AU2008200363B2 - Nucleic acids and corresponding proteins entitled 101P3A11 or PHOR-1 useful in treatment and detection of cancer - Google Patents

Description

AUSTRALIA FB RICE & CO Patent and Trade Mark Attorneys Patents Act 1990 AGENSYS, INC. COMPLETE SPECIFICATION STANDARD PATENT Invention Title: Nucleic acids and corresponding proteins entitled 10 1P3A 11 or PHOR-1 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:- IA NUCLEIC ACIDS AND CORRESPONDING PROTEINS ENTITLED 101P3AI1 or PHOR-1 USEFUL IN TREATMENT AND DETECTION OF CANCER This is a divisional of AU 2002309873, the entire contents of which are 5 incorporated herein by reference. CROSS-REFERENCE TO RELATED APPLICATIONS This application claims benefit of priority from U.S. Application Serial Number 10/017, 066, filed December 14, 2001, which is a continuation of; pending U.S. 10 Application Serial Number 10/001, 469, filed October 31, 2001, which claimed priority of; pending U.S. Provisional Application Serial Number 60/291,118, filed May 15, 2001; the present application is also related to U.S. Application Serial Number 09/680,728, filed October 5, 2000, which claims benefit of priority from U.S. Provisional Application Serial Number 60/157,902, filed October 5, 1999; each of the 15 applications referenced in this paragraph are hereby incorporated in their entireties as if fully set forth herein. STATEMENT OF RIGHTS TO INVENTIONS MADE UNDER FEDERALLY SPONSORED RESEARCH 20 Not applicable. FIELD OF THE INVENTION The invention described herein relates to a gene and its encoded protein, termed 101P3A II or PHOR-1, expressed in certain cancers, and to diagnostic and therapeutic 25 methods and compositions useful in the management of cancers that express IOlP3Al 1. BACKGROUND OF THE INVENTION Cancer is the second leading cause of human death next to coronary disease. 30 Worldwide, millions of people die from cancer every year. In the United States alone, 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 35 predicted to become the leading cause of death.

lB 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 5 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. 10 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 15 cancer. Surgical prostatectomy, radiation therapy, 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 et al., 1996, Proc. Nati. Acad. Sci. USA 93: 7252), prostate-specific membrane (PSM) antigen (Pinto et aL., Clin Cancer Res 1996 Sep 2 (9): 1445-5 1), 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. Natl. 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, including 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 8 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 will 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 2 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 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 I 1% 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 of86.5 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 cancer deaths. 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 choice 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. 3 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. 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 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 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 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 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 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 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. G Protein-Coupled Receptors G protein-coupled receptors (GPCR) share a common structural motif. All these receptors have seven sequences of between 22 to 24 hydrophobic amino acids that form seven alpha helices, each of which spans the membrane. The transmembrane helices are joined by strands of amino acids having a larger loop between the fourth and fifth transmembrane helix on the extracellular side of the membrane. Another larger loop, composed primarily of hydrophilic amino acids, joins transmembrane helices five and six on the intracellular side of the membrane. The carboxy terminus of the receptor lies intraccllularly with the amino terminus in the extracellular space. It is thought that the loop joining helices five and six, as well as the carboxy terminus, interact with the G protein. There is evidence that in certain GPCRs the first intracellular loop is also important for G-protein interactions. Currently, Gq, Gs, Gi, and Go are G proteins that have been identified. 4 5 Under physiological conditions, GPCRs exist in the cell membrane in equilibrium between two different states or conformations: an "inactive" state and an "active" state. A receptor in an inactive state is unable to link to the intracellular transduction pathway to produce a biological response. Changing the receptor conformation to the active state allows linkage to the transduction pathway and produces a 5 biological response. A receptor may be stabilized in an active state by an endogenous ligand or an exogenous agonist ligand. Recent discoveries, including but not exclusively limited to, modifications to the amino acid sequence of the receptor, provide alternative mechanisms other than ligands to stabilize the active state conformation. These approaches effectively stabilize the receptor in an active state by simulating the 10 effect of a ligand binding to the receptor. Stabilization by such ligand-independent approaches is termed "constitutive receptor activation." A receptor for which the endogenous ligand is unknown or not identified is referred to as an "orphan receptor." Concerning traditional compound screening, in general, the use of an orphan receptor for screening purposes to identify compounds that modulate a biological response associated with such 15 receptor has not been possible. This is because the traditional "dogma" regarding screening of compounds mandates that the ligand for the receptor be known, whereby compounds that competitively bind with the receptor, i.e., by interfering or blocking the binding of the natural ligand with the receptor, are selected. By definition, then, this approach has no applicability with respect to orphan receptors. Thus, by adhering to this dogmatic approach to the discovery of therapeutics, the art, in essence, has 20 taught and has been taught to forsake the use of orphan receptors unless and until the natural ligand for the receptor is discovered. The pursuit of an endogenous ligand for an orphan receptor can take several years and cost millions of dollars. Furthermore, and given that there are an estimated 2,000 GPCRs in the human genome, the majority of which being orphan receptors, the traditional dogma castigates a creative approach to the 25 discovery of therapeutics to these receptors. Numerous orphan G protein-coupled receptors are constitutively active in their endogenous state. Mouse olfactory receptor MOR 18- 1(>gil 18479284, Figure 64). The endogenous ligand for 10 1 P3AI I is unknown. SUMMARY OF THE INVENTION 30 The present invention relates to a gene, designated 10 1 P3A 11, that has now been found to be overexpressed in the cancer(s) listed in Table I. Northern blot expression analysis of 101P3AI I 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 101P3AI I are provided. The tissue related profile of 10 1 P3AI I in normal adult tissues, combined with the over-expression observed in the 35 tissues listed in Table !, shows that 10 1 P3AI 1 is aberrantly over-expressed in at least some cancers, and 5A thus serves as a useful diagnostic, prophylactic, prognostic, and/or therapeutic target for cancers of the tissue(s) such as those listed in Table 1. The invention provides polynucleotides corresponding or complementary to all or part of the 101 P3A 1 1 genes, mRNAs, and/or coding sequences, preferably in isolated form, including 5 polynucleotides encoding 10 I P3AI 1 -related proteins and fragments of 4, 5, 6, 7, 8, 9, 10, II, 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, 317 or 318; or more than 317 or 318 contiguous amino acids of alO I P3A 11-related protein, as well as 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 S10 1 P3AI I genes or mRNA sequences or parts thereof, and polynucleotides or oligonucleotides that hybridize to the 10 1 P3A 11 genes, mRNAs, or to 101 P3A 11- 6 encoding polynucleotides. Also provided are means for isolating cDNAs and the genes encoding 10 1 P3A 1I. Recombinant DNA molecules containing 101 P3AI I polynucleotides, cells transformed or transduced with such molecules, and host-vector systems for the expression of 101P3A 1 I gene products are also provided. The invention further provides antibodies that bind to 10 1 P3A I I proteins and 5 polypeptide fragments thereof, including polyclonal and monoclonal antibodies, murine and 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, either of which can be in respective human unit dose forms. In certain embodiments, the 10 entire nucleic acid sequence of Figure 2 is encoded and/or the entire amino acid sequence of Figure 2 is prepared, either of which can be in respective human unit dose forms. The invention further provides methods for detecting the presence and status of 10 1P3A I I polynucleotides and proteins in various biological samples, as well as methods for identifying cells that express 101 P3AI 1. A typical embodiment of this invention provides methods for monitoring 101P3A 11 15 gene products in a tissue or hematology sample having or suspected of having some form of growth dysregulation such as cancer. The invention further provides various immunogenic or therapeutic compositions and strategies for treating cancers that express IOIP3AI I such as cancers of tissues listed in Table I, including therapies aimed at inhibiting the transcription, translation, processing or function of 101 P3AI I as well as 20 cancer vaccines. In one aspect, the invention provides compositions, and methods comprising them, for treating a cancer that expresses 101P3A1 1 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 10 1 P3A 11. Preferably, the carrier is a uniquely human carrier. In another aspect of the invention, the agent is a moiety that is immunoreactive with 10 1 P3A 1 I protein. Non 25 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 molecule as defined herein. In another aspect, the agent comprises one or more than one peptide which comprises a 30 cytotoxic T lymphocyte (CTL) epitope that binds an HLA class I molecule in a human to elicit a CTL response to 10 1 P3A 1I and/or one or more than one peptide which comprises a helper T lymphocyte (HTL) epitope which binds an HLA class II 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 35 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 nucleic acid molecule may express a moiety 6A that is immunologically reactive with 101P3AI I as described above. The one or more than one nucleic acid molecule may also be, or encodes, a molecule that inhibits production of 101 P3A 11. Non-limiting examples of such molecules include, but are not limited to, those complementary to a nucleotide sequence essential for production of 101 P3A I I (e.g. antisense sequences or molecules that form a triple 5 helix with a nucleotide double helix essential for 10 1 P3A I I production) or a ribozyme effective to lyse 101P3A I I mRNA. The present invention also provides a method to identify an agent that decreases the activity of a protein having the amino acid sequence set forth in positions 2-318 of SEQ ID NO:28, which method comprises 10 providing a first sample of cells and a second sample of cells, wherein the cells of each sample produce said protein; contacting the first sample with a candidate compound; measuring the activity of said protein in the first sample with the candidate compound; measuring the activity of said protein in the second sample, wherein the second sample has not 15 been contacted with said candidate compound; comparing the measured activity of said protein in said first and second samples; whereby a decrease in the activity of said protein in said first sample as compared to said second sample identifies said compound as an agent that decreases activity of said protein; wherein said activity comprises cAMP accumulation mediated by said protein 20 The present invention also provides a method to deliver a cytotoxic agent or a diagnostic agent to a cell, wherein said cell produces a protein having the amino acid sequence of positions 2-318 of SEQ ID NO:28, which method comprises exposing said cell to a conjugate of the cytotoxic agent or diagnostic agent coupled to an antibody or fragment thereof that binds said protein. 25 The present invention also provides a method to identify a peptide useful as a vaccine to elicit an immune response to a protein comprising positions 2-318 of the amino acid sequence of SEQ ID NO:28, which method comprises identifying an HLA supertype for which binding of epitopes of said vaccine is desired; selecting from the peptides listed in one of Tables VI to LI any epitopes of SEQ ID NO:28 30 disclosed to bind alleles of said identified supertype; experimentally assessing the ability of said peptides to bind to at least one allele of said HLA supertype and identifying as a peptide useful as a vaccine a peptide that binds with an IC 50 equal to, or less than, 500 nanomolar to said HLA supertype allele.

6B Note: To determine the starting position of any peptide set forth in Tables V-XVIII and XXII to IL (collectively 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 in Table LII. Generally, a unique Search Peptide is used to obtain HLA peptides of a partiular for a particular variant. The position of each Search Peptide relative to its respective parent molecule is listed in Table LIU. Accordingly if a Search Peptide begins at position "X", one must add the value "X - 1" to each position in Tables V-XVIll and XXII to IL to obtain the actual position of the HLA peptides in their parental molecule. For example if a particular Search Peptide begins at position 150 of is 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. BRIEF DESCRIPTION OF THE FIGURES: Figure 1. The IOP3Al I SSH sequence. Figures 2A-2C. The cDNA and amino acid sequence of 1OP3AI [variants 1-3. The start methionine is underlined. The open reading frame for variants I and 3 extends from nucleic acid 133 to 1086 including the stop codon, The codon for the initial M in each variant can be omitted as the shorter peptide can have a more favorable Kozak sequence). Figure 3A-C. Amino acid sequences of 101P3AI I variants 1-3. Figure 4. Alignment of IO1P3AI I (Sbjct) with mouse olfactory receptor S25 (Query.) The transmembrane regions of 101P3AI I and mouse olfactory receptor S25 (ORS25)predicted using the TMHMM algorithm are highlighted in gray. The amino acids of ORS25 predicted (Floriano, W.B., et al, 2000, Proc. Nati. Acad. Sci., USA, 97:10712-10716) to be involved in binding of the ligand hexanol and/or involved in the formation of the ligand binding pocket are italicized and bolded in the Figure, and are: Leu 131, Val 134, Val 135, Gly 138, Thr139, Ser 193, Ser 197, Phe 225, Ala 230, Ile 231, Gly 234, Thr 284, Phe 287, Gin 300, Lys 302. Figure 5. Hydrophilicity amino acid profile of 101 P3A 11 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 (www.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 6. Hydropathicity amino acid profile of 101 P3A I I 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 (www.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 7. Percent accessible residues amino acid profile of 10 lP3A II determined by computer algorithm sequence analysis using the method of Janin (Janin J., 1979 Nature 277:491-492) accessed on the ProtScale website (www.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 8. Average flexibility amino acid profile of IOP3Al I 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 (www.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 9. Beta-turn amino acid profile of 101P3AI 1 determined by computer algorithm sequence analysis using the method of Deleage and Roux (Dclcage, G., Roux B. 1987 Protein Enginecring 1:289-294) accessed on the ProtScale website (www.expasy.chlcgi-bin/protscale.pl) through the ExPasy molecular biology server. 7 Figure 10A. Expression of 101P3A II by RT-PCR. First strand cDNA was prepared from vital pool 1 (VP 1: liver, lung and kidney), vital pool 2 (VP2, pancreas, colon and stomach), prostate xenograft pool, prostate cancer pool, kidney cancer pool , colon cancer pool, breast cancer pool, and cancer metastasis pool. Normalization was performed by PCR using primers to actin and GAPDH. Semi-quantitative PCR, using primers to IOP3Al 1, was performed at 30 cycles of amplification. Expression of lOIP3AI I was observed in prostate xenograft pool, prostate cancer pool, kidney cancer pool , colon cancer pool, breast cancer pool, and cancer metastasis pool, but not in VPl and VP2. Figure 1OB. Expression of 10 lP3AI I in human cancers demonstrated by dot blot analysis of tumor RNA (T) and normal RNA (N) matched samples using patient-derived amplified cDNAs. Up-regulation of PHOR-1 expression was found in 3 of 3 prostate cancer patients, 6 of 14 kidney cancer patients, 2 of 8 uterine cancer patients, 3 of 8 stomach cancer patients and 7 of 7 rectal cancer patients. Figure 11. Expression of 101P3A1 1 in human patient cancer specimens. RNA was extracted from a pool of three prostate cancer tumors, kidney cancer tumors, colon cancer tumors, breast cancer tumors, and a cancer metastasis pool derived from cancer patients, as well as from normal prostate (NP), normal bladder (NB), normal kidney (NK) and normal colon (NC). Northern blots with 10 pg of total RNA/lane were probed with a I1P3A1 1 fragment. Size standards in kilobases (kb) are indicated on the side. The results showed expression of IOIP3A1 I in prostate cancer tumors, kidney cancer tumors, colon cancer tumors, breast cancer tumors, cancer metastasis pool, bladder cancer pool, and in the normal prostate but not in the other normal tissues. A picture of the ethidium-brornide staining of the RNA gel is also presented. Figure 12A. Expression of IOlP3AI 1 in prostate cancer patient specimens. RNA was extracted from prostate tumors (T) and their normal adjacent tissues (Nat) derived from prostate cancer patients. Northern blots with 10 pg of total RNA/lane were probed with lO1P3Al I sequences. Results show upregulated expression of lOP3A1I1 in 8 of 10 tumor specimens. Figure 12B. Photomicrograph showing OP3AI I expression in prostatic intraepithelial neoplasia (PIN) by in situ hybridization with an anti-sense 1OlP3Al I riboprobe. Figure 12C. Photomicrograph showing 1OlP3Al 1 expression in prostate cancer tissue by in situ hybridization with an anti-sense 101P3A I1 nboprobe. Figure 12D. Photomicrograph showing IOlP3Al 1 expression in prostate cancer by in situ hybridization with an anti-sense 1OlP3A I1 riboprobe. Note up-regulation of expression relative to normal prostate, FIG. 12E. Figure 12E. Photomicrograph showing 101P3AI I expression in normal prostate by in situ hybridization with an anti-sense 1OIP3AlI riboprobe. Figure 13. Expression of OlP3A1 1 in colon cancer patient specimens. RNA was extracted from colon tumors (T) and their normal adjacent tissues (Nat) derived from colon cancer patients. Northern blots with 10 pg of total RNA/lane were probed with 10 IP3Al I sequences. Size standards in kilobases (kb) are indicated on the side. Results showed expression of 101P3AI I in colon tumors but not in normal tissues. Expression was also seen in the colon cancer cell line T84. A picture of the ethidium-bromide staining of the RNA gel is also presented. Figure 14. Expression or 101 P3A I I in kidney cancer patient specimens. RNA was extracted from kidney tumors (T) and their normal adjacent tissues (Nat)-derived from kidney cancer patients. Northern blots with 10 pg of total RNA/lane were probed with lOlP3AI 1 sequences. Size standards in kilobases (kb) are 8 indicated on the side. The results showed expression of 101P3A 1 in five of six kidney tumor specimens. The expression detected in normal adjacent tissues (isolated from diseased tissues) but not in normal tissues (isolated from healthy donors) indicates that these tissues are not fully normal and that 101 P3A I1 is expressed in early stage tumors. A picture of the ethidium-bromide staining of the RNA gel is also presented. Figures 15A-15C. Androgen regulation of 101P3AI 1 in tissue culture cells. LAPC-9 cells were grown in charcoal-stripped medium and stimulated with the synthetic androgen mibolerone, for either 14 or 24 hours. Northern blots with 10 pag of total RNA/lane were probed with 101P3A1 1 sequences (Figure 15A). A picture of the ethidium-bromide staining of the RNA gel is also presented (Figure 15C). Results showed expression of 101P3A II was not regulated by androgen. The experimental samples were confirmed by testing for the expression of the androgen-regulated prostate cancer gene PSA (Figure 15B). This experiment showed that, as expected, PSA levels go down in presence of charcoal-stripped serum, and expression is induced at 14 and 24 hours in presence of nibolerone. Figure 16. Andrdgen regulation of 101P3AI 1 in vivo. Male mice were injected with LAPC-9AD tumor cells. When tumors reached a palpable size (0.3-0.5cm in diameter), mice were castrated and tumors harvested at different time points following the castration. RNA was isolated from the xenograft tissues. Northern blots with 10 jig of total RNA/lane were probed with 101P3A IIsequences. Size standards in kilobases (kb) are indicated on the side. A picture of the ethidium-bromide staining of the RNA gel is also presented. The results showed that expression of 101P3A II is not androgen regulated. Figure 17. Expression and detection of 101P3AI 1(159-202)-psecFc fusion protein. The 101P3A 11(159-202)-psecFc vector was constructed. The recombinant expression vector DNA was transfected into either 293T cells or Cos-7 cells. Cells as well as culture supernatants (media) were harvested 24 hours later. The cells were lysed, and run on SDS-PAGE gel along with the media samples. The gel was transferred to nitrocellulose, stained with HRP-labeled anti-human IgG and developed using the ECL chemiluminescence detection kit. Results showed expression of the 1OIP3AIl (159-202)-psecFc fusion protein in the lysates of both 293T and Cos-7 cells. The 101P3A1 1(159-202)-pseeFc fusion protein was also secreted and detected in the culture supernatants of both cell types. Figure 18. Expression of 1OIP3AIl in 300.19 cells following retroviral-mediated gene delivery. 300.19 cells were transduced with the pSRa retroviral vector encoding the IOP3AI I gene. Following selection with neomycin, the cells were expanded and RNA was extracted. A Northern blot with 10 pg of total RNA/lane was probed with the 101P3AI I sequence. Size standards in kilobases (kb) are indicated on the side. Results showed expression of the OIP3A1 1 transcript driven from the retroviral LTR. LAPC-4AD and LAPC-9AD showed expression of the endogenous 101P3AI I transcript. The figure shows results of a short exposure of the autoradiogram. Figures 19A-19C. Secondary structure and transmembrane prediction for 101P3AI11. Figure 19A: The secondary structure of IOIP3AI I protein was predicted using the HNN - Hierarchical Neural Network method (Guermeur, 1997, http://pbil.ibcp.fr/cgi-bin/npsa-automat.pl?page=npsann.html), accessed from the ExPasy molecular biology server (http://www.expasy.ch/tools/. This method predicts the presence and location of alpha helices, extended strands, and random coils from the primary protein sequnce. The percent of the protein in a given secondary structure is also given. Figure 19B is a schematic representation of the probability of existence of transmembrane regions and orientation of 1OlP3AI I based on the TMpred algorithm of Hofmann and Stoffel 9 which utilizes TMBASE (K. Hofmann, W. Stoffel. TMBASE - A database of membrane spanning protein segments Biol. Chem. Hoppe-Seyler 374:166, 1993). Figure 19C is a schematic representation of the probability of the existence of transmembrane regions and the extracellular and intracellular orientation of 101P3AI I based on the TMHMM algorithm of Sonnhanmer, 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. 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 (http://www.expasy.ch/tools/). The results of the transmembrane prediction programs presented in Figure 19B and 19C depict 10 P3A 11 as containing 7 transmembrane domains consistent with that of a G-protein coupled receptor. Figure 20. Expression of 1OP3AI 1 in NIH-3T3 Tumors. Mice were injected subcutaneously with control 3T3-neo or NIH3T3 cells expressing 101 P3A 11. Tumors were allowed to grow, the mice were then sacrificed and tumors harvested. RNA was isolated from LAPC-4AD and LAPC-4AI xenografts, 3T3-neo and 3T3-101P3AI I cells grown in culture were used as controls. RNA isolated from six different tumors derived from 3T3- 10 IP3A 11 cells (Tumor # 1-3) were compared by Northern blotting. Northern blots with 10 pg of total RNA/lane were probed with IOP3AI1 sequence. A picture of the ethidium-bromide staining of the RNA gel is also presented. Results showed expression of OIP3AI I in all 3T3-10IP3AI I tumors as well as in 3T3/10IP3AIl cells used to derive the tumors, but not in the negative control cells 3T3/neo cells. Figure 21. 1OP3AI 1 Induces Tumor Formation of 3T3 Cells. Injection of 106 3T3-neo, 3T3-Ras or 3T3-101P3A I cells (106 of the indicated cells mixed with Matrigel) subcutaneously into 6 male SCID mice (right flank) revealed that 6/6 3T3-vl 2Ras-injected mice formed tumors, 6/6 3T3-10IP3AI I- injected mice formed tumors, and 0/6 3T3-neo-injected mice formed tumors. Each data point represents the mean tumor volume (n = 6) in each group. Figure 22. PTX reduces the in vivo growth of 3T3-101P3AI I Tumors. Pertussis toxin was found to inhibit the sub-cutaneous growth of 3T3-10IP3A I tumors in SCID mice in a dose dependent manner. Figure 23. Alignment of 101P3A 1-PHOR-I (Phor) with the rat GPCR RA1C (gil3420759). Identities = 179/299 (59%), Positives = 231/299 (76%), Gaps = 1/299 (0%). Figure 24. Alignment of IOIP3A 11-PHOR-l (Phor) with the human prostate specific GPCR.(gi113540539). Identities = 179/299 (59%), Positives - 233/299 (77%), Gaps = 1/299 (0%). Figure 25. Alignment of 1OP3AI l-PHOR-1 (Phor) with human olfactory receptor 51112, HORS, (gil14423836). Identities = 163/304 (53%), Positives = 214/304 (69%), Gaps = 1/304 (0%). Figure 26. O1P3Al1 Modulated Tyrosine Phosphorylation inNIH-3T3 Cells. IOIP3Al 1 mediated the de-phosphorylation of proteins at 200, 120-140, 85-90 and 55 kDa. 101P3AI I induced the phosphorylation of proteins at 80 and 29 kDa in NIH-3T3 cells. Figure 27. ERK Phosphorylation by PCR ligands in IOP3AI 1 Expressing Cells. FBS, lipophosphatidic acid, gastrin releasing peptide, leukotriene and platelet activating factor induced the phosphorylation of ERK in 101P3AI 1 expressing cells. Figure 28. Inhibition of IOIP3A 1I-Mediated ERK Activation by PD98059. ERK-phosphorylation was inhibited by a MEK specific(PD98059) but not a p38 specific (SB203580) inhibitor in PC3-10iP3A I I cells. Figure 29. Enhanced ERK Phosphorylation in Sodium Orthovanadate Treated PC3-101P3A II Cells. Sodium orthovanadate induced increased ERK phosphorylation in PC3-101P3AI I cells relative to PC3-neo cells. 10 Figure 30. Inhibition of 101P3AI 1-Mediated ERK Phosphorylation by AG1517. The EGFR inhibitor, AG1517, inhibits EGF-mediated ERK phosphorylation in control and IOIP3AI 1-expressing PC3 cells. AG1517 partially inhibits 101P3A I I mediated ERK phosphorylation in PC3 cells. Figures 31A-31B. Activation of p38 in PC3-10IP3AI 1 Cells. Expression of IOIP3AI I mediates p38 phosphorylation in cells treated with 10% FBS as shown by blotting with antibodies to phospho-p38 (Figure 3 IA) compared to p38 (Figure 3 1 B). Figure 32. IOIP3AI I Induced Accumulation of cAMP in PC3 Cells. Expression of 101P3A1 I increased the accumulation of cAMP in cells treated with 0.1% and 10% FBS. FBS-induced cAMP accumulation in 101P3A1 1 cells was inhibited by pertussis toxin. Figure 33. Pertussis Toxin Inhibits 1OIP3A1 I Mediated ERK Phosphorylation. Pertussis toxin inhibited FBS- mediated ERK phosphorylation in 101P3AI I expressing cells. Figure 34. Pertussis Toxin Inhibited ERK Phosphorylation in PC3-101P3AI I Cells. Pertussis toxin inhibited FBS- mediated ERK phosphorylation in 101P3A1 1 expressing cells. The inhibitory activity of pertussis toxin on ERK phosphorylation was more dramatic in FBS-trcated than EGF or GRP-trcatcd PC3-1011P3A II cells Figure 35. Inhibition of 101P3A 11-mediated signaling by Suranim, a G protein inhibitor. Control NIH 3T3 and 3T3-101P3A 1 cells were grown in the presence of absence of G protein inhibitors Surinam and NF449. Proliferation was analyzed by Alamar blue after 72 hours. Suranim and NF449 inhibited the proliferation of 101P3A II expressing but not control cells. Figures 36A-36B. 1OIP3AI I Mediated ERK Phosphorylation By Conditioned Media. Figure 36A: blotting with anti-phospho ERK antibodies; Figure 36B: blotting with anti-ERK antibodies. Supernatants from PC3, PC3-10IP3A1I, PrEC and LAPC42 cells induce ERK phosphorylation in PC3 IOIP3AI I but not PC3 cells. Supernantants from 3T3 and 293T cells had little specific effect on ERK phosphorylation. Figure 37. 101P3A1I Enhances the Proliferation of 3T3 Cells. Control NIH 3T3 and 3T3-101P3AI I cells were grown in the presence of absence 0.5 or 10% FBS. Proliferation was analyzed by Alamar blue after 48 hours. Expression of 101P3A1 1 induced a 6 fold increase in the proliferation of 3T3 cells grown in 0.5% FBS. Figure 38. Inhibition of 10 P3A 1I Mediated ERK Phosphorylation by IOIP3A 1I Specific Antibodies. Expression of IOP3AI 1 induced ERK phosphorylation in 293T cells. Anti-1OIP3AI I pAb inhibited ERK Phosphorylation in 293T-101P3A II cells. Figure 39. Anti-101P3AI I Ab Mediated cAMP Accumulation in PC3-101P3AI I Cells. Control PC3 cells and cells expressing 1OlP3AI I were treated with anti-IOP3Al I pAb for 2 min and evaluated for intracellular cAMP content. The assay was performed in duplicate. Figures 40A-40F. Photomicrographs showing inmunohistochemical analysis using anti-IOP3A 1I (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded prostate cancer tissues (Figure 40A); anti-101P3A II (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded prostate cancer cell line, LNCaP (Figure 40B); anti-101P3A II (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded prostate cancer tissues (Figure 40C); anti- 101 P3A I I (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded normal prostate (Figure 40D); anti- 101P3A 11 (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded prostate cancer tissues (Figure 40E); and anti-IO1P3Al I (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded normal prostate (Figure 40F). 11 12 Figures 41A-41F. Photomicrographs showing immunohistochemical analysis usinganti-101P3A 11 (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded prostate cancer tissues (Figure 41 A); anti- 101 P3A I I (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded bladder cancer tissues (Figure 41B); anti-101P3AI I 5 (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded kidney cancer tissues (Figure 41C); anti-10 1 P3A 1 I (peptide 1; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded colon cancer tissues (Figure 41 D); anti- 10 1 P3A 11 (peptide I; amino acids 1-14) rabbit polyclonal antibody on formalin fixed and paraffin embedded lung cancer tissues (Figure 41 E); and anti-101P3AI I (peptide 1; amino acids 1-14) rabbit polyclonal antibody 10 on formalin fixed and paraffin embedded breast cancer tissues (Figure 41 F). Figure 42 shows that 101P3AI I induces orthotopic growth of tumors. 5x10 5 cells were injected orthotopically into SCID mice, 7 mice per group; tumor weight was evaluated 24-25 days post cell injection. Figure 43 shows that 101P3A 1I induces colony formation in a soft agar assay. 15 Figure 44 Schematic of 101P3AI I Gene Variants. Figure 45 Schematic of 101P3A 1I Proteins Variants. Figure 46 Exon Map. Figure 47: Recognition of PHOR-1 protein in transfected 293T cells by sera from GST-PHOR 1 immunized mice. 20 Figure 48: Data showing that four hybridomas reactive to MBP-PHOR-l exhibited strong specific reactivity to PHOR-l protein expressed in cells. This was demonstrated by Western analysis of 293T cells transfected with the epitope tagged PHOR-I cDNA Figure 49: Mouse polyclonal antibodies raised to amino acids 1-23 detect PHOR-I expressed in 293T cells 25 Figure 50: Inhibition of ERK Phosphorylation by GPCR Inhibitors Figure 51: Inhibition of PC3 Proliferation by GPCR Inhibitors Figure 52: Inhibition of PC3-AGS-3 Proliferation by PTX Figure 53: AGS-3 Enhances Proliferation of 3T3 and PC3 Cells Figure 54: AGS-3 Induces in Vivo Tumor Formation of 3T3 Cells 30 Figure 55: Inhibition of 3T3-AGS-3 Tumor Formation by PTX Figure 56: AGS-3 Induces the Orthotopic Growth of 3T3 Tumors Figure 57: AGS-3 Enhances Orthotopic Growth of PC3 Cells Figure 58: Partial Inhibition of 3T3-AGS-3 Tumor Formation by Suramin Figure 59: AGS-3 Induces Intratibial Tumor Growth of 3T3 Cells 35 Figure 60: AGS-3 Enhances Intratibial Tumor Growth of PC3 Cells Figure 61: Inhibition of AGS-3 Mediated ERK Phosphorylation by AGS-3 Specific Antibodies 13 Figure 62: AGS-3 Enhances Cell Cycle Entry of 3T3 and PC3 Cells Figure 63: Anti-AGS3 Staining of MDCK Cells Figure 64: Nucleic Acid Alignments Figure 65: Expression and detection of 101P3A I .GFP fusion protein. The 5 pcDNA3.1/101P3A 1 l.GFP vector was constructed. 293T cells were transfected with either the pcDNA3.1/10IP3AI l.GFP recombinant expression vector (A), pcDNA3.1/GFP vector (B) or control pcDNA3.1 vector (C). Cells were harvested 24 hours later and analyzed by microscopy for detection of green fluorescence. Results show expression of the 10 lP3Al I.GFP fusion protein is localized mostly at the cell membrane, whereas expression of the free GFP is throughout the cells. The control vector did 10 not show any fluorescence. We conclude that the 10 lP3AI I.GFP fusion protein is expressed from the pCDNA3.1/101P3AI I.GFP construct, and that the fusion protein is localized at the cell membrane. Figure 66 The cDNA and amino acid sequence of the open reading frames of codon optimizedsl0lP3Al I v. (A) and slO P3A1 I v.3(B). Figure 67 Expression and detection of codon optimized sI0lP3A l1.GFP fusion protein. The 15 pcDNA3.l/sl0lP3A 1.GFP vector for codon optimized I0lP3A1 I was constructed. 293T cells were transfected with either pcDNA3.1 vector control (light line), or one of the three different pcDNA3.l/sl0lP3Al 1.GFP vector clones, 1G2, 2G3, or 3H5 (dark line). Cells were harvested 24 hours later and either analyzed directly for green fluorescence (A), or stained viably using polyclonalanti 101P3AI I antibody (B) and analyzed by flow cytometry. Results show strong expression of the codon 20 optimized PHOR-1.GFP fusion protein at the cell surface. DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions 25 II.) 101P3A11 Polynucleotides II.A.) Uses of 101P3A1I Polynucleotides II.A.1.) Monitoring of Genetic Abnormalities II.A.2.) Antisense Embodiments II.A.3.) Primers and Primer Pairs 30 II.A.4.) Isolation of 101P3A11-Encoding Nucleic Acid Molecules II.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems III.) 101P3AI1-related Proteins III.A.) Motif-bearing Protein Embodiments III.B.) Expression of 101P3A11-related Proteins 35 III.C.) Modifications of 101P3A11-related Proteins III.D.) Uses of 101 P3A11-related Proteins 13A IV.) 101P3All Antibodies V.) 101P3Al1 Cellular Immune Responses VI.) 101P3AlI Transgenic Animals VII.) Methods for the Detection of 101P3A11 5 VIII.) Methods for Monitoring the Status of 1OP3AI-related Genes and Their Products IX.) Identification of Molecules That Interact With 1OP3A11 X.) Therapeutic Methods and Compositions X.A.) Anti-Cancer Vaccines X.B.) 101P3AI I as a Target for Antibody-Based Therapy 10 X.C.) 101P3AII as a Target for Cellular Immune Responses X.C.I. 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 X.E.) Administration of Vaccines for Therapeutic or Prophylactic Purposes XI.) Diagnostic and Prognostic Embodiments of IO1P3A1I. XII.) Inhibition of 101P3A11 Protein Function XII.A.) Inhibition of 1O1P3AIl With Intracellular Antibodies XII.B.) Inhibition of 101P3AI1 with Recombinant Proteins XII.C.) Inhibition of O11P3A11 Transcription or Translation XI.D.) General Considerations for Therapeutic Strategies XIII.) KITS/Articles of Manufacture XIV.) Evaluation of GPCRs and Modulators Thereof XV.) Screening of Candidate Compounds XVI.) GPCR Fusion Proteins I.) 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 clarity 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 include stage C disease under the American Urological Association (AUA) system, stage CI - C2 disease under the Whitnore-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 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 vesicles. "Altering the native glycosylation pattern" is intended for purposes herein to mean deleting one or more carbohydrate moieties found in native sequence 1OlP3A 11 (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 14 sites that are not present in the native sequence 101P3A 11. In addition, the phrase includes 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 1OIP3A 1-related protein). For example an analog of a 10lP3AI I protein can be specifically bound by an antibody orT cell that specifically binds to I0lP3A1 1. 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-IOIP3AI I antibodies comprise monoclonal and polyclonal antibodies as well as fragments containing the antigen-binding domain and/or one or more complementarity 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-IOIP3A 1I antibodies and clones thereof (including agonist, antagonist and neutralizing antibodies) and anti 101P3Al I 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%. Nucleotide sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exon/intron 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." 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, fungal, plant or animal origin, including fragments and/or variants thereof. Examples of cytotoxic agents include, but are not limited to maytansinoids, yttrium, bismuth, ricin, ricin A-chain, doxorubicin, daunorubicin, taxol, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dine, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE40, 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 Ae", 1131, Im, Y9, Re" 6 , Re', SmIS, Bi 2 n, P 2 and radioactive isotopes of Lu. Antibodies may also be conjugated to an anti-cancer pro-drug activating enzyme capable of converting the pro-drug to its active form. 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 "H LA" is a human class I or class I Major Histocompatibility Complex (MHC) protein (see, e.g., Stites, et aL., IMMUNOLOGY, 8"' ED., 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% formamidc/6XSSC/0.1% SDS/100 pg/mI ssDNA, in which tempcraturcs for hybridization arc above 37 degrees C and temperatures for washing in 0.IXSSC/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 15 in atlcordance with the invention preferably do not contain materials normally associated with the peptides in their in situ environment. For example, a polynucleotide is said to be "isolated" when it is substantially separated from contaminant polynucleotides that correspond or are complementary to genes other than the I01P3AI 1 genes or that encode polypeptides other than 10OP3A1 I gene product or fragments thereof. A skilled artisan can readily employ nucleic acid isolation procedures to obtain an isolated 101 P3A I1 polynucleotide. A protein is said to be "isolated," for example, when physical, mechanical or chemical methods are employed to remove the 101P3AI I proteins from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated 1OIP3AI I 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 oflen 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 "monoclonal 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 10 lP3AI I-related protein, refers to any pattern 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 lILA allele and differ in the pattem of the primary and secondary anchor residues. A "pharmaceutical excipient" 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. 16 The term "polynucleotide" means a polymeric form of nucleotides of at least 10 bases or base pairs in length, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide, and is meant to include 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 disclosed 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. In another embodiment, for example, the primary anchor residues of a peptide that will bind an HLA class 11 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. A "recombinant" DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vitro. Non-limiting examples of small molecules include compounds that bind or interact with 10 IP3A 11, ligands including hormones, neuropeptides, chemokines, odorants, phospholipids, and functional equivalents thereof that bind and preferably inhibit 10 I P3A I I 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, 101P3AI I protein; are not found in naturally occuITing 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 17 hybridization reactions, see Ausubel el 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 50*C; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v/v) 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 *C; 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 *C, with washes at 42*C in 0.2 x SSC (sodium chloride/sodium citrate) and 50% formamide at 55 *C, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55 *C. "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 overnight incubation at 37*C 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 Denhardt's solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in I x SSC at about 37-50*C. 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. 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 cellular 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 II 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. 18 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 OIP3AI 1 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 "IOP3AI 1-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 IOIP3A1l I proteins or fragments thereof, as well as fusion proteins of a 101P3A1 I protein and a heterologous polypeptide are also included. Such IOIP3A 1I proteins are collectively referred to as the IOP3A 1-related proteins, the proteins of the invention, or IOP3Al 1. The term "101P3A1 I related protein" refers to a polypeptide fragment ora IOIP3AI I 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, 30,35, 40,45, 50, 55, 60, 65, 70, or 317 or 318 or more amino acids. "Active ingredient" in the context of a "Pharmaceutical Composition" shall mean a component of a Pharmaceutical Composition that provides the primary pharmaceutical benefit, as opposed to an "inactive ingredient" which would generally be recognized as providing no pharmaceutical benefit. "Agonists" shall mean moietics that activate the intracellular response when they bind to the receptor, or enhance GTP binding to membranes. In the context of the disclosed invention, a Pharmaceutical Candidate comprising a 101P3A 1I Agonist can be utilized for affecting metabolism. "Partial agonists" shall mean moieties that activate the intracellular response when they bind to the receptor to a lesser degree/extent than do agonists, or enhance GTP binding to membranes to a lesser degree/extent than do agonists. "Antagonist" shall mean moieties that competitively bind to the receptor at the same site as the agonists but which do not activate the intracellular response initiated by the active form of the receptor, and can thereby inhibit the intracellular responses by agonists or partial agonists. Antagonists do not diminish the baseline intracellular response in the absence of an agonist or partial agonist. "Candidate compound," in the context of the disclosed invention, shall mean a small molecule that is amenable to a screening technique. "Composition" shall having a meaning in accordacne with standard use. For example, a composition can mean a material comprising at least two compounds, components or substituents; for example, and not limitation, a Pharmaceutical Composition comprising at least one Active Ingredient and at least one other component. "Compound efficacy" shall mean a measurement of the ability of a compound to inhibit or stimulate receptor functionality, as opposed to receptor binding affinity. "Constitutive receptor activation" shall mean stabilization of a receptor in the active state by means other than binding of the receptor with its endogenous ligand or a chemical equivalent thereof. "Contact" or "contacting" shall mean bringing at least two moieties together, whether in an in vitro system or an in vivo system. "Endogenous" shall mean a material that a mammal naturally produces. Endogenous in reference to, for example and not limitation, the term "receptor" shall mean that which is naturally produced by a mammal (for example, and not limitation, a human), yeast, bacterium or a virus. In contrast, the term "non-endogenous" in this context shall mean that which is not naturally produced by a mammal (for example, and not limitation, a human) yeast, bacterium or a viims. For example, and not limitation, a receptor which is not constitutively active in its 19 20 endogenous form, but when manipulated becomes constitutively active, is most preferably referred to herein as a "non-endogenous, constitutively activated receptor." Both terms can be utilized to describe both "in vivo" and "in vitro" systems. For example, and not a limitation, in a screening approach, the endogenous or non-endogenous receptor may be in reference to an in vitro screening system. As a 5 further example and not limitation, where the genome of a mammal has been manipulated to include a non-endogenous constitutively activated receptor, screening of a candidate compound by means of an in vivo system is viable. "G protein coupled receptor fusion protein" and "GPCR fusion protein," in the context of the invention disclosed herein, each mean a non-endogenous protein comprising an endogenous, 10 constitutively activated orphan GPCR fused to at least one G protein, most preferably, the alpha (a) subunit of such G protein (this being the subunit that binds GTP), with the G protein preferably being of the same type as the G protein that naturally couples with endogenous orphan GPCR. For example, and not limitation, in an endogenous state, the G protein "Gsa" is the predominate G protein that couples with 10 IP3AI I such that a GPCR Fusion Protein based upon 10 1P3AI I would be a non-endogenous protein 15 comprising 101P3AI 1 fused to Gscc. The G protein can be fused directly to the c-terminus of the endogenous, constitutively active orphan GPCR or there may be spacers between the two. "Inhibit" or "inhibiting", in relationship to the term "response" shall mean that a response is decreased or prevented in the presence of a compound as opposed to in the absence of the compound. "Inverse agonists" shall mean moieties that bind the endogenous form of the receptor, and which 20 inhibit the baseline intracellular response initiated by the active endogenous form of the receptor below the normal base level of activity that is observed in the absence of the endogenous ligand, agonists or partial agonists, or decrease GTP binding to membranes. Preferably, the baseline intracellular response is decreased in the presence of the inverse agonist by at least 30%, more preferably by at least 50%, and most preferably by at least 75%, as compared with the baseline response in the absence of the inverse 25 agonist. Biologically, "I01P3AI 1 inverse agonist" shall mean moieties that can be assessed in vivo by factors other than just determination that the moiety has interacted with 101 P3A 11. "Ligand" shall mean an endogenous, naturally occurring molecule specific for an endogenous, naturally occurring receptor. "Pharmaceutical composition" shall mean a composition comprising at one Active Ingredient 30 and at least one ingredient that is not an Active Ingredient (for example and not limitation, a filler, dye, or a mechanism for slow release), whereby the composition is amenable to investigation for a specified, efficacious outcome in a mammal or in cells thereof such as in vitro (e.g., without limitation, the mammal is a human). Those of ordinary skill in the art will understand and appreciate the techniques appropriate for determining whether an active ingredient has a desired efficacious outcome based upon 35 the needs of the artisan.

20A "Small molecule", in the context of the invention disclosed herein, is a non- protein based moiety; for example, and not limitation, NF449is a small molecule within the context of this invention. In a preferred embodiment, the endogenous ligand for a receptor is not a "small molecule." Throughout this specification the word "comprise", or variations such as "comprises" or 5 "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. 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 10 invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed before the priority date of each claim of this application. II.) 101P3A1 Polynucleotides 15 One aspect of the invention provides polynucleotides corresponding or complementary to all or part of a 101P3AI I gene, mRNA, and/or coding sequence, preferably in isolated form, including polynucleotides encoding a 101 P3A Il-related protein and fragments thereof, DNA, RNA, DNA/RNA hybrid, and related molecules, polynucleotides or oligonucleotides complementary to a IOIP3AI I gene or mRNA sequence or a part thereof, and polynucleotides or oligonucleotides that hybridize to a IOIP3AI1 gene, mRNA, or to a IOIP3AI1 encoding polynucleotide (collectively, "101P3A1 I polynucleotides"). In all instances when referred to in this section, T can also be U in Figure 2. Embodiments of a 101 P3AI I polynucleotide include: a 101P3A I I polynucleotide having the sequence shown in Figure 2, the nucleotide sequence of 101P3AI 1 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polynucleotide 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 101P3A 1 nucleotides comprise, without limitation: (1) a polynucleotide comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2, wherein T can also be U; (II) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 130 through nucleotide residue number 1086, optionally including the last, stop codon, wherein T can also be U; (III) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 133 through nucleotide residue number 1086, optionally including the last, stop codon, wherein T can also be U; (IV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2B, from nucleotide residue number 130 through nucleotide residue number 348, optionally including the last, stop codon, wherein T can also be U; (V) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2B, from nucleotide residue number 133 through nucleotide residue number 348, optionally including the stop codon, wherein T can also be U; (VI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2C, from nucleotide residue number 130 through nucleotide residue number 1086, optionally including the last, stop codon, wherein T can also be U; (VII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2C, from nucleotide residue number 133 through nucleotide residue number 1086, optionally including the last, stop codon, wherein T can also be U; (VIII) a polynucleotide that encodes a 101P3A Il-related protein that is at least 90% homologous to an entire amino acid sequence shown in Figure 2A-C; 21 (IX) a polynucleotide that encodes a 101P3A II-related protein that is at least 90% identical to an entire amino acid sequence shown in Figure 2A-C; (X) a polynucleotide that encodes at least one peptide set forth in Tables V-XVIII and XXII to IL, optionally with a proviso that the polynucleotide is not a contiguous sequence from a nucleic acid sequence of Figure 2; (XI) a polynucleotide that encodes at least two peptides seleected from the peptides set forth in Tables V-XVIII and XXII to IL, optionally with a proviso that the polynucleotide is not a contiguous sequence from a nucleic acid sequence of Figure 2; (XII) a polynucleotide that encodes at least two peptides selected from the peptides set forth in Tables V-XVIII and XXII to IL, optionally with a proviso that the polynucleotide is not a contiguous sequence from a nucleic acid sequence of Figure 2; (XIII) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XIV) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XV) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XVI) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XVII) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figure 9; (XVIII) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3B in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XIX) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3B in any whole number increment up to 317 or 318 that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6; 22 23 (XX) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3B in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XXI) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 5 3B in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XXII) a polynucleotide that encodes a peptide region of at least 5 amino acids of a peptide of Figure 3B in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figure 9; 10 (XXIII) a polynucleotide that encodes monoclonal antibody or binding region thereof secreted by a hybridoma entitled X18(1)4 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110-2209 USA) as Accession No. ATCC-PTA-4351 on 15 May 2002; (XXIV) a polynucleotide that encodes monoclonal antibody or binding region thereof secreted by a hybridoma entitled X 18(1)10 deposited with American Type Culture Collection (ATCC; 10801 University 15 Blvd., Manassas, VA 20110-2209 USA) as Accession No. ATCC-PTA-4352 on 15 May 2002; (XXV) a polynucleotide that encodes monoclonal antibody or binding region thereof secreted by a hybridoma entitled X18(1)23 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110-2209 USA) as Accession No. ATCC-PTA-4353 on 15 May 2002; (XXVI) a polynucleotide that encodes monoclonal antibody or binding region thereof secreted by a 20 hybridoma entitled X18(4)7 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110-2209 USA) as Accession No. ATCC-PTA-4354 on 15 May 2002; (XXVII) a polynucleotide that is fully complementary to a polynucleotide of any one of (I)-(XXVI); and, (XXVIII) a peptide that is encoded by any of (I)-(XXVI); 25 (XXIX) a peptide that occurs at least twice in Tables V-XVIII and XXII to IL collectively, or an oligonucleotide that encodes such HLA peptide; (XXX) a peptide that occurs at least once in Tables V-XVIII and at least once in tables XXII to IL, or an oligonucleotide that encodes such HLA peptide; (XXXI) a peptide which comprises peptide regions, or an oligonucleotide encoding the peptide, that 30 has one two, three, four, or five of the following characteristics: 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, 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of Figure 5; 35 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 Figure 6; 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 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 Figure 7; 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 Figure 8; 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 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 Figure 9; (XXXII)a polynucleotide of any of (1)-(XXVII) or peptide of (XXVII)-(XXXI) together with a pharmaceutical excipient and/or in a human unit dose form. As used herein, a range is understood to specifically disclose all whole unit positions thereof. Typical embodiments of the invention disclosed herein include 101P3A II polynucleotides that encode specific portions of 10 1P3A 11 mnRNA 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, 80, 85, 90., 95, 100, 125, 150, 175, 200, 225, 250, 375, 300 or 317 or 318 contiguous amino acids of O1P3AI 1. For example, representative embodiments of the invention disclosed herein include: polynucleotides and their encoded peptides themselves encoding about amino acid I to about amino acid 10 of the 10 lP3A 11 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 10 to about amino acid 20 of the 1OP3AI I protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 20 to about amino acid 30 of the lOlP3Al I protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 30 to about amino acid 40 of the 101 P3A II protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 40 to about amino acid 50 of the 101P3AI I protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 50 to about amino acid 60 of the 1OlP3AI 1 protein shown in Figure 2 or Figure 3, or polynucleotides encoding about amino acid 60 to about amino acid 70 or amino acid 317 or 318 of the OIP3A 1I protein shown in Figure 2 or Figure 3. Accordingly polynucleotides encoding portions of the amino acid sequence (of about 10 amino acids), of amino acids 1 through the carboxyl terminal amino acid of the lOIP3AI I protein arc 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 101P3AI I protein are also within the scope of the invention. For example, polynucleotides encoding from about amino acid 1 (or 20 or 30 or 40 etc.) to about 24 amino acid 20, (or 30, or 40 or 50 etc.) of the 101P3AI I protein "or variant" shown in Figure 2 or Figure 3 can be generated by a variety of techniques well known in the art. These polynucleotide fragments can include any portion of the 101P3AI I sequence as shown in Figure 2. Additional illustrative embodiments of the invention disclosed herein include 101P3AI I polynucleotide fragments encoding one or more of the biological motifs contained within a IOP3A 1I protein "or variant" sequence, including one or more of the motif-bearing subsequences of a lOIP3A1 I protein "or variant" set forth in Tables V-XVIII and XXII to IL. In another embodiment, typical polynucleotide fragments of the invention encode one or more of the regions of 101P3AI I 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 IOIP3A1 1 protein or variant N-glycosylation sites, cAMP and cGMP-dependent protein kinase phosphorylation sites, casein kinase II phosphorylation sites or N-myristoylation site and amidation sites. Note that to determine the starting position of any peptide set forth in Tables V-XVIII and Tables XXII to IL (collectively 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 LVII. 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 LLII. Accordingly if a Search Peptide begins at position "X", one must add the value "X minus 1" to each position in Tables V-XVIH and Tables XXII-IL to obtain the actual position of 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 IO1P3A1I Polynucleotides II.A.1.) Monitoring of Genetic Abnormalities The polynucleotides of the preceding paragraphs havd a number of different specific uses. The human 10 IP3A 11 gene maps to the chromosomal location set forth in the Example entitled "Chromosomal Mapping of 101P3AI 1." For example, because the 101P3AI 1 gene maps to this chromosome, polynucleotides that encode different regions of the 101P3A 11 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 bccn identified as frequent cytogenetic abnormalities in a number of different cancers (see e.g. Krajinovic et al., Mutat. Res. 382(3-4): 81-83 (1998); Johansson et al., Blood 86(10): 3905-3914 (1995) and Finger et al., P.N.A.S. 85(23): 9158-9162 (1988)). Thus, polynucleotides encoding specific regions of the 101 P3A 11 proteins provide new tools that can be used to delineate, with greater precision than previously possible, cytogenetic abnormalities in the chromosomal region that encodes 101P3AI 1 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 al., Am. J. Obstet. Gynecol 171(4): 1055-1057 (1994)). Furthermore, as 101 P3A II was shown to be highly expressed in bladder and other cancers, 101 P3A 11 polynucleotides are used in methods assessing the status of 101P3A II gene products in normal versus cancerous tissues. Typically, polynucleotides that encode specific regions of the 101P3A 11 proteins are used to assess the 25 presence of perturbations (such as deletions, insertions, point mutations, or alterations resulting in a loss of an antigen etc.) in specific regions of the IO1P3AI I 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 c al., J. Cutan. Pathol. 26(8): 369-378 (1999), both of which utilize polynucleotides encoding specific regions of a protein to examine 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 nucleic 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 1OIP3AI 1. 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 classes of nucleic acid molecules using the 101 P3A 11 polynucleotides and polynucleotide sequences disclosed herein. Antisense technology entails the administration of exogenous oligonucleotides 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., 101P3A 11. See for example, Jack Cohen, Oligodeoxynucleotides, Antisense Inhibitors of Gene Expression, CRC Press, 1989; and Synthesis 1:1-5 (1988). The 10 IP3A II antisense oligonucleotides 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 oligonucleotide (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 O-oligos with 3H-1,2-benzodithiol-3 one-1,I-dioxide, which is a sulfur transfer reagent. See, e.g., lycr, R. P. et al., J. Org. Chem. 55:4693-4698 (1990); and lyer, R. P. el al., J. Am. Chem. Soc. 112:1253-1254 (1990). Additional 1IP3AI I antisensc oligonucleotides of the present invention include morpholino antisense oligonucleotides known in the art (see, e.g., Partridge et a., 1996, Antisense & Nucleic Acid Drug Development 6: 169-175). The OIP3A 1I antisense oligonucleotides of the present invention typically can be RNA or DNA that is complementary to and stably hybridizes with the first 100 5' codons or last 100 3' codons of a 10IP3AI 1 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 I0IP3A1 I mRNA and not to mRNA specifying other regulatory subunits of protein kinase. In one embodiment, 10lP3A1I1 antisense oligonucleotides of the present invention are 15 to 30-mer fragments of the antisense DNA molecule that have a sequence that hybridizes to 101P3AI I mRNA. Optionally, 101P3A II antisense oligonucleotide is a 30-mer oligonucleotide that is complementary to a region in the first 10 5' codons or last 10 3' codons of 101P3A 11. Alternatively, the antisense molecules are modified to employ ribozymes in the inhibition of 101P3AI 1 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 this nucleotides of the invention include primers and primer pairs, which allow the specific amplification of polynucleotides of the invention or of any specific parts thereof, and 26 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 lOIP3AI 1 polynucleotide in a sample and as a means for detecting a cell expressing a 101P3AI I protein. Examples of such probes include polypeptides comprising all or part of the human 10lP3AI I cDNA sequence shown in Figure 2. Examples of primer pairs capable of specifically amplifying 101P3AI 1 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 101P3AI I mRNA. The 101P3AI I 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 101 P3A 1I 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 10 IP3AI I polypeptides; as tools for modulating or inhibiting the expression of the IOIP3AI I genc(s) and/or translation of the IOIP3AI I transcript(s); and as therapeutic agents. The present invention includes the use of any probe as described herein to identify and isolate a 10 IP3A II or 10IP3AI I related nucleic acid sequence from a naturally occurring source, such as humans or other mammals, as well as the isolated nucleic acid sequence per se, which would comprise all or most of the sequences found in the probe used. I.A.4.) Isolation of 10IP3A11-Encoding Nucleic Acid Molecules The 101P3AI I cDNA sequences described herein enable the isolation of other polynucleotides encoding 101P3AI I gene product(s), as well as the isolation of polynucleotides encoding 10 1P3AI I gene product homologs, alternatively spliced isoforms, allelic variants, and mutant forms of a IOIP3A II gene product as well as polynucleotides that encode analogs of IOP3A 1-related proteins. Various molecular cloning methods that can be employed to isolate full length cDNAs encoding a IOIP3Al I 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 101P3A 1 gene cDNAs can be identified by probing with a labeled 10IP3AI 1 cDNA or a fragment thereof. For example, in one embodiment, a 101P3AI I cDNA (e.g., Figure 2) or a portion thereof can be synthesized and used as a probe to retrieve overlapping and full-length cDNAs corresponding to a OIP3AI Igene. A IOIP3A 1I gene itself can be isolated by screening genomic DNA libraries, bacterial artificial chromosome libraries (BACs), yeast artificial chromosome libraries (YACs), and the like, with IOP3AI I DNA probes or primers. D.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems The invention also provides recombinant DNA or RNA molecules containing a IOIP3Al I 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 transfected with such recombinant DNA or RNA molecules. Methods for generating such molecules are well known (see, for example, Sambrook et al., 1989, supra). 27 The invention further provides a host-vector system comprising a recombinant DNA molecule containing a IOP3Al I polynucleotide, fragment, analog or homologue thereof within a suitable prokaryotic or eukaryotic 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 TsuPrl, 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 101P3AI 1 or a fragment, analog or homolog thereof can be used to generate 101P3AI I 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 101P3A II 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 arc 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, 10IP3A1 I can be expressed in several prostate cancer and non-prostate cell lines, including for example 293, 293T, rat-I, NIH 3T3 and TsuPrl. The host-vector systems of the invention are useful for the production of a OIP3AI I protein or fragment thereof. Such host-vector systems can be employed to study the functional properties of IOP3A1 1 and 101P3A 1I mutations or analogs. Recombinant human 101 P3A 11 protein or an analog or homolog or fragment thereof can be produced by mammalian cells transfected with a construct encoding a 10 1P3A Il-related nucleotide. For example, 293T cells can be transfected with an expression plasmid encoding 1OP3AI 1 or fragment, analog or homolog thereof, a 101P3A II-related protein is expressed in the 293T cells, and the recombinant 101P3AI I protein is isolated using standard purification methods (e.g., affinity purification using anti-101P3AI I antibodies). In another embodiment, a 101P3AI I coding sequence is subcloned into the retroviral vector pSRaMSVtkneo and used to infect various mammalian cell lines, such as NIH 3T3, TsuPrl, 293 and rat-I in order to establish 10 1P3A II 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 101 P3A 11 coding sequence can be used for the generation of a secreted form of recombinant 101P3A II protein. As discussed herein, redundancy in the genetic code permits variation in 10 IP3Al I 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 www.dna.affrc.go.jp/~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 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 28 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)). Il.) 101P3AI1-related Proteins Another aspect of the present invention provides 101 P3A I I-related proteins. Specific embodiments of 101P3A 1 proteins comprise a polypeptide having all or part of the amino acid sequence of human 101P3AI I as shown in Figure 2 or Figure 3. Alternatively, embodiments of 10 1 P3A 11 proteins comprise variant, homolog or analog polypeptides that have alterations in the amino acid sequence of 10P3A1 1 shown in Figure 2 or Figure 3. Embodiments of a 101 P3AI 1 polynucleotide include: a 101 P3A II polynucleotide having the sequence shown in Figure 2, the nucleotide sequence of 101P3A II as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polynucleotide 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 101 P3A 11 nucleotides comprise, without limitation: (I) an protein comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2; (II) a 101P3A 1-related protein that is at least 90% homologous to an entire amino acid sequence shown in Figure 2A-C; (III) a 101P3A 1I-related protein that is at least 90% identical to an entire amino acid sequence shown in Figure 2A-C; (IV) a protein that comprises at least one peptide set forth in Tables V-XVIII or Tables XXII to IL, 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 V-XVIII, collectively, which peptide is also set forth in Tables XXII to IL, 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 V XVIII and XXII to IL, 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 V XVIII and XXII to IL, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (VIII) a protein that comprises at least one peptide selected from the peptides set forth in Tables V XVIII; and at least one peptide set forth in Tables XXII to IL, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; 29 30 (IX) a polypeptide comprising at least 5 amino acids of a protein of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (X) a polypeptide comprising at least 5 amino acids of a protein of Figure 3A or 3C in any whole 5 number increment up to 317 or 318 that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure6; (XI) a polypeptide comprising at least 5 amino acids of a protein of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; 10 (XII) a polypeptide comprising at least 5 amino acids of a protein of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XIII) a polypeptide comprising at least 5 amino acids of a protein of Figure 3A or 3C in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the 15 Beta-turn profile of Figure 9; (XIV) a polypeptide comprising at least 5 amino acids of a protein of Figure 3B in any whole number increment up to 72 that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XV) a polypeptide comprising at least 5 amino acids of a protein of Figure 3 in any whole number 20 increment up to 72 that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XVI) a polypeptide comprising at least 5 amino acids of a protein of Figure 3 in any whole number increment up to 72 that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; 25 (XVII) a polypeptide comprising at least 5 amino acids of a protein of Figure 3 in any whole number increment up to 72 that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XVIII) a polypeptide comprising at least 5 amino acids of a protein of Figure 3 in any whole number increment up to 72 that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile 30 of Figure 9; (XIX) a monoclonal antibody or binding region thereof secreted by a hybridoma entitled X18(1)4 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110 2209 USA) as Accession No. ATCC-PTA-4351 on 15 May 2002; 31 (XX) a monoclonal antibody or binding region thereof secreted by a hybridoma entitled X18(1)10 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110 2209 USA) as Accession No. ATCC-PTA-4352 on 15 May 2002; (XXI) a monoclonal antibody or binding region thereof secreted by a hybridoma entitled Xl18(1)23 5 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110 2209 USA) as Accession No. ATCC-PTA-4353 on 15 May 2002; (XXII) a monoclonal antibody or binding region thereof secreted by a hybridoma entitled X18(4)7 deposited with American Type Culture Collection (ATCC; 10801 University Blvd., Manassas, VA 20110 2209 USA) as Accession No. ATCC-PTA-4354 on 15 May 2002; 10 (XXIII) a peptide that occurs at least twice in Tables V-XVIII and XXII to IL, collectively; (XXIV) a peptide that occurs at least once in Tables V-XVIII, and at least once in tables XXII to IL; (XXV) a peptide which comprises one two, three, four, or five of the following characteristics, or an oligonucleotide encoding such peptide: i) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number 15 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 Figure 5; 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 an amino acid position having a value 20 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 Figure 6; iii) 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 tol .0, in the Percent Accessible Residues 25 profile of Figure 7; iv) 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 Average Flexibility profile of Figure 8; or, 30 v) 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 tol.0, in the Beta-turn profile of Figure 9; (XXVI) a peptide of (I)-(XXV) together with a pharmaceutical excipient and/or in a human unit dose 35 form. As used herein, a range is understood to specifically disclose all whole unit positions thereof.

