MXPA99004356A

MXPA99004356A - Human proteins having transmembrane domains and dnas encoding these proteins

Info

Publication number: MXPA99004356A
Application number: MXPA/A/1999/004356A
Authority: MX
Inventors: Kato Seishi; Sekine Shingo; Kobayashi Midori; Kimura Tomoko
Original assignee: Kato Seishi; Kimura Tomoko; Kobayashi Midori; Sekine Shingo
Priority date: 1996-11-13
Filing date: 1999-05-12
Publication date: 2000-12-06

Abstract

Proteins containing any of the amino acid sequences represented by Sequence No. 1 to Sequence No. 2 or by Sequence No. 4 to Sequence No. 25 and DNAs encoding said proteins exemplified by cDNAs containing any of the base sequences represented by Sequence No. 26 to Sequence No. 50. Said proteins can be provided by expressing cDNAs encoding human proteins having transmembrane domains and recombinants of these human cDNAs.

Description

HUMAN PROTEINS THAT HAVE TRANSMEMBRANE DOMAINS AND DNAs THAT CODIFY FOR THESE PROTEINS Field of the Invention The present invention relates to human proteins having transmembrane domains, DNAs encoding these proteins and eukaryotic cells expressing those DNAs. The proteins of the present invention can be used as pharmaceutical compounds or as antigens for the preparation of antibodies against said proteins. The cDNAs of the present invention can be used as probes for the diagnosis of genes and as sources of genes for gene therapy. In addition, cDNAs can be used as gene sources for the large-scale production of the proteins encoded by said cDNAs. Moreover, cells introduced with DNAs encoding transmembrane proteins and expressing transmembrane proteins in large amounts can be used for the detection of the corresponding ligands as well as for the screening of new lower molecular drugs.

Background of the Invention Membrane proteins play important roles, such as signal receptors, ion channels, transporters, etc., for the transport of material and the transmission of information that are mediated by the cell membrane. Their examples include receptors for a variety of cytokines, ion channels for the sodium ion, potassium ion, chlorine ion, etc., transporters for saccharides and amino acids and the like, wherein the genes for many of them have already been cloned. It has been clarified that the abnormalities of these membrane proteins are related to a number of diseases up to now cryptogenic. For example, a gene for a membrane protein having 12 transmembrane domains was identified as the gene responsible for cystic fibrosis [Romens, J. M. et al., Science 245: 1059-1065 (1989)]. In addition, it has been clarified that several membrane proteins act as receptors when a virus infects the cells. For example, it has been revealed that HIV-1 infects cells through the mediation of a 1-membrane protein, a membrane protein in the T-cell membrane, which has a CD-4 antigen and 7 domains of transmembrane [Feng, Y. Et al., Science 272: 872-877 (1996)]. Therefore, it is anticipated that the discovery of a new membrane protein leads to the clarification of the causes of many diseases, which is why the isolation of a new gene coding for the membrane protein has been desired. Until now, due to the difficulty in purification, many of the membrane proteins have been isolated through an approach coming from the side of the genes. A general method is the so-called expression cloning, which comprises the transfection of a cDNA library in animal cells to express the cDNA and the subsequent detection of the cells expressing the target membrane protein in the membrane by a immunological technique using an antibody or a biological technique for changing the permeability of the membrane. However, this method is applicable only to the cloning of a gene for a membrane protein with a known function. In general, membrane proteins possess hydrophobic transmembrane domains within the proteins that are synthesized in the ribosome and then remain in the phospholipid that will be trapped in the membrane. Accordingly, cDNA evidence for membrane protein coding is provided by determining the entire base sequence of a full-length cDNA followed by the detection of highly hydrophobic transmembrane domains in the amino acid sequence of the protein encoded by said cDNA.

OBJECTIVES OF THE INVENTION The objective of the present invention is to provide new human proteins having transmembrane domains, DNAs coding for said proteins and transformed eukaryotic cells capable of expressing said DNAs.

Brief Description of the Drawings Figure 1 is an illustration of the structure of the detection vector pSSD3 of the secretory signal sequence.

Figure 2 is an illustration of the hydrophobicity / hydrophilicity profile of the protein • encoded by clone HP00442. Figure 3 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP00804. Figure 4 shows the result of the northern-blot hybridization of clone HP00804. Figure 5 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP01098. Figure 6 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP01148. 10 Figure 7 shows the result of the northern-blot hybridization of clone HP01148. Figure 8 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP01293. Figure 9 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10013. Figure 10 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP 10034. Figure 11 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10050. Figure 12 is an illustration of the hydrophobicity / hydrophilicity profile of protein 20 encoded by clone HP 10071. Figure 13 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by HP 10076 clone. Figure 14 is a illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by HP 10085 clone. Figure 15 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10122. Figure 16 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10136. Figure 17 is an illustration of the hydrophobicity / hydrophilicity profile of the protein 30 encoded by clone HP10175.

Figure 18 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10179. Figure 19 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by HP 10196 clone. Figure 20 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP10235. Figure 21 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP 10297. Figure 22 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP 10299. Figure 23 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by the HP 10301 clone. Figure 24 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by the HP 10302 clone. Figure 25 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP 10304. Figure 26 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by clone HP 10305. Figure 27 is an illustration of the hydrophobicity / hydrophilicity profile of the protein encoded by the HP 10306 clone. Figure 28 is an illustration of the hydrophobicity / hydrophilicity profile of the encoded protein for the HP 10328 clone.

Detailed Description of the Preferred Modalities As a result of intensive studies, the present inventors succeeded in cloning cDNAs having transmembrane domains, from a full-length human cDNA library, thereby completing the present invention. That is, the present invention provides proteins that contain any of the amino acid sequences represented by Sequence No. 1 to Sequence No. 2 or Sequence No. 4 to Sequence No. 25 which are human proteins having amino acid domains. transmembrane The present invention also provides DNAs encoding said proteins such as cDNAs containing any of the base sequences represented by Sequence No. 26 to Sequence No. 50 and transformed eukaryotic cells capable of expressing said DNAs. Each of the proteins of the present invention can be obtained, for example, by a method for isolation from human organs, cell lines, etc., a method for the preparation of the peptide by chemical synthesis based on the amino acid sequence of the present invention, or a production method with recombinant DNA technology using the DNA encoding the transmembrane domains of the present invention, wherein the method of obtaining by recombinant DNA technology is preferably employed. For example, an in vitro expression can be achieved by the preparation of an RNA by in vitro transcription from a vector having the cDNA of the present invention, followed by in vitro translation using this RNA as a model. Also, recombination of the translation domain to an appropriate expression vector by the method known in the art leads to the expression of a large amount of the encoded protein by the use of prokaryotic cells (e.g., Escherichia coli, Bacillus subtilis) or eukaryotic cells (e.g., yeast, insect cells and animal cells).

In the case where a protein of the present invention is expressed by a microorganism such as Escherichia coli, the translation region of the cDNA of the present invention is constructed in an expression vector having an origin, a promoter, site ( s) of ribosome binding, cDNA cloning site (s), a termination, etc. which can be replicated in the microorganism and, after transformation of the host cells with said expression vector, the transformant thus obtained is incubated, whereby the protein encoded by said cDNA can be produced on a large scale in the microorganism. In that case, a protein fragment containing an optional region can be obtained by performing the expression with the insertion of an initiation codon and a stop codon before and after the optional translation region. Alternatively, a fusion protein with another protein can be expressed. Only a portion of the protein encoding said cDNA can be obtained by dividing said fusion protein with an appropriate protease.

In the case where a protein of the present invention is to be produced in eukaryotic cells the translation region of said cDNA can be subjected to recombination to an expression vector for eukaryotic cells having a promoter, a splicing domain, an Poly (A) addition site, etc. and transfected into eukaryotic cells so that the protein is produced as a membrane protein on the surface of the cell membrane. Examples of the expression vector are pKAl, pCDM8, pSVK3, pMSG, pSVL, pBK-CMV, pBK-RSV, EBV vector, pRS, pYES2, etc. Examples of eukaryotic cells are cells from cultures of mammalian animals (e.g., COS7 monkey kidney cells, Chinese CHO hamster ovary cells), blast yeast, cleavage yeast, silkworm yeast, toad oocyte with pincer South African, etc. However, any eukaryotic cells can be used as long as the protein of the invention can be expressed on the surface of the cell membrane. In order to introduce the expression vector into the eukaryotic cells any conventional method per se such as the electrophoresis method, the calcium phosphate method, the liposome method, or the DEAE dextran method can be used. For the separation and purification of the protein of the invention from the culture medium after the expression of said protein in prokaryotic cells or eukaryotic cells, conventional separation operations may be adopted, if necessary, in their appropriate combinations. Examples of conventional separation operations are treatment with a denaturing agent (e.g., urea) or a surfactant, ultrasonic treatment, enzymatic digestion, salting, solvent precipitation, dialysis, centrifugation, ultrafiltration, gel filtration, SDS-PAGE, Isoelectric point electrophoresis, ion exchange chromatography, hydrophobic chromatography, affinity chromatography, reverse phase chromatography, etc. The proteins of the present invention include peptide fragments (residues of more than 5 amino acids) containing any partial amino acid sequence of the amino acid sequence represented by Sequence No. 1 to Sequence No. 2 or Sequence No. 4 to Sequence No. 25. These fragments can be used as antigens for the preparation of the antibodies. Also, proteins of the present invention having signal sequences appear in the form of maturation proteins on the cell surface, after the signal sequences are eliminated. Therefore, these maturation proteins will fall within the scope of the present invention. The N-terminus amino acid sequences of the maturation proteins can be easily identified using the method for determination of the cleavage site in a signal sequence [Japanese Patent Kokai Publication No. 1996-187100]. further, many membrane proteins are subjected to processing on the cell surface to be converted to secretory forms. These peptides or secretory proteins will fall within the scope of the present invention. When glycosylation sites are present in the amino acid sequences, expression in appropriate animal cells will provide glycosylated proteins. Therefore, these glycosylated proteins or peptides will also fall within the scope of the present invention. The DNAs of the present invention include all the DNAs that code for the aforementioned proteins. Said DNAs can be obtained using the chemical synthesis method, the DNA cloning method and the like. Each of the cDNAs of the present invention can be cloned from, for example, a cDNA library of the human cell origin. The cDNA is synthesized using a poly (A) + RNA extracted from human cells as a model. Human cells can be cells released from the human body, for example, by operation or they can be cultured cells. The cDNA can be synthesized using any method selected from the Okayama-Berg method [Okayama, H. and Berg, P. Mol. Cell. Biol. 2: 161-170 (1982)], the Gubler-Hoffman method [Gubler, U. and Hoffman, J. Gene 25: 263-269 (1983)] and the like, but the capping method is preferred [Kato , S. et al., Gene 150: 243-250 (1994)] as illustrated in the Examples in order to obtain a full-length clone in an effective form. The primary selection of a cDNA encoding a human protein having a transmembrane domain (s) is performed by sequencing a partial base sequence of the cDNA clone randomly selected from the cDNA library, sequencing the sequence of amino acids encoded by the base sequence, and recognition of the presence or absence of hydrophobic site (s) in the region of the amino acid sequence with resultant N-terminus. Next, the secondary selection is carried out by the determination of the complete base sequence by sequencing and the expression protein by in vitro translation. The investigation of the cDNA of the present invention for the coding of the protein having the sequence of the secretory signal is carried out using the method of detection of the signal sequence [Yokoyama-Kobayashi, M. cl al., Gene 163: 193- 196 (1995)]. In other words, the inquiry for the coding portion of the inserted cDNA fragment to function as a signal sequence is provided by fusing a cDNA fragment encoding the N terminus of the target protein with a cDNA encoding the urokinase protease domain. and subsequently expressing the resulting cDNA in COS7 cells to detect urokinase activity in the cell culture medium. On the other hand, it is judged that the termination region N remains in the membrane in the case where urokinase activity is not detected in the cell culture medium. The cDNAs of the present invention are characterized as containing any of the base sequences represented by Sequence No. 26 to Sequence No. 50 or by any of the base sequences represented by Sequence No. 51 to Sequence No. 75 Table I summarizes the number of clone (HP number), the cells that provide the cDNA, the number of total bases of the cDNA and the number of amino acid residues of the encoded protein, for each of the DNAs.

