 V.7: 1312 cagtetacacttggatatgtcgctctgctcataagtactttccatgttttaatttatgga 1371 V.1: 1597 tggaaacgagettttgaggaagagtactacagattttatacaccaccaaactttgttctt 1656 ll l l lli 1 1 1 1ll'illil 11 11 1 il l il ill1 11lil I i ililillliii l V.7: 1372 tggaaacgagettttgaggaagagtactacagattttatacaccaccaaactttgttctt 1431 V.1: 1657 gctcttgttttgccctcaattgtaattctggatct 1691 ii lI ill li i 11 ill11 ill iii iil 1111111 V.7: 1432 gctcttgttttgccctcaattgtaattctggatct 1466 Table LIV(f). Peptide sequences of protein coded by 98P486 v.7 (SEQ ID NO: 184) MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVs AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLPT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ STLGYVALLI STFHVLIYGw 360 KRAFEEEYYR FYTPPNFVLA LVLPSIVILD LSVEVLASPA AAWKCLGANI LRGGLSEIVL 420 PIEWQQDRKI PPLSTPPPPA MWTEEAGATA EAQESGIRNK SSSSSQIPVV GVVTEDDEAQ 480 DSIDPPESPD RALKAANSWR NPVLPHTNGv GPLWEFLL. LKSQAASGTL SLAFTSWSLG 540 EFLGSGTWMK LETIILSKLT QEQKSKHCMF SLISGS 576 269 Table LV(f). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 185) and 98P4B6 v.7 (SEQ ID NO: 186) Score = 753 bits (1944), Expect = 0.0dentities = 390/446 (87%), Positves = 390/446 (87%), Gaps = 55/446 (12%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSET LPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.7: 1 MESISMMGSPKSLSETFLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.7: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.7: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.7: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIETVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTK.YRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.7: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQ V.7: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQ ------------------- 340 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 STLGYVALLISTFHVLIYGWKRAFE V.7: 341 ------------------------------------ STLGYVALLISTFHVLIYGWKRAFE 365 V.1: 421 EEYYRFYTPPNFVLALVLPSIVILDL 446 EEYYRFYTPPNFVLALVLPSIVILDL V.7: 366 EEYYRFYTPPNFVLALVLPSIVILDL 391 Table 111(g). Nucleotide sequence of transcript variant 98P486 v.8 (SEQ ID NO: 187) gccccctccg agctccccga ctcctccccg cgctccacgg ctcttcccga ctccagtcag 60 cgttcctcgg gccctcggcg ccacaagctg tccgggcacg cagcccctag cggcgcgtcg 120 ctgccaagcc ggcctccgcg cgcctccctc cttccttctc ccctggctgt tcgcgatcca 180 gcttgggtag gcggggaagc agctggagtg cgaccgccac ggcagccacc ctgcaaccgc 240 cagtcggagg tgcagtccgt aggccctggc ccccgggtgg gcccttgggg agtcggcgcc 300 gctcccgagg agctgcaagg ctcgcccctg cccggcgtgg agggcgcggg gggcgcggag 360 gatattcttg gtgatcttgg aagtgtccgt atcatggaat caatctctat gatgggaagc 420 cctaagagcc ttagtgaaac ttgtttacct aatggcataa atggtatcaa agatgcaaqg 480 aaggtcactg taggtgtgat tggaagtgga gattttgcca aatccttgac cattcgactt 540 attagatgcg gctatcatgt ggtcatagga agtagaaatc ctaagtttgc ttctgaattt 600 tttcctcatg tggtagatgt cactcatcat gaagatgctc tcacaaaaac aaatataata 660 tttgttgcta tacacagaga acattatacc tccctgtggg acctgagaca tctgcttgtg 720 ggtaaaatcc tgattgatgt gagcaataac atgaggataa accagtaccc agaatccaat 780 gctgaatatt tggcttcatt attcccagat tctttgattg tcaaaggatt taatgttgtc 840 tcagcttggg cacttcagtt aggacctaag gatgccagcc ggcaggttta tatatgcagc 900 aacaatattc aagcgcgaca acaggttatt gaacttgccc gccagttgaa tttcattccc 960 attgacttgg gatccttatc atcagccaga gagattgaaa atttacccct acgactcttt 1020 actctctgga gagggccagt ggtggtagct ataagcttgg ccacattttt tttcctttat 1080 tcctttgtca gagatgtgat tcatccatat gctagaaacc aacagagtga cttttacaaa 1140 attcctatag agattgtgaa taaaacctta cctatagttg ccattacttt gctctcccta 1200 gtataccttg caggtcttct ggcagctgct tatcaacttt attacggcac caagtatagg 1260 agatttccac