Typical embodiments of the invention disclosed herein include 101 P3A I I polynucleotides that encode specific portions of IOIP3A1 I 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, or 317 or 318 contiguous amino acids of O10P3Al 1. In general, naturally occurring allelic variants of human 101P3AI I protein share a high degree of structural identity and homology (e.g., 90% or more homology). Typically, allelic variants of a IOIP3AI I protein contain conservative amino acid substitutions within the 10 1P3AI 1 sequences described herein or contain a substitution of an amino acid from a corresponding position in a homologue of IO1P3AlI. One class of IOIP3AI I allelic variants are proteins that share a high degree of homology with at least a small region of a particular 101P3AlI1 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 paralogy 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 II. Conservative amino acid substitutions can frequently 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, or 15 conservative substitutions. Such changes include substituting any of isoleucine (I), valine (V), and leucine (L) for any other of these hydrophobic amino acids; aspartic 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. Table Ill herein; pages 13-15 "Biochemistry" 2"' 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 disclosed herein include a wide variety of art-accepted variants or analogs of IOIP3A1I proteins such as polypeptides having amino acid insertions, deletions and substitutions. IOP3AII 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 aL., Nucl. Acids Res., 13:4331 (1986); Zoller et aL., Nucl. 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 101P3A II 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, serine, 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 32 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 isosteric amino acid can be used. As defined herein, 101P3A I 1 variants, analogs or homologs, have the distinguishing attribute of having at least one epitope that is "cross reactive" with a 101P3A II 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 101 P3AI I variant also specifically binds to a 10 1 P3AI I 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 I01P3AI I 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 at., Mol Immunol (1989) 26(9):865-73; Schwartz et al., J Immunol (1985) 135(4):2598-608. Other classes of 10IP3Al 1-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 101P3AI 1 protein variants or analogs comprise one or more of the 101 P3A 11 biological motifs described herein or presently known in the art. Thus, encompassed by the present invention are analogs of 101 P3A 11 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 101P3AI I 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 101P3A 1 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 101 P3A I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 10 to about amino acid 20 of a 10 1P3A II protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 20 to about amino acid 30 of a 101P3AI I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 30 to about amino acid 40 of a 101P3A II protein shown in Figure 2 or Figure 3, polypcptides consisting of about amino acid 40 to about amino acid 50 of a 101P3A I I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 50 to about amino acid 60 of a IO1P3A 1I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 60 to about amino acid 70 of a 101P3AI I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 70 to about amino acid 80 of a 101P3AI I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 80 to about amino acid 90 of a I01P3AI I protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 90 to about amino acid 100 of a 101P3A I 1 protein shown in Figure 2 or Figure 3, etc. throughout the entirety of a 10IP3A 1I amino acid sequence. Moreover, polypeptides consisting of about amino acid I (or 20 or 30 or 40 etc.) to about amino acid 20, (or 130, or 140 or 150 etc.) of a 101P3A II 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. 33 101 P3A Il -related proteins are generated using standard peptide synthesis technology or using chemical cleavage methods well known in the art. Alternatively, recombinant methods can be used to generate nucleic acid molecules that encode a 101 P3A 11-related protein. In one embodiment, nucleic acid molecules provide a means to generate defined fragments of a 101P3A 1 protein (or variants, homologs or analogs thereof). III.A.) Motif-bearing Protein Embodiments Additional illustrative embodiments of the invention disclosed herein include OIP3AI 1 polypeptides comprising the amino acid residues of one or more of the biological motifs contained within a I01P3A 1 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 a number of publicly available Internet sites (see, e.g., URL addresses: pfam.wustl.edu/; searchlauncher.bcm.tmc.edu/seq-search/struc-predict.html; psort.ims.u-tokyo.ac.jp/; www.cbs.dtu.dk/; www.ebi.ac.uk/interpro/scan.html; www.expasy.ch/tools/scnpsitl.html; EpimatrixTm and Epimertm, Brown University, www.brown.edu/Researchf[lHIVLab/epimatrix/epimatrix.html; and BIMAS, bimas.dcrt.nlh.gov/.). Motif bearing subsequences of all IOIP3AI 1 variant proteins are set forth and identified in Tables V XVIII and XXII TO ILL. ' Table XIX sets forth several frequently occurring motifs based on pfam searches (see URL address pfamn.wustl.edu/). The columns of Table XIX 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 101P3A I 1 motifs discussed above are useful in elucidating the specific characteristics of a malignant phenotype in view of the observation that the 101P3AI 1 motifs discussed above are associated with growth dysregulation and because 101P3AI I is overexpressed in certain cancers (See, e.g., Table 1). Casein kinase II, 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 a., 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., Biochcmn. Biophys. Acta 1473(l):21-34 (1999); Raju el 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 V-XVIII and XXII TO IL. CTL epitopes can be determined using specific algorithms to identify peptides within a I0IP3A 11 protein that are capable of optimally binding to specified HLA alleles (e.g., Table IV; Epimatrix T m and EpimerTm, Brown University, URL www.brown.edu/ResearchfB-HIV_Lab/epimatrix/epimatrix.html; and BIMAS, URL bimas.dcrt.nih.gov/.) 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. 34 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 II 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, one can substitute out a deleterious residue in favor of any other residue, such as a preferred residue as defined in Table IV; substitute a less-preferred residue with a preferred residue as defined in Table IV; or substitute an originally-occurring preferred residue with another preferred residue as defined in Table IV. 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 al.; 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 a., J. Immunol. 1996 157(8): 3480 90; and Falk et a., Nature 351: 290-6 (1991); Hunt et aL., Science 255:1261-3 (1992); Parker et al., J. Immunol. 149:3580-7 (1992); Parker et al., J. Imrmunol. 152:163-75 (1994)); Kast et a., 1994 152(8): 3904-12; Borras Cuesta et al., Hum. Irnunol. 2000 61(3): 266-278; Alexander et at., J. Immunol. 2000 164(3); 164(3): 1625 1633; Alexander et al., PMID: 7895164, UI: 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 XX, and/or, one or more of the predicted CTL epitopes of Tables V-XVII and XXII XLVII, and/or, one or more of the predicted HTL epitopes of Tables XLVIII-LI, 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 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 I to about 100 amino acid residues, preferably 5 to about 50 amino acid residues. 10 1 P3A 11-related proteins are embodied in many forms, preferably in isolated form. A purified I0IP3A1I1 protein molecule will be substantially free of other proteins or molecules that impair the binding of 101P3AI I to antibody, T cell or other ligand. The nature and degree of isolation and purification will depend on the intended use. Embodiments of a 10lP3A 1-related proteins include purified IOIP3AI I-related proteins and functional, soluble IOIP3A1 1-related proteins. In one embodiment, a functional, soluble IOP3AI I protein or fragment thereof retains the ability to be bound by antibody, T cell or other ligand. The invention also provides 101P3A II proteins comprising biologically active fragments of a 10 1P3AI I amino acid sequence shown in Figure 2 or Figure 3. Such proteins exhibit properties of the starting IOP3A1 1 protein, such as the ability to elicit the generation of antibodies that specifically bind an epitope associated with the starting 101P3A1 1 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. 1OIP3A1 I-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, Kyte-Doolittle, Eisenberg, Karplus-Schultz or Jameson-Wolf analysis, or on the basis of immunogenicity. Fragments that contain such strutures are particularly useful in generating subunit-specific anti 35 I1P3AI I antibodies, or T cells or in identifying cellular factors that bind to 101P3A 11. 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 Doolittle, 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-turn 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 101P3A 1 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/I; the listings in Table IV(A)-(E); Epimatrix T m and Epimerm, Brown University, URL (www.brown.edu/Research/TB-HIVLab/epimatrix/epimtrix.html); and BIMAS, URL bimas.dcrt.nih.gov/). Illustrating this, peptide epitopes from 101P3A II that are presented in the context of human MHC Class I molecules, e.g., HLA-A1, A2, A3, A11, A24, B7 and B35 were predicted (see, e.g., Tables V-XVIII, XXII TO IL). Specifically, the complete amino acid sequence of the 10 1P3A 1 protein and relevant portions of other variants, i.e., for HLA Class I predictions 9 flanking redisues on either side of a point mutation, and for HLA Class II predictions 14 flanking residues on either side of a point mutation, were entered into the HLA Peptide Motif Search algorithm found in the Bioinformatics and Molecular Analysis Section (BIMAS) web site listed above; and the site SYFPEITHI at URL syfpeithi.bmi-heidelberg.com/ was used. 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 et 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 II -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 101P3A 1I predicted binding peptides are shown in Tables V-XVIII and XXII TO IL herein. In Tables V-XVIII and XXII TO IL, selected candidates, 9-mers, 1 0-mers, and 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 37*C 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, Epimerm and EpimatrixTm sites, or specified by the HLA class I or class II 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.com/, or BIMAS, 36 bimas.dcrt.nih.gov/) are to be "applied" to a IOIP3A1 I protein in accordance with the invention. As used in this context "applied" means that a IOIP3AI I 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 lOlP3A 1I protein of 8, 9, 10, or II 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 II motif are within the scope of the invention. III.B.) Expression of 101P3AlI-related Proteins In an embodiment described in the examples that follow, 101 P3A 11 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 101P3AI I with a C-terminal 6X1is 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 I0IP3A1I1 protein in transfected cells. The secreted HIS-tagged IOlP3AI I in the culture media can be purified, e.g., using a nickel column using standard techniques. Ill.C.) Modifications of 101P3AII-related Proteins Modifications of 101 P3A 11-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 101P3A1 I polypeptide with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of a 101P3A II protein. Another type of covalent modification of a 10 IP3A II polypeptide included within the scope of this invention comprises altering the native glycosylation pattern of a protein of the invention. Another type of covalent modification of 10IP3A 1I comprises linking a 101P3AI I 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 101P3A1 1-related proteins of the present invention can also be modified to form a chimeric molecule comprising 101P3A1 1 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. Alternatively, a protein in accordance with the invention can comprise a fusion of fragments of a 101P3AI I 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 101 P3A 11. A chimeric molecule can comprise a fusion of a 101 P3A 11-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 carboxyl- terminus of a 10 1P3A 11 protein. In an alternative embodiment, the chimeric molecule can comprise a fusion of a 101 P3A II related protein with an immunoglobulin 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 IOP3AI I 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. 37 1II.D.) Uses of 101P3AI 1-related Proteins The proteins of the invention have a number of different specific uses. As IOIP3AI I is highly expressed in prostate and other cancers, 1OIP3AI I-related proteins are used in methods that assess the status of 1OIP3AI I gene products in normal versus cancerous tissues, thereby elucidating the malignant phenotype. Typically, polypeptides from specific regions of a 101P3A II 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 101P3A1 I-related proteins comprising the amino acid residues of one or more of the biological motifs contained within a 101P3A 11 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, 1OIP3AI 1-related proteins that contain the amino acid residues of one or more of the biological motifs in a 101P3Al I protein are used to screen for factors that interact with that region of 101P3A1 1. 101P3A1I1 protein fragments/subsequences are particularly useful in generating and characterizing domain specific antibodies (e.g., antibodies recognizing an extracellular or intracellular epitope of a 1OIP3AI I protein), for identifying agents or cellular factors that bind to 101P3AI 1 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 101P3A II 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 IOP3A1I1 gene product. Antibodies raised against a IOIP3AI 1 protein or fragment thereof are useful in diagnostic and prognostic assays, and imaging methodologies in the management of human cancers characterized by expression of 101P3A1 1 protein, such as those listed in Table I. Such antibodies can be expressed intracellularly and used in methods of treating patients with such cancers. 1IOP3Al1-related nucleic acids or proteins are also used in generating HTL or CTL responses. Various immunological assays useful for the detection of 101P3AI I proteins are used, including 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 101P3A II-expressing cells (e.g., in radioscintigraphic imaging methods). IOP3A1 1 proteins are also particularly useful in generating cancer vaccines, as further described herein. IV.) 101P3AH1 Antibodies Another aspect of the invention provides antibodies that bind to 101P3A 1I-related proteins. Preferred antibodies specifically bind to a 101P3A1 -related protein and do not bind (or bind weakly) to peptides or proteins that are not lOP3Al 1-related proteins. For example, antibodies that bind 1OIP3A1 1 can bind IOP3AI 1-related proteins such as the homologs or analogs thereof. 1OIP3Al I antibodies of the invention are particularly useful in cancer (see, e.g., Table I) 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 IOIP3AI 1 is also expressed or overexpressed in these other cancers. Moreover, intracellularly expressed antibodies (e.g., single chain antibodies) are therapeutically useful in treating cancers in which the expression of 101 P3A 11 is involved, such as advanced or metastatic prostate cancers. 38 The invention also provides various immunological assays useful for the detection and quantification of 101 P3A I1 and mutant 10 1P3A Il-related proteins. Such assays can comprise one or more 101 P3A II antibodies capable of recognizing and binding a 101 P3A 11-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 radioirnmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-linked immunofluorescent 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 101P3A1 I are also provided by the invention, including but not limited to radioscintigraphic imaging methods using labeled 101P3A1 1 antibodies. Such assays are clinically useful in the detection, monitoring, and prognosis of 101 P3A 1 expressing cancers such as prostate cancer. 101P3AI I antibodies are also used in methods for purifying a 101P3A 1-related protein and for isolating 101P3A II homologues and related molecules. For example, a method of purifying a 101P3A1 1-related protein comprises incubating a 10IP3A1 1 antibody, which has been coupled to a solid matrix, with a lysate or other solution containing a 101P3A1 1-related protein under conditions that permit the IOP3AI I antibody to bind to the IOIP3AI I related protein; washing the solid matrix to eliminate impurities; and eluting the IO1P3AI 1-related protein from the coupled antibody. Other uses of 101P3Al1 I antibodies in accordance with the invention include generating anti idiotypic antibodies that mimic a 10tP3A II 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 1OIP3A 1-related protein, peptide, or fragment, in isolated or immunoconjugated form (Antibodies: A Laboratory Manual, CSH Press, Eds., Harlow, and Lane (1988); Harlow, Antibodies, Cold Spring Harbor Press, NY (1989)). In addition, fusion proteins of O1P3A1 I can also be used, such as a IOIP3Al I 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 used as an immunogen to generate appropriate antibodies. In another embodiment, a 101 P3A 1 1-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 101P3A 1I-related protein or IOIP3AI I 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 101 P3A II protein as shown in Figure 2 or Figure 3 can be analyzed to select specific regions of the I1P3AI 1 protein for generating antibodies. For example, hydrophobicity and hydrophilicity analyses of a I10P3A1 I amino acid sequence are used to identify hydrophilic regions in the 1OIP3AI I structure. Regions of a IOIP3A1 1 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-tum profiles can be generated using the method of Deleage, G., Roux B., 1987, 39 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 10 1 P3A II 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 IOIP3A 11 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. IOIP3AI I 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 IOIP3Al 1-related protein. When the appropriate immortalized cell culture is identified, the cells can be expanded and antibodies produced either from in vitro 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 101P3AI 1 protein can also be produced in the context of chimeric or complementarity determining region (CDR) grafted antibodies of multiple species origin. Humanized or human IOP3AI I 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 a., 1988, Nature 332: 323-327; Verhoeyen et a., 1988, Science 239: 1534-1536). See also, Carter et at, 1993, Proc. NatI. Acad. Sci. USA 89: 4285 and Sims et a., 1993, J. Immunol. 151: 2296. Methods for producing fully human monoclonal antibodies include phage display and transgenic methods (for review, see Vaughan et a., 1998, Nature Biotechnology 16: 535-539). Fully human 101P3AI 1 monoclonal antibodies can be generated using cloning technologies employing large human Ig gene combinatorial libraries (i.e., phage display) (Griffiths and Hoogenboom, Building an in vitro 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. Id., pp 65-82). Fully human 1OIP3A II monoclonal antibodies can also be produced using transgenic mice engineered to contain human immunoglobulin gene loci as described in PCT Patent Application W098/24893, Kucherlapati and Jakobovits et a., 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 101P3A II antibodies with a 101P3A I 1-related protein can be established by a number of well known means, including Western blot, immunoprecipitation, ELISA, and FACS analyses using, as appropriate, IOP3AI 1-related proteins, 101P3AI -expressing cells or extracts thereof. A 10 iP3AI 1 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 40 more 101 P3AI 1 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 aL., Cancer Res. 53: 2560-2565). Thus, the present invention relates to polyclonal and monoclonal antibodies raised in response to either IOIP3Al 1, or biologically active fragments thereof. The polyclonal and/or monoclonal antibodies of the present invention, especially IO1P3AI I neutralizing antibodies (antibodies that block IOIP3AI 1 function and/or block its binding with ligands), will also be useful as therapeutics to modulate 1OP3AI I expression and/or activity. In addition, the polyclonal and/or monoclonal antibodies of the present invention are useful as (1) diagnostics for qualitative and/or quantitative detection of 101 P3A1.1 expression in a variety of immunoassays, e.g., Western blotting; immunohistochemistry and immunoprecipitation (of samples/biopsies of material such as tissue, serum, blood, urine or semen); and, (ii) as noted above, inhibition of 1OP3Al I function using 1OIP3AI I neutralizing antibodies for the treatment of diseases associated with I10P3AI I overexpression such as cancers of tissues listed in Table I. Antibodies that antagonize the effect of 1OP3A I (for example, inhibition of OIP3Al I's ability to protect certain cells from apoptosis, cell death or inhibition of 101P3Al l's ability to bind to its ligand) can be administered directly by methods known in the art (see, e.g., Antibodies in Human Diagnosis and Therapy by Raven Press, New York (1977)). Monoclonal antibodies are especially preferred for the treatment of tumors associated with an abnormal 101P3A 1 expression. For example, a 101P3AI 1 monoclonal antibody which slows the progression of a cancer associated with an increase in 101P3AI 1 expression within cancer cells, and in turn can cause tumor shrinkage over time, will be especially useful. A useful paradigm is the early success of Herceptinm, a recombinant DNA-derived humanized monoclonal antibody that selectively binds to the extracellular domain of the human epidermal growth factor 2 (HER2). The antibody is produced in CHO cells and the final product is available as a lyophilized powder. HER2 has been shown to be overexpressed in 25-30% of primary breast cancers. In turn, administration of Herceptiny" has been shown to inhibit the proliferation of tumor cells which overexpress HER2. A prospcctivc O1P3AI I monoclonal antibody can be "humanized" by methods well known in thc art, such as XcnomouscTM technology (Abgenix), or antibody phage display, in order to reduce any unwanted immunological effects of human administration of the antibody. Alternatively, the 101 P3A 11-based antibody can be a chimera, most likely a mouse/human or rat/human chimera. In addition, any such therapeutic 101P3A II-based antibody can be administered alone or within a regime that includes other cancer therapies, such as known chemotherapeutic agents, which can act in concert to reduce tumor growth associated with increased 10 lP3AI I expression. Another example of the use of monoclonal antibodies to treat various cancers is Rituxanym, a recombinant DNA based mouse/human chimeric monoclonal antibody which has been shown to be effective in treating patients with low grade B-cell non-Hodgkin's lymphoma (NHL), a cancer of the immune system. Rituxan targets and destroys white blood cells (B cells) involved in the disease, resulting insignificant tumor shrinkage with less severe side effects than most cancer treatments. Additional monoclonal antibodies currently under development include (i) an anti-CD-20 monoclonal antibody to treat patients with low-grade lymphomas, (ii) a combination anti-EGFr antibody with doxorubicin in patients with hormone refractory prostate cancer as well as a combination anti EGFr antibody with cisplatin in patients with head and neck and lung cancer. A 101P3A1 1 anti-idiotype antibody can also be administered so as to stimulate a host immune response to tumors overexpressing 101 P3A 11. Therefore, it is evident that IOP3AI I antibodies, especially IOIP3AI I monoclonal antibodies, are potentially useful tools, along or in combination with other cancer therapies, for direct therapeutic intervention of cancers characterized by an increase in 101P3A 11 expression. 41 Skilled artisans understand that equivalent molecules known in the art which mimic the inhibitory activity of an antibody capable of inhibiting OIP3A1 I function are aspects of the presently disclosed methods which employ an antibody capable of inhibiting 101P3A1 I function. Examples of such molecules include anti 10IP3AI I peptide mimetics which inhibit the growth of at least a comparable or like manner to an antibody capable of inhibiting 101P3A II function. Polyclonal Antibodies The antibodies of the invention also comprise polyclonal antibodies. Methods of preparing polyclonal antibodies are known to the skilled artisan. Polyclonal antibodies can be raised in a mammal, for example, by one or more 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 subcutaneous or intraperitoneal injections. The immunizing agent can include a 1OIP3A 1I polypeptide or a fusion protein thereof. It can be useful to conjugate the immunizing agent to a protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include but are not limited to keyhole limpet hemocyanin, serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. Examples of adjuvants which can be employed include Freund's complete adjuvant and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). The immunization protocol can be selected by one skilled in the art without undue experimentation. The mammal can then be bled, and the serum assayed for antibody titer. If desired, the mammal can be boosted until the antibody titer increases or plateaus. Monoclonal Antibodies The antibodies of the invention can, alternatively, be monoclonal antibodies. Monoclonal antibodies can be prepared using hybridoma methods, such as those described by Kohler and Milstein, Nature, 256:495 (1975). In a hybridoma method, a mouse, hamster, or other appropriate host animal, is typically immunized with an immunizing agent to elicit lymphocytes that produce or are capable of producing antibodies that will specifically bind to the immunizing agent. Alternatively, the lymphocytes can be immunized in vitro. The immunizing agent will typically include a 101P3AI I polypeptide or a fusion protein thereof. Generally, either peripheral blood lymphocytes ("PBLs") are used if cells of human origin are desired, or spleen cells or lymph node cells are used if non-human mammalian sources are desired. The lymphocytes are then fused with an immortalized cell line using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding, Monoclonal Antibodies: Principles and Practice, Academic Press, (1986) pp. 59-103]. Immortalized cell lines are usually transformed mammalian cells, particularly myeloma cells of rodent, bovine and human origin. Usually, rat or mouse myeloma cell lines are employed. The hybridoma cells can be cultured in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, immortalized cells. For example, if the parental cells lack the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT or HPRT), the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine ("HAT medium"), which substances prevent the growth of HGPRT deficient cells. Alternatively, SLAM technology can be employedfor screening as appreciated by one of skill in the art. Preferred immortalized cell lines are those that fuse efficiently, support stable high level expression of antibody by the selected antibody-producing cells, and are sensitive to a medium such as HAT medium. More preferred immortalized cell lines are murine myeloma lines, which can be obtained, for instance, from the Salk Institute Cell Distribution Center, San Diego, Calif. and the American Type Culture Collection, Manassas, Vir. 42 An example of such a urine myeloma cell line is P3X63AgU.1. Human myeloma and mouse-human heteromyeloma cell lines also have been described for the production of human monoclonal antibodies (Kozbor, J. Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, (1987) pp. 51-63). The culture medium in which the hybridoma cells are cultured can then be assayed for the presence of monoclonal antibodies directed against the 10IP3A1 1. Preferably, the binding specificity of monoclonal antibodies produced by the hybridoma cells is determined by immunoprecipitation or by an in in vitro binding assay, such as radioimmunoassay (RIA) or enzyme-linked immunoabsorbent assay (ELISA). Such techniques and assays are known in the art. The binding affinity of the monoclonal antibody can, for example, be determined by the Scatchard analysis of Munson and Pollard, Anal. Biochem., 107:220 (1980). After the desired hybridoma cells are identified, the clones can be subcloned by limiting dilution procedures and grown by standard methods (Goding, Monoclonal Antibodies: Principles and Practice, Academic Press, (1986)). Suitable culture media for this purpose include, for example, Dulbecco's Modified Eagle's Medium or RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal. The monoclonal antibodies secreted by the subclones can be isolated or purified from the culture medium or ascites fluid by conventional immunoglobulin purification procedures such as, for example, protein A Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography. The monoclonal antibodies can also be made by recombinant DNA methods, such as those described in U.S. Pat. No. 4,816,567. DNA encoding the monoclonal antibodies of the invention can be readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies). The hybridoma cells of the invention serve as a preferred source of such DNA. Once isolated, the DNA can be placed into expression vectors, which are then transfected into host cells such as simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of monoclonal antibodies in the recombinant host cells. The DNA also can be modified, for example, by substituting the coding sequence for human heavy and light chain constant domains in place of the homologous murine sequences (see, e.g., U.S. Pat. No. 4,816,567; Morrison et al., Proc. Nall. Acad. Sci. USA, 81:6851-6855 (1984)) or by covalcntly joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. Such a non-immunoglobulin polypeptide can be substituted for the constant domains of an antibody of the invention, or can be substituted for the variable domains of one antigen-combining site of an antibody of the invention to create a chimeric bivalent antibody. Optionally, chimeric antibodies can be constructed which include at least one variable or hypervariable domain of an anti-1OIP3AI I antibody selected from the antibodies disclosed herein. Optionally, the antibody capable of inhibiting 101P3AI I function of the present invention will bind to the same epitope(s) as any of the antibodies disclosed herein. This can be determined by conducting various assays, such as described herein. For instance, to determine whether a monoclonal antibody has the same specificity as the antibodies referred to herein, one can compare its activity in blocking assays or inhibition assays or functional assays. The antibodies of the invention include "cross-linked" antibodies. The term "cross-linked" as used herein refers to binding of at least two IgG molecules together to form one (or single) molecule. The 101P3AI I antibodies can be cross-linked using various linker molecules and optionally the antibodies are cross-linked using 43 an anti- IgG molecule, complement, chemical modification or molecular engineering. It is appreciated by those skilled in the art that complement has a relatively high affinity to antibody molecules once the antibodies bind to cell surface membrane. Accordingly, complement can be used as a cross-linking molecule to link two or more antibodies bound to cell surface membrane. Among the various murine Ig isotypes, IgM, IgG2a and IgG2b are known to fix complement. The antibodies of the invention can optionally comprise dimeric antibodies, as well as multivalent forms of antibodies. Those skilled in the art can construct such dimers or multivalent forms by techniques known in the art and using the anti-101P3A 1 antibodies herein. The antibodies of the invention can also comprise monovalent antibodies. Methods for preparing monovalent antibodies are well known in the art. For cxamplc, onc method involves recombinant expression of immunoglobulin light chain and modified heavy chain. The heavy chain is truncated generally at any point in the Fc region so as to prevent heavy chain crosslinking. Alternatively, the relevant cysteine residues are substituted with another amino acid residue or are deleted so as to prevent crosslinking. In vitro methods are also suitable for preparing monovalent antibodies. Digestion of antibodies to produce fragments thereof, particularly, Fab fragments, can be accomplished using routine techniques known in the art. For instance, digestion can be performed using papain. Examples of papain digestion are described in WO 94/29348 published Dec. 22, 1994 and U.S. Pat. No. 4,342,566. Papain digestion of antibodies typically produces two identical antigen binding fragments, called Fab fragments, each with a single antigen binding site, and a residual Fc fragment. Pepsin treatment yields an F(ab')2 fragment that has two antigen combining sites and is still capable of cross-linking antigen. The Fab fragments produced in the antibody digestion also contain the constant domains of the light chain and the first constant domain (CHI) of the heavy chain. Fab' fragments differ from Fab fragments by the addition of a few residues at the carboxy terminus of the heavy chain CH I domain including one or more cysteines from the antibody hinge region. Fab'-SH is the designation herein for Fab' in which the cysteine residue(s) of the constant domains bear a free thiol group. F(ab')2 antibody fragments originally were produced as pairs of Fab' fragments which have hinge cysteines between them. Other chemical couplings of antibody fragments are also known. Single chain Fv fragments can also be produced, such as described in Iliades et al, FEBS Letters, 409:437-441 (1997). Coupling of such single chain fragments using various linkers is described in Kortt et al., Protein Engineering, 10:423-433 (1997). In addition to the antibodies described herein, it is contemplated that chimeric or hybrid antibodies are prepared using known methods in synthetic protein chemistry, including those involving crosslinking agents. For example, immunotoxins can be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate. The 101 P3A 11 antibodies of the invention further comprise humanized antibodies or human antibodies. Humanized forms of non- human (e.g., murine) antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab', F(ab') 2 or other antigen-binding subsequences of antibodies) which contain minimal sequence derived from non-human immunoglobulin. Humanized antibodies include human immunoglobulins (recipient antibody) in which residues from a complementary determining region (CDR) of the recipient are replaced by residues from a CDR of a non-human species (donor antibody) such as mouse, rat or rabbit having the desired specificity, affinity and capacity. In some instances, Fv framework residues of the 44 human immunoglobulin are replaced by corresponding non-human residues. Humanized antibodies can also comprise residues which are found neither in the recipient antibody nor in the imported CDR or framework sequences. In general, the humanized antibody will comprise substantially all of at least onc, and typically two, variable domains, in which all or substantially all of the CDR regions correspond to those of a non-human immunoglobulin and all or substantially all of the FR regions are those of a human immunoglobulin consensus sequence. The humanized antibody optimally also will comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin (Jones et al., Nature, 321:522-525 (1986); Riechmann et al., Nature 332:323-329 (1988); and Presta, Curr. Op. Struct. Biol., 2:593-596 (1992)). Methods for humanizing non-human antibodies are well known in the art. Generally, a humanized antibody has one or more amino acid residues introduced into it from a source which is non-human. These non human amino acid residues are often referred to as "import" residues, which are typically taken from an "import" variable domain. Humanization can be essentially performed following the method of Winter and co- workers (Jones et al., Nature, 321:522-525 (1986); Riechmann et al. , Nature 332:323-327 (1988); Verhoeyen ct al., Science 239;1534-1536 (1988)), by substituting rodent CDRs or CDR sequences for the corresponding sequences of a human antibody. Accordingly, such "humanized" antibodies are chimeric antibodies (U.S. Pat. No. 4,816,567), wherein substantially less than an intact human variable domain has been substituted by the corresponding sequence from a non-human species. In practice, humanized antibodies are typically human antibodies in which some CDR residues and possibly some FR residues are substituted by residues from analogous sites in rodent antibodies. Sources of such import residues or import variable domains (or CDRs) include antibodies that specifically bind 101 P3A 11. The choice of human variable domains, both light and heavy, to be used in making the humanized antibodies is very important in order to reduce antigenicity. According to the "best-fit" method, the sequence of the variable domain of a rodent antibody is screened against the entire library of known human variable domain sequences. The human sequence which is closest to that of the rodent is then accepted as the human framework (FR) for the humanized antibody (Sims et al., J. Immunol., 151:2296-2308 (1993); Chothia and Lesk, J. Mol. Biol., 196:901- 917 (1987)). Another method uses a particular framework derived from the consensus sequence of all human antibodies of a particular subgroup of light or heavy chains. The same framework can be used for several different humanized antibodies (Carter et al., Proc. Nat]. Acad. Sci. USA, 89:4285-4289 (1992); Presta et al., J. Immunol., 151:2623- 2632 (1993)). It is further important that antibodies be humanized with retention of high affinity for the antigen and other favorable biological properties. To achieve this goal, according to a preferred method, humanized antibodies are prepared by a process of analysis of the parental sequences and various conceptual humanized products using three dimensional models of the parental and humanized sequences. Three dimensional inmnunoglobulin models are commonly available and are familiar to those skilled in the art. Computer programs are available which illustrate and display probable three-dimensional conformational structures of selected candidate immunoglobulin sequences. Inspection of these displays permits analysis of the likely role of the residues in the functioning of the candidate immunoglobulin sequence, i.e., the analysis of residues that influence the ability of the candidate immunoglobulin to bind its antigen. In this way, FR residues can be selected and combined from the consensus and import sequence so that the desired antibody characteristic, such as increased affinity for the target antigen(s), is achieved. In general, the CDR residues are directly and most substantially involved in influencing antigen binding (see, WO 94/04679 published 3 March 1994). 45 Human monoclonal antibodies can be made via an adaptation of the hybridoma method first described by Kohler and Milstein by using human B lymphocytes as the fusion partner. Human B lymphocytes producing an antibody of interest can, for example, be isolated from a human individual, after obtaining informed consent. For instance, the individual can be producing antibodies against an autoantigen as occurs with certain disorders such as systemic lupus erythematosus (Shoenfeld et al. J. Clin. Invest,, 70:205 (1982)), immune-mediated thrombocytopenic purpura (ITP) (Nugent et al. Blood, 70(1):16-22 (1987)), or cancer. Alternatively, or additionally, lymphocytes can be immunized in vitro. For instance, one can expose isolated human peripheral blood lymphocytes in vitro to a lysomotrophic agent (e.g., L- leucine-O-methyl ester, L-glutamic acid dimethly ester or L-leucyl-L- leucine-O-methyl ester) (U.S. Pat. No. 5,567,610, Borrebaeck et al.); and/or T-cell depleted human peripheral blood lymphocytes can be treated in vitro with adjuvants such as 8-mercaptoguanosine and cytokines (U.S. Pat. No. 5,229,275, Goroff et al.). The B lymphocytes recovered from the subject or immunized in vitro, are then generally immortalized in order to generate a human monoclonal antibody. Techniques for immortalizing the B lymphocyte include, but ate not limited to: (a) fusion of the human B lymphocyte with human, murine myelomas or mouse-human heteromycloma cells; (b) viral transformation (e.g. with an Epstein-Barr virus; see Nugent et al., supra, for example); (c) fusion with a lymphoblastoid cell line; or (d) fusion with lymphoma cells. Lymphocytes can be fused with myeloma cells using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding, Monoclonal Antibodies: Principles and Practice, pp. 59- 103 (Academic Press, 1986)). The hybridoma cells thus prepared ate seeded and grown in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, parental myeloma cells. For example, if the parental myeloma cells lack the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT or HPRT) , the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine (HAT medium), which substances prevent the growth of HGPRT-deficient cells. Suitable human myeloma and mouse-human heteromyeloma cell lines have been described (Kozbor, J. Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, pp. 51-63 (Marcel Dekker, Inc., New York, 1987)). Culture medium in which hybridoma cells are growing is assayed for production of monoclonal antibodies directed against the antigen. Preferably, the binding specificity of monoclonal antibodies produced by hybridoma cells is determined by immunoprecipitation or by an in vitro binding assay, such as radioimmunoassay (RIA) or enzyme-linked immunoabsorbent assay (ELISA). After hybridoma cells are identified that produce antibodies of the desired specificity, affinity, and/or activity, the clones can be subcloned by limiting dilution procedures and grown by standard methods (Goding, Monoclonal Antibodies: Principles and Practice, pp.59-103 (Academic Press, 1986)). Suitable culture media for this purpose include, for example, D-MEM or RPMI- 1640 medium. The monoclonal antibodies secreted by the subclones are suitably separated from the culture medium, ascites fluid, or serum by conventional immunoglobulin purification procedures such as, for example, protein A chromatography, gel electrophoresis, dialysis, or affinity chromatography. Human antibodies can also be generated using a non-human host, such as a mouse, which is capable of producing human antibodies. As noted above, transgenic mice are now available that are capable, upon immunization, of producing a full repertoire of human antibodies in the absence of endogenous immunoglobulin production. For example, it has been described that the homozygous deletion of the antibody heavy-chain joining region JH) gene in chimeric and germ-line mutant mice results in complete inhibition of endogenous antibody 46 production. Transfer of the human germ-line immunoglobulin gene array in such germ- line mutant mice resulted in the production of human antibodies upon antigen challenge. See, e.g., Jakobovits et al., Proc. Nati. Acad. Sci. USA, 90:2551 (1993); Jakobovits et al., Nature, 362:255-258 (1993); Bruggermann et al., Year in Immuno., 7:33 (1993); U.S. Pat. No. 5,591,669; U.S. Pat. No. 5,589,369; and U.S. Pat. No. 5,545,807. Human antibodies can also be prepared using SCID-hu mice (Duchosal et al Nature 355:258-262 (1992)). In another embodiment, the human antibody can be selected from a human antibody phage display library. The preparation of libraries of antibodies or fragments thereof is well known in the art and any of the known methods can be used to construct a family of transformation vectors which can be introduced into host cells. Libraries of antibody light and heavy chains in phage (Huse et al., Science, 246:1275 (1989)) or of fusion proteins in phage or phagemid can be prepared according to known procedures. See, for example, Vaughan et al, Nature Biotechnology 14:309-314 (1996); Barbas et al., Proc. Natd. Acad. Sci., USA, 88:7978-7982 (1991); Marks et al., J. Mol. Biol., 222:581-597 (1991); Hoogenboom and Winter, J. Mol Biol., 227:381- 388 (1992); Barbas et al., Proc. Nati. Acad. Sci., USA, 89: 4457-4461 (1992); Griffiths et al., EMBO Journal, 13:3245-3260 (1994); de Kruif et al., J. Mol. Biol., 248:97-105 (1995); WO 98/05344; WO 98/15833; WO 97/47314; WO 97/44491; WO 97/35196; WO 95/34648; U.S. Pat. No. 5,712,089; U.S. Pat. No. 5,702,892; U.S. Pat. No. 5,427,908; U.S. Pat. No. 5,403,484; U.S. Pat. No. 5,432,018; U.S. Pat. No. 5,270,170; WO 92106176; WO 99/06587; U.S. Pat. No. 5,514,548; WO 97/08320; and U.S. Pat. No. 5,702,892. The antigen of interest is panned against the phage library using procedures known in the field for selecting phage- antibodies which bind to the target antigen. The I0lP3A1I1 antibodies, as described herein, will optionally possess one or more desired biological activities or properties. Such antibodies can include but are not limited to chimeric, humanized, human, and affinity matured antibodies. As described above, the antibodies can be constructed or engineered using various techniques to achieve these desired activities or properties. In one embodiment, the 101P3A II antibody will have a 101P3AI 1 binding affinity of at least 105 M, preferably at least in the range of 10~* M to 10'" M, mote preferably, at least in the range of 10'8 M to 10'12 M and even more preferably, at least in the range of I0e M to 10'12 M. The binding affinity of the antibody can be determined without undue experimentation by testing the antibody in accordance with techniques known in the art, including Scatchard analysis (Munson and Pollard, Anal. Biochem., 107:220 (1980)). For example, a 11OP3AI 1 antibody can be assayed for binding affinity to 101P3A1 1, including constructs or fragments thereof. In another embodiment, the antibody interacts in such a way to create a steric conformation which prevents binding of an antibody capable of inhibiting or enhancing 101 P3A 11 function. The epitope binding property of the antibody of the present invention can be determined using techniques known in the art. Other Modifications Other modifications of the IOIP3AI 1 antibodies are contemplated herein. The antibodies of the present invention can be modified by conjugating the antibody to a cytotoxic agent (like a toxin molecule) or a prodrug activating enzyme which converts a prodrug (e.g. a peptidyl chemotherapeutic agent, see W081/01145) to an active anti-cancer drug. See, for example, WO 88/07378 and U.S. Pat. No. 4,975,278. This technology is also referred to as "Antibody Dependent Enzyme Mediated Prodrug Therapy" (ADEPT). The enzyme component of the immunoconjugate useful for ADEPT includes any enzyme capable of acting on a prodrug in such a way so as to covert it into its more active, cytotoxic form. Enzymes that are useful in the method of this invention include, but are not limited to, alkaline phosphatase useful for converting 47 phosphate-containing prodrugs into free drugs; arylsulfatase useful for converting sulfate-containing prodrugs into free drugs; cytosine deaminase useful for converting non-toxic 5- fluorocytosine into the anti-cancer drug, 5 fluorouracil; proteases, such as serratia protease, thermolysin, subtilisin, carboxypeptidases and cathepsins (such as cathepsins B and L), that are useful for converting peptide-containing prodrugs into free drugs; caspases such as caspase-3; D-alanylcarboxypeptidases, useful for converting prodrugs (hat contain D- amino acid substituents; carbohydrate-cleaving enzymes such as beta- galactosidase and neuraminidase useful for converting glycosylated prodrugs into free drugs; beta-lactamase useful for converting drugs derivatized with beta-lactams into free drugs; and penicillin amidases, such as penicillin V amidase or penicillin G amidase, useful for converting drugs derivatized at their amine nitrogens with phenoxyacetyl or phenylacetyl groups, respectively, into free drugs. Alternatively, antibodies with enzymatic activity, also known in the art as "abzymes", can be used to convert the prodrugs of the invention into free active drugs (see, e.g., Massey, Nature 328: 457-458 (1987)). Antibody abzyme conjugates can be prepared as described herein for delivery of the abzyme to a tumor cell population. The enzymes can be covalently bound to the antibodies by techniques well known in the art such as the use of heterobifunctional crosslinking reagents. Alternatively, fusion proteins comprising at least the antigen binding region of an antibody of the invention linked to at least a functionally active portion of an enzyme of the invention can be constructed using recombinant DNA techniques well known in the art (see, e.g., Neuberger et al., Nature, 312: 604-608 (1984). Further modifications to the polypeptides of the invention are contemplated. For example, the antibodies can be linked to one of a variety of nonproteinaceous polymers, e.g., polyethylene glycol, polypropylene glycol, polyoxyalkylenes, or copolymers of polyethylene glycol and polypropylene glycol. The antibody also can be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization (for example, hydroxymethylcellulose or gelatin-microcapsules and poly- (methylmethacylate) microcapsules, respectively), in colloidal drug delivery systems (for example, liposomes, albunin microspheres, microemulsions, nano-particles and nanocapsules), or in macroemulsions. Such techniques are disclosed in Remington's Pharmaceutical Sciences, 16th edition, Oslo, A., Ed., (1980). To increase the serum half life of the antibody, one can incorporate-a salvage receptor binding epitope into the antibody (especially an antibody fragment) as described, e.g., in U.S. Pat. No. 5,739,277, for example. As used herein, the term "salvage receptor binding epitope" refers to an epitope of the Fc region of an IgG molecule (e.g., IgG 1, IgG2, IgG3, or IgG4) that is responsible for increasing the in vivo serum half-life of the IgG molecule. Formulations The antibody capable of inhibiting 10 IP3AI I function are preferably administered in a carrier. The molecules can be administered in a single carrier, or alternatively, can be included in separate carriers. Suitable carriers and their formulations are described in Remington's Pharmaceutical Sciences, 16th ed., 1980, Mack Publishing Co., edited by Oslo et al. Typically, an appropriate amount of a pharmaceutically-acceptable salt is used in the carrier to render the formulation isotonic. Examples of the carrier include saline, Ringer's solution and dextrose solution. The pH of the solution is preferably from about 5 to about 8, and more preferably from about 7.4 to about 7.8. It will be apparent to those persons skilled in the art that certain carriers are preferred depending upon, for instance, the route of administration and concentration of agent being administered. The carrier can be in the form of a lyophilized formulation or aqueous solution. Acceptable carriers, excipients, or stabilizers are preferably nontoxic to cells and/or recipients at the dosages and concentrations employed, and include buffers such as phosphate, citrate, and other organic acids; 48 antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride, benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m cresol); low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; and/or non-ionic surfactants such as TWEEN@, PLURONICS@ or polyethylene glycol (PEG). The formulation can also contain more than one active compound as necessary for the particular indication being treated, preferably those with complementary activities, and preferably that do not adversely affect each other. Alternatively, or in addition, the composition can comprise a cytotoxic agent, cytokine or growth inhibitory agent. Such molecules are suitably present in combination in amounts that are effective for the purpose intended. The antibody capable of inhibiting 101P3A II function can also be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin- microcapsules and poly-(methylmethacylate) microcapsules, respectively, in colloidal drag delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles and nanocapsules) or in macroemulsions. Such techniques are disclosed in Remington's Pharmaceutical Sciences 16th edition, Oslo, A. Ed. (1980). The formulations to be used for in vivo administration should be sterile. This is readily accomplished by filtration through sterile filtration membranes. Sustained-release preparations can be prepared. Suitable examples of sustained-release preparations include semipermeable matrices of solid hydrophobic polymers containing the antibody, which matrices are in the form of shaped articles, e.g. films, or microcapsules. Examples of sustained-release matrices include polyesters, bydrogels (for example, poly(2-hydroxyethyl-methacrylate), or poly(vinylalcohol)), polylactides (U.S. Pat. No. 3,773,919), copolymers of L-glutamic acid and ( ethyl-L- glutamate, non-dcgradable ethylene-vinyl acetate, degradable lactic acid- glycolic acid copolymers such as the LUPRON DEPOT@ (injectable microspheres cormposed of lactic acid-glycolic acid copolymer and leuprolide acetate), and poly-D-(-)-3-hydroxybutyric acid. While polymers such as ethylene-vinyl acetate and lactic acid-glycolic acid enable release of molecules for over 100 days, certain hydrogels release proteins for shorter time periods. Modes of Administration An antibody(s) capable of inhibiting 101P3AI I function can be administered in accord with known methods, such as intravenous administration as a bolus or by continuous infusion over a period of time, by intramuscular, intraperitoneal, intrathecal, subcutaneous, intra-articular, intrasynovial, intrathecal, oral, topical, or inhalation routes. Optionally, administration can be performed through mini-pump infusion using various commercially available devices. Effective dosages and schedules for administering an antibody capable of inhibiting 101 P3A II function can be determined empirically, and making such determinations is within the skill in the art. Effective dosage or amount of an antibody capable of inhibiting lOP3AI 1 function used alone may range from about 1 pg/kg to about 100 mg/kg of body weight or more per day. Interspecies scaling of dosages can be performed in a manner 49 known in the art, e.g., as disclosed in Mordenti et al., Pharmaceut. Res., 8:1351 (1991). Those skilled in the art will understand that the dosage of an antibody capable of inhibiting 101P3A II function that must be administered will vary depending on, for example, the mammal which will receive the an antibody capable of inhibiting I0IP3A I function, the route of administration, and other drugs or therapies being administered to the mammal. Depending on the type of cells and/or severity of the disease, about I pg/kg to 15 mg/kg (e.g. 0.1-20 mg/kg) of antibody is an initial candidate dosage for administration, whether, for example, by one or more separate administrations, or by continuous infusion. A typical daily dosage might range from about 1 pg/kg to 100 mg/kg or more, depending on the factors mentioned above. For repeated administrations over several days or longer, depending on the condition, the treatment is sustained until a desired suppression of disease symptoms occurs. However, other dosage regimens can be useful. It is contemplated that yet additional therapies can be employed in the methods. The one or more other therapies can include but are not limited to, other chemotherapies (or chemotherapeutic agents) and/or radiation therapy, immunoadjuvants, growth inhibitory agents, cytokines, and other non-Her-2 antibody-based therapies. Examples include interleukins (e.g., IL-i, IL-2, IL-3, IL-6), leukemia inhibitory factor, interferons, erythropoietin, thrombopoietin, and anti-VEGF antibody. Other agents known to inhibit the growth of mammalian cells -can also be employed, and such agents include TNF-c CD30 ligand, 4-IBB ligand, and Apo-I ligand. Additional chemotherapies contemplated by the invention include chemical substances or drugs which are known in the art and are commercially available, such as Adriamycin, Doxorubicin, 5-Fluorouracil, Cytosine arabinoside ("Ara-C"), Cyclophosphamide, Leucovorin, Thiotcpa, Busulfan, Cytoxin, Taxol, Toxotere, Methotrexate, Cisplatin, Melphalan, Vinblastine, Bleomycin, Etoposide, Ifosfamide, Mitomycin C, Mitoxantrone, Vincreistine, Vinorelbine, Carboplatin, Teniposide, Daunomycin, Carrainomycin, Amimopterin, Dactinomycin, Mitomycins, Esperamicins (see U. S. Pat. No. 4,675,187), Melphalan and other related nitrogen mustards. Also included are agents that act to regulate or inhibit hormone action on tumors such as tamoxifen and onaptistone. Preparation and dosing schedules for such chemotherapy can be used according to manufacturers' instructions or as determined empirically by the skilled practitioner. Preparation and dosing schedules for such chemotherapy are also described in Chemotherapy Service Ed., M. C. Perry, Williams & Wins, Baltimore, Md. (1992). The chemotherapeutic agent can precede, or follow administration with the antibody capable of inhibiting 101P3A II function, or can be given simultaneously therewith. The chemotherapy is preferably administered in a carrier, such as those described above. The mode of administration of the chemotherapy can be the same as employed for an antibody capable of modulating, such as inhibiting or enhancing, 10 1P3A 11 function, or it can be administered via a different mode. Radiation therapy can be administered according to protocols commonly employed in the art and known to the skilled artisan. Such therapy can include cesium, iridium, iodine, or cobalt radiation. The radiation therapy can be whole body irradiation, or can be directed locally to a specific site or tissue in or on the body. Typically, radiation therapy is administered in pulses over a period of time from about I to about 2 weeks. The radiation therapy can, however, be administered over longer periods of time. Optionally, the radiation therapy can be administered as a single dose or as multiple, sequential doses. An antibody capable of inhibiting 10 1P3AI I function (and one or more other therapies) can be administered concurrently or sequentially. Following administration of an antibody capable of inhibiting 101P3AI 1 function, treated cells in vitro can be analyzed. Where there has been in vivo treatment, a treated 50 mammal can be monitored in various ways well known to the skilled practitioner. For instance, tumor mass can be observed physically, by biopsy or by standard x-ray imaging techniques. V.) 101P3Al 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 a., Cell 47:1071, 1986; Babbitt, B. P. et al., Nature 317:359, 1985; Townsend, A. and Bodmer, H., Annu. Rev. Immunol. 7:601, 1989; Germain, R. N., Annu. Rev. Immunol. 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 arc set forth in Tablc IV (see also, e.g., Southwood, et i/., J. Iinino/. 160:3363, 1998; Rammensec, et a., Inmunogenetics 41:178, 1995; Rammensec et a., SYFPEITH I1, access via World Wide Web at URL syfpeithi.bmi-heidelberg.con/; Sette, A. and Sidney, J. Curr. Opin. /mmunol. 10:478, 1998; Engelhard, V. H., Curr. Opin. Immunol. 6:13, 1994; Sette, A. and Grey, H. M., Curr. Opin. Immunol. 4:79, 1992; Sinigaglia, F. and Hammer, J. Curr. Biol. 6:52, 1994; Ruppert et a., Cell 74:929-937, 1993; Kondo et al., J. Immunol. 155:4307-4312, 1995; Sidney et a., J. Immunol. 157:3480-3490, 1996; Sidney et al., Human Immuno. 45:79-93, 1996; Sette, A. and Sidney, J. Immunogenetics 1999 Nov; 50(3-4):201-12, Review). Furthermore, x-ray 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. Immunol. 13:587, 1995; Smith, et al., Immunity 4:203, 1996; Fremont et al., Immunity 8:305, 1998; Stem et al., Structure 2:245, 1994; Jones, E.Y. Curr. Opin. Immunol. 9:75, 1997; Brown, J. H. et al., Nature 364:33, 1993; Guo, H. C. et al., Proc. Natl. Acad. Sci. USA 90:8053, 1993; Guo, H. C. et al., Nature 360:364, 1992; Silver, M. L. et al., Nature 360:367, 1992; Matsumura, M. et al., Science 257:927, 1992; Madden et aL, Cell 70:1035, 1992; Fremont, D. H. et a., Science 257:919, 1992; Saper, M. A. , Bjorkman, P. J. and Wiley, D. C., J. Mo, Biol. 219:277, 1991.) Accordingly, the definition of class I and class II allele-specific HLA binding motifs, or class I or class 1H 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 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., Mol. Immunol. 32:603, 1995; Celis, E. et a., Proc. Nat. Acad. Sci. USA 91:2105, 1994; Tsai, V. et al., J. Immuno. 158:1796, 1997; Kawashima, 1. et al., Human Immunol. 59:1, 1998). This procedure involves the stimulation of 51 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 aL., J. Immunol. 26:97, 1996; Wentworth, P. A. et al., Int. Immunol. 8:651, 1996; Alexander, J. et a., 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 5 1 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 al., 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 5 1 Cr release involving peptide-sensitized targets, T cell proliferation, or lymphokine release. VI.) 1O1P3A1I Transgenic Animals Nucleic acids that encode a 101P3AI I-related protein can also be used to generate either transgenic animals or "knock out" animals that, in turn, are useful in the development and screening of therapeutically useful reagents. In accordance with established techniques, cDNA encoding 101P3A1I1 can be used to clone genomic DNA that encodes 101 P3A 11. The cloned genomic sequences can then be used to generate transgenic animals containing cells that express DNA that encode 101P3A11. 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 101P3Al I transgene incorporation with tissue-specific enhancers. Transgenic animals that include a copy of a transgene encoding 101P3AI I can be used to examine the effect of increased expression of DNA that encodes OlP3Al 1. 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 101P3AI I can be used to construct a 101P3AI I "knock out" animal that has a defective or altered gene encoding IOP3A II as a result of homologous recombination between the endogenous gene encoding 101P3AI 1 and altered genomic DNA encoding 101P3A1 1 introduced into an embryonic cell of the animal. For example, cDNA that encodes 101P3A II can be used to clone genomic DNA 52 encoding 101P3A II in accordance with established techniques. A portion of the genomic DNA encoding 101P3A I I 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, Cejl, LI: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, 6:915 (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 Practical Approach, 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 out" 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 101P3AI I polypeptide. VII.) Methods for the Detection of 101P3A11 Another aspect of the present invention relates to methods for detecting 101P3A1 1 polynucleotides and 101P3AII-related proteins, as well as methods for identifying a cell that expresses 10 1P3A11. The expression profile of 101P3AI 1 makes it a diagnostic marker for metastasized disease. Accordingly, the status of 101P3A II 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 10 IP3AI 1 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 101P3A1 I polynucleotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, cell preparations, and the like. Detectable 101P3A1 I polynucleotides include, for example, a IMP3AI I gene or fragment thereof, 10P3A 1I mRNA, alternative splice variant 101P3AI I mRNAs, and recombinant DNA or RNA molecules that contain a 101P3A II polynucleotide. A number of methods for amplifying and/or detecting the presence of 101P3A II 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 101P3AI I 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 O10P3A1I1 polynucleotides as sense and antisense primers to amplify IIP3A I cDNAs therein; and detecting the presence of the amplified I0lP3A1I1 cDNA. Optionally, the sequence of the amplified IOP3A 1I cDNA can be determined. In another embodiment, a method of detecting a 1I0lP3A1 I gene in a biological sample comprises first isolating genomic DNA from the sample; amplifying the isolated genomic DNA using 10lP3A 1 polynucleotides as sense and antisense primers; and detecting the presence of the amplified I0lP3AI I gene. Any number of appropriate sense and antisense probe combinations can be designed from a 101P3A II nucleotide sequence (see, e.g., Figure 2) and used for this purpose. 53 The invention also provides assays for detecting the presence of a 101P3A 11 protein in a tissue or other biological sample such as serum, semen, bone, prostate, urine, cell preparations, and the like. Methods for detecting a 101P3A II-related protein are also well known and include, for example, immunoprecipitation, immunohistochemical analysis, Western blot analysis, molecular binding assays, ELISA, ELIFA and the like. For example, a method of detecting the presence of a 101P3AII-related protein in a biological sample comprises first contacting the sample with a 101 P3A 11 antibody, a 101 P3A 11 -reactive fragment thereof, or a recombinant protein containing an antigen binding region of a IOIP3AI I antibody; and then detecting the binding of IOIP3AI 1-related protein in the sample. Methods for identifying a cell that expresses OIP3AI I are also within the scope of the invention. In one embodiment, an assay for identifying a cell that expresses a 10 1P3A II gene comprises detecting the presence of IOIP3AI I mRNA in the cell. Methods for the detection of particular mRNAs in cells are well known and include, for example, hybridization assays using complementary DNA probes (such as in situ hybridization using labeled IOIP3Al I riboprobes, Northern blot and related techniques) and various nucleic acid amplification assays (such as RT-PCR using complementary primers specific for IOIP3AI 1, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like). Alternatively, an assay for identifying a cell that expresses a 101P3A1I1 gene comprises detecting the presence of 10lP3A 1-related protein in the cell or secreted by the cell. Various methods for the detection of proteins arc well known in the art and are employed for the detection of IOIP3Al I-related proteins and cells that express 101P3A1 1-related proteins. IOP3A1 1 expression analysis is also useful as a tool for identifying and evaluating agents that modulate IO1P3A1 I gene expression. For example, O1P3AI 1 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 IOP3AI I 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 101 P3A 1 expression by RT-PCR, nucleic acid hybridization or antibody binding. V1II.) -Methods for Monitoring the Status of 1OIP3AI1-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 et al., Cancer Surv. 23: 19-32 (1995)). In this context, examining a biological sample for evidence of dysregulated cell growth (such as aberrant 10 lP3A II 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 101P3A 11 in a biological sample of interest can be compared, for example, to the status of IOIP3AI I 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 101 P3AI 1 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 IOIP3A1 I 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 54 state of a gene and its products. These include, but are not limited to the location of expressed gene products (including the location of lOP3A II expressing cells) as well as the level, and biological activity of expressed gene products (such as IOIP3AI I mRNA, polynucleotides and polypeptides). Typically, an alteration in the status of IOP3A1 I comprises a change in the location of IOIP3A1 I and/or lOIP3A1 I expressing cells and/or an increase in 101P3Al I mRNA and/or protein expression. 10IP3A I I 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 101 P3A 11 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 Blotting), 15 (Immunoblotting) and 18 (PCR Analysis). Thus, the status of 101P3AI 1 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 101P3AI I gene), Northern analysis and/or PCR analysis of 1OP3A 1I mRNA (to examine, for example alterations in the polynucleotide sequences or expression levels of 101 P3A I I 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 101P3AI I proteins and/or associations of 101P3A 1I proteins with polypeptide binding partners). Detectable 1OIP3AI 1 polynucleotides include, for example, a 1OIP3AI I gene or fragment thereof, 101P3AI 1 mRNA, alternative splice variants, 101P3AI I mRNAs, and recombinant DNA or RNA molecules containing a 10 1P3A I I polynucleotide. The expression profile of 101 P3A I 1 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 1OlP3AI I provides information useful for predicting susceptibility to particular disease stages, progression, and/or tumor aggressiveness. The invention provides methods and assays for determining IO1P3AI I status and diagnosing cancers that express 101P3A 11, such as cancers of the tissues listed in Table I. For example, because 101P3Al 1 mRNA is so highly expressed in prostate and other cancers relative to normal prostate tissue, assays that evaluate the levels of OIP3Al1 nRNA transcripts or proteins in a biological sample can be used to diagnose a disease associated with 1OIP3AI I dysregulation, and can provide prognostic information useful in defining appropriate therapeutic options. The expression status of 1OIP3AI I 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. Consequently, an aspect of the invention is directed to the various molecular prognostic and diagnostic methods for examining the status of 10 1 P3AI I 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 1OIP3AI 1 in a biological sample can be examined by a number of well known procedures in the art. For example, the status of OIP3A II 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 IOP3AI I expressing cells (e.g. those that express 1OP3A1 I mRNAs or proteins). This examination can provide evidence of dysregulated cellular growth, for example, when IOIP3Al1 I-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 IOIP3Al I in a biological sample are often associated with dysregulated cellular growth. Specifically, one 55 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 et al., Prostate 42(4): 315-317 (2000);Su et al., Semin. Surg. Oncol. 18(1): 17-28 (2000) and Freeman et a., J Urol 1995 Aug 154(2 Pt 1):474-8). In one aspect, the invention provides methods for monitoring 101 P3A I I gene products by determining the status of 101P3AI I 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 101 P3AI I gene products in a corresponding normal sample. The presence of aberrant 101P3A II 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 lOlP3Al1 mRNA or protein expression in a test cell or tissue sample relative to expression levels in the corresponding normal cell or tissue. The presence of IO1P3A 1I mRNA can, for example, be evaluated in tissues including but not limited to those listed in Table I. The presence of significant 101P3A II 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 101P3AI I nRNA or express it at lower levels. In a related embodiment, IOlP3A1 1 status is determined at the protein level rather than at the nucleic acid level. For example, such a method comprises determining the level of 10 1 P3AI I protein expressed by cells in a test tissue sample and comparing the level so determined to the level of 101P3A II expressed in a corresponding normal sample. In one embodiment, the presence of 101P3A1 1 protein is evaluated, for example, using immunobistochemical methods. IOP3A11 antibodies or binding partners capable of detecting 1OIP3AI I 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 101P3AI 1 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules. These perturbations can include insertions, deletions, substitutions and the like. Such evaluations are useful because perturbations in the nucleotide 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 101P3AI 1 may be indicative of the presence or promotion of a tumor. Such assays therefore have diagnostic and predictive value where a mutation in 1OlP3AI 1 indicates a potential loss of function or increase in tumor growth. A wide variety of assays for observing perturbations in nucleotide and amino acid sequences are well known in the art. For example, the size and structure of nucleic acid or amino acid sequences of 101P3AI I gene products are observed by the Northern, Southern, 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 101 P3A 11 gene in a biological sample. Aberrant demethylation and/or hypermethylation of CpG islands in gene 5' regulatory regions frequently occurs in 56 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 el 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 al., Cancer Epidemiol. Biomarkers Prev., 1998, 7:531-536). In another example, expression of the LAGE-I 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 bisulfite (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 el al. eds., 1995. Gene amplification is an additional method for assessing the status of IOIP3AI 1. Gene amplification is measured in a sample directly, for example, by conventional Southern blotting or Northern blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Natil. Acad. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or in situ hybridization, using an appropriately labeled probe, based on the sequences provided herein. Alternatively, antibodies are employed that recognize specific duplexes, including 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 detcctcd. Biopsied tissue or peripheral blood can be conveniently assayed for the presence of cancer cells using for example, Northern, dot blot or RT-PCR analysis to detect 101P3A I I expression. The presence of RT-PCR amplifiable IOIP3AI I 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 include RT-PCR assays for the detection of cells expressing PSA and PSM (Verkaik et aL, 1997, Urol. Res. 25:373-384; Ghossein el al., 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 IOIP3AI I mRNA or IOP3A1 I protein in a tissue sample, its presence indicating susceptibility to cancer, wherein the degree of IOIP3Al I mRNA expression correlates to the degree of susceptibility. In a specific embodiment, the presence of IOIP3AI 1 in prostate or other tissue is examined, with the presence of IOP3AI I 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 IOIP3AI I 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 57 perturbations in.IOIP3A II 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 101P3A 11 mRNA or 101P3A 11 protein expressed by tumor cells, comparing the level so determined to the level of 101P3A 11 mRNA or 101 P3A II protein expressed in a corresponding normal tissue taken from the same individual or a normal tissue reference sample, wherein the degree of IOIP3AI I mRNA or IOP3AI 1 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 1OIP3AI I is expressed in the tumor cells, with higher expression levels indicating more aggressive tumors. Another embodiment is the evaluation of the integrity of I1P3AI I 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 IO1P3Al I mRNA or lOP3AI I protein expressed by cells in a sample of the tumor, comparing the level so determined to the level of IOIP3AI I iRNA or 101P3A1 I protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of IOIP3Al I mRNA or IOIP3A 1I 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 O1P3AI 1 expression in the tumor cells over time, where increased expression over time indicates a progression of the cancer. Also, one can evaluate the integrity 10 1P3AI 1 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 O1P3A1 I gene and IOIP3AI 1 gene products (or perturbations in OIP3A11 gene and 101P3A1 1 gene products)ind 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 at., 1998, Mod. Pathol. I 1(6):543-51; Baisden et aL, 1999, Am. J. Surg. Pathol. 23(8):918-24). Methods for observing a coincidence between the expression of IOP3A II gene and IOIP3AI 1 gene products (or perturbations in 10 IP3AI I gene and IOP3AI I 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 10 1 P3A I I gene and OP3A II gene products (or perturbations in 1OP3A II gene and 1OP3AI I gene products) and another factor associated with malignancy entails detecting the overexpression of 101 P3A II 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 58 observing a coincidence of IOP3AI 1 mRNA or protein and PSA mRNA or protein overexpression (or PSCA or PSM expression). In a specific embodiment, the expression of 10 1 P3A I I and PSA mRNA in prostate tissue is examined, where the coincidence of 101 P3A 11 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 101 P3A 11 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 IOIP3AI I mRNA include in situ hybridization using labeled 1OIP3A1 I riboprobes, Northern blot and related techniques using IOIP3A1 1 polynucleotide probes, RT-PCR analysis using primers specific for IO1P3Al 1, 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 1OP3A 1I mRNA expression. Any number of primers capable of amplifying 1OP3A 11 can be used for this purpose, including 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 10 IP3A I I protein can be used in an immunohistochemical assay of biopsied tissue. IX.) Identification of Molecules That Interact Will 101 P13A11 The IOIP3Al I protein and nucleic acid sequences disclosed herein allow a skilled artisan to identify proteins, small molecules and other agents that interact with 10 IP3A 11, as well as pathways activated by IO1P3AI I 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 IOP3AI I protein sequences. In such methods, peptides that bind to 101P3AI I 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 10 lP3A I I 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 1OIP3A II 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 101P3AI I are used to identify protein-protein interactions mediated by 10 1P3A 11. Such interactions can be examined using immunoprecipitation techniques (see, e.g., Hamilton B.J., et al. Biochem. Biophys. Res. Commun. 1999, 261:646-51). 101P3AI I protein can be immunoprecipitated from IOIP3AI 1-expressing cell lines using anti-lOIP3AI I antibodies. Alternatively, antibodies against His-tag can be used in a cell line engineered to express fusions of 101 P3A 11 and a His-tag (vectors mentioned above). The immunoprecipitated complex can be examined for protein association by procedures such as Western 59 blotting, "S-methionine labeling of proteins, protein microsequencing, silver staining and two-dimensional gel electrophoresis. Small molecules and ligands that interact with 101P3AI I 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 101P3AI I'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 I0IP3A 1I-related ion channel, protein pump, or cell communication functions are identified and used to treat patients that have a cancer that expresses 10 1P3A 11 (see, e.g., Hille, B., Ionic Channels of Excitable Membranes 2 "d Ed., Sinauer Assoc., Sunderland, MA, 1992). Moreover, ligands that regulate I0IP3A1 I function can be identified based on their ability to bind I0IP3A1 I 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 u fusion protein of 101P3AI I and a DNA-binding protein arc used to co-express a fusion protein of a hybrid ligand/small molecule and a cDNA 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 101P3A11. An embodiment of this invention comprises a method of screening for a molecule that interacts with a I01P3AlI1 amino acid sequence shown in Figure 2 or Figure 3, comprising the steps of contacting a population of molecules with a 101P3AI 1 amino acid sequence, allowing the population of molecules and the 10 IP3A II amino acid sequence to interact under conditions that facilitate an interaction, determining the presence of a molecule that interacts with the 101 P3A 1 amino acid sequence, and then separating molecules that do not interact with the I0IP3A1 I 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 101P3A1 1 amino acid sequence. The identified molecule can be used to modulate a function performed by 1OIP3AI 1. In a preferred embodiment, the 101P3A II amino acid sequence is contacted with a library of peptides. X.) Therapeutic Methods and Compositions The identification of 10IP3A1 I 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, 101P3A I I 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 IO1P3AII protein are useful for patients suffering from a cancer that expresses 101 P3A 11. These therapeutic approaches generally fall into two classes. One class comprises various methods for inhibiting the binding or association of a IOIP3A 1I protein with its binding partner or with other proteins. Another class comprises a variety of methods for inhibiting the transcription of a 10IP3A11 gene or translation of IOIP3AI I niRNA. X.A.) Anti-Cancer Vaccines 60 The invention provides cancer vaccines comprising a 101P3A 1I-related protein or 10 lP3Al 1-related nucleic acid. In view of the expression of 1OIP3AI 1, cancer vaccines prevent and/or treat 1OIP3A1 1-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 been employed in prostate cancer using human PSMA and rodent PAP immunogens (Hodge et a., 1995, Int. J. Cancer 63:231-237; Fong et a., 1997, J. Immunol. 159:3113-3117). Such methods can be readily practiced by employing a 101P3A1 1-related protein, or a IOIP3AI I encoding nucleic acid molecule and recombinant vectors capable of expressing and presenting the 101 P3A 11 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 a., 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 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 101P3A II 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 101P3A1 1 immunogen contains a biological motif, see e.g., Tables V-XVIII and XXI TO IL, or a peptide of a size range from 101P3A1 1 indicated in Figure 5, Figure 6, Figure 7, Figure 8, and Figure 9. The entire I1P3AI I 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 a., J. Clin. Invest. 95:341, 1995), peptide 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 a., Nature 344:873-875, 1990; Hu et a., Clin Exp Immunol. 113:235-243, 1998), multiple antigen peptide systems (MAPs) (see e.g., Tam, J. P., Proc. Nat!. Acad. Sci. U.S.A. 85:5409-5413, 1988; Tam, J.P., J. Immunol. Methods 196:17-32, 1996), peptides formulated as multivalent peptides; peptides for use in ballistic delivery systems, typically crystallized peptides, viral delivery vectors (Perkus, M. E. et a., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 379, 1996; Chakrabarti, S. et a., Nature 320:535, 1986; Hu, S. L. et a., Nature 320:537, 1986; Kieny, M.-P. et al., AIDS Bio/Technology 4:790,1986; Top, F. H. et al., J. Infect. Dis. 124:148, 1971; Chanda, P. K. et a., Virology 175:535, 1990), particles of viral or synthetic origin (e.g., Kofler, N. et a., J. Immunol. Methods. 192:25, 1996; Eldridge, J. H. et a., Semn. Henatol. 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; Gupta, R. K. et a., 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 a., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 423, 1996; Cease, K. B., and Berzofsky, J. A., Annu. Rev. Immunol. 12:923, 1994 and Eldridge, J. H. et a., 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. 61 In patients with 101P3AI I-associated cancer, the vaccine compositions of the 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: CTL epitopes can be determined using specific algorithms to identify peptides within I0lP3Al I protein that bind corresponding HLA alleles (see e.g., Table IV; Epimer" and EpimatrixTm, Brown University (URL www.brown.edu/ResearchrfB-HIVLab/epimatrix/epimatrix.htmil); and, BIMAS, (URL biias.dcrt.nih.gov/; SYFPEITHI at URL syfpeithi.bmi-heidelberg.com/). In a preferred embodiment, a 101 P3A 11 immunogen contains one or more amino acid sequences identified using techniques well known in the art, such as the sequences shown in Tables V-XVIII and XXII TO IL or a peptide of 8, 9, 10 or I1 amino acids specified by an HLA Class I motiflsupermotif (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 II 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 long. In contrast, the HLA Class II binding groove is essentially open ended; therefore a peptide of about 9 or more amino acids can be bound by an HLA Class 1H molecule. Due to the binding groove differences between HLA Class I and II, 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 I1 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 II 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 I0IP3A1 I protein) so that an immune response is generated. A typical embodiment consists of a method for generating an immune response to l01P3Al1 in a host, by contacting the host with a sufficient amount of at least one IOP3AI I B cell or cytotoxic T-cell epitope or analog thereof; and at least one periodic interval thereafter re contacting the host with the l10P3A 11 B cell or cytotoxic T-cell epitope or analog thereof. A specific embodiment consists of a method of generating an immune response against a 101P3Al1 -related protein or a man-made multiepitopic peptide comprising: administering 101P3AI I immunogen (e.g. a 101P3AI I protein or a peptide fragment thereof, a 101P3AI I 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 PADRET" peptide (Epimmune Inc., San Diego, CA; see, e.g., Alexander et a., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et a., Immunity 1994 1(9): 751 761 and Alexander et a., Immunol. Res. 1998 18(2): 79-92). An alternative method comprises generating an immune response in an individual against a 101 P3A 11 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 101 P3A II 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 62 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 101P3A 11, 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 O1P3A1 1. Constructs comprising DNA encoding a IOIP3AI I-related protein/immunogen and appropriate regulatory sequences can be injected directly into muscle or skin of an individual, such that the cells of the muscle or skin take-up the construct and express the encoded IOP3A1 I protein/immunogen. Alternatively, a vaccine comprises a 1OP3AI 1-related protein. Expression of the IOIP3A 1I-related protein immunogen results in the generation of prophylactic or therapeutic humoral and cellular immunity against cells that bear a 1OIP3A1 1 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 www.genweb.com). Nucleic acid-based delivery is described, for instance, in Wolff et. al., 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, fowlpox, canarypox, adenovirus, influenza, poliovirus, adeno-associated virus, lentivinms, and sindbis virus (see, e.g., Restifo, 1996, Curr. Opin. Immunol. 8:658-663; Tsang et al. J. NatI. Cancer 1isL 87:982-990 (1995)). Non-viral delivery systems can also be employed by introducing naked DNA encoding a OIP3AI I-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 101P3A1 1-related nucleic acid molecule. In one embodiment, the full-length human 1OIP3Al I cDNA is employed. In another embodiment, OP3A II 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 10 1 P3A I I antigen to a patient's immune system. Dendritic cells express MHC class I and i 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 63 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 101P3A II peptides to T cells in the context of MHC class I or I molecules. In one embodiment, autologous dendritic cells are pulsed with 101P3AI I peptides capable of binding to MHC class I and/or class II molecules. In another embodiment, dendritic cells are pulsed with the complete IOP3A I 1 protein. Yet another embodiment involves engineering the overexpression of a 101 P3A I1 gene in dendritic cells using various implementing vectors known in the art, such as adenovirus (Arthur et at., 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 al., 1997, Cancer Res. 57:2865-2869), or tumor-derived RNA transfection (Ashley et al., 1997, J. Exp. Med. 186:1177-1182). Cells that express 101P3A II can also be engineered to express immune modulators, such as GM-CSF, and used as immunizing agents. X.B.) 101P3A11 as a Target for Antibody-based Therapy 101P3A II 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 101P3A1 1 is expressed by cancer cells of various lineages relative to corresponding normal cells, systemic administration of 101P3AI I-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 101P3Al 1 are useful to treat 101P3AI I-expressing cancers systemically, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting cell proliferation or function. 10 1P3Al I antibodies can be introduced into a patient such that the antibody binds to 101 P3A 11 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 1O1P3A 11, 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 10 lP3AI 1 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 aL 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. 1O1P3A 11), 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-IOIP3AI I antibody) that binds to a marker (e.g. 1lP3Al I) 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 1lP3A1 1, comprising conjugating the cytotoxic agent to an antibody that immunospecifically binds to a 101P3AI 1 epitope, and, exposing the cell to the antibody-agent conjugate. 64 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-101P3A II 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 (Arlen et al., 1998, Crit. Rev. Immunol. 18:133-138), multiple myeloma (Ozaki et al., 1997, Blood 90:3179-3186, Tsunenari et al., 1997, Blood 90:2437-2444), gastric cancer (Kasprzyk et al., 1992, Cancer Res. 52:2771-2776), B-cell lymphoma (Funakoshi et 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 al., 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 Y 9 ' or I"' to anti-CD20 antibodies (e.g., Zevalinm, IDEC Pharmaceuticals Corp. or BexxarTM, Coulter Pharmaceuticals), while others involve co-administration of antibodies and other therapeutic agents, such as Herceptin" m ' (trastuzumab) with paclitaxel (Genentech, Inc.). The antibodies can be conjugated to a therapeutic agent. To treat prostate cancer, for example, 101 P3A 11 antibodies can be administered in conjunction with radiation, chemotherapy or hormone ablation. Also, antibodies can be conjugated to a toxin such as calichearnicin (e.g., Mylotarg'M, Wyeth-Ayerst, Madison, NJ, a recombinant humanized IgG 4 kappa antibody conjugated to antitumor antibiotic 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 10lP3AI I 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 10P3AI 1 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 prcscnce and level of 101P3AI I expression, preferably using immunohistochemical assessments of tumor tissue, quantitative 101 P3A II imaging, or other techniques that reliably indicate the presence and degree of 101P3AI I expression. lmmunohistochemical 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. 65 Anti-101P3AI 1 monoclonal antibodies that treat prostate and other cancers include those that initiate a potent immune response against the tumor or those that are directly cytotoxic. In this regard, anti-lOlP3A1l monoclonal antibodies (mAbs) can elicit tumor cell lysis by either complement-mediated or antibody-dependent cell cytotoxicity (ADCC) mechanisms, both of which require an intact Fc portion of the immunoglobulin molecule for interaction with effector cell Fc receptor sites on complement proteins. In addition, anti-101P3A1 I mAbs that exert a direct biological effect on tumor growth are useful to treat cancers that express 101 P3A 11. 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-101P3AI I 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 clearance 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 IOIP3A I 1 antigen with high affinity but exhibit low or no antigenicity in the patient. Therapeutic methods of the invention contemplate the administration of single anti-101P3A 11 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- 101 P3A II 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-101P3AI I mAbs are administered in their "naked" or unconjugated form, or can have a therapeutic agcnt(s) conjugated to them. Anti-101P3A1 1 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. Treatment generally involves repeated administration of the anti-IOP3AI 1 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., I, 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 HerceptinTm 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-101 P3A 11 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 10IP3AI 1 expression in the patient, the extent of circulating shed 101P3AI 1 antigen, the desired steady-state antibody concentration level, frequency of 66 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 101P3AI 1 in a given sample (e.g. the levels of circulating IOP3Al 1 antigen and/or IOIP3AI I 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-101P3AI I antibodies can also be used in anti-cancer therapy as a vaccine for inducing an immune response to cells expressing a O1P3A1 I-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-101P3A1 1 antibodies that mimic an epitope on a IOIP3AI 1-related protein (see, for example, Wagner et al., 1997, Hybridoma 16: 33-40; Foon et aL., 1995, J. Clin. Invest. 96:334-342; Herlyn et aL., 1996, Cancer Immunol. Immunother. 43:65-76). Such an anti-idiotypic antibody can be used in cancer vaccine strategies. X.C.) 1OIP3All 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., recombinantly or by chemical synthesis. Carriers that can be used with vaccines of the invention are well 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) 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 lipids, such as tripalmitoyl-S-glycerylcysteinlyseryl- serine (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 10IP3Al I antigen, or derives at least some therapeutic benefit when the antigen was tumor-associated. 67 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 11 epitopes in accordance with the invention. An alternative embodiment of such a composition comprises a class I and/or class 11 epitope in accordance with the invention, along with a cross reactive HTL epitope such as PADREm (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 dendritic 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 arc utilized when selecting an array of epitopcs for inclusion in a polyepitopic composition for use in a vaccine, or for selecting discrete epitopes to be included 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. I.) 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 II a similar rationale is employed; again 3-4 epitopes are selected from at least one TAA (see, e.g., Rosenberg et al., 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 ICw of 500 nM or less, often 200 nM or less; and for Class II an ICs, 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 antigens 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 II 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. 68 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 epitopcs (an epitope recognized by the immune system, not present in the target antigen, and only created by the nian-nmade 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 11 binding peptide be conserved in a designated percentage of the sequences evaluated for a specific protein antigen. X.C.I. 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 al., J. Immunol. 162:3915-3925, 1999; An, L. and Whitton, J. L., J Virol. 71:2292, 1997; Thomson, S. A. er a., J Immunol. 157:822, 1996; Whitton, J. L. et a., J. Virol. 67:348, 1993; Hanke, R. et a., Vaccine 16:426, 1998. For example, a multi-epitope DNA plasmid encoding supermotif- and/or motif-bearing epitopes derived I0lP3A1 1, the PADRE@ universal helper T cell epitope or multiple HTL epitopes from I0lP3A 11, (see e.g., Tables V-XVIII and XXII to IL), and an endoplasmic reticulum-translocating signal sequence can be engineered. A vaccine may also comprise epitopes that are derived from other TAAs. The innunogenicity 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 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 I epitopes, antibody epitopes, a ubiquitination signal sequence, and/or an endoplasmic reticulum 69 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 CTIL 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 cells. 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-12, GM-CSF), cytokine-inducing molecules (e.g., LeIF), costimulatory molecules, or for HTL responses, pan-DR binding proteins (PADRE", Epimmune, San Diego, CA). Helper (HTL) epitopes can be joined to intracellular 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 II 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 cell bank are used to inoculate growth medium, and grown to saturation in shaker flasks or a bioreactor according to well-known techniques. Plasmid DNA can be purified using standard bioseparation technologies such as solid phase anion-exchange resins supplied by QIAGEN, Inc. 70 (Valencia, California). If required, supercoiled DNA can be isolated from the open circular and linear forms using gel electrophoresis or other methods. Purified plasnid 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, Bio Techniques 6(7): 682 (1988); U.S. Pat No. 5,279,833; WO 91/06309; and Feigner, et aL, Proc. Nat 'lAcad. 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 (''Cr) labeled and used as target cells for epitope-specific CTL lines; cytolysis, detected by 5t 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 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 CTLs. Immunogenicity of HTL epitopes is confirmed in transgenic mice in an analogous manner. Alternatively, the nucleic acids 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, DNA can 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. 71 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 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 genetically diverse population. This can be accomplished by selecting peptides that bind to many, most, or all of the HLA class II molecules. Examples of such amino acid bind many HLA Class Il molecules include sequences from antigens such as tetanus toxoid at positions 830-843 QYIKANSKFIGITE (SEQ ID NO: _, Plasmodlumfalciparum circumsporozoite (CS) protein at positions 378-398 DIEKKIAKMEKASSVFNVVNS (SEQ ID NO: __J, and Streplococcus 18kD protein at positions 116-131 GAVDSILGGVATYGAA (SEQ ID NO: __). 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., PADRETM, Epimmune, Inc., San Diego, CA) are designed to most preferably bind most HLA-DR (human HLA class II) molecules. For instance, a pan-DR-binding epitope peptide having the formula: aKXVAAWTLKAAa (SEQ ID NO: __), 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 "L" 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 6-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 lipidated peptide can then be administered cithcr directly in a micelle or particle, incorporated into a liposome, 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 72 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- serine (P3CSS) can be used to prime virus specific CTL when covalently attached to an appropriate peptide (see, e.g., Deres, et al., Nature 342:561, 1989). Peptides of the invention can be coupled to