Table 1 Accordingly, the same clone as any of the cDNAs of the present invention can be easily obtained by screening the cDNA library constructed from the human cell line or tissue used in the present invention, by the use of a DNA probe. oligonucleotide synthesized on the basis of the corresponding cDNA base sequence described in Sequence No. 51 Sequence No. 75. In general, polymorphism due to individual difference is frequently observed in human genes. Therefore, any cDNA that is subjected to insertion or deletion of one or more nucleotides and / or substitution with other nucleotides in Sequence No. 50 to Sequence No. 75 will fall within the scope of the present invention. In a similar manner, any protein that is produced by these modifications comprising the insertion or deletion of one or multiple nucleotides and / or substitution with other nucleotides will fall within the scope of the present invention, as long as said protein possesses the activity of the corresponding protein having the amino acid sequence represented by Sequence No. 1 to Sequence No. 2 or Sequence No. 4 to Sequence No. 25. The cDNAs of the present invention include cDNA fragments (greater than 10 bp) containing any partial base sequence of the base sequence represented by Sequence No. 26 to No. 50 or of the base sequence represented by Sequence No. 51 to No. 75. Also, DNA fragments consisting of a chain of sense and a chain of anti-sense will fall within this scope. These cDNA fragments can be used as probes for the diagnosis of genes.

BEST METHOD FOR CARRYING OUT THE INVENTION EXAMPLE The present invention is embodied in greater detail by the following examples but this embodiment is not intended to restrict the present invention. The basic operations and enzyme reactions in relation to DNA recombination are carried out according to the literature [Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory, 1989]. Unless otherwise specified, the restriction enzymes and a variety of modifying enzymes to be used were those available from Takara Shuzo Co., Ltd. The manufacturer's instructions were used for the regulatory compositions as well as for the reaction conditions , in each of the enzyme reactions. The cDNA synthesis was carried out according to the literature [Kato, S. et al., Gene 150: 243-250 (1994)]. (1) Preparation of Poly (A) RNA + The HT-1080 fibrosarcoma cell line (ATCC CCL 121), the epidermoid carcinoma cell line KB (ATCC CRL 17), the histiocyte lymphoma cell line U937 (ATCC CRL 1593) , osteosarcoma U-2 OS (ATCC HTB 96), a leukocyte isolated from peripheral blood, stomach cancer tissues obtained by operation, and liver were used for the extraction of mRNAs from human cells. Each of the cell lines was cultured by a conventional procedure. After approximately 1 g of human tissue was homogenized in 20 ml of 5.5 M guanidine thiocyanate solution, total mRNAs were prepared according to the literature [Okayama, H. et al., "Methods in Enzymology", vol. 164, Academic Press, 1987]. These mRNAs were subjected to chromatography using an oligo (dT) -cellulose column washed with 20 mM Tris-hydrochloric acid buffer (pH 7.6), 0.5 M NaCl, and 1 mM EDTA to obtain a po! Y RNA ( A) + according to the aforementioned literature. (2) Construction of a cDNA Library To a solution of 10 μg of the aforementioned poly (A) + RNA in Tris buffer solution of 100 mM hydrochloric acid (pH 8) was added an alkaline phosphatase unit of bacterial origin and free of RNase and the resulting solution was allowed to react at 37 ° C for one hour. Then the reaction solution experienced phenol extraction followed by ethanol precipitation, the granules obtained were dissolved in a mixed solution of 50 mM sodium acetate (pH 6), 1 mM EDTA, 0.1% 2-mercaptoethanol and 0.01% Triton X-100. To this was added one unit of a pyrophosphatase originating from tobacco (Epicenter Technologies) and the resulting solution in a total volume of 100 μl was allowed to react at 37 ° C for one hour. After the reaction solution experienced phenol extraction followed by precipitation with ethanol, the granules thus obtained were dissolved in water to obtain a solution of pickled poly (A) + RNA. To a solution of poly (A) + RNA pickling and 3 nmol of a DNA-RNA chimeric oligonucleotide (5'-dG-dG-dG-dG-dA-dA-dT-dT-dC-dG-dA-GGA- 3 ') in a mixed aqueous solution of buffer solution of Tris-hyhloric acid 50 mM (pH 7.5), 0.5 mM ATP, 5 mM MgCl2, 10 mM 2-mercaptoethanol and 25% polyethylene glycol were added 50 units of T4 RNA ligase and the resulting solution in a total volume of 30 μl was allowed to react at 20 ° C for 12 hours. After the reaction solution experienced phenol extraction followed by ethanol precipitation, the granules thus obtained were dissolved in water to obtain a poly (A) + oligo-caped chimeric RNA. After the pKAl vector developed by the present inventors (Japanese Patent Kokai Publication No. 1992-1 17292) was digested with Kpnl, a tail of approximately 60 dT was inserted by a terminal transferase. This product was digested with EcoRV to eliminate the dT tail on one side and the resulting molecule was used as a vector primary.

After 6 μg of the previously prepared chimeric psi (A) + oligo-caped RNA was annealed with 1.2 μg of the vector primary, the product was dissolved in a mixed solution of 50 mM Tris-hydrochloric acid buffer (pH 8.3) , 75 mM KCl, 3 mM MgCl 2, 10 mM dithiothreitol and 1.25 mM dNTP (dATP + dCTP + dGTP + dTTP), mixed with 200 units of a reverse transferase (GIBCO-BRL) and the resulting solution in a total volume of 20 μl it was allowed to react at 42 ° C for one hour. After the reaction solution experienced phenol extraction followed by ethanol precipitation, the granules obtained in this manner were dissolved in a mixed solution of 50 mM Tris-hydrochloric acid buffer (pH 7.5), 100 mM NaCl, 10 mM MgCl 2 and 1 mM dithiothreitol. To this, 100 units of EcoRI were added and the resulting solution in a total volume of 20 μl was allowed to react at 37 ° C for one hour. After the reaction solution experienced phenol extraction followed by ethanol precipitation, the granules thus obtained were dissolved in a mixed solution of Tris buffer-20 mM hydrochloric acid (pH 7.5), 100 mM KCl, MgCl 2 4 mM, 10 mM (NH) 2 SO 4 and bovine serum albumin 50 μg / ml. To this was added 60 units of Escherichia coli DNA ligase and the resulting solution was allowed to react at 16 ° C for 16 hours. To the reaction solution were added 2 μl of 2 mM dNTP, 4 units of Escherichia coli DNA polymerase I and 0.1 units of Escherichia coli DNase H, and the resulting solution was allowed to react at 12 ° C for one hour and subsequently at 22 ° C for one hour. Next, the solution of the cDNA synthesis reaction was used to transform DH12S from Escherichia coli (GIBCO-BRL). The transformation was carried out by the electrophoration method. A portion of the transformant was inoculated in a culture medium of 2xYT agar containing 100 μg / ml of ampicillin, which was incubated at 37 ° C overnight. A growth of the colony in the culture medium was taken randomly and inoculated in 2 ml of the 2xYT culture medium containing 100 μg / ml of ampicillin, which was incubated at 37 ° C overnight. The culture medium was centrifuged to separate the cells, from which a plasmid DNA was prepared by the alkaline lysis method. After the plasmid DNA was digested twice with EcoRI and NotI, the product was subjected to electrophoresis on an 8% agarose gel to determine the size of the cDNA insert. In addition, by using the plasmid obtained as a model, the sequence reaction using universal primary M13 labeled with a fluorescent dye and Taq polymerase (a team from Applied Biosistems Inc.) was carried out and the product was analyzed by a sequencer. of fluorescent DNA (Applied Biosystems Inc.) to determine the base sequence of the 5 'terminus of the approximately 400 bp cDNA. The sequence information was presented as a database of a homo-protein cDNA library. (3) Selection of DNAs that Code for Proteins that Have Transmembrane Domains. The base sequence recorded in the homo-protein cDNA library was converted to three frames of amino acid sequences and the presence or absence of an open reading frame (ORF) starting from the initiation codon. Subsequently, the selection was made for the presence of a signal sequence that is characteristic for a protein secreted at the N-terminus of the portion encoded by ORF. These clones were sequenced from both 5 'and 3' directions using the deletion method to determine the complete base sequence. The hydrophobicity / hydrophilicity profiles were obtained for proteins encoded by ORF by the Kyte-Doolittle method (Kyte, J. &Doolittle, RF, J. Mol. Biol. 157: 105-132 (1982)] to examine the presence or absence of a hydrophobic region In the case where there is a hydrophobic region of putative transmembrane domain (s) in the amino acid sequence of an encoded protein, this protein was considered as a membrane protein. (4) Construction of a Vector pSSD3 for Secretory Signal Detection. A microgram of pSSDl carrying the SV40 promoter and a cDNA coding for the urokinase protease domain (Yokoyama-Kobayashi, M. et al., Gene 163: 193-196 (1995)] was digested with 5 units of BglII and 5 EcoRV units Then, after dephosphorylation at the 5 'end by the CIP treatment, a DNA fragment of approximately 4.2 kbp was purified by cutting from agarose gel electrophoresis.