cttggttgga aacctggtta cagtgtagaa aacagcttgg attactaagt 1320 tttttcttcg ctatggtcca tgttgcctac agcctctgct taccgatgag aaggtcagag 1380 agatatttgt ttctcaacat ggcttatcag caggttcatg caaatattga aaactcttgg 1440 aatgaggaag aagtttggag aattgaaatg tatatctcct ttggcataat gagccttggc 1500 ttactttccc tcctggcagt cacttctatc ccttcagtga gcaatgcttt aaactggaga 1560 270 gaattcagtt ttattcagtc tacactigga tatgtcgctc tgctcataag tactttccat 1620 gttttaattt atqqatggaa acgagctttt gaggaagagt actacagatt ttatacacca 1680 ccaaactttg ttcttgctct tgttttgccc tcaattgtaa ttctgggtaa gattatttta 1740 ttccttccat gtataagccg aaagctaaaa cgaattaaaa aaggctggga aaagagccaa 1800 tttctggaag aaggtatqgg aggaacaatt cctcatgtct ccccggagag ggtcacagta 1860 atgtgatgac aaatggtgtt cacagctqcc atataaagtt ctactcatgc cattattttt 1920 atgacttcta cgttcagtta caagtatgct gtcaaattat cgtgggttga aacttgttaa 1980 atgagatttc aactgactta gtqatagagt tttcttcaag ttaattttca caaatgtcat 2040 gtttgccaat atgaattttt ctagtcaaca tattattgta atttaggtat gttttgtttt 2100 gttttgcaca actgtaaccc tgttgttact ttatatttca taatcaggca aaaatactta 2160 cagttaataa tatagatata atgttaaaaa caatttgcaa accagcagaa ttttaagctt 2220 ttaaaataat tcaatggata tacatttttt tctgaagatt aagattttaa ttattcaact 2280 taaaaagtag aaatgcatta ttatacattt ttttaagaaa ggacacgtta tgttagcatc 2340 taggtaaggc tgcatgatag cattcctata tttctctcat aaaataggat ttgaaggatg 2400 aaattaattg tatgaagcaa tgtgattata tgaagagaca caaattaaaa agacaaatta 2460 aacctgaaat tatatttaaa atatatttga gacatgaaat acatactgat aatacatacc 2520 tcatgaaaga ttttattctt tattgtgtta cagagcagtt tcattttcat attaatatac 2580 tgatcaggaa gaggattcag taacatttqg cttccaaaac tgctatctct aatacggtac 2640 caatcctagg aactgtatac tagttcctac ttagaacaaa agtatcaagt ttgcacacaa 2700 gtaatctgcc agctgacctt tgtcgcacct taaccagtca ccacttgcta tqgtatagga 2760 ttatactgat gttctttgag ggattctgat gtgctaggca tggttctaag tactttactt 2820 gtattatccc atttaatact tagaacaacc ccgtgagata agtaqttatt atcctcattt 2880 tacacatgag ggaccgaagg atagaaaagt tatttttcaa aggtcttgca gttaataaat 2940 ggcagagtga gcattcaagt ccaggtagtc atattccaga ggccacggtt ttaaccacta 3000 ggctctagag ctcccgccgc gcccctatgc attatgttca caatgccaat ctagatgctt 3060 cctcttttgt ataaagtcac tgacattctt tagagtgqgt tgggtgcatc caaaaatgta 3120 taaaaatatt attataataa acttattact gcttgtaggg taattcacag ttacttaccc 3180 tattcttgct tggaacatga gcctqgagac ccatggcagt ccatatgcct ccctatqcag 3240 tgaagggccc tagcagtgtt aacaaattgc tgagatccca cggagtcttt caaaaatctc 3300 tgtagagtta gtcttctcct tttctcttcc tgagaagttc tcctgcctgc ataaccattc 3360 attagggagt actttacaag catgaaggat attagggtaa gtggctaatt ataaatctac 3420 tctagagaca tataatcata cagattattc ataaaatttt tcagtgctgt ccttccacat 3480 ttaattgcat tttgctcaaa ctgtagaatq ccctacattc cccccacccc aatttgctat 3540 ttccttatta aaatagaaaa ttataggcaa gatacaatta tatgcgttcc tcttcctgaa 3600 attataacat ttctaaactt acccacgtag gtactactga atccaactgc caacaataaa 3660 aagactttta tttagtagag gctacctttc ccaccagtga ctctttttct acaactgcct 3720 tgtcagtttg gtaattcact tatgattttc taatgttctc ttggtgaatt ttattatctt 3780 gtaccctctt tttttttttt ttttttttta aagacagagt cttgctctgt cacccaggct 3840 ggagtgcagt ggcacgatct cggctcactg caagctctgc ctcccgggtt cacgccattc 3900 tcctgcctca gcctcccgag tagctgggac tacaggtgcc cgccaccatg cccggctgat 3960 ttctttttgt atttttagta gagacggagt ttcaccgtgt tagccaggat ggtctcgatc 4020 tcctgacctc gtgatccgcc cgccttggcc tccaaagtgc tgggattaca gqtgtgagct 4080 accgcgcccg gcctattatc ttgtactttc taactgagcc ctctattttc tttattttaa 4140 taatatttct ccccacttga gaatcacttg ttagttcttg gtaggaattc agttggqcaa 4200 tgataacttt tatgggcaaa aacattctat tatagtgaac taatgaaaat aacagcgtat 4260 tttcaatatt ttcttattcc ttaaattcca ctcttttaac actatgctta accacttaat 4320 gtgatgaaat attcctaaaa