P

3 CSS, for example, and the lipopeptide administered to an individual to specifically prime an immune response to the target antigen. Moreover, because the induction of neutralizing antibodies can also be primed with P 3

CSS

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 and/or 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 ProgenipoietinTM (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 O1P3AI1. Optionally, a helper T cell (HTL) peptide, such as a natural or artificial loosely restricted HLA Class II 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 101 P3A 11. X.D. Adoptive Immunotherapy Antigenic IOP3AI I-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 Purposcs Pharmaceutical and vaccine compositions of the invention are typically used to treat and/or prevent a cancer that expresses or overexpresses 101P3A 11. 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 101P3A 11. The peptides or 73 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 10 l P3A I 1-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 101P3A1 1, a vaccine comprising IOIP3AI I-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 effectively stimulate a cytotoxic T cell response; compositions which stimulate helper T cell responses can also be given in accordance with this embodiment of the invention. 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 patient's 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 carrier, preferably an aqueous carrier. 74 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 volumc/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, 17"' 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 pug, 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 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 5-10' to 5x10' pfu. For antibodies, a treatment generally involves repeated administration of the anti- 101P3A 11 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 10-500 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- 101 P3A 11 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 101 P3AI 1 expression in the patient, the extent of circulating shed 1OIP3AI I 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, img - 50mg, 50mg - 100mg, 100mg - 200mg, 200mg - 300mg, 400mg - 500mg, 500mg - 600mg, 600mg - 700mg, 7 00mg - 800mg, 800mg - 900mg, 900mg - lg, 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; I-6 0 0mg m 2 of body area weekly; 2 25-400mg m 2 of body area weekly; these does can be followed by weekly doses for 2, 3, 4, 5, 6, 7, 8, 9, 19, I1, 12 or more weeks. 75 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, I 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 104 cells to about 10 cells, about 106 cells to about 10' cells, about 10' to about 10"1 cells, or about 10' to about 5 x 1010 cells. A dose may also about 10* cells/m 2 to about 10'0 cells/m 2 , or about 10* cells/rn to about 10' 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. Liposomes include emulsions, foams, micelles, insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. In these preparations, the 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. 76 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 cnploycd excipicnts, 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/o by weight, preferably about %o-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, linoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cyclic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. The surfactant may constitute about 0.l%-20% by weight of the composition, preferably about 0.25 5%. The balance of the composition is ordinarily propellant. A carrier can also be included, as desired, as with, e.g., lecithin for intranasal delivery. XI.) Diagnostic and Prognostic Embodiments of 101P3A1 1. As disclosed herein, OIP3A1I1 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 lOlP3AI 1 in normal tissues, and patient specimens"). 101 P3AI 1 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 a!., J. Urol. 163(2): 503-5120 (2000); Polascik et a., J. Urol. Aug; 162(2):293-306 (1999) and Fortier et a., J. Nat. 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 a., Int J Mol Med 1999 Jul 4(1):99-102 and Minimoto et a., Cancer Detect Prev 2000;24(1):1-12). Therefore, this disclosure of IOP3AI I polynucleotides and polypeptides (as well as lO1P3A 1I polynucleotide probes and anti-IOP3Al I 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. Typical embodiments of diagnostic methods which utilize the lOlP3A 1 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 a., 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 101P3A II polynucleotides described herein can be utilized in the same way to detect 101 P3A I I overexpression or the metastasis of prostate and other cancers 77 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 10 lP3AI I polypeptides described herein can be utilized to generate antibodies for use in detecting 101P3AI I 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 lymph node), assays which examine a biological sample for the presence of cells expressing 101 P3A II 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 101 P3A 11-expressing cells (lymph node) is found to contain 101 P3A 11 -expressing cells such as the 101P3Al I expression seen in LAPC4 and LAPC9, xenografts isolated from lymph node and bone metastasis, respectively, this finding is indicative of metastasis. Alternatively O1P3A 11 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 101P3A II or express 101P3Al 1 at a different level are found to express 101P3AI I or have an increased expression of 101P3A1 1 (see, e.g., the 101P3AI I 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 a second tissue restricted marker (in addition to 101P3AI I) 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, 101P3A 11 polynucleotide fragments and polynucleotide variants are used in an analogous manner. In particular, typical PSA polynucleotides used in methods of monitoring PSA are probes or primers which consist of fragments of the PSA cDNA 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 101P3A1 1 in normal tissues, and patient specimens," where a 101P3AI 1 polynucleotide fragment is used as a probe to show the expression of OIP3A 11 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 11 (6):407-13 and Current Protocols In Molecular Biology, Volume 2, Unit 2, Frederick M. Ausubel et aL. 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 101P3A1 1 polynucleotide shown in Figure 2 or variant thereof) under conditions of high stringency. 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. IOP3AI 1 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 78 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 101P3AI I 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 IOIP3A 1I polypeptide shown in Figure 3). As shown herein, the 101P3AI 1 polynucleotides and polypeptides (as well as the 101P3AI 1 polynucleotide probes and anti-101P3A II 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 I. Diagnostic assays that measure the presence of 101P3A 1 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 al., Pathol. Res. Pract. 192(3): 233-237 (1996)), and consequently, materials such as 101P3A1 I polynucleotides and polypeptides (as well as the lOlP3A1 I polynucleotide probes and anti-1OP3A1 I 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 101P3A 1I polynucleotides 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 10IP3A1 I gene maps (see the Example entitled "Chromosomal Mapping of 1OIP3AI I" below). Moreover, in addition to their use in diagnostic assays, the 1OIP3AI 1-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, 10 P3A1 I-related proteins or polynucleotides of the invention can be used to treat a pathologic condition characterized by the over-expression of 101P3A 11. 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 IOP3Al1 antigen. Antibodies or other molecules that react with 1OP3Al I can be used to modulate the function of this molecule, and thereby provide a therapeutic benefit. XII.) Inhibition of 101P3A1I Protein Function The invention includes various methods and compositions for inhibiting the binding of 101P3AI Ito its binding partner or its association with other protein(s) as well as methods for inhibiting 10 1P3A 11 function. XU.A.) Inhibition of 1OIP3A11 With Intracellular Antibodies In one approach, a recombinant vector that encodes single chain antibodies that specifically bind to 101P3AI I are introduced into 101P3A II expressing cells via gene transfer technologies. Accordingly, the encoded single chain anti-101P3AI 1 antibody is expressed intracellularly, binds to 101P3AI I protein, and thereby inhibits its function. Methods for engineering such intracellular single chain antibodies are well known. 79 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. Natl. Acad. Sci. USA 92: 3137-3141; Beerli el al., 1994, ). Biol. Chem. 289: 23931-23936; Deshane el 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 precisely target 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 (SEQ ID NO: ) 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 101P3A I tin the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals arc engineered into such 101P3AI I intrabodics in order to achieve the desired targeting. Such 101P3A I I intrabodics arc designed to bind specifically to a particular 1OIP3AI 1 domain. In another embodiment, cytosolic intrabodies that specifically bind to a l10P3AI 1 protein are used to prevent 101P3Al I from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 101P3AI 1 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). XIT.B.) Inhibition of 10IP3A11 with Recombinant Proteins In another approach, recombinant molecules bind to 101 P3A 11 and thereby inhibit 101P3A 11 function. For example, these recombinant molecules prevent or inhibit 101 P3A 11 from accessing/binding to its binding partner(s) or associating with other protein(s). Such recombinant molecules can, for example, contain the reactive part(s) of a 101P3A1 I specific antibody molecule. In a particular embodiment, the IOP3A1 I binding domain of a IOP3A1 I binding partner is engineered into a dimeric fusion protein, whereby the fusion protein comprises two OP3AI I ligand binding domains linked to the Fc portion of a human IgG, such as human IgGl. Such IgG portion can contain, for example, the CH2 and CH 3 domains and the hinge region, but not the CHI domain. Such dimeric fusion proteins are administered in soluble form to patients suffering from a cancer associated with the expression of IOIP3A 1I, whereby the dimeric fusion protein specifically binds to 10IP3AII and blocks 10IP3A1 I interaction with a binding partner. Such dimeric fusion proteins are further combined into multimeric proteins using known antibody linking technologies. 80 XII.C.) Inhibition of 101P3AI Transcription or Translation The present invention also comprises various methods and compositions for inhibiting the transcription of the 101P3A 1 gene. Similarly, the invention also provides methods and compositions for inhibiting the translation of 10 1P3A I1 mRNA into protein. In one approach, a method of inhibiting the transcription of the 101P3AI I gene comprises contacting the 10lP3AI I gene with a O10P3AI I antisense polynucleotide. In another approach, a method of inhibiting 101P3A1 I mRNA translation comprises contacting a 10lP3A11 mRNA with an antisense polynucleotide. In another approach, a 10IP3AI 1 specific ribozyme is used to cleave a 101P3A I message, thereby inhibiting translation. Such antisense and ribozyme based methods can also be directed to the regulatory regions of the 10 1P3Al 1 gene, such as 101 P3A 11 promoter and/or enhancer elements. Similarly, proteins capable of inhibiting a IOP3AI 1 gene transcription factor are used to inhibit 10IP3AI 1 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 10 1P3AI I by interfering with 101P3AI I transcriptional activation are also useful to treat cancers expressing 101P3Al 1. Similarly, factors that interfere with 101P3AI I processing are useful to treat cancers that express 101P3A 11. 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 polynucleotide molecules to tumor cells synthesizing IOP3AI I (i.e., antisense, ribozyme, polynucleotides encoding intrabodies and other 1OIP3AI 1 inhibitory molecules). A number of gene therapy approaches are known in the art. Recombinant vectors encoding 101P3A1 I antisense polynucleotides, ribozymes, factors capable of interfering with I0IP3A1I1 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 vitro and in vivo assay systems. In vitro assays that evaluate therapeutic activity include 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 OIP3AI 1 to a binding partner, etc. In vivo, the effect of a 10lP3A1 I 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 a., 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 metastascs characteristic of late stage disease. Efficacy can be predicted using assays that measure inhibition of tumor formation, tumor regression or metastasis, and the like. 81 In vivo 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. The therapeutic compositions used in the practice of the foregoing methods can be formulated into pharmaceutical compositions comprising a carrier suitable for the desired delivery method. Suitable carriers include 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 polyvinylchloride 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. XIH.) 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 fom 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 82 or in vitro-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 "article 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), nucleic 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 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 alternatively 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 IOP3AI 1 and modulating the function of O1lP3AI1. 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 I. The article of manufacture can further comprise a second container comprising a pharmaceutically-acceptable buffer, such as phosphate-buffered saline, Ringer's 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. XIV.) Evaluation of GPCRs and Modulators Thereof The traditional study of receptors has always proceeded from the a priori assumption (historically based) that the endogenous ligand must first be identified before discovery could proceed to find antagonists and other molecules that could affect the. receptor. Even in cases where an antagonist might have been known first, the search immediately extended to looking for the endogenous ligand. This mode of thinking has persisted in receptor research even after the discovery of constitutively activated receptors. What has not been recognized is that it is the active state of the receptor that is most useful for discovering agonists, partial agonists, and inverse agonists of the receptor. For those diseases that result from an overly active receptor, what is desired in a therapeutic, drug is a compound which acts to diminish the active state of a receptor, not necessarily a drug which is an antagonist to the endogenous ligand. This is because a compound (e.g., therapeutic, prophylactic, diagnostic, prognostic, or laboratory reactant) that reduces the activity of the active receptor state need not bind at the same site as the endogenous ligand. In accordance with the present disclosure, any search for relevant compounds should start by screening compounds against the ligand-independent active state. The search, then, is for an inverse agonist to the active state receptor. 83 Screening candidate compounds against orphan receptors, for example, including and not limited to, 10IP3AI I and 101P3A II Fusion Protein, allows for the direct identification of candidate compounds which act at the orphan cell surface receptor, without requiring any prior knowledge or use of the receptor's endogenous ligand. By determining areas within the body where such receptors are expressed and/or over-expressed, it is possible to determine related disease/disorder states which are associated with the expression and/or over expression of these receptors; such an approach is disclosed herein. Disease/Disorder Identification and/or Selection. Inverse agonists and agonists to 101P3AI 1 can be identified by the methodologies disclosed herein. Such inverse agonists and agonists are ideal candidates as lead compounds in drug discovery programs for treating diseases related to this receptor. Indeed, an antagonist to such a receptor (even if the ligand were known) may be ineffective given that the receptor is activated even in the absence of ligand-receptor binding. Because of the ability to directly identify inverse agonists and agonists to these receptors, thereby allowing for the development of pharmaceutical compositions, a search for diseases and disorders associated with these receptors is possible. For example, 101P3A II is expressed in cancers of the tissues set forth in Table I. XV.) Screening of Candidate Compounds General GPCR Sscreening Assay techniques When a G protein receptor becomes constitutively active, it binds to a G protein (for example Gq, Gs, Gi, Go) and stimulates the binding of GTP to the G protein. The G protein then acts as.a GTPase and slowly hydrolyzes the GTP to GDP, whereby the receptor, under normal conditions, becomes deactivated. However, constitutively activated receptors continue to exchange GDP to GTP. A non-hydrolyzable analog of GTP, [35S)GTP7S, can be used to monitor enhanced binding to membranes which express constitutively activated receptors. It is reported that (35 S]GTP7S can be used to monitor G protein coupling to membranes in the absence and presence of ligand. An example of this monitoring, among other examples well-known and available to those in the art, was reported by Traynor and Nahorski in 1995 (Mol Pharmacol. 1995 Apr;47(4):848-54). Generally, this preferred use of this assay system is for initial screening of candidate compounds because the system is generically applicable to all G protein-coupled receptors regardless of the particular G protein that interacts with the intracellular domain of the receptor. Specific GPCR screening assay techniques Once candidate compounds are identified using the "generic" G protein- coupled receptor assay (i.e. an assay to select compounds that are agonists, partial agonists, or inverse agonists), farther screening to confirm that the compounds have interacted at the receptor site is preferred. For example, a compound identified by the "generic" assay may not bind to the receptor, but may instead merely "uncouple" the G protein from the intracellular domain. Thus, by screening those candidate compounds, which have been identified using a "generic" assay in an agonist and/or antagonist competitive binding assay, farther refinement in the selection process is provided. In the case of IOP3AI lit has been determined that this receptor couples the G protein Gs. Gs stimulates the enzyme adenylyl cyclase (Gi, on the other hand, inhibits this enzyme). Adenylyl cyclase catalyzes the conversion of ATP to cANT; thus, assays that detect cANT can be utilized, for example and not limitation, cell-based cANT assay, to determine if a candidate compound is an inverse agonist to the receptor (i.e., such a compound which contacts the receptor would decrease the levels of 84 cAMP relative to the uncontacted receptor). As a result, "cyclase-based assays" can be used to further screen those compounds selected from an agonist and/or antagonist competitive binding assay. XVI.) GPCR Fusion Proteins The use of an endogenous, constitutively activated orphan GPCRs, such as 101P3A 1, for use in screening of candidate compounds for the direct identification of inverse agonists, agonists and partial agonists, provides a unique challenge in that, by definition, the endogenous receptor is active even in the absence of an endogenous ligand bound thereto. Thus, in order to differentiate between, e.g., the endogenous receptor in the presence of a candidate compound and the endogenous receptor in the absence of that compound, with an aim of such a differentiation to allow for an understanding as to whether such compound may be an inverse agonist, agonist, partial agonist or have no affect on such a receptor, it is preferred that an approach be utilized that can enhance such differentiation. A preferred approach is the use of a GPCR Fusion Protein. Generally, once it is determined that an endogenous orphan GPCR is constitutively activate, using the assay techniques set forth herein (as well as others known in the art), it is possible to determine the predominant G protein that couples with the endogenous GPCR. Coupling of the G protein to the GPCR provides a signaling pathway that can be assessed. Because it is most preferred that screening take place by use of a mammalian expression system, such a system will be expected to have endogenous G protein therein. Thus, by definition, in such a system, the endogenous, constitutively active orphan GPCR will continuously signal. In this regard, it is preferred that this signal be enhanced such that in the presence of, e.g., an inverse agonist to the receptor, it is more likely that one will be able to more readily differentiate, particularly in the context of screening, between the receptor when it is contacted with the inverse agonist. A GPCR Fusion Protein is intended to enhance the efficacy of G protein coupling with the endogenous GPCR. The GPCR Fusion Protein appears to be important for screening with an endogenous, constitutively activated GPCR because such an approach increases the signal that is most preferably utilized in such screening techniques. This is important in facilitating a significant "signal to noise" ratio. A significant ratio is preferred for the screening of candidate compounds as disclosed herein. The construction of a construct useful for expression of a GPCR Fusion Protein is within the purview of those having ordinary skill in the art. Commercially available expression vectors and systems offer a variety of approaches that can fit the particular needs of an investigator. The criteria of importance for such a GPCR Fusion Protein construct is that the endogenous GPCR sequence and the G protein sequence both be in- frame (preferably, the sequence for the endogenous GPCR is upstream of the G protein sequence) and that the "stop" codon of the GPCR must be deleted or replaced such that upon expression of the GPCR, the G protein can also be expressed. The GPCR can be linked directly to the G protein, or there can be spacer residues between the two (preferably, no more than about 12, although this number can be readily ascertained by one of ordinary skill in the art). Both approaches have been evaluated, and in terms of measurement of the activity of the GPCR, the results are substantially the same; however, there is a preference (based upon convenience) for use of a spacer in that some restriction sites that are not used will, upon expression, effectively, become a spacer. Most preferably, the G protein that couples to the endogenous GPCR will have been identified prior to the creation of the GPCR Fusion Protein construct. Because there are only a few G proteins that have been identified, it is preferred that a construct comprising the sequence of the G protein (i.e., a universal G protein construct) be available for insertion 85 of an endogenous GPCR sequence therein; this provides for efficiency in the context of large-scale screening of a variety of different endogenous GPCRs having different sequences. Pharmaceutical Compositions Candidate compounds selected for further development as active ingredients can be formulated into pharmaceutical compositions using techniques well known to those in the art. Suitable pharmaceutically-acceptable carriers are available to those in the art; for example, see Remington's Pharmaceutical Sciences, 16t" Edition, 1980, Mack Publishing Co., (Oslo et al., eds.). 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: Expression analysis of 101P3AII In normal tissues and patent specimens Analysis of 1OlP3AI 1 by RT-PCR is shown in Figure 10A. First strand cDNA was prepared from vital pool I (VP I: liver, lung and kidney), vital pool 2 (VP2, pancreas, colon and stomach), prostate xenograft pool, prostate cancer pool, kidney cancer pool, colon cancer pool, breast cancer pool, and cancer metastasis pool. Normalization was performed by PCR using primers to actin and GAPDH. Semi-quantitative PCR, using primers to lOP3AI 1, was performed at 30 cycles of amplification. Expression of 1OP3AI I was observed in prostate xenograft pool, prostate cancer pool, kidney cancer pool, colon cancer pool, breast cancer pool, and cancer metastasis pool, but not in VP 1 and VP2. Dot blots using patient-derived amplified cDNAs (Clontech, CA) show upregulation of PHOR-I in 3/3 prostate cancer patients, 6/14 kidney cancer patients, 2/8 uterine cancer, 1/1 cervical cancer, 3/8 stomach cancer, and in 7/7 rectal cancer patients (Figure 10B). Expression of 10lP3Al I was assayed in a panel of human patient cancer specimens (Figure 11). RNA was extracted from a pool of three prostate cancer tumors, kidney cancer tumors, colon cancer tumors, breast cancer tumors, and cancer metastasis pool derived from cancer patients, as well as from normal prostate (NP), normal bladder (NB), normal kidney (NK) and normal colon (NC). Northern blots with 10 pg of total RNA/lane were probed with a l0lP3A1 I sequence fragment. Size standards in kilobases (kb) are indicated on the side. The results show expression of lOP3A I in prostate cancer tumors, kidney cancer tumors, colon cancer tumors, breast cancer tumors, cancer metastasis pool, bladder cancer pool, and in the normal prostate but not in the other normal tissues. Northern blot analysis on individual prostate patient tumor specimens is shown in Figure 12A. RNA was extracted from prostate tumors (T) and their normal adjacent tissues (Nat) derived from prostate cancer patients. Northern blots with 10 pg of total RNA/lane were probed with 101 P3A II sequence. Results showed expression of 10IP3AI 1 in all three patient specimens, and expression is especially upregulated in one of the three prostate tumor tissues. RNA in situ analysis using anti-sense 101 P3AI I riboprobe showed significant glandular epithelial and basal cell expression in normal prostate (4/4), PIN (1/1), and prostate cancer (6/6) patients. IOIP3Al I sense riboprobe had little to no staining. The RNA in situ staining in PIN and prostate cancer is shown in Figure 12B and Figure 12C. The staining intensity in the cancer cells was generally higher than that observed in normal glands (Figure 12D and 12E). The RNA in situ results also demonstrate that the expression observed in the prostate tissues is in the glandular epithelia, basal cells, and cancer cells. 86 Endogenous expression of the 101P3AI 1 protein is demonstrated in the immunohistochemistry analysis of the anti-101P3A1 1 (PEPTIDE 1: amino acids 1-14) rabbit polyclonal antibody (Figure 40A-40F). Staining in prostate cancer is greater than the staining observed in normal prostate. The staining is localized apically within the luminal epithelia of the normal prostate (Figures 40E and 40F). The staining observed in prostate cancer is also localized apically in low to intermediate grade cancer (Figures 40B and 40C) and throughout all cells of more advanced prostate cancer (Figure 40A). Staining was observed in 19/20 normal prostate patients and in all of the nineteen prostate cancer patients analyzed. The prostate cancer cell line, LNCaP also shows similar staining (Figures 40D and 40F) in almost all cells. In addition, the present protocol was used to identify endogenous expression of the IOP3AI I protein in prostate cancer, bladder cancer, kidney cancer, colon cancer, lung cancer, and breast cancer. Immunohistochenical analysis was performed with the anti-101P3AI I (PEPTIDE 1: amino acids 1-14) rabbit polyclonal antibody (prostate cancer, Figure 41 A; bladder cancer, Figure 41 B; kidney cancer, Figure 41 C; colon cancer, Figure 41 D; lung cancer, Figure 41 E; and breast cancer, Figure 41 F). Specific staining is observed in tumor cells of the six cancers analyzed. Expression of 101P3AI 1 was also detected in the tumors of two colon cancer patients but not in normal colon tissues (Figure 13), and in five out of six kidney tumors isolated from kidney cancer patients (Figure 14). The expression detected in normal adjacent tissues (isolated from diseased tissues) but not in noimal tissues of the kidney (isolated from healthy donors) indicates that these tissues are not fully normal and that 101P3A II is expressed in early stage tumors. In order to assay for androgen regulation of 101P3AI 1 expression, LAPC-9 cells were grown in charcoal-stripped medium and stimulated with the synthetic androgen mibolerone, for either 14 or 24 hours (Figure 15A, Figure 15B, and Figure 15C). Northern blots with 10 pg of total RNA/lane were probed with the 101P3AI I sequences (Figure 15A). A picture of the ethidium-bromide staining of the RNA gel is also presented (Figure 15C). Results showed expression of 101 P3A II is not regulated by androgen. The experimental samples were confirmed bytesting for the expression of the androgen-regulated prostate cancer gene PSA (Figure 15B). This experiment showed that, as expected, PSA levels go down in presence of charcoal-stripped serum, and expression is induced at 14 and 24 hours in presence of mibolerone. Analysis of androgen regulation of 101P3AI 1 in vivo is shown in Figure 16. Male mice were injected with LAPC-9AD tumor cells. When tumors reached a palpable size, mice were castrated and tumors harvested at different time points following castration. RNA was isolated from the xenograft tissues. Northern blots with 10 pg of total RNA/lane were probed with IO1P3A1 Isequences. Size standards in kilobases (kb) are indicated on the side. A picture of the ethidium-bromide staining of the RNA gel is also presented in Figure 16. The results showed that expression of IOIP3AI I was not affected by androgen deprivation, and therefore, is not androgen regulated. Example 2: Splice Variants/ Transcript Variants of 101P3All 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 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 amino acid sequence. Accordingly, a given gene can have zero to many alternative transcripts and each transcript can have zero to many splice variants. 87 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 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. 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 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 (see, e.g., URL www.doubletwist.com/products/c 11 agentsOverview.jhtml). 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. 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.ornl.gov/Grail-bin/EmptyGrailForm) and GenScan (URL genes.mit.edu/GENSCAN.htnl). 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. 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 a., Albumin banks peninsula: a new termination variant characterized by electrospray mass spectrometry, Biochem Biophys Acta. 1999 Aug 17;1433(1-2):321-6; 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 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 a., Discovery of new human beta-defensins using a genomics-based approach, Gene. 2001 Jan 24; 263(1-2):211-8. For PCR-based and 5' RACE Validation: Brigle, K.E., et a., 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. 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 10P3A1I1 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 10P3AI I may also be involved in cancers in the same or different tissues, thus serving as tumor-associated markers/antigens. The exon composition of the original transcript, designated as lOP3A1I1 v.1, are: Exon number Start End 88 89 1 90 2 91 3136 Using the full-length gene and EST sequences, one transcript variant was identified, designated as 10 1 P3AI 1 v.2. Compared with 10 1 P3A1 1 v.1, transcript variant 101 P3AI I v.2 has spliced out a fragment from the second exon of variant 1, as shown in Figure 46. All other exons are the same 5 corresponding exons of 10 1 P3A 1 v.1. Theoretically, each different combination of exons in spatial order, e.g. exons 2 and 3, is a potential splice variant. Figure 46 shows the schematic alignment of exons of the two transcript variants. Figure 2 shows nucleotide sequence of the transcript variant (10 P3AI I v.2). Figure 68 shows the alignment of the transcript variant with nucleic acid sequence of 10 1 P3AI 1 v.. Figure 69 lays out 10 amino acid translation of the transcript variant for the identified reading frame orientation. Figure 70 displays alignments of the amino acid sequence encoded by the splice variant with that of 10 1 P3A I I v.1. Example 3: Single Nucleotide Polymorphisms (SNPs) of IIP3A11 A Single Nucleotide Polymorphism (SNP) is a single base pair variation in a nucleotide 15 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 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. SNPs that occur on a cDNA are called 20 cSNPs. These cSNPs may change amino acids of the protein encoded by the gene and thus change the functions of the protein. Some SNPs cause inherited diseases; others contribute to quantitative variations in phenotype and reactions to environmental factors including diet and drugs among individuals. Therefore, SNPs and/or combinations of alleles (called haplotypes) have many applications, including diagnosis of inherited diseases, determination of drug reactions and dosage, identification of genes 25 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; 1 (5):637-64 1; 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 nucleotide polymorphisms in the isolation of common disease genes," Pharmacogenomics. 30 2000 Feb;l(1):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). SNPs are identified by a variety of art-accepted methods (P. Bean, "The 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-scale pharmacogenetic 35 studies by high-throughput mutation detection and genotyping technologies," Clin. Chem. 2001 Feb; 89A 47(2):164-172). For example, SNPs are identified by sequencing DNA fragments that show polymorphism by gel-based methods such as restriction fragment length polymorphism (RFLP) and denaturing gradient gel electrophoresis (DGGE). They can also be discovered by direct sequencing of DNA samples pooled from different individuals or by comparing sequences from different DNA 5 samples. With the rapid accumulation of sequence data in public and private databases, one can discover SNPs by comparing sequences using computer programs (Z. Gu, L. Hillier and P. Y. Kwok, "Single nucleotide polymorphism hunting in cyberspace," Hum. Mutat. 1998; 12(4):221-225). SNPs 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, 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, five SNPs were identified in the original transcript, IOP3A I v.1, at positions 441 (T/G), 1430 (G/A), 1532 (G/A), 2774 (C/G), and 2833 (G/A). The transcripts or proteins with alternative alleles were designated as variants IOIP3AI 1 v.3, v.4, v.5, v.6 and v.7, respectively. Figure 44 shows the schematic alignment of the SNP variants. Figure 45 shows the schematic alignment of protein variants, corresponding to nucleotide variants. Nucleotide variants that code for the same amino acid sequence as variant I are not shown in Figure 11. These alleles of the SNPs, though shown separately here, can occur in different combinations (haplotypes) and in any one of the transcript variants (such as 101 P3A 11 v.2) that contains the sequence context of the SNPs. Example 4: Production of Recombinant 101 P3A1 I in ProkarVotic and Yeast Systems To express recombinant 101P3AI 1 in prokaryotic cells, the full or partial length 101P3A II cDNA sequences can be cloned into any one of a variety of expression vectors known in the art. One or more of the following regions of 101P3Al I are expressed in these constructs, amino acids 1 to 317; 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 10P3A1 1, variants, or analogs thereof. A. In vitro transcription and translation constructs: RCRIl: To generate 10P3All sense and anti-sense RNA probes for RNA in situ investigations, pCRII constructs (Invitrogen, Carlsbad, CA) are generated encoding either all or fragments of the 101P3A II cDNA. The pCRII vector has Sp6 and T7 promoters flanking the insert to drive the transcription of 101 P3A 11 RNA for use as probes in RNA in situ hybridization experiments. These probes are used to analyze the cell and tissue expression of 101P3AI 1 at the RNA level. Transcribed 101P3AI I RNA representing the cDNA amino acid coding region of the 10lP3A1 I gene is used in in vitro translation systems such as the TnTTm Coupled Reticulolysate System (Promega, Corp., Madison, WI) to synthesize 101P3A II protein. B. Bacterial Constructs: pGEX Constructs To generate recombinant IOIP3AI 1 proteins in bacteria that are fused to the Glutathione S-transferase (GST) protein, all or parts of the 101P3AI I cDNA protein coding sequence are fused to the GST gene by cloning into pGEX-6P-1 or any other GST- fusion vector of the pGEX family (Amersham Pharmacia Biotech, Piscataway, NJ). These constructs allow controlled expression of recombinant 10 1P3AI I 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, can be employed that permits cleavage of the GST tag from IOIP3AI I-related protein. The ampicillin resistance gene and pBR322 origin permit selection and maintenance of the pGEX plasmids in E. coli. In one embodiment, amino acids 86-317 are cloned into the pGEX-2T expression vector, the protein is expressed and purified. 90 pMAL Constructs: To generate, in bacteria, recombinant 101P3AI I proteins that are fused to maltose binding protein (MBP), all or parts of the 10 IP3AI I 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 101P3AI I 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 101P3A 11. The pMAL-c2X and pMAL-p2X vectors are optimized to express the recombinant protein in the cytoplasm or pcriplasm respectively. Periplasm expression enhances folding of proteins with disulfide bonds. In onc embodiment, amino acids 86-3 10 is cloned into the pMAL-c2X expression vector, the protein is expressed and purified. pET Constructs: To express OIP3A1 I in bacterial cells, all or parts of the 1OP3A1 I cDNA protein coding sequence are cloned into the pET family of vectors (Novagen, Madison, WI). These vectors allow tightly controlled expression of recombinant 1OIP3A1 I 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 TM 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 101 P3A 11 protein are expressed as amino-terminal fusions to NusA. C. Yeast Constructs: pESC Constructs: To express 101P3AI I in the yeast species Saccharomyces cerevisiae for generation of recombinant protein and functional studies, all or parts of the 101 P3A11 cDNA protein coding sequence are cloned into the pESC family of vectors each of which contain I 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 FlagiM or Myc epitope tags in the same yeast cell. This system is used to confirm protein-protein interactions of 101 P3A 11. 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 101P3A1 1 in the yeast species Saccharomyces pombe, all or parts of the I OIP3A 11 cDNA protein coding sequence are cloned into the pESP family of vectors. These vectors allow controlled high level expression of a 101P3AI I 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 FlagTM epitope tag allows detection of the recombinant protein with anti- Flag"M antibody. Example 5: Production of Recombinant 1OIP3A11 in Higher Eukarotic Systems A. Mammalian Constructs: To express recombinant IOIP3A1 I in eukaryotic cells, full or partial length IOIP3A1I1 cDNA sequences can be cloned into any one of a variety of expression vectors known in the art. One or more of the following regions of 101P3AI I are expressed in these constructs, amino acids 1 to 318 of v.1 and v.3, amino acids I to 72 of v.2; or any 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 101 P3A 11, variants, or analogs thereof. 91 92 The constructs can betransfected into any one of a wide variety of mammalian cells such as 293T cells. Transfected 293T cell lysates can be probed with the anti-10 l P3A l I polyclonal serum, described herein. pcDNA4/HisMax Constructs: To express 10 l P3A l I in mammalian cells, the 10 l P3AI I ORF 5 was 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 XpressTM and six histidine (6X His) epitopes fused to the amino-terminus. The pcDNA4/HisMax 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 10 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 I origin permits selection and maintenance of the plasmid in E. coli. pcDNA3.1/MycHis Constructs: To express 101P3AI I in mammalian cells, the 10 P3AI I ORF, with a consensus Kozak translation initiation site, was cloned into pcDNA3. 1/MycHis Version A 15 (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-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 20 resistance gene can be used, as it allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and Col El origin permits selection and maintenance of the plasmid in E. coli. pcDNA3. 1/GFP Construct: To express 101 P3AI I in mammalian cells and to allow detection of the recombinant proteins using fluorescence, the 101P3Al I ORF, with a consensus Kozak translation initiation site, was cloned into pcDNA3.l/GFP. Protein expression was driven from the cytomegalovirus 25 (CMV) promoter. The recombinant proteins have the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-invasive, in vivo detection and cell biology studies. The pcDNA3. I/GFP 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 30 resistance gene allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and CoI E I origin permits selection and maintenance of the plasmid in E. coli. Figure 65 shows expression and detection of 10 1 P3A I .GFP fusion protein. 293T cells were transfected with either pcDNA3.1/10l P3A I l.GFP recombinant expression vector (A), pcDNA3.1 /GFP vector (B) or control pcDNA3.1 vector (C). Cells were harvested 24 hours later and analyzed by microscopy for 35 detection of green fluorescence. Results show expression of the 10i P3A I L.GFP fusion protein is localized mostly at the cell membrane, whereas expression of the free GFP is throughout the cells. The 93 control vector did not show any fluorescence. We conclude that the 10 1P3A II.GFP fusion protein is expressed from the pCDNA3.I/10 1P3A I L.GFP construct, and that the fusion protein is localized at the cell membrane. Additional constructs with an amino-terminal GFP fusion are made in pcDNA3.l/NT-GFP 5 TOPO spanning the entire length of the 10 1 P3AI I proteins. Codon optimized 101 P3A 11: To enhance protein translation of 10 1 P3AI 1, the nucleic acid sequence of 101P3AI I was codon optimized (s10 1 P3A 11). The sequence of codon optimized s101P3A I I is listed in Figure 66. The s10 1 P3A I I was cloned into the pcDNA3.I/GFP construct and into the pSRa retroviral vector, to generate the s101 P3A I .GFP fusion protein. The recombinant protein 10 has the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-invasive, in vivo detection and cell biology studies. Figure 67 shows expression and detection of the codon optimized s10 1 P3A I I.GFP fusion protein. 293T cells were transfected with either pcDNA3.1 vector control (light line), or one of the three different pcDNA3.1/sIOIP3AI .GFP vector clones, IG2, 2G3, or3H5 (dark line). Cells were harvested 24 hours later and either analyzed directly for green fluorescence (A), or 15 stained viably using polyclonalanti-10 P3A I 1 antibody (B) and analyzed by flow cytometry. Results show strong expression of the codon optimized s101P3A I l.GFP fusion protein at the cell surface of transfected cells. PAPtag: The 101P3AI I ORF, or portions thereof, of 101P3AI I are cloned into pAPtag-5 (GenHunter Corp. Nashville, TN). This construct generates an alkaline phosphatase fusion at the 20 carboxyl-terminus of the0l P3A l I proteins while fusing the IgGK 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 101P3AI I proteins. The resulting recombinant 10 1 P3AI I 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 the 10 1 P3AI I proteins. Protein 25 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. ptae5: The IOP3AI I ORF, or portions thereof, of 10 I P3AI I are cloned into pTag-5. This 30 vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generated 10 1 P3AI I 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 10 1 P3AI I protein was optimized for secretion into the media of transfected mammalian cells, and was used as immunogen or ligand to identify proteins such as ligands or receptors that interact with the 35 10 1 P3A II proteins. Protein expression is driven from the CMV promoter. The Zeocin resistance gene 93A 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: The101P3A II ORF, or portions thereof, of 10 l P3AI I are also cloned into psecFc. The psecFc vector was assembled by cloning the human immunoglobulin G I (IgG) Fc (hinge, CH2, CH3 5 regions) into pSecTag2 (Invitrogen, California). This construct generates an IgGI Fc fusion at the carboxyl-terminus of the 10 1 P3AI I proteins, while fusing the IgGK signal sequence to N-terminus. 10 1P3AI I fusions utilizing the murine IgG I Fc region are also used. The resulting recombinant 101 P3A I I 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 the S10 1 P3AI I 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. The amino acid region 159-202 of the 101P3AI I ORF was cloned into psecFc. The resulting recombinant 10 1 P3AI I (159-202)-psecFc construct was transfected into 293T and Cos-7 cells, and the 15 expression of recombinant 101 P3A 11(1 59-202)-psecFc protein assayed by Western blotting (Figure 17). Results show that 10 1 P3A I l(159-202)-psecFc fusion protein was expressed in the lysates of both 293T and Cos-7 cells. The 10 1 P3A 11(1 59-202)-psecFc fusion protein was also secreted and detected in the culture supernatants of both cell types.