Two oligo ^ Ll DNA linkers (5'-GATCCCGGGTCACGTGGGAT-3 ') and L2 (5'-ATCCCACGTGACCCGG-3') were synthesized and phosphorylated by T4 polynucleotide kinase. After annealing of both linkers, followed by binding with the pSSdl fragment previously prepared by T4 DNA ligase, Escherichia coli JM109 was transformed. A plasmid pSSD3 was prepared from the transformant and the target recombinant was confirmed by determining the base sequence of the fragment inserted into the linker. Figure 1 illustrates the structure of the plasmid thus obtained. The present plasmid vector carries three types of restriction enzyme sites with blunt end formation, Smal, PmaCl and EcoRV. Since these cleavage sites are placed in succession at a range of 7 bp, the selection of an appropriate site in combination with three types of frames for cDNA insertion allows the construction of a vector that expresses a fusion protein. (5) Functional Verification of Secretory Signal Sequence If the hydrophobic region with N-terminus in the secreted protein clone candidate obtained in the above-mentioned steps works as the secretory signal sequence was verified by the method described in the literature [Yokoyama- Kobayashi, M. et al., Gene 163: 193-196 (1995)]. First, the plasmid containing the target cDNA was divided into an appropriate restriction enzyme site that existed downstream of the portion expected for coding for the secretory signal sequence. In the case where this restriction enzyme site was a 5 'terminus protruding, the site was made blunt ended by the Klenow treatment or mung bean nuclease treatment. Digestion with HindIII was further carried out and a DNA fragment containing the SV40 promoter and a cDNA encoding the secretory sequence downstream of the promoter was separated by agarose gel electrophoresis. This fragment was inserted between the HindIII site of pSSD3 and a selected restriction enzyme site in order to match the urokinase coding frame, thereby constructing a vector expressing a fusion protein of the secretory signal portion of the cDNA. target and the protease domain of urokinase.

After the Escherichia coli (host: JM109) carrying the fusion protein expression vector was incubated at 37 ° C for 2 hours in 2 ml of the 2xYT culture medium containing 100 μg / ml of ampicillin, the helper phage M13KO7 ( 50 μl) was added and the incubation was continued at 37 ° C overnight. A supernatant separated by centrifugation was subjected to precipitation with polyethylene glycol to obtain single-stranded phage particles. These particles were suspended in 100 μl of 1 mM Tris-0.1 mM EDTA, pH 8 (TE). Also, a suspension of single-stranded particles prepared in the same manner as that of the pKAl-UPA vector containing pSSD3 and a full-length urokinase cDNA was used as a control [Yokoyama-Kobayashi, M. et al., Gene 163: 193-196 (1995)]. The cells from the simian kidney-derived culture, COS7, were incubated at 37 ° C in the presence of 5% CO2 in the Dulbecco's modified Eagle culture medium (DMEM) containing 10% fetal bovine albumin. In a 6-well dish (Nunc Inc., 3 cm well diameter), 1 x 105 COS7 cells were inoculated and the incubation was carried out at 37 ° C for 22 hours in the presence of 5% CO2. After the culture medium was removed, the cell surface was washed with a phosphate buffer and subsequently washed again with DMEM containing 50 mM Tris-hydrochloric acid (pH 7.5) (TDMEM). To the cells were added 1 μl of the single-chain phage suspension, 0.6 ml of DMEM culture medium, and 3 μl of TRANSFECTAM ™ (IBF Inc.) and the resulting mixture was incubated at 37 ° C for 3 hours. in the presence of 5% CO2. After the sample solution was removed, the surface of the cells was washed with TDMEM, 2 ml per well of DMEM containing 10% fetal bovine albumin were added, and the incubation was carried out at 37 ° C for 2 days in the presence of 5% CO2. To 10 ml of 50 mM phosphate buffer (pH 7.4) containing 2% bovine fibrinogen (Miles Inc.), 0.5% agarose and 1 mM potassium chloride were added 10 units of human thrombin (Mochida Pharmaceutical Co., Ltd .) and the resulting mixture was solidified in a dish 9 cm in diameter to prepare a fibrin plate. Ten microliters of the culture medium supernatant of the transfected COS7 cells were dispersed on the fibrin plate, which was incubated at 37 ° C for 15 hours. The diameter of the clear circle thus obtained was taken as an index to determine the urokinase activity. In the case where a cDNA fragment codes for the amino acid sequence that functions as a secretory signal sequence, a fusion protein is secreted to form a clear circle by its urokinase activity. Therefore, in the case where a clear circle was not formed, the fusion protein remains trapped in the membrane and the cDNA fragment is considered to encode a transmembrane domain. (6) Protein Synthesis by In Vitro Translation The plasmid vector carrying the cDNA of the present invention was used for in vitro transcription / translation by the rabbit reticulocyte lysate TNT (Promega Biotec). In this case, [35 S] methionine was added and the expression product was labeled with the radioisotope. All the reactions were carried out following the protocols attached to the equipment. Two micrograms of the plasmid were allowed to react at 30 ° C for 90 minutes in 25 ml total of a reaction solution containing 12.5 μl of the rabbit reticulocyte lysate TNT, 0.5 μl of the buffer solution (attached to the kit), 2 μl of a mixture of amino acids (methionine-free), 2 μl (0.37 MBq / μl) of [35 S] methionine (Amersham Corporation), 0.5 μl of T7 RNA polymerase and 20 U of RNsin. To 3 μl of the reaction solution were added 2 μl of an SDS sample buffer (Tris buffer solution 125 mM hydrochloric acid, pH 6.8, 120 mM 2-mercaptoethanol, 2% SDS solution, 0.025% bromophenol blue and 20% glycerol) and the resulting solution was heated at 95 ° C for 3 minutes and then subjected to SDS-polyacrylamide gel electrophoresis. The molecular weight of the translation product was determined by carrying out the autoradiography. (7) Northern Blot Hybridization Northern Blot hybridization was carried out in order to examine the expression pattern in human tissues. The membranes on which poly (A) + RNAs were scattered isolated from each human tissue were stained and acquired at Clontech Inc. The cDNA fragments that were cut from the target clones with appropriate restriction enzymes were subjected to separation by electrophoresis. on agarose gel followed by [32P] dCPT (Amersham Corporation) labeling using the Random Primer Labeling Equipment (Takara Shuzo Co., Ltd.). Hybridization was carried out using a solution attached to the stained membrane according to the protocol. (8) Expression in COS7 Escherichia coli possessing an expression vector of the protein of the invention was infected with helper phage M13KO7 and single-stranded phage was obtained by the above method. Using the phage thus obtained, the expression vector was introduced into cultured COS7 cells of monkey kidney origin according to the above method. The culture was carried out at 37 ° C in the presence of 5% CO2 for 2 hours and then in a medium containing [35S] cysteine for 1 hour. The cells were harvested, dissolved and subjected to SDS-PAGE, whereby a band corresponding to a protein was revealed as an expression product, which was not present in the COS cells. (9) Clone Examples < HP00442 > (Sequences Nos. 1, 26, 51) The determination of the complete base sequence for the cDNA insert of clone HP00442 obtained from the cDNA libraries of the human fibrosarcoma cell line HT-1080 revealed the structure consisting of a 5 'non-translation region of 81 bp, an ORF of 618 bp, and a 3' non-translation region of 287 bp. The ORF codes for a protein consisting of 205 amino acid residues with 5 transmembrane domains, Figure 2 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The result of the in vitro translation did not reveal the formation of different bands for the translation products and revealed the formation of fuzzy bands in the high molecular weight position. Investigation of the protein database using the amino acid sequence of the present invention revealed that the protein was analogous to the proteolipid protein PPA1 of baker's yeast proton ATPase (SWISS-PROT Accession No. P23968). Table 2 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the proteolipid protein PPA1 of baker's proton ATPase (PL). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins had a homology of 56.8% in the entire region except for the N-terminus.

Table 2 HP MTGI_ALLYS6VFVAF ACALAVGVCYTIF-DLGFR DVAW LTETSPFMWS * _. *. *. ** ***. **, PL MN ESIO) DDMSLGKFSFSHFLYYLVLIVVIVYGLYKLFTGHGSDINFGKFLLRTSPYMWA HP NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRI TrarLVSIIFCEAVAIYGI3_MAIV ****. *,. **********. *****. **, **. ** **. ****. ****** "*****. *. *** PL NI? IALCVGLSVVGAAWGIFITGSSMIGAGVRAPRITTKNLISIIFCEVVAIYGLIIAIV HP ISNMAEPFSATDPKAIGHRNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNP. * ,. ** *,. ***. * **. *** ***. **. ***. * .. ** .. ** ... PL FSSKL- TVATAENMYSKSNLYTGYSLFWAGITVGASNLICGIAVGITGATAAISDAADS HP SLFVKILIVEIFGSAIGLFGVIVAILQTSRVKMGD. ****** .. *****. **. *. ** .. * ... PL ALFVKILVIEIFGSILGLLGLIVGLUMAGKASEFQ In addition, the GenBank research using the present ANDc base sequence revealed that there were some ESTs possessing 90% or more homology and that they also contained the initiation codon (eg, Accession No. H87379), but the protein present it can not be predicted from this sequence. The proteolipid protein PPA1 of baker's yeast proton ATPase is an essential membrane protein for cell growth [Apperson, M. et al., Biochem. Biophys. Res. Commun. 168: 574-579 (1990)]. Accordingly, the protein of the present invention, which is homologous to said protein, is considered essential for the growth of human cells and can be used for the diagnosis and treatment of diseases caused by the abnormality of the present protein. < HP00804 > (Sequences Nos. 2, 27, 52) The determination of the complete base sequence for the cDNA insert of clone HP00804 obtained from the cDNA libraries of the human leukocyte cell revealed the structure consisting of a non-translation region. 5 'of 132 bp, an ORF of 1116 bp, and a 3' non-translation region of 576 bp. The ORF codes for a protein consisting of 371 amino acid residues with 7 transmembrane domains. Figure 3 illustrates the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The result of the in vitro translation did not reveal the formation of different bands for the translation products. Examination of the expression pattern in tissues by hybridization by northem blot using the cDNA fragment of the present invention revealed that the expression occurred in all tissues examined as shown in Figure 4. Thus, the protein of the present invention invention is considered a homemade protein. Investigation in the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the rat-glutamate NMDA receptor binding subunit (GenBank Accession No. S61973). Table 3 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the NMDA receptor binding subunit of rat-glutamate (RN). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. This subunit consists of 516 amino acid residues and a glutamine region at position 68 to arginine at position 342 possessed 92.6% homology with the 270 amino acid residue of the C terminus in the protein of the present invention. However, no homology was observed in the region of the N-terminus. Accordingly, a characteristic repeat sequence that is rich in proline, tyrosine and glycine was observed in the N-terminus region of the protein of the present invention.