gttaaatgac tattaaagca tatattgttg catgtatata 4380 ttaagtagcc gatactctaa ataaaaatac cactgttaca gataaatggq gcctttaaaa 4440 atatgaaaaa caaacttgtg aaaatgtata aaagatgcat ctgttgtttc aaatggcact 4500 atcttctttt cagtactaca aaaacagaat aattttgaag ttttagaata aatgtaatat 4560 atttactata attctaaatg tttaaatgct tttctaaaaa tgcaaaacta tgatgtttag 4620 ttgctttatt ttacctctat gtgattattt ttcttaattg ttatttttta taatcattat 4680 ttttctgaac cattcttctg gcctcagaag taggactgaa ttctactatt gctaggtgtg 4740 agaaagtggt ggtgagaacc ttagagcagt-ggagatttgc tacctggtct gtgttttgag 4800 aagtgcccct tagaaagtta aaagaatgta gaaaagatac tcagtcttaa tcctatgcaa 4860 aaaaaaaaat caagtaattg ttttcctatg aggaaaataa ccatgagctg tatcatgcta 4920 cttagctttt atgtaaatat ttcttatgtc tcctctatta agagtattta aaatcatatt 4980 taaatatgaa tctattcatg ctaacattat ttttcaaaac atacatggaa atttagccca 5040 gattgtctac atataaggtt tttatttgaa ttgtaaaata tttaaaagta tgaataaaat 5100 atatttatag gtatttatca gagatgatta ttttgtgcta catacaggtt ggctaatgag 5160 ctctagtgtt aaactacctg attaatttct tataaagcag cataaccttg gcttgattaa 5220 ggaattctac tttcaaaaat taatctgata atagtaacaa ggtatattat actttcatta 5280 caatcaaatt atagaaatta cttgtgtaaa agggcttcaa gaatatatcc aatttttaaa 5340 271 tattttaata tatctcctat ctgataactt aattcttcta aattaccact tgccattaag 5400 ctatttcata ataaattctg tacagtttcc ccccaaaaaa gagatttatt tatgaaatat 5460 ttaaagtttc taatgtggta ttttaaataa agtatcataa atgtaataag taaatattta 5520 tttaggaata ctgtgaacac tqaactaatt attcctgtgt cagtctatga aatccctgtt 5580 ttgaaatacg taaacagcct aaaatgtgtt gaaattattt tgtaaatcca tgacttaaaa 5640 caagatacat acatagtata acacacctca caqtgttaag atttatattg tgaaatgaqa 5700 caccctacct tcaattgttc atcagtgggt aaaacaaatt ctgatgtaca ttcaggacaa 5760 atgattagcc ctaaatgaaa ctgtaataat ttcagtggaa actcaatctg tttttacctt 5820 taaacagtga attttacatg aatgaatggg ttcttcactt tttttttagt atgagaaaat 5880 tatacagtgc ttaattttca gagattcttt ccatatgtta ctaaaaaatg ttttgttcag 5940 cctaacatac tgagtttttt ttaactttct aaattattga attccatca tgcattcatc 6000 caaaattaag gcagactgtt tggattcttc cagtggccag atgagctaaa ttaaatcaca 6060 aaagcagatg cttttgtatg atctccaaat tgccaacttt aaggaaatat tctcttgaaa 6120 ttgtctttaa agatcttttg cagctttgca gatacccaga ctgagctgga actggaattt 6180 gtcttcctat tgactctact tctttaaaag cggctgccca ttacattcct caqctgtCCt 6240 tgcagttagg tgtacatgtg actgagtqtt gqccaqtgag atgaagtctc ctcaaaggaa 6300 ggcagcatgt gtcctttttc tcccttcat cttgctgctg ggattgga tataacagga 6360 gccctggcag ctgtctccag agqatcaaag ccacacccaa agagtaaggc agattagaga 6420 ccagaaagac cttgactact tccctacttc cactgctttt tcctgcattt aagccattgt 6480 aaatctgggt gtgttacatg aaqtgaaaat taattctttc tgcccttcag ttctttatcc 6540 t gataccatt taacactgtc tgaattaact agactgcaat aattctttct tttgaaagct 6600 tttaaaggat aatgtgcaat tcacattaaa attgattttc cattgtcaat tagttatact 6660 cattttcctg ccttgatctt tcattagata ttttgtatct gcttggaata tattatcttc 6720 tttttaactg tgtaattggt aattactaaa actctgtaat ctccaaaata ttgctatcaa 6780 attacacacc atgttttcta tcattctcat agatctgcct tataaacatt taaataaaaa 6840 gtactattta atgattt c8t57 Table 1.1I1(g). Nucleotide sequence alignment of 98P486 v.1 (SEQ ID NO: 188) and 98P4136 v.8 (SEQ ID NO: 189) Score = 3201 bits (1665), Expect z0.Oldentities = 1665/1665 (100%) Strand =Plus / Plus V.t: 23 gttcctcgggccctcggcgccacaagctgtccggcacgcagcccctacggcgcgtcgc 82 V.8: 62 gttcctcgggccctcggcgccacaagctgtccgggcacgcagcccctagcggcggtcgc 121 V. 1: 83 tgccaagccggcctccgcgcgcctccctccttccttctcccctggctgttcgcgatccag 142 V.8: 122 tgccaagccggcctccgcgcgcctccctccttccttctcccctggctgttcgcgatccag 181 V. 1: 143 cttgggtaggcgggaagcagctggagtcgaccgccacggcagccaccctgcaaacgat 202 V.8: 182 1tagtggaa V. 1: 203 agtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcgcgccg 262 