liSRa Constructs: To generate mammalian cell lines that express 101P3AI 1, constitutively, the ORF of 1OP3AI I was cloned into pSRa constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRa constructs into the 293T-IOAI packaging line or co-transfection of pSRa and a helper plasmid (containing deleted packaging sequences) into the 293 cells, respectively. The retrovirus was used to infect a variety of mammalian cell lines, resulting in the integration of the cloned gene, 101P3A 11, 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 ColE 1 origin permit selection and maintenance of the plasmid in E. coli. Figure 18 shows that 101 P3A 11 was expressed using the pSRa retroviral vector in the cell line 300.19. The retroviral vectors can thereafter be used for infection and generation of various cell lines using, for example, PC3, NIH 3T3, TsuPrl, 293 or rat-I cells. Additional pSRa constructs are made that fuse an epitope tag such as the FLAG'm tag to the carboxyl terminus of 1OlP3AI 1 sequences to allow detection using anti-Flag antibodies. For example, the FLAG'm sequence 5' gat tac aag gat gac gac gat aag 3' is added to cloning primer at the 3' end of the ORF. Additional pSRct constructs are made to produce both amino-terminal and carboxyl-terminal GFP and myc/6X His fusion proteins of the full-length 101P3AI 1 proteins. Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 10IP3Al 1. High virus titer leading to high level expression of 1OP3A1I1 is achieved in viral delivery systems such as adenoviral vectors and herpes amplicon vectors. The 101P3AI I 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. Alternatively, IO1P3All coding sequences or fragments thereof are cloned into the HSV-1 vector (Imgenex) to generate herpes viral vectors. The viral vectors are thereafter used for infection of various cell lines such as SCaBER, NIH 3T3, 293 or rat-I cells. Regulated Expression Systems: To control expression of 101P3AI I in mammalian cells, coding sequences of 101 P3A 11, 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 IOP3A 1I. These vectors are thereafter used to control expression of lOlP3AI1 in various cell lines such as SCaBER, NIH 3T3, 293 or rat-I cells. B. Baculovirus Expression Systems To generate recombinant 1OlP3AI 1 proteins in a baculovirus expression system, 1OIP3AI I 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, pBlueBac-1OIP3A1 I is co-transfected with helper plasmid pBac-N-Blue (Invitrogen) into SF9 (Spodopterafrugiperda) 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 101P3AI I protein is then generated by infection of HighFive insect cells (Invitrogen) with purified baculovirus. Recombinant IOIP3AI l protein can be detected using anti-IOIP3AI I or anti-His-tag antibody. 1OP3AI I protein can be purified and used in various cell-based assays or as immunogen to generate polyclonal and monoclonal antibodies specific for lOP3A 1. 94 Example 5: Production of Recombinant 101P3AII in Higher Eukarvotic Systems A. Mammalian Constructs: To express recombinant 10lP3Al I in eukaryotic cells, full or partial length 101P3AI 1 cDNA sequences can be cloned into any one of a variety of expression vectors known in the art. One or more of the following regions of 10lP3AI I are expressed in these constructs, amino acids I to 317 or 318; or any 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 10P3A 11, 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-101P3A 11 polyclonal serum, described herein. pcDNA4/HIsMax Constructs: To express 10lP3A1 1 in mammalian cells, the l10P3AlI1 ORF was cloned into pcDNA4/HisMax Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter and the SP 16 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) 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 I origin permits selection and maintenance of the plasmid in E. coli. pcDNA3.1/MycHis Constructs: To express I01P3A1I1 in mammalian cells, the 10lP3A1I1 ORF, 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-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 ampicillin resistance gene and CoEil origin permits selection and maintenance of the plasmid in E. coli. pcDNA3.1/CT-GFP-TOPO Construct: To express O10P3AI I in mammalian cells and to allow detection of the recombinant proteins using fluorescence, the 101P3AI I ORF, with a consensus Kozak translation initiation site, was cloned into pcDNA3. l/CT-GFP-TOPO (Invitrogen, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-invasive, in vivo detection and cell biology studies. The pcDNA3. 1CT GFP-TOPO 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 allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColEI origin permits selection and maintenance of the plasmid in E. coli. Additional constructs with an amino-terminal GFP fusion are made in pcDNA3.1/NT-GFP-TOPO spanning the entire length of the l0lP3Al 1 proteins. PAPtag: The IOP3Al 1 ORF, or portions thereof, of lOP3Al I are cloned into pAPtag-5 (GenHunter Corp. Nashville, TN). This construct generates an alkaline phosphatase fusion at the carboxyl-terminus of the 10P3AI I proteins while fusing the IgGK signal sequence to the amino-terminus. Constructs are also generated 95 in which alkaline phosphatase with an amino-terminal IgGK signal sequence is fused to the amino-terminus of 101P3A II proteins. The resulting recombinant 101P3AI I 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 the 1IP3AI I 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. pta5: The 10 lP3AI I ORF, or portions thereof, of lO1P3A 1I are cloned into pTag-5. This vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generated lOP3AI I 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 10 1P3AI 1 protein was optimized for secretion into the media of transfected mammalian cells, and was used as immunogen or ligand to identify proteins such as ligands or receptors that interact with the 101P3A1 I 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: The 10 1P3A 11 ORF, or portions thereof, of 101 P3A 11 are also cloned into psecFc. The psecFc vector was assembled by cloning the human immunoglobulin GI (IgG) Fc (hinge, CH2, CH3 regions) into pSecTag2 (Invitrogen, California). This construct generates an IgGI Fc fusion at the carboxyl-terminus of the lO1P3AI 1 proteins, while fusing the IgGK signal sequence to N-terminus. lOlP3A1 I fusions utilizing the murine IgGI Fc region are also used. The resulting recombinant 10 1P3AI I 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 the 101 P3A 11 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. The amino acid region 159-202 of the IOlP3AI I ORF was cloned into psecFc. The resulting recombinant OlP3AI 1(159-202)-psecFc construct was transfected into 293T and Cos-7 cells, and the expression of recombinant 1OP3A1 1(159-202)-psecFc protein assayed by Western blotting (Figure 17). Results show that 1OlP3A1 1(159-202)-psecFc fusion protein was expressed in the lysates of both 293T and Cos-7 cells. The IO1P3AI 1(159-202)-psecFc fusion protein was also secreted and detected in the culture supernatants of both cell types. pSRot Constructs: To generate mammalian cell lines that express 101P3A 11, constitutively, the ORF of OlP3AI I was cloned into pSRa constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRa constructs into the 293T-1OAI packaging line or co-transfection of pSRL and a helper plasmid (containing deleted packaging sequences) into the 293 cells, respectively. The retrovirus was used to infect a variety of mammalian cell lines, resulting in the integration of the cloned gene, 101P3A 11, 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 ColEI origin permit selection and maintenance of the plasmid in E. coli. Figure 18 shows that 101P3AI I was expressed using the pSRa retroviral vector in the cell line 300.19. The retroviral vectors can thereafter be used for infection and generation of various cell lines using, for example, PC3, NIH 3T3, TsuPrl, 293 or rat-I cells. 96 Additional pSRa constructs are made that fuse an epitope tag such as the FLAGTM tag to the carboxyl terminus of 101P3Al I sequences to allow detection using anti-Flag antibodies. For example, the FLAGTM sequence 5' gat tac aag gat gac gac gat aag 3' 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 101P3A II proteins. Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 1OlP3AI 1. High virus titer leading to high level expression of lOlP3A1 I is achieved in viral delivery systems such as adenoviral vectors and herpes amplicon vectors. The 101P3A Il 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. Alternatively, IOP3AI 1 coding sequences or fragments thereof are cloned into the HSV-1 vector (Imgenex) to generate herpes viral vectors. The viral vectors are thereafter used for infection of various cell lines such as SCaBER, NIH 3T3, 293 or rat-I cells. Regulated Expression Systems: To control expression of OlP3AI I in mammalian cells, coding sequences of 1lP3A1 1, 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 101P3AI 1. These vectors are thereafter used to control expression of lOIP3AI I in various cell lines such as SCaBER, NIH 3T3, 293 or rat-I cells. B. Baculovirus Expression Systems To generate recombinant 101P3A I1 proteins in a baculovirus expression system, 101P3A I1 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, pBlueBac-101P3A1 I is co-transfected with helper plasmid pBac-N-Blue (Invitrogen) into SF9 (Spodopterafrugiperda) 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 OlP3AI 1 protein is then generated by infection of HighFive insect cells (Invitrogen) with purified baculovirus. Recombinant 1OIP3Al I protein can be detected using anti-IOIP3AI I or anti-His-tag antibody. 101P3A1 1 protein can be purified and used in various cell-based assays or as immunogen to generate polyclonal and monoclonal antibodies specific for 101 P3AI 1. Example 6 Antigenicity Profiles and Secondary Structure Figure 5, Figure 6, Figure 7, Figure 8, and Figure 9 depict graphically five amino acid profiles of the O1P3Al I amino acid sequence, each assessment available by accessing the ProtScale website (URL www.expasy.ch/cgi-bin/protscale.pl) on the ExPasy molecular biology server. These profiles: Figure 5, Hydrophilicity, (Hopp T.P., Woods K.R., 1981. Proc. NatI. Acad. Sci. U.S.A. 78:3824-3828); Figure 6, Hydropathicity, (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132); Figure 7, Percentage Accessible Residues (Janin J., 1979 Nature 277:491-492); Figure 8, Average Flexibility, (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept. Protein Rcs. 32:242-255); Figure 9, Beta-turn (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294); and optionally others available in the art, such as on the ProtScale website, were used to identify antigenic regions of the lOlP3A1 I protein. Each of the above amino acid profiles of OIP3A II were generated using the following ProtScale parameters for analysis: 1) A window size of 9: 2) 97 100% weight of the window edges compared to the window center; and, 3) amino acid profile values normalized to lie between 0 and 1. Hydrophilicity (Figure 5), Hydropathicity (Figure 6) and Percentage Accessible Residues (Figure 7) profiles 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 are available for immune recognition, such as by antibodies. Average Flexibility (Figure 8) and Beta-turn (Figure 9) 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 portions of the protein and thus are accessible to immune recognition, such as by antibodies. Antigenic sequences of the 101P3A II protein indicated, e.g., by the profiles set forth in Figure 5, Figure 6, Figure 7, Figure 8, and/or Figure 9 are used to prepare immunogcns, either peptides or nucleic acids that encode them, to generate anti-10IP3AI I antibodies. The immunogen can be any 5, 6, 7, 8, 9, 10, I1, 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 the IO1P3AI I protein. In particular, peptide immunogens of the invention can comprise, a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to 317 or 318.that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to 317 or 318 that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6; a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profile on Figure 8; and, a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to 317 or 318 that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figure 9. Peptide immunogens of the invention can also comprise nucleic acids that encode any of the forgoing. 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 101P3AI 1, namely the 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/npsa-automat.pl?page=npsann.html), accessed from the ExPasy molecular biology server http://www.expasy.chltools/. The analysis indicates that IOIP3A 11 is composed 47.95% alpha helix, 21.45% extended strand, and 30.60% random coil (Figure 19A). Analysis for the potential presence of transmembrane domains in 101P3A 1 was carried out using a variety of transmembrane prediction algorithms accessed from the ExPasy molecular biology server http://www.expasy.ch/tools. The programs predict the presence of 7 transmembrane domains in 101 P3A 11, consistent with the structure of a G-protein coupled receptor. Shown graphically in Figure 19A are the results of analysis using the TMpred (Figure 19B) and TMHMM (Figure 19C) prediction programs depicting the location of 98 the 7 transnembrane domains. The results of each program, namely the amino acids encoding the transmembrane domains are summarized in Table XXI. Example 7: Generation of 101P3A11 Polyclonal Antibodies Polyclonal antibodies can be raised in a mammal, for example, by one or more 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 subcutaneous or intraperitoneal injections. In addition to immunizing with the full length 101P3AI I protein, computer algorithms are employed in design of immunogens that, based on amino acid sequence analysis are antigenic and available for recognition by the immune system of the immunized host (see the Example entitled "Antigenicity Profiles and Secondary Structure"). Such regions would generally be hydrophilic, flexible, in beta-turn conformations, and/or exposed on the surface of the protein (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9 for amino acid profiles that indicate such regions of 10 IP3A I I). For example, IOIP3AI 1 recombinant bacterial fusion proteins or peptides containing hydrophilic, flexible, beta-turn regions of the I01P3AI I amino acid sequence, such as amino acids 1-23, plus or minus 1-10 amino acids at available termini, and amino acids 159-202, plus or minus 1-10 amino acids at available termini, are used as antigens to generate polyclonal antibodies in New Zealand White rabbits. It is useful to conjugate the immunizing agent to a protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic 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 1-23 of IOP3A1 1 is conjugated to KLH and used to immunize the rabbit. Alternatively the immunizing agent may include all or portions of the 101P3A II protein, analogs or fusion proteins thereof. For example, the 101P3A1 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. Such fusion proteins are purified from induced bacteria using the appropriate affinity matrix. In one embodiment, a GST-fusion protein encoding amino acids 86-317, plus or minus 1-10 amino acids at available termini, is produced and purified and used as immunogen. 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 10 lP3A 11 in Prokaryotic Systems" and Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et 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 vectors such as the Tag5 and Fc-fusion vectors (see the section entitled "Production of Recombinant 101P3AI I in Eukaryotic Systems"), and retain post-translational modifications such as glycosylations found in native protein. In one embodiment, amino acids 159-202 is cloned into the Tag5 mammalian secretion vector. The recombinant protein is purified by metal chelate chromatography from tissue culture supernatants of 293T cells stably expressing the recombinant vector. The purified Tag5 IO1P3A1 1 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 include, but are not limited to, complete Freund's adjuvant (CFA) and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). 99 In a typical protocol, rabbits are initially immunized subcutaneously with up to 200 pg, typically 100-200 pg, of fusion protein or peptide conjugated to KLH mixed in complete Freund's adjuvant (CFA). Rabbits are then injected subcutaneously every 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 Tag5 101P3AI 1 encoding amino acids 159-202, the full-length 101P3AI I cDNA is cloned into pCDNA 3.1 myc-his expression vector (Invitrogen, see the Example entitled "Production of Recombinant 10 1 P3A I1 in Eukaryotic Systems"). After transfection of the constructs into 293T cells, cell lysates are probed with the anti 10 P3A I serum and with anti-His antibody (Santa Cruz Biotechnologies, Santa Cruz, CA) to determine specific reactivity to denatured 101P3AI I protein using the Western blot technique. Immunoprecipitation and flow cytometric analyses of 293T and other recombinant IOIP3Al 1-expressing cells determine recognition of native protein by the antiserum. In addition, Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometric techniques using cells that endogenously express 1OP3AI I are carried out to test specificity. The anti-serum from the Tag5 101P3A II immunized rabbit is affinity purified by passage over a column composed of the Tag5 antigen covalently coupled to Affigel matrix (BioRad, Hercules, Calif.). The serum is then further purified by protein G affinity chromatography to isolate the IgG fraction. Serum from rabbits immunized with 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 partner either alone or in the context of an irrelevant fusion protein. Sera from other His-tagged antigens and peptide immunized rabbits as well as fusion partner depleted scra are affinity purified by passage over a column matrix composed of the original protein immunogen or free peptide. Example 8: Generation of 10IP3A1I1 Monoclonal Antibodies (mAbs) In one embodiment, therapeutic mAbs to 101P3AI I comprise those that react with epitopes of the protein that would disrupt or modulate the biological function of 101P3AI 1, for example those that would disrupt its interaction with ligands or proteins that mediate or are involved in its biological activity. Therapeutic mAbs also comprise those that specifically bind epitopes of 101P3A1 I exposed on the cell surface and thus are useful in targeting mAb-toxin conjugates. Monoclonal antibodies may also be raised to other antigenic epitopes of lO1P3AI 1 including amino acid sequences predicted to be in intracellular regions. These monoclonal antibodies are useful as intrabodies if they disrupt the signaling mechanisms of 101P3A 11, such as the interaction with hetemtrimeric G proteins. . Such antibodies are also useful as diagnostic agents for techniques such as inununohistochemistry. Immunogens for generation of such mAbs include those designed to encode or contain the entire IOIP3AI I protein or regions of the 101P3A II protein predicted to be exposed to the extracellular environment or hydrophilic cytoplasmic environment, and/antigenic from computer analysis of the amino acid sequence (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9, and the Example entitled "Antigenicity Profiles and Secondary Structure"). Immunogens include peptides, recombinant bacterial proteins, and mammalian expressed Tag 5 proteins and human and murine IgG FC fusion proteins. In addition, cells expressing high levels of IO1P3AI 1, such as 293T-101P3A1 1 or 300.19- IOIP3AI I murine Pre-B cells, are used to immunize mice. 100 To generate mAbs to 101P3A1, mice are first immunized intraperitoneally (IP) with, typically, 10-50 pg of protein immunogen or 107 101P3A 1-expressing cells mixed in complete Freund's adjuvant. Alternatively, mice are immunized intradermally. Mice are then subsequently immunized IP every 2-4 weeks with, typically, 10-50 pg 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 strategies, a DNA-based immunization protocol is employed in which a mammalian expression vector encoding 101 P3AI I sequence is used to immunize mice by direct injection of the plasmid DNA. For example, the predicted first extracellular loop, amino acids 82-104, or second extracellular loop of 10 1P3A 11, amino acids 159-202, or the third extracellular loop, amino acids 258 - 275 (in each instance plus or minus 10 amino acids) 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 101 P3A 1I sequence is fused at the amino-terminus to an IgK leader sequence and at the carboxyl-terminus to the coding sequence of the human IgG Fc region. This recombinant vector is then used as immunogen. Amino acid sequences from intracellular regions may also be used as antigens using similar strategies. These regions include amino acids 50-63, amino acids 121 146, amino acids 261-275, and amino acids 295-318 (in each instance plus or minus 10 amino acids, except for the C-terminus residue). The plasmid immunization protocols are used in combination with purified proteins expressed from the same vector and with cells expressing 101P3A11. 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, inmunoprecipitation, fluorescence microscopy, and flow cytometric analyses, fusion and hybridoma generation is then carried out with established procedures well known in the art (see, e.g., Harlow and Lane, 1988). In one embodiment for generating 101P3AII monoclonal antibodies, a Tag5-10 IP3AI I antigen encoding amino acids 159-202 is expressed and purified from stably transfected 293T cells. Balb C mice are initially immunized intraperitoneally with 25 pg of the Tag5-101P3A 1 protein mixed in complete Freund's adjuvant. Mice are subsequently immunized every two weeks with 25 pg of the antigen mixed in incomplete Freund's adjuvant for a total of three immunizations. ELISA using the TagS antigen determines the titer of serum from immunized mice. Reactivity and specificity of serum to full length 101 P3A 11 protein is monitored by Western blotting, immunoprecipitation and flow cytometry using 293T cells transfected with an expression vector encoding the I0lP3AI I cDNA (see e.g., the Example entitled "Production of Recombinant IOIP3Al I in Eukaryotic Systems"). Other recombinant IOP3A 1-expressing cells or cells endogenously expressing 101P3Al I 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 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 IOIP3AI I specific antibody-producing clones. The binding affinity of a 101P3A 11 monoclonal antibody is determined using standard technologies. Affinity measurements quantify the strength of antibody to epitope binding and are used to help define which IOP3AI 1 monoclonal antibodies preferred, e.g., 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 101 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 conveniently generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. Example 9: HLA Class I and Class II Bindine Assays HLA class I and class II binding assays using purified HLA molecules are 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. /mmunol. 31:813 (1994)). Briefly, purified MHC molecules (5 to 500 nM) are incubated with various unlabeled peptide inhibitors and 1-10 nM I '-radiolabeled probe peptides 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 [label)<[HLA] and ICso2[HLA], the measured IC5 0 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 ICs 0 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 IC5o nM values by dividing the IC 50 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 10: 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 evitoes The searches performed to identify the motif-bearing peptide sequences in the Example entitled "Antigenicity Profiles" and Tables V-XVIll and XXII TO IL employ the protein scquencc data from the gene product of 1OlP3AI 1 set forth in Figures 2 and 3; the specific peptides used to generate the tables are listed in Table L11. Computer searches for epitopes bearing HLA Class I or Class II supermotifs or motifs are performed as follows. All translated 101P3AI I 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 102 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"= a,, x a 1 x a ...... x a, where aj is a coefficient which represents the effect of the presence of a given amino acid (j) 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 residuej occurs at position i in the peptide, it is assumed to contribute a constant amount, 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 al, Human Immunol. 45:79-93, 1996; and Southwood et al., J Immunol. 160:3363-3373, 1998). Briefly, for all i positions, anchor and non-anchor alike, the geometric mean of the average relative binding (ARB) of all peptides carrying is calculated relative to the remainder of the group, and used as the estimate ofj,. For Class II 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 suertype cross-reactive n eptides Protein sequences from 101P3AI I are scanned utilizing motif identification software, to identify 8-, 9 10- and I 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 five 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 three or more HLA-A2 supertype molecules. Selection of HLA-A3 supermotif-bearing epitopes The IOP3AI 1 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*680 1) to identify those that can bind at least three of the five HLA-A3-supertype molecules tested. 103 Selection of HLA-B7 supermotif bearing enitones The IOP3A1 I protein(s) scanned above is also analyzed for the presence of 8-, 9- 10-, or I 1-mer peptides with the HLA-B7-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 IC 50 of s500 nM are identified using standard methods. These peptides are then tested for binding to other common B7-supertype molecules (e.g., B*3501, B*5 101, 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 epitones To further increase population coverage, HLA-AI and -A24 epitopes can also be incorporated into vaccine compositions. An analysis of the 1OP3Al1 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 11: Confirmation of Immunogeniclty 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: 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. I restricted CTL. This cell line 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 ofDendritic 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 monocytcs are purified by plating 10 x 106 PBMC/well in a 6-well plate. After 2 hours at 37"C, the non-adherent cells arc 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 U/mi 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-450) and the detacha-bead@ reagent. Typically about 2 0 0-250x106 PBMC are processed to obtain 24x10 6 CD8' T-cells (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/l% AB serum at a concentration of 20xlOcells/ml. The magnetic beads are washed 3 times with PBS/AB serum, added to the cells (140d beads/20x 106 cells) and incubated for I hour at 4*C with continuous mixing. The beads and cells are washed 4x with PBS/AB serum to remove the nonadherent cells and resuspended at 1OOx106 104 cells/nl (based on the original cell number) in PBS/AB serum containing 1 00pl/ml detacha-bead@ reagent and 30 pg/ml 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 1-2x104/ml in the presence of 3pg/ml 82- 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 Ix 105 cells/ml) are co-cultured with 0.25ml of CD8+ T-cells (at 2x104 cell/ml) 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/ml. 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 5x10 6 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*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/mil of peptide in the presence of 3 pg/mI B 2 microglobulin in 0.25m1 RPMI/5%AB per well for 2 hours at 37*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/mi (Tsai et al., Critical Reviews in Immunology 18(1-2):65-75, 1998). Seven days later, the cultures are assayed for CTL activity in a "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 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 Cr release. Seven days after the second restimulation, cytotoxicity is determined in a standard (5 hr) SICr release assay by assaying individual wells at a single E:T. Peptide-pulsed targets are prepared by incubating the cells with I Opg/ml peptide overnight at 37*C. Adherent target cells are removed from culture flasks with trypsin-EDTA. Target cells are labeled with 200jpCi of SICr sodium chromate (Dupont, Wilmington, DE) for I hour at 37*C. Labeled target cells are resuspended at 106 per ml and diluted 1:10 with K562 cells at a concentration of 3.3x10 6 /ml (an NK-sensitive erythroblastoma cell line 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*C. At that time, 100 p1 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 5t Cr release sample)/(cpm of the maximal "Cr release sample- cpm of the spontaneous "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. 105 In situ Measurement of Human IFNY Production as an Indicator of Pentide-specific and Endogenous Recognition Immulon 2 plates are coated with mouse anti-human IFNI monoclonal antibody (4 pg/ml 0.1M NaHCO 3 , pH8.2) overnight at 4*C. The plates are washed with Ca2+, Mg 2 +-free PBS/0.05% Tween 20 and blocked with PBS/10% FCS for two hours, after which the CTLs (100 pl/well) 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 Ix 106 cells/rn. The plates are incubated for 48 hours at 37*C with 5% Co 2 . 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 0 C. The plates are washed and 100 pl of biotinylated mouse anti-human IFN-gamma monoclonal antibody (2 microgrami/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 IM H 3 P0 4 and read at OD450. A culture is considered positive if it measured at least 50 pg of IFN-gamma/well 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, 5x10 4 CD8+ cells arc added to a T25 flask containing the following: 1x10 6 irradiated (4,200 rad) PBMC (autologous or allogeneic) per ml, 2x105 irradiated (8,000 rad) EBV- transformed cells per ml, 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 penicillin/streptomycin. Recombinant human IL2 is added 24 hours later at a final concentration of 200IU/ml and every three days thereafter with fresh media at 5011/ml. The cells are split if the cell concentration exceeds lxlO'/ml and the cultures are assayed between days 13 and 15 at E:T ratios of 30, 10, 3 and 1:1 in the "Cr release assay or at Ix10 6 /ml 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 following: Ix1O 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); 2x 105 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 CTLs 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 IOIP3AI 1. Briefly, PBMCs are isolated from patients, re-stimulated with peptide-pulsed monocytes 106 and assayed for the ability to recognize peptide-pulsed target cells as well as transfected cells endogenously expressing the antigen. Evaluation of A*03/A I1 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 immunogenicity Immunogenicity screening of the B7-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-A 1, HLA-A24 etc. are also confirmed using similar methodology Example 12: Implementation of the Extended Supermotif to Improve the Bindine Capacity of Native Epitopes by Creatine Analops .HLA motifs and supermotifs (comprising primary and/or secondary residues) are useful in Ile identification and preparation of highly cross-reactive native pcptides, 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 IC5 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 et aL., J. hnmunol. 157:2539, 1996; and Pogue et al., Proc. Natl. A cad. Sci. USA 92:8166, 1995). In the cellular screening of these peptide analogs, it is important to confirm that analog-specific CTLs arc 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 peptides 107 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 arc then tested for the ability to bind A*03 and A*] I (prototype A3 supcrtypc alleles). Thosc peptides that demonstrate s 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-terminal 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 B7 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-B7-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 101P3AI I-expressing tumors. Other analoging strategies Another form of peptide analoging, unrelated to anchor positions, involves the substitution of a cysteine with cc-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 et 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 13: Identification and confirmation of 10IP3A11-derived sequences with HLA-DR binding motifs 108 Peptide epitopes bearing an HLA class 11 supermotif or motif are identified and confirmed as outlined below using methodology similar to that described for HLA Class I peptides. Selection of HLA-DR-supermotif-bearing epitopes. To identify O1P3AI 1-derived, HLA class 11 HTL epitopes, a 10 IP3AI I 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 et al., J. Immunol. 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 efficiently 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 DRl, DR4w4, and DR7, can efficiently select DR cross-reactive peptides. The 101P3A II-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: DRl, DR4w4, and DR7. Peptides binding at least two of these three DR molecules are then tested for binding to DR2w2 P1, DR2w2 P2, DR6wl9, 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 DR4wl5, DRSwl 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. 101P3AI I-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 101P3A II 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 lIpM or better, i.e., less than I pM. Peptides are found that meet this binding criterion and qualify as HLA class II 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 I 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 14: Immunogenicity of 101P3AII-derived HTL epitopes 109 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 101P3A1 I-expressing tumors. Example 15: Calculation of phenotypic frequencies of HLA-supertypes In various ethnic backgrounds 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=l-(SQRT(I-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 inverse formula [af=I -(1 -Cgf)2]. 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, A11, A3 1, 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-like supertype family arc 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: B7, B*3501-03, B51, B*5301, B*5401, B*5501-2, B*5601, B*6701, and B*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 five major ethnic groups. Coverage may be extended by including peptides bearing the Al and A24 motifs. On average, A I 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%. An analogous approach can be used to estimate population coverage achieved with combinations of class II motif bearing epitopes. Immunogenicity studies in humans (e.g., Bertoni et al., J. Clin. Invest. 100:503, 1997; Doolan et aL., Immunity 7:97, 1997; and Threlkeld et aL., J. Immunol. 159:1648, 1997) have shown that highly cross-reactive 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. 110 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 16: 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 assayed for cytotoxicity and the cell lines that contain peptide-specific cytotoxic activity are further re-stimulated. An additional six days later, these cell lines are tested for cytotoxic activity on "Cr labeled Jurkat-A2. 1/Kb target cells in the absence or presence of peptide, and also tested on "Cr labeled target cells bearing the endogenously synthesized antigen, i.e. cells that are stably transfected with IOP3AI I expression vectors. The results demonstrate that CTL lines obtained from animals primed with peptide epitope recognize endogenously synthesized 10 1P3AI 1 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 Al 1, which may also be used to evaluate A3 epitopes, and B7 alleles have been characterized and others (e.g., transgenic mice for HLA-Al and A24) are being developed. HLA-DR I and HLA-DR3 mouse models have also been developed, which may be used to evaluate HTL epitopes. Example 17: Activity Of CTL-HTL Coniugated Epitopes In Transgenic Mice This example illustrates the induction of CTLs and HTLs in transgenic mice, by use of a 101P3A I1 derived CTL and HTL peptide vaccine compositions. The vaccine composition used herein comprise peptides to be administered to a patient with a IOIP3AI 1-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. Inmunol. 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 HILA-A2 supermotif-bcaring 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 i1 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 A2.1/Kb chimeric gene (e.g., Vitiello et al., J. Exp. Med. 173:1007, 1991) In vitro CTL activation: One week after priming, spleen cells (30x 106 cells/flask) are co-cultured at 37"C with syngeneic, irradiated (3000 rads), peptide coated lymphoblasts (IOx 106 cells/flask) in 10 ml of culture medium/T25 flask. After six days, effector cells are harvested and assayed for cytotoxic activity. Assayfor cytotoxic activity: Target cells (1.0 to l.SxlO) are incubated at 37*C in the presence of 200 p1 of "Cr. After 60 minutes, cells are washed three times and resuspended in RIO medium. Peptide is added where required at a concentration of I pg/ml. For the assay, 10' "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, % 5Cr release data is expressed as lytic units/10' cells. One lytic unit is arbitrarily defined as the number of effector cells required to achieve 30% lysis of 10,000 target cells in a six hour "Cr release assay. To obtain specific lytic units/l 0', the lytic units/I 0' obtained in the absence of peptide is subtracted from the lytic units/I 06 obtained in the presence of peptide. For example, if 30% "Cr release is obtained at the effector (E): target (T) ratio of 50:1 (i.e., 5x10' effector cells for 10,000 targets) in the absence of peptide and 5:1 (i.e., 5x10 4 effector cells for 10,000 targets) in the presence of peptide, the specific lytic units would be: [(1/50,000)-(1/500,000)] x 106 = 18 LU. The results are analyzed to assess the magnitude of the CTL responses of animals injected with the immunogenic CTL/HTL 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 Imunogenicity." 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 18: Selection of CTL and HTL Epitopes for Inclusion In a I03AI1-specific Vaccine. This example illustrates 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 onc 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 IOP3AI I clearance. The number of epitopes used depends on observations of patients who spontaneously clear 1lP3A1l. For example, if it has been observed that patients who spontaneously clear 101P3AII-expressing cells generate an immune response to at least three (3) epitopes from 101 P3A II antigen, then at least three epitopes should be included for HLA class I. A similar rationale is used to determine HLA class I epitopes. 112 Epitopes are often selected that have a binding affinity of an IC 50 of 500 nM or less for an HLA class I molecule, or for class II, an ICs0 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 overlapping 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. 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. 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 prcscnt in IOIP3Al 1, thus avoiding the 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 clears cells that bear or overexpress 101P3A 11. Example 19: 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, -B7 supermotif-bearing peptide epitopes and HLA-A I 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 101P3A 1, are selected such that multiple supermotifs/motifs are represented to ensure broad population coverage. Similarly, HLA class 11 epitopes are selected from 101 P3A II to provide broad population coverage, i.e. both HLA DR- -4-7 supermotif-bearing 113 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 class II epitope sequence so that HLA class II epitope is directed to the endoplasmic reticulum, where the epitope binds to an HLA class 11 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 nucleotide overlaps, are synthesized and HPLC-purified. The oligonucleotides encode the selected peptide cpitopes 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 PerkinfElmer 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 oligonucleotides, i.e., four pairs of primers, oligonucleotides 1+2, 3+4, 5+6, and 7+8 are combined in 100 pi reactions containing Pfu polymerase buffer (1x= 10 mM KCL, 10 mM (NH4) 2 S0 4 , 20.mM Tris-chloride, pH 8.75,2 mM MgSO 4 , 0.1% Triton X-100, 100 pg/ml 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 addcd 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 20: The Plasmid Construct and the Degree to Which It Induces Immunogenicity. 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 al., 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 114 concentration of peptide necessary to obtain equivalent levels of lysis or lymphokine release (see, e.g., Kageyama etal., 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. I/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 II 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 pg 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 cells, 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 al. 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., Barnett 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 a., Vaccine 16:439-445, 1998; Sedegah et a., Proc. Nat!. 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.f/Kb transgenic mice are immunized IM with 100 pg of a DNA minigene encoding the 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 10' pfu/mouse 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 115 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 pcptide-specific activity in an alpha, bela and/or gamma IFN ELISA. It is found that thc minigcnc utilized in a princ-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-Al I 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 21: Peptide Compositions for Prophvlactic Uses Vaccine compositions of the present invention can be used to prevent 101P3A1 1 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 10 1P3Al 1-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 101P3A 1-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 22: Polyepitopic Vaccine Compositions Derived from Native 1OIP3A1l Sequences A native 10lP3AI I polyprotein sequence is analyzed, preferably using computer algorithms defined for each class I and/or class II 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. 116 The vaccine composition will include, for example, multiple CTL epitopes from 101P3AI I antigen and at least one HTL epitope. This polyepitopic native sequence is administered either as a peptide or as a nucleic acid sequence which 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 101 P3A 11, 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 23: Polvepitopic Vaccine Compositions From Multiple Antigens The 10 1P3A1 1 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 l0lP3AI I and such other antigens. For example, a vaccine composition can be provided as a single polypeptide that incorporates multiple epitopes from 101 P3A 11 as well as tumor-associated antigens that are oflen expressed with a target cancer associated with 10 IP3AI I 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 24: 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 IOP3Al 1. Such an analysis can be performed in a manner described by Ogg et al., 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, 101P3Al1 HLA-A*020 1-specific CTL frequencies from HLA A*0201-positive individuals at different stages of disease or following immunization comprising a 1OIP3AI 1 peptide containing an A*0201 motif. Tetrameric complexes are synthesized as described (Musey et al., N. Engl. J. Med. 337:1267, 1997). Briefly, purified HLA heavy chain (A*0201 in this example) and 02-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 117 added in a 1:4 molar ratio, and the tetrameric product is concentrated to I mg/ml. The resulting product is referred to as tetramer-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 101P3AI I epitope, and thus the status of exposure to OIP3AI 1, or exposure to a vaccine that elicits a protective or therapeutic response. Example 25: 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 1OIP3A1 1-associated disease or who have been vaccinated with a OIP3A1I1 vaccine. For example, the class I restricted CTL response of persons who have been vaccinated may be analyzed. The vaccine may be any 1OP3A 1I 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/ml), and Hepes (10mM) containing 10% heat-inactivated human AB serum (complete RPMI) and plated using nicroculture formats. A synthetic peptide comprising an epitope of the invention is added at 10 pg/mil 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 10' PBMC are stimulated with peptide in 8 replicate cultures in 96-well round bottom plate in 100 pl/well of complete RPMI. On days 3 and 10, 100 p1 of complete RPMI and 20 U/mI final concentration of rIL-2 are added to each well. On day 7 the cultures are transferred into a 96-well flat bottom plate and restimulated with peptide, rIL-2 and 10' 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 "Cr release, based on comparison with non-diseased control subjects as previously described (Rehermann, et aL., Nature Med. 2:1104,1108, 1996; Rehermann et al., J. Clin. Invest. 97:1655-1665, 1996; and Rehermann et aL. J. Clin. Invest. 98:1432-1440, 1996). Target cell lines are autologous and allogencic 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). 118 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 "Cr (Amersham Corp., Arlington Heights, IL) for I hour after which they are washed four times with HBSS. Cytolytic activity is determined in a standard 4-h, split well $ 1 Cr release assay using U-bottomed 96 well plates containing 3,000 targets/well. Stimulated PBMC are tested at effector/target (E/T) 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 all experiments. The results of such an analysis indicate the extent to which HLA-restricted CTL populations have been stimulated by previous exposure to 101P3A II or a 101P3AI 1 vaccine. Similarly, Class 11 restricted HTL responses may also be analyzed. Purified PBMC are cultured in a 96 well flat bottom plate at a density of 1.5x 105 cells/well and are stimulated with 10 pg/ml synthetic peptide of the invention, whole 101P3A II 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 lOU/mi IL-2. Two days later, 1 pCi 3H-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 '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 26: 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 designed, for example, as follows: A total of about 27 individuals are enrolled and divided into 3 groups: Group I: 3 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 111: 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 rcvcrsibility. 119 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 27: Phase II Trials In Patients Expressing IOIP3AIl Phase II trials are performed to study the effect of administering the CTL-HTL peptide compositions to patients having cancer that expresses IOIP3Al 1. The main objectives of the trial are to determine an effective dose and regimen for inducing CTLs in cancer patients that express 101P3A 11, 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. All of them have a tumor that expresses 101P3A11. 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 1OP3All -associated disease. Example 28: Induction of CTL Responses Using 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 fowlpox virus administered at a dose of 5-107 to 5xl0' 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 120 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 101P3AI I is generated. Example 29: 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 101P3AI 1 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 ProgenipoietinTM (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 ProgenipoietinT" are injected into patients without purification of the DC. The total number of PBMC that are administered often ranges from 10' 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 ProgenipoietinTm 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 10' peptide-loaded PBMC. The percent DC mobilized by an agent such as ProgenipoietinTM is typically estimated to be between 2-10%, but can vary as appreciated by one of skill in the art. Er vivo activation of CTL/HTL responses Alternatively, ex vivo CTL or HTL responses to 101P3A II 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 cells are infused into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cells, i.e., tumor cells. Example 30: An Alternative Method of Identifying and Confirming 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 121 type of HLA molecule. These cells can be transfected with nucleic acids that express the antigen of interest, e.g. lOIP3AI 1. 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 al., J. /mmunol. 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 nucleic acids that encode IOP3Al I to isolate peptides corresponding to IOIP3AI I 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 31: Complementary Polynucleotides Sequences complementary to the OIP3AI I-encoding sequences, or any parts thereof, arc used to detect, decrease, or inhibit expression of naturally occurring 101 P3A 11. Although use of oligonucleotides comprising from about 15 to 30 base pairs is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonucleotides are designed using, e.g., OLIGO 4.06 software (National Biosciences) and the coding sequence of 101 P3A 11. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5' sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent ribosomal binding to a 101 P3A 1 encoding transcript. Example 32: Purification of Naturally-occurring or Recombinant 1OIP3AI1 Using 1O1P3AI1 Speeific Antibodies Naturally occurring or recombinant O1P3A1 I is substantially purified by immunoaffinity chromatography using antibodies specific for 1OP3A1 1. An immunoaffinity column is constructed by covalently coupling anti-OIP3AI I 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 101 P3A 1 are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of 101P3AI 1 (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/OIP3AI 1 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 33; Identification of Molecules Which Interact with IOIP3AI1 122 123 10 1 P3A 11, or biologically active fragments thereof, are labeled with121 1 Bolton-Hunter reagent. (See, e.g., Bolton el al (1973) Biochem. J. 133:529). Candidate molecules previously arrayed in the wells of a multiwell plate are incubated with the labeled 10 1 P3A 11, washed, and any wells with labeled 10 1 P3A I I complex are assayed. Data obtained using different concentrations of 101P3A I I are 5 used to calculate values for the number, affinity, and association of 10 1 P3A II with the candidate molecules. Example 34: In Vivo Assay for 101P3AI I Tumor Growth Promotion The effect of the 101P3A I I protein on tumor cell growth can be confirmed in vivo by gene 10 overexpression in a variety of cancer cells, including prostate, kidney, colon and bladder. For example, SCID mice can be injected subcutaneously on one flank with I x 106 prostate, kidney, colon or bladder cancer cells (such as PC3, LNCaP, SCaBER, UM-UC-3, SK-CO, Caco, RT4, T24, Caki, A-498 and SW839 cells) containing tkNeo empty vector or 10 1 P3A 11. At least two strategies can be used: 15 (1) Constitutive 101 P3A II expression under regulation of a promoter such as a constitutive promoter obtained from the genomes of viruses such as polyoma virus, 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 20 promoters are compatible with the host cell systems. (2) Regulated expression under control of an inducible vector system, such as ecdysone, tet, etc., can be used provided such promoters are compatible with the host cell systems. Tumor volume is then monitored at the appearance of palpable tumors and is followed over time to validate that 101 P3A 1 expressing cells grow at a faster rate and that tumors produced by 10 1 P3AI I -expressing cells 25 demonstrate characteristics of altered aggressiveness (e.g., enhanced metastasis, vascularization, reduced responsiveness to chemotherapeutic drugs). Figure 21 compares subcutaneous growth of control 3T3 neo and 3T3-101P3AI I cells. One million cells stably expressing neo or 10 1P3A I I were injected subcutaneously in SCID mice along with matrigel. Tumor volume was evaluated by caliper measurements. This experiment demonstrates that expression of 101P3AI I in NIH 3T3 cells is induces 30 tumor formation in 6/6 mice. In an experiment comparing the effect of a strong oncogene such as Ras to that of 10 1 P3A 11, we showed that 10 1 P3A I I induced tumor growth of 3T3 cells in a more rapid and aggressive manner that 1 2 V-Ras (Figure 54). The results indicated that expression of 101P3AI I is sufficient to induce tumor formation in vivo. Figure 42 shows demonstrates that 10 1 P3A I I induces orthotopic growth of tumors. Additionally, SCID mice were implanted with the same 3T3-10IP3A 11 35 cells orthotopically in the prostate to determine if IOIP3AI 1I has an effect on local growth in the prostate or on the ability of the cells to metastasize, specifically to lungs or lymph nodes. This experiment 124 (Figure 56) shows that while control 3T3-neo cells fail to induce tumor formation in the prostate of SCID mice, significant tumor growth was seen in cells expressing 101P3A11. In an analogous manner, cells can be implanted orthotopically in the bladder, colon or kidney. (Saffran, D., et al., PNAS 10:1073-1078; Fu, X., et al., Int. J. Cancer, 1991.49:p. 938-939; Chang, S., et al., Anticancer Res., 1997.17:p. 3239 5 3242; Peralta, E. A., et al., J. Urol., 1999, 162:p. 1806-1811). The tumor enhancing effect of 101P3A I I was also observed when 101P3A1 1 is expressed in prostate cancer cells such as PC3 and introduced into the prostate of SCID mice (Figure 57). A 2.5 fold increase in tumor weight is observed in tumors expressing 10 1P3AI I relative to control cells. Expression of 101P3A 11 also enhances tumor growth and progression in the tibia of SCID mice. 10 Clinical studies have repeatedly shown that prostate cancer may become metastatic to the bone. In order to investigate the contribution of 10 1 P3A 1I to bone tropism and tumor growth in the bone, control and 101P3A 11-expressing cells were compared for their ability to induce tumor growth in the tibia of SCID mice. Experiments in Figures 60 and 61 show that injection of 10 1 P3A I I expressing 3T3 or PC3 cells into the bone of SCID mice results in increase tumor growth and tumor formation relative to control 15 cells. Furthermore, these assays is useful to confirm the anti-101P3AI I inhibitory effects of candidate therapeutic compositions, such as for example, 101 P3A I1 antibodies or intrabodies, and 10 1 P3A I I antisense molecules or ribozymes, or 10 1P3AI 1 directed small molecules. In Figure 22, we depict the effect of a small molecule, pertussis toxin (PTX) on tumor formation by 3T3-101P3AI I cells. In this 20 experiment, SCID mice were injected with 3T3-101P3AI I alone or in conjunction with PTX. Each mouse was given 5 doses of PTX at 3-4 days interval. Tumor volume was evaluated by caliper measurements. Figure 22 shows that PTX inhibits tumor growth in a dose dependent manner. Delivery of PTX at shorter intervals, such as 5 time per week, resulted in a larger rate of inhibition of tumor growth, with 70% inhibition of tumor growth observed after 25 days (Figure 55). Similarly, treatment 25 with the G-protein inhibitor suramin inhibits the growth of 3T3-10IP3AI I tumors (Figure 59). In addition to demonstrating that 101P3AI I plays an important role in tumor growth, Figures 21 22 and M9 identify a signaling pathway associated with 10 1P3AI I and indicate that 101P3AI I produced its effect on tumor growth by activating an adenylate cyclase dependent pathway. 30 Example 35: 101P3A11 Monoclonal Antibody-mediated Inhibition of Tumors In Vivo The significant expression of 101P3AI I in cancer tissues, together with its restricted expression in normal tissues, makes 10 1P3A1 1 an excellent target for antibody therapy. In cases where the monoclonal antibody target is a cell surface protein, as is 101P3A I1, antibodies have been shown to be efficacious at inhibiting tumor growth (See, e.g., Saffran, D., et al., PNAS 10:1073-1078 or on the www 35 at pnas.org/cgi/doi/10.1073/pnas.051624698). In cases where the target is not on the cell surface, such as PSA and PAP in prostate cancer, antibodies have also been shown to recognize and inhibit growth of 124A cells expressing those proteins (Saffran, D. C., et al., Cancer and Metastasis Reviews, 1999, 18:437 449). As with any cellular protein with a restricted expression profile, 101P3AI l is a target for T cell based immunotherapy. Accordingly, the therapeutic efficacy of anti-10 1 P3A I I mAbs in human colon, kidney, bladder 5 and prostate cancer mouse models is modeled in 10 P3AI I -expressing kidney, colon, bladder or prostate cancer xenografts or cancer cell lines, such as those described in the Example entitled "In Vivo Assay for 10 1 P3A I I Tumor Growth Promotion", that have been engineered to express 10 1 P3A 1I. Antibody efficacy on tumor growth and metastasis formation is confirmed, e.g., in a mouse orthotopic prostate, colon, bladder or kidney cancer xenograft model. The antibodies can be 10 unconjugated, or can be conjugated to a therapeutic modality, as appreciated in the art. It is confirmed that anti-10 1 P3AI I mAbs inhibit formation of 10 1 P3AI I -expressing kidney, colon, bladder and prostate tumors. Anti- 10 1 P3A II mAbs also retard the growth of established orthotopic tumors and prolong survival of tumor-bearing mice. These results indicate the utility of anti-101P3AI I mAbs in the treatment of local and advanced stages of cancer. (See, e.g., Saffran, D., et al., PNAS 10:1073-1078 or 15 www. pnas.org/cgi/doi/l 0.1073/pnas.051624698).

Administration of anti-101P3AI I mAbs retard established orthotopic tumor growth and inhibit metastasis to distant sites, resulting in a significant prolongation in the survival of tumor-bearing mice. These studies indicate that O1P3Al I is an attractive target for immunotherapy and demonstrate the therapeutic potential of anti-OIP3AI I mAbs for the treatment of local and metastatic kidney, colon, bladder and prostate cancer. Similar studies manifest that 1OP3A1 I is safe and effective when used in combination with other therapeutic modalities such as surgery, radiation therapy, hormone therapy or chemotherapy. This example demonstrates that unconjugated 101P3A II monoclonal antibodies effectively to inhibit the growth of human bladder tumors grown in SCID mice; accordingly a combination of such efficacious monoclonal antibodies is also effective. Tumor inhibition using multiple unconjugated 101P3A1I mAbs Materials and Methods IOP3AI I Monoclonal Antibodies: Monoclonal antibodies are raised against 101 P3A II as described in the Example entitled "Generation of IOP3A1 1 Monoclonal Antibodies (mAbs)." The antibodies are characterized by ELISA, Western blot, FACS, and immunoprecipitation for their capacity to bind 101 P3AI 1. Epitope mapping data for the anti- 101 P3A I I mAbs, as determined by ELISA and Western analysis, recognize epitopes on the 101P3AI I protein. Immunohistochemical analysis of prostate cancer tissues and cells with these antibodies is performed. The monoclonal antibodies are purified from ascites or hybridoma tissue culture supernatants by Protein G Sepharose chromatography, dialyzed against PBS, filter sterilized, and stored at -20*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 UM-UC3, J82, CaKi 1, 769P, CaOv I or PA I tumor xenografts. Cell Lines The bladder, kidney and ovary carcinoma cell lines, UM-UC3, J82, CaKil, 769P, CaOvl and PAl as well as the fibroblast line NIH 3T3 (American Type Culture Collection) are maintained in DMEM supplemented with L-glutamine and 10% FBS. A UM-UC3-10IP3AI 1, J82-10IP3AI 1, CaKil-1OIP3AI 1, 769P-IOIP3AI 1, CaOvl-1OP3A 11, PAl 1lP3A1I1 and 3T3-10lP3Al I cell populations are generated by retroviral gene transfer as described in Hubert, R.S., et al., Proc Nati Acad Sci U S A, 1999. 96(25): 14523. Xenograft Mouse Models. Subcutaneous (s.c.) tumors are generated by injection of I x 10 *cancer 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 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. Orthotopic injections are performed under anesthesia by using ketamine/xylazine. For bladder orthotopic studies, an incision is made through the abdomen to expose the bladder, and tumor cells (5 x 103) mixed with Matrigel are injected into the bladder wall in a 10-pil volume. To monitor tumor growth, mice are palpated and 125 blood is collected on a weekly basis to measure BTA levels. For kidney and ovary orthopotic models, an incision is made through the abdominal muscles to expose the kidney or the ovary. Tumor cells mixed with Matrigel are injected under the kidney capsule or into the ovary in a 10-jul volume (Yoshida Y et al, Anticancer Res. 1998, 18:327; Ahn et al, Tumour Biol. 2001, 22:146). To monitor tumor growth, blood is collected on a weekly basis measuring G250 and SM047 levels. The mice are segregated into groups for the appropriate treatments, with anti 101P3A II or control mAbs being injected i.p. Anti-101P3AI 1 mAbs Inhibit Growth of 10 1 P3A l -Expressing Xenoaraft-Cancer Tumors The effect of anti-lOP3AI 1 mAbs on tumor formation is tested on the growth and progression of bladder, kidney and ovarian cancer xenografis using UC3-01 P3A 11, J82-101P3A 1, CaKil-101P3Al 1, 769P 1OIP3Al 1, CaOv1-10 IP3A1 I and PAl-IO1P3Al I orthotopic models. As compared with the s.c. tumor model, the orthotopic model, which requires injection of tumor cells directly in the mouse bladder, kidney and 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; Kubota, 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 nAbs on clinically relevant end points. Accordingly, tumor cells are injected into the mouse bladder, kidney or ovary, and 2 days later, the mice are segregated into two groups and treated with either: a) 2 00-500gg, of anti-IOIP3AI I Ab, or b) PBS three times per week for two to five weeks. A major advantage of the orthotopic cancer models 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 tumor-specific cell-surface protein such as anti-CK20 for bladder cancer, anti-G250 for kidney cancer and SM047 antibody for ovarian cancer models (Lin S et al, Cancer Detect Prev. 2001;25:202; McCluggage W et al, Histopathol 2001, 38:542). Mice bearing established orthotopic tumors are administered 10OOpg injections of either anti-IO1P3A1 1 mAb or PBS over a 4-week period. Mice in both groups are allowed to establish a high tumor burden, to ensure a high frequency of metastasis formation in mouse lungs. Mice then are killed and their bladders, livers, bone and lungs are analyzed for the presence of tumor cells by IHC analysis. These studies demonstrate a broad anti-tumor efficacy of anti-1OP3A1 I antibodies on initiation and progression of prostate and kidney cancer in xenograft mouse models. Anti-IOIP3AI I antibodies inhibit tumor formation of tumors as well as retarding the growth of already established tumors and prolong the survival of treated mice. Moreover, anti-1O1P3A1 I mAbs demonstrate a dramatic inhibitory effect on the spread of local bladder, kidney and ovarian tumor to distal sites, even in the presence of a large tumor burden. Thus, anti OlP3Al ImAbs are efficacious on major clinically relevant end points (tumor growth), prolongation of survival, and health. Example 36: Therapeutic and Diagnostic use of Anti-101P3All Antibodies in Humans. Anti-101P3A II 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-1OP3Al 1 mAb show strong extensive staining in carcinoma but significantly lower or undetectable levels in normal tissues. Detection of 101P3AI I in carcinoma and in 126 metastatic disease demonstrates the usefulness of the mAb as a diagnostic and/or prognostic indicator. Anti IOIP3AI I 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-IOIP3AI I mAb specifically binds to carcinoma cells. Thus, anti 1OP3AI I 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 101P3AI 1. Shedding or release of an extracellular domain of 101P3A1 1 into the extracellular milieu, such as that seen for alkaline phosphodiesterase BlO (Meerson, N. R., Hepatology 27:563-568 (1998)), allows diagnostic detection of IOIP3Al I by anti 1OP3Al I antibodies in serum and/or urine samples from suspect patients. Anti-1OP3AI 1 antibodies that specifically bind IOIP3AI 1 are used in therapeutic applications for the treatment of cancers that express 10 1P3A 11. Anti-101P3A II 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-1OP3A 1I 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 "O1P3AI I Monoclonal Antibody-mediated Inhibition of Bladder, Kidney and Ovarian Tumors In Vivo"). Conjugated and unconjugated anti- 101P3A 1l 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 37: Human Clinical Trials for the Treatment and Diagnosis of Human Carcinomas through use of Human Anti-101P3A11 Antibodies In vivo Antibodies are used in accordance with the present invention which recognize an epitope on 101 P3A 11, and are used in the treatment of certain tumors such as those listed in Table I. Based upon a number of factors, including 1OP3A 11 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. I.) Adjunctive therapy: In adjunctive therapy, patients are treated with anti- 101 P3AI I antibodies in combination with a chemotherapeutic or antineoplastic agent and/or radiation therapy. Primary cancer targets, such as those listed in Table 1, are treated under standard protocols by the addition anti-101P3A 1 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 101P3A I antibodies are utilized in several adjunctive clinical trials in combination with the chemotherapeutic or antineoplastic agents adriamycin (advanced prostrate carcinoma), cisplatin (advanced head and neck and lung carcinomas), taxol (breast cancer), and doxorubicin (preclinical). II.) Monotherapy: In connection with the use of the anti- 10 1 P3A 11 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. 127 111.) Imaging Agent: Through binding a radionuclide (e.g., iodine or yttrium (Im3, yn) to anti 101P3AI I 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 I0IP3AI 1. In connection with the use of the anti-IOP3AI I 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 ("' In)-101P3A1 1 antibody is used as an imaging agent in a Phase I human clinical trial in patients having a carcinoma that expresses 10IP3AI I (by analogy see, e.g., Divgi etal. J. Nall. 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- 101 P3A II 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-101P3AI 1 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 10IP3A1 I antibodies that are fully human antibodies, as compared to the chimeric antibody, have slower clearance; accordingly, dosing in patients with such fully human anti-10lP3A 1I antibodies can be lower, perhaps in the range of 50 to 300 mg/rm 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- 101 P3A 11 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-101 P3A II 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-101P3AI I antibodies. As will be appreciated, one criteria that can be utilized in connection with enrollment of patients is 101P3AI 1 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 101P3A 11, Standard tests and follow-up are utilized to monitor each of these safety concerns. Anti-OIP3AI I antibodies are found to be safe upon human administration. 128 Example 38: Human Clinical Trial Adiunctive Therapy with Human Anti-1O1P3A11 Antibody and Chemotheraneutic Agent(s) A phase I human clinical trial is initiated to assess the safety of six intravenous doses of a human anti 101P3AI 1 antibody in connection with the treatment of a solid tumor, e.g., a cancer of a tissue listed in Table I. In the study, the safety of single doses of anti-1OP3AI I antibodies when utilized as an adjunctive therapy to an antineoplastic or chemotherapeutic agent, such as cisplatin, topotecan, doxorubicin, adriamycin, taxol, or the like, is asscsscd. The trial design includes delivery orsix single doscs of an anti-10P3AI I antibody with dosage of 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 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) 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 HAHA response); and, (iii) toxicity to normal cells that express lOP3A1 1. 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-101P3AI 1 antibodies are demonstrated to be safe and efficacious, Phase II trials confirm the efficacy and refine optimum dosing. Example 39: Human Clinical Trial: Monotherapy with Human Anti-101P3A11 Antibody Anti-1OP3AI 1 antibodies are safe in connection with the above-discussed adjunctive trial, a Phase 11 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- 101 P3A 11 antibodies. Example 40: Human Clinical Trial: Diagnostic Imaging with Anti-IOIP3AI1 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-10IP3AI I 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. Nall. Cancer Inst. 83:97-104 (1991). The antibodies are found to be both safe and efficacious when used as a diagnostic modality. 129 130 Example 41: Identification of 1O1P3A1I sequences involved in ligand binding. As shown in Figure 4, the transmembrane regions of 101P3AI I and mouse olfactory receptor S25 (ORS25) predicted using the TMHMM algorithm are highlighted in gray. The amino acids of ORS25 predicted by Floriano, et al. to be involved in binding of the ligand hexanol and/or involved in 5 the formation of the ligand binding pocket are italicized and bolded in Figure 4, and are listed below. (Floriano, W. B., et al, 2000, Proc. Nat]. Acad. Sci., USA, 97:10712-10716) Leu 131 Ala 230 Val 134 lie 231 10 Val 135 Gly 234 Gly 138 Thr284 Thr 139 Phe287 Ser 193 Gln 300 Ser 197 Lys302 15 Phe225 Sequences of 101P3A1 I involved in ligand binding are identified based on homology to mouse olfactory receptor S25. Shown is the amino acid alignment of 10 1 P3A I I with mouse olfactory receptor S25 depicting the predicted transmembrane domains of each GPCR. The amino acids of S25 involved in 20 the recognition and binding of its ligand hexanol or that lie in the proximity of the binding pocket (Floriano, W. B., et al, 2000, Proc. Nati. Acad. Sci., USA, 97:10712-10716), are also shown. These amino acids lie close to or within the transmembrane domains of ORS25. Accordingly, the structurally homologous regions of 101P3A 1 are involved in the binding of its cognate ligand. These regions encode the amino acids of the first extracellular loop and of the amino terminal end of transmembrane 25 domain 3 (amino acids 82-112), the amino acids at the carboxyl terminal end of transmembrane domain 4 and into the second extracellular loop (amino acids 160-185), the amino acids at the end of the second extracellular loop and into transmembrane domain 5 (amino acids 186-212), and the amino acids at the carboxyl terminal end of transmembrane domain 6, the third extracellular loop, and the amino terminal end of transmembrane domain 7 (amino acids 250-280). Thus, ligands of 10 1 P3A II are identified that 30 interact with at least 3 of the following regions of 10 l P3A 11: amino acids 82-112, amino acids 160-185, amino acids 186-212, and, amino acids 250-280. Example 42 : Homology Comparison of 101P3A11 to Known Sequences The 101 P3A 11 protein of Figure 3 has 318 amino acids with calculated molecular weight of 35 35.2 kDa, and pl of 8.7. 10 1 P3A II is predicted to be a cell surface protein. Cellular localization was demonstrated by FACS analysis and immunofluorescence in cells engineered to express 10 1 P3A 11, as 131 shown in Figure 63 (panel B). Immunofluorescence staining of permeabilized cells revealed thatl0l P3A l I becomes internalized and localizes then to the cytosol (Figure 63). 10 1 P3A II shows best homology to rat olfactory receptor RAI c (gi 3420759, http://www.ncbi.nlm.nih.gov) sharing 59% identity and 76% homology with that protein. 101P3A1 I 5 also shows homology to human prostate specific GPCR (gi 13540539) and human olfactory receptor 51112 (gi 14423836), sharing 59% identities/ 77% homology, and 53% identities/ 69% homology with each, respectively (Figures 23-25). More recent studies have identified a mouse homolog of 101 P3A 11, namely MOR 18-1, (gi 18479284, Figure 64). MOR18-1 is a mouse olfactory receptor that shares 93% identity and 96% homology with the 10 1 P3AI I protein. 10 In addition to 10 1 P3AI I variant I used predominantly in the studies listed below, 10 1 P3A1 I has 2 additional variants. Variant 3 is a SNP of variant I and exhibits a mutation at position 104, with an exchange of isoleusine to methionine at that position. Variant 3 is expected to be localized to the cell surface, in a manner similar to variant 1, and exhibits the same motifs and transmembrane domains as variant I (table XXI). Variant 2 of 101P3AI I is 72 amino acids long, contains 2 transmembranes and 15 localizes predominantly at the cell surface with some cytoplasmic localization. Sequence and motif analysis indicate that 101 P3AI I belongs to the family of olfactory receptors. Bioinformatic analysis revealed 10 1 P3AI I to be a 7 transmembrane protein, with strong domain and structural homology to G-protein coupled receptors (GPCRs) (see Table XXI, TM Pred, Sosui, Pfam, Blocks, Print). Proteins that are members of the G-protein coupled receptor family exhibit 20 an extracellular amino-terminus, three extracellular loops, three intracellular loops and an intracellular carboxyl terminus. G-protein coupled receptors are seven-transmembrane receptors that are stimulated by polypeptide hormones, neurotransmitters, chemokines and phospholipids (Civelli 0 et al, Trends Neurosci. 2001, 24:230; Vrecl M et al, Mol Endocrinol. 1998, 12:1818). Ligand binding traditionally occurs between the first and second extracellular loops of the GPCR. Upon ligand binding GPCRs 25 transduce signals across the cell surface membrane by associating with trimeric G proteins. Their signals are transmitted via trimeric guanine-nucleotide binding proteins (G proteins) to effector enzymes or ion channels (Simon et al.,1991, Science 252:802). Signal transduction and biological output mediated by GPCR can be modulated through various mechanisms including peptide mimics, small molecule inhibitors and GPCR kinases or GRK (Pitcher JA et al, J Biol Chem. 1999, 3; 274:34531 ;Fawzi AB, et 30 al. 2001, Mol. Pharmacol., 59:30). Recently, GPCRs have also been shown to link to mitogenic signaling pathways of tyrosine kinases (Luttrell et al., 1999, Science 283:655; Luttrell et al., 1999 Curr Opin Cell Biol 11:177). GPCRs are regulated by phosphorylation mediated by GPCR kinases (GRKs), which themselves are indirectly activated by the GPCRs (Pitcher et al., 1998, Ann. Rev. Biochem. 67:653). Olfactory GPCRs transmit 35 their signals by activating the cAMP pathway via adenylate cyclase resulting in downstream signaling to protein kinase A, and by activating the phospholipase C pathway by generating inositol 1,4,5- 131A trisphosphate (IP3) and diacyl-glycerol (DAG) (Breer, 1993, Ciba Found Symp 179:97; Bruch, 1996, Comp Biochem Physiol B Biochem Mol Biol 113:451). IP3 results in an increase in intracellular calcium, while DAG activates protein kinase C. Recent studies have associated GPCRs with cellular transformation. In particular, KSHV G 5 protein-coupled receptor was found to transform NIH 3T3 cells in vitro and induces multifocal KS-like lesions in KSHV-GPCR-transgenic mice (Schwarz M, Murphy PM. J Immunol 2001,167:505). KSHV GPCR was capable of producing its effect on endothelial cells and fibroblasts by activating defined signaling pathways, including the AKT survival pathway (Montaner S et al, Cancer Res 2001, 61:2641). In addition, KSHV-GPCR induced the activation of mitogenic pathways such as AP-I and NFkB, 10 resulting in the expression of pro-inflammatory genes (Schwarz M, Murphy PM. J Immunol 2001,167:505). Other GPCR associated with tumor formation include G2A, and the PAR-I, which has been found to induce transformation of NIH 3T3 cells (Whitehead I et al, Oncogene 2001, 20:1547).

This information indicates that 101P3AI I plays a role in the transformation of mammalian cells, induces mitogenic responses including activation of various signaling pathways, and regulate gene transcription by transmitting cell surface signals to the nucleus, see also, the Example entitled, "In Vivo Assay for O1P3AI I Tumor Growth Promotion". Accordingly, when 1OIP3A I I functions as a regulator of cell transformation, tumor formation, or as a modulator of transcription involved in activating genes associated with inflammation, tumorigenesis or proliferation, 101P3AI I is used for therapeutic, diagnostic, prognostic and/or preventative purposes, in manners analogous to or that track other GPCRs as discussed herein and in the art.. Example 43: 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). In particular, GPCRs have been reported to activate MAK cascades as well as G proteins, and been associated with the EGFR pathway in epithelial cells (Naor, Z., et al, Trends Endocrinol Metab. 2000, 11:91; Vacca F et al, Cancer Res. 2000, 60:5310; Della Rocca GJ., et al, J Biol Chem. 1999, 274:13978). Using immunoprecipitation and Western blotting techniques, proteins are identified that associate with 101P3AI 1 and mediate signaling events. Several pathways known to play a role in cancer biology can be regulated by O1P3AI 1, 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). Using Western blotting and other techniques, the ability of 101P3A 1 to regulate these pathways is confirmed. Cells expressing or lacking 101P3A II are either left untreated or stimulated with cytokines, androgen and anti-integrin antibodies. Cell lysates were analyzed using anti-phospho-specific antibodies (Cell Signaling, Santa Cruz Biotechnology) in order to detect phosphorylation and regulation of ERK, p38, AKT, P13K, PLC and other signaling molecules. Using such techniques, we showed that 101P3Al I alters the tyrosine phosphorylation pattern of NIH 3T3 cells (Figure 26) indicating that LOP3A1 1 is regulating protein kinases and phosphatases. In the experiment, data shown in Figure 26, control 3T3-neo and 3T3-10P3A1 I cells were either treated with 0.5 or 10% FBS and whole cell lysates were analyzed by anti-phosphotyrosine Western blotting. Expression of 1OIP3AI 1 resulted in reduced phosphorylation of several proteins in NIH-3T3 cells, while inducing the phosphorylation of proteins at 79-81 and 28-32 kDa. Using anti-Phospho-ERK antibodies, we demonstrated that expression of 101 P3A 11 induced ERK phosphorylation in the prostate cancer cell line PC3 (Figures 27A and Figure 27B), and that ERK phosphorylation in IOIP3A1 I expressing cells was regulated by GPCR ligands. In this experiment, control PC3-neo cells and PC3-10IP3A 1I cells were left untreated (0.1% FBS) or were stimulated with 10% FBS, lipophosphatidic acid (LPA), gastrin releasing peptide (GRP), leukotriene (LKB4) or platelet activating factor (PAF). The cells were lysed and analyzed by Western blotting using anti-Phospho-ERK (Figure 27A) or anti-ERK (Figure 27B) mAb. The results showed that expression of 1OP3Al I mediated significant ER.K phosphorylation by FBS, LPA, GRP and PAF, while LKB4 resulted in a more modest level of ERK phosphorylation in PC3-101P3AI I cells. In contrast, none of the GPCR ligands induced significant ERK phosphorylation in PC3-Neo cells, demonstrating the specificity of GPCR ligands-mediated responses in 101P3A 1I expressing cells. The ERK overlay demonstrated 132 equal loading, supporting the specificity of this data. In order to delineate the signaling pathway by which 101P3A1 I mediates ERK phosphorylation in cancer cells, it was confirmed which of the two pathway inhibitors: MEK inhibitor PD98059 or the p38 inhibitor SB203580 regulate lOP3AI I mediated ERK phosphorylation (Figure 28). To obtain this data, PC3-neo and PC3- 101 P3A I I cells were treated with media alone or in the presence of PD98059, SB203580, or genistein were stimulated with FBS or GRP. Cells were lysed and analyzed by Western blotting using anti-Phospho-ERK or anti-ERK mAb. Treatment with 10% FBS or with GRP induced the phosphorylation of ERK in PC3-l0IP3Al I but not in control PC3-neo cells. IOIP3AI 1-mediated ERK phosphorylation was inhibited by the MEK-l inhibitor PD98059 but not the p38 inhibitor SB203580 or genistein. The ERK overlay demonstrated equal loading, supporting the specificity of the results. These results were confirmed by those obtained in two additional sets of experiments. The inhibition of 101P3AI I-mediated ERK phosphorylation by PD98059 demonstrates that 101 P3A 1 activated the classical MEK-ERK cascade, a pathway associated with mitogenesis, proliferation and tumorigenesis. Results in Figures 26-28 indicate that 101P3AI 1 regulates the activity of kinases, including ERK, and phosphatases. In order to confirm the association of 101P3A II with phosphatase activity, the effect of the protein phosphatase inhibitor sodium orthovanadate on 101 P3A II mediated ERK phosphorylation was determined (Figure 29). PC3-neo and PC3-10IP3AI 1 cells were grown in media alone or in the presence of sodium orthovanadate (Na3VO4), and were stimulated with 0.1% or 10% FBS. Cells were lysed and analyzed by Westem blotting using anti-Phospho-ERK or anti-ERK mAb. Treatment with Na3VO4 resulted in a 4.5-fold increase in ERK phosphorylation in PC3-l0IP3Al I cells, compared to a two-fold increase in PC3-neo cells. Results in Figure 29 confirm the contribution of protein phosphatases to 10 1P3A 11 mediated signaling. Several GPCRs have been shown to transactivate receptor tyrosine kinases associated with the cell membrane, such as the EGF receptor (EGFR) (Pierce K.L., et al, J Biol Chem. 2001, 276:23155; Nath, D., et al, J Cell Sci. 2001, 114:1213). In order to determine whether 10IP3A1 I signaling results in the activation of EGFR, we compared the effect of the EGFR inhibitor, AG1517, on EGFR- and 101P3AI 1-mediated ERK phosphorylation (Figure 30). In Figure 30, PC3-neo and PC3-101P3A1 1 cells were grown in media alone (0.1% FBS) or in the presence of AG1517. The cells were stimulated with 0.1% or 10% FBS, GRP or EGF, lysed and analyzed by Western blotting using anti-Phospho-ERK or anti-ERK mAb. Treatment with 10% FBS, GRP and EGF induced ERK phosphorylation in PC3-10IP3AI I cells. ERK phosphorylation by EGF was completely inhibited by AG1517. 1OIP3A I mediated ERK phosphorylation in cells treated with 10% FBS was partially inhibited by AG 1517. Data in Figure 30 indicate that some cross talk occurred between 101P3AI I and EGFR signaling pathways. In addition to activating the ERK cascade, IOIP3A I1 activated a parallel MAK pathway, namely p38. In Figure 31A and Figure 31B, PC3-neo and PC3-l10P3AI 1 cells were grown in 1% or 10% FBS. Cells were lysed and analyzed by Western blotting using anti-Phospho-p38 (Figure 31A) or anti-p38 (Figure 31B) monoclonal antibody (mAb). Our results demonstrate that expression of 1OP3AI 1 mediated p38 phosphorylation in cells treated with 10% FBS. Equal loading was demonstrated in the p38 overlay. Results shown in Figures 26-30 and Figure 31A-31B confirm that IOP3AI I activates several signaling pathways in cancer cells, including the ERK and p38 cascades. In addition to MAPK, 101P3A I I signaling was associated with protein phosphatase activity and EGFR transactivation. These signaling pathways have been associated with cell growth, survival and transcriptional activation, all of which play an important role in tumor initiation and progression. When 10 1P3Al I plays a role in the regulation of signaling pathways, whether 133 individually or communally, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. To confirm that- 101 P3A 11 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, SRFITCF/ELKI; MAPK/SAPK; growth/differentiation 3. AP-1 -luc, FOS/JUN; MAPK/SAPK/PKC; growth/apoptosis/stress 4. ARE-luc, androgen receptor; steroids/MAPK; growth/differentiation/apoptosis 5. p53-luc, p53; SAPK; growth/differentiation/apoptosis 6. CRE-luc, CREB/ATF2; PKA/p38; growth/apoptosis/stress Gene-mediated effects can be assayed in cells showing mRNA expression. Luciferase reporter plasmids can be introduced by lipid-mediated transfection (TFX-50, Piomega). 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 O1P3A1 I are mapped and used for the identification and validation of therapeutic targets. When IOP3AI I is involved in cell signaling, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 44: 101P3A1I Functions as a GPCR Sequence and homology analysis of 101P3AI I indicated that I0IP3AI I is a member of the olfactory receptor family of GPCR. Olfactory receptors are known to regulate biological responses by activating adenylate cyclase. In order to confirm that 10IP3AlI functions as a GPCR and mediates the activation of adenylate cyclase, cAMP accumulation in PC3 and PC3-101P3A 1 cells were compared (Figure 32). Control PC3 and PC3 1OP3A 1I cells were grown in a low concentration of fetal bovine serum (FBS) for 14 hrs in the presence or absence of pertussis toxin (PTX). The cells were stimulated with 0.1% or 10% FBS, washed in PBS and lysed using a lysis buffer provided by Amersham Pharmacia. Intracellular concentration of cAMP was measured using a commercially available enzyme immunoassay (EIA) according to the manufacturer's recommendations (Amersham Pharmacia). Each assay was performed in duplicate. Calculations of cAMP concentrations were based on OD450 of the standard curve. Expression of 101P3AlI induced a four-fold increase in cAMP accumulation in the absence of stimulation. Treatment with 10% FBS further enhanced cAMP accumulation in PC3-l0P3All cells to nearly seven-fold over control PC3-neo cells. 10lP3AIl mediated cAMP accumulation was inhibited by PTX. These results were confirmed by two separate sets of experiments. Results shown in Figure 32 demonstrate that IOP3AlI functions as a GPCR in prostate cancer cells and exhibits classical GPCR characteristics, such as cAMP accumulation that is inhibited by PTX. Since adenylate cyclase activity modulates intracellular levels of cAMP and induce downstream signaling events such as activation of protein kinase A, calcium and ERK MAPK signaling (Pierce K.L., et al, 134 135 Oncogene,: 2001, 20:1532), we determined that PTX, an inhibitor of adenylate cyclase signaling, prevents 10 1 P3A 1 1-mediated ERK phosphorylation along with inhibiting cAMP accumulation (Figure 33 and Figure 34). PC3-neo and PC3-10 1P3AI I cells were grown overnight in 0.1 % FBS in media alone or in the presence of pertussis toxin (PTX). Cells were stimulated with 0.1% or 10% FBS (Figure 5 33) or 10% FBS, EGF or GRP (Figure 34). Cells were lysed and analyzed by Western blotting using anti-Phospho-ERK mAb. Expression of 10 1 P3AI I mediated ERK phosphorylation by 10% FBS in PC3 cells, which was inhibited by PTX (Figure 33 and Figure 34). In contrast, GRP and EGF-mediated ERK phosphorylation was relatively unaffected by PTX (Figure 34), demonstrating the specificity of 101P3AI I mediated responses. These results were replicated in additional experiments. In addition to 10 inhibiting ERK phosphorylation and 101P3AI I -mediated signaling, PTX had a marked effect on the proliferation of PC3-101 P3A I I but not control PC3-neo cells (Figure 52). Figure 52 shows that PTX inhibited the proliferation of 10 1 P3A I I expressing cells in a dose dependent manner, and confirms that the GPCR function of 10 1 P3A 11 is important for tumor growth. GPCR transmit their signal by activating trimeric G proteins. Once GPCRs are activated, the 15 associated Ga subunit binds GTP, dissociates from the receptor and participates in downstream signaling events (Schild, D.,and Restrepo, D. Physiol Rev. 1998, 78:429-66). In order to determine that inhibition of Ga subunits has an effect on 10 1P3AI I mediated cell growth, the effect of two Ga inhibitors on the proliferation of 3T3-101 P3AI I cells was investigated. Control 3T3 and 3T3-10 1P3A I I cells were grown in the presence or absence of suramin or its derivative NF 449 (Sigma). Cells were analyzed for 20 proliferation 72 hours later (Figure 35). The experiment was performed in triplicate. The data showed that suramin and NF449 inhibited the proliferation of 3T3-101P3AI I cells by 60% and 80%, respectively. This response was 10 1 P3A I I specific as suramin and NF449 had no effect on the proliferation of control 3T3 cells. Similarly, inhibition of G protein activation by suramin and NF449 in PC3 cells inhibits the proliferation of PC3-101 P3AI I cells grown in 5% FBS (Figure 51). In parallel 25 with the inhibitory effect of suramin and NF449 on PC3-10 1P3AI I proliferation, we demonstrate their inhibitory effect on 101 P3AI 1 -mediated signaling in prostate cancer cells (Figure 50). As shown in Figures 27 and 28, treatment with FBS induces ERK phosphorylation in 101P3AI I-expressing cells. This ERK phosohorylation and activation was inhibited by suramin and NF449 in PC3-101P3AI I and 3T3-10 1 P3A I I cells. ERK phosphorylation was inhibited in a dose dependent manner in PC3 30 10 1 P3AI I cells treated with suramin. Thus, as 10 1 P3AI I is involved in GPCR activity, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. GPCRs can be activated by a variety of ligands, including hormones, neuropeptides, chemokines, odorants and phospholipids. In the case of olfactory receptors, individual olfactory receptors may recognize multiple odorants, and can are activated by a diverse array of molecules. These 35 ligands and molecules recognized by a receptor (as described above) are small molecules as described herein.