Table 3 HP MSHEKSFLVSGDNYPPPNPGYPGGPQPPMPPYAQPPYPGAPYPQPPFQPSPYGQPGYPHG RN MKRVSWSLGTAILPQTLAILWGHKPLCLPMFSLPTLG HP PSPYPQGGYP GPYPQGGYPQGPYPQEGYPQGPYPQGGYPQGPYPQSPFPPNPYGQPQVF **. **************. * RN PHTHRPLSSPLPMVNQGIPMVPVPITR LPIJDLIJCEATHQGHYPQSPFPPNPYGqPPPF HP PGQDPDSPQHGNYQEEGPPSYYDNQDFPATNWDDKSIRQAFIRKVFLVLTLQLSVTLSTV ***. ********************** .. ** ****************** ********* RN -QDPGSPQHGNYQEEGPPSYYDNQDFPSVNW-DKSIRQAFIRKVFLVLTLQLSVTLSTV HP SVFTFVAEV GITIuO p? YVSYAVFFISLIVLSCCGDFRRCT. , ****. *******. **********. ***************. ********* *. ** **** RN AIFTFVGEV GFVRANV TYYVSYAIFFISLIVLSCCGDFRKKHPWNLVALSILTISLSY HP WGMIASFYNTEAVIMAVGITTAVCFTVVIFSM TRYDFTSCMGVLLVSMVVLFIFAILC **************************************** ** ********** RN MVGMIASFYNTEAVIMAVGITTAVCFTWIFSMQTRYDFTSCMGVLLVSVWLFIFAILC HP IFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFL ********************************************** ********** RN IFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFL HP YILTIIGRAKE ********. , RN YILTIIGRSQGIGQAPAQVAWAQTHAPAMTLPSVLPPLOTPAMAWSRGSPSRPRVCTLQ In addition, the search in GenBank using the base sequence of the present cDNA revealed that there are some ESTs that have 90% or more homology (for example, Access No. W25936), but none of them was shorter than the present cDNA and did not contain the initiation codon. It has been found that the binding subunit of the rat-glutamate NMDA receptor is one of the subunits of the NMDA receptor complex that exists specifically in the brain [Kumar. K. N. et al., Nature 354: 70-73 (1991)]. Despite a high homology with the protein of the present invention, the subunit shows different patterns of expression in the N-terminus sequence and tissues, so both molecules are considered to have different functions. Since the protein of the present invention possesses 7 transmembrane domains that are characteristic for channels and transporters, this protein is considered to play a role as a channel and a transporter. Because the protein of the present invention is an essential home protein for cells, the present protein can be used for the diagnosis and treatment of diseases caused by the abnormality of this protein. < HP01098 > (Sequences Nos. 3, 28, 53) The determination of the complete base sequence for the cDNA insert of the clone HP01098 obtained from human stomach cancer cDNA libraries revealed the structure consisting of a 5 'non-translation region of 61 bp, an ORF of 540 bp, and a 3' non-translation region of 475 bp. The ORF codes for a protein consisting of 179 amino acid residues with a transmembrane domain. Figure 5 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method.

The in vitro translation resulted in the formation of a translation product of 20 kDa that was almost consistent with the molecular weight of 20,625 predicted from ORF. Searching for the protein in the database using the amino acid sequence of the present protein revealed that the protein was completely identical with an 18 kDa subunit of the canine microsomal signal peptidase (SWISS-PROT, Accession Number P21378). It was therefore verified that the cDNA of the present invention codes for the human homolog of the 18 kDa subunit of the microsomal signal peptidase.

Searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs possessing the homology of 90% or more (eg, Accession No. T60549), but many sequences were not distinct and the same ORF was not identified as that in the cDNA present. The 18 kDa subunit of the canine micromosomal signal peptidase has been found as one of the subunits of the signal peptidase complex that exist in the microsome [Schelness, G. S. & Blobel, G., J. Biol. Chem. 265: 9512-9519 (1990)]. The signal peptidase is an enzyme that divides the signal sequence during the secretion of a secretory protein in the endoplasmic reticulum. Accordingly, the cDNA of the present invention can be used for the production of the present protein as well as for the diagnosis and treatment of diseases caused by the abnormality of the present protein. < HP01148 > (Sequences Nos. 4, 29, 54) The determination of the complete base sequence for the cDNA insert of clone HP01148 obtained from the human liver cDNA libraries revealed the structure consisting of a 5 'non-translation region. of 101 bp, an ORF of 1044 bp, and a 3 'non-translation region of 446 bp. The ORF codes for a protein consisting of 347 amino acid residues with a transmembrane domain at the N-terminus. Figure 6 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein remained in the membrane from the observation that the urokinase secretion was not identified, during transduction in COS7 cells of an expression vector in which a HindIII-PvulI fragment containing a cDNA fragment coding for 178 amino acid residue of the N-terminus in the present protein was inserted into the HindlII-PmaCI site of pSSD3. Therefore, the present protein was considered to be a type II membrane protein. The in vitro translation resulted in the formation of a translation product of 41 kDa that was almost consistent with the molecular weight of 38.101 predicted by ORF. Examination of the tissue expression pattern by northern blot hybridization using the cDNA fragment of the present invention revealed that a strong expression occurred in the spleen, as shown in Figure 7. It was also indicated that a slight expression occurred in the liver. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the bovine WC1 antigen (SWISS-PROT Accession No. P30205). Table 4 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the bovine WC1 antigen (WC). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 38%.

Table 4 HP MALLFSLILAICTRPGFLASPSGVRLVGGLHRCEGRVEVEQKGQWGTVCDDGW. ***. *. *. ****. . . * *** *** * WC VLPQCNDFLSQPAGSAASEESSPYCSDSRQLRLVDGGGPCGGRVEIL QGSWGTICDDDW HP DIKDVAVLCRELGCGAASGTPSGILYEPPAEKEQKVLI SVSCTGTEDTLAQCEQEE-V WC DLDDARWCRQLGCGEALNATGSAHF - GAGSGPIWLDDLNCTGKESHVWRCPSRGWGR HP YDCSHEEDAGASCENPESSFSPVPEGVRLADGPGHCKGRVEV HQNQWYTVCQTGWSLRA. **. *. ****. *. * * .. * * * .. ** ... *. ** ... . WC HDCRHKEDAGVIC- - SE- F LALRMVSEDQQCAGWLEVFYNGTWGSVCRSPMEDIT HP AKVVCRQI? CGRAVLTQKRCNKHAYGRK_? IWLSQMSCSGREATLQDCPSGPWGKNTCNHD WC VSVICRQLGCGDSGS NTSVGLRE-GSRPRWVDLIQCR MDTSLWQCPSGPWKYSSCSPK HP EDTWVECE DPFDLRLVGGDNLCSGRLEVLHKGVWGSVCDDNWGEKE *. . . . . ** * •. *** *** **** ** *. * ** **** *, * WC EEAYISCEGRRPKSCPTAAACTDREKLRLRGGDSECSGRVEVWHNGSWGXVCDDSWSLAE HP DQWCKQLGCGKSLSPSDRDR CYGPGVGRIWLDNVRCSGEEQSLEQCQHRFWGFHDCTH. ***. ***** .. *,. *** *. ****. *. *. * * **. * ** **. * WC AEWCQQLGCGQALE-AVR- SAAFGPGNGSIWLDEV CGGRESSLWDCVAEPWGQSDCKH HP QEDVAVICSG. **. . * *** WC EEDAGVRCSGVRTTLPTTTAGTRTTSNSLPGIPSLPGVLC ILGSLLFLVLVILVT LL In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed the homology of 90% or more (for example, Accession No. H91200), but it could not be assessed if these ESTs with partial sequences encoded for the same protein as the protein of the present invention. The bovine WC1 antigen has been found as a membrane antigen that is expressed specifically in T? D cells [Wijngaard, P.L.J. et al., J. Immunol. 149: 3273-3277 (1992)]. The region showing an analogy is termed the cysteine-rich domain of the scavenger receptor (SRCR) which also existed as a repeat sequence in macrophage scavenging receptors [Matsumoto, A. et al., Proc. Nati Acad. Sci, USA 87: 9133-9137 (1990)] The CD6 T cell differentiation antigen [Aruffo, A et al., J. Exp. Med 174: 949-952 (1991)] and the like. Since the present protein is expressed specifically in the spleen. This protein is considered to be deeply associated with the functions of the spleen and also functions as a receptor in the same way as other members of the SRCR family. < HP01293 > (Sequences Nos. 5, 30, 55) The determination of the complete base sequence for the cDNA insert of the clone HP01293 obtained from the human liver cDNA libraries revealed the structure consisting of a 5 'non-translation region of 89 bp, an ORF of 1665 bp, and a 3' non-translation region of 134 bp. The ORF codes for a protein consisting of 554 amino acid residues with 12 transmembrane domains. Figure 8 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation did not reveal the formation of different bands and revealed the formation of fuzzy bands in the high molecular weight position. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the rat cation transporter (Genbank, Accession No. X78855). Table 5 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the mouse interstitial cell protein (MM). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 78.1% between whole regions.

Table 5 HP MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAISLSQ ******. ****** *********. *** ** .. *** **********. *. **. ******** RN MPTVDDVLEQVGEFGWFQKQAFLLLCLI SASLAPIYVGIVFLGFTPGHYCQNPGVAELSQ HP RCWSPAEELNYTVPGLGPAGEA-FLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLG *****. ************* .. ** **. **. *********. *. ***** . ** .. ***. **** RN RCGWSQAEELNYTVPGLGPSDEASFLSQCMRYEVDWNQSTLDCVDPLSSLVANRSQLPLG HP PCQDGWVYDTPGSSIVTEFNLVCADSW LDLFQSCLNAGFFFGSLGVGYFADRFGRKLCL ** .. *******************. *. **. ******. * ***. *** *** . ********** RN PCEHGWV? DTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRI CL HP I? TVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIM * *. ** .. ***** *. *. * **********. ****. * .. ********** ** ***. **.

RN LVTT VTSVSGVLTAVAPDYTSML FRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAIL HP YQMAFTVGLVALTGLAYA PHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAI **********. *. *. ***. *. ******************** ** ***********. * * # RN YQMAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQ RTTRAV HP KIMDHIAQ NGKLPPADIJCMLSIJ_? DVTEiU_SPSFADLFRTPRl_ ^. ** .. *******. ********. ****., ** *********** . ***. * ******* t # * RN RJMEQIAQKNGKVPPADLKlíLCLEEDASEKRSPSFADLFRT ^ HP LYQGLILHMGATSGNLYLDFLYSA VEIPGAFIALITIDRVGRIYPMAVSNL AGAACLV ******. *. *** .. ****** ** *** *. *** *. **** ***** m * # *** # ***** m RN LYQGLIMHVGATGANLYLDFFYS SLVEFPAAFIILVTIDRIGRIYPIAASNLVTGAACLL HP MIFISPDLHWI ^ IIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGII **** ... ***** ... *. **** ** .. **. *********** # **** ** ** t ***. ***.

RN ÍCtFIPHEIJIWLNVTLACLGRMGATIVLQMVCLVNAELYPTFIRNLGMMVCSALCDLGGIF HP TPFIVFRI? EVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETH DAENLG-RKAKPK ***. **** ***********. **** * ... *************** # # ***** ** f *. * RN TPFM \ n? RIJdí? RWQALPLILFGVLGLTAGAMTLLLPETKGVALPETIEEAENLGRRKSKAK HP ENTIYLKVQTSEPSGT ******. ***.,. *. * RN ENTIYLQVQTGKSSST In addition, the search for GenBank using the base sequence of the present cDNA revealed that there was no human gene and human EST that possessed the homology of 90% or more.