V.8: 242 agtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgccg 301 V.1: 263 ctcccgaggagctgcaaggctcgcccctgcccggcgtggagggcgcggggggcgcggagg 322 V.8:-302 ctcccgaggagctgcaaggctcgcccctgcccggcgtggagggccggggggcgcggagg 361 V.g1: 323 2cgtgcag V.8: 362 atattcttggtgatcttggaagtgtccgtatcatgaatcaatcttatgatgggaagcc 421 V.1: 383 ctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgaagga 442 272 V.8: 422 ctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaagga 481 V.1: 443 aggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattegactta 502 V.8: 482 aggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgactta 541 V.1: 503 ttagatgcggetatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatttt 562 V.8: 542 ttagatgeggetatcatgtggtcataggaagtagaaatectaagtttgettctgaatttt 601 V.1: 563 ttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataatat 622 ||111| I | 1| ||||1 I 1111|1 |||||I I||I ||||||||111 |1 |11|||||||||1 ||||11 |1 V.8: 602 ttcctcatgtggtagatgtcactcatcatgaagatgetctcacaaaaacaaatataatat 661 V.1: 623 ttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgtgg 682 li|||||lt 1||1|1||111|||1||||1||||I Illil 11|||||1|||1||||1|11|| V.8: 662 ttgttgctatacacagagaacatta-tacctccctgtgggacctgagacatctgcttgtgg 721 V.1: 683 gtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaatg 742 V.8: 722 gtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaatg 781 V.1: 743 ctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgtct 802 I 1 ||||1111 ||||||||1111 11111 11|||||1|||1111|||ll 1||| V.8: 782 ctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgtct 841 V.1: 803 cagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcagca 862 V.8: 842 cagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcagca 901 V.1: 863 acaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattccca 922 V.8: 902 acaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattccca 961 V.1: 923 ttgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactcttta 982 V.8: 962 ttgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactcttta 1021 V.1: 983 ctctctggagagggccagtggtggtagctataagettggccacattttttttcctttatt 1042 V.8: 1022 ctctctggagagggccagtggtggtagctataagcttggccacattttttttcctttatt 1081 V.1: 1043 cctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaaaa 1102 I i 11 111 11 I I 11111 j l i ll l ii lii III l II || 1| 111||||||||||||111|||||| V.8: 1082 cctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaaaa 1141 V.1: 1103 ttcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccctag 1162 V.8: 1142 ttcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccctag 1201 273 V.1: 1163 tataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatagga 1222 V.8: 1202 tataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatagga 1261 V.1: 1223 gatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaagtt 1282 Ilillill1111l11ll1l11il11l11l11l11111111111l111111111111ll V.8: 1262 gatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaagtt 1321 V.1: 1283 ttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcagaga 1342 111lll11111111111111ll1111lfillllllilllllil 111111111111lili V.8: 1322 ttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcagaga 1381 V.1: 1343 gatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactcttgga 1402 V.8: 1382 gatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactcttgga 1441 V 17 1403 atgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttggct 1462 ||111llll11111l1111lilllll11111ff|111|11|f|ll ||11||11|11|||||1 V.8: 1442 atgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttggct 1501 V.1: 1463 tactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactggagag 1522 