135A In order to identify 10 1 P3A I I (small molecule) ligand(s), the possibility that epithelial cells may be secreting 101P3A I I activators was investigated (Figure 36A and Figure 36B). Prostate cancer epithelial cells, (PC3, PC3-10IP3A 11, LAPC4 2 hT), normal prostate cells (PrEC), fibroblasts (3T3, 3T3 101P3A 11), and human kidney epithelial cells (293T) were grown in the presence or absence of FBS. 5 Cell supernatants were collected and used to stimulate PC3 and PC3-10 P3AI I cells. Cell lysates from resting and supernatant treated PC3 andPC3- 10 1 P3A II cells were lysed and analyzed by Western blotting with anti-Phospho-ERK (Figure 36A) and anti ERK (Figure 36B) mAb. As shown in Figure 36A and Figure 36B, supernatants form normal prostate cells, PrEC, and prostate cancer cells, PC3, PC3 101 P3A I I and LAPC4 2 hT, induced the phosphorylation of ERK in PC3-101P3AI I but not control PC3 cells. In contrast, no specific ERK phosphorylation was observed using supernatants from 3T3 or 293T cells. Our results show that prostate cells, grown in the absence of serum, produce one or more factors that contribute to the activation of 10lP3A II mediated signaling events. Thus, as 101P3A II responds to stimuli and functions in signaling and GPCR activity, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 45: Inhibitors of 101 P3A11 GPCR Function As mentioned in the Example entitled "Homology Comparison of 101P3AI 1 to Known Sequences," GPCRs are activated by ligand binding to the extracellular loops, resulting in the activation of trimeric G proteins and the initiation of several signaling cascades. Using this information, several therapeutic and small molecule strategies are utilized to inhibit GPCR activation or downstream signaling events. One strategy inhibits receptor and ligand binding. Recent studies using several types of GPCRs, have demonstrated the effectiveness of this strategy (Fawzi AB, ct al. 2001, Mol. Pharmacol., 59:30). Using a compound named SCH-202676, they inhibited agonist and antagonist binding to GPCRs by allosterically hindering ligand-GPCR interaction. Using this and even more specific allosteric (small molecule) inhibitors, signal transduction through IOP3AI 1 is inhibited, thereby providing therapeutic, prognostic, diagnostic and/or prophylactic benefit. A second approach is to inhibit G alpha subunit activation. Activation of GPCRs results in the exchange of GTP for GDP on the G alpha subunit of the trimeric G protein. Inhibition of Ga activation prevents the activation of downstream signaling cascades and therefore biological effects of GPCR. One molecule used to inhibit GDP exchange on Ga subunits is Suranim (Freissmuth M et al, 1996, Mol. Pharmacol, 49:602). Since suranim functions as a universal Ga inhibitor, it prevents the activation of most Ga subunits. Using techniques described, for example and without limitation, in the present Examples entitled "In Vivo Assay for IOP3AI I Tumor Growth Promotion; " "Identification and Confirmation of Potential Signal Transduction Pathways," "10 P3Al I Functions as a GPCR," and "Regulation of Transcription", small molecules are identified that selectively inhibit the Ga subunit that associates with IOIP3Al , thereby providing therapeutic, prognostic, diagnostic and/or prophylactic benefit. A third approach is to inhibit Ga subunit association with GPCR. In order for trimeric G proteins to be activated following GPCR/ligand interaction, it is necessary for them to associate with their corresponding GPCR. Mutational analysis has mapped the interaction of Ga to the first and third intracellular loops of GPCRs (Heller R at al. 1996, Biochem. Biophys. Res. Commun). Several studies have used synthetic (small molecule) peptides corresponding to the intracellular sequence of loops I and 3 as inhibitors (Mukherjee, S., et al. 1999, J. Biol. Chem.). Using such short peptides that serve as receptor mimics, they are used to compete for binding of Ga subunits to 1OIP3AI I and thereby provide therapeutic, prognostic, diagnostic and/or prophylactic benefit. Thus, compounds and small molecules designed to inhibit 101P3A II function and downstream signaling events are used for therapeutic diagnostic, prognostic and/or preventative purposes. Example 46: Involvement in Tumor Progression The IOIP3A11 gene can contribute to the growth of cancer cells. The role of 10IP3AI1 in tumor growth is confirmed in a variety of primary and transfected cell lines including prostate, colon, bladder and kidney cell 136 137 lines, as well as NIH 3T3 cells engineered to stably express 10 1 P3A 11. Parental cells lacking 101P3AI I and cells expressing 101P3A I I are evaluated for cell growth using a well-documented proliferation assay (Fraser SP, et al., Prostate 2000; 44:61, Johnson DE, Ochieng J, Evans SL. Anticancer Drugs. 1996, 7: 288). Using such a technique, we demonstrated (see Figure 37) that 10 1 P3AI 1 imparts a 5 growth advantage on NIH 3T3 cells. 3T3-neo and 3T3-101P3A I I cells were grown in 0.5% or 10% FBS and analyzed 48 hours later. The assay was performed in triplicate. Expression of 10 1 P3AI I resulted in 6-fold increase in proliferation relative to control 3T3 cells grown in 0.5% FBS. In addition, 10 I P3AI I imparts a growth advantage to PC3 cells as shown in Figures 53 and 62. PC3 cells grown in 0.5% and 10% FBS were compared to PC3-101 P3A1 I. Figure 53 shows that expression of 101P3AI I 10 enhances the proliferation of PC3 cells under both conditions. The effect of 10 P3AI I was also observed on cell cycle progression. Control and 10 1 P3AI 1-expressing cells were grown in low serum overnight, and treated with 10% FBS for 48 and 72 hrs. Cells were analyzed for BrdU and propidium iodide incorporation by FACS analysis. Figure 62 shows that expression of 10 1 P3A 1I enhances cell cycle entry in both 3T3 and PC3 cells. 15 To confirm the role of 10 1 P3A I I in the transformation process, its effect in colony forming assays was investigated. Parental NIH-3T3 cells lacking 10 1 P3AI I were compared to NIH-3T3 cells expressing 10 1 P3A 11, using a soft agar assay under stringent and more permissive conditions (Song Z. et al. Cancer Res. 2000; 60:6730). The results are shown in Figure 43, where 10 1 P3AI I induces colony formation of over 100 fold increase relative to neo resistant controls. We previously showed that 20 expression of 101P3AI I in NIH 3T3 cells induces the growth of these cells in soft agar (129-24usul), indicating that 10 1 P3A I I participates in the process of transformation. To confirm the role of 10 1 P3AI I in invasion and metastasis of cancer cells, a well-established assay is used. A non-limiting example is the use of an assay which provides a basement membrane or an analog thereof used to detect whether cells are invasive (e.g., a Transwell Insert System assay (Becton 25 Dickinson) (Cancer Res. 1999; 59:6010)). Control cells, including prostate, colon, bladder and kidney cell lines lacking 10 1 P3AI 1 are compared to cells expressing 10 1 P3A 11. Cells are loaded with the fluorescent dye, calcein, and plated in the top well of a support structure coated with a basement membrane analog (e.g. the Transwell insert) and used in the assay. Invasion is determined by fluorescence of cells in the lower chamber relative to the fluorescence of the entire cell population. 30 10 1 P3AI I can also play a role in cell cycle and apoptosis. Parental cells and cells expressing 10 1P3A I I 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. 35 Alternatively, the effect of stress on apoptosis is evaluated in control parental cells and cells expressing IOIP3AI 1, including normal and tumor prostate, colon and lung cells. Engineered and parental cells are 137A 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 10 1 P3AI I can play a critical role in regulating tumor progression and tumor load. 5 When 101 P3AI I 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 47: Involvement in Angiogenesis Angiogenesis or new capillary blood vessel formation is necessary for tumor growth (Hanahan ,D.; Folkman, J.; Cell. 1996, 86:353; Folkman J. Endocrinology. 1998 139:441). Several assays have been developed to measure angiogenesis in vitro and in vivo,. such as (lie tissue culture assays endothelial cell tube formation and endothelial cell proliferation. Using these assays as well as in vitro neo-vascularization, the role of 101P3A1 1 in angiogenesis, enhancement or inhibition, is confirmed . For example, endothelial cells engineered to express 101 P3A 11 are evaluated using tube formation and proliferation assays. The effect of 101P3A I I is also confirmed in animal models in vivo. For example, cells either expressing or lacking 101P3A1 I are implanted subcutaneously in immunocompromised mice. Endothelial cell migration and angiogenesis are evaluated 5-15 days later using immunohistochemistry techniques. OIP3AI 1 affects angiogenesis, and it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes Example 48: Regulation of Transcription The cell surface localization of IO1P3A1 I and its similarity to GPCRs indicate that 1OlP3A I 1 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 101P3A 11. For this purpose, two types of experiments are performed. In the first set of experiments, RNA from parental and 101P3A I-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, SRE-luc, ELKl-luc, ARE-luc, p53-luc, 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, 1IP3AI I plays a role in gene regulation, and it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 49: Involvement in Cell Adhesion Cell adhesion plays a critical role in tissue colonization and metastasis. 1OP3Al1 can participate in cellular organization, and as a consequence cell adhesion and motility. To confirm that 101 P3A 11 regulates cell adhesion, control cells lacking 101P3AI I are compared to cells expressing 101P3A 11, using techniques previously described (see, e.g., Haier et al, Br. J. Cancer. 1999, 80:1867; Lehr and Pienta, J. Natl. Cancer Inst. 1998, 90:118). Briefly, in one embodiment, cells labeled with a fluorescent indicator, such as calcein, are incubated on tissue culture wells coated with media alone or with matrix proteins. Adherent cells are detected by fluorimetric analysis and percent adhesion is calculated. In another embodiment, cells lacking or expressing 1OP3A 11 are analyzed for their ability to mediate cell-cell adhesion using similar experimental techniques as described above. Both of these experimental systems are used to identify proteins, antibodies and/or small 138 molecules'that modulate cell adhesion to extracellular matrix and cell-cell interaction. Cell adhesion plays a critical role in tumor growth, progression, and, colonization, and 101P3AI I is involved in these processes. Thus, it serves as a diagnostic, prognostic, preventative and/or therapeutic modality. Example 50: Protein-Protein Association Several GPCRs have been shown to interact with other proteins, thereby regulating signal transduction, gene transcription, transformation and cell adhesion (Sexton PM et al, Cell Signal. 2001, 13:73; Turner CE, J Cell Sci. 2000, 23:4139). Using immunoprecipitation techniques as well as two yeast hybrid systems, proteins are identified that associate with l0lP3AI 1. Immunoprecipitates from cells expressing 10P3AI I and cells lacking I0lP3AI I are compared for specific protein-protein associations. Studies are performed to confirm the extent of association of 101P3AI I with effector molecules, such as receptors, adaptor proteins and paxillin, kinases, phsophates and Ga proteins. Studies comparing 101P3A1 I positive and 10P3Al I 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 I10P3Al I-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 10 1P3A 11, 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 101P3A 11. Thus it is found that I0lP3AI I associates with proteins and small molecules. Accordingly, 10lP3Al land these proteins and small molecules are used for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 51: Biological effect of Anti-101P3AI1 Antibodies. The generation of anti-101P3A1 1 polyclonal Ab (pAb) using an amino-terminal peptide encoding amino acids 1-14 (MVDPNGNESSATYF; SEQ ID NO: ) as antigen was reported in our Priority Application. The effect of this antibody on 101P3A1 I mediated ERK phosphorylation (Figure 38) and cAMP accumulation (Figure 39) was determined. 293T cells were transfected with control or lOP3Al I cDNA. Cells were allowed to rest overnight, and treated with anti-1OIP3AI 1 or control Ab in the presence of 0.5% or 10% FBS. Cells were lysed and analyzed by Westerm blotting with anti-Phospho-ERK and anti-ERK mAb. Figure 38 shows that expression of 101P3AI I induces ERK phosphorylation in cells treated with 0.5 or 10% FBS. Anti-101P3A1 1 pAb reduced the phosphorylation of ERK in 293T-IOIP3A1 1 cells treated with 0.5% FBS. The ERK overlay demonstrated equal loading, supporting the specificity of this data. In order to confirm that anti-IO1P3AI 1 pAb has a detectable effect on cAMP accumulation, PC3 and PC3-10IP3AI I cells were grown in 0.1% FBS and treated with anti-1OIP3AI I pAb. Cells were analyzed for cAMP content as described in Figure 32. Expression of O10P3AI I induced a 5-fold increase in cAMP accumulation in PC3 cells, which was partially inhibited by PTX. Treatment of PC3-10IP3Al I cells with anti I0IP3Al I pAb resulted in a 4-fold increase in cAMP accumulation in PC3-10IP3Al 1 but not control PC3 cells. 139 Results shown in Figure 38 and Figure 39 indicate that anti-1OP3AI I pAb produces a measurable biological effect in cells expressing IOIP3AI 1. Accordingly, OIP3AI I is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 52: 1OIP3A11 Promoters A eukaryotic cells promoter is a short DNA sequence located in the 5' region of a gene. It provides binding sites for RNA polymerase and associated transcriptional cofactors, which upon assembly promotes transcription of the gene. In humans, most genes are transcribed by RNA polymerase II. The promoter DNA sequence normally contains binding motifs for RNA polymerases and its associated cofactors and activators including a TATA-box, cap signal, CCAAT-box and the GC-box. A eukaryotic cell enhancer is DNA sequence where transcriptional factors and their associated coactivators or suppressors bind and interact with promoter bound RNA polymerase to regulate the expression of the gene located next to the promoter. While a promoter(s) locates close to the transcription starting site(s) of a gene (usually 25-30 base pairs), enhancers can be found up to 50,000 base pairs in either direction to the transcription starting site(s) of the gene. There are many different gene regulatory proteins, namely transcription factors and their associated coactivators and cosuppressors that bind to specific enhancer sequences and regulate gene expression. These proteins, upon interaction with specific DNA regulatory sequences and with each other, allow each gene to be regulated up or down in different tissues and cell types. Chapter 9. "Control of gene expression" in Molecular Biology of the Cell. 3 'd ed. Ed. by Alberts et al., (New York and London) Garland Publishing, 1994). Tissue specific gene expression is associated with the presence of specific combinations of transcription factors and their associated coactivators and suppressors, the presence of specific binding sites present in the DNA regulatory region of the gene for these factors, and the activation or inactivation of signaling pathways that modulate their relative activity. For example, prostate specific expression of prostate specific antigen, (PSA, or human kallikrein 3), is dependent on the presence of androgen receptor binding elements in defined 5' upstream enhancer and promoter sequences of the gene and intact androgen receptor signaling pathway (Pang S, et al., Cancer Res 1997 Feb 1; 57(3):495-9). It is also dependent on the presence of other cis-acting DNA regulatory elements in the promoter region (Zhang J, et al., Nucleic Acids Res. 1997, Aug. 1; 25(15):3143-50.) and on the expression of other transcription factors, such as the prostate specific ets-like transcription factor (Oettgen P, et al., J Biol Chem. 2000, Jan. 14; 275(2):1216-25). With the accumulation of data and knowledge on human gene expression, promoters and enhancers are identified using different algorithms and computer programs (Chapter 8 "Gene Prediction" in Bioinformatics Sequence and Genome Analysis, ed. by David W. Mount. Cold Spring Harbor Laboratory Press, 2001). Accordingly, we identified (Table LV) promoters in a 5.04 kB 5' upstream genomic region of the 101P3AI I coding sequence using Neural Network Promoter Prediction computer program (http://www.fruitfly.org/seq_tools/nnppAbst.html; Reese, M.G. and Eeckman, F.H. (1995) Novel Neural Network Algorithms for Improved Eukaryotic Promoter Site Recognition. Accepted talk for The Seventh International Genome Sequencing and Analysis Conference, Hyatt Regency, Hilton Head Island, South Carolina, September 16-20, 1995), indicated by the underlined sequences in Table LIV. Using a program called SIGNAL SCAN (http://bimas.dcrt.nih.gov/molbio/signal/; Prestridge, D.S. (1991) SIGNAL SCAN: A computer program that scans DNA sequences for eukaryotic transcriptional elements. CABIOS 7, 203-206.), which searches a comprehensive database of regulatory element binding sites, we found numerous transcriptional binding sites for 140 various known transcription factors in the 5.04 kB sequence 5' to the 101 P3A II gene, suggesting the presence of specific enhancer regions that may mediate tissue specific 101P3AI I transcription. Such transcription factors include, but are not limited to, NFAT, NF-1, NF-E, CP2, API, AP-2, Spl, OCT-I, OCT-2, NFKB, CREB, CTF, TFIIA, TFIIB, TFIID, Pit-I, C/EBP, SRF, and various steroid receptors, such as glucocorticoid receptor (GR) and androgen receptors (AR) (Mitchell P J and Tijan R (1989) Science 245: 37 1). Comparison of the 5 kB upstream sequence of the I0IP3AlI gene to the 5 kB upstream sequence of the PSA gene, 5 homologous regions were found that are important for prostate cell specific expression. Table LVI shows the alignment of the these sequences and also indicates predicted transcription factor binding sites common to both sequences identified using SIGNAL SCAN. Experimentally, one defines the regions in the 5' genomic upstream regions of the I01P3Al1 gene using various methods well known in the art, such as deletion and mutation analysis of the putative regulatory regions fused to a transcriptional reporter gene such as luciferase or chloramphenicol acetyl-transferase. These transcriptional reporter vectors are then introduced into cell lines, tissues, or transgenic animals to analyze the tissue and cell type specificity of transcription and expression of the reporter gene. To identify transcription factors and proteins that interact with specific 101P3A 11 transcriptional regulatory sequences, one employs one or more of various techniques known in the art such as DNAse footprinting, gel mobility shift assays, and DNA/protein affinity chromatography. Various techniques concerning use of promoters are set forth, e.g., U.S. Patent 5,919,652 which concerns embodiments of nucleic acid compositions that comprise prostate specific antigen (PSA) promoter alone or in combination with a cytomegalovirus (CMV) promoter and related uses.; and, U.S. Patent 6,110,702 which concerns PSA positive regulatory sequence (PSAR) and related uses. Once regulatory sequences are identified that mediate 101 P3A 11 tissue-specific expression, these sequences are employed in various gene therapeutic strategies for cancer, such as driving tissue-specific expression of a toxic gene or a cell suicide gene. Such cell suicide strategies are currently employed using the PSA-promoter enhancer using the thymidinc kinase/ganciclovir system (Suzuki S, Tadakuma T, Asano T, Hayakawa M. Cancer Res. 2001 Feb 15;61(4):1276-90). Unlike PSA, which is an androgen regulated gene, I0IP3A1 1 does not exhibit androgen regulated expression. Thus, identification and use of regulatory sequences of the 101P3AI I gene that mediate, e.g., prostate-specific, but androgen insensitive gene expression, is useful for the treatment of both early stage androgen sensitive and late stage androgen insensitive or hormone refractory prostate cancer. Example 53: Generation of PHOR-1 monoclonal antibodies The use of agents to identify the presence of PHOR- I in biopsy specimens or to neutralize the effect of PHOR-1 has a beneficial effect in diagnosis, prognoosis, prophylaxis and/or therapy. One particularly useful class of anti PHOR-l agents is antibodies, in particular monoclonal antibodies (mAbs) to PHOR-I. Anti PHOR-1 Abs, such as niAbs, are generated that react with the epitopes of the PHOR-I protein such that they either indicate it's presence, disrupt or modulate it's biological function (for example those that would disrupt the interaction with ligands or proteins that mediate or are involved in it's biological activity) or are able to carry a toxin to the cell which is expressing PHOR-l. The term anti PHOR-1 antibody as used herein is to be understood to cover antibodies to any epitope of the PHOR-l gene product. Diagnostic mAbs, e.g. those used for imaging or imnmunocytochemistry, comprise those that specifically bind epitopes of PHOR-I protein and thus demonstrate its presence. Therapeutic mAbs 141 include thbse that are useful for diagnosis but also comprise those that specifically bind epitopes of PHOR-1 exposed on the cell surface and thus are useful to modulate growth and survival of cells expressing PHOR-1 by disrupting the function of a cell expressing PHOR-1 and/or disrupting the interaction of cells expressing PHOR-I and the ligand for PHOR-1. Preferred antibodies which form one aspect of the invention include but are not limited to antibodies named X18(1)4, X18(1)10, X18(1)23, X18(4)7 or prefixed by the number X20 and X47 and derivatives thereof, the production of which is described herein. Hybridomas,respectively, that produce these antibodies were deposited with the ATCC on 14 May 2002. Pathological conditions which are characterized by the presence of PHOR- 1 expression include, but are not restricted to, neoplasms of tissues such as. those listed in Table I. One aspect of the invention provides a method of detecting the presence of PHOR- 1. A further aspect of the invention provides a method of treatment of conditions characterized by the presence of PHOR-1, comprising administering an effective amount of an anti PHOR-1 antibody. The administration of anti-PHOR-1 antibody is particularly advantageous in the treatment of conditions characterized by the presence of PHOR-1. The antibodies against PHOR-1 for use according to the invention can be from any species, and can belong to any immunoglobulin class. Thus, for example, the anti PHOR- 1 antibody for use according to the invention can be an immunoglobulin G, Immunoglobulin M or immunoglobulin A, Immunoglobulin E,. The anti PHOR- I antibody can be from an animal, for example mammalian or avian origin, and can be for example of murine, rat or human origin. The antibody can be a whole immunoglobulin, or a fragment thereof, for example a fragment derived by proteolytic cleavage of a whole antibody, such as F(ab') 2 , Fab' or Fab fragments or fragments obtained by recombinant DNA techniques, for example Fv fragments. Particularly useful antibodies for use according to the invention include humanized or fully human anti PHOR- I antibodies and fragments thereof. These antibodies are produced by any suitable procedure including, but not restricted to, mammalian cell and bacterial cell fermentation systems. The anti PHOR-1 mAbs are prepared by immunological techniques employing PHOR-1 antigens. Thus, for example, any suitable host can be injected (immunized) with a suitable reagent which makes PHOR- I available as an immunogen. Immune cells from the host, for example splenocytes or lymphocytes, are recovered from the immunized host and immortalized, using for example the method of Kohler et al, Eur. J. Immunol 6, 511 (1976), or their immunoglobulin genes can be isolated and transferred to an appropriate DNA vector for expression in an appropriate cell type. The resulting cells, generated by either technique, will be selected to obtain a single genetic line producing a single unique type of antibody more commonly known as a monoclonal antibody. Antibody fragments can be produced using techniques such as enzymatic digestion of whole antibodies e.g. with pepsin (Parham, J. Immunol 131:2895 (1983)) or papain (Lamoyi and Nisonoff, J. Immunol Meth. 56:235 (1983)), or by recombinant DNA techniques. Suitable hosts for the production of Mab's to PHOR-1 include mice, rats, hamsters and rabbits. For example, mice are immunized with a number of different reagents which make PHOR-I available as a source of antigenic material (immunogen). The route and timing if the immunizations will depend on the source and/or embodiment of the immunogen. Sources of immunogen for PHOR- I include, but are not restricted to, peptide, protein, fusion protein, DNA, RNA, cells or cell membranes. These can be used separately as immunogens or in combination to produce a specific immune reaction to PHOR-1. The use and application of these various immunogens is described fully in the accompanying examples. 142 EXAMPLE 54: Generation of antibodies to PHOR 1 using peptide encoding the first 23 N' terminal amino acids of PHOR-1 as the immunogen. In one embodiment eptides encoding the first 23 amino acids of PHOR-I (MVDPNGNESSATYFILIGLPGLE) (SEQ ID: ) were generated. These were, synthesized by SigmaGenosys using their custom peptide services. The peptide was synthesized with the addition of a Serine-Glycine-Serine Glycine-Cysteine (SGSGC) C-terminal linker sequence and then coupled to KLH through the C-terminal cysteine residue. In this orientation the N-terminal PHOR-l sequence remains free for antigenic recognition. Balb/c mice were immunized intraperitoneally (i.p.) with 10pg of peptide every 2 weeks over a 4 week period. The initial immunization was given i.p. in Complete Freunds Adjuvant (CFA) and the subsequent two immunizations were given i.p. in Incomplete Freunds Adjuvant (IFA). To determine the specificity of the response following immunization, mice were bled 10 days after the final immunization. Reactivity was determined by Enzyme Linked Immunosorbent Assay (ELISA) using non KLH conjugated (free) peptide as a target. All five mice had very high titers to the antigen. Two mice with the highest titers were given a final boost of 10 pg peptide in PBS and sacrificed for fusion 3 days later. Spleen cells from the immunized mice were fused with mouse Sp2/0 myeloma cells using PEG. 1500 according to standard protocols (Kohler et al, Eur. J. Immunol 6: 511 (1976)). Fused cells were plated in 10 96 well rmicrotiter plates and hybridomas were selected using HAT media supplement. Supernatants from fusion wells were screened 10-17 days later by ELISA against PHOR- I peptide. Twenty-one positive hybridomas were identified; these hybridomas are set forth in Table L Table L Clone number O.D. Clone number O.D. X20(5)1 0.157 X20(5)11 0.172 X20(5)2 0.511 X20(5)12 0.159 X20(5)3 0.310 X20(5)13 0.244 X20(5)4 0.735 X20(5)14 1.204 X20(5)5 0.160 X20(5)15 0.245 X20(5)6 0.322 X20(5)16 0.220 X20(5)7 0.179 X20(5)17 0.225 X20(5)8 0.173 X20(5)18 0.186 X20(5)9 0.170 X20(5)19 0.176 X20(5)10 1.171 X20(5)20 0.224 X20(5)21 0.502 EXAMPLE 55: Generation mAbs to PHOR I Using DNA Immunization. Therapeutic mAbs to PHOR-I comprise those that react with PHOR-I epitopes that disrupt or modulate the biological function of PHOR-1, for example those that disrupt its interaction with ligands or proteins that mediate or are involved in its biological activity. Structural modeling and experimental binding data of the murine olfactory receptor S25 indicates that amino acid residues at the junction of extracellular loop I and transmembrane domain 3, the region of extracellular loop 2 between transmembrane domains 4 and 5, and the 143 region of extracellular loop 3 between transmembrane domains 6 and 7 are involved in the binding of the ligand hexanol (Floriano, W.B., et al, 2000, Proc. Natl. Acad. Sci., USA, 97:10712-10716). Thus, in one embodiment, a vector was constructed that encodes the amino acids of extracellular loop 2 (159-202) between transmembrane domains 4 and 5 of PHOR-1 fused at the C-terminus to the human immunoglobulin GI (IgG) Fc (hinge, CH2, CH3 regions). This construct was used in a DNA based immunization strategy. Five Balb/c mice were immunized intra-dermally (ID) at the base of their tail. Three immunizations were given to each mouse of 10Opg of DNA in PBS over a two week period. To increase the immune response, each mouse was given an i.p. boost of 2 pg of PHOR-l-Fc protein in tissue culture media 10 days after the final DNA immunization. Bleeds were collected 10 days after the final immunization and reactivity in the sera to the middle loop of PHOR-I was tested by ELISA using PHOR-l-Fc fusion protein as a target (test 1). In parallel the sera were also tested on an unrelated human Fc fusion protein (test 2). Specific reactivity to the PHOR-I portion of the fusion protein was indicated. All mice were sacrificed and fusions and hybridoma selection was carried out as described in Examplc 54. Hybridoma supernatants were screened 10-17 days later by ELISA using PHORI-Fc protein as target. PHOR-1-Fc positives were subsequently cross screened on irrelevant Fc proteins to identify PHORI specific clones. A total of 16 positives specific for PHOR I-Fc but not reactive to other Fc fusion proteins were identified, these hybridomas are set forth in Table LI. Table LI Clone number O.D. Clone number O.D. Xl(l)l 0.557 XI(l)11 0.672 X1(1)2 0.511 Xl(1)12 1.209 X1(1)3 0.610 Xl(1)13 0.244 XI(1)4 0.735 XIa(2)1 1.109 Xl(l)5 0.860 XIa(2)2 .654 Xl(l)6 0.322 XIa(2)3 0.220 XI(1)7 0.779 Xl(1)8 0.473 X1(1)9 0.770 XI(l)I0 0.541 Example 56: Generation of Monoclonal Antibodies specific to Amino Acids 86-310 of PHOR-1 A fusion protein was constructed that encodes amino acids 86-310 of PHOR- I fused at the amino terminus to glutathione-S-transferase (GST). This fusion protein, GST-PHOR-1, encompasses sequences that proceed transmembrane domain 3 through transmembrane domain 7 so that all of the extracellular loops of PHOR-I are represented and the only extra-cellular domain that is not represented is the N' terminal. The fusion protein was purified from induced bacteria using standard glutathione affinity chromatography and used to immunize five mice following the protocol of Example 54. The PHOR-1 specific titer of the sera was determined 144 145 following the fourth immunization (bleed 2) using a fusion protein composed of amino acids 86-310 of PHOR-1 fused to maltose binding protein (PHORI-MBP), see Table LII below and Figure 48. The sera from each mouse specifically recognized PHOR-l protein in 293T cells transfected with an epitope tagged PHOR-1 cDNA as assessed by Western analysis (Figure 47). When screened on 293T-PHOR 1 5 cells compared to 293T-neo cells by FACS several of the sera were positive indicating generation of antibodies specific to cell associated PHORT1, see Figure 49. Table LII Mouse Titer,Bleed 2 I _ _ _I_ x 10 2 1x10- 6 3 2x10 4 lX10 5 5x10-' 10 Two mice with high titers were given a final boost of MBP-PHOR-I fusion protein in PBS and sacrificed for fusion 3 days later. Fusion and hybridoma growth selection was carried out as in Example 54. Hybridomas were screened by ELISA against GST-PHORI and cross-screened against MBP PHOR-I to identify PHOR-I sequence reactive clones. 48 hybridomas were identified that exhibited 15 specific reactivity to MBP-PHOR-I. These hybridomas are set forth in Table LIII. Table LIII Number Clone number O.D. I X18(l)l 0.425 2 X18(1)2 0.445 3 X18(1)3 0.573 4 X18(1)4 0.228 5 X18(1)5 0.218 6 X18(1)6 0.333 7 X18(1)7 1.459 8 X18(1)8 0.260 9 X18(1)9 0.253 10 X18(1)10 0.282 11 -X18(1)11 0.362 12 X18(1)12 0.343 13 X18(1)13 0.261 14 X18(1)14 0.773 15 X18(1)15 0.631 16 X18(1)16 1.427 17 X18(1)17 0.372 18 X18(1)18 0.657 19 X18(1)19 0.677 20 X18(1)20 0.338 21 X18(1)21 0.398 22 X18(1)22 0.232 23 X18(1)23 0.560 24 X18(1)24 0.554 25 X18(1)25 0.442 26 X18(4)1 0.848 27 X18(4)2 0.420 28 X18(4)3 0.230 29 X18(4)4 0.333 30 X18(4)5 0.389 31 X18(4)6 0.264 32 X18(4)7 0.358 33 X18(4)8 0.669 34 X18(4)9 0.429 35 X18(4)10 0.253 36 X18(4)11 0.277 37 X18(4)12 0.536 38 X18(4)13 0.662 39 X18(4)14 0.344 40 X18(4)15 0.256 41 X18(4)16 0.212 42 X18(4)17 0.304 43 X18(4)18 0.531 44 X18(4)19 0.286 45 X18(4)20 0.472 46 X18(4)21 0.770 47 X18(4)22 0.877 48 X 18(4)23 0.450 146 147 Four hybridomas reactive to MBP-PHOR-l exhibited strong specific reactivity to PHOR-I protein expressed in cells. This was demonstrated by Western analysis of 293T cells transfected with the epitope tagged PHOR-1 cDNA. The positive clones are indicated in bold, namely 18(1)4; 18(1)10; 18(1)23; and, 18(4)7. Hybridomas expressing, respectively, 18(1)4; 18(1)10; 18(1)23; and, 18(4)7 were deposited with 5 the ATCC on 14 May 2002. Example 57: Activation of 1OIP3A1. It is possible to measure the constitutive and ligand-mediated activation ofl0lP3Al I using the cAMP accumulation assay mentioned in Example 44 above or by measuring the binding of the GTP 10 analog, namely [35S]GTPyS. [35S]GTPyS binding is generically applicable to all GPCRs; and occurs proximal to the membrane surface, where the GPCR is located. Preferably, a GPCR:Fusion-Protein is utilized for these assays. The assay utilizes the ability of G protein-coupled receptors to stimulate [35S]GTPyS binding to membranes expressing the relevant receptors. Therefore, the assay may be used to directly screen compounds and antibodies for their effect on the activation of 101P3A 1. 15 A scintillation proximity assay can be utilized to monitor the binding of [35S]GTP7S to membranes expressing 10 1 P3A II -Gs-Fusion Protein (expressed in 293 or 3T3 cells). In brief, membrane proteins are incubated with [35 S]GTPyS and GDP for 60 minutes. The assay plates are counted in a scintillation counter. Throughout this application, various website data content, publications, patent applications and 20 patents are referenced. Websites are referenced by their Uniform Resource Locator, or URL, addresses on the World Wide Web (WWW.) 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 illustrations of individual aspects of the invention, and any that are functionally 25 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.

TABLE I: Tissues that Express 101P3AII When Malignant Normal Tissues: Prostate Ovary (by RT-PCR only) Malignant Tissues: Rectum Prostate Colon Kidney Breast Uterus Cervix Stomach Metastases Pool 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 Q GIn glutamine R Arg arginine I Ile isoleucine M Met methionine T Thr threonine N Asn asparagine K Lys lysine Val valine A Ala alanine D Asp aspartic acid B Glu glutamic acid G Gly glycine 148 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 URL www.ikp.unibe.ch/imanual/blosum62.html ) 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 1 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 149 TABLE IV HLA Class I/II Motifs/Supermotlfs TABLE IV (A): HLA Class I Supermotifs/Motifs SUPERMOTIFS POSITION POSITION POSITION 2 (Primary Anchor) 3 (Primary Anchor) C Terminus (Primary Anchor) Al TIL VMS FWY A2 LIVMAT2 IVMATL A3 VSMATLI RK A24 YFWIVLMT FIYWLM B7 P VILFMWYA B27 RHK FYL WMIVA B44 ED FWYLIMVA B58 ATS FWYLIVMA B62 QLIVMP FWYMIVLA MOTIFS Al TSM Y Al DEAS Y A2.1 LMVQIA T VLIMAT A3 LMVISATFCGD KYRHFA All VTMLISAGNCDF KRYH A24 YFWM FLIW A*3101 MVTALIS RK A*3301 MVALFIST RK A*6801 AVTMSLI RK B*0702 P LMFWYAIV B*3501 P LMFWYIVA B51 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 II Supermotif 1 6 9 W, F, Y, V,.I, L A, V, I, L, P, C, S, T A, V, I, L, C, S, T, M, Y 150 000 0 q -,U 4u c( 0 ~ , 4 ) ,,( 'V4 E k .- 8 151 00 .LI w b o 1oj > ~~~ W', ~ - -tn-kn 0-~ I,00 152I- 0 0) V 0 -15 EX. 0 0. o 0. 2 04) 0 4 .~ .~ .cl 4)) ) ) )4 04 -~ - - I - I - I o4 154 E.~E C -. 0 40 0 0 0' 0 41iie 00 r0 155 able V-101P3All-V1-Al-9mers Table V.-lO1P3A11-Vl-A1-9mers lStartjSubsequencel Score JIk~ue StartJ ubsequencejcrJs. ID Num] 211 GLDSLLISF]125.0o0I01[: 9 ESSATYFILIE 0075 46 30 LAFPLCSLY1.0 2 177 LSHSYCLHQ 47 2_____ IVPGN. 1 .0 1 1 NSTTIQFDA]1005] 48 22 1V QFWL]14.5011 4 1 211 ISFSYLLIL 11005 49____ 213 DSLLISFSY 3.7501 5 ] 56 HSLHEPMYI 110.0751 50 42 VLGNLTIIY 12.5001 6 219 FSYLLILKT 0.075 51 246 HVCAVFIFY 2.500 7 271 DSPLPVIL 0.075 52 112 GMESTVLLA 8SSATYFILI 53 58 LHEPMYIFL [2.250 9 78 TSSMPKMLA 0.0751- 54 7 GNESSATYF 12.250 10 LSGIDILIS10.0751 55 260 LSMVHRFSK [[ PPVLNPIVY 1.501 56 115 STVLLAMAF 111.25011 12 PVFIKQLPF '10.05 57 191 ACDDIRVNV I1.000 13 1 63][ YIFLCMLSG [F5-j[ 58 159 MAPLPVFIK 11.000 14[2547[ YVPFIGM ; ] 59 75 LISTSSMPK 1 5 1 46]1 LTIIYIVRT_ 60 173 RSNILSHSY 0.750 16 182 11 CLHQDVMKL 10.0501 61 [9 SSMPKML 0.75 7 FIKQLPFCR 170.o0o1 62 [71j GIDILISTS 10.500] 18 _29[LNPIVYGVI(10.sK 63 ] 135 HATVLTLPR_150 19 [ F269 64 ] [li LLAAMAFDRY losol 20_ [F2* 1] LISFSYLLI II...so] 65 ] 117 VLLAMAFDR 21 224T] EAQAKAFGT 110.o050 66 3 (451 NLTIIYIVR 11oso[ 22 [17[VAICHPLRH [ i][ 67 1 232 TRAQAKAF J 23 LCMLSGIDI I 68 181 YCLHQDVMK 0.400 24 F84 MLAIFWFNS 69 138 VLTLPRVTK 0.40011 25 DACLLQIFA 70 184 HQDVMKLAC 0.375 26 55 EHSLHEPMY1 71 139 LThPRVTKI 0.250][ 27 ILANIYLLV105 72 6 NGNESSATY 0.250F 28 F2 41 GTCVSHVCA 73 53 RTEHSLHEP 10.2251 29 1 LPGLEEAQF 1 74 257 FIGLSMVHR 10.200 30 LLQIFAIHS 75 1 57 SLHEPMYIF 10.200 11 31 1 ATVLTLPRVJ1o.oso I 243 CVSHVCAVF 0.200 32 LLVPPVLNP 0 0 146 KIG 110.200 33 I I AALMAPLPV 10.05011 78 126 YVAICHPLR 10.2001 1 341 I PFIG 110.05011 7.9 S ALMAPLPVF35 SMVHRFSKR 80 249 AVFIFYVPF 0.200 36 99 ACLLQIFAI 1 81 288 VLNPIVYGV 37 11 SATYFILIG 82 160 APLPVFIKQ 0.125 38 1 198 NVVYGLIVI r 83 274 LPVILANIY 0.125 39 14 LCSLYLIAV 84 96 QFDACLLQI 0.1251 1_ 40 MLSG4D0LI 0 0j 85 12 1 ATYFILIGL 0.125 41 I 0.050 272 SPLPVILAN ]20.125[ 42 IAVGLTI 0.050 86 284 LVPPVLNPI 0 0 IVIISAIGL 0.050 88 158 LMAPLPVFI 10.100 44 218 1 SFSYLLILK H o.0501E 89 19 L SAYI 9 ICHPLRHAT1.7 45 ]1899 LI 0.05 156 Table V-1O1P3A11-V1-A1-9mers 1 QFDACLLQM |0 .125L130 Start Subsequence|| Score[Seq. ID Num 3 DACLLQMFA |0.050 131 F209 AIGLDSLLI_ 4 [ ACLLQMFAI 0.050 132 [247 VCAVFIFYV | 0.0501| 92 6 LLQMFAIHS |0.050 133 TTIQFDACL |0.050| 93 5 CLQMFAIH 134 LEEAQFWLA || 045 i 94 __81 QMFAIHSLS | 135 298 TKEIRQRIL j[0.045 95 ] 2 FDACLLQMF 0.005 136 CSLYLIAVL ||0.0301| 96 ] 9 MFAIHSLSG 0.003 137 76 ISTSSMPKM I0. 030 I 97 7 LQMFAIHSL 0.002 38 114 ESTVLLAMA 98 0 . 030i 98 244 VSHVCAVFI 0. 030 Table VI: 101P3A11-V1-Al-10mers 92 s[ STTIQFDAC |0.025| 100 q [StarIt Subsequenc ID. Num J181 __ LMAPLPVFIK s.00 iTable V:101P3A11-V2-Al-9mers I 2 MVDPNGNESS5.000 140 Start Subsequence| Score Seq ID. Num 79 SSMPKMLAIF 3.000 141 7 VLASGVTLR 0.100 101 192 CDDIRVNVVY 2.500 142 18 i SSWPISICW 0.075 102 1 AVGNLTIIY 2.500 143 22 ISICWFLLC 00.07513 23 LEEAQFWLAF2.250 144 SICWFLLCS 104 2 KEIRQRILR 2.250 145 28 LLCSTQLSM 0.050 105 53 RTEHSLHEPM 2.250 146 LASGVTLRC 0.050 106 58 LHEPMYIFLC 2.250 147 _RCPSSWPIS 0.020 107 3 112_ G V 2.250 148 AVLASGVL 020 108 28VLP I.INPIVYGVK 2.000 149 3 YLIAVLASG 0.020 109 21 ISFSYLLILK 1 150 11 GVTLRCPSS 1.20 110 25 1 GLSMVHRFSK 1.000 151 1 1 SLYLIAVLA 0_.020 111_ 74 1ILISTSSMPK 1.00011 152 16 CPSSWPISI |0.013 112 [22 GLEEAQFWLA 0 153 27 FLLCSTQLS ||0.010K 113 114 IESTVLLAMAF 0.7501 154 IAVLASGVT |10.010]| 114 244[ CFIF 0 4 LIAVLASGV |0 .010|| 115 128 0.625 156 14 LRCPSSWPI 0.005 116 r 191 JACDDIRVNVV 10.500 157 [21 PISICWFLL 0.005 117 j117 VLLAMAFDRY||0.0 158 _ F19 SWPISICWF H0.005|| 118 2 L0.500 1L9isghj WPISICWFL H0.003| 119 TVLLAMAFDR .500 160 2 LYLIAVLAS 10.003 120 71 GIDILISTSS 0.500 161 12 VTLRCPSSW 0.003 21 29 WLAFPLCSLY 0.500 10 SGVTLRCPS 0.003 122 30 LAFPLCSLYL 0.500 163 9__ ASGVTLRCP 0.0023 123 7 GNESSATYFI|0.45 0 164 17 PSSWPISIC 10.002| 124 137 TVLTLPRVTKIO.400 165 24 ICWFLLCST 0.00 125 HEPMYIF .300 166 29 LCSTQLSME 0.001 126 139 LTLPRVTKIG 0.250|| 167 [F251 CWFLLCSTQ 10.0011 127 F CLLQIF|. | 168 26 WFLLCSTQL 10.001 128 10.200 169 13 TLRCPSSWP 0.000 129 284 LVPPVLNPIV 0.200 170 242 iTCVSHVCAVF||0.20011 171 able V: 101P3A11-V3-A1-9mers 156 R AALMAPLPVF10 .200|| 172 Start S que Scor eq ID Num 248 ||CAVFI FYVPF |10 .200H 73 157 able VI: 101P3A11-V1-A1-10mers Table VI: 11PA11-V1-A1-mers Start Subsequence Score Se ID. Num SttSubsequence Score Seq ID. Num 19 GLPGLEEAQF 0.200 174 1 RVNVVYGLIV 0.0501 219 260 LSMVHRFSKR 0.150 75 11 SATYFILIGL 0.o,5 22 IGLDSLLISF 0.125 1 251 FIFYVPFIGL 162 LPVFIKQLPF 0.125 177 98 DACLLQIFAI 0.050 222 44 GNLTIIYIVR 0.125 178LLILKTVLL 0.050 77 STSSMPKML7A 181 YCLHQDVMa 0050 224 245 1SHVCAVFIFY 0.125 180 2 [Ti ii QAKO0.050 225 212 LDSLLISFSY 0.125 181 1 283 LLVPPVLNPI 01 182 103 QIFAIHSLSG 0.052 257 FIGLSMVHRF 0.1001 183 209 1 AIGLDSLLIS _R 0 228 TREAQAKAFG0.090 184 35ICSLYLIAVLG 0.030 229 ESSATYFILI 15 [110 LSGESTVL0 230 10 SSATYFILIGl0.075 186 83 [MIFWFNS 02 1 69 LSGIDILIST 0 1 2___ 0.025 232 271 DSPLPVILAN 0.075 8 2 27 ][ v~ J 1 8j[172 1CRSNILS14sy 0l. 025 233 78 TSSMPKMLAI0.075 19 270 RDSPLPVILA 0.025 272 SPLPVILANI 0.050 190 6 II!! 0 2 216 LISFSYLLIL 0.0501r2 I icvLrEA O 236 273 1PLPVILANIY . 192 134 R 0.025 237 224 ILKTVLGLTR 10. 050 193 136 ATVLTLPRVT 0.025 238 126 YVAICHPLRHII0.050 194 106 AIHSLSGMES II.0501 195 ableV:101P3A11-V2-A10mers 199 VVYGLIVIIS 0.050 196 t Susequence Score se ID. New 269 RRDSPLPVIL 1005 197 19 JSSWPISICWF 0.150 239 94 TIQFDACLLQ0.5 1098 7 1 ASGVTLR 240 25 AQFWLAFPL . 050 92 STTIFDACL 0.050 200 28 QLSM 0.050 242 215 1LLISFSYLLI 0.050 201 2 SLYLIAVLAS 0.050 243 54 TESLHEPMY 0.050 202VLASGVTLRC 42 1 V IYjp 10.0501 203 16 PISI 0.050 39 LIAVLGNLTI ||0.0501 2041 CSLYLIAVLA 0.030 2 205 VIISAIGLDS |0.050I 205 6 IAVLASGVTLIqO.020 247 159 MAPLPVFIKQ 0.050 206 10 ASGVTLRCPS 0.015 248 68 MLSGIDILIS . 21 WPISICWFLL 0.013 249 36 [SLYLIAVIGN 10.0501 208 hGVTLRCPSSW 0.010 250208 100 [ CLLQIFAIHS 10.050 209 ISICWFLLCST 0.0101 Z251 57 ISLHEPMYIFL 0.050 2 4 YLIAVLASGV 0.111 25 65 FLC4LSGIDISGDI0.5 21[ 15 1 LRCPSSWPIS 0.010 203 LIVIISAIGL 0.050 212 5]LIAV1 ASGvr 2 276 VILANIYLLV 0.050 213 1 PSSWPISICW [,pO Jj25 261 SMVHRFSKRR 0,050 214 22 PISIiWFL LC125 208 SAIGLDSLLI. 215 11 q SGVTLRCPSS |0.0055 257 246 HVCAVFIFYV 0.050p 216 17 flCPSSWPISIC 0 176 ILSHSYCLHQ 0.050 217 29 H10.001 259 NPIVYGVKTK.050I 0.00 260 158 able VI:1O1P3A11-V2-A1-10mers ITable VII:1OlP3A11-V1-A2-9mers Start|Subsequence Score e ID. New sequence Sore ISeq. ID Num 25 |ICWFLLCSTQ 0.001 261 ] 119 LAMAFDRYV 2 298 9 LASGVTLRCP 0. 0011 262GLIVIISAI 299 3 1LYLIAVLASG 0.001 263 3 [i7]IRLFHA[ 300 3 0.0011 264 J8 ___ LEG L ]17.736[ 301 27 WFLLCSTQL 0.001 265 6 _________ 14.407 302 ISWPISICWFL 0.001 [ YIVRTEHSL 13.512 303 13T VTLRCPSSWP 00 j~ [67 NILSHSYCL 10. 868 304 ___QLPFCRSNI ][0lo.43 3[ 305. [6 fPMYIFLCML 9.9 [ 306 j able VI:101P3A11-V3-Al-10mers 1 LFIS [ 4 307 Startjsubsequence Scoreq ID. Num [ 2 [QFDACLLQMF 0.250 268 MAFDRYVAI 1[ 5.605 If 309 4 DACLLQMFAI|0.050 269 mLAiFwFNS . 7 7 310 6 1[CLLQMFAIHS 0.050 270 VVYGLIVII 311 I~IQFAISLS Wi~ 27 11111PLPVFIKQL I410 f 312 1 [ CQMFAIH S l . 025 2730 ILR1LFHAT 1I3.69] 313 L5-JLACLLQMFAIH 1LO.0120 L 272 7[LLQMFAIHSL 010 273 __ LISFSYLLI I365 f 314 jIQFDACLLQMj 2.0 74~:j16 AALMAPLPV 11 3.574 If 315___ 3 FDACLLQMFA 0.003 275 1284 LVPPVLNPI 3 8 [QFAIHSL 260.002 10 MFAIHSLSGI 0.001 277 417If VLGNLTII 3 318 [j F04 IVIISAIGL 11 3.178 If 319 trable VII:101P3A11-V1-A2-9mers TIQFDACLL'I 320 iStartjfSubsequence Score Seq. ID Num I FPLCSLYLIJI 2.666 321 214 SLLISFSYL 825.977 278 ATVLTLPRV I22 322 ~ 29 [11 ATYFILIGL7 I2 184i 323 3 288 VLNPIVYGV 1271.948 F 29ISMSVL 2 189 KLACDDIRV J243.432 280 [ TVLLI1 324 29 WLAFPLCSL 226.014 281 P I 2 247 VCAVFIFYV |215.192 282 [04 YILSM 1f 2.000 ][ 326 22 GLEEAQFWL 178.8151 283 27711 ILANIYLLV L177.358 284 34 1 LIAV I 1 328 3 (22111 YLLILKTaL1149.071[285 I1 1lil FSYLLILKT]I .4 329 215 11 LLISFSYLL] 138.001 1 YIV 1584 F 331 115 11 FIIJIGLPGIJ1J114.98Ii8 [ 44 8NTI FS3] 3 158 LMAPLPVFI 708 . 450 28 280 ~ 7.45 ][ea [ ~fLGNLTIIYI If1.465 I1 333 i 2 NIYLLVPPV 70.387 289 AIGLDSLLI E5 109 SLSGMESTV 69.52 290 = 3 4 8 KMLAIFWFN 291 YGLIVIISA 135 ~ 3 KL IFJj562] 29 YLLVPPVLN I1.8 f 336 3 1-2 CLHQDVMKL 149.134 2 I TTIQFDACL 337 26 AQFWLAFPL:] 46.480] 293 E 338 223 LILKTVLGL 42.494 294 2 81 TCVSHVCAV Ef 13 276 1 VILANIYLL I 42.494 295 198 NVVYGLV 6 3 3 38 1 YLIAVLGNL 29. 382 296 CMLSGIDIL H 2776 297 L SACDDIR 1J 7 342 159 able VII:101P3A11-V1-A2-9mers able VII:1O1P3A11-V2-A2-9mers Start Subsequence Score [Seq. ID Num ~ Start SubsecquenceJScorejjSeq ID. NumJ T_____ 13 YLIAVLASG i1 0

.

7 881 38 244 [VSHVCAVF I JE: 06 3 7 ] 344 J [21 PISICWFLL ]0.637iF386 79 SSMPKMLAI 0.580 345 26 WFLLCSTQL 0.2521 387 117 VLLAMAFDR 0.544 ][ 346 8 LAS__TRC 388 112 GMESTVLLA 0.528 347 2 11211 1fG4SVL [ 3712J ISICWFLLC 389 j 273 PLPVILANI 0.528 348 23 SICWFLLCS 0.090 35 CSLYLIAVL 0.487 349CPSSWPISI 0.0 68 391 101 LLQIFAIHS 0.481 350 VLASGVTLR 0.058][92 70 SGIDILIST 0.459 351 14 LRCPSSWPI 0.018 393 143 RVTKIGVAA 0.435 352 5 IAVLAsGvT 6.669 394 151 AVVRGAALM 0.4351 353 11 GVTLRCPSS 0.007 39 I 66 LCMLSGIDI 0.428 354 VTLRCPSSW 1O0.00711 396 251 FIFYVPFIG ][ 0.415 355 13 TLRCPSSWP 1F0.006 397 46 || LTIIYIVRT 0.405 11356 1 sswpisicw 0.004 398 63 YIFLCMLSG 0.401 357] 17 PSSWP II[C I 0 9 113 || MESTVLLAM 0.378 358 i0 SGVTLRCPS 400 169 LPFCRSNIL 0.360 359 29 LCSTQLSME 401 85 LAIFWFNST 0,334 360 ] [s RCPSSWPIS 402 TVLGLTREA 0.322 361 2 LYLIAVLAS 0 403 154 RGAALMAPL 0[31 362 SWPISICWF 03404 197 VNVVYGLIV 0.316 363 ASGVTLRCP[ 405 285 VPPVLNPIV 0.316 364 CWFLLCSTQ]IfO.OQf 40 128 AICHPLRHA 0.314 365 150 AAVVRGAAL 0.297 366 able VII: 101P3A11-V3-A2-9mers 208 IfSAIGLDSLL 1 0.2971 367 ] StartjSubsequence Score [Seq ID. u 77 L STSSMPKL 0.297 368 7 1 LQMFAIHSL 11331 407 57 SLHEPKYIF 0.288 369 ACLLQMFAI 331 4 4 207 ISAIGLDSL 0.267 370 6 LLQMFAIHS 11.481I 409 157 ALMAPLPVF [ 0.260 371 F5 CLLQMFAIH 0.215] 410 40 IAVLGNLTI 0.246 372 8 IHSLS 10.199 11 411 -6 SLYLIAVLG 0.238 373 3 11 DACLLQMFA 0.02811 412 _IGLPGLEEA 0.230 374 1 QFDACLLQM 1 413 S PVLA 0.226 375 2 FDACLLQMF H 0. 001 414 VMKLACDDI 0.220 376 ]j MFAIHSLSG o. j 415 100 CLLQIFAIH 11 0.215 377 lable VIII:1V1P3AI-V1-A2-Vmers able VII:1O1P3A1I-V2-A2-9mers- Str useune Seg. ID Num tart [Subsequence Score Seq ID. um 57 ILPMYIFL 722.583 416 20 WPISICWFL 26.460 378 118 LLAMAFDRYV 494.23 417 4 LIAVLASGV 16.258 379 SLLISFSYLL 300.355 418 1 SLYLIAVLA 15.898 380 VLGNLTIIYI 224.357 28 LLCSTQLSM 8.446 381 ALMAPLPVFI212,307 420 6 AVLASGVTL 6.916 382 251 FIFYVPFIGL1.94.987 421 24 ICWFLLCST 1.579 383 276 iLM IFV 0.231 422 27 FLLCSTQLS 384 L222 ILLILKTvLGL][3.527 160 Table VIII:101P3A11-V1-A2-10mers able VIII:I01P3A11-Vl-A2-Iomers Start Subsequence Score Seq. ID Num Start Subsequence Score Seq. ID Num 101 ifLLQIFAIHSL 83.527][1 424 3 Lz1iiLISTSSMPKM4]I2.67I]1 469 140 2014704252 254 YVPFIGLSMV 64.388 426 196 471 95][IQFDACLLQI[62.741 427 39 LIAVLGNLTI 2.439 472 246 HVCAVFIFYV[57.690 428 241[GTCVSHVCAV 2.222 473 63 YIFLCMLSGI 5 6 .155 429 1[7 42LILKTVLGLT 1.927 _ 474 65 FLCMLSGIDI 1 47.991 430 1 MAFDRYVAIC 1.678 475 249 AVFIFYVPFI 42.727 431 2 1 476 283 LLVPPVLNPI 4

.