The rat cation transporter has been found as a membrane protein that is related to the excretion of drug in the kidney [Grundermann, D. et al., Nature 372: 549-552 (1994)]. Consequently, the protein of the present invention that is homologous to this transporter is considered to have a similar function and can be used for the diagnosis and treatment of diseases caused by the abnormality of this protein. In addition, since the present protein is considered to be related to drug excretion, the cells in which this protein is expressed can be used as a tool for designing drugs from these drugs. Additionally, since the present protein is expressed primarily in the liver and kidney, a molecule that is prepared to possess an affinity for this protein is applicable to the drug's release system in these tissues. < HP10013 > (Sequences Nos. 6, 31, 56) The determination of the complete base sequence for the cDNA insert of clone HP10013 obtained from the cDNA libraries of the human epidermoid carcinoma cell line KB revealed the structure consisting of a 5 'non-translation region of 96 bp, an ORF of 1053 bp, and a 3' non-translation region of 884 bp. The ORF codes for a protein consisting of 350 amino acid residues with a signal sequence at the N terminus and an internal transmembrane domain. Figure 9 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein functioned as a signal sequence in the N-terminus from the observation that the urokinase activity was detected in the culture medium, during transduction in the COS7 cells of an expression vector in which a HindIII-Eco065I fragment (treated with mung bean nuclease) containing a cDNA fragment encoding the 65 amino acid residues of the N-terminus in the present protein was inserted into the HindIII-EcoRV site of pSSD3. Therefore, the present protein is considered to be a type I membrane protein. The in vitro translation resulted in the formation of a 39 kDa translation product that was almost consistent with the molecular weight of 39.008 predicted by the ORF.

The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous with any of the known proteins. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there are some ESTs that possess 90% or more homology (eg, Accession No. HO7998), but none of them was shorter than the present cDNA. and did not contain the initiation codon < HP10034 > (Sequences Nos. 7, 32, 57) The determination of the complete base sequence for the cDNA insert of the HP 10034 clone obtained from the cDNA libraries of the HT-1080 human fibrosarcoma cell line revealed the consistent structure in a 5 'non-translation region of 175 bp, an ORF of 630 bp, and a 3' non-translation region of 106 bp. The ORF codes for a protein consisting of 209 amino acid residues with 4 transmembrane domains. Figure 10 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 21 kDa translation product that was almost consistent with the molecular weight of 22,432 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the human tumor associated antigen L6 (SWISS-PROT, Accession No. P30408). Table 6 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the tumor-associated L6 antigen of human (L6). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 31.8%.

Table 6 HP MVSSPCTQASSRTCSRILGLSLGTAALFAAGANVALLLPNWDVTYLLRGLLGRHAMLGTG *. *. * ** **. *. * L6 'MCYGKCARCIGHSLVGLALLCIAANILLYFPNGETKYASENHLSRFVWFFSG HP LWGGGLMVLTAA-ILISL-MGWRYGCFS - KSGLCRSVLTALLSGGLALLGALICFVTSG. **** .. *. * .. *. *. ** .. * .. * ... * *. * .... L6 IVGGGLL LLPAFVFIGLEQDDCCGCCGHENCGKRCAMLSSVLAALIGIAGSGYCVIVAA HP VAI? _DGPFC »ÍFDVSSFNQTQAWICYGYPFKDLHSRNYLYDRSLWNSVCLEPSAAVVWHVSL .. *. **. *. *. *. * ** * * * .. * **. * *. *** L6 LGLAEGPLCL-D SLGQWNYTFASTE- -GQYLLDTSTWSE-CTEPKHIVE NVSL HP FSALLCISLLQLLLVWHVINSLLGLFCSLCEK ** ** * ... *** .. ** •. * .. * L6 FSILLALGGIEFILCLIQVINGVLGGICGFCCSHQQQYDC In addition, the search for GenBank using the base sequence of the present cDNA revealed that no human gene existed and Est possessed the homology of 90% or more. The human tumor-associated L6 antigen is a member of the membrane superfamily of TM4 antigen proteins that are abundantly expressed on the cell surface of human tumors [Marken, J. S. et al., Proc Nati. Acad Sci. USA 89: 3503-3507 (1992)]. Since these membrane antigens are specifically expressed in specific cells and in cancer cells, an antibody that is prepared in order to bind to this antigen is applicable for a variety of diagnosis and as a carrier for drug release. In addition, the cells in which said membrane antigen is expressed by transduction of the membrane antigen gene are applicable for the detection of the corresponding ligand. < HP10050 > (Sequences Nos. 8, 33, 58) The determination of the complete base sequence for the cDNA insert of the HP 10050 clone obtained from the cDNA libraries of the HT-1080 human fibrosarcoma cell line revealed the consistent structure in a 5 'non-translation region of 9 bp, an ORF of 492 bp, and a 3' non-translation region of 100 bp. The ORF codes for a protein consisting of 163 amino acid residues with a transmembrane domain. Figure 11 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 23 kDa translation product that was almost consistent with the molecular weight of 18,364 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any of the known proteins. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there are some ESTs that possessed 90% or more homology (eg, Accession No. HO3117), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. < HP10071 > (Sequences Nos. 9, 34, 59) The determination of the complete base sequence for the cDNA insert of the HP 10071 clone obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a non-human region. 5 'translation of 46 bp, an ORF of 279 bp, and a 3' non-translation region of 69 bp. The ORF codes for a protein consisting of 92 amino acid residues with 2 transmembrane domains. Figure 12 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 12 kDa translation product that was almost consistent with the molecular weight of 10,094 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any of the known proteins.

In addition, searching for GenBank using the base sequence of the present protein revealed that there are some ESTs that possessed 90% or more homology (eg, Accession No. R097442), but many sequences were not distinct and the same ORF that the one in the present cDNA was not identified. < HP10076 > (Sequences Nos. 10, 35, 60) The determination of the complete base sequence for the cDNA insert of the clone HP 10076 obtained from the cDNA libraries of the U937 human lymphoma cell line revealed the structure consisting of a 5 'non-translation region of 81 bp, an ORF of 519 bp, and a 3' non-translation region of 132 bp. The ORF encoded for a protein consisting of 172 amino acid residues with 2 transmembrane domains. Figure 13 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein remained in the membrane from the observation that the urokinase secretion was not identified during transduction in COS7 cells of an expression vector in which a fragment of HindIII-Eco0651 (previously treated with nuclease mung bean) containing a cDNA fragment encoding the 167 amino acid residues of the N-terminus in the present protein was inserted into the HindIII-EcoRV site of pSSD3. The in vitro translation resulted in the formation of a 24 kDa translation product that was almost consistent with the molecular weight of 18,450 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the baker yeast hypothetical membrane protein of 23.1 kDa (SWISS-PROT Accession No. P34222). Table 7 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the hypothetical 23.1 kDa yeast membrane protein (SC). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 47.5%. in the region of 139 amino acid residues of the termination C.

Table 7 HP HEYLAHPSTLGLAVGVACGMCLGWS SC MITSFIiffiiaíTVSSNYTIALWATFTAISFAVGYQI? TSNASSTKKSSATLLRSKEMKEGK HP LRVCFGMLPKSKTSKTHTDTESEASILGD- SGEYZMILWRNDLKMGKGKVAAQCSHAAV ... * .. * .. *. *. **. * **. *. ** *. ***. ****. ***. SC LHNBTDEEESESEDESEDEDTSTSLNDIPGEV? MALVIRQDLGMTKGKIAAQCCHAAL HP SAYKQI QR NP__íIJ? Q EYCGQPKVVV APDEEXLIALI ^ HAKM GLT S IQD * ... * .. ** * .. * **. * ... * **. *. . * *. * ** *. * SC SCFRH_ATNPARASYNPIMT RWI_NAGQAKITI_KCPDKFTMDELYAKAISLGVNAAVIHD. HP AGRTQIAPGSQTVLGIGPGPADLID VTGHL LY *******. ** **** ** * ... * .. **. **** SC AGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY In addition, searching for GenBank using the base sequence of the present protein revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. T74847), but many sequences were not distinct and the same ORF that the one in the present cDNA was not identified. < HP10085 > (Sequences Nos. 11, 36, 61) The determination of the complete base sequence for the cDNA insert of the HP 10085 clone obtained from the cDNA libraries of the human lymphoma cell line U937 revealed the structure consisting of a 5 'non-translation region of 150 bp, an ORF of 450 bp, and a 3 'non-translation region of 97 bp. The ORF codes for a protein consisting of 149 amino acid residues with a transmembrane domain at the N-terminus. Figure 14 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein remained in the membrane from the observation that the urokinase secretion was not identified during transduction in COS7 cells of an expression vector in which a fragment of HindlII-EcoRI (after the Klenow treatment ) containing a cDNA fragment encoding the 57 amino acid residues of the N-terminus in the present protein was inserted into the HindIII-EcoRV site of pSSD3. Therefore, the present protein is considered to be a type II membrane protein. The in vitro translation resulted in the formation of a translation product of 20 kDa that was almost consistent with the molecular weight of 17,307 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the early activation human antigen CD69 (SWISS-PROT Accession No. Q07108). Table 8 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the early activation human antigen CD96 (CD). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 36.6%. in the region of 112 amino acid residues of the termination C.