1illll1l11ill1lll1l1111111111ll1l11l11ll1ll1l11111l111l111ll V.8: 1502 tactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactggagag 1561 V.1: 1523 aattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttccatg 1582 111llll ff1111111111111111111111111111111 |ll fill lii||li|i||l V.8: 1562 aattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttccatg 1621 V.1: 1583 ttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacaccac 1642 11111111111111111ff 111l1111111||1||1||1|111|111||11|1111||1| V.8: 1622 ttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacaccac 1681 V.1: 1643 caaactttgttcttgctcttgttttgccctcaattgtaattctgg 1687 V.8: 1682 caaactttgttcttgctcttgttttgccctcaattgtaattctgg 1726 Score = 1381 bits (718), Expect = O.Oldenlities = 7251726 (99%), Gaps = 1/726 (0%) Strand = Plus I Plus V.1: 1687 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1746 1111|111111|11|1111|1111||||||1|111|1|11|111||11|111|11||1111 V.8: 6132 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 6191 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1806 V.8: 6192 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 6251 V.1: 1807 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1866 V.8: 6252 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 6311 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1926 274 V.8: 6312 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 6371 V.1: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1986 ||| I1 1 1|1 || | 1 |||||||11 |||||1 l I llililli l i 1 1111 i11 l1l I I l 11111ll V.8: 6372 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 6431 V.1: 1987 ttgactacttccctacttccactgctttt-cctgcatttaagccattgtaaatctgggtg 2045 V.8: 6432 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 6491 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 V.8: 6492 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 6551 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 -V.8: 6552 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 6611 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2225 |||11||1111|||11|||||1||11|1|||1|1|||1|11||||||11|1111|11|1|| V.8: 6612 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 6671 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 V.8: 6672 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 6731 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatAttgctatcaaattacacacca 2345 V.8: 6732 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 6791 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 ||1|||||1||||l ||||||1| |||111 i 1 ||111111 11111 l11lIi 111111111l I l ii| | V.8: 6792 tgttttctatcattctcatagatetgccttataaacatttaaataaaaagtactatttaa 6851, V.1: 2406 tgattt 2411 H||I|| V.8: 6852 tgattt 6857 Table LV(g). Peptide sequences of protein coded by 98P486 v.8 (SEQ ID NO: 190) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGMGGTIP 480 D KVSAPERVTVM 490 275 Table LV(g). Amino acid sequence alignment of 98P486 v.1 (SEQ ID NO: 191) and 98P486 v.8 (SEQ ID NO: 192) Score = 888 bits (2294), Expect = 0.0ldentities = 444/444 (100%), Positives = 444/444 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.8: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.8: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.8: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.8: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.8: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY V.8: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFVLIYGWKRAFE V.8: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 EEYYRFYTPPNFVLALVLPSIVIL V.B: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 276