7 2 432 8 SATYFIL .82 477 138 _VLTLPRVTKI 40.79211 433 17 LIGLPGLEEA 1.309 478 38 YLIAVLGNLTJ34.279 434 274 LPVILANIYL 1.304 479 238 KAFGTCVSHVJJ28.772 435 221 Jf L LG1268 480 67 CMLSGIDILI 27.879 436 .___ 1.139 481 235 AQAKAFGTCV 26 .797 SGMESTVLLA 1132 482 215 LLISFSYLLII26.604 438 1.127 483 83 JKMLAIFWFNS 26.114 439 100]JrCLLQIFAIHS 048 484 84 MLAIFWFNST 24.070 440 ] 279 ANIYLLVPPv 485 22I[ GLEEAQFWLA 18.576 441 ] 128 ][AICHPLRHATI 1.025 486 45 NLTIIYIVRT 442 GAALMAPLPVJ 0 487 219 JFSYLLILKTV15.71 443 FNSTIQFDA 0.865 488 304 RILRLFHVAT F14 .407 444 ] NVVYGLIVI 0 489 143 RVTKIGVAAV 13.997 445 233 REAQAKAFGT 0.840 490 167 KLPFCRSNI 13.698 446 129 ICHPLRHATV 0.772 491 82YCLHQDVMKLAIV 0.728 1__492 120 AMAFDRYVAI 11.302 448 191 ACDDIRVNVV 0.702 493 30 LAFPLCSLYL 10.264 449 11 SATYFILIGL 49 3 109 i SLSGMESTVL 8.759 450 85 LAIFWFNSTT 0 95 168 || QLPFCRSNIL 8 .759 451 188 MKLACDD 496 228 ||VLGLTREAQA 8.446 452 282 YLLVPPVLNP 497 302 ||RQRILRLFHV 7.149 453 272 ISPIPVILANI 0.580 190 || LACDDIRVNV 6.733 454 36[SLYLIAVLGN 499 206 IISAIGLDSL 5.628 455 112 GMESTVLLAM 500 181 ||YCLHQDVMKL 549 46VAVGA .0 0 86 ||AIFWFNSTTI 5.308 .457 163 0.504][ 50 3 243 CVSHVCAVFI 5.021 458 VLLAMAFDRY 503 203 || LIVIISAIGL 4.993 459 311 AVVRGAALMA 504 230 GLTREAQAKA 4460 66 LMLSGIDIL 0.405 292 IVYGVKTKE411DSLLISFSL 0.404 506 216 ISFSYLLILSTVLLAMA 0.378 507 160 APLPVFIKQL 4.510 463 211 IGLDSLLISFS[0.377 508 284ILVPPVrNPIV 4.242 _4 509 280 NIYLLVPPVL 3.854 465 29 WLAFPLCSLY 0.343 510 26 AQFWLAFPLC 3.541 466 32 FPLCSLYLI 0.339 511 299 KEIQRILRLJ 3.344 467i EPMYIFcNj 0.38 1 512 3 468:: [ET TTQDCL 0.9 513 161 Table VIII:101P3A11-V1-A2-10mers ACLLQMFAIH10. 0 0 5 Start 1Subsequenceil Score Seq. ID Numl ]QFDACLLQMF 805-67 SMPKMLAIFW 0.296 4 RLFHVATHA ae .12711-V1-A3-9ara able VIII:1O1P3A11-V2-A2-10mers 23 GAQAK 555 Start Subse uence Score K 30.000 556 4 YLIAVLASGV 319.939 57 SLHEPMYIFJ20.25 O 557 28 FLLCSTQLSM 84.555 517 211 GLDSLLISF 18.000 558 8 VLASGVTLRC 8.446 518 J_261 SMVHRFSKR 11.000 559 21 WPISICWFLL 6.325 519 117 VLLAMAFDR 118.000 560 14 TLRCPSSWPI 5.947 520 0.4I[ IVR 24 SICWFLLCST 2.357 521 LL FDRY 12.000 562 __0.548 52218.1001[ 563 6 IAVLASGVTL 0.504GLEEAQFWL 564 20 SWPISICWFL 0.122 524VLGNLTIIY 565 1 ][SLYLIAVLAI 0.12 525 I CLYI 10 525 ] 1571 ALMAPLPVF 116.7501 566 5 LIAVLASGVT 0.093 1[ 526 202 CLIVIISAI 6.07S 567 16 RCPSSWPISI [ 0.068 ][ 527 ]288 VLNPIVYGv-400 568 29 LLCSTQLSME [0.058 528 LISTSSMPK114.0001 569 19 SSWPISICWF 0.051 529 GMESTVLLA 3.600,1 570 17 ]CPSSWPISIC 0.031 530 ]124] HVCAVFIF 13.600 ~f 571 22 PISICWFLLCIf 0.029 If 531 J i18271 cLHQDvmKL 13601 572 7 AVLASGVTLR 0.011 532 ] AVIFYVPP 573 26 CWFLLCSTQLI 0.011 533 ________IF 3 .000 574 23 ISICWFLLCS 0.007 534 ]6 MLSGIDILi 12.700 575 13 VTLRCPSSWP 0.007 535 SLLISFSYL1 576 12 GVTLRCPSSW 0.007 536 I MAPLPVFIK 12.70011 577 25 ICWFLLCSTQ 037 1_0_ RLFHVATHA 1.500 578 27 WFLLCSTQLS 0.001 538 WLAFPLCSL_ 579 111SGVTLRCPSS 0.000 539 ii~[GTLCPSf ~ooII ~ 1611 PMYIFLCML. 131.3501 580 10 ASGVTLRCPS 0.000 540 100 CLLQIFAI1. 1 9 LASGVTLRCP 0.000 541 67 CSGIDILI1.3 582 3 LYLIAVLASG 0.000 542 KMLAIFWFN 583 15 1 LRCPSSWPIS 0.000 543 KIGVAAVVR 11.20011 584 18 j PSSWPISICW 10.000 544 1LPFCR 1.200 585 [T~TJLA DDIRV120, 58 -able VIII:101P3A11-V3-A2-10mers 221 YLLILKTVL 1.0 587 StartiS;ubequence Score Seq ID. Num 158 LMAPLPVFI 0.900 58a 7 LLQMFAIHSL I83.527 545 VVYGLIVII 589 1J IQFDACLLQM 129.77 546 j 112j YFILIGL 0 675 5 [ ]CLLQMFAIHS 11.048 11 547 ] 8 [YLIAVLGNL 5t 601 5 1 9 QMFAIHSLSG 0.199 548 AMAFDRYVA 106 1 592 3 I FDACLLMFA 0.175 549 J 257 1 FIGLSMVHR]0.600 5 4 DACLLQMFAI 0.145 550 277:] ILANIYLLV 0.600 594 [LQMFAIHSLS 0.048 551 F 168 1 QLPFCRSNI 10.600 S95 FAIHSLSF 552 H 187 VMKLACDD 0.00 596 162 able IX:101P3A11-V1-A3-9mers Table IX:1O1P3A11-V1-A3-9mers IStartitSubsequence Score Seq. ID Num Subsequence Seq. ID Nu] 262 MVHRFSKRR 10.6001 597 YVPFIGLSM 0.060 642 LILKTVLGL 598 152 VVRGAALMA 110.06011 643 -2911 ]PIVYGVKTK 599 300 EIRQRILRL 0.054 644 LSMVHRFSK 0.450 600 3 10 SSATYFILI 645 283 LLVPPVLNP I1 425 601 FIFYVPFIG 646 276 IAIL 040 60LVPN 126 YVAICHPLR 0 603 238 KAFGTCVSH 648 MLAIFWFNS 11 604 ] 32 FPLCSLYLI]0.041 649 [ 11-5 JTVLMF 10.300 605 9 H ACLLQIFAI [0.0411[ 650 05 ILRL AT 0.300[ 606 102 LQIFAIHSL 10.041 651 280 NIYLLVPPV 0.300 607 2 DSLLISFSY 110.041 652 109 SLSGMESTV .300f 608 PLCSLYLIA 0. 04=0 653 181 YCLHQDVMK 0.300 609 j 46 LTIIYIVRTL0.034 654 F243 CVSHVCAVF _.300 610 30 LAFPLCSLY 110.300[ 611 [rable IXl01P3A11-V2-A3-9mers 26 AQFWLAFPL ](0.270 612 ce S Se ID. Num 1981 NVVYGLIVI 0.270 613 VLASGVrLR10 655 L175 1 NILSHSYCL 0.270 614 [ill SLYLIAVLA 11i._500_ 656 101 1 LLQIFAIHS ]0.24 615 1 28 LLCSTQLSM 110.400 657 139 LTLPRVTKI 0.203 616 [ AVIASGVTL 658 297 KTKEIRQRI 0.203 617 YLIAVLAS 659 [_±iIf AVLGN=LTII 11.03 68[71 FLLCSTQLS H0.096 660n .LVPPVLNPI 023 619 WPISICWFL 661 176 ILSHSYCLH 0.20031 620 2 SICWFLLCS] 6627 163 PVFIKQLPF6 CPSSWPISI 663 IVIISAIGL 622 13 TLRCPSSWP 664 SLYLIAVLG o[0.iso] 623 ISICWFLLC102 665 AIFWFNSTT . 624 18 SSWPISICW 10.02211 666 4 fIIYIVRTE:H ]oij[ 625 [ ] IVAG 6 0.150 1 iv~r 93 TTIQFDACL] 0.135 [ 626 PISICWFLL ]EO. F1 668 273 PLPVILANI 0.135 627 VTLRCPSSW ][0.015 669 [ifISSYLLIL 10.115 628 [F][ GVTLRCPSS J10.0121 670 3 J.161 PLPVFIKQL .13 629 LASGVTLRC 15 FILIGLPGL 0.135] 630 ICWFLLCST 672 _ 209 AIGLDSLLI 0.120 19 SWPISICWF H1.00311 673 216 LISFSYLLI 0.12011 632 3 [ LRCPSSWPI 00003 674 1 [ 99 _[KEIRQRILR 11 0.ioa][ 633 32 fWFLLCSTQL 1o] oI 675 3 50I YIVRTEHSL 10.090 634 ] 5 67 3 304 j RILRLFHVA E0.0901[ 635 1 RCPSSWPIS 110.000 11 677 F19 I GLPGLEEAQ 10.0901 636 2 LYLIAVLAS 110 678 135_7 _HATVLTLPR_ .80 3 [135 1IRTLLR ~~e] 637 3291LCSTQLS4E 110.000 11 679 3 11224-1 ILKTVL0LT 0.06811 638 3 17:II PSSWPISIC ooj 680 11218JI SFSYLLILK I0.0601 639 3 2511 CWFLLjCSTQ O~OOjj 681 9 TIQFDACLL 10.0601L 640 SGVTLRCPS [ 682 274 LPVILANIY 0641 jEIASGVTLRL 0.01 683 163 [Fable IX:101P3A11-V3-A3-9mers Fable X:101P3A11-V1-A3-10mers Start SSubsequence Score ISeq ID. NumJ [stat~jubsguecelscoelleg D. um]36 SLYLIAVLGN]I 0.600 If 725 J 5 CLLQMFAIH 0.900 684 305 ILRLFHVATHI[ 0.600 726 a iFAHSLF 0.3001 685 168 ][QLPFCRSNILI 0.600 ] 727 6 LLQMFAIHS230 LTREAQAKA 0.600 728 7 LQMFAIHSL 0 .041 687 120 AMAFDRYVAI] 0.600 1[ 729 4 H~ ACLLQMFAI 10.0411 688 i57 FI[LMVH][ 0.600 Jr 730 ] 2 FDACLLQMF 0.003 689 216 LISFSY 0.540 731 3 D LQMFA 0001 6903 _ I LLIL[ 0.450 732 1 QFDACLLQM 0.90 01 9[80 Jr________ 0.450 733 able X:101P3A11-V1-A3-10mers ITLPRVTKIGV 736 Start [Subseguence Score Seq. ID Num IPLPViLAi[ 737 158 LMAPLPVFIK 4 os.0001 693 jSMPKMLAIFW 0 738 259 IGLSMVHRFSK 180.0001 69410J1CLL IFAXHSJ1 0.360 6 9739 74 ILISTSSMPK 695 1 [ 12 JPL 0.360 740 117 VLLAMAFDRYU18.000 696 AIFWFNSTIIf0.300[ 741 288 VLNPIVYGVK 13 .500 697 2 HVCAVFIFYVj 0.270 1 742 19 II QLPGLEEAQFf9.00j[ 698 95 IFACLLQIJ[ .7 743 261 SMVHRFSKRRII 9.000 1[ 699 28 LYLP~PVN[ 0.270 744~ 214 SLLISFSYLL[ 1 7 [_19jVVYGLIVIIS 745 22 GLEEAQFWLA 8.100 701 L] 746 224 ILKTVLGLTR 8.000 702 292TIVYGVY... 0.225 747 222 ILLILKTVLGL[ 5.4001J 703 1 182 IrCLHQDVMKLA i 0.225 1r 748 137 JjTVLTLPRVTKIL 4.50011L 704 j 1228 jVLGLTREAQA j0.200 J[ 9 187 VMKLACDDIR 4.000 705 29 WLAFPLCSLYI 4.000 706 ILIVIISAIGL1 751 283 LLVPPVLNPI 3.038 707 MLSGIDILIS 0.180 752 249 ]AVFIFYVPPI 2.700 708 2IYLLV!J[ 0.180 753 112 GMESTVLLAM[ 2.70011 709 133 IPC LTAII 1 7 251 FIFYVPFIGL 2.700 1 211 GLDSLLISFS 0.180 755 6 CMSIILI r2.700 1711] __IQ~~I_____ 67 j CMsG.IDIL 711 295 JrGVKTKEIQH0.8 756 116 11[TVLLAKAFDRJ[f 1. 8 0[ 712 ]38 JrYLIALG 0T.150I 757 42 VLNLIII 1.800 11 712 42JVLNL~ii1[1.00If 713 J 98JrNVVYGLIVII] I0.135 758 : 57 ISLHEPMYIFL L1.800 1 714 ILIGLPGLEEI 01 H '50 138 VLTLPRVTKI][ 1.800 f 715 1202 GLIVIISAIG 760 41 AVLGNLTIIY 1.800 716 215 ILLISFSYLLIJr 1.800 717 167 KQLPFCRSNII 762 83 K4LAIFWFNS 1.620 718 217 jISFSYLLILK F1.500 719 176 IILSHSYCLHQ 0.120 764 65 FLCMLSIDI 1.200 720 _ 7 101 LLQIFAIHSL 0.900 72 H 157 ALMAPLPVFI 0.900 72276 SGESTVLj0.900[ 723 3 S IJAL 767 84 R MLAIFWFNSTI 03.900 I724FAT 0.090 768 164 761 able X:1O1P3A11-V1-A3-10mers [able X.:lOlP3AI1-V2-k3-lomers Start Subsequence Score Seq. ID Num [Start, Subsequence Score Seq ID. Num 121 MAFDRYVAIC 0.090 770 13 VTLRCPSSWP 812 206 IISAIGLDSL 0.090 771 1 ]I 0 81 MPKMLAIFWF772 25 ICWFLLCST 0.001 814 276 VILANIYLLV 0.090 773 18 PSSWPISICW 0.000 815 241 GTCVSHVCAV 0.090 774 [0 ASGVTLRCPS 816 30 LAFPLCSLYLL 0.090 775 3 ____ [0.000 817 260 LSMVHRFSKR j0.090~f 776 2 WFLLCSTQLS 000 IB 24 jCAVFIFYVPF[ 0.090 777___ 11]SGVTLRCPSS10.0 819 26 AQFWLAFPLC 0.09 778_______ . 00 82 25vppviLiPXVY 0.080 779 ]AGTRPj0 -01 8 231 LTEA__KA 0.075 ][ 780 156 _AALMAPLPVF 0.068 781 151 AVVRGAALMA 0.060 782 _______X: ____________________ 243 783 t Subsequence Score Seq ID. Numi 162 LPVFIKQLPF 0.060 784 [ ILLQMFAIHSL]E0o90 822 143 _RVTKIGVAAV 0.060 7851 [ii[RvrKIv~vf .06 ][ 785 j 6 ]CLLQMFAIHS J0. 36011 823 1 MMVDPNGNES 0.00 7 QMFAIHSLSG 0.20 824 118 LLAMAFDRYV 0.20605 245[ SHVCAVFIFY 0.054 788 ACLLQMFAIH 0.0091 826 181 YCLHQDVMKL 0.054 789 DACLLQMFAI 827 93 TTIQFDACLL 0.045 790FDACLL F 0.0031 828 304 RILRLFHVAT 0.045 791 3 LQMFAIHSLS 0.003 829 [ i TIIYIVRTEHI 0.04 792 ] 3 JFDACLLQMFA 0 .0 00 83 0 107jIMFAIHSLSGM 0.000 831 able X:101P3A11-V2-A3-10mers Start Subsequence Score Seq ID. Num XI:101P3A11-V1.A3-9mers 14 TLRCPSSWPI 1.800 793 Ience Score Seq. ID Num] AVLAS TR 1.800 [20794 GLTREAQAK 1.200 832 2 SLYLIAVLAS 1.200 7957 LISTSSMPK 0800 833 28 FLLCSTQLSM 0.600 796 181 VLASGVTLRC 0.6001 797 3 126 J[YVAICHPLR J0.400~ 835 4 YLIAVLASGV 0.300 798 218 SFSYLLILK 0.400 836 19 3SSWPISICWF 799 VTLPRVTK 0.400 837 12 GVTLRCPSSW .00 800 1FD 0.6 83 22 PISICWFLLC 0.06 0L M 16 RCPSSWPISI 0.036 802 ] 0. 840__ 29 LLCSTQLSME 0.030 803 FIKLPFCR 841 21 WPISICWFLL 80 262 MVHRFSRR 0.200 842 24 SICWFLLCST .1 805 45 NLTIIYIVR 0.160 843 [63 IAVLASGVL 0.009jf806 26 [2~..[LSMVHRFSK 0.120h 8 44 17 | CPSSWPISIC 0.005 807 SM26 FSKR 0.120 84 26 CWFLLCSTQL]0.003 0 [1 846 5 |LIAVLASGVT 0.003 809 13 TLPR 0.080 847 20 |SWPISICWFL10.003 810 0 848 2311 ISI C 0.003 811 CW1FLLC0 84 165 able XI:101P3A11-V1-A3-9mers able XI:1O1P3A11-V1-A3-9mers Start Subsequence Score Seq. ID Numi Seq. ID um 143 RVTKIGVAA 0.060 850 216 LISFSYLLI00 895 198 ]NVVYGLIVI 0.060 851 42 VLGNLTIIY 0.008 896 204 IVIISAIGL 0.060 852 288]1 VLNPIVYGV 0.008 897 289 LNPIVYGVK 0.040 853 66 JjMLSGIDI0.008 254 YVPFIGLSM 0.040 854 225][ LKTvLGLTR 0.008 899 12 JATYFILIGL 0.040 855 68 MLSGIDILI 0.008 900 199 VVYGLIVII 0.040 856 277 ILANIYLLV 0.008 152 VVRGAALMA 0.040 857 209 AIGLDSLLI 0.008 902 249 0 120 AMAFDRYVA 0.008 903 246 HVCAVFIFY 0.040 859 280 NIYLLVPPV 0.008 904 22 GLEEAQFWL 0.036 860 57 0 905 26 AWPL 0.036 861 48 jIjVTEH 0.008 906 302 RQRILRLFH 0.036 862 157 ALMAPLPVF 0 9 291 PIVYGVKTK 0.030 863 188 MKLACDDIR 0.006 908 297 KTKEIRQRI 0.030 864 294 YGVKTKEIR 0.006 909 115 STVLLAMAF 0.030 865 275 PVILANIYL 0 006 910 151 AVVRGAALM 0.030 866 6 MSII .0 1 41 GNLTI 0.030 91 241 GTCVSHVCA 0.030 868 1 IYLLVPPVL 112 IfGMESTVLLA 0.024 869 [221 YLLILKTVL 0.006 14 1 189 KLACDDIRV 0.024 870 F[1 ][ LPGL 0.006 915 211 GLDSLLISF 0.024 871 [24 If FSL1 0.00 916 307 IRLFHVATHA 0.024 872 100 ]LQFAIH 0.006 917 243 CVSHVCAVF 0.020 873 127 VAICHPLRH 00I 51 IfIVRTEHSLH 0.020 874 32 If LCSLhIJ0.006IZ919 284 LVPPVLNPI 0.020 875 [7 AVFIFYI10.006 202 GLIVIISAI 0.018 876 4 IAVLGNLTI 0.006 9 1251 RYVAICHPL ] .E01 877 F ]1 AALMAPLPV 0.006 922 304 _RILRLFHVA .018 878 [0 ][RHSL 0.006 2 136 ATVLTLPRV 0.o015 879 38 YIAVLGNL-o.006 924 139 LTLPRVTKI 0.015 880 SrSSMPKML 0.005 925 TTIQFDACL 0.015 881 226 0 05 1:26 276 VILANIYLL0.012 882 [-57I SMPK I0.004 927 223 LILKTVLGL 0.012 883 29 WLAFPLCSL 0.004 92 215 LLISFSYLL 0.012 884 ] 109 If 0.004L929 175 NILSHSYCL 0.012 885 ]LAFPLCSY 93 25 GVKTKEIRQ 0.012 886 ] 87IfVMKCDDI 0.004M 931 238I KAFGTCVSH 0.012 887 231 LTREAQAKA 0.010 888A11--A-mers 144 VTKIGVAAV 0.010 889 Start Subsequence Score S IumI 99 ACLLOIFAI 0.009 890 7 VLASGVTLR 0.080 932 102 LQIFAIHSL 0.009 891 6 AVLASGVTL 0.030 933 163 PVFIKOLPF 0.008 892 12 VTLRCPSSW 0.015 934 252 IFYVPFIGL 0.008 893 28 LLCSTQLSM 0.00 9 18211 CLHQDVMKL 0.008 894008 166 Table XI:101P3A11-V2-A11-9mers able XII:lO1P3Al1-Vl-Al1-lomers Start|[Subsequence Score Seq ID. NumJ [tart Subsequence Score Seq. ID Num] n GVTLRCPSS 10.006 937 ] VIMPIVYGVK 0.400 975 20 WPISICWFL 0.006 938 ] 180 SYCLHQDVMKJ0.400 976 16 [CPSSWPISI_ o.004 939 125 RYVAICHPLR 0.360 977 4 LIAVLASGV 0.0041~ 940 j r164IVFIKQLPFCR 0.180 978 26 WFLLCSTOL 0.003 941 2 21 PISICWFLL 0.O0011 942 290NPIVYGVKTK.150 980 2 LYLIAVLAS 0.001[ 943 295 GVKTKEIRQR 0.120 981 23 SICWFLLCS o.001[ 944 196 RVNVVYGLIV 0.1 82 18i SSWPISIW 0]I.0o01] 945 217 IF 0 27 _f FLLCSTQLS 0.0011[ 946 187 VMKLACDDIR 0.080 15 RCPSSWPIS 0.001 947 293 VYGVKTKEIR 0.080[985 3 IYLIAVLASG 10.001 948 44 GNLTIIYIVR 0.072 986 13I1 TLRCPSSWP .000 949 246 I IFYV 0.[ 987 .147 ILCPSSWPI H0.0001 950 ]151 jjjjGALM 0.060 988= 8 1 LASGVTLRC 0.000 951 148 GVAAVVRGAA 0.060 989 24 ICWFLLCS .000 952 __143 RVTKIGVAAV 990 5 IAVLASGVT O.000 953261 SMVHRFSKRR 29 If000CSTQLSME 0 954 4 AVLGNLTIIY 0 19 Ij SWPISICWF 0.000 955 302 R RILRLFHV 22 ISICWFLLC 0.000 956 ]26C 25 IfCWFLLCSTQ 0.000 957 J 249 IAVFIFYVPFI 0.040 995 10 OJ[ SGVTLRCPS 0.000 958 1 229 JLGLTREAQAK .030 996 ASG LRCP 0.000 959 241 I 0 ~T PssiISIC 0001---~ - 960 __________________________ I 98 f~vYGLIVII 110.,_03011 __999 able XI:101P3A11-V3-A11-9mers 1 I KOLPFCRSNI JO0027Li000 StartiSubsequence Score Seq ID. Num 134 I RHAVLTPR 1001 7 LQMFAIHSL 0.012 961 J 0 4 [ACLLQMFAI 0.009 9 9 )ACLLQIIIo7024 1003 5 CLLQMFAIH .006 22 GLEEAFWLA 634 1004 1 QFDACL 0.004 964 .020 1005 3 DACLLMFA 0.001 965 ] ____ 0.020 8 ][ 9MFAIHSLII 0.001 966 292[1YKE 0020 1007 6 LLMFAIHS 0.001 967 28 IYJ 020 9 MFAIHSLSG 0.000 968 243 CVSHVCAVFI 0.020 1009 2 FDACLLQMF 0 000o 969 21I7 2~~~~~~~~ ]~LF 000 99 j21IfFIFYVPFIGL 0.06 1010~~jy F9 JTTIQFDACLL 0.0151 1011 Table XII:1O1P3A11-V-A11-10mers 186 j DVMKLACDD 10.012 1012 Start Subsequence Score Seq. ID Num [22TI1LLILK L 10.0121 1 259 GLSMVHRFSK 3.600 970230IGLTREAQAKA 0.012 1014 [17ITVLTLPRVTK 3.000 971 155 IfGAALMAPLPV 0.012[ 1015 116 TVLLAMAFDR 1.800 972 [14 SLLISFSYLL 012 1016 158 LMAPLPVFIK 1.200 973253 FYVPFIGLSM 1017 [ I ILISTSSMPK JI __ 974 2 38 IfKAFGTCVSH ~10.010 118 276 VILANIYLLV 9_70.0 0 167 able XII:101P3A11-V1-A11-10mers Table XI1OPA11-V-A11-lomers S eStartn Score Seq. ID Num Start Subsequence Score Seq. ID Num] LLISFSYLLI .012 1020 299 KEIRQRILRL 0.005'1 1065 ]GLPGLEEAQF0.012 1021 231 LTREAQAKAF 0.005 1066 203 LIVIISAIGL 0.012 1022 226 KTVLGLTREA1005 1067 67 CLGDL 1.021 12 305 ]L IR L FHATH E. 04 1 1068 92 ISTTIQFDACL 0.010 1024 3101 ]LLIAIHSLI. 0.04L,_30 144 IVTKIGVAAVV 0O.010j 1025 30 LAFPLCSLYL 0.008 1026 able XII:1OPA11-W-AII-lomers 80 SMPKMLAIFW 0.008 1027 StartSubsequence Score Se ID.Num 280 NIYLLVPPVL 0.008 1028 7 IAVLASGVR 0.600p 1070 63 YIFLCMLSGI . 1029 ] 12 iGVLRCPSSI, 1071 57 SLHEPMYIFL 0.008 1030 16 RCPSSWPISI 1072 119 ILAMAFDRYVA 0.008 1031 28 F TQLSM 1073 199 VVYGLIVIIS 0.008 1032 F 21 WPISICWFL 0.009 1074 216 LISFSYLLIL 0.008 1033 14 TLRCPSSWPI 1075 42 VLGNLTIIYI 0.008 1034 0.006 1076 255 VPFIGLSMVH .00 1035 I IAVLAS 0.003 1077 157 ALMAPLPVFI 0.008 1036 2 [SLYLIAVAS 1 200 VYGLIVIISA 1 VTLRCPSSWP 0.002 1079 39]iLIAVLGNLTI 1O.008 1038 VLASGVTLRC .01080= 140 TLPRVTKIGV [0.008 1039 1 3 ) 298 TKEIRQRILR .00 1040 26 ICWFLLCSTQLI0.000 1082 65 FLCMLSGIDI 0.008 1041 SSWPISICWF I[- L103 86 AIFWFNSTrI 0.008 1042 IICWFLLCSTQ 256 IPFIGLSMVHR 0.006 1044 J24 IfSICWFLLCSTI 0.0 1086 3 145 TKIGVAAVVR 0.006 1045 29 LLCSTQLSME 0T01 1087 50_ 006 1046 2 WIIWL~.O~ 18 so YIVRTESLH ____11 106ISPR p 18-, 162 LPVFIKQLPF 0.006 1047 ___ 0000 1089 47 TIIYIRE 0.006 1048 F27-jWLCTL 0.000 19 265 RFSKRRDSPL 0 .0 06 1049 1CSWII 1.001 19 81 MPKMLAIFWF 0.0061 1050R2 1.0] 1927 37 LYLIAVLGNL 1051 220 SYLLILK'rVLJIO.006[ 0q2 180.00011 19 275 PVX .AIYLL110.oo 011 1053 11 [SGVTLRCPSS 10.0001 1095 275 NILSHSYCLH 0.006 1_00 181 YCLHODVMKL0.006 1055 1 ASGVTLRCPS0 0 1097 283 LLVPPVLNPI 0006 1056 9 0.000 1098 32 FPLCSLYLIA 10.016j 1057 7 - PVLNPIVYGV IIOL0 058[ XII:1OPA11-V3-A11-l0mera 235 JAQAKAFGTCV 0.006 ] ;equenceJSce 274 LPVILANIYL .06IF6 ~~LvIAIYl0. 0061 1060 ]1 I QFDACLLQM -0.0241 10.99 3 49 I AAYIVRTEHSL 0.0061 1061L IHSL 0.004 1100 117 ______ 0.006 1062IS1 ACLLMFA 208 1 0.0061 1063 IQFDACLLQMF 0 112) K4LAIFWFNq T0.005a 1064 X 1MFAPHSLSGM 0 -V 1103 168 able XII:101P3A11-V3-A11-10mers able XII:1O1P3A11-V1-A24-4mers Start Subseguence S Seq ID. Num ISubsequence Se 4 DACLLQMFAI O.002 1104 12 1 ATYFILIGL 15.6001] 1145 QMFAIHSLSG 0. [ 8705 IFWFNSTTI 5.000 1146 CLLQMFAIHS 0.001 1106 F96 QFDACLLQI 5.000 1147 8-77 LOMAIH|SS 0.001 1107 16 1 LPFCRSNIL 4.800 Jf1148 FF-3 LDACLLQMFA 10. 0001 1108 126 11 AQFWLAFPL 4 . 11i1149 1821 __________ [.400[ 1150 ] Table XIII:101P3A11-V1-A24-9mers RVNVVYGLJ 1151 Start Subse uence Score Seq. ID Num 27 .032 [ 152 F125 RYVAICHPL 840.00011 ESSATYFIL 1153 ___ IYLVPPVL 1420.01 1110 1 00 EIRQRILRL ]4 .000] 1154 293 VYGVKTKEI 5[s.o5. 000] 11 1 FSKRRDSP [4000 15 AFPLCSLYL H730.000 1112 WLAFPLCSL i 4.000 [ 1156 180 25LHV 000 [io] YCHQV ]25oo f 1113 ]10 LSGMESTVL J[400 1157 252 IFYVPFIGL ] 24.000 14 ISFSYLLIL 4 0 1158 89 WFNSTTIQF .L 4.000 1159 220 1 S STSSMPK. 4.000 154 RGAALMAPL 1117 STVLLAMAF 1161 [ 2 j MYIFLCMLS 9.000 1118 LVPPVLNPI ][ 3.024 1162 253 FYVPFIGLS 9.00 1119 GNESSATYF Jr .00 1163 38 YLIAVLGNL 8.400 1120AMAPLPVF 1164 250 VFIFYVPFI I 7rGLSMVHRF 64_ IFLCMLSGI 7.500 1122 SMPKNLAIF 3 1166 9 IYIVRTEHS 07.500 J 1123 CVSHVCAVF 2 1167 37 LYLIAVLGN 7.500 Jr 1124 SLHEPMYIF Jr 2400.168 r22 GLEEAQFWL 7.200 1125 ][GLDSLLISF 1169 214 SLLISFSYL 7.200 16 202 GLIVIISAI 2 1170 SGMESTVLL 7.200 1127 AVFIFYVPF 2.000 1171 1281SAIGLDSLL 1.01 1128 J2 JrLPGLEEAQF 2.000 17 N 3S CSLYLIAVL 7.200 1129 1139 LTLPRVrKI J1.980 1 173 22111 YLLILKTVL 117.200 1130 19 SSMPIGIAI 1.800 1174 200 VYGLIVIISj 7.000 1131 AVLGNLTIIJ1 1175 150 AAVVRGAAL 1 60 [ 1132 FPLCSLYLI ][ 1.500 31176 67 CMLSGIDIL JF6.000 1133 LCMLSGIDI 1 1177 11311 HPLRHATVL 6.000 1134 ACLLQIFAI 1178 15 | FILIGLPGL 6.000 1135 IAVLGNLTI 1179 175 NILSHSYCL 6.000 1136 [19871 NVVYGLIVI 1.500 1180 193 I TTIQFDACL 6.000 1137 j HSLHEPMYI 1.500 1181. 215[ LLISFSYLL 11 6,00[ 1138 [ QLPFCRSNI 1.500 1182 102 LQIFAIHSL 6.000 1139 [2_ILGNLTIIYI 1.500 1183 50 4YIVRTEHSL 6,000 1140 1 lMAPLPVFI I 1.4 1184 19411 TIQFDACLL 1[~~~ 1141 [ L7iI MLSGIDILI If1.400 If 1185 276JF VILANIYLL 60 1142 [ EPMYIFLCM 1.260 1186 204 _ IVIISAIGL 16.000 I 1143 SSATYFILI 1187 2231aLILKTVLGL be X I : 044 13 A -RVAIA2 4 1188 192 VVYGLIVII 1189 169 able XIII:101P3A11-V1-A2 4-9mers able XIII: 10123A11-V2-A24-9mers Start Subsequence Score jjSeq. ID NumJ Start subsequencel Score Seg ID. Num 270 1.SPLPVIL ]9i.152 1190 25 CWFLLCSTQ 10.012]1 1232 254 YVPFIGLS [ 1.050 1191 9 1[ ASGVTLRCp F 216 LISFSYLLI IL1.000 1192 J [29 j LCSTQLSME 0.0101 1234 244 ]VSHVCAVFI ]1.000 1193 13 TLRCPSSWP 0 ojo] 1235 187 VMKLACDDIJl 1.000 1194 [SGVTL I ] 1236 209 AIGLDSLLI 1.000 1195 [ 00 195 IRVNVVYGL 0.840 1196 164 | VFIKQLPFC 0.750 3[197 _____ XIII:1OPAI1-V-A24-9mers 151 AVVRGAALM 0.750 1 Subseauence Score Se ID. 73 DILIST:: = 0.750 _1199 7 LQMFAIHSL 6.000 1238 105 FAIHSLSGM 0.750 1200 1 lFDACLLOM 2.500 1239 58 LHEPMYIFL 0.720 1201 4 JLA . 1240 13 TYFILIGLP 0.600 1202 ] j [ LQMF0.288 1241 298 TKEIRORIL [ 0.600 1203 6 I4MAIHSi010 1242 1275 ] PVILANIYL J(0.600 7 1204 ] fMFAHSLS 1243 161 PLPVFIKQL 1 0.600 1205 DACLLQM4FA -120 1244 27 QFWLAFPLC 0.600 1206 G05 1245 76 1[ISTSSMPKM 0 1207 ] ISf1 018[: 1246 83 i KMLAIPWFN[ 0.504 1208 LRLLIFWN 1 '108 able XIV:1O1P3A11-V1-A24-lomers able XIII: 1O1P3A11-V2-A24-9mers S Start Subsequence|score|Seq ID. NumS 30.000YIALGL 20020149 26 WFLLCSTQL A30.00 1209 22 IYLIKT u9.0001 24 1 20 WPISICWFL 8.400 1210[49 IYIVRTEHSL 30 1249 2 LYLIAVLAS 7.500 1211 J 253-J[ FYVPFIGLSM 00 6 AVLASGVTL 6.0001 1212 2 RF4.00][ 25 19 SWPISICWF 3_0 1213 1 16 1.000 1214L 3.00 15 16] CPSSWPISI 11ioo IE0000 124 96 f IQFDACLIQIFjF] 1253 28 LLCSTQLSM 0.500 12 297]KTKEIRQRIL71 9.600 1254 21 ] PISICWFLL 0.400 1216 31 [ .50 ] 1255 L15 LRCPSSWPIS JL0.300 1217 IYLLVPPV71 1256 10 IfSGVTLRCPS 0 . 18 0 ][1218 1 LPFCRSNILI 1257 22 ISICWFLLC 110.180]1 1219 213 DSLLISFSY 1 7.200 1258 27 FLLCSTQLS o.18o[ 1220 16071 APLPVFIKQL 1259 i SSWPISIC 16 1221 2 EAQFWLAFPLI 1260 IAVLASGVT 0.1501 1222 VYGLIVIISA 1261 12 VTLRCPSSW 0.150 31223 YCLHQDVMKL 6.600 1262 a LASGVTLRC 0.1 1224 LPVI IYL 6.000 12 1263 1 SLYLIAVLA F0.140 1225 60 ]EPMYIFLCML[ 6.000 =1264 4 LIAVLASGV 0.120 1226 20 [LIVIISAIGL 6.000 1265 14 LRCPSSWPI 10.120 1227 93 TTIQFDACLL 1266 24 ICWFLLCST 0.120]1 1228 1 _ ILLOIFIHSL 6.000 1267 23 SICWFLLCSF .100 1 [28 1IWAFPLCSI 6.000 1268 11 j QVLRCPSS 0.100 120 j166 1 LCMLSGIDIL IL 6.-0 00 1 12 6 9 _ 3 Y-12331231 _ 170 able XIV:101P3A11-V1-A24-10mers : able XIV:l01P3A11-V1.A24-10mers Startsubseguence Score ISeq. ID Num Subsequenc Score [Seq. ID Numj 214 SLLISFSYLL 6.000 1270 1 FI.T]r.DVMKLACD.]r 1,00 1315 14 SNILSHSYCL71IR PT ~ 60001 17,1* 1 112 1FYVAIC.H ~R1 I. 00 3.316 1 222 T]LLILKTVLGL] 60 00 1 1272 [7fONSSATYFI J[1.500 Lf 1317, [ 9 [DIRVN~VVYGLJ 5.600 Jj 1273 ] [25]LLISFSYLLI J[ .50 1318 11]SATYFILIGLE:ES.6 J 1274 J 208]I SAIGLDSLLI][_1.500 11_1319 280 NIYLLVPPVL[ 5.600 1275 299 KEIRQRILRL 1.200 1 1320 251 FIFYVPFIGL 4.800 1276 F ESSATYFILIJ1 1.200 1321 I LCSLYLIAVL[ 4.800 1277 IQPDACLLQI 1 1322 57 SLHEPMYIFLI[ 4.800 1278 1 IvLTLPRVTKI 1.100 1323 30 LAFPLCSLYL 4.800 1279 jIVYGVKTKEI 1.100 1324 ]ISAIGLDSLL 4.800 1280 J GMESTvLLAMf 1.050 1325 210 IGLDSLLISF 4.320 ] 1281 [ 242 IITCVSHVCAVF] 4.200 [ 1282 1 42 VLGNLTIIYIII 1.000 jf 1327 206 IISAIGLDSLI 4.000 | 1283_]7[ 98 [DACLLQIFAI 1328 149 VAAVVRGAAL AVFIFYVPFI 1.000 1329 109 SLSGMESTVL 4.000 1285 1 7 ITSSMPKMLAIJ[ 1.000 1330 216 LISFSYLLIL 400 1286 1 F4 VHCVI13 76 ISTSSMPKML 4.000 1288 ][AVwNsTI][ 1.00] 1 110 LSGMESTVLL 4.000 1[ 1289 IYIFLCMLSGI[ 1334 79 SSMPKMLAIFI 3.600 [ 1290 1335 6 NGNESSATYF 3.60011 1291 1 269 RRDSPLPVIL [ 0.960 1336 1 167 IKQLPFCRSNI 3.600 1292 3 0.750 1337 28 LPVNI 3.024 1293 MILMSI13 248 CAVFIFYVPF 3.000 1294 PGLEEAQFWLI 020 1338 ] 162 ILPVFIKQLPF[ 3.000 1295 I AFGTCVSI 7 1340 3 56 IHSLHEPMYIFII 3.000 1296 13]1TYFILIGLP;f 0.700 1341 119 GLPGLEEAQF 3.000 ][ 1[ SFSYLLILKT 1342 156 j AALMAPLPVFJ 3.000 1298 130 ][CHPLRHATVL)[0.600 1343 j 300 fEIRQRILRLF 2.800 1299 PVILANIYLL 0 1344 272 SPLPVILANI 2.520 1300 1AIC 1345 104 IFAIHSLSGM 2.500 1301 L 7 5 LISTSSMPKM[os 1346 114 ESTVLLAMAF 2.400 13 0 2 231 LTREAQAKAF 2.400 1303 Fble XIV:1O1P3A11-V2-A24-lom 67 CMLSGIDILII 2.100 1304Subse enceScore se ID. New 201 JIYGLIVIISAI 2.100 1 1305 20 SWPISICWFL 1347 257 FIGLSMVHRF 2.000 1306 ] H 1348 81 MPMLAIFWF 2.000 1307 6 ][IAVLASGVTL 349 88 ]FWFNSTrIQFjf 2.000 JI 1308 ]26 1][1CWFLLCSTQL 11.001 15 244 [ VSHVCAVFIFI 2.000 1309 16 RCPSs 1351 i- NVVYGLIVII 1.800 1310 19 SSWPISICWF1 1352 53 jRTEHSLHiEPMJ 1.0 1311 J3 ]ILYLIAVLASGJI1. 050I 1353 157 ALMAPLPVFI1 1.800 1312 14 TLRCPSSWPI]1.000 1354 YGLIVIj 1.500 1 1313 275 WFLLCSTQI 0. 900 1355 40I[IAV| GSNLTISTI 1.500I50 1314 O131 ______ 1 1FLCT LS i Ii 171 able XIV:101P3A11-V2-A24-10mers [Table XV:1O1P3A11-V1-B7-9mers Start Subsequence Score Seg ID. Newly S cor Seq. ID Num 1 CSLYLIAVLA 0.210 1357 208 SAIGLDSLL 12.0001 1395 1 4 0YLIAVLASGV 80 1358 Sl _ __ .0 1396 23 ISICWFLLCS 0.150 1359 1 [ ATYFILIGL 1397 11 SGVTLRCPSS 10.150 1360 3 PLCSLYLI 8.0001 1398 SIWLLS .12 1363 18 CSWPISC1 0.140 13651 41 AVLGNLTII 6.000 1399 12 GVTLRCPS 0.120 1362 29 WLAFPLCSL 6.000 1400 24 ICWLLCST 12 0 1363 J1 254T YVPFIGLSM 15.000 1 1401 J 5 ~0.10016 2 SLYIAViLASI 00 1364 JF15 VVRGAA.MA I15.000 1 1402 1 1 [CPSSWPISIC I M0100 136.5 J1][FILIGOjPGL A 4

.

000 1 1403 12IGVTLRCPSSW 0.100 13 6 s YIVRTEHSL 400 1404 ~ LIAVLASGVT 0j.1001 1367 102 LQIFAIHSL 4. 000_ 1405 13 VTLRCPSSWP 0.015 1368 j 2761 VILANIYLL [00 1406 7 AVLASGVTLR .05 36 p? I 1369 110E LSGMESTVL 11.01 1407 _ 8_PSSWPISICW FO._014- 1370 94 TIQFDACLL 000 1408 5 I[LRCP ~ 10.012 1371 93[TIQFDACL 140 25 1372 IWLCTVPFIGLSMV F40.21410 22 11PISICWFLLC 703.0121122111F 10 1411 29 LLCSTQLSME 0.010 1374j7

T

iI MPKL 1412 9 LASGVTLRCP .010 1375 LIAVL 1413 ~ [CLHQDVMKL 4.00 =_ 1414 able XIV:101P3A11-V3-A24-10mer2s 14.000 1415 Start Subsequence Score Seq ID. Num VPPVLNPIV1 1416 2 QFDACLLQMF|14.4001 1376 1 ISFSYLLIL 4 1417 LLQ1FAIHSL377 ISAIGLDSL 0 1418 10 MFAIHSLSGM 182.500 1 6 1 CMLSGIDIL 4 1419 ] 4 A 1379 ]381YLIAVLGNL 14.0001 1420 J [ 1 IQFDACLLQMIO.600 1 1380 792661 SKR1421 8 ________SL 1__ 138 22 ~F LILKTVLr.L 111107 1423 6 CLLQMFAIHS 0.150 1382 ]_ _ _ _ _ _ S ACLLMFAIH 0.018 1383 ] 115411 RGAALMAPLJ14o 1 1424 16 3 [ LLQMFAI 0.0012 1384 6 SLLISFSYL 4.000111425 131 QMFAIHSLSG 8.000 1385 9 ESSATYFIL F_ 1i26 60 EPMYIFLCM60.000 1031 1427 XV:TO1P3Aa1-Vb-B7-9mers X: [PA 11- - 1428 Start Subsequence Score rSe. ID Nuu 4 mI 2 1429 1697 LPSNIL 1 1 1386 ) 198 LNVVYGLIVI j4~[ 1430 11311 _PRAVL8.0 1387 ] 201NPIVYGVKT 2.000 111 SGMESTVLL 12.0000139 60 1 EPMYIFLCN1 1388 1] 1 196 ARVNVVYGLI 1.0003143 F4 LPRVTKIGV 4000 1389 ] 19[VVYGLIVI 201 43 00 EIRRILRL40.0 1390 24 LVPPVLNPI .0001 1434 10 AAVRGAAL 1136.00012 1391 1 AALMAPLPV 6.000 | 1435 204 IVIISAIGL YPI 1392 1.800 1436 151If AVVRGAALM 115.O 1393 V VGLDSLLI 1.200 1437 2 1 AQFWLAFPL 112.000A 3 99 ACLLIFAI 1.200 1438 1106 LCMLSGT |. 1439 94|1IQDCL72.00 10 Table XV:101P3A11-V1-B7-9mers -able XV:lO1P3A11-VI-B7-9mera Start Subsequence Score Seq. ID Num [ Score Se ID NumI 7~91 SSMPKNLAI Jf1.2001 1440 j [1_3 5]J AQAKAFGTC J[0. 3 0 0 145 22 GLEEAQFWL 1.200 1441 121 MAFDRYVAI 1.200 1442 able XV:l01P3A11-V2-B7-9mers 40f IAVLGNLTI 3 StartSub14431.20 Score Se ID. Num 31 JAFPLCSLYL 1.200 1444 ] l20][ 80.0001 1486 76_ ISTSSMPKM 1.000OJ 1445 6 AVAGT 0 OI 1487 J 73 DILISTSSM 1.000_1446_1____ J 8.000 1488 305 0ILRLFHVAT [.00 1447 28 J[ SLSM11.00011 1489 231 LTREAQAKA 1.000 1448 ] [ 0.400 1490 252 IFYVPFIG .600 1449 26 WFLLCSTQL 0.001J 1491 236 QAKAFGTCV 0.600 1450 8 LASGVTLRC 0.300 1492 297 KTKEIRQRI 0.600 1451 [AVLASGVT [.30[ 1493 116811 QLPFCRSNI 0[.600J[ 1452 4 LIAVLASGV 0.200 1494 136 ATVLTLPRV 0.600 1453 [3 TLRCPSSWP 1495 (16011 APLPVFIKQ 10.600[ 1454 22 ISICWFLLC 10[ 1496 143 RVTKIGVAA 0.500 1455 1 SLYLIAVLA 1497 L148 If GVAAVVRGA 10.5001 1456 11 JjGVTLRCPSS 100Ti[Z 1 49 8 227 TVLGLTREA 0.500 1457 24 If ICWFL 0.100 1499 137 TVLTLPRVT 0.5001 1458 4 1S00 51 IVRTEHSLH 0.500 1459 ASGVTLRCP 0.03 149 VAAVVRGAA 0.450 1460 10 SGVTLRCPS 0.0301 1502 128 AICHPLRA 0.± OI 1461 27 FLLCSTQLS 0.020 1503 120 AMAFDRYVA 0.450 1462 18 SSWPISICW 0.020 1504 272 SPLPVILAN 0.400 1463 12 VTLRCPSSW 0.020 1505 216 LISFSYLLI 0.400 1464 23 1 SICWFLLCS 0.020 1506 274 LPVILANIY 0.400 1465 _1507 56 HSLHEP4YI J.400 1466 sic 1508 125 RYVAICHPL 0.400 1467 VLASGVTLR 1509 195 IRVNVVYGL 0.4001 1468 29 LCSTQLSME 1510 270 RDSPLPVIL 0.400 1469 YLIAVLASG 0.010 1511 3 LGNLTIIYI 0.400 1470 SWPISICWF 0.002 1512 158 LMAPLPV 2 0.400 1472 002 1513 81T] rIPKr..AIFW ][3.] 472 ] [ ][CWFLLCSTQ .01I 11 187 VMKLACDDI 0.400 1473 22 GLIVIIS 0.400 47 4 [T eXV:11P3A-V3-B79mers 281 IYLLVPPVL 0.400 1475 Start Subsequence Score Seq ID. Num) 161 PLPVFIKQL 170.400 476 7 LQMFAIHSL 1 0 1ss 68 ]IMLSGIDILI 0.400] 1477 ]4 IfACLLQMFAI 1i. 20011 1516 133 |_RHATVLTL 0.400 1478 3 DACLLQMFA 0.300 1517 139 I LTLPRVTKI 0.400 1479 1 QFDACLLQM 0.030 ][ 1518 61 PMYIFLCML 0.400 1480 QMFAIHSLS 0.020 1519 [20 IILPGLEEAQF If0.400 i 141 6 fLLQMFAIH~S 15T~ii 2 0 244 VSHVCAVFI 10.4001 1482 CLLQMFA 0.011 1521 1 SSATYFILI 1483 2 1 FDACLLQMF0.4 Start ubseque173nce ScoreH|LSeq. IDNum lable XVI:101P3A11-V1-B7--mers Sable XVI:101P3A1-V1-b7-smers StartSubsequence Score Se. ID Num Start SbeuneScorelSeq. ID NumJ 302 IRQRILRLFHV F2.0007 1568 60 EPMYIFLCML 240.000 1524 151[AVVRGAALMA 1.500 1569 160 APLPVFIKQL 240.000 1525 19 LAMAFDRYVA f 1.350 1570 274 LPVILANIYL 80.00 1526 1 AMAFDRYVA 1.200 1571 194 DIRVNVVYGL 40.000 1527 IAVLGNL 1572 141 LPRVTKIGVAII2O.oo] 1528 86 AIFWFNSTT00 1573 149 ifVAAVVRGAAL 1 12. 0 1529 98 DACLLQIFAI 1.200 1574 30 LAFPLCSLYL 12. 1530 11 12.000 1531 11 ____ SAYIIG 112.000__ 1 517 LISTSSMPK4 1.000 1576 66 LCMLSGIDIL 12.00 1532 246 HVCAVFIFV[ 1 25 EAQFWLAFPL 12.000 0 1533 284 LVPPVL 1.000 157 J 150 AAVVRGAALM 9.00I 1534 IRVNVvyGLI 1.000 1579 272 SPLPVILANI 8.000 1535RVTKIGVAAV 1580 249 AVFIFYVPFI 6.000 1536 17 HSYCLHQDVM 1.000 251 FIFYVPFIGLJ 6.000 15IS37__ 254 I G1,SV 000 1582 186 DVMKLACDDI 6.000 1538 10 L DR F18 216 LISFSYLLIL 4.000 1539 1584 110 LSGMESTVI.0 1540 ] 1585 181 1 YCLHQDVMKL[ 4.000 3.541 28 IfFWLAFPLCSL[ 0. 600 ][ 1586 93 TTIQFDACLL 4.000 1542 1 GAALMAPLPV]L 0.600] 1587 297 [T 4.000 1543 167 1 KQLPFCRSNI][ 0.600 158 213[ DSLLISFSYL 4.000 1544 235 AQAKAFGTCV][0 .600 1589 57 SLHEPMYIFL 4.000 1545 ] 238 KAFGTCVSHVJ 0.600 1590 168 QLPFCRSNIL 4.000 1546 268 KRRDSPLPVI][1_0._600 159 92 STTIQFDACL 4.000 1547 279 1ANIYLLVPPV 0.600 1 1592 206 IISAIGLDSL 4.000 1548 152 IVVRGAALMAP 0.500 1593 203 LIVIISAIGL 4.000 1549 IVRTEHSLHE 0 0 1594 222]LLILKTVLL[ 4.000 1550 VAICHPLRRAII 0.450 11 1595 280 NIYLLVPPVL 4.000 1551 AICHPLRHAT 0.450 1596 ISTSSMPKML 4.000 1552 0.400 1597 SLIFSL E4.00 1556GII 101 LLOIFAIHSL1 4.000 1553 20 LPGLEEAQ 0 1598 132 LSGETVLT4.000 If 1554 DRYVAI PL ]LO. _OI 174 ][ SNILSHSYLIl 4.000I1 1555 2991 ]IKEIRQRILRLJI1 0.400 1600 214 JIfSLLISFSYLLII 4.000 If 1556 J 81 )fMPKMLAIFWF][0.00I 1601 207 ifISAIGLDSLLI 4.000 IF771557 [8ITSSMPn. IfTW 1602 10 JSLSGMESTV I 4.000 If 158 ][VLTLPRVTKI] 0.400f 1603 34 LCSLYLIAVL 4.000 1 1559 E 1 0.400 Jf 1604 157 ALMAPLPVFf 3.600 1560 201 1 1605 13 1 HPif HATVLT ___2.000 1 15 ] [0.400 11 1606 243 CVSHVCAVFI 2.000 1562 ]i rv GNLTIIYI .400 L 1607 32 FPLCSLYLIA 2.000 1563 37 LYLIAVLGNL 0.400 1608 198 NVVYGLIVII 1 2.000 1564 65 FLCMSGI 0.400 09 292 IVYGVKTKEI 2.000 1565 283 LLVPPVLNPI 0.400 1 10 4 DPNGNESSAT 2.000 1566 162 LPVFIKQLPF o 04 1 1611 5 PVILANIYLLF 1567 215 LLISGLMA 0.400 1612 174 .Fable XVI:101P3A11-V1-B7-10mers Start bquence Num SStartcore Jseq. ID NumI 7 LLQM IHSL 4.000 [ 130 ICHPLRHATVL 0.400 1613 4 J D MFAI 1654 28 IVPPVLNPIV] 0.400 1j 1614 1 ]IIQFDACLLQM 11001 1655 153 VRGAALMAPL[ 0.400 1615 10 [ 1 9 IQFDACLLQI 0.400 1616 8 [LQMFAIHSLS I 1657 [63I YIFLCMLSGI 0.400 1617 1 [ ACLLQMFAIH. 1658 14 1 YFILIGLPGLI 14 1618 - 6 ] LQMFAIHSHO020 1659 21 PGLEEAQFW]I 0.400 1619 3 SYLLILKTVII 0.400 1620 9 L 491 _IYIVRTEHSL 0.400 1621 2 1662 197 iVNVVYGLIVI IO.400 1622 39 LIAVLGNLTI 0 0 1623 ] able XVII:1O1P3A11-V1-B35-9mers [Ist]tI Subs equenceScor Seq. ID Num] able XVI:1O1P3A11-V2-B7-1Omers .000 1663 Startifsubsequence Score Seq ID. New 274 LPVILANIY 40.000 1664 21 WPISICWFLL180-000 1624 1 20]j LPGLEEAQF 1665 F6 1 IAVLASGVTL12.0 0[ 1625 81 4PIQLAIFW 1 1666 14 TLRCPSSWPI 4.000 1626 J 131Jj HPLRHATVL 1001 167 IcPSSwPIsI627 [01§2j LPFN 120.000 1668 8IFLLCSTQLSMI[ 1 628 1 000 1669 16 RCPSSWPISI 110.400 1 1629 1 266 FSKRRDSPL 15.000 1 20 SWPISICWFL11.400I[ 1630 [ 1_ LPRVTK.GV_4 [26LCWFLLCSTQL1:010 163 [213 11 DSLLISFSY 1001 1672 [ [m IAVL.SG7VI .200I[ 1632 1 7 ISTSSMP=KM 1001 1673 7 AVLASGVTLR10.15jI 1633 1 32 C.LYLI [ 1674 IVLASGVTLRC1 0.100I[ 1634 .0 LSGMESTVL 167 1 j CSLYLIAVLAI I0_._100JF 1 Ii CLYLIAVLA J0. 100J 163 ][30 JI CSLY 6.000] JL 1676 ___L5Is~~j~i] 1636 ] [?]IFAIHSLSG-;M- 6I- 000 1677 24 1 SICWFLLCST 0.100 . 1637 SYLLIL 5.000J1678 12 IGVTLRCPSSW 1638 207 ISAIGLDSL 15.000 1600 10 ASGVTLRCPS J0.090[ 1639 J ESSATYFIL 0 1680 - LASGVTLRCI- 0T~30 1640 J CSLYLIAVL[ 1681 111 IfSGVTLRCPSS [_____[164 ] 297 1KTEI RQRI 148] = 1682 19 SSWPISICWF l 1-][ 1642 - 285 1 VPPVLNPIV [ 1683 SLYLIAVLAS 0.020 1643 VPFIGLSMV 1 1684 ISICWFLLCS 0.020[ 1644 j PPVLNPIVY714.000 1685 1 VTLRCPSS 1645 NGNESSATY 11 4.00001 186 [7 LLCSTQLSME[0. 010 1646 F 20 [SAIGLDSLL 13.0001 1687 25 ICWFLLCSTQ]0.01[ 1647 EIRQRILRL [3.000 1688 22 PISICWFLLC0.010 1648 10GAA [3.000 1689 18 j PSSWPISICW F0.002][ 1649 56 HSLHEPMY 1 1690 27 IWFLLCSTQLS 0.002 1650 121 MAFDRYVAI12 1691 15 1[LRCPSSWPIS[ 0002 1651 1 254 I YVPFIGLSM 2 1692 ]J LYLIAVLASGJ j 1652 4 DPNGNESSA 12.000 1693 113. SGMESTVLL 12.000 1694 able XVI:1O2P3A11-V3-B7-1mers 290 F NPIVYGV I .00 1695 175 TableXVII:101P3A11V1-B35-9mers Fable XVII:11P3A11-V1-B35-9mers Start Subsequen coe e Score Se . ID Num 272 SPLPVILAN 2.00011 1696 189 1741 244 VSHVCAVFI 2.000 1697 ] _______ 060 1742 [ 10I SSATYFILI 2.0 f 1698 ] 231( LTREAQAKA 0I.600J 1743 79~j SSMPKMLAI 12001 1699 ] 209[ AIGLDSLLI 11.01 1744J 57 1f SLHEPMYIF j[2.0001J[ 1700 ] 22 11 GLEEAQFWL 10.6001If 1745 118I LLAI4AFDRY 112.0001[ 1701 ][2711 DSPLPVILA E~oj 1746 246 HVCAVFIFY I [ 1702 ] 219 FSYLLILKT 0.50011 1747 151 AVVRGAALM ]2.01 1703 78 TSSMPKMLA 1o.500j1 1748 73 DILISTSSM 12. 1 1704 LLAMA 110.50011 1749 42f VLGNLTIIY [2. 000] 1 705 ] 18[HSLSGMEST If 0.50011 1750 154 RGAALMAPL 2.00011 1706 9 NSTTIQFDA 0.5001[ 1751 236 QAKAFGTCV 111.800 1707 J 43 [GNLTIIYI 0.400 1752 94 j TIQFDACLL 170 ] 58 NVVYGLIVI .500 1753 182 JrCLHQDVMKL j 1.50oo] 170_9_-] 1991 VVYGLIVII 10.40011 15 40 1r IAVLGNLTI 111.200 1710 216 LISFSYLLI 0.400 1755 187 VMKLACDDI] 1.200 1 202 GLIVIISAI 0.400 [ 1756 221 YLLILKTVL I1.000 1712 28[ P I 0 400 1757 215 LLISFSYLL 1.00 1713 5i 1758 214 SLLISFSYL ]Ii._00] LI j10.400 R 1759 115 STVLLAMAF I.000 1715 [ QLPFCRSNI H0.4001 1760 175 || NILSHSYCL 1.000[ 1716F0400L .1761 67 CMLSGIDIL i_.00 1717 41LTIIE11.400117620 38 YLIAVLGNL 01718 .93 TTIQFDACL] 1719 ] Lable XVII:1O1P3A11-V2-B35-9mers 77 ST S T1.000 170 1tjSubseence S Se ID. NumJ 15 FILIGLPGL- 1.000 1721 12 PSCF pi 16 26 AQFWLAFPL _.000 1722-_7_ CPSSWPISI1 1764 243 IfCVSHVCAVF 3r.oo000 172 18is SSWPISICW 11.0 I 1765 276 f VILANIYLL j1.000 172 LLCSTQLSM 1766 204 rf IVIISAIGL 1. 000 I 1725S fAVAGT 11.001 176 2.9 IfWLAFIPLCSL 111.0001 1726 ]12 IfVTLRCP-SSW1 10001 1768 j [80 If KMAI 1tpo 4 i [.000l 1727 ]22 I SICWFLLC 0.500~i 1769 157 ALMAPLPVF 1.000 1728 8EII LASGVTLRC 10 223 LILKTVLGL 1.000 1729 IAVLASGVT 0 0[ 7 249 if AVFIFYVPF 1.00011 1730 ] o:.2001 1772 12 LQIFAIHSL 1f.0090F 1731 [sfRCPSSWPIS 1 2011773 258 IGLSMVHRP [1.000 1732 SWPISICWF 0.101 1774 179 HSYCLHQDV 1.000 1733 WFLLCSTQL .100 1775 12 || ATYFILIGL 11.000 01 1734 27 FLLCSTQLS 110.100 1776 50s|| YIVRTEHSL 1. -000 1735 GVTLRCPSS 0.100 1777 190 LACDDIRVN 0.900 1736 [ 196 Ir RVNVVYGLI 0.8001 1737 1 [ SGVTLRCPS 110.100 1779 LSGIDILIS 0.750 1738 PISICWFLL 1780 JVTKIGVAAV 7.600 SLYLIAVLA [ 1781 AALMAPLPV 1740 ICWFLLCST 17821 176 able XVII:101P3A11-V2-B35-9mers Table XVIII: lO1P3A11-Vl-B3S-loners Start Subsequence Score Seg ID.Num Start Subseuence Score . ID Nu] 9Z~J ASGVTLRCP 0[o.050 j[ 1783 156 AALMAPLPVF 3.000 1822 ] 17.. PSSWPISIC 0.050T 1784 [1IA0 AFPLCSLYL 11 3. 0 00 jj 1823 14 J LRCPSSWPI 0.040 1785 4 DPNGNESSATJ[3.0001[ 1824 131 fTLRCPSSWP 0.030 1786 300 EIRQRILRLF]3.OOOIj 1825 29 LCSTQLSME ].oi0) 1787 149 VAAVVRGAAL][3.O0o0j 1826 3_ [ YLIAVLASG 0.010 1788194 DIRVNVVYGL3.0001 1827 7 VLASGVTLR 0 *i010 1789 24 CAFFVF .01 182-8 [: YLIVLAS 0.010~ 1790 11 i]SATYFILIGLJ[3.000~ 1829 2 1CFLSO 0.0011 1791 ]25 ]jEAQFWLAFPLJ3o][ 10 ________ 3.000 18310 57bl - - PMYFLf2.00 18321 able XVII:101P3A11-V3-B35-9mers 1 __________ 2.000 1832 [StartSubsequence Score jSeq ID. NumJ 210 IGLDSLLISFI 1833 7 ][ LQMFAIHSL 1.000 1792 6 INGNESSATYFI2.000 1834 4 ACLLQMFAI 0.400 1793 1 29 IIWLAFPLCSLYI 2.0001 1835 3 DACLLQMFA 0.300 1794 ILISTSSMPKMI 1836 8 _QMFAIHSLS 0.100 1795131HPLRHATVLT 2.000] 1837 2 FDACLLQMF 0.100 1796 -AVLGNLTIIY2.000 1838 6 LLQMFAIHS 0.100 1797 ESSATYFILI 2.000l 1839 1 QFDACLLQM 0.060 1798 FPLCSLYLIAI[2.000 18 5 1 CLLQMFAIH 0010 11 1799 F787I TSSMPKMLAI 2.0 I 1841 9 0 1M L.001l 1800 1- VLMFDRY 2.00011 1842 HSAIGLDSLI 1.800 1843 -able XVIII: 101P3A11-V1-B35-10mers 1 SLSGMESTVI 1.5001 1844 Start S~seuenceliScore Seq. ID Num YCLHQDVMKL 1845 81 IMPKMLAIFWF 60.000 1801 TTIQFDACLL V 1846 285 VPPVLNPIVY 40.000 1802 ] GLPGLEEQF 1847 60 EPFLCML20.000 1803 LACDDIR 1848 160 1PLPVFIKQL~0-00 ~ 180- -DACLLQIFAI 1.200 1849 162 LPVFIKQLPF 20.000RQRILRLFV 1.2 1850 274 1f LPVILANIYL 12 0.0 001 1801; j 10 [IAVLGNLTII][1.200J 1851 1 JPGLEEAQFW 15.000 1807 KAFGTCVSHV 1.200 1852 297 KTKEIRQRIL 12.000 1808 RTEHSLHEPM]1.200 1853 179 HSYCLHQDVM 10.000JI 1809 ]T1 1854 272 ISPLPVILANI 8.000 1810 173]RSNILSHSYC1.000 1855 LPRVTKIGVA 6.000 1811 16 LPFCRSNIL 1856 150 AAVVRGAALM 6.000 1812 LISFSYLLIL[1.000 1857 231 LTREAQAKAF 6.000SNILSHSYCL 1.000 1858 11 LSGMESTVLL 5.000 1814 ] 66 LCMLS 1.000 1859 114 ESTVLLAMAF 5.000 1815 SLLISFSYLL 1.000 If 1860 213 DSLLISFSYL 5.000 1816 IISAIGLDSL 1.00011 1861 207 ISAIGLDSLL 5.000 1817 LCSLYLIv 1-000 1862 76 ISTSSMPKML 5.000 1618 2 TCVSHVCAVF 1863 79 IfSSMPKMLAIF 5.ooo 1819 LIVIISAIGL 1.000 244 VSHVCAVFIF 1820 LLQIFAIHSis 5 ~ 1821 2156 ALMLVF 3[.000 '1826 177 000 1823 41PGE7A7.00 12 able XVIII: 101P3A11-V1-B35-10mera] able XVIII1oIP3A11-V2-B35-10mers Start|Subsequence Score Seq. ID Num 280 ] I YLLVPPVL 1.000 1867 23_IF LLCS .500J1 1908 219 FSYLLILKTV 1.000 1868 10 ASGVTLRCPS][.500 1909 257 FIGLSMVHRF 1.000 1869 1 _____ 00 19 251 FIFYVPFIGL 1.000 1870 1__0 1911 108 HSLSGMESTV 1.000 1871 18 ISrCW0.5 19 236 QAKAFGTCVS 1.900 872 4 YLIAVLASGVI0.200 1913 95 IQFDACLI 0.8001[ 1873 26 CWFLLCSTQLI0.10[ 1914 167 KQLPFCRSNI 0.800 1874 2 SLYLIAVLAS 0.100 1915 121 MAPDRYVAIC 0.60 1875C 0.1001 1916 144 J[VTKIGVAAVVo .600 1876 24 SICWFLLCST 0.100 1917 15 GAALMAPLPV 0.600 1877 11 SGVTLRCPSS 0.100 1918 112 GMESTVLLAM 0.600 1878 20 SWPISICWFL 0_100 1 135 HATVLTLPRV 0.60j 1879 [50LIAVLASGVTO.100 1910 69 LSGIDILIST 0.500 1880 [-[ GVTILRCP 0 030 1921 271 DSPLPVILAN 0.500[ 1881 [ ] VLASGVTL.1922 80 SMPKMLAIFW 10.500 1 1882 15 LRCPSSWPISI0.010 1923 91 NSTTIQFDAC 0.500 1883 TQLSJ10.0101 1924 268 KRRDSPLPVI 0.48 188 2 LLC 1925 119 JLAMAFDRYVAI0.4501 188522]PscFc]olo[ 16 201 YGLIVIISAI 10.4001 1 ICWFLLCSTO]1o. 0 1927 198 J NVVYGLIVII 0.400I 1887 r131 jVTLRCPSSWPJ[0. 0101 1928 243 CVSHVCAVFI 0.400 1888 LYLIAVLASG]IO -0T31 1929 283 LLVPPVLNPI 0.400 188.9 67 CMLSGIDILI 0.400 189 XVII:1O1P3A1-V3-B35-lmers] 120 AMAFDRYVAI 0.400 1891 S [ core ID. Numl 65 FLCMLSGIDI 0.400 1892 1 4000 42 VLGNLTIIYI 0.400 1893 j 4 ]1DACLLQIFAI 1.200 1931 186 11D CDII0.400 1894 7 LLQMFAIHSL 1.000 39 JLIAVLGNLTI 0.400 1895 MFAIHSLSGM 0.200 1933 157 ALMAPLPVFI 0.400 1896 6 CLLQMFAIHS 0.100 1934 292 IVYGVKTKEI 0.400 1897 8 MFAIHSLS 0.100 1935 1 RVTKIGVAAV 0.400 1898 [ [QFDACLIQNF 0.030 1936 AIFWFNSTTI 0.400 1899 FDACLL F 0.10 1937 1 RVNVVYGLIV 0.400J 1900 I 9 IFHSLS0 93 _i ALQ4AXH 3.93. able XVIII:101P3A11-V2-B35-10mers StartSubsequence ore S .New 21 1WPISICWFLL 20.0001 90 19 SSWPISICWF 5.000[ 1902 6 IAVLASGVTL 3.000 1903 28 FLLCSTQLSM][ 2.000 1904 17 CPSSWPISIC 2.000 1905 14 TLRCPSSWPI 1.200 1906 ISCWLCS0.0710 16SGVTLRCPS70.50081909 12 GTLCSW .00 11 11SLLAVA8.0 Table XIX: Motifs and Post-translational Modifications of lOlP3A1l N-glycosylation site Number of matches! 3 1 7-10 NESS 2 44-47 NLTI 3 90-93 NSTT cAMP- and cGMP-dependent protein kinase phosphorylation site 268-271 RRDS Protein kinase C phosphorylation site 266-268 SKR Casein kinase II phosphorylation site Number of matches: 3 1 56-59 SLHE 2 69-72 SGID 3 110-113 SGME N-myristoylation site Number of matches: 4 1 6-11 GNESSA 2 21-26 GLEEAQ 3 111-116 GMESTV 4 240-245 GTCVSH G-protein coupled receptors family 1 signature 112-128 MESTVLLAMAFDRYVAI 179 Table XX: Motifs vyrg. % Name Description Potential Function identityDeciin Nucleic acid-binding protein functions as z-H22 34% Zinc finger, C21-12 type transcription factor, nuclear location probable Cytochrome b(N vtochrome b N 68% terminal)/b6/petB embrane bound oxidase, generate superoxide domains are one hundred amino acids long and ! 19% Immunoglobulin domain include a conserved intradomain disulfide bond. tandem repeats of about 40 residues, each :ontaining a Trp-Asp motif. Function in signal WD0 18% WD domain, G-beta repeat sduction and protein interaction nay function in targeting signaling molecules to 23% DZ domain sub-membranous sites short sequence motifs involved in protein-protein 28% Leucine Rich Repeat interactions conservedd catalytic core common to both serine/threonine and tyrosine protein kinases containing an ATP binding site and a catalytic ie 23% rotein kinase domain site pleckstrin homology involved in intracellular 16% PH domain signaling or as constituents of the cytoskeleton 30-40 amino-acid long found in the extracellular domain of membranc-bound proteins or in OF 34% EGF-like domain secreted proteins Reverse transcriptase (RNA 49% dependent DNA polymerase) Cytoplasmic protein, associates integral atk 25% Ank repeat membrane proteins to the cytoskeleton