Table 8 HP MMTKHKKCFI CD MSSENCFVAENSSI ^ PESGQENDATSPHFSTRHEGSFQVPVLCAVM_TyVFITILIIALIA HP IVGVLITTNIIXLIVKLTRDSQSLCPYDWIGFQNKCYYFS EEGDWNSSKYNCSTQHADL. *. *. ** * * CD LSVGQYNCPGO.YTFSMPSDSHVSSCSEDWVGYQRKCYFISTVKRSWTSAQNACSEHGATL HP TIIDNIEEMNFRRYKCSSDHWIGUOMAKNRTGWVDGATFTKSFGMRGSEGCAYLSDDG. **. .. ****. ** ... **. *** .. **. CD AVIDSEKDMNFLKRYAGREEHWVGLK EPGHPWKWSNGKEFNNWFNVTGSDKCVFLKNTE HP AATARCYTERKWICRKRIH ***. * CD VSSMECEKNLYWICNKPYK In addition, searching for GenBank using the base sequence of the present protein revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. H11808), but many sequences were not distinct and the same ORF that the one in the present cDNA was not identified. The early activation human antigen CD69 is a glycoprotein that appears on the surface of activated lymphocytes and a member of the type C lectin superfamily [Hamann, J. et al., J. Immunol. 150: 4920-4927 (1993)]. Since these membrane antigens are expressed specifically in some specific cells, an antibody that is prepared in order to bind to this antigen is applicable to a variety of diagnosis and as a carrier for drug release. In addition, cells in which said membrane antigen is expressed by transduction of the membrane antigen gene are applicable for the detection of the corresponding ligand. < HP 10122 > (Sequences Nos. 12, 37, 62) The determination of the complete base sequence for the cDNA insert of clone HP10122 obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a non-translational region. 'of 138 bp, an ORF of 567 bp, and a 3' non-translation region of 481 bp. The ORF codes for a protein consisting of 188 amino acid residues with two transmembrane domains. Figure 15 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 22 kDa translation product that was almost consistent with the molecular weight of 21,175 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed the homology of 90% or more (eg, Accession No. T80360), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. < HP10136 > (Sequences Nos. 13, 38, 63) The determination of the complete base sequence for the cDNA insert of clone HP10136 obtained from the cDNA libraries of the human lymphoma cell line U937 revealed the structure consisting of a region of no translation 5 'of 81 bp, an ORF of 648 bp, and a non-translation region of 680 bp. The ORF codes for a protein consisting of 215 amino acid residues with a transmembrane domain at the C terminus. Figure 16 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 28 kDa translation product that was almost consistent with the molecular weight of 24,740 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the baker's yeast protein transport protein SLY2 (SWISS-PROT, Accession No. P22214). Table 9 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the transport protein of baker yeast protein SLY2 (SC). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 36.1%. in the complete regions.

Table 9 HP MV LTMIARVADGLP ^ SMQISDEQSGRDLQQYQSqAKQLFRiaLNE SPTRCTLEAGAMT * * * ***** **. * ***. *.

SC MIKSTLIYRE-DGLPLCTSVDNENDPS- LFEQ QKVKIWSRLTPQSATEATLESGSFE HP FHYIIEQGVCYLVLCEAAFP KI? FAYLEDLHSEFDEQHGKKVPTVS-RPYSFIEFDTFI. **. . *. *. *. ** ... * .. ***. **. *. ** *. . *** * .. **. *. SC IHYl ^ SMVY r ICESGY RNl ^ SY iro ^ QE EHSFA ^ HP QKT KLYIDSRARRNLGSINTELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSEK *. *** * *, **. . * **. * .. ** *** ._ * **. ** sc QMTKKSYSDHECVQDNLDQLNQELVGVKQ: I ^ HP YRQDAKYLNMRSTYAKLAAVAVFFIMLIVYVRFWWL ** .. *. *** SC YRKSAQKINFDLLISQYAPI-VIVAFFFVFL-FWWIFLK In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed the homology of 90% or more (eg, Accession No. R80136), but were shorter in length than the present cDNA and no molecule containing the initiation codon was identified. It is known that the transport protein of baker yeast SLY2 protein is essential for the transport of endoplasmic reticulum protein to Golgi and that it is also associated with cell cycle control [Dascher, C: et al., Mol. Cell. Biol.11: 872-885 (1991)]. Therefore, the cDNA of the present invention can be used for the production of the present protein as well as for the diagnosis and treatment of diseases caused by the abnormality of the present protein. < HP10175 > (Sequences Nos. 14, 39, 64) The determination of the complete base sequence for the cDNA insert of clone HP10175 obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a non-translational region. 'of 173 bp, an ORF of 339 bp, and a 3' non-translation region of 462 bp. The ORF codes for a protein consisting of 112 amino acid residues with 4 transmembrane domains. Figure 17 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a translation product of 13 kDa that was almost consistent with the molecular weight of 11,564 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. W52852), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. < HP10179 > (Sequences Nos. 15, 40, 65) The determination of the complete base sequence for the cDNA insert of clone HP10179 obtained from the cDNA libraries of the human epidermoid carcinoma cell line KB revealed the structure consisting of a 5 'non-translation region of 121 bp, an ORF of 345 bp, and a 3' non-translation region of 459 bp. The ORF codes for a protein consisting of 114 amino acid residues with 4 transmembrane domains. Figure 18 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 14 kDa translation product that was almost consistent with the molecular weight of 12,078 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. However, this protein was analogous to the protein encoded by the HP 10175 cDNA clone of the present invention. Table 10 indicates the comparison of the amino acid sequences between the protein encoded by HP 10179 and the protein encoded by HP 10175. "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 80.8%. in the complete regions.

Table 10 179 MEKPLFPLVPLHWFGFGYTALWSGGIVGYVKTGSVPS AAGLLFGSLAGLGAYQLYQDP. . **********. *** **** **** *********************** *** 175 MQDTGSWPLHWFGFGYAALVASGGIIGYVKAGSVPSLAAGLLFGSLAGLGAYQLS DP 179 RNVWGFIAATSVTFVGVMGMRSYYYGKFMPVGLIAGASLIilAA VGV? Lbl ÍTSD **** ** *** *. . *. **** *, *****. **********. ***** *. 175 RNVWVT'L-ATSGTI_AGIMGMRI? YHSGKFMPAGLIAGASLLMVAKVGVSMFNRPH In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. N55991), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. < HP10196 > (Sequences Nos. 16, 41, 66) The determination of the complete base sequence for the cDNA insert of the clone HP10196 obtained from the cDNA libraries of the HT-1080 human fibrosarcoma cell line revealed the structure consisting of a 5 'non-translation region of 9 bp, an ORF of 984 bp, and a 3' non-translation region of 122 bp. The ORF codes for a protein consisting of 327 amino acid residues with a transmembrane domain at the N-terminus. Figure 19 describes the profile of hydrophobicity / hydrophilicity of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein remained in the membrane from the observation that the urokinase secretion was not identified during transduction in COS7 cells of an expression vector in which a HindIII-BglII fragment (after Klenow treatment ) containing a cDNA fragment encoding the 162 amino acid residues of the N-terminus in the present protein was inserted into the HindIII-EcoRV site of pSSD3. Thus, the present protein is considered to be a type II membrane protein. The in vitro translation resulted in the formation of a translation product of 37 kDa that was almost consistent with the molecular weight of 36,163 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. TI 7026), but were shorter in length than the present cDNA. and no molecule containing the initiation codon was identified. < HP10235 > (Sequences Nos. 17, 42, 67) The determination of the complete base sequence for the cDNA insert of clone HP 10235 obtained from the cDNA libraries of the HT-1080 human fibrosarcoma cell line revealed the consistent structure in a 5 'non-translation region of 5 bp, an ORF of 1122 bp, and a 3' non-translation region of 594 bp. The ORF codes for a protein consisting of 373 amino acid residues with 11 transmembrane domains. Figure 20 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation did not reveal the formation of different bands and revealed the formation of fuzzy bands in the high molecular weight position. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was analogous to the human nucleolar protein HNP36 (EMBL Accession No. X86681). Table 11 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the human nucleolar protein HNP36 (NP). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 45.3%. in the complete regions. Table 11 HP MTLCAMLPLLLF YLNSFLH RIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVIT HP HIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSE * ... ****. *. ******* *. * .. *., .. *******, ** .. **. ., ***. ..

NP MASVCFINSFSAVLGSLFGQLGTMPSTYSTLFLSG? GLAGIFAAAMLLSMASGVDAET HP SAFGYFITACAVIILTIICYLGLPRLEFYRYYQ LKLEGPGEQE-TKLDLISKGEE- **. ***** .., * ... *. ***. **. *. * ***. *. . ** **. *. .. *.

NP SAI? YFITPYVGIUlSIVCYLSLPHU ^ ARYYLAireSSQAQAQELETKAELLQSDENGIP HP - PRAGKEESGVSV- SNSQPTNESHSIK AILKNISVLAFSVCFIFTITIGMFPA *. »** • • • • • • • • • • • • • • • • • • • • • • • • • NP SSPQKVALTLJ3LDLEKEPESEPDEPQKPGKPSVFTVFKIWLTALCLVLVFTVTLSVFPA HPVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARL. *. *, ** * ... * * .. *** ***. ********. *. ** .. *** ** ** *.

NP ITAMVTSS-TSPGKWS FFNPICCFLLFNIl ^ WI? RSLTSYFLWPDiOSRLLPI VCI? F HP VFVPLLLLCNII0PIU.YL VVFEHDAWFIFFMAAFAFSNGY1? SLCMCFGPKECV PAEAET. **** .. ** ... *. * ... *. **. ** ** ** ** *****. ** ** .. * .. * * * *, NP LFVPLFMLCHVPQRSRLPILFPQDAYFITFMLLFAVSNGYLVSLTMCLAPRQVLPHEREV HP AGAIMAFFLCLGLAGAVFSFLFRAIV ***. *. *** ** *, **. ****, * .. NP AGALMTFFLALGLSCGASLSFLFKALL In addition, the search for GenBank using the base sequence of the protein of the present invention revealed that there were some ESTs that possessed the homology of ninety percent or more (by example, Accession No. R57372), but it was not possible to assess whether these ESTs with partial sequences encoded for the same protein as the protein of the present invention. The human nucleolar protein HNP36 has been found as a product gene that plays a role in the growth and multiplication of cells [Williams, J. B. & Lanahan, A. A., Biochem. Biophys. Res. Commun. 213: 325-333 (1995)]. As a consequence of this, the protein of the present invention, which is homologous to said protein, is considered as a home protein essential for the growth and multiplication of cells and therefore can be used for the diagnosis and treatment of diseases caused for the abnormality of the protein. < HP10297 > (Sequences Nos. 18, 43, 68) The determination of the complete base sequence for the cDNA insert of the clone HP 10297 obtained from human stomach cancer cDNA libraries revealed the structure consisting of a 5 'non-translation region of 62 bp, an ORF of 552 bp, and a 3' non-translation region of 890 bp. The ORF codes for a protein consisting of 183 amino acid residues with a signal sequence at the N terminus and an inner transmembrane domain. Therefore, the present protein is considered to be a type I membrane protein. Figure 21 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 24 kDa translation product that was almost consistent with the molecular weight of 20, 574 predicted by the ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. R47823), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. < HP 10299 > (Sequences Nos. 19, 44, 69) The determination of the complete base sequence for the cDNA insert of the HP 10299 clone obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a non-translation region. 5 'of 92 bp, an ORF of 351 bp, and a 3' non-translation region of 89 bp. The ORF codes for a protein consisting of 116 amino acid residues with a transmembrane domain at the N-terminus. Figure 22 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the protein of the present invention remained in the membrane from the observation that the urokinase secretion was not identified during transduction in COS7 cells of an expression vector in which a fragment of HindIII-VspI (after of subjecting it to the Klenow treatment) containing a cDNA fragment encoding the 65 amino acid residues of the N-terminus in the present protein was inserted into the HindlII-PmaCI site of pSSD3. Therefore, the present protein is considered to be a type II membrane protein. The in vitro translation resulted in the formation of a 13 kDa translation product that was almost consistent with the molecular weight of 12,498 predicted by the ORF. Searching the protein database using the amino acid sequence of the protein of the present invention revealed that the protein was analogous to the hypothetical membrane protein of the baker's 16.5 kDa yeast (SWISS-PROT, No. Access P42834). Table 12 illustrates the comparison between the amino acid sequences of the human protein of the present invention (HP) and the hypothetical membrane protein of baker yeast of 16.5 kDa (SC). In Table 12 it should be understood that "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." Represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 53.0%. in the region of 66 amino acid residues of the termination C.