Claims

1. A composition comprising: a) a peptide of Tables VIII-IX or XII-XXI or an analog thereof wherein an 5 amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV; b) a peptide of Tables XXII, XXV, XXVII, XXXIV, XXXVII, and XXXIX or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with a preferred amino acid as shown in Table IV; or 10 c) a peptide of Tables XLVI to XLIX or an analog thereof wherein an amino acid at a primary anchor site of the peptide is substituted with an amino acid as shown in Table IV; wherein the peptide is a peptide of SEQ ID NO: 3. 15

2. A polynucleotide that encodes a peptide of claim 1.

3. A vector that comprises a polynucleotide of claim 2.

4. A method of generating a mammalian immune response directed to a protein 20 comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: exposing cells of the mammal's immune system to a) a peptide of claim 1 and/or b) a nucleotide sequence that encodes said peptide, whereby an immune response is generated to said protein. 25

5. The method of claim 4, wherein the immune system cell is a cytotoxic T cell (CTL).

6. The method of claim 4, wherein the immune system cell is a helper T cell (HTL). 30

7. An antibody or fragment thereof that specifically binds to a peptide of claim 1.

8. An antibody or fragment thereof of claim 7, which is monoclonal. 35

9. An antibody or fragment thereof of claim 7, which is a human, humanized, or chimeric antibody or fragment thereof. 277

10. A method for detecting the presence of a protein comprising the amino acid sequence of SEQ ID NO: 3 in a sample comprising: contacting the sample with an antibody or fragment thereof of claim 7, and determining that there is a complex of the 5 antibody or fragment thereof and said protein.

11. A method of claim 10, wherein the sample is from a patient who has or who is suspected of having cancer. 10

12. A method of claim 11, wherein the cancer occurs in a tissue set forth in Table I.

13. An antibody-agent conjugate comprising the antibody or fragment of claim 7 conjugated to a cytotoxic agent or diagnostic agent. 15

14. The antibody-agent conjugate of claim 13, wherein the antibody or fragment is conjugated to a cytotoxic agent.

15. The antibody-agent conjugate of claim 14, wherein the cytotoxic agent is an auristatin or a maytansinoid. 20

16. The antibody-agent conjugate of claim 14, wherein the cytotoxic agent is a calcium channel inhibitor.

17. The antibody-agent conjugate of claim 16, wherein the calcium channel 25 inhibitor is agatoxin.

18. A method of delivering a cytotoxic agent or a diagnostic agent to a cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, said method comprising: exposing said cells to the antibody-agent conjugate of any of claims 13 to 30 17.

19. A method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: exposing said cells to an antibody-agent conjugate as in any of claims 14 to 17. 35 278

20. The method of claim 19, wherein said antibody-agent conjugate is administered with another cancer therapeutic agent.

21. The method of claim 20, wherein the other cancer therapeutic agent is 5 trastuzumab or paclitaxel.

22. A composition comprising a polynucleotide that encodes an antibody or fragment thereof of claim 7. 10

23. A composition comprising human T cells, wherein said T cells specifically recognize a peptide as defined in claim 1 in the context of a particular HLA molecule.

24. A method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising administering to 15 said cells an antibody or fragment thereof of claim 7.

25. The method of claim 24, wherein the antibody is a monoclonal antibody, a human antibody, a humanized antibody, or a single-chain antibody, or a fragment thereof. 20

26. A method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: administering to said cells a) a peptide of claim I and/or b) a nucleotide sequence that encodes said peptide. 25

27. A method of inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, and a particular HLA molecule, the method comprising: administering human T cells to said cancer cells, wherein said T cells specifically recognize a peptide of claim I wherein the peptide is in the context of the 30 particular HLA molecule.

28. A method for inhibiting growth of cancer cells that express a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising: administering to the cancer cells a vector that delivers a nucleotide that encodes a single chain monoclonal 35 antibody having the specificity of an antibody of claim 7, whereby the encoded single chain antibody is expressed intracellularly within said cancer cells. 279

29. A method of delivering a calcium channel inhibitor to a cancer cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising exposing the cell to an antibody-inhibitor conjugate comprising an antibody 5 or fragment thereof conjugated to a calcium channel inhibitor, wherein the antibody or fragment thereof specifically binds to the protein.

30. The method of claim 29, wherein the calcium channel inhibitor is agatoxin. 10

31. A method of inhibiting the growth of a paclitaxel-resistant cancer cell that expresses a protein comprising the amino acid sequence of SEQ ID NO: 3, the method comprising exposing the cell to an antibody-agent conjugate comprising an antibody or fragment thereof conjugated to a cytotoxic agent or therapeutic agent, wherein the antibody or fragment thereof specifically bind to the protein. 15

32. The method of claim 31, wherein the antibody or fragment is conjugated to a cytotoxic agent.

33. The method of claim 32, wherein the cytotoxic agent is an auristatin or a 20 maytansinoid.

34. The method of claim 32, wherein the cytotoxic agent is a calcium channel inhibitor. 25

35. The method of claim 34, wherein the calcium channel inhibitor is agatoxin. 30 280