NADH

Ubiquinone/plastoquinone membrane associated. Involved in proton axioqiglgj. 32% (complex 1), various chains slocation across the membrane alcium-binding domain, consists of a12 residue loop flanked on both sides by a 12 residue alpha afhand 24% EF hand helical domain Aspartyl or acid proteases, centered on a catalytic rlp 79% Retroviral aspartyl protease aspartyl residue :xtracellular structural proteins involved in formation of connective tissue. The sequence Collagen triple helix repeat (20 onsists of the G-X-Y and the polypeptide chains oila 2% pies) orms a triple helix. 180 Table XX: Motifs avrg. % Name adentit Description Potential Function identityDsriin Located in the extracellular ligand-binding region of receptors and is about 200 amino acid rcsiducs long with two pairs of cysteines involved in n 0% Fibronectin type IIf domain disulfide bonds seven hydrophobic transmembrane regions, with the N-terminus located extracellularly while the 7 transmembrane receptor -terminus is cytoplasmic. Signal through G IMHL 19% rhodopsin family) roteins 181 TABLE XXI: Properties of 1O13AI Bioinformatic Variants I and 3 Program URL Outcome ORF ORF Finder http://www.ncbi.nlm.gov/gorf 133-1086 (includes stop) Protein Length n/a n/a 317 amino acids Transmembrane region TM Pred http://www.ch.embnet.org/ 7 TM at aa: 27-52, 63-88, 104 129, 146-165, 196 224, 239-262,273 295 HMMTop http://www.enzim.hu/hmmtop/ 7 TM at aa: 27-50, 63-86, 99 121, 146-165,201 224, 239-262, 275 294 Sosui http://www.genomc.ad.jp/SOSui/ 6 TM, at aa: 29-51, 63-85, 100 122, 203-225, 239 261, 273-295 TMHMM http:/www.cbs.dtu.dk/services/TMHM 7 TM, at aa: M 29-51, 63-85, 100 122, 143-165, 202 224, 236-258, 273 295 Signal Peptide Signal P http://www.cbs.dtu.dk/scrvices/SignalP indicates no signal p1 p1/MW tool http://www.expasy.ch/tools/ pl 8.7 Molecular weight p1/MW tool http://www.expasy.ch/tools/ 35.2 kDa Localization PSORT http://psort.nibb.ac.jp/ Plasma membrane 64% PSORT 11 http://psort.nibb.ac.jp/ Plasma membrane 56.4% Motifs Pfam http://www.sangcr.ac.uk/PfanV 7 transmembranc receptor (rhodopsin family) Prints http://www.biochem.ucl.ac.uk/ Rhodopsin-like GPCR supcrfamily Blocks http://www.blocks.fhcrc.org/ Rhodopsin-like GPCR superfamily Prositc http://www.gcnome.ad.jp/ G-protcin coupled receptors family I IOIP3AI I var.2 Bioinformatic URL Outcome Program ORF ORF finder 130-348bp including stop Protein length 72aa Transmembrane region TM Pred http://www.ch.cmbnet.org/ 2TM hcliccs aa28-49, 55-72 N terminus cxtraccllular HMMTop http://www.cnzim.hu/hmmtop/ 2TM helices N terminus extracellular Sosui http://www.genome.ad.jp/SOSui/ 2TM helices aa28-50, 52-72 TMHMM http://www.cbs.dtu.dk/services/TMHMM I TM helix, aa27-49 182 101P3A I I var.2 Bioinformatic URL Outcome Program Signal Peptide Signal P http://www.cbs.dtu.dk/scrvices/SignalP/ no pl pl/MW tool http://www.expasy.ch/tools/ p1 4.12 Molecular weight pl/MW tool http://www.expasy.ch/tools/ 7.95kB Localization PSORT http://psort.nibb.ac.jp/ 82% extracellular, 16% peroxisome PSORT II http://psort.nibb.ac.jp/ 39% cytoplasmic, 17% mito chondrial, 17% nuclear Motifs Pfam http://www.sanger.ac.uk/Pfam/ no motifs found Prints http://www.biochem.uc.ac.uk/ no motifs found Blocks http://www.blocks.fhcrc.org/ Zcin sced storage protein 183 Table XXII - 101P3A11 vi. HLA-Al 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 246A V F I F Y 24 1940 30 L A F P L C S L Y 21 1941 42 V L G N L T I I y 21 1942 286 P P V L N P I V Y 20 1943 112 G M E S T V L L A 19 1944 118 L L AM A F D R Y 19 1945 173 R S N I L S H S Y 19 1946 193 D D I R V N V V Y 19 1947 213 D S L L I S F S Y 19 1948 58 L H E P M Y I F L 18 1949 23 L E E A Q F W L A 17 1950 10 S S A T Y F I L I 16 1951 53 R T E H S L H E P 16 1952 55H S L H E P M Y 16 1953 79 S S M P K M L A I 16 1954 96 Q F D A C L L Q I 16 1955 160 A P L P V F I K Q 16 1956 184 H Q D V M K L A C 16 1957 2 M V D P N G N E S 15 1958 6 N G N E S S A T Y 15 1959 211 G L D S L L I S F 15 1960 274 L P V I L A N I Y 15 1961 272 S P L P V I L A N 14 1962 92 S T T IQ F D A C 13 1963 122 A F D R Y V A I C 13 1964 139 L T L P R V T K I 13 1965 219 F S Y L L I L K T 13 1966 283 L L V P P V L N P 13 1967 191 A C D D I R V N V 12 1968 192 C D D I R V N V V 12 1969 232 T R E A Q A K A F 12 1970 269 R R D S P L P V I 12 1971 271 D S P L P V I L A 12 1972 12 A T Y F I L I G L 11 1973 22 G L E E A Q F W L 11 1974 177 L S H S Y C L H Q 11 1975 217 I S F S Y L L I L 11 1976 Table XXII - 1O1P3A11 v2 HLA Al - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 22 I S I C W F L L C 15 1977 18 S S W P I S I C W 14 1978 8 L A S G V T L R C 9 1979 23 S I C W F L L C S 8 1980 2 L Y L I A V L A S 7 1981 7 VL A S G V T L R 7 1982 12 V T L R C P S S W 7 1983 28 L L C S T Q L S M 7 1984 Table XXII - 101P3A11 v3 HLA Al 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 184 Table XXII - 1OlP3A1l v3 HLA Al 9-mers 123456789 score SEQID Q F DA C L LQ M 16 1985 Table XXIII - 101P3A1l v1. HLA-A0201 9-mers POO 1 2 3 4 5 6 7 8 9 score SEQ ID 288 V L N P I V Y G V 30 1986 15 F I L I G L P G L 29 1987 29 W L A F P L C S L 28 1988 38 Y L I A V L G N L 28 1989 223 L I L K T V L G L 28 1990 67 C M L S G I D I L 26 1991 109 S L S G M E S T V 26 1992 182 C L H Q D V M K L 26 1993 202 G L I V I I S A I 26 1994 215 L L I S F S Y L L 26 1995 276 V I L A N I Y L L 26 1996 158 L M A P L P V F I 25 1997 221 Y L L I L K T V L 25 1998 277 I L A N I Y L L V 25 1999 280 N I Y L L V P P V 25 2000 139 L T L P R V T K I 24 2001 214 S L L I S F S Y L 24 2002 50 Y I V R T E H S L 23 2003 144 V T K I G V A A V 23 2004 189 K L A C D D I R V 23 2005 199 V V Y G L I V I I 23 2006 22 G L E E A Q F W L 22 2007 41 A V L G N L T I I 22 2007 207 I S A I G L D S L 22 2008 12 A T Y F I L I G L 21 2009 61 P M Y I F L C M L 21 2010 136 A T V L T L P R V 21 2011 161 P L P V F I K Q L 21 2012 175 N I L S H S Y C L 21 2013 208 S A I G L D S L L 21 2014 273 P L P V I L A N I 21 2015 284 L V P P V L N P I 21 2016 68 M L S G I D I L I 20 2017 102 L Q I F A I H S L 20 2018 283 L L V P P V L N P 20 2019 300 E I R Q R I L R L 20 2020 305 I L R L F H V A T 20 2021 40 I A V L G N L T I 19 2022 46 L T I I Y I V R T 19 2023 93 T T IQ F D A C L 19 2024 111 S G M E S T V L L 19 2025 128 A I C H P L R H A 19 2026 133 L R H A T V L T L 19 2027 150 A A V V R G A A L 19 2028 156 A A L M A P L P V 19 2029 157 A L M A P L P V F 19 2030 204 I V I I S A I G L 19 2031 209 A I G L D S L L I 19 2032 185 ___________Table XXIII - 1OlP3A11 vi. HLA-A0201 9-merB Poe 12 34 5 67 89 score SEQ ID 217 I S F S Y L L I L 19 2033 220 S YL LIL K TV 19 2034 222 L LI LK"T VLG 19 2035 224 1L KT V LG LT 19 2036 18 IG LP G LE EA 18 2037 34 LC SL Y L IAV 18 2038 35 CS L yL I AVL 18 2039 39 LI AV L G NLT 18 2040 44 GQNL TI I YI V 18 2041 86 A I FW FN STT 18 2042 119 LA MA F DR YV 18 2043 195 1R V NVV Y GL 18 2044 211 G LD SL L ISF 18 2045 216 LI S FS Y LLI 18 2046 247 VC AV F I FYV 18 2047 255 VP F IG LS MV 18 2048 16 1IL10L P G LE 17 2049 64 1IFLC ML SGI1 17 2050 73 DI LI ST S SM 17 2051 94 T1Q0F DA C LL 17 2052 99 AC L L (I FAI1 17 2053 112 GM ES T V LLA 17 2054 121 MA F DRY VAI1 17 2055 168 Q LP FC RSNI1 17 2056 198 NV VY GL IVI1 17 2057 227 T V L L TR EA 17 2058 282 Y LL V PP VLN 17. 2059 32 FP LC SL YLI1 16 2060 57 SL H EP M YIF 16 2061 71 GI DI LI S TS 16 2062 79 S S M PK MLAI1 16 2063 80 SM P K ML AIF 16 2064 105 FA I HS LS GM 16 2065 120 AM AF DR Y VA 16 2066 145 T KIG0V A AVV 16 2067 148 GV A AV VR GA 16 2068 187 VM K LA CDDI1 16 2069 231 L TR E AQ AKA 16 2070 239 AF GT C VS HV 16 2071 250 -VF IF Y VPFI1 16 2072 303 Q RIL RL F HV 16 2073 304 RI L R LF HVA 16 2074 19 GL PG L E EAQ 15 2075 36 S LY LI A VLG 15 2076 43 LG N LT I I YI i5 2077 47 TI I YIV R TE 15 2078 70 S GI DI LI ST 15 2079 77 S T SS M PK ML 15 2080 132 P LR HAT V LT 15 2081 138 VL TL PR V TK i5 2082 154 R GAA LM A PL 15 2083 191 AC D DIR V NV 15 2084 192 CD DI RV N VV 1s 2085 205 VI IS A I GLD 15 2086 242 -TC VS HV C AV 15 2087 186 Table XXIII - 101P3A1 vI. HLA-A0201 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 252 I F Y V P F I G L 15 2088 270 R D S P L P V I L 15 2089 281 I Y L L V P P V L 15 2090 307 R L F H V A T H A 15 2091 17 L I G L P G L E E 14 2092 26 A Q F W L A F P L 14 2093 42 V L G N L T I I Y 14 2094 63 Y I F L C M L S G 14 2095 74 I L I S T S S M P 14 2096 85 L A I F W F N S T 14 2097 100 C L L Q I F A I H 14 2098 118 L L A M A F D R Y 14 2099 130 C H P L R H A T V 14 2100 151 A V V R G A A L M 14 2101 169 L P F C R S N I L 14 2102 201 Y G L I V I I S A 14 2103 219 F S Y L L I L K T 14 2104 236 Q A K A F G T C V 14 2105 269 R R D S P L P V I 14 2106 297 K T K E I R Q R I 14 2107 Table XXIII - 1O1P3A11 v2 HLA A0201 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 4 L I A V L A S G V 24 2108 3 Y L I A V L A S G 22 2109 6 A V L A S G V T L 22 2110 1 S L Y L I A V L A 19 2111 7 V L A S G V T L R 19 2112 28 L L C S T Q L S M 19 2113 23 S I C W F L L C S 16 2114 21 P I S I C W F LL 15 2115 27 F L L C S T Q L S 15 2116 24 I C W F L L C S T 13 2117 14 L R C P S S W P I 12 2118 20 W P I S I C W F L 12 2119 26 W F L L C S T Q L 12 2120 8 L A S G V T L R C 11 2121 13 T L R C P S S W P 11 2122 Table XXIII- 1O1P3A11 v3 HLA A0201 9-mers Poo 1 2 3 4 5 6 7 8 9 score SEQ ID 7 L Q M F A I H S L 19 2123 5 C L L Q M F A I H 14 2124 4 A C L L Q M F A I 13 2125 6 L L Q M F A I H S 13 2126 1 Q F D A C L L Q M 9 2127 8 Q M F A I H S L S 9 2128 Table XXIV: 101P3A11- V1 HLA-A0203 9-mers- No Results. Table XXIV: 1O1P3A11- V2 HLA-A0203 9-mers- No Results. Table XXIV: 101P3A11- V3 HLA-A0203 9-mers- No Results. Table XXV - 101P3A11 vI. HLA-A3 9-mers 187 Pos 12 34 5 67 89 score SEQ ID 138 VLT LP R V TK 30 2129 230 GLTREAQA K 27 2130 146 K I GVAA V VR 26 2131 151 AVVRGAALM 24 2132 291 P IVY GV K TK 24 2133 36 S L YLI A VLG 23 2134 157 ALMAPLPVF 23 2135 48 2YIVRTEH 22 2136 51 VRTE SILH 22 2137 143 RVT KI G V AA 22 2138 152 VV R GA A L MA 22 2139 243 CV S HV C A V 22 2140 249 AVF I FY V PF 22 2141 117 VLLAMAFDR 21 2142 193 DDIRVNVVY 21 2143 304 R LRLFHV A 21 2144 305 LRLFHVAT 21 214 109 SLSGMESTV 2146 19 VVYG8L2IV 20 2147 292 1IV Y GV KT KE 20 2148 16 1ILIG LP G LE 19 2149 45 NLTIIYIV R 19 2150 74 1LXS TSSMP 19 2151 75 L ISTSSMPK 19 2152 100 CLLQ FAIH 19 2153 163 P VFIKQLPF 19 2154 204 1V II SA I GL 19 2155 222 LL IL KT V LG 19 2156 246 HV CAVFIFY 19 2157 307 R LF HV A THA 19 2158 41 A V LG0NL TI 1 1 2159 86 AI FWFNSTT 18 2160 206 1 ISA I GL DS 18 2161 221 Y LL I LK TVL 18 2162 254 Y V PFIGLS 818 2163 38 Y LIA VL G NL 17 2164 42 V LG NL T IIY 17 2165 118 L LA M AF DRY 17 2166 132 PL R HAT V LT 17 2167 137 T VLT L PR VT 17 2168 181 Y CL H0D V MK 17 2169 202 C L IV II SA1 17 2170 214 S L L ISFS YL 17 2171 257 1 0L S MV HR 17 2172 262 M VH R FSKXRR 17 2173 277 1IL A KIY LLV 17 2174 282 YL LV P PV LN 17 2175 287 PV L NP IV YG 17 2176 289 LN P IV YG VK 17 2177 310 HVA T HA S EP 17 2178 2 M V DP N G NES 16 2179 57 SL HE PM Y IF 16 2180 71 G ID IL IS TS 16 2181 73 DIL I ST S SM 16 2182 116 T VL LA M AFD 16 2183 126 YV AI CH P LR 16 2184 188 Table XXV - 101P3A11 vi. HLA-A3 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 145 T K I G V A A V V 16 2185 168 Q L P F C R S N I 16 2186 176 I L S H S Y C L H 16 2187 196 R V N V V Y G L I 16 2188 198 N V V Y G L I V I 16 2189 211 G L D S L L I S F 16 2190 283 L L V P P V L N P 16 2191 300 E I R Q R I L R L 16 2192 302 R Q R I L R L F H 16 2193 17 L I G L P G L EE 15 2194 47 T I I Y I V R T E 15 2195 103 Q I P A I H S L S 15 2196 194 D I R V N V V Y G 15 2197 209 A I G L D S L L I 15 2198 224 I L K T V L G L T 15 2199 238 K A P G T C V S H 15 2200 6 N G N E S S A T Y 14 2201 63 Y I F L C M L S G 14 2202 101 L L Q I F A I H S 14 2203 140 T L P R V T K I G 14 2204 148 G V A A V V R G A 14 2205 165 F I K Q L P F C R 14 2206 189 K L A C D D I R V 14 2207 225 L K T V L G L T R 14 2208 227 T V L G L T R E A 14 2209 2S6 P F I G L S M V H 14 2210 275 P V IL AN I Y L 14 2211 284 L V P P V L N P I 14 2212 299 K E I R Q R I L R 14 2213 Table XXV - 101P3A11 v2 HLA A3 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 6 A V L A S G V T L 28 2214 1 S L Y L I A V L A 23 2215 3 Y L I A V L A S G 21 2216 7 V L A S G V T L R 18 2217 13 T L R C P S S W P 17 2218 4 L I A V L A S G V 15 2219 11 G V T L R C P SS 15 2220 28 L L C S T Q L S M 15 2221 Table XXV - 101P3A11 v3 HLA A3 9-mers Pos 1 2 3 4 5 6 7 5 9 score SEQ ID 5 C L L Q M F A I H 19 2222 6 L L Q M F A I H S 13 2223 1 Q F D A C L L Q M 10 2224 Table XXVI - 101P3A11 v1. HLA-A26 9-mers POS 1 2 3 4 5 6 7 8 9 score SEQ. ID No. 189 Table XXVI - lO1P3AIl vi. HLA-A26 9-mers Pos 1 2 3 4 5 6 7 8 9 I score SEQ. ID No. 300 EIRQRILRL 30 2225 73 DILISTSSM 27 2226 249 AVFIFYVPF 27 2227 211 GLDSLLISF 26 2228 15 FILIGLPGL 24 2229 57 SLHEP M YIF 24 2230 118 LLAlMAFDRY 24 2231 223 LILKTVILGL 24 2232 246 HVCAVFIFY 24 2233 12 ATYFILIGL 23 2234 38 YLIAVLGNL 23 2235 115 STVLLAMAF 23 2236 157 ALMAPLPVF 23 2237 163 PVFIKQLPF 23 2238 182 CILHQDVMKL 23 2239 29 WLAFPLCSL 22 2240 93 TTIQFDACL 22 2241 161 PLPVFIKQL 22 2242 204 1VIISAIGL 22 2243 214 SLLISFSYL 22 2244 276 VILANIYLL 22 2245 194 DIRVNVVYG 21 2246 243 CVSHVCAVF 21 2247 77 STSSMPKML 20 2248 254 YVPFIGLSM 20 2249 275 PVILANIYL 20 2250 24 EEAQFWLAF 19 2251 42 V L G N L T I I Y 19 2252 50 YIVRTEHSL 19 2253 151 AVVRGAALM 19 2254 175 NILSHSYC 19 2255 193 DD I R V N V V Y 19 2256 215 L L I S F S Y L L 19 2257 252 1FYVPFIGL 19 2258 9 E S S A T Y F I L 18 2259 22 GLEEAQFWL 18 2260 46 L T I I Y I V R T 18 2261 55 E H S L H E P M Y 18 2262 60 E P M Y I F L C M 18 2263 89W F N S T T 18 2264 94 T I Q F D A CL L 18 2265 186 D V M K L A C D D 18 2266 199 VVYGLIV11 18 2267 63 YI FLCMLS G 17 2268 71G I D I L I S T S 17 2269 80 SMPKMLAIF 17 2270 97 FDACLLQIF 17 2271 105 FAIHSLSGM 17 2272 139L T L P R V T K 17 2273 144 V T K I G V A A V 17 2274 205 V I I S A I G L D 17 2275 213 D S L L I S F S Y 17 2276 221Y L L I L K T V L 17 2277 257 F I G L S M V H R 17 2278 284L V P P V L N P I 17 2279 190 Table XXVI - 101P3A1l vi. HLA-A26 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ. ID No. 30 L A F P L C S L Y 16 2280 41 A V L G N L T I I 16 2281 47 T I I Y I V R T E 16 2282 53 R T E H S L H E P 16 2283 76 I S T S S M P K M 16 2284 92 S T T I Q F D A C 16 2285 136 A T V L T L P R V 16 2286 148 G V A A V V R G A 16 2287 202 G L I V I I S A I 16 2288 258 I G L S M V H R F 16 2289 280 N I Y L L V P P V 16 2290 31 A F P L C S L Y L 15 2291 102 L Q I F A I H S L 15 2292 116 T V L L A M A F D 15 2293 128 A I C H P L R H A 15 2294 154 R G A A L M A P L 15 2295 164 V F I K Q L P F C 15 2296 216 L I S F S Y L L I 15 2297 217 I S F S Y L L I L 15 2298 226 K T V L G L T R E 15 2299 273 P L P V I L A N I 15 2300 283 L L V P P V L N P 15 2301 287 P V L N P I V Y G 15 2302 288 V L N P I V Y G V 15 2303 297 K T K E I R Q R I 15 2304 304 R I L R L F H V A 15 2305 2 M V D P N G N E S 14 2306 6 N G N E S S A T Y 14 2307 33 P L C S L Y L I A 14 2308 35 C S L Y L I A V L 14 2309 58 L H E P M Y I F L 14 2310 82 P K M L A I F W F 14 2311 100 C L L Q I F A I H 14 2312 196 R V N V V Y G L I 14 2313 198 N V V Y G L I V I 14 2314 207 I S A I G L D S L 14 2315 208 S A I G L D S L L 14 2316 227 T V L G L T R E A 14 2317 231 L T R E A Q A K A 14 2318 245 S H V C A V F I F 14 2319 291 P I V Y G V K T K 14 2320 301 I R Q R I L R L F 14 2321 Table XXVI - 101P3A11 v2 HLA A26 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 6 A V L A S G V T L 20 2322 21 P I S I C W F L L 18 2323 28 L L C S T Q L S M 18 2324 3 Y L I A V L A S G 16 2325 19 S W P I S I C W F 16 2326 26 W F L L C S T Q L 15 2327 4 L I A V L A S G V 14 2328 7 V L A S G V T L R 14 2329 191 Table XXVI - 101P3Al v2 HLA A26 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 23 S I C W F L L C S 14 2330 11 G V T L R C P S S 12 2331 12 V T L R C P S S W 12 2332 20 W P I S I C W F L 11 2333 27 F L L C S T Q L S 10 2334 1 S L Y L I A V L A 9 2335 13 T L R C P S S W P 9 2336 Table XXVI - 101P3A11 v3 HLA A26 9-mers Poo 1 2 3 4 5 6 7 8 9 score SEQ ID 1 Q F D A C L L Q M 20 2337 2 F D A C L L Q M F 18 2338 5 C L L Q M F A I H 14 2339 7 L Q M F A I H S L 13 2340 6 L L Q M F A I H S 9 2341 Table XXVII - 101P3A1: v1. HLA-B0702 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 131 H P L R H A T V L 22 2342 60 E P M Y I F L C M 21 2343 169 L P F C R S N I L 20 2344 290 N P I V Y G V K T 19 2345 4 D P N G N E S S A 18 2346 20 L P G L E E A Q F 18 2347 141 L P R V T K I G V 18 2348 285 V P P V L N P I V 17 2349 32 F P L C S L Y L I 16 2350 255 V P F I G L S M V 16 2351 270 R D S P L P V I L 16 2352 150 A A V V R G A A L is 2353 154 R G A A L M A P L 15 2354 157 A L M A P L P V F 15 2355 252 I F Y V P F I G L 15 2356 300 E I R Q R I L R L 15 2357 9 E S S A T Y F I L 14 2358 29 W L A F P L C S L 14 2359 31 A F P L C S L Y L 14 2360 111 S G M E S T V L L 14 2361 133 L R H A T V L T L 14 2362 160 A P L P V F I K Q 14 2363 223 L I L K T V L G L 14 2364 272 S P L P V I L A N 14 2365 26 A Q F W L A F P L 13 2366 110 L S G M E S T V L 13 2367 125 R*Y V A I C H P L 13 2368 217 I S F S Y L L I L 13 2369 269 R R D S P L P V I 13 2370 281 I Y L L V P P V L 13 2371 12 A T Y F I L I G L 12 2372 35 C S L Y L I A V L 12 2373 192 Table XXVII - 1O1P3A11 v1. HLA-B!0702 9-mers Pos 12 34 56 7 89 score SEQ ID 58 LH EP MY I FL. 12 2374 77 ST SS MP K ML 12 2375 143 RV T KIG V AA 12 2376 152 VV R GAA L MA 12 2377 191 AC DD IR V NV 12 2378 195 1R VN VV Y GL 12 2379 207 1IS AI GL DSL 12 2380 208 S AI G LDS LL 12 2381 221 YL LI LK T VL 12 2382 268 KR RD S PL PV 12 2383 305 1ILJRL F HV AT 12 2384 15 F IL IGL P GL 11 28 24 EE A QFW L AF 1!38 38 YL IA VL G NL 11 28 41 AV LGN L TII1 11 28 78 TS S MP K MLA 11 28 79 SS MP K*MLA 1 11 2390_____ 81 M P K MLA IFW 11 2391_____ 93 T TIQ0F DA CL 11 2392_____ 113 M E ST V LL AM 11 2393 120 AM AF DR Y VA 11 2394 128 A IC H PL RHA 11 2395 132 P L RHA T VLT 11 2396 156 A AL M A PL PV 11 2397 158 L MA PL PVF 1 11 2398 182 CLH Q D VM KL 11 2399 204 1V I I SA I GL 11 2400 209 A IGL DS LL 1 11 2401 214 SL L ISF S YL 11 2402 249 AV FI FY V PF 11 2403 266 FS K RRD S PL 11 2404 276 V I L AN1Y L L 11 2405 286 P PVL N P IVY 11 2406 8 NE S SAT YFI1 10 2407 22 GL EE AQ F WL 10 2408 50 Y IVR TE H SL 10 2409 61 P MY IF LC ML 10 2410 67 CM LS G I DIL 10 2411 68 MLS GI DI LI1 10 2412 94 T IQF D A CLL 10 2413 96 F DA CL LQI1 10 2414 102 L Q IFA I HSL 10 2415 109 S L S G ME STV 10 2416 129 1C HP L R HAT 10 2417 145 TK I GVA A VV 10 2418 161 P LP VF I KQL 10 2419 162 LP VF IK QL P 10 2420 175 NI L SH SY CL 10 2421 199 V VY G L IVI I 10 2422 215 LL IS F S YLL 10 2423 216 L ISF SY LLI1 10 2424 239 A FGT C V SH 10 2425 243 CV S HVC A VF 10 2426 271 DS PL PV I LA 10 2427 274 L P VIL A NIY 10 2428 193 Table XXVII - 101P3A11 v1. HLA-B0702 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 275 P V I L A N I Y L 10 2429 277 I L A N I Y L L V 10 2430 298 T K E I R Q R I L 10 2431 Table XXVII - 101P3A11 v2 HLA B0702 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 20 W P I S I C W F L 21 2432 16 C P S S W P I S I 18 2433 6 A V L A S G V T L 16 2434 21 PI S I C W F L L 12 2435 26 W F L L C S T Q L 11 2436 Table XXVII - 101P3A1l v3 HLA B0702 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 7 L Q M F A I H S L 11 2437 1 Q F D A C L L Q M 10 2438 4 A C L L Q M F A I 9 2439 2 F D A C L L Q M F 7 2440 3 D A C L L Q M F A 7 2441 Table XXVIII - 101P3All v1. HLA-B08 9-mers Poo 1 2 3 4 5 6 7 8 9 score SEQ ID 300 E I R Q R I L R L 31 2442 266 F S K R R D S P L 29 2443 150 A A V V R G A A L 24 2444 169 L P F C R S N I L 24 2445 295 G V K T K E I R Q 21 2446 121 M A F D R Y V A I 20 2447 293 V Y G V K T K E I 20 2448 22 G L E E A Q F W L 19 2449 79 S S M P K M L A I 19 2450 161 P L P V F I K Q L 19 2451 187 V M K L A C D D I 18 2452 214 S L L I S F S Y L 18 2453 222 L L I L K T V L G 18 2454 297 K T K E I R Q R I 18 2455 298 T K E I R Q R I L 18 2456 131 H P L R H A T V L 17 2457 182 C L H Q D V M K L 17 2458 224 I L K T V L G L T 17 2459 29 W L A F P L C S L 16 2460 38 Y L I A V L G N L 16 2461 57 S L H E P M Y I F 16 2462 81 M P K M L A I F W 16 2463 163 P V F I K Q L P F 16 2464 202 G L I V I I S A I 16 2465 208 S A I G L D S L L 16 2466 194 Table XXVIII - 1O1P3A11 v1. HLA-B08 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 215 L L I S F S Y L L 16 2467 221 Y L L I L K T V L 16 2468 234 E A O A K A F G T 16 2469 276 V I L A N I Y L L 16 2470 305 I L R L F H V A T 16 2471 15 F I L I G L P G L 15 2472 111 S G M E S T V L L 15 2473 139 L T L P R V T K I 15 2474 165 F I K Q L P F C R 15 2475 223 L I L K T V L G L 15 2476 Table XXVIII - 101P3A11 v2 HLA BOB - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 20 W P I S I C W F L 16 2477 21 P I S I C W F L L 14 2478 13 T L R C P S S W P 12 2479 16 C P S S W P I S I 12 2480 6 A V L A S G V T L 11 2481 26 W F L L C S T Q L 11 2482 1 S L Y L I A V L A 10 2483 11 G V T L R C P S S 10 2484 19 S W P I S I C W F 9 2485 7 V L A S G V T L R 8 2486 27 F L L C S T Q L S 7 2487 Table XXVIII - 101P3A11 v3 HLA BOB 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 7 L Q M F A I H S L 11 2488 4 A C L L Q M F A I 8 2489 2 F D A C L L Q M F 7 2490 5 C L L Q M F A I H 6 2491 6 L L Q M F A I H S 6 2492 3 D A C L L Q M F A 5 2493 Table XXIX - 101P3A11 v1. HLA-B1510 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 58 L H E P M Y I F L 23 2494 245 S H V C A V F I F 17 2495 270 R D S P L P V I L 16 2496 281 I Y L L V P P V L 16 2497 263 V H R F S K R R D 15 2498 300 E I R Q R I L R L 15 2499 107 I H S L S G M E S 14 2500 207 I S A I G L D S L 14 2501 221 Y L L I L K T V L 14 2502 252 I F Y V P F I G L 14 2503 298 T K E I R Q R I L 14 2504 22 G L E E A Q F W L 13 2505 35 C S L Y L I A V L 13 2506 55 E H S L H E P M Y 13 2507 195 Table XXIX - 101P3A11 v1. HLA-B1510 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 111 S G M E S T V L L 13 2508 195 I R V N V V Y G L 13 2509 9 E S S A T Y F I L 12 2510 15 F I L I G L P G L 12 2511 29 W L A F P L C S L 12 2512 67 C M L S G I D I L 12 2513 77 S T S S M P K M L 12 2514 93 T.T IQ F D A C L 12 2515 110 L S G M E S T V L 12 2516 131 H P L R H A T V L 12 2517 133 L R H A T V L T L 12 2518 150 A A V V R G A A L 12 2519 154 R G A A L M A P L 12 2520 161 P L P V F I K Q L 12 2521 182 C L H Q D V M K L 12 2522 183 L H Q D V M K L A 12 2523 204 I V I I S A I G L 12 2524 217 I S F S Y L L I L 12 2525 223 L I L K T V L G L 12 2526 276 V I L A N I Y L L 12 2527 38 Y L I A V L G N L 11 2528 50 Y I V R T E H S L 11 2529 94 T I Q F ) A C L L 11 2530 102 L Q I F A I H S L 11 2531 130 C H P L R H A T V 11 2532 134 R H A T V L T L P 11 2533 178 S H S Y C L H Q D 11 2534 208 S A I G L D S L L 11 2535 258 I G L S M V H R F 11 2536 Table XXIX - 101P3A11 v2 HLA B1510 - 9-mere Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 6 A V L A S G V T L 13 2537 21 P I S I C W F L L 11 2538 20 W P I S I C W F L 10 2539 26 W F L L C S T Q L 10 2540 19 S W P I S I C W F 7 2541 28 L L C S T QL S M 6 2542 Table XXIX - 101P3A11 v3 HLA B1510 9-mers Pos 123456789 score SEQ ID 7 L Q M F A I H S L 11 2543 2 F D A C L L Q M F 7 2544 1 Q F D A C L L Q M 6 2545 196 __________ -Table XXX - l1P3A11 vi. HLA-B2705 9-niers Pos 123 4 56 7 89 score SEQ ID 195 1R VN VV Y GL 25 2546 269 RR D S P LPV1 24 2547 133 L RHA TV L TL 23 2548 301 -1R 0R IL RL F 23 2549 306 LR LF HV A TH 23 2550 232 T REA Q A KAF 21 2551 35 CS L YLI A VL 18 2552 300 E I RQRI L RL 18 2553 7 G NE SS AT YF 17 2554 67 C M LSGCI DIL 17 2555 163 P V F I KQLPF 17 2556 208 S AIG L DS LL 17 2557 211 GL DS LL I SF 17 2558 221 YL LI LK T VL 17 2559 238 KAF G T CV SH 17 2560 270 RD S PL P VIL 17; 2561 281 1IYL L VP PVL 17 2562 296 VK T KEI R QR 17 2563 12 AT YF IL I GL 16 2564 15 F I LIGL P GL 16 2565 22 G LEE AQ F WL 16 2566 26 AQ F WL AF PL 16 2567 38 Y LIA VL G NL 16 2568 93 T T IQ FD ACL 16 2569 102 LQI FA I HS L 16 2570 125 RYV A IC H PL 16 2571 131 H PLR HA T VL 16 2572 142 PR VT K I GVA 16 2573 154 RG A ALM A PL 16 2574 182 CL HQ D V MKL 16 2575 202 G L IVI I SAI1 16 2576 204 1V I I SA I GL 16 2577 217 1 S FS YL L IL 16 2578 223 L IL KTV L GL 16 2579 256 PF ICL S M VH 16 2580 258 1G LS MV H RF 16 2581 276 V IL A NI YLL 16* 2582 48 1 1 Y I V R T E H 15 2583 110 LS GM ES T VL 15 2584 115 ST VL LA M AF 15 2585 124 DR YV AI C HP 15 2586 146 KI GV A AV VR 15 2587 157 AL MA PL P VF 15 2588 169 L PFC RS N IL 15 2589 173 R S NI LS HSY 15 2590 199 V V YGL I VI I 15 2591 207 1S AI GL D SL 15 2592 230 GL T REA Q AK 15 2593 249 A V FI FY V PF 15 2594 252 1I FY V PFI GL 15 2595 275 P VIL A NI YL ___is 2596 291 PIV Y GV K TK 15 2597 299 KE I RQR I LR is 2598 20 L P GL E E AF 14 2599 30 -L AFP LC S LY 14 2600 197 Table XXX - lO1P3A11 v1. HLA-B2705 9-mers Pos -1 234 5 67 89 score SEQ ID 31 A FPLCSLYL 14 2601 40 1AVLGNLT1 14 2602 41 A V L G N L T I I 14 2603 80 S MPKMLAIF 14 2604 82_ PK ML A I FWF 14 2605 100 C L L FAI H 14 2606 138 VL TLPRVT K 14 2607 139 L TLPRVTK1 14 2608 151 AVVRGAAL M 14 2609 161 -P LPVFIKL 14 2610 175 NILSHSYC L 14 2611 181 Y C LHQDVMK 14 2612 193 DDIRVNVV Y 14 2613 213 D SLLISFSY 14 2614 214 SLL I SF S YL 14 2615 215 LL IS FS Y LL 14 2616 261 SMVHRFSK R 14 2617 264 HRFSKRRD S 14 2618 268 KRRDSPLP V 14 2619 294 YGVKTKEIR 14 2620 302 V R F K R LFH 14 2621 303 QRILRZFH V 14 2622 6 N GNESSATY 13 2623 24 EEAQFWLAF 13 2624 29 W LAF P LC SL 13 2625 45 N LTIIYIVR 13 2626 52 VRTEHSLH1E 3 2627 57 SLHEPMYIF 13 2628 61 P MYIFLCML 13 2629 73 DI LI S TS SM 13 2630 75 L IST SS M PK 13 2631 76 1ST S S MP KM 13 2632 99 ACL L QI FAI1 13 2633 105 F AI HS L SGM 13 2634 ill S GME ST V LL 13 2635 117 V LL A MA FDR 13 2636 127 V AIC HP L RH 13 2637 150 -A AVV R GA AL 13 2638 159 M A PL P VF IK 13 2639 165 F I KQL PF CR 13 2640 171 FC RS NI LS H 13 2641 172 CR S NI L SHS 13 2642 188 M KL AC D DIR 13 2643 218 A FS YL L I LK 13 2644 225 L KT VLG L TR 13 2645 243 C VS HVC A VF 13 2646 257 FI G LSM V HR 13 2647 262 M VHR FS K RR 13 2648 50 YI VR T E HSL 12 2649 58 LH EP MY I FL 12 2650 89 WF N ST TI QF 12 2651 97 F DA CLL Q IF 12 2652 135 H ATV LT L PR 12 2653 153 V RG A AL MAP 12 2 6 54 180 S YC LH Q D VM 12 2655 198 Table XXX - 101P3A11 v1. HLA-B2705 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 198 N V V Y G L I V I 12 2656 245 S H V C A V F I F 12 2657 266 F S K R R D S P L 12 2658 274 L P V I L A N I Y 12 2659 286 P P V L N P I V Y 12 2660 289 L N P I V Y G V K 12 2661 297 K T K E I R Q R I 12 2662 298 T K E I R Q R I L 12 2663 Table XXX - 101P3A11 v2 HLA B2705 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 14 L R C P S S.W P I 20 2664 26 W F L L C S T Q L 17 2665 6 A V L A S G V T L 16 2666 7 V L A S G V T L R 15 2667 19 S W P I S I C W F 14 2668 20 W P I S I C W F L 14 2669 28 L L C S T Q L S M 12 2670 21 P I S I C W F L L 10 2671 Table XXX - 101P3A11 v3 HLA B2705 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 7 L Q M F A I H S L 14 2672 5 C L L Q M F A I H 13 2673 2 F D A C L L Q M F 12 2674 1 Q F D A C L L Q M 11 2675 4 A C L L Q M F A I 10 2676 Table XXXI - 101P3A11 v1. HLA-B2709 9-mers POS 1 2 3 4 5 6 7 8 9 score SEQ ID 195 I R V N V V Y G L 24 2677 269 R R D S P L P V I 24 2678 133 L R H A T V L T L 22 2679 268 K R R D S P L P V 21 2680 301 I R Q R I L R L F 20 2681 232 T R E A Q A K A F 19 2682 303 Q R I L R L F H V 19 2683 125 R Y V A I C H P L 16 2684 270 R -D S P L P V I L 16 2685 44 G N L T I I Y I V 15 2686 217 I S F S Y L L I L 15 2687 12 A T Y F I L I G L 14 2688 26 A Q F W L A F P L 14 2689 154 R G A A L M A P L 14 2690 199 Table XXXI - lOlP3A11 V2. HLA-B2709 9-mers Pos 1234567819 score SEQID 175 N ILS HS Y CL 14 2691 223 L I LK T VLGL 14 2692 258 1,G LS MV H RF 14 2693 281 1IY LL VP P VL 14 2694 7 G NE SSA T YF 13 2695 15 F ILIGLPGL 13 2696 22 G L EE AQF WL 13 2697 67 C MIsS G ID IL 13 2698 131 H PLR H AT VL 13 2699 202 G L IVI I SAI1 13 2700 204 1V I I S A IGL 13 2701 215 L LI SF S YLL 13 2702 252 1IFYV P FI GL 13 2703 264 H R FSK R R DS 13 2704 276 V ILANIYLL 13 2705 306 LR LF HV A TH 13 2706 31 AF PL CS L YL 12 2707 35 C S L Y L I A V L 12 2708 38 Y L I A V LGN L 12 2709 52 V R T E H S L H E 12 2710 61 P MYI FL C ML 12 2711 76 1S T S S M PK M 12 2712 94 T1FDACL L 12 2713 124 DRY V AI C HP 12 2714 136 ATVLTLPRV 12 2715 139 V F I F V K 12 2716 150 AAVVRGAAL 12 2717 156 A A L M AP L P V 12 2718 169 P F C RS N L I 12 2719 182 CL HQ DV M KL 12 2720 189 KL AC DD I RV 12 2721 191 AC D DI RV NV 12 2722 196 V Y G L 12 2723 211 L D S L L I SF 12 2724 214 SLIISFSYL 12 2725 221 T S S K VL 12 2726 249 AVFIFYVPF 12 2727 280 NIYLLVPPV 12 2728 288 V L N P IVY G V 12 2729 297 KT KE I RQRI1 12 2730 300 E IR Q RI LRL 12 2731 32 F P L C SL11 2732 40 1A V L G N LT 2 11 002733 41 A V L NL TII1 11 _ __2734 5o YI V RTE H SL 11 _ __2735 58 ELHE PM YI FL 11___ 2736 64 1IF LC ML SG1 11 _ __2737 77 S TS S MP K ML 11 ____2738 93 T T IQ(PD AC L 11___ __ 2739 99 A C L LQ1F A 1 11 __ 2740__ __ _ 102 L Q IF AI H SL 11___ 2741 ill SG ME ST V LL 11 _ __2742 121 M AF DRY VAI1 11 2743 142 pR VT KI G VA 11 _ __2744 151 AV V RG AA LM 11 _ __2745 200 Table XXXI - 101P3A11 v1. HLA-B2709 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 161 P L P V F I K Q L 11 2746 163 P.V F I K Q L P F 11 2747 172 C R S N I, L S H S 11 2748 199 V V Y G L I V I I 11 2749 207 I S A I G L D S L 11 2750 208 S A I G L D S L L 11 2751 209 A I G L D S L L I 11 2752 220 S Y L L I L K T V 11 2753 242 T C V S H V C A V 11 2754 250 V F I P Y V P F I 11 2755 275 P V I L A N I Y L 11 2756 277 I L A N I Y L L V 11 2757 Table XXXI - 1O1P3A11 v2 HLA B2709 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 14 L R C P S S W P I 19 2758 6 A V L A S G V T L 14 2759 20 W P I S I C W F L 13 2760 26 W F L L C S T Q L 13 2761 21 P I S I C W F L L 10 2762 28 L L C S T Q L S M 10 2763 4 L I A V L A S G V 9 2764 16 C P S S W P I S I 9 2765 Table XXXI - 101P3A11 v3 HLA B2709 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 4 A C L L Q M F A I 11 2766 1 Q F D A C L L Q M 10 2767 7 L Q M F A I H S L 10 2768 2 F D A C L L Q M F 8 2769 Table XXXII - 1O1P3A11 vI. HLA-B4402 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 24 E E A Q F W L A F 25 2770 8 N E S S A T Y F I 21 2771 99 A C L L Q I F A I 18 2772 299 K E I R 0 R I L R 18 2773 102 L Q I F A I H S L 17 2774 161 P L P V F I K Q L 17 2775 202 G L I V I I S A I 17 2776 300 E I R Q R I L R L 17 2777 12 A T Y F I L I G L 16 2778 26 A Q F W L A F P L 16 2779 30 L A F P L C S L Y 16 2780 31 A F P L C S L Y L 16 2781 79 S S M P K M L A I 16 2782 113 M E S T V L L A M 16 2783 150 A A V V R G A A L 16 2784 157 A L M A P L P V F 16 2785 193 D D I R V N V V Y 16 2786 208 S A I G L D S L L 16 2787 249 A V F I F Y V P F 16 2788 201 Table XXXII - 1O1P3All vi. HLA-B4402 9-mers Poe 1 2 3 4 5 6 78 9 score SEQID 270 R D S P L PVI L 16 2789 276 V I L A N I YIL L16 2790 35 CSLYLIAVL 15 2791 41 AVLGINLTII 15 2792 59 HEPMYIFLC 15 2793 77 STSSMPKML s15 2794 82P K M L A I F W F 15 2795 ill SGMESTVL L 15 2796 115S T V L L A M A F 2797 121 MA FDRYVA1 15 2798 139L T L P R V T K I 2799 204 V I I S A I G L 15 2800 232 TREAQAKA F 15 2801 275 PVILANIYL 15 2802 286P P V L N P I V Y 15 2803 301 1R QRILRLF 15 2804 38Y L I A V L G N L 14 2805 55 EHSLHEPMY 14 2806 58 LHEPMYIFL 14 2807 67 C M L S G I D I L 14 2808 131H P L R H A T V L 14 2809 169 LPFCRSNIL 14 2810 209 AIGLDSLL 14 2811 215 LLISFSYLL 14 2812 217 I S F S Y L L I L 14 2813 281 1YLLVPPVL 14 2814 284L V P P V L N P I 14 2815 9 - ESSATYFIL 13 2816 10 S S A T Y F I L I 13 2817 42 VLGNLTIIY 13 2818 43 LGNLTIIY 13 2819 68 MLSGIDIL 13 2820 80 S M P K M L A I F 13 2821 89 W F N S T T I Q F 13 2822 93 T T I Q F D A C L 13 2823 133 LRHATVLTL 13 2824 158 LMA PLPVF 113 2825 163 PVFIKQLPF 13 2826 199 V V Y G L I V I I 13 2827 211G L D S L L I S F 13 2828 213 D S L L I S F S Y 13 2829 214 S L L I S F S Y L 13 2830 223L I L K T V L G L 13 2831 258 G L S M V H R F 13 2832 6N G N E S S A T Y 12 2833 15 F I L I G LPG L 12 2834 20 LPGLEEAQF 12 2835 21P G L E E A Q F W 12 2836 23 L E E A Q F W L A 12 2837 50 Y I V R T E H S L 12 2838 81 MPKMLAIFW 12 2839 94T I Q F D A C L L 12 2840 96 QF D A C L L Q I 12 2841 125R Y V A I C H P L 12 2842 175 N I L S H S Y C L 12 2843 202 Table XXXII - 101P3A11 v1. HLA-B4402 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 182 C L H Q D V M K L 12 2844 195 I R V N V V Y G L 12 2845 198 N V V Y G L I V I 12 2846 221 Y L L I L K T V L 12 2847 243 C V S H V C A V F 12 2848 245 S H V C A V F I F 12 2849 246 H V C A V F I F Y 12 2850 250 V F I F Y V P F I 12 2851 252 I F Y V P F I G L 12 2852 266 F S K R R D S P L 12 2853 274 L P V I L A N I Y 12 2854 298 T K E I R Q R I L 12 2855 Table XXXII - 101P3A11 v2 HLA B4402 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 6 A V L A S G V T L 16 2856 18 S S W P I S I C W 16 2857 19 S W P I S I C W F 15 2858 20 W P I S I C W F L 14 2859 12 V T L R C P S S W 13 2860 26 W F L L C S T Q L 13 2861 21 P I S I C W F L L 12 2862 14 L R C P S S W P I 11 2863 16 C P S S W P I S I 11 2864 Table XXXII - 101P3A11 v3 HLA B4402 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 4 A C L L Q M F A I 15 2865 7 L Q M F A I H S L 15 2866 2 F D A C L L Q M F 11 2867 Table XXXIII - 101P3A11 v1. HLA-B5101 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 40 I A V L G N L T I 26 2868 32 F P L C S L Y L I 25 2869 121 M A F D R Y V A I 24 2870 131 H P L R H A T V L 23 2871 119 L A M A F D R Y V 22 2872 141 L P R V T K I G V 22 2873 156 A A L M A P L P V 22 2874 43 L G N L T I I Y I 21 2875 255 V P F I G L S M V 21 2876 285 V P P V L N P I V 21 2877 169 L P F C R S N I L 20 2878 236 Q A K A F G T C V 20 2879 139 L T L P R V T K I 19 2880 160 A P L P V F I K Q 18 2881 190 L A C D D I R V N 18 2882 199 V V Y G L I V I I 18 2883 278 L A N I Y L L V P 18 2884 208 S A I G L D S L L 17 2885 284 L V P P V L N P I 17 2886 203 Table XXXIII - lO1P3Al1 vi. HLA-B5101 9-mers Pos 1 234 56 7 89 score SEQ ID 64 1IF LC ML SG1 16 2887 87 1IFW FN ST T 1i6 2888 ill SCM E S TV LL 16 2889 145 T KIG VA A VV 16 2890 150 AA VV R GA AL 16 2891 198 N VV YG L IV 1 16 2892 272 SPL PV I L AN 16 2893 281 1Y LL VP P VL 16 2894 4 D PN1G NE S SA 15 2895 41 A VL G NLTII1 15 2896 98 DAC LL Q I FA 15 2697 133 LRH A TV L TL 15 2898 223 LIL K TV L GL 15 2899 280 NI YL L V PPV 15 2900 286 P P VLNP IV Y 15 2901 290 NP IV Y GV KT 15 2902 10 SS AT YF ILI1 14 2903 66 LC ML S GIDI1 14 2904 85 LA I F WF NST 14 2905 127_ V AI CH P LRH 14 2906 158 LM A PLP VFI1 14 2907 159 M AP LPV F IK 14 2908 192 CD DI R V NVV 14 2909 201 Y G L I V I I S A 14 2910 210 1IG LD SL LIS 14 2911 216 L I S F S Y L L 1 14 2912 220 S Y L LI L KTV 14 2913 221 YL LI L KT VL 14 2914 238 KA FG TC V SH 14 2915 246 CA VF IF Y VP 14 2916 250 V FIFY V PF 1 14 2917 252 1IFY V PF IGL 14 2918 258 1G LS MV H RF 14 2919 269 RR DS PL PVI1 14 2920 274 L PV I LA NIY 14 i2921 30 LA FP LC S LY 13 2922 34 L CS LYL I AV 13 2923 56 HS L HEP MYI1 13 2924 68 M L S GID ILI1 13 2925 81 MP K M LAI FW 13 2926 96 QF D ACL LQI1 13 2927 99 AC L LQ1FAI1 13 2928 105 FA IH S LS GM 13 2929 147 1IG V AA V VR 13 2930 149 VA AV VR G AA 13 2931 154 R GAA L MA PL 13 2932 234 E AQA KA F GT 13 2933 244 VS H VC AVFI1 13 2934 293 V YGVK T KEI1 13 2935 297 KT K EI RQRI1 13 2936 6 N GNE SS A TY 12 2937 11 S AT Y FI LIG 12 2938 12 AT Y FI LI GL 12 2939 20 L PG L EE AQF 12 2940 35 C SL Y LI AVL 12 2941 204 Table XXXIII - 1O1P3A11 v1. HLA-B5101 9-mers Pos 1 2 3 4 5 6 7 8 9 score - SEQ ID 38 Y L I A V L G N L 12 2942 44 G N L T I I Y I V 12 2943 60 E P M Y I F L C M 12 2944 79 S S M P K M L A I 12 2945 109 S L S G M E S T V 12 2946 110 L S G M E S T V L 12 2947 155 G A A L M A P L P 12 2948 162 L P V F I K Q L P 12 2949 179 H S Y C L H Q D V 12 2950 195 I R V N V V Y G L 12 2951 196 R V N V V Y G L I 12 2952 217 I S F S Y L L I L 12 2953 239 A F G T C V S H V 12 2954 240 F G T C V S H V C 12 2955 268 K R R D S P L P V 12 2956 273 P L P V I L A N I 12 2957 292 I V Y G V K T K E 12 2958 Table XXXIII - 1O1P3A1I v2 HLA B5101 - 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 16 C P S S W P I S I 22 2959 8 L A S G V T L R C 17 2960 20 W P I S I C W F L 16 2961 5 I A V L A S G V T 15 2962 6 A V L A S G V T L 13 2963 14 L R C P S S W P I 13 2964 4 L I A V L A S G V 11 2965 Table XXXIII - 101P3A11 v3 HLA B5101 9-mers Pos 1 2 3 4 5 6 7 8 9 score SEQ ID 3 D A C L L Q M F A 14 2966 4 A C L L Q M F A I 12 2967 7 L Q M F A I H S L 9 2968 Table XXXIV - 101P3A11 v1. HLA-Al 10-mers Poo 1 2 3 4 5 6 7 8 9 0 score SEQ ID 192 C D D I R V N V V Y 27 245 S H V C A V F I F Y 24 2969 41 A V L G N L T II Y 21 2970 285 V P P V L N P I V Y 21 2971 117 V L L A M A F D R Y 20 2972 29 W L A F P L C S L Y 18 2973 298 T K E I R Q R I LR 17 2974 22 G L E E A Q F W L A 16 2975 23 L E E A Q F W L A F 16 2976 53 R T E H S L H E P M 16 2977 54 T E H S L H E P M Y 16 2978 58 L H E P M Y I F L C 16 2979 112 G M E S T V L L A M 16 2980 273 P L P V I L A N I Y 16 2981 2 M V D P N G N E SS 15 2982 205 Table XXXIV - 101P3A11 v1. HLA-Al 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 5 P N G N E S S A T Y 15 2983 122 A F D R Y V A I C H 15 2984 172 C R S N I L S H S Y 15 2985 212 L D S L L I S F S Y 15 2986 9 E S S A T Y PI LI 13 2987 191 A C D D I R V N V V 13 2988 Table XXXIV - 101P3A11 v2 - HLA Al 10-meres Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 22 P I S I C W F L L C 11 2989 2 S L Y L I A V L A S 10 2990 19 S S W P I S I C W F 10 2991 23 I S I C W F L L C S 10 2992 8 V L A S G V T L R C 8 2993 18 P S S W P I S I C w 8 2994 28 F L L C S T Q L S M 8 2995 13 V T L R C P S S W P 7 2996 1 C S L Y L I A V L A 6 2997 10 A S G V T L R C P S 6 2998 Table XXXIV - 101P3A11 v3 HLA Al 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 2 Q F D A C L L Q M F 11 2999 S1 F D A C L L Q M 6 3000 9 Q M F A I H S L S G 6 3001 6 C L L Q M F A I H S 5 3002 Table XXXV - 101P3AI1 v1. HLA-A0201 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 222 L L I L K T V L G L 30 3003 101 L L Q I F A I H S L 29 3004 283 L L V P P V L N P I 27 3005 206 II S A I G L D S L 26- 3006 214 S L L I S F S Y L L 25 3007 57 S L H E P M Y I F L 24 3008 63 Y I F L C M L S G I 24 3009 109 S L S G M E S T V L 24 3010 118 L L A M A F D R Y V 24 3011 132 P L R H A T V L T L 24 3012 138 V L T L P R V T K I 24 3013 216 L I S F S Y L L I L 24 3014 39 L I A V L G N L T I 23 3015 42 V L G N L T I I Y I 23 3016 157 A L M A P L P V F I 23 3017 194 D I R V N V V Y G L 23 3018 206 _________ Table XXXV - 101P3A11 vI. HLA-A0201 10-mers ________ Pos -12 34 5 67 890 score SEQ ID 215 L L I S F S Y L L 1 23 3019 33 P L CS L YL IAV 22 3020 120 A MA FD RY VAI1 22 3021 238 K AF G TC V SHV 22 3022 276 V IL AN IY LL V 22 3023 86 A IF WF NS TTI1 21 3024 140 T LP RV TK IG V 21 3025 203 L I VI IS AI GL 21 3026 14 Y FI L IG L PGL 20 3027 17 L IG LP GL E EA 20 3028 30 L AF PL CS L YL 20 3029 143 R VT KI GV A AV 20 3030 149 V AA V VRG A AL 20 168 Q LP FC R SN IL 20 3031 181 Y C LH QD V MKL 20 3032 223 1IL KT VL G LT 20 3033 241 G TC VS HV C AV 20 3034 249 A VFI F YV PFI1 20 3035 251. F I FYV P FIGL 20 3036 272 S PL PV IL ANI1 20 3037 280 N IY LL V PP VL 20 3038 305 1ILR LF HV A TH 20 3039 11 S AT Y FIL I GL 19 ___3040 16 1ILI G L PGL EE 19 __3041 28 FW LA FP L CS L 19 3042 36 IS LY LI AV LGN 19 3043 38 Y LI AV L G NLT 19 304 45 NL T II YI V RT 19 3045 65 F L C MLS GIDI1 19 3046 84 M L A IFWF N ST 19 3047 160 A PLP V FI K QL 19 3048 190 L A CD DIR VN V 19 3049 208 -S AI G L D SLL 1___ 19 3050 254 Y VP FI GL S MV 19 3051 277 1ILA N IY L LVP 19 3052 282 Y LL VP P VLN P 19 3053 284 L VP PV LN P IV 19 3054 287 P VL N PIV Y GV 19 3055 34 LC S L YLI A VL 18 3056 37 L Y LI A VL GNL 18 3057 40 '1A V LG NLTI I 18i 3058 43 L G NLT I IYI V 18 3059 67 C M LSG ID ILI1 18 3060 112 G ME ST V LL AM 18 3061 129 1C H PL R H ATV 18 3062 135 H A TVL TL P RV 18 3063 155 G AA LM A PL PV 18 3064 158 IL MAP L PV FIK 18 3065 191 A CD DI RV N VV 18 3066 230 G LT RE AQ A KA ___i 3067 246 H VC A VF IF YV 18 3068 275 P V IL A NI YLL 18 3069 279 A NI YL LV P PV 18 3070 292 1IV Y GV KT K E 18 3071 299 K E I RQR IL RL 18 3072 207 Table XXXV - 1O1P3A11 vI. HLA-A0201 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 49 I Y I V R T E H S L 17 3073 66 L C M L S G I D I L 17 3074 68 M L S G I D I L I S 17 3075 75 L I S T S S M P K M 17 3076 92 S T T I Q F D A C L 17 3077 95 I Q F D A C L L Q I 17 3078 189 K L A C D D I R V N 17 3079 198 N V V Y G L I V I I 17 3080 201 Y G L I V I I S A I 17 3081 219 F S Y L L I L K T V 17 3082 228 V L G L T R E A Q A 17 3083 304 R I L R L F R V A T 17 3084 22 G L E E A Q F W L A 16 3085 93 T T I Q F D A C L L 16 3086 98 D A C L L Q I F A I 16 3087 128 A I C H P L R H A T 16 3088 144 V T K I G V A A V V 16 3089 196 R V N V V Y G L I V 16 3090 221 Y L L I L K T V L G 16 3091 297 K T K E I R Q R I L 16 3092 19 G L P G L E E A Q F 15 3093 31 A F P L C S L Y L I 15 3094 127 V A I C H P L R H A 15 3095 146 K I G V A A V V R G 15 3096 174 S N I L S H S Y C L 15 3097 202 G L I V I I S A I G 15 3098 209 A I G L D S L L I S 15 3099 211 G L D S L L I S F S is 3100 268 K R R D S P L P V I 15 3101 46 L T I I Y I V R T E 14 3102 74 I L I S T S S M P K 14 3103 108 H S L S G M E S T V 14 3104 110 L S G M E S T V L L 14 3105 111 S G M E S T V L L A 14 3106 207 I S A I G L D S L L 14 3107 220 S Y L L I L K T V L 14 3108 224 I L K T V L G L T R 14 3109 235 A Q A K A F G T C V 14 3110 243 C V S H V C A V F I 14 3111 257 F I G L S M V H R F 14 3112 288 V L N P I V Y G V K 14 3113 302 R Q R I L R L F H V 14 3114 Table XXXV - 1O1P3A11 V2 - HLA A0201 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 4 Y L I A V L A S G V 25 3115 6 I A V L A S G V T L 20 3116 24 S I C W F L L C S T 20 3117 28 F L L C S T Q L S M 20 3118 2 S L Y L I A V L A S 19 3119 14 T L R C P S S W P I 18 3120 5 L I A V L A S G V T 16 3121 29 L L C S T Q L S M E 16 3122 208 Table XXXV - 101P3A11 v2 - HLA A0201 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 8 V L A S G V T L R C 14 3123 3 L Y L I A V L A S G 12 3124 7 A V L A S G V T L R 12 3125 9 L A S G V T L R C P 12 3126 20 S W P I S I C W F L 12 3127 21 W P I S I C W F L L 12 3128 Table XXXV 101P3A11 v3 HLA A0201 10-mers Pos 1 2 3 4 5 67890 score SEQ ID 7 L L Q M F A I H S L 29 3129 Table XXXVI - 101P3A11 v1. HLA-A0203 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 142 P R V T K I G V A A 19 3130 148 G V A A V V R G A A 19 3131 113 M E S T V L L A M A 18 3132 228 V L G L T R E A Q A 18 3133 230 G L T R E A Q A K A 18 3134 143 R V T K I G V A A V 17 3135 149 V A A V V R G A A L 17 3136 3 V D P N G N E S S A 10 3137 17 L I G L P G L E E A 10 3138 22 G L E E A Q F W L A 10 3139 32 F P L C S L Y L I A 10 3140 77 S T S S M P K M L A 10 3141 90 F N S T T I Q F D A 10 3142 97 F D A C L L Q I F A 10 3143 111 S G M E S T V L L A 10 3144 119 L A M A F D R Y V A 10 3145 127 V A I C H P L R H A 10 3146 141 L P R V T K I G V A 10 3147 147 I G V A A V V R G A 10 3148 151 A V V R G A A L M A 10 3149 182 C L H Q D V M K L A 10 3150 200 V Y G L I V I I S A 10 3151 226 K T V L G L T R E A 10 3152 240 F G T C V S H V C A 10 3153 270 R D S P L P V I L A 10 3154 303 Q R I L R L F H V A 10 3155 306 L R L F H V A T H A 10 3156 4 D P N G N E S S A T 9 3157 18 I G L P G L E E A Q 9 3158 23 L E E A Q0F W L A F 9 3159 33 P L C S L Y L I A V 9 3160 78 T S S M P K M L A I 9 3161 209 Table XXXVI - 101P3A11 v1. HLA-A0203 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 91 N S T T I Q F D A C 9 3162 98 D A C L L Q I F A I 9 3163 112 G M E S T V L L A M 9 3164 114 E S T V L L A M A F 9 3165 120 A M A F D R Y V A I 9 3166 128 A I C H P L R H A T 9 3167 152 V V R G A A L M A P 9 3168 183 L H Q D V M K L A C 9 3169 201 Y G L I V I I S A I 9 3170 227 T V L G L T R E A O 9 3171 229 L G L T R E A Q A K 9 3172 231 L T R E A Q A K A F 9 3173 241 G T C V S H V C A V 9 3174 271 D S P L P V I L A N 9 3175 304 R I L R L F H V A T 9 3176 307 R L F H V A T H A S 9 3177 Table XXXVI - 101P3A11 v2 - HLA A0203 10-mers Poo 1 2 3 4 5 6 7 8 9 0 score SEQ ID 1 C S L Y L I A V L A 10 3178 2S L Y L I A V L A S 9 3179 3 L Y L I A V L A S G 8 3180 Table XXXVI - 101P3A11 v3 HLA A0203 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 3 F D A C L L O M F A 10 3181 4 D A C L L Q M F A I 9 3182 5 A C L L Q M F A I H 8 3183 Table XXXVII - 101P3A11 v1. HLA-A3 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 137 T V L T L P R V T K 31 3184 288 V L N P I V Y G V K 28 3185 224 I L K T V L G L T R 27 3186 305 I L R L F H V A T H 27 3187 74 I L I S T S S M P K 26 3188 16 I L I G L P G L E E 23 3189 41 A V L G N L T I I Y 23 3190 151 A V V R G A A L M A 23 3191 259 G L S M V H R F S K 23 3192 19 G L P G L E E A Q F 22 3193 304 R I L R L F H V A T 22 3194 277 I L A N I Y L L V P 21 3195 29 WL A F P L C S L Y 20 3196 116 T V L L A M A F D R 20 3197 117 V L L A M A F D R Y 20 3198 126 Y V A I C H P L R H 20 3199 132 P L R H A T V L T L 20 3200 145 T K I G V A A V V R 20 3201 157 A L M A P L P V F I 20 3202 210 Table XXXVII - 101P3A11 v1. HLA-A3 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 196N V V Y G L I V 20 3203 36 S L Y L I A V L G N 19 3204 273 P L P V I L A N I Y 19 3205 38 Y L I A V L G N L T 18 3206 50 Y I V R T E H S L H 18 3207 51 I V R T E H S L H E 18 3208 109 S L S G M E S T V L 18 3209 143 R V T K I G V A A V 18 3210 189 K L A C D D I R V N 18 3211 280 N I Y L L V P P V L 18 3212 292 I V Y G V K T K E I 18 3213 295 G V K T K E I R Q R 18 3214 47 T I I Y I V R T E H 17 3215 103 Q I F A I H S L S G 17 3216 152 V V R G A A L M A P 17 3217 180 S Y C L H Q D V M K 17 3218 204 VI I S A I G L D 17 3219 205 V I I S A I G L D S 17 3220 221 Y L L I L K T V L G 17 3221 222 L L I L K T V L G L 17 3222 228 V L G L T R E A Q A 17 3223 243 C V S H V C A V F I 17 3224 290 N P I V Y G V K T K 17 3225 39 L I A V L G N L T I 16 3226 86 A I F W F N S T T I 16 3227 148 G V A A V V R G A A 16 3228 199 V V Y G L I V I I S 16 3229 202 G L I V I I S A I G 16 3230 215 L L I S F S Y L L I 16 3231 227 T V L G L T R E A Q 16 3232 229 L G L T R E A Q A K 16 3233 230 G L T R E A Q A K A 16 3234 2 M V D P N G N E S S 15 3235 45 N L T I I Y I V R T 15 3236 48 II Y I V R T E H S 15 3237 68 M L S G I D I L I S 15 3238 73 D I L I S T S S M P 15 3239 100 C L L Q I F A I H S 15 3240 106 A I H S L S G M E S 15 3241 X46 K I G V A A V V R G 15 3242 176 I L S H S Y C L H Q 15 3243 192 C D D I R V N V V Y 15 3244 209 A I G L D S L L I S 15 3245 276 V I L A N I Y L L V 15 3246 282 Y L L V P P V L N P 15 3247 300 E I R Q R I L R L F 15 3248 307 R L F H V A T H A S 15 3249 Table XXXVII - 101P3A11 v2 - HLA A3 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 7 A V L A S G V T L R 22 3250 4 Y L I A V L A S G V 21 3251 2 S L Y L I A V L A S 20 3252 12 G V T L R C P S S W 17 3253 211 Table XXXVII - 1OlP3Al1 v2 - HLA A3 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 28 F L L C S T Q L S M 17 3254 5 L I A V L A S G V T 14 3255 6 I A V L A S G V T L 14 3256 8 V L A S G V T L R C 14 3257 29 L L C S T Q L S M E 14 3258 14 T L R C P S S W P I 13 3-259 22 P I S I C W F L L C 12 3260 24 S I C W F L L C S T 11 3261 Table XXXVII - Q1P3A11 v3 HLA A3 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 6 C L L Q M F A I H S 15 3262 5 A C L L Q M F A I H 13 3263 7 L L Q M F A I H S L 12 3264 S1 Q F D A C L L Q M 9 3265 2 Q F D A C L L Q M F 9 3266 9 Q M F A I H S L S G 9 3267 Table XXXVIII - 101P3A11 v1. HLA-A26 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 300 E I R Q R I L R L F 31 3268 194 D I R V N V V Y G L 29 3269 251 F I F Y V P F I G L 25 257 F I G L S M V H R F 25 3270 75 L I S T S S M P K M 24 3271 275 P V I L A N I Y L L 24 3272 19 G L P G L E E A Q F 23 3273 117 V L L A M A F D R Y 23 3274 206 I I S A I G L D S L 23 3275 222 L L I L K T V L G L 23 3276 231 L T R E A Q A K A F 23 3277 14 Y F I L I G L P G L 22 3278 41 A V L G N L T I I Y 22 3279 57 S L H E P M Y I F L 22 3280 96 Q F D A C L L Q I F 22 3281 216 L I S F S Y L L I L 22 3282 93 T T I Q F D A C L L 21 3283 101 L L Q I F A I H S L 21 3284 104 I F A I H S L S G M 21 3285 297 K T K E I R Q R I L 21 3286 29 W L A F P L C S L Y 20 3287 132 P L R H A T V L T L 20 3288 60 E P M Y I F L C M L 19 3289 92 S T T I Q F D A C L 19 3290 203 L I V I I S A I G L 19 3291 213 D S L L I S F S Y L 19 3292 273 P L P V I L A N I Y 19 3293 280 N I Y L L V P P V L 19 3294 53 R T E H S L H E P M 18 3295 63 Y I F L C M L S G I 18 3296 73 D I L I S T S S M P 18 3297 109 S L S G M E S T V L 18 3298 212 Table XXXVIII - 1O1P3A11 v1. HLA-A26 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 114 E S T V L L A M A F 18 3299 152 V V R G A A L M A P 18 3300 79 S S M P K M L A I F 17 3301 143 R V T K I G V A A V 17 3302 163 P V F I K Q L P F C 17 3303 165 F I K Q L P F C R S 17 3304 168 Q L P F C R S N I L 17 3305 186 D V M K L A C D D I 17 3306 249 A V F I F Y V P F I 17 3307 254 Y V P F I G L S M V 17 3308 46 L T I I Y I V R T E 16 3309 146 K I V A A V V R G 16 3310 199 V V Y G L I V I I S 16 3311 204 I V I I S A I G L D 16 3312 210 I G L D S L L I S F 16 3313 214 S L L I S F S Y L L 16 3314 256 P F I G L S M V H R 16 3315 265 R F S K R R D S P L 16 3316 295 G V K T K E I R Q R 16 .3317 17 L I G L P G L E E A 15 3318 81 M P K M L A I F W F 15 3319 115 S T V L L A M A F D 15 3320 156 A A L M A P L P V F 15 3321 160 A P L P V F I K Q L 15 3322 175 N I L S H S Y C L H 15 3323 198 N V V Y G L I VI I 15 3324 211 G L D S L L I S F S 15 3325 215 L L I S F S Y L L I 15 3326 223 L I L K T V L G L T 15 3327 241 G T C V S H V C A V 15 3328 248 C A V F I F Y V P F 15 3329 287 P V L N P I V Y G V 15 3330 299 K E I R Q R I L R L 15 3331 Table XXXVIII - 101P3A11 v2 - HLA A26 1C-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 28 F L L C S T Q L S M 17 3332 19 S S W P I S I C W F 16 3333 24 S I C W F L L C S T 15 3334 29 L L C S T Q L S M E 15 3335 7 A V L A S G V T L R 14 3336 22 P I S I C W F L L C 14 3337 2 S L Y L I A V L A S 13 3338 4 Y L I A V L A S G V 12 3339 12 G V T L R C P S S W 12 3340 s L I A V L A S G V T 11 3341 V L A S G V T L R C 11 3342 13 V T L R C P S S W P 11 3343 21 W P I S I C W F L L 11 3344 26 C W F L L C S T Q L 11 3345 6 I A V L A S G V T L 9 3346 20 S W P I S I C W F L 9 3347 14 T L R C P S S W P I 8 3348 213 Table XXXVIII - 101P3A11 v3 HLA A26 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 2 Q F D A C L L Q M F 23 3349 7 L L Q M F A I H S L 21 3350 10 M F A I H S L S G M 21 3351 S1 F D A C L L Q M 16 3352 4 D A C L L Q M F A I 11 3353 Table XXXIX - 101P3A11 v1. HLA-B0702 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 160 A P L P V F I K Q L 23 3354 60 E P M Y I F L C M L 22 3355 274 L P V I L A N I Y L 20 3356 4 D P N G N E S S A T 19 3357 131 H P L R H A T V L T 19 3358 141 L P R V T K I G V A 19 3359 162 L P V F I K Q L P F 19 3360 32 F P L C S L Y L I A 18 3361 272 S P L P V I L A N I 18 3362 81 M P K M L A I F W F 16 3363 109 S L S G M E S T V L 16 3364 132 P L R H A T V L T L 15 3365 265 R F S K R R D S P L 15 3366 34 L C S L Y L I A V L 14 3367 110 L S G M E S T V L L 14 3368 153 V R G A A L M A P L 14 3369 206 II S A I G L D S L 14 3370 216 L I S F S Y L L I L 14 3371 269 R R D S P L P V I L 14 3372 30 L A F P L C S L Y L 13 3373 149 V A A V V R G A A L 13 3374 157 A L M A P L P V F I 13 3375 194 D I R V N V V Y G L 13 3376 222 L L I L K T V L G L 13 3377 299 K E I R Q R I L R L 13 3378 8 N E S S A T Y F I L 12 3379 20 L P G L E E A Q F W 12 3380 25 E A Q F W L A F P L 12 3381 120 A M A F D R Y V A I 12 3382 130 C H P L R H A T V L 12 3383 207 I S A I G L D S L L 12 3384 220 S Y L L I L K T V L 12 3385 280 N I Y L L V P P V L 12 3386 286 P P V L N P I V Y G 12 3387 9 E S S A T Y F I L I 11 3388 14 Y F I L I G L P G L 11 3389 28 F W L A F P L C S L 11 3390 49 I Y I V R T E H S L 11 3391 57 S L H E P M Y I F L 11 3392 66 L C M L S G I D I L 11 3393 76 I S T S S M P K M L 11 3394 78 T S S M P K M L A I 11 3395 92 S T T I Q F D A C L 11 3396 214 Table XXXIX - lO1P3A11 v1. HLA-B0702 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 124 D R Y V A I C H P L 11 3397 143 R V T K I G V A A V 11 3398 181 Y C L H Q D V M K L 11 3399 191 A C D D I R V N V V 3400 213 D S L L I S F S Y L 11 3401 235 A Q A K A F G T C V 11 3402 243 C V S H V C A V F I 11 3403 249 A V F I F Y V P F I 11 3404 251 F I F Y V P F I G L 11 3405 255 V P F I G L S M V H 11 3406 267 S K R R D S P L P V 11 3407 268 K R R D S P L P V I 11 3408 270 R D S P L P V I L A 11 3409 279 A N I Y L L V P P V 11 3410 285 V P P V L N P I V Y 11 3411 290 N P I V Y G V K T K 11 3412 297 K T K E I R Q R I L 11 3413 Table XXXIX - 1O1P3A11 v2 - HLA B0702 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 21 W P I S I C W F L L 20 3414 6 I A V L A S G V T L 13 3415 17 C P S S W P I S I C 12 3416 20 S W P I S I C W F L 11 3417 26 C W F L L C S T Q L 11 3418 14 T L R C P S S W P I 9 3419 Table XXXIX - 1O1P3A11 v3 HLA B0702 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 7 L L Q M F A I H S L 10 3420 S1 Q F D A C L L Q M 9 3421 2 Q F D A C L L Q M F 8 3422 3 F D A C L L Q M F A 8 3423 4 D A C L L Q M F A I 7 3424 10 M F A I H S L S G M 7 3425 5 A C L L Q M F A I H 4 3426 Table XL- 1O1P3A11 V1-HLA B08 10-mers No Results. Table XL- 101P3A11 V2-HLA B08 10-mers No Results. Table XL- 101P3A11 V3-HLA B08 10-mers No Results. Table XLI - 1O1P3Al1 vI - HLA B1510 10-mers No results. Table XLI - 1O1P3A11 v2 - HLA B1510 10-mers No results. Table XLI - 101P3A11 v3 HLA B1510 10-mers No results. Table XLII - 1O1P3A11 v1 - HLA B2705 10-mers No results. Table XLII - 1O1P3A11 v2 - HLA B2705 10-mers No results. 215 11- IL. e. U :' U / L*. "7-.- rlI:Ul Table XLII - O1P3A11 v3 HLA B2705 10-mers No results. Table XLIII - 101P3A11 vi - HLA B2709 10-mers No results. Table XLIII - 101P3A11 v2 - HLA B2709 10-mers No results. Table XLIII - 101P3A11 v3 HLA B2709 10-mers No results. Table XLIV - 101P3A11 v1. HLA-B4402 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ. ID No. 299 K E I R Q R I L R L 29 3427 23 L E E A Q F W L A F 23 3428 160 A P L P V F I K Q L -23 3429 8 N E S S A T Y F I L 22 3430 54 T E H S L H E P M Y 20 3431 275 P V I L A N I Y L L 18 3432 41 A V L G N L T I I Y 17 3433 30 L'A F P L C S L Y L 16 3434 34 L C S L Y L I A V L 16 3435 79 S S M P K M L A I F 16 3436 88 F W F N S T T IQ F 16 3437 156 A A L M A P L P V F 16 3438 222 L L I L K T V L G L 16 3439 14 Y F I L I G L P G L 15 3440 31 A F P L C S L Y L I 15 3441 66 L C M L S G I D I L 15 3442 93 T T I Q F D A C L L 15 3443 114 E S T V L L A M A F 15 3444 174 S N I L S H S Y C L 15 3445 208 S A I G L D S L L I 15 3446 231 L T R E A Q A K A F 15 3447 300 E I R Q R I L R L F 15 3448 9 E S S A T Y F I L I 14 3449 49 I Y I V R T E H S L 14 3450 60 E P M Y I F L C M L 14 3451 80 S M P K M L A I F W 14 3452 86 A I F W F N S T T I 14 3453 95 I Q F D A C L L Q0I 14 3454 98 D A C L L Q I F A I 14 3455 101 L L Q I F A I H S L 14 3456 109 S L S G M E S T V L 14 3457 120 A M A F D R Y V A I 14 3458 130 C H P L R H A T V L 14 3459 157 A L M A P L P V F I 14 3460 167 K Q L P F C R S N I 14 3461 201 Y G L I V I I S A I 14 3462 210 I G L D S L L I S F 14 3463 220 S Y L L I L K T V L 14 3464 249 A V F I F Y V P F I 14 3465 251 F I F Y V P F I G L 14 3466 272. S P L P V I L A N I 14 3467 280 N I Y L L V P P V L 14 3468 285 V P P V L N P I V Y 14 3469 216 Table XLIV - 1O1P3A11 v2 - HLA B4402 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 19 S S W P I S I C W F 17 3470 21 W P I S I C W F L L 14 3471 26 C W F L L C S T Q L 14 3472 6 I A V L A S G V T L 13 3473 12 G V T L R C P S S W 12 3474 18 P S S W P I S I C W 12 3475 20 S W P I S I C W F L 12 3476 16 R C P S S W P I S I 11 3477 14 T L R C P S S W P I 8 3478 Table XLIV - 101P3A11 v3 HLA B4402 10-mers Pos 1 2 3 4 5 6 7 8 9 0 score SEQ ID 7 L L Q M F A I H S L 14 3479 2 Q F D A C L L Q M F 12 3480 4 D A C L L Q M F A I 11 3481 1 I Q F D A C L L Q M 6 3482 5 A C L L Q M F A I H 6 3483 Table XLV - 101P3A11 vi - HLA B5101 10-mers No Results Table XLV - 101P3A11 v2 - HLA B5101 10-mers No Results Table XLV - 101P3A11 v3 HLA B5101 10-mers No results. 217 Table XLVI - 101P3All vl. DRB-0101 15-mers Pos 12 34 56 7 890 1 234 5 score SEQI11 201 Y GLIV I IS A IG L DSL 36 3484 69 L S G ID I LI S TS SMPK 34 3485 63 YI FL CM LS GI D IL IS 33 3486 104 1IFAI HS LS GM E S TVL 32 3487 46 LT II YI V RTE HS L HE 31 3488 194 DI RV NV VY G LIV II S 31 3489 278 L A NI YLL VP PVL NP 1 31 3490 98 D AC LL QI FAI HS L SG 30 3491 107 1H SL SG ME ST VL L AM 30. 3492 241 GT C VSH VCA V FI F YV 30 3493 11 SA TY F ILI GL PG L EE 29 3494 290 NP IV YG V KTK E I RQR 29 3495 12 AT Y FI L IG LP G LEEA 28 3496 251 F IFY V PF IGL SM V HR 27 3497 14.1 LP RVT K IG VA AV V RG 26 3498 184 HOQDV M KLA CD DI R VN 26 3499 218 SF S YLL IL KT VL G LT 26 3500 17 LI GLP G LE E AQF W LA 25 3501 25 EA QF WL AF PL CS L YL 25 3502 37 LY LI A VLG NL T I IY1 25 3503 71 GI D ILIS T SS M PK ML 25 3504 112 G M ES TV LLA MA F DRY 25 3505 149 VA AV VR GA AL MA PL P 25 3506 163 PV F I KQL PF C R SNIL 25 3507 198 N VV Y G LIVI IS AI G L 25 3508 212 LD S LL IS FSY LL I LK 25 3509 219 F SY LLI L KT VL GL TR 25 3510 14 Y F IL IGL PG L EE AQF 24 3511 31' A FP LC S LY LIA V LGN 24 3512 40 1IAV LG NL TI I YI VRT 24 3513 78 T SS M PKM LA I F W F S 24 3514 86 AI F WF NS T TI0F DA C 24 3515 138 VL TL P RVT K IGV A AV 24 3516 152 VV R GAA L MA PL PVFI1 24 3517 162 L PVF I KQL PF CR SNI1 24 3518 197 V NV VY G L IVII S A IG 24 3519 203 LI VI I S AI GL DS LLI1 24 3520 209 AI G LDS L LIS F SY LL 24 3521 249 A VFI FYV P FI GL SM V 24 3522 252 1FY V PF IG LS MV H RF 24 3523 84 N L A I F W F N S T T I Q F D 23 3524 102 L QI FA IH SL SG M EST 23 3525 166 1IKQL PF CR S NIL SH S 23 3526 204 1V I I SA IG LD SL L IS 23 3527 222 LL IL KT VL G L TRE AQ 23 3528 279 A NI YL L VP PV LN PIV 23 3529 28 FW L A FPLC SL YL I AV 22 3530 36 SY L IA VL G NLT II Y 22 3531 62 M YIF LC M LS G IDILI1 22 3532 66 LC ML SG I DI LI ST SS 22 3533 81 M PKM LA I F W NS TTI1 22 3534 146 KI GV A AV VRG AA L MA 22 3535 218 -Table XLVI - 1lP3A11 vI. DRB-0101 15-mers Poe 1 234 56 78 9 012 34 5 score SEQ ID 147 1G VA AV V RGA A L MAP 22 3536 155 GAA L MA PL PV F IKQ L 22 3537 206 1I1SA IG LD SL L ISF S 22 3538 244 vS H VC AV F IF YV PF1 22 3539 271 DS P LP VIL AN I YL LV 22 3540 275 P VIL AN IY LL V P PVL 22 3541 282 YLL V PP VL NP IV Y GV 22 3542 35 C SL YLI A VL G NLTII 1 21 3S43 70 SGI DI L IS TS SM P KM 21 3544 153 VR GA AL M APL P VF IK 21 3545 300 EIR Q RI LR L FHV A TH 21 3546 101 L LQI F AIH S LS GM ES 20 3547 136 A TV LT L PRV T KI GVA __20 __ 3548 142 PRV TK I GVA A VV R GA __20 3549 192 CD DI R VN VVY GL IVI1 20 3550 200 V Y GL IV I I SA IG L DS 20 3S51 263 V HR F SKR RDS P LPVI1 20 3552 272 SPL P VI LA NI YL LV P 20 3553 29 WLA F PL C S LY LI AVL 19 3554 59 HE P MY IF LC ML SG ID 19 3555 60 EPM YI F LCM L SG IDI1 19 3556 61 P MYI FL CM LS G ID IL 19 3557 99 AC L LQ IF AI HS LS GM 19 3558 216 LI S FSYL L IL K TV LG 19 3559 220 SY LL IL K TVL G LT RE 19 3560 229 L GL T RE AQA KAF G TC 19 3561 233 RE AQ AK AF GT CV S HV 19 3562 247 VC A VFI FY VP FI GL S 19 3563 298 TK E IRQ RI L RL F HVA 19 3564 4 DP N GN E SS AT YF ILI 18 3565 15 FI L IG LP G LE E A FW 18 3566 26 AQ0F WL AFP LC SL YL 1 18 3567 43 LG NL TI IY IV RT EH S 18 3568 47 T IIY IV R TE H SL HEP 18 3569 79 SS MP KM LA IF WF N ST 18 3570 85 LA I FW F NS TT10F D A 18 3571 90 F NST TI QF D AC L LQI 18 3572 94 TI QF DAC L LQ01F A IH 18 3573 116 T VLL AM A FD RYV AI C 18 3574 120 AM AF DRYTV AI CH P LR is 3575 128 AI C HP LRH AT V LT LP 18 3576 130 C H PL RHA TV LT L PRV 18 3577 148 GVA AV V RGA A LM A PL 18 3578 150 AA VV R G AAL MA P LPV 18 3579 217 1ISF S YL LIL KT V LGL 18 3580 228 V LG L TR E AQ AK A FT 18 3581 250 V FI F YV PF IGCLS M VH 18 3582 254 Y VPF I GLS M VHR F SK 18 3583 265 vpPPV LNP I VY GV K TK 18 3584 287 PV L N PIV YG V KT KEI1 18 3585 304 R-IL R LF HV AT H AS EP 18 3586 13 TY FI LI GL PG L EE AQ 17 3587 219 Table XLVI - 101P3Al1 v1. DRB-0101 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 23 L E E A Q F W L A F P L C S L 17 3588 34 LCSL Y L I A V L G N L T I 17 3589 73 D I L I S T S S M P K M L A I 17 3590 96 Q F D A C L L Q I F A I H S L 17 3591 114 E S T V L L A M A F D R Y V A 17 3592 118 L L A M A F D R Y V A I C H P 17 3593 123 F D R Y V A I C H P L R H A T 17 3594 124 D R Y V A I C H P L R H A T V 17 3595 133 L R H A T V L T L P R V T K I 17 3596 140 T L P R V T K I G V A A V V R 17 3597 180 S YC L H Q D V M K L A C D D 17 3598 196 R V N V V Y G L I V I I S A I 17 3599 199 V V Y G L I V I I S A I G L D 17 3600 207 I S A I G L D S L L I S F S Y 17 3601 214 S L L I S F S Y L L I L K T V 17 3602 224 I L K T V L G L T R E A Q A K 17 3603 226 K T V L G L T R E A Q A K A F 17 3604 248 C A V F I F Y V P F I G L S M 17 3605 255 V P F I G L S M V H R F S K R 17 3606 273 P L P V I L A N I Y L L V P P 17 3607 281 I Y L L V P P V L N P I V Y G 17 3608 Table XLVI - 1O1P3A11 v2 DRB 0101 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 29 S I C W F L L C S T Q L S M E 34 3609 7 S L Y L I A V L A S G V T L R 32 3610 2 A F P L C S L Y L I A V L A S 24 3611 4 P L C S L Y L I A V L A S G V 24 3612 17 G V T L R C P S S W P I S I C 24 3613 5 L C S L Y L I A V L A S G V T 23 3614 8 L Y L I A V L A S G V T L R C 22 3615 23 P S S W P I S I C W F L L C S 21 3616 9 Y L I A V L A S G V T L R C P 18 3617 14 L A S G V T L R C P S S W P I 17 3618 15 A S G V T L R C P S S W P I S 16 3619 Table XLVI 101P3A11 v3 DRB 0101 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 15 M F A I H S L S G M E S T V L 32 3620 9 D A C L L Q M F A I H S L S G 30 3621 13 L Q M F A I H S L S G M E S T 23 3622 12 L L Q M F A I H S L S G M E S 20 3623 1 F N S T T I Q F D A C L L Q M 18 3624 5 T IQ F D A C L L Q M F A I H 18 3625 7 Q F D A C L L Q M F A I H S L 17 3626 10 A C L L Q M F A I H S L S G M 17 3627 2 N S T T I Q F D A C L L Q M F 16 3628 6 I Q F D A C L L Q M F A I H S 16 3629 Table XLVII - 1O1P3A11 v1. DRB-0301 15-mers Poo 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 17 L I G L P G L E E A Q F W L A 26 3630 220 ________ Table XLVII - 1OlP3A11 vi. DRB-0301 15-mere Poe 12 34 5 67 89 0 1234 5 score SEQ ID 207 1SA I GL DS LL IS FS y 23 3631 92 ST T IQ FDA CL L QI FA 22 3632 118 LL A M AF D RY V AIC HP 22 3633 39 LI AV LG NL T II YI VR 21 3634 180 S YCL H0D V M KL AC DD 21 363S 212 LD S LL ISF SY LL I LK 21 3636 220 SY LL I LKT V LG LT RE 21 3637 273 PL PVI L AN IY LL V PP 21 3638 27 QFW L AF P LCS L YL IA 20 3639 115 ST VL LA M AFD RY VAI1 20 3640 130 C HP LRHA T VL T L PRV 20 3641 135 HAT V LT LP R V*TK IGV 20 3642 187 V MKL AC D DI RV NVV Y 20 3643 201 YG LI V IIS AI GL D SL 20 3644 271 DS PL P VI LA N IY LLV 20 3645 298 TKE I RQ RI L RLF H VA 20 3646 12 AT Y FI LIG LP G LE EA 19 3647 55 EHS LH EP M YI F LC ML 19 3648 107 1H S LSGM E S TVL LA M 19 3649 166 1IKQL P FCR S NIL SH S 19 3650 192 CD DI R V NV VYGL IVI1 19 3651 204 1 V I I S A I G L D S L L I S 19 3652 214 S LL I SF S YL LIL KTV 19 3653 225 LK TVL G LT R E AQA KA 19 3654 228 V LGL TR E AQ AK AF GT 19 3655 249 AV FI FYV P FI G LS MV 19 3656 255 V PFI GL SM VH R F SKR 19 3657 278 LA NIY L LV PP V LNPI1 19 3658 37 L YL I A VLGCN LT IIY1 18 3659 94 T I Q FD AC L LQ1F AIH 18 3660 99 ACL L QI F AI HS L SGM 18 3661 126 YV AIC HP LR H AT V LT 18 3662 159 M AP L PVF IKQ()L PF CR 18 3663 188 MK L ACD DI RV N VV YG 18 3664 218 SF S YLL IL K TVL G LT 18 3665 226 KT VL G LTR EAOQA K AF 18 3666 282 YL L VPP VL NP IV Y GV 18 3667 289 L NPI VY GV KT KE IROQ 18 3668 19 GL P GL E EAQF WL AF P 17 3669 45 NL TI IY I VRT E HS LH 17 3670 146 KI G VAA V VR G AA LMA 17 3671 160 AP LP V FIK QL P FC RS 17 3672 257 FI GL SM VH RF SK R RD 17 3673 260 L SMV H RFS KR R DS PL 17 3674 138 VL TL PR VT KI GV A AV 16 3675 263 VHR F SK RR DS PL PVI1 16 3676 295 VK T KEI ROR I L RL F 16 3677 47 T I I YIV RT E HS L HE 1i 3678 52 VRTE H SLH E PM YI FL 15 3679 173 RS NI LS HS Y CL HQ DV 15 3680 190 L ACD D IR V NV VYGL 1 15 3681 213 DSL L IS FS YL LI L KT 15 3682 221 Table XLVII - lO1P3A11 v1. DRB-0301 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 219 F S Y L L I L K T V L G L T R 15 3683 272 S P L P V I L A N I Y L L V P 15 3684 280 NI Y L L V P P V L N P I V Y 15 3685 13 T Y F I L I G L P G L E E A Q 14 3686 36 S L Y L I A V L G N L T I I Y 14 3687 65 F L C M L S G I D I L I S T S 14 3688 141 L P R V T K I G V A A V V R G 14 3689 274 L P V I L A N I Y L L V P P V 14 3690 302 R Q R I L R L F H V A T H A S 14 3691 14 Y F I L I G L P G L E E A Q F 13 3692 48 II Y I V R T E H S L H E P M 13 3693 72 I D I L I S T S S M P K M L A 13 3694 81 M P K M L A I F W F N S T T I 13 3695 110 L S G M E S T V L L A M A F D 13 3696 114 E S T V L L A M A F D R Y V A 13 3697 136 A T V L T L P R V T K I G V A 13 3698 196 R V N V V Y G L I V I I S A I 13 3699 203 L I V I I S A I G L D S L L I 13 3700 221 Y L L I L K T V L G L T R E A 13 3701 222 L L I L K T V L G L T R E A Q 13 3702 265 R F S K R R D S P L P V I L A 13 3703 281 I Y L L V P P V L N P I V Y G 13 3704 303 Q R I L R L F H V A T H A S E 13 3705 15 F I L I G L P G L E E A Q F W 12 3706 20 L P G L E E A Q F W L A F P L 12 3707 31 A F P L C S L Y L I A V L G N 12 3708 34 L C S L Y L I A V L G N L T I 12 3709 43 L G N L T I I Y I V R T E H S 12 3710 49 I Y I V R T E H S L H E P M Y 12 3711 59 H E P M Y I F L C M L S G I D 12 3712 63 Y I F L C M L S G I D I L I S 12 3713 71 G I D I L I S T S S M P K M L 12 3714 73 D I L I S T S S M P K M L A I 12 3715 98 D A C L L Q I F A I H S L S G 12 3716 104 I F A I H S L S G M E S T V L 12 3717 108 H S L S G M E S T V L L A M A 12 3718 149 V A A V V R G A A L M A P L P 12 3719 150 A A V V R G A A L M A P L P V 12 3720 154 R G A A L M A P L P V F I K Q 12 3721 155 G A A L M A P L P V F I K Q L 12 3722 156 A A L M A P L P V F I K Q L P 12 3723 163 P V F I K Q L P F C R S N I L 12 3724 185 Q D V M K L A C D D I R V N V 12 3725 200 V Y G L I V I I S A I G L D S 12 3726 202 G L I V I I S A I G L D S L L 12 3727 209 A I G L D S L L I S F S Y L L 12 3728 211 G L D S L L I S F S Y L L I L 12 3729 285 V P P V L N P I V Y G V K T K 12 3730 293 V Y G V K T K E I R Q R I L R 12 3731 Table XLVII - 101P3A11 v2 DRB 0301 15-mers Poe 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 222 _Table XLVII - 101P3A11 v2 DRE 0301 15-mers POS 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 10 L I A V L A S G V T L R C P S 14 3732 5 L C S L Y L I A V L A S G V T 13 3733 2 A F P L C S L Y L I A V L A S 12 3734 7 S L Y L I A V L A S G V T L R 12 3735 9 Y L I A V L A S G V T L RC P 12 3736 11 I A V L A S G V T L R C P S S 12 3737 15 A S G V T L R C P S S W P I S 12 3738 17 G V T L R C P S S W P I S I C 12 3739 25 S W P I S I C W F L L C S T 12 3740 3 F P L C S L Y L I A V L A S G 11 3741 24 S S W P I S I C W F L L C S T 11 3742 27 P I S I C W F L L C S T Q L S 11 3743 B L Y L I A V L A S G V T L R C 10 3744 22 C P S S W P I S I C W F L L C 10 3745 29 S I C W F L L C S T Q L S M E 9 3746 23 P S S W P I S I C W F L L C S 8 3747 13 V L A S G V T L R C P S S W P 7 3748 Table XLVII 1OIP3A11 v3 DRB 0301 15-mers Poo 1 2 3 4 5 6.7 8 9 0 1 2 3 4 5 score SEQ ID 3 S T T I Q F D A C L L Q M F A 22 3749 10 A C L L Q M F A I H S L S G M 19 3750 5 T I Q F D A C L L Q M F A I H 18 3751 9 D A C L L Q M P A I H S L S G 12 3752 15 M F A I H S L S G M E S T V L 12 3753 12 L L Q M F A I H S L S G M E S 11 3754 1 F N S T T I Q F D A C L L Q M 10 3755 2 N S T T I Q F D A C L L Q M F 10 3756 Table XLVIII - 101P3A11 v1. DR1-0410 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 37 L Y L I A V L G N L T I I Y I 26 3757 46 L T I I Y I V R T E H S L H E 26 3758 69 L S G I D I L I S T S S M P K 26 3759 84 M L A I F W F N S T T I Q F D 26 3760 135 H A T V L T L P R V T K I G V 26 3761 146 K I G V A A V V R G A A L M A 26 3762 225 L K T V L G L T R E A Q A K A 26 3763 228 V L G L T R E A Q A K A F G T 26 3764 257 F I G L S M V H R F S K R R D 26 3765 282 Y L L V P P V L N P I V Y G V 26 3766 290 N P I V Y G V K T K E I R Q R 26 3767 302 R Q R I L R L F H V A T H A S 26 3768 12 A T Y P I L r G L P G L E E A 22 3769 25 E A Q F W L A F P L C S L Y L 22 3770 26 A Q F W L A F P L C S L Y L I 22 3771 35 C S L Y L I A V L G N L TI I 22 3772 85 L A I F W F N S T T I Q F D A 22 3773 123 F D R Y V A I C H P L R H A T 22 3774 198 N V V Y G L I V I I S A I G L 22 3775 223 STable XLVIII - l1P3Al1 vi. DRl-0410 15-mere Po 1234567890123435 score SEQID 216 LI SFSYLLILKTVLG 22 3776 218 SF SYLLILKTVLGLT 22 3777 251 FIFYVPFIGLSMVHR 22 3778 279 AN IYLLVPPVLNPIV 22 3779 20 LPGLEEAQFWLAFPL 20 3780 31 AFPLCSLYLIAVLGN 20 3781 34 LCS L Y L I A VLGNLT 1 20 3782 36 SL YLI AV L GN LT I IY 20 3763 40 AVLGNLTIIYIVRT 20 3764 43 L G N L T I I Y I V R T E H S 20 3785 45 NL T I.I Y IV RTEHSLH 20 3786 49 1Y IVRTEHSLHEPMY 20 3787 59 HE PMYIFLCMLSGID 20 3788 63 YIFL C M L S G IDILIS 20 3789 66 LC M L S G I DILISTSS 20 3790 72 DILISTSSMPKMLA 20 3791 81 MP K M L AIFWNSTT 1 20 3792 82 PK ML AI F WFNSTTIQ 20 3793 92 ST T IQ F DACLLQIFA 20 3794 98 DACLLQIFAIHSLSG 20 3795 99 AC L LQFAIHSLSM 20 3796 .101 LLQIFAIHSLSGMES 20 3797 104 1FAIHSLSGMESTVL 20 3798 107 1HS L SG M EST VL L AM 20 3799 116 TVLLAMAFDRYVAIC 20 3800 118 LL AMAFDRYVAICHP 20 3801 126 YV AICHPLRHATVLT 20 3802 130 CHPLRHATVLTLPRV 20 3803 138 VLTLPRVTKIGVAAV 20 3804 141 LP RVTKIGVAAVVR 20 3805 156 AALMAPLPVFIKQLP 20 3806 163 PVFIKQLPFCRSNIL 20 3807 166 1K LPFCRSNILSHS 20 3808 180 S Y C LH D V MK L I S F D 20 3809 184 I D V MK L A C D D VN 20 3810 187 VMKLACDDIRVNVVY 20 3811 194 DIRVNVVYGLIVIIS 20 3812 197 VNVVYGLIVIISAIG 20 3813 200 T C V L V I A V I VDS 20 3814 201 S V I i S A I G L D S L 20 381 203 C V F I F I G L DSLL 20 3816 204 V I F Y I G LD S L LIS 20 3817 207 1S AI G LD SLL I SF SY 20 3818 209 A IGL DS LL I SFS Y LL 20 3819 212 LDSLLISFSYLLILK 20 3820 213 D SLISFSYLLILKT 20 3821 219 FS Y LL IL K TV LG LTR 20 3822 241 GT CV S HVC AV F IF YV 20 3823 244 VS HV C AVF I FYV PFI1 20 3824 247 VC AV F IF YVP FI G LS 20 3825 249 AV FI FYV P FI GL S MV 20 3826 252 IF Y VP FI G LSM V H RF 20 3827 224 _________ Table XLVIII - lO1P3AIl vl. DRl-0410 15-mers Pos 12 3 456 78 90 12 34 5 score SEQ ID 273 PL PV I LA NI YLL V PP 20 3828 278 LAN I YL LV P PVL NPI1 20 3829 286 pPPVL NP IV YG VK T KE 20 3830 19 GL P GL EE AQF WL A FP 18 3831 28 FWL A FP LC SL YL I AV 18 3832 70 SG I DIL IS TS S M PKM 18 3833 95 1 QF D AC L LQ1FA I HS 18 3834 100 CLL QI FA I HS LS G ME 18 3835 108 HS LS G M EST V LL AMA 18 3836 117 V L LA MA F DRY V A ICH 18 3837 127 V AI CH P LR H ATV LTL 18 3838 165 FI KQ L PFCR S N IL SH 18 3839 177 L S HSY CL HQ0DV M KLA 18 3840 188 M K L AC DDI RV NV V YG 18 3841 206 1 1 S A I G L 0) S L L I S F S 18 3842 234 E AQ0A KA FG TCV S HVC 18 3843 238 K AFGT C VS H VCA VFI1 18 3844 272 SP LP VI LAN I YL LV P 18 3845 294 YG V KT KE I RQ RI LR L 18 3846 295 GV KT KEI R QR I LR LF 18 3847 11 S AT YF ILI GL PG L EE 16 3848 29 WL AFP L CS LY LI A VL 16 3849 60 E PMY I FLC M LSG IDI1 16 3850 62 M YIF LC ML SG ID ILI1 16 3851 86 A IFW F NS T TIQF D AC 16 3852 102 LQI F AI HS LS G ME ST 16 3853 178 S HSY CL HQ DV MK LA C 16 3854 237 AKA F GT CV S HV CA VF 16 3855 250 VF IF YV P FI GL S MVH 16 3856 254 Y VP FI GL S M VHR FSK 16 3857 14 yF ILI GL P GL EE AQ F 14 3858 is F I LI GL P GL EE AQFW 14 3859 17 LI GL PG L EEAQ0F W LA 14 3860 39 LI AV LGN L TI I YI VR 14 3861 48 11Y I VR TE H SL HEp m 14 3862 55 EH SL H EPMY I FL C ML 14 38653 61 PM YI FL C ML S GI DIL 14 3864 65 FL C MLS GI D ILI S TS 14 3865 71 GI DI LI S TSS M PK ML 14 3866 73 DIL I ST SS MPK M LAI1 14 3867 110 LS GM E ST V L LA MAFD 14 3868 114 E ST VL L A MAF DR YVA 14 3869 136 AT VL TL PRV T KI G VA 14 3870 144 V T K IG VA A VV R AAL 14 3871 149 VAA V VR GA AL M APL P 14 3872 150 AA VVR GA A LM AP L PV 14 3873 155 G AA L MA PL PV FI KQL 14 3874 159 MA PL PVF IKXQ LP F CR 14 3875 174 SNI L S HSY C LHQ DVM 14 3876 185 QDV M KL AC DD IR V NV 14 3877 192 C DD IR VNVV Y GL IVI1 14 3878 __96 RVN V VY GL IV II SAI1 14 3879 225 ___________ Table XLVIII - 1O1P3A11 vl. DR1-0410 15-mers________ Poe 123456789012345 score SEQID 214 SLLISFSYLLILKT V14 3880 221 YLLILKTVLGLTREA 14 3881 222 LLILKTVLGLTREAQ 14 3882 226 KTVLGLTREAQAKAF 14 3883 260 LSMVHRFSKRRDSPL 14 3884 271 DSPLPVILANIYLL 14 3885 274 LPVILANIYLLVPPV 14 3886 275 P V I L A N I Y L L V P P V L 14 3887 281 I Y L L V P P V L N P I V Y G 14 3888 285 V P P V L N P I V Y G V K T K 14 3889 303 Q R I L R L F H V A T H A S E 14 3890 2 M V D P N G N E S S A T Y F I 12 3891 3 V D P N G N E S S A T Y F I L 12 3892 5 P N G N E S S A T Y F I L I G 12 3893 6 NGNESSATYFILIGL 12 3894 9 E S S A T Y F I L I G L P G L 12 3895 51 I V R T E H S L H E P M Y I F 12 3896 58 L H E P M Y I F L C M L S G I 12 3897 67 C M L S G I D I L I S T S S M 12 3898 68 M L S G I D I L I S T S S M P 12 3899 80 S M P K M L A I F W F N S T T 12 3900 83 K M L A I F W F N S T T I Q F 12 3901 88 F W F N S T T IQ F D A C L L 12 3902 91 N S T T IQ F D A C L L Q I F 12 3903 93 T T I Q F D A C L L Q I F A I 12 3904 96 QFDACLLQIFAIHSL 12 3905 111 S G M E S T V L L A M A F D R 12 3906 122 A F D R Y V A I C H P L R H A 12 3907 129 1CHPLRHATVLTLPR 12 3908 132 PLRHATVLTLPRVTK 12 3909 133 L R H A T V L T L P R V T K I 12 3910 145 T K I G V A A V V R G A A L M 12 3911 147 I G V A A V V R G A A L M A P 12 3912 151 A V V R G A A L M A P L P V F 12 3913 158 LMAPLPVFIKQLPFC 12 3914 160 APLPVFIKQLPFCRS 12 3915 170 P F C R S N I L S H S Y C L H 12 3916 171 F C R S N I L S H S Y C L H Q 12 3917 172 CR SNI L S H S YCLHQD 12 3918 176 I L S H S Y C L H Q D V M K L 12 3919 189 KLACDDIRVNVVYGL 12 3920 193 D D I R V N V V Y G L I V I 12 3921 199I VYGLIV I I S A I G L D 12 3922 210 GLDSLLISFSYLL1 12 3923 211 G L D S L L I S F S Y L L I L 12 3924 217 SFSYLLILKTVLGL 12 3925 224 1LKTVLGLTREAQAK 12 3926 231 LTREAQAKAFGTCVS 12 3927 233 REAQAKAFGTCVSHV 12 3928 256 PFIGLSMVHRFSKRR 12 3929 261 S M V H R F S K R R D S P L P 12 3930 265 RFSKRRDSPLPVILA 12 3931 226 Table XLVIII - lOlP3A11 v1. DR1-0410 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 268 K R R D S P L P V I L A N I Y 12 3932 270 R D S P L P V I L A N I Y L L 12 3933 277 I L A N I Y L L V P P V L N P 12 3934 287 P V L N P I V Y G V K T K E I 12 3935 299 KE I R Q R I L R L F H V A T 12 3936 300 E I R Q R I L R L F H V A T H 12 3937 Table XLVIII - 1OlP3A1l v2 DRB 0401 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 29 S I C W F L L C S T Q L S M E 28 3938 8 L Y L I A V L A S G V T L R C 26 3939 2 A F P L C S L Y L I A V L A S 20 3940 5 L.CSL Y L I A V L A S G V T 20 3941 7 S L Y L I A V L A S G V T L R 20 3942 17 G V T L R C P S S W P I S I C 20 3943 27 P I S I C W F L L C S T Q L S 20 3944 6 C S L Y L I A V L A S G V T L 16 3945 23 P S S W P I S I C W F L L C S 16 3946 II I A V L A S G V T L R C P S S 14 3947 Table XLVIII 101P3A11 v3 DRB 0401 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 3 S T T IQ F D A C L L Q M F A 20 3948 10 A C L L Q M F A I H S L S G M 20 3949 12 L L Q M F A I H S L S G M E S 20 3950 15 M F A I H S L S G M E S T V L 20 3951 6 IQ F D A C L L Q M F A I H S 18 3952 11 C L L Q M F A I H S L S G M E 18 3953 13 L Q M F A I H S L S G M E S T 16 3954 9 D A C L L Q M F A I H S L S G 14 3955 2 N S T T IQ F D A C L L Q M F 12 3956 4 T T I Q F D A C L L Q M F A 12 3957 7 Q F D A C L L Q M F A I H S L 12 3958 5 T I Q F D A C L L Q M F A I H 10 3959 Table XLIX - 101P3A1I vi. DRBl-1101 15-mere Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 146 K I G V A A V V R G A A L M A 28 3960 123 F D R Y V A I C H P L R H A T 25 3961 218 S F S Y L L I.L K T V L G L T 25 3962 198 N V V Y G L I V I I S A I G L 24 3963 11 S A T Y F I L I G L P G L E E 23 3964 256 P F I G L S M V H R F S K R R 23 3965 45 N L T I I Y I V R T E H S L H 22 3966 60 E P M Y I F L C M L S G I D I 22 3967 159 M A P L P V F I K Q L P F C R 22 3968 238 K A F G T C V S H V C A V F I 22 3969 75 L I S T S S M P K M L A I F W 21 3970 135 H A T V L T L P R V T K I G V 20 3971 138 V L T L P R V T K I G V A A V 20 3972 163 P V F I K Q L P F C R S N I L 20 3973 227 Table XLIX - 1O1P3All VI. DR~l-1101 15-mere ________ Pos 1 23 456 7 890 12 3 45 score SEQ ID 200 VYG LIVIISAIGLDS 20 3974 225 LKT V L G LTRE A QA KA 20 3975 257 FI G LS MVH R FS KR RD 20 3976 291 P IV YGV K TKE IR QRI1 20 3977 302 R Q RIL RL FHV A TH AS 20 3978 66 LC M LSG ID I LI ST SS 19 3979 101 L LQ I FAI HS L SG MES 19 3980 197 V NVVY G LIV I IS A IG 19 3981 219 FS YLL I L KTV LG L TR 19 3982 248 C AV FI FYVP FIG L SM 19 3983 275 P VIL A NI YL LV P PVL 19 3984 46 LT II Y IV RTE H S LHE 18 3985 69 L SGI DI LI S T SS MPK 18 3986 81 MP KM L AIF WF NS TTI1 18 3987 98 DAC L LQI FA I HS L SG 18 3988 104 1F AI HS LS G ME S TVL 18 3989 209 AIG L DSL L IS FS Y LL 18 3990 250 VFI F YV PF I GL S MVH 18 3991 62 MYI F LC M LSG ID IL 1 17 3992 216 L IS F SY LL ILK T VLG 17 3993 260 L S MVHR FS KR R DS PL 17 3994 279 A NIY LL VP PV L N PIV 17 3995 289 LN PI V YGV KT K EI RQ 17 3996 12 AT YF IL IG LP G LE EA 16 3997 25 EA QF WL AF P LC S LYL 16 3998 43 LG N LT IIY IV RT E HS 16 399.9 254 Y V P I GLS MV H RF SK 16 4000 48 11YIVRTEHSLHEPM s15 4001 100 CL LQIFAIHSLSGME 15 4002 117 VL LAMAFDRYVAICH 15 4003 144 VTKIGVAAVVRGAAL 15 4004 180 S YC L H DV M KLA C DD 15 4005 228 VL G LTREAAKAFGT 15 4006 261 SMVHRFSKRRDSPL P 15 4007 262 MVHRFSKRRDSPLP1V 1 4008 278 LA NI YL LV P PV LN PI 15 4009 286 PP VLN PIVYGVKTKE 15 4010 115 STVLLAMAFDRYVA 1 14 4011 126 YVAICHPLRHATVLT 14 4012 127 V AIC H PLR H ATV L TL 14 4013 141 L P RVTK I GVA AV V RG 14 4014 171 FC RS NI LS HS YC L HQ 14 4015 181 Y C L HQD VM K L AC DD1 14 4016 194 DI RV NV VY GL IV II S 14 4017 230 G L TR E AQAK AFG TC V 14 4018 271 DS PL PV IL A NI YL LV 14 4019 299 KE IRRILRLFHVAT 14 4020 10 SSATY F ILIGLPGLE 13 4021 20 1L PGL EEAFWLAFPL 13 4022 33 PC S L YLIAVLGNL T 13 4023 36 SL Y L I AVLNLTIIY 13 4024 37 L Y LIAVLGNLTIIY 1 13 4025 228 Table XLIX - 101P3A11 v1. DRB1-1101 15-mers Pos 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 59 H E P M Y I F L C M L S G I D 13 4026 107 I H S L S G M E S T V L L A M 13 4027 152 V V R G A A L M A P L P V F I 13 4028 156 A A L M A P L P V F I K Q L P 13 4029 207 S A I G L D S L L I S F S Y 13 4030 237 A K A F G T C V S H V C A V F 13 4031 249 A V F I F Y V P F I G L S M V 13 4032 268 K R R D S P L P V I L A N I Y 13 4033 280 N I Y L L V P P V L N P I V Y 13 4034 282 Y L L V P P V L N P I V Y C V 13 4035 Table XLIX - 101P3A11 v2 DRB 1101 15-mers Pos 1 2 3 4 5 6 7 0 9 0 1 2 3 4 5 score SEQ ID 5 L C S L Y L I A V L A S G V T 18 4036 6 C S L Y L I A V L A S G V T L 18 4037 29 S I C W F L L C S T Q L S M E 17 4038 13 V L A S G V T L R C P S S W P 15 4039 8 L Y L I A V L A S G V T L R C 14 4040 4 P L C S L Y L I A V L A S G V 13 4041 12 A V L A S G V T L R C P S S W 13 4042 2 A F P L C S L Y L I A V L A S 12 4043 7 S L Y L I A V L A S G V T L R 12 4044 14 L A S G V T L R C P S S W P I 12 4045 11 I A V L A S G V T L R C P S S 10 4046 23 P S S W P I S I C W F L L C S 10 4047 15 A S G V T L R C P S S W P I S 8 4048 Table XLIX 101P3A11 v3 DRB 1101 15-mers PoS 1 2 3 4 5 6 7 8 9 0 1 2 3 4 5 score SEQ ID 12 L L Q M F A I H S L S G M E S 19 4049 9 D A C L L Q M F A I H S L S G 18 4050 15 M F A I H S L S G M E S T V L 18 4051 11 C L L Q M F A I H S L S G M E is 4052 6 I Q F D A C L L Q M F A I H S 12 4053 5 T I Q F D A C L L Q M F A I H 10 4054 13 L Q M F A I H S L S G M E S T 10 4055 229 Table LIV. Nucleotide sequence in the 5' region close to 1P3A~l gene. 1 TGCGCTCCAC CAAGCCTGGC TAACTTTTGC ATTTTFAATA GAGGCAGGGT TTCACCATGT 61 TGGCCTGGCT GGTCTCGAAC CCCTGACCTT GCGATCTGCC CACCTCGGCC TCCCAAAGTG 121 CTGGGATTAC AGGCGTGAGC CACTGTACCT GGCGGGGCTT ATTGTTTTTT AAAAAGATTr 5 181 CCAAAACCTT GCCCTGGCAA TTCTGATrI- CTGGGCCTGG AGCAGGACCT GGAGGGATGG 241 TGTTGTCAAT TACTTTAGAT GTTTCTATCA GGAAAGTTTG AGAAATGGTA TTCAGGCCTA 301 AACACAAACC TCTCTTGAAA TCTCATCCCA GACTGAGCCC CTGCTCCCTA TCTTAAATTA 361 GATTATAGTA GGTCTTAAAG TCAGCTGTAG ACTGAGCCTC TAAATCTGAA CCCAGACCCA 421 CCCTAACCCC AGGATACATC AGAAGAGCTG GTCAATGTGG ACCATTCTGA GCAATCCTGC 10 481 AAGTCTACTC TGATGGGAAA AGGCTAAGAG CAGTGCCCTG GGCAGCAACA TCAGCTCTGA 541 AGATGCAGGA CTGTGTTACA TGTTTTATGA GTGGGTCTTC ACACACTGAG ATTCATGGGA 601 CAGTAATAGA ATCTGCTTGT GCAGCACTGG GGCCTTGGAG GGTCAGGGTA AGGCTCAAGA 661 TGTCCAGGAA GTTGTATATA AGGAGAATCA GAGCAGAGAG AGACTAGGGT TCAGAATTAC 721 CAGGATGACT TAGTCCTGTT TGTTACTGTC ACCACTCCAA TGCCTTTTCC TCATTAGTCC 15 781 TTTCTCTCCT CTGAGCCACA ACTAAATGAT GTTTCTACTT TTCCCTTTCT ACTTTCCTAG 841 ACCCTGGATT TTGTATGCAG AAGCCCCAGC TCTTGGTCCC TATCATAGCC ACTTCAAATG 901 GAAATCTGGT CCACGCAGCA TACTTCCTTT TGGTGGGTAT CCCTGGCCTG GGGCCTACCA 961 TACACTTTTG GCTGGCTTTC CCACTGTGTT TTATGTATGC CTTGGCCACC CTGGGTAACC 1021 TGACCATTGT CCTCATCATT CGTGTGGAGA GGCGACTGCA TGAGCCCATG TACCTCTTCC 20 1081 TGGCCATGCT TTCCACTATT GACCTAGTCC TCTCCTCTAT CACCATGCCC AAGATGGCCA 1141 GTCTTTTCCT GATGGGCATC CAGGAGATCG AGTTCAACAT TTGCCTGGCC CAGATGTTCC 1201 TTATCCATGC TCTGTCAGCC GTGGAGTCAG CTGTCCTGCT GGCCATGGCT TTTGACCGCT 1261 TTGTGGCCAT TTGCCACCCA TTGCGCCATG CTTCTGTGCT GACAGGGTGT ACTGTGGCCA 1321 AGATTGGACT ATCTGCCCTG ACCAGGGGGT TTGTATTCTT CTTCCCACTG CCCTTCATCC 25 1381 TCAAGTGGTT GTCCTACTGC CAAACACATA CTGTCACACA CTCCTTCTGT CTGCACCAAG 1441 ATATTATGAA GCTGTCCTGT ACTGACACCA GGGTCAATGT GGTTTATGGA CTCTrCATCA 1501 TCCTCTCAGT CATGGGTGTG GACTCTCTCT TCATTGGCTT CTCATATATC CTCATCCTGT 1561 GGGCTGTTTT GGAGCTGTCC TCTCGGAGGG CAGCACTCAA GGCTTTCAAC ACCTGCATCT 1621 CCCACCTCTG TGCTGTTCTG GTCTTCTATG TACCCCTCAT TGGGCTCTCG GTGGTGCATA 30 1681 GGCTGGGTGG TCCCACCTCC CTCCTCCATG TGGTTATGGC TAATACCTAC TTGCTGCTAC 1741 CACCTGTAGT CAACCCCCTT GTCTATGGAG CCAAGACCAA AGAGATCTGT TCAAGGGTCC 1801 TCTGTATGTT CTCACAAGGT GGCAAGTGAG ACACCTTAGT GTCTCGCTTC TACTACTACT 1861 ACAGAAGATG GGAATATTAG GATCCTATTG AATGCCTTGG TGATTAAAGT ATCAAACCTA 1921 TTGTGCTGTC TTCTTCCAGC AATTTAAGTA GATCATGTAT TCTGTCTCCA GGAATGTGTC 35 1981 AGTACTGAAC TTATGACCCT GTCTGGACAT CCTGGAGAAT GACTGCACTA GTCCCTCTGC 2041 TATGGTGGTC TTGCCTTCTC CTTCTCTCTC AGCTAGAAAA TACATCTAGT TTTGACATGG 2101 GGAGGCTGTA AAGATCACAC CTCATGGTTC ATTCCAGTTT TGAAGTATGA TTTTAATGTT 2161 CTTGCCCCCA TGTGCCCATG TTGGTGAATT TGCATGGACT ATAAACGTTA TTGCAAATAC 2221 CCTAAAGTGG TTACCCAGCC ATAATCAGGG GTTAATGAAG GTATTTGGGG AATAGTAACT 40 2281 GGAGAGACAG CAACAAGACA AGAGGCAGCT CACATGCAAT GTTGAAGTTT CTGTATGCAA 2341 GAGGGTGTGT TGGCAGATTT GTGAAATCTG CCCATTTGCA TCTGTATGGC TCTATATGAC 2401 TATTTGTCCA TAAGGGTGCC ATGTATTCTG GTTGTGGGTG TGAATGTGTG GGTGTGTTTA 2461 TGTGGACACT TGCTTTTCAG TGTGCGTATA TGTGAGAGAG AGGGTGCACA CATGGAATAC 2521 GTACTGGTTG TGTCCTGGTG AGTGTGGTAG CTATGTCCTG GCACATGTAT GTTICATGAG 45 2581 ACGTGTCTCT GATTGCGCAT TTGTATTTCT GTGGTATCTG TTAGTTGGTA TATGATATGT 2641 GTCTACGTGA GAATGCTGGT GTCTGTATCT GCATGGTGGG CAGTACCTTT ATGTGTATCT 2701 GGTAAGAATG CTGCCTCTAC CTTTTCTTCC TATTTGTACT ATGTGAATGT GGTGCATGAA 2761 TGTGTGGAAT GTGTGGAATG TGTAGTATTG GGATGCCTGT ATCTTTCAGC GTGTTTGGGT 2821 GTATGTCCAC TGTGCATAAT ATTTGAGATG TAAAACCATT TTGTGCGGTA TATGTGTTAT 50 2881 TAGTTGTAAG TCGGTGAAAT GTACATCTGA ATTCTGTGTG CATATTGTTG GTACTGATGC 2941 TATTTTCGTG CATATGTCTA GTGTATATGT TTTAAGGCAA ACTTTCTTTG TGTGTTGGGT 3001 GTGTATGTGA CACGAATGGG GACAGCATCT GTATTTCTGA GCATGGATTG ATGTGTGGTG 3061 TCTGTATGTA TCTTGGAATG GAGGAGGGAG ATTGAAGAAG TCTGGCTGTG AGCAGCAGAA 3121 ATAATTTCCA AAGTTGAGTG ACATGACTCT AAGATGCCCA GTTTCTCGGC CTGGGGTCAG 55 3181 CCTGGGTGAT AGCTCAGTCT GTCAGAATGA AAGGAAACAC GGTGCTTCCT TGCTCCACCT 3241 TTTCACAGGC CAGACCACAC CTTCTTCATC CTGAACACAA GGATTTCAAG GGCTTTTGTT 3301 ACCTCTTCCT ACGTTTCCTG CCTCTGCTAT CCGAGGCACT GGCCTCCCTA AACCCTGCCC 3361 TCCTGCCTCA ATAGCAAGTC ATGGTATCCT CACCTCTCCC TTCCCTTTTT GGCTTATCTG 3421 CCAAACATGT ATAAAAGTCC TTGGTTCCCC ATCTCTACTA AAAATACAAC AATTAGCCGG 60 3481 GTGTGATGGC GCGTGCCTGT AGTCCCAGCT AGTTGGGAGG CTGAGGCAGG AGAAACGCTT 3541 GAGCCCGCAA GGTGGAGGTT GCAGTGAGCC GAGATCATGC CACTGCACTC CAGCCTGGTG 3601 ACAGAGCAAG ACTCTGTGTC AAAAAAAAAA AAAAAAAAAA AGCCTTGGTT GTAGGGAGTT 3661 TCTCCTAATC CCTCTGGGAA AGCAAGGGTG GAGGGGAAGC CAGTCAATCT CCCTTCTGTT 230 3721 GCCGCATGGA AACTCCCTTA AGGCAGGAAG CTGAAAAAAC TGTAGCATTC ACCTCATTAT 3781 TCACCTTGTC TCATGTCTCA CTGTCCTTCC ACATGTCTCA TTGTTACTCC ATATTGGATG 3841 GAAGTAGAAG TCCCTTTGGT ATTTTTTAAA GTCTTTGCCA TGTCTAAGTT AATGAGGTTA 3901 ATGGAGGCAG CAGAGATGGC TCCAGGGTTC TGATAGCAAG TGTCAGGCTG CGTGCTCTGT 5 3961 AGGtACCAGA AACTGTTGTC ACCAGTAATT TTGATGTGGT CTG;AGTTAGA ATGGTCTGAT 4021 TTGCCATGAT CTATTTAACA TAGCTTGATT TAGCGTGTCC TGTGTTCTGA ATTTAAAACT 4081 CACAGTTGTG AAACTGATCA GTAAAAAATA AGGGGAGACC AACTAAmAC CATGTTGTTC 4141. TATTTATAGA TGTAGTTTTT ACTTATTTcA AAATACGAG.G TATTTAGTTT TACATTCAAA 4201 TRGTTCTCTA ACTCTCTAAA ATGTTCTCTG ACTATTTTTG CCCTTAAGGG AGAAACCAGA 10 4261 TGTCATTGGT CTTACGTGGC TGGTGTTGGG GGTGGGGAGG GTTAAAGAAA CCACGTTCTC 4321 TGTCCTCAGC CAGAAGTTCA GTAATCCAAG GCCAGAGAGT GGACGGCAGA GGCACTGTCC 4381 CTGGGGACCT TGGTTATAAG TrATCCAGAC ACAGGGACCA GAGCCTGGGA (3ACAAAAAAA 4441 GATGTAGCCC TAGGGC7TTG GGAAAAGGAG GATGGACCCA GTGAATTCCA CGCTTAGCAA 4501 GGACCTAAAC AGTGTCCCCC AAATGAGAGA AGGGAGGACA GAAAGAACAC TTCAGGATGG 15 4561 AAATGGGCTG ACACTTAACC GTGGAGTGTC TCTGCAAACT TCCTTTGCCA TTCTCCTGTT 4621 TGAGTTTGAT AAACCTGAGA AGAGACTTGG ATAAAGACCG TCACGAAGAC TACACTAATG 4681 AGTTTCTTCT AGCTTTTTTC TACTCACTTT CCCTATCTAT CCTTCACATT GGGAGTTGGC 4741 ATGAGGATCC CAGCAGCCCA TCAGGGGAGG ACTCTAGAGA TCCCTTTCCC CATTGCCTCT 4801 CCTCCCCATA CCCCCAGGCA TATCCTCCCA GGGCACGGAA GCTGAGAAGC AGTCCAGAAC 20 4861 CACAGTGGGC TAGTGAGGGG TACCTGCTGA TGTACCCTTT GGACAGCATT CTGCCCCACC 4921 CTGCAGGAAG AAGCAGAAGG AGGGAGAGGG TGAGGCAGAG AATAAATAAC CCTGACCAGG 4981 GAGOTCCAAG GOAGTAG;GCG GAGAcagaga ggctqtattt cagtgcagcc tgccagqacct Note: The three high score predictions of promoters were bold and underlined. The 25 lower case sequence indicates the beginning part of the transcript of 101P3A11 gene. Table LV: Promoters and their positions predicted by Neural Network Promoter 30 Prediction computer program. Start End Score Promoter Sequence 25 75 0.91 TTTTGCATTTTTAATAGAGGAGGGTTTCACCATGTTGGCGCGGTC 665 715 0.95 CAGGAAGTTGTATATAAGGAGAATCAGAGCAGAGAGAGATAGGTCAG 2477 2527 0.91 TCAGTGTGCGTATATGTGAGAGAGAGGGTGCACACATGGJATACGTACTG 35 3139 3189 0.82 TGACATGATCTAAATGCCCAGTTTCTCGGCCTGGGQTCAGCCTGGGTG 3420 3470 0.96 GCCAAACATGTATAAAAGTCCTTGGTTCCCCATTATAAAATACAA 4092 4142 0.99 AACTGATCAGTAAAAAATAAGGGAGACCAACTAAACCATGTGTTCT 4953 5003 0.97 AGGCAGAGAATAAATAACCCTGACCAGGAGGTCCAJAGGGAGTAGGCGGA 40 231 Table LVI: Alignment of five homologous 5' upstream genomic regulatory regions of the human lOlP3All and PSA genes. Query: 5' upstream regulatory region of the PSA gene 5 Subject: Putative 5' upstream regulatory region of the 101P3A1i gene. Nucleic acid sequences predicted to be binding sites for the indicated transcription factors are bolded, underlined, or italicized. 1. 10 NF-1 SP-1 NF-1 Query: 3864 ccaggctggagtgcagtggcgcagtctcggctcactgcaacctctgcctcccaggttcaa 3923 Sbjct: 3598 ccaggctggagtgcagtggcatgatetcggetcactgcaacctccaccttgcgggetcaa 3539 15 Query: 3924 gtgattctcctgcctcagcctcctgagttgctgggattacaggcatgcagcaccatgcco 3963 | | illllillllllll ttlIli|||||l|l |Il tilt| lit Sbjct: 3538 gcgtttetectgcctcagcetcccaactagctgggactacaggcacgcgccatcacaccc 3479 Query: 3984 agctaatttttgtatttttagtagagatgggg 4015 20 | 111111 l l i il l l litli Sbjct: 3478 ggctaattgttgtatttttagtagagatgggg 3447 2. 25 Query: 4670 cctgtaatcccagctactgaggaggctgaggcaggagaatcacttgaacccagaaggcag 4729 li1l11 tiltlllil I ll~ltltllilllItl 1 1i1ll liI liii I Sbjct: 3496 cctgtagtcccagctagttgggaggctgaggcaggagaaacgcttgagcccgcaaggtgg 3555 SPI NF-E 30 NF-1 NF-1 OR OR Query: 4730 aggttgcaatgagccgagattgcgccactgcactccagcctgggtgacagagtgagactc 4789 lillllli lilllllIl Iilltlllltlllil llltllil 1111 Sbjct: 3556 aggttgcagtgagccgagatcatgccactgcactccagcct-ggtgacagagcaagactc 3614 35 Query: 4790 tgtctcaaaaaaaaaaaa 4807 Sbjct: 3615 tgtgtcaaaaaaaaaaaa 3632 40 3. OR NF-1 SP1 Query: 142 tgagactgagtctcgctctgtgcccaggctggagtgcagtggtgcaaccttggetcactg 201 Sbjct: 3621 tgacacagagtcttgctctgtcaccaggctggagegcagtggcatgatctcggctcactg 3562 45 Query: 202 caagctccgcctcctgggttcacgccattctcctgcctcagcctcctgagtagctgggac 261 IlIl till l I i 11111 1lltll ll ll tltllll l I lilllitllt Sbjct: 3561 caacctccaccttgcgggctcaagcgtttctcctgcctcagcctcccaactagctgggac 3502 50 NF-1 Query: 262 tacaggcacccgccaccacgcctggctaannnnnnngtatttttagtagagatgggg 318 Sbjct: 3501 tacaggcacgcgccatcacacccggctaa--ttgttgtatttttagtagagatgggg 3447 4. 55 Query: 300 atttttagtagagatggggtttcactgtgttagccaggatggtctcagtctcctgacctc 359 | | | | | | i l l I l Il l i 1 1 | |1 | |1| | 1| | | | | ||1| |11 1 1 Sbjct: 31 atttttaatagaggcagggtttcaccatgttggcctggctggtctcgaacccctgacctt 90 SPl NF- 1 60 LF-Al CP2 Query: 360 gtgatctqcccaccttggcctcccaaagtgctgggattacaggcgtgag2ccactgcgcct 419 I lilllllllllll lillllllllllllllllti ll t il li l li lll i l lt Sbjct: 91 gcgatctqcccacctcggcctcccaaagtgctgggattacaggcgtgagccactgtacct 150 232 NF-1 Query: 420 ggc 422 III 5 Sbjct: 151 gc 153 5. NF-1 10 NF-1 CP2 Query: 4506 gccaggcacagtt etcacgcctgtaatcccaacaccatgggaggetgagatgggtggat 4565 lillli lillllllllllllilllllli Ill lillllil IlI |||| III Sbjct: 153 gccaggtacagt2Sc~tcacgcctgtaatcccagcactttgggaggcegaggtgggcagat 94 15 Query: 4566 cacgaggtcaggagtttgagaccagcctgaccaacatggtgaaactctgtetcta 4620 1 1 lillllli 111 illlllllll 1 |||||||||1||11 |11 Hilli Sbjct: 93 cgcaaggtcaggggttegagaccagccaggccaacatggtgaaaccctgcctcta 39 233 Table LVII >1O1P3A11 v.1 aa 1-318: for 9-mers, 10-mers, 15-mers MMVDPNGNES SATYFILIOL PGLEEAQFWL AFPLCSLYLI AVLGNLTIIY IVRTEHSLHE 5 PMYIFLCMLS GIDILISTSS MPKMLAIFWF NSTTIQFDAC LLQZFAIHSL SGMESTVLLA MAFDRYVAIC HPLRHiATVLT LPRVTKIGVA AVVRGAALI4A PLPVFIKQLP FCRSNILSHS YCLHQDVMKL ACDDIRVNVV YGLIVIISAI GLDSLLISFS YLLILKTVLG LTREAQAKAF GTCVSHVCAV FIFYVPFIGL SMVHRFSKRR DSPLPVILAN IYLLVPPVLN PIVYGVKTKE IRQRILRLFH VATHASEP 10 >1O1PA11 v.2 9-mers, aa 36-72 15 SLYLIAVLASGVTLRCPSSWPIS ICWFLLCSTQLSME 10-mere, aa 35-72 CSLYLIAVLASGVTLRCPSSWPIS ICWFLLCSTQLsME 20 15-mers, aa 30-72 LAFPLCSLYLIAVLASGVTLRCPSSWPIS ICWFLLCSTQLSME >101P3A11 v.3 25 9-mere; aa 96-112 QFDACLLQNFAIHSLSG 10-mere: aa 95-113 30 IQFDACLLQNFAIHSLSGM iS-mers, aa 90-118 FNSTTIQFDACLLQMFAIHSJSGMESTVM 35 234