Table 12 HP MASTVVAVGLTIAAAGFAGRYVLQAMKHMEP VKQVF SC MV PIIIGI? VTMVALSVKSGLNAWTVYKTLSPLTIAKLNNIRIENPTAGYRDALKFKSS HP QSLPKSAFSGGYYRGGFEPKMTKREAALILGVSP TANKGKIRDAHRRIMLLNHPDK *. ***. *. **. . ** *** . *. . . . ** *. **** SC LIDEELKNRLNQYQGGFAPRMTEPEALLILDISAREINHLDEKXLKKKHRKAMVRNHPDR HP GGSPYIAAKINEAKDLLEGQAKK *****. ******** .. ** SC GGSPYMAAKINEAKEVLERSVLLR R In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. R27748), but many sequences were not distinct and the sequence was not identified. same ORF as that in the present cDNA. < HP10301 > (Sequences Nos. 20, 45, 70) The determination of the complete base sequence for the cDNA insert of the clone HP 10301 obtained from the cDNA libraries of the human epidermoid carcinoma KB cell line revealed the structure consisting of a 5 'non-translation region of 91 bp, an ORF of 459 bp, and a 3' non-translation region of 1 12 bp. The ORF codes for a protein consisting of 152 amino acid residues with 4 transmembrane domains. Figure 23 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of an 18 kDa translation product that was almost consistent with the molecular weight of 16,516 predicted from ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. N28828), but many sequences were not distinct and the sequence was not identified. same ORF as that in the present cDNA < HP 10302 > (Sequences No. 21, 46, 71) The determination of the complete base sequence for the cDNA insert of clone HP 10302 obtained from the human liver cDNA libraries revealed the structure consisting of a non-translational region. 'of 133 bp, an ORF of 1680 bp, and a 3' non-translation region of 560 bp. The ORF codes for a protein consisting of 559 amino acid residues with 12 transmembrane domains. Figure 24 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation did not reveal the formation of different bands and revealed the formation of fuzzy bands in the high molecular weight position. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. N72434), but were shorter in length than that of the present cDNA. and no molecule containing the initiation codon was identified. < HP10304 > (Sequences Nos. 22, 47, 72) The determination of the complete base sequence for the cDNA insert of clone HP 10304 obtained from the human osteosarcoma cDNA libraries U-2 revealed the structure consisting of a region of no 5 'translation of 10 bp, an ORF of 993 bp, and a 3' non-translation region of 313 bp. The ORF codes for a protein consisting of 330 amino acid residues with a signal sequence at the N terminus and an inner transmembrane domain. Therefore, the present protein is considered to be a type I membrane protein. Figure 25 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a translation product of 36 kDa that was almost consistent with the molecular weight of 36,840 predicted by ORF. The search of the protein database using the amino acid sequence of the present protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed the homology of 90% or more (eg, Accession No. N26840), but the same ORF was not identified as that in the present cDNA. < HP10305 > (Sequences Nos. 23, 48, 73) The determination of the complete base sequence for the cDNA insert of clone HP 10305 obtained from the human osteosarcoma cDNA libraries U-2 OS revealed the structure consisting of a region of non-5 'translation of 109 bp, an ORF of 327 bp, and a 3' non-translation region of 457 bp. The ORF codes for a protein consisting of 108 amino acid residues with a transmembrane domain. Figure 26 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It was indicated that the present protein remained in the membrane from the observation that the urokinase secretion was not identified during transduction in COS7 cells of an expression vector in which a HindIII-Apal fragment (treated with nuclease of mung bean) containing a cDNA fragment encoding the 162 amino acid residues of the N-terminus in the present protein was inserted into the HindlII-PmaCI site of pSSD3. Therefore, the present protein is considered to be a type II membrane protein. The in vitro translation resulted in the formation of a translation product of 15 kDa that was almost consistent with the molecular weight of 12,199 predicted by the ORF. The search of the protein database using the amino acid sequence of the protein revealed that it was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. H02768), but many sequences were not distinct and the sequence was not identified. same ORF as that in the present cDNA. < HP10306 > (Sequences Nos. 24, 49, 74) The determination of the complete base sequence for the cDNA insert of the clone HP10306 obtained from cDNA libraries osteosarcoma U-2 OS human revealed the structure consisting of a region of no translation 5 '229 bp, an ORF of 306 bp, and a region of no translation 3' 155 bp. The ORF codes for a protein consisting of 101 amino acid residues with 2 transmembrane domains. Figure 27 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. The in vitro translation resulted in the formation of a 14 kDa translation product that was almost consistent with the molecular weight of 12,029 predicted from ORF. The search of the protein database using the amino acid sequence of the protein revealed that the protein was not analogous to any known protein. In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. H44711), but many sequences were not distinct and the sequence was not identified. same ORF as that in the present cDNA < HP10328 > (Sequences Nos. 25, 50, 75) The determination of the complete base sequence for the cDNA insert of the clone HP 10328 obtained from cDNA libraries cell line KB human epidermoid carcinoma revealed the structure consisting of a region of no translation 5 '117 bp, an ORF of 1119 bp, and a region of no translation 3' 950 bp. The ORF codes for a protein consisting of 372 amino acid residues with a transmembrane domain. Figure 28 describes the hydrophobicity / hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. It indicated that this protein remained in the membrane from the observation that the secretion of urokinase was not identified during transduction in COS7 cells of an expression vector in which a fragment HindlII- PMACI (treated with nuclease mung bean) containing a cDNA fragment encoding the 129 amino acid residues of the N-terminus in the present protein was inserted into the HindIII-Smal site of pSSD3. Therefore, it is considered that this is a type II membrane protein. The in vitro translation resulted in the formation of a translation product of 41 kDa that was almost consistent with the molecular weight of 42,514 predicted by ORF. The search of the protein database using the amino acid sequence of the protein revealed that it was analogous to the Drosophila neurological secretory signal protein (Gen Bank Accession No. U41449). Table 13 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the neurological secretory signal protein of Drosophila (DM). "-" represents an opening, "*" represents an amino acid residue identical to that in the protein of the present invention, and "." represents an amino acid residue analogous to that in the protein of the present invention. Both proteins have a homology of 38.6%. in the middle region of 202 amino acid residues. Table 13 HP MKyLRHRRPNATLILAIGAFTLLLFSLLVSPPTC VQEQPPAIPEALAWPTPPTRPAPAP DM MQSKHRKLLLRCLLVLPLILLVDYCGLLTHL HP CHANTSMVTHPDFATQPQHVQNFLLYRHCRHFPLLQDVPPSKCAQPVFLLLVIKSSPSNY DM HEUIFERHFHYPIJNDDTGSGSASSGLDKFAYLRVPSFTAEVPVDQPARLTMLIKSAVGNS HP VRRELIiRRTWGRER VRGL LRLLFLVGTASNPHEARKVNRLLELEA THGDII ^ WDFHD ***. ***** * **. **. *** *. . *. . . ****** ** * DM RRREAIRRTWGYEGRFSDVHLRRVFLLGTAEDS - EKDVAW ESREHGDILQADFTD HP SFFNLTLKQVLFLQWQETRCANASFVLNGDDDVFAHTDNMVFYL QDHDPGRHLFVG ** *** * * *** * * *..... **. * DM AYFNNTIJCTMLGMRWASEQFNRSEFYLFVDDDYYVSAia? VLKFLGRGRQSHQPE-LLFAG HP QLIQNVGPIRAFWS YYVPEWTQNERYPPYCGGGGFLLSRFTAAAIJIRAAHVLDIFPID. *. . *. *. ** **. . *. ***. *. *. **. DM-TSPIJUIKFSKWYVSLEEYPFDRWPPYVTAGAFILSQKALRQLYAASVHLPLFRFD HVFQ HP DVFL (^ ^ CLELEGI PASHSGIRTSGVRAPSQHLSSFDPCFYRDLLLVHRFLPYEMLI_M D **. **. DM DVYLGIVALKAGISLQHCDDFRFHRPAY GPDSYS SVIASHEFGDPEEMTRVWNECRSAN HP ALNQPNLTCGNQTQIY DM YA In addition, searching for GenBank using the base sequence of the present cDNA revealed that there were some ESTs that possessed 90% or more homology (eg, Accession No. R75815), but were shorter in length than the present cDNA and no molecule containing the initiation codon was identified. The present invention provides human proteins having transmembrane domains, cDNAs encoding said proteins and eukaryotic cells expressing said cDNA. All of the proteins of the present invention are putative proteins that control the proliferation and differentiation of cells, because said proteins exist in the cell membrane. Therefore, the proteins of the present invention can be used as pharmaceutical compounds or as antigens for the preparation of antibodies against said proteins. Additionally, said DNAs can be used for the expression of large amounts of said proteins. Cells that express large amounts of membrane proteins with transfection of the genes of these membrane proteins can be applied for the detection of the corresponding ligands, the screening of novel low molecular weight drugs, and the like. In addition to the activities and uses described above, the polynucleotides and proteins of the present invention may present one or more of the biological uses or activities (including those associated with assays cited herein) that are identified below.

The uses or activities described for the proteins of the present invention may be provided by the administration or use of such proteins or by the administration or use of polynucleotides that encode such proteins (such as, for example, in the therapy of genes or vectors suitable for the introduction of DNA).