Claims (14)

1. A method to generate monoclonal antibodies that are specifically immunoreactive with an extracellular portion of a protein of SEQ ID NO:28, which 5 method comprises assessing immortalized antibody-producing cells from a subject immunized with an immunogen which is a peptide consisting of positions 2-28; positions 86-99; positions 159-202; or positions 262-272 of SEQ ID NO:28 or a fusion thereof with heterologous protein or 10 which is a nucleotide sequence encoding said immunogen for ability to secrete antibodies that immunoreact with the protein of SEQ ID NO:28 and recovering monoclonal antibodies that immunoreact with said protein. 15

2. The method of claim I wherein said immortalized cells are hybridomas.

3. The method of claim I which further comprises recovering the nucleotide sequences from said immortalized cells that encode the monoclonal antibodies. 20

4. The method of claim 3 which further comprises recombinantly producing said antibodies encoded by the nucleotide sequences recovered.

5. Monoclonal antibodies obtainable by the method of any of claims 1 to 4, or immunoreactive fragments thereof. 25

6. The antibodies or fragments of claim 5 that are chimeric or humanized.

7. The antibodies or fragments of claim 5 that are human. 30

8. The antibodies of claim 5 selected from the group consisting of X18(1)4 (ATCC-PTA-4351); X18(1)10 (ATCC-PTA-4352); X18(1)23 (ATCC-PTA-4353); and X18(4)7 (ATCC-PAT-43 54).

9. The antibodies or fragments of any of claims 5 to 8 coupled to a therapeutic 35 agent or to a toxin. 236

10. The antibodies or fragments of claim 9 wherein the toxin is maytansinoids, yttrium, bismuth, ricin, ricin A-chain, doxorubicin, daunorubicin, taxol, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin, diphtheria toxin, Pseudomonas 5 exotoxin (PE) A, PE40, abrin, abrin A chain, modeccin A chain, alpha-sarcin, gelonin, mitogellin, restrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Saponaria officinalis inhibitor, At"', I"',125, Y 90 , Re 16, Re1 88 , Sm' 53 , Bi 21 2 , p 32 , a radioactive isotope of Lu, or an anti-cancer pro-drug activating enzyme capable of converting the pro-drug to its active form. 10

11. The antibodies or fragments of any of claims 5 to 8 coupled to a detectible label.

12. The antibody or fragments of claim 11 wherein the label is a radioisotope or an enzyme. 15

13. A method to treat tumors in a subject, which method comprises administering to a subject in need of such treatment, the antibodies or fragments of any of claims 5 to 8 and 9 to 10. 20

14. A method to assess the presence of malignancy in a subject, which comprises contacting a sample of tissue or bodily fluids from said subject with the antibodies or fragments of any claims 5 to 8 and I I to 12 and detecting the presence or absence of a complex formed by said antibody with said tissue or bodily fluid.