Uses in Research and Utilities The polynucleotides provided by the present invention can be used by the research community for various purposes. The polynucleotides can be used to express recombinant protein for analysis, characterization or therapeutic use; as markers for tissues in which the corresponding protein is expressed preferentially (either constitutively or in a particular stage of tissue differentiation or development or in diseased states); as molecular weight markers on Southern gels; as markers or flags of chromosomes (when marked) to identify chromosomes or for mapping of related gene positions; for comparison with endogenous DNA sequences in patients to identify potential genetic disorders; as probes for hybridization and thus discover new related DNA sequences; as a source of information to derive primary PCR for genetic screening; as a probe for "subtracting" known sequences in the process of discovering new polynucleotides; for the selection and labeling of oligomers for binding to a "genetic chip" or other support, including for the examination of expression patterns; to generate anti-protein antibodies using DNA immunization techniques; and as an antigen to generate anti-DNA antibodies or to stimulate another immune response: Where the polynucleotide codes for a protein that binds or potentially binds to another protein (such as, for example, in a receptor-ligand interaction) , the polynucleotide can also be used in interaction trap assays (such as, for example, that described in Guris et al., Cell 75: 791-803 (1993)) to identify polynucleotides that encode the other protein with which it occurs the binding or to identify inhibitors of the binding interaction. The proteins provided by the present invention can similarly be used in assays to determine biological activity, including in a panel of multiple proteins for high-throughput screening; to generate antibodies or to produce another immune response; as a reagent (including marker reagent) in assays designed to quantitatively determine levels of the protein (or its receptor) in biological fluids; as markers for tissues in which the corresponding protein is preferentially expressed (either constitutively or at a particular stage of tissue differentiation or development or in a diseased state); and, of course, to isolate correlative receptors or ligands. Where the protein binds or potentially binds to another protein (such as, for example, in a receptor-ligand interaction), the protein can be used to identify the other protein with which the binding occurs or to identify inhibitors of the union interaction. The proteins involved in these binding interactions can also be used to screen peptides or small inhibitors of molecules or agonists of the binding interaction. Any of these research utilities are capable of being developed in reactive grade or in game format (kit) for commercialization as research products. The methods for performing the uses listed above are well known to those skilled in the art. References describing such methods include, without limitation, "Molecular Cloning: A Laboratory Manual", 2nd ed. Cold Spring Harbor Laboratory Press, Sambrook, J., E.F. Fritsch and T. Maniatis eds., 1989, and "Methods in Enzymology: Guide to Molecular Cloning Techniques", Academic Press, Berger, S.L. walk. Kimmel eds., 1987.

Nutritional Uses The polynucleotides and proteins of the present invention can also be used as nutritional sources or supplements. Such uses include, without limitation, use as an amino acid or protein supplement, use as a carbon source, use as a nitrogen source and use as a carbohydrate source. In such cases the protein or polynucleotide of the invention can be added to the feed of a particular organism or it can be administered as a separate solid or liquid preparation, such as in the form of a powder, pills, solutions, suspensions or capsules. In the case of microorganisms, the protein or polynucleotide of the invention can be added to the medium in or on which the microorganism is cultured.

Cytokine and Proliferation Activity / Cell Differentiation A protein of the present invention can exhibit cell proliferation, cytokine (either induction or inhibition) or cell differentiation (either induction or inhibition) activity, or it can induce production of other cytokines in certain cell populations. Many protein factors discovered to date, including all known cytokines, have exhibited activity in one or more factor-dependent cell proliferation assays, and hence the assays serve as a convenient confirmation of cytokine activity. The activity of a protein of the present invention is evidenced by one of a number of routine factor-dependent cell proliferation assays for cell lines including, without limitation, 32D, DA2, DA1G, UNCLE, B9, B9 / 11, BaF3 , MC9 / G, M + (preB M +), 2E8, RB5, DA1, 123, TI 165, HT2, CTLL2, TF-1, Mo7e and CMK. The activity of the protein of the invention may, among other means, be measured by the following methods: Assays for proliferation of thymocytes or T cells include, without limitation, those described in Current Protocols in Immunology, Ed. By J.E. Coligan, A.M. Kruisbeek, D.H. Marguiles, E.M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley Interscience (Chapter 3, In Vitro Assays for Mouse Lymphocyte Function 3.1-3.19; Chapter 7, Immunologic Studies in Humans); Takai et al., J. Immunol. 137: 3494-3500, 1986; Bertagnolli et al., J. Immunol. 145: 1706-1712, 1990; Bertagnolli et al., Cellular Immunology 133: 327-341, 1991; Bertagnolli, et al., J. Immunol. 149: 3778-3783, 1992; Bowman et al., J. Immunol. 152: 1756-1761, 1994. Assays for determining cytokine production and / or proliferation of spleen cells, lymph node cells or thymocytes include, without limitation, those described in: Polyclonal T cell stimulation, Kruisbeek, A.M. and Shevach. In Current Protocols in Immunology. J.E.e.a. Coligan eds. Vol. 1 pp. 3.12.1-3.12.14, John Wiley and Sons, Toronto, 1994; and Measurements of mouse and human Interferon ?, Schreiber, R.D. In Current Protocols in Immunology, J.E.e.a. Coligan eds. Vol 1 pp. 6.8.1-6.8.8, John Wiley and Sons, Toronto, 1994. Trials to determine the proliferation and differentiation of hematopoietic and lymphopoietic cells include, without limitation, those described in: Measurement of Human and Murine Interleukin 2 and Interleukin 4, Bottomly, K., Davis, LS and Lipsky, P.E. In Current Protocols in Immunology. J.E.e.a Coligan eds. Vol 1 pp. 6.3.1-6.3.12, John Wiley and Sons, Toronto. 1991; deVries et al., J. Exp. Med. 173: 1205-1211, 1991; Moreau et al., Nature 336: 690-692, 1988; Greenberger et al., Proc. Nati Acad. Sci. U.S.A. 80: 2931-2938, 1983; Measurement of mouse and human interleukin 6 - Nordan, R. In Current Protocols in Immunology. J.E.e.a Coligan eds. Vol 1 pp. 6.6.1-6.6.5, John Wiley and Sons, Toronto. 1991; Smith et al., Proc. Nati Acad. Sci. U.S.A. 83: 1857-1861, 1986; Measurement of human Interleukin 11 - Bennett, F. Giannotti, J. Clark, S.C. and Turner, K.J. In Current Protocols in Immunology. J.E.e.a Coligan eds. Vol 1 pp. 6.15.1, John Wiley and Sons, Toronto. 1991. Measurement of mouse and human Interleukin 9 - Ciarletta, A. Giannotti, J., Clark, S.C. and Turner, K.J. In Current Protocols in Immunology. J.E.e.a Coligan eds. Vol 1 pp. 6.13.1, John Wiley and Sons, Toronto. 1991. Assays to determine the responses of T cell clones to antigens (which will identify, among others, proteins that affect the interactions of APC-T cells as well as the effects of direct T cells by measuring proliferation and cytokine production) include , without limitation, those described in: Current Protocols in Immunology, Ed by JEea Coligan, AM Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro Assays for Mouse Lymphocyte Function; Chapter 6, Cytokines and their cellular receptors; Chapter 7, Immunologic studies in Humans); Weinberger et al., Proc. Nati Acad. Sci. U.S.A. 77: 6091-6095, 1980; Weinberger et al., Eur. J. Immun. 1 1: 405-41 1, 1981; Takai et al., J. Immunol. 137: 3494-3500, 1986; Takei et al, J. Immunol. 140: 508-512, 1988.

Immunological Stimulation or Suppression Activity A protein of the present invention may also exhibit immunological stimulation or immune suppression activity, including without limitation the activities for which assays have been described herein. A protein may be useful in the treatment of various immune deficiencies and disorders (including severe combined immunodeficiency (SCID)), for example, in the regulation (up or down) of the growth and proliferation of T and / or B lymphocytes, as well as carrying out the cytolytic activity of NK cells and other cell populations. These immunological deficiencies can be genetic or viral (eg, HIV) as well as bacterial or fungal infections, or they can result from autoimmune disorders. More specifically, infectious diseases caused by viruses, bacteria, fungi or other infection can be treated using a protein of the present invention, including HIV infections, hepatitis viruses, herpes viruses, _ mycobacteria, lesmania spp, malaria spp and various fungal infections such as candidiasis. Of course, in this regard, a protein of the present invention may also be useful where it is generally indicated to strengthen the immune system, for example, in the treatment of cancer. Autoimmune disorders that can be treated using a protein of the present invention include, for example, connective tissue disease, multiple sclerosis, systemic lupus erythromatosis, rheumatoid arthritis, autoimmune pulmonary inflammation, Guillain-Barre syndrome, autoimmune thyroiditis, diabetes mellitus dependent of insulin, myasthenia gravis, graft versus host disease and eye inflammation disease by autoimmunity. Said protein of the present invention may also be useful in the treatment of reactions and allergic conditions, such as asthma (particularly allergic asthma) and other respiratory problems. Other conditions, in which immunological suppression is desired (including, for example, organ transplantation) can also be treated using a protein of the present invention. The use of the proteins of the invention may also be possible for immune responses, in a number of ways. The hyporegulation may be in the form of inhibition or blocking of an immune response already in progress, or may involve the prevention of the induction of an immune response. The functions of activated T cells can be inhibited by suppressing T cell responses or by inducing specific tolerance in T cells, or both. The immunosuppression of T cell responses is generally an active, not antigen-specific process, which requires continuous exposure of the T cells to the suppressive agent. Tolerance, which involves the induction of non-response or anergy in T cells, is susceptible to distinction from immunosuppression because it is generally antigen-specific and persists after the exposure to the tolerance-creating agent has ended. Operationally, tolerance can be demonstrated by the lack of a T cell response under re-exposure to a specific antigen in the absence of the tolerance creating agent. The hyporegulation or prevention of one or more antigenic functions (including without limitation functions of B lymphocyte antigen (such as, for example, B7)), for example, preventing the synthesis of high level lymphokine by activated T cells, will be useful in situations of tissue, skin and organ transplants and in graft versus host disease (GVHD). For example, blocking T cell function should result in reduced destruction of tissue in tissue transplants. Typically, in tissue transplants, rejection of the transplant is initiated through recognition as foreign by the T cells, followed by an immune reaction that destroys the transplant. The administration of a molecule that inhibits or blocks the interaction of a B7 lymphocyte antigen with its natural ligand (s) (s) in immune cells (such as a soluble monomeric form of a peptide having B7-2 activity alone or in conjunction with a monomeric form of a peptide having an activity of another B lymphocyte antigen (e.g., B7-1, B7-3) or blocking antibody), before transplantation can lead to the binding of the molecule to the natural ligand (s) in the immune cells without the transmission of the corresponding signal. -stimulating. Blocking the antigen function of the B lymphocyte in this case prevents the synthesis of cytokine by immune cells, such as T cells, and thus acts as an immunosuppressant. Moreover, the lack of costimulation may also be sufficient to anergize the T cells, thereby inducing tolerance in a subject. The induction of long-term tolerance by B lymphocyte antigen blocking reagents can avoid the need for repeated administration of these blocking reagents. To achieve sufficient immunosuppression or tolerance in a subject, it may also be necessary to block the function of a combination of B lymphocyte antigens. The effectiveness of a particular blocking reagent in the prevention of a rejection of organ transplantation or GVHD can be evaluated using animal models that are capable of predicting efficacy in humans. Examples of suitable systems that can be used include allogeneic cardiac grafts in rats and islet cell grafts, xenogenic pancreatic grafts in mice, both of which have been used to examine the immunosuppressive effects of CTLA4Ig fusion proteins in vivo as described in Lenschow et al. al., Science 257: 789-792 (1992) and Turka et al., Proc. Nati Acad. Sci. USA, 89: 11102-1 1105 (1992). In addition, murine models of GVHD (see Paul de., Fundamental Immunology, Raven Press, New York, 1989, pp. 846-847) can be used to determine the blocking effect of the B cell antigen function in vivo in the development of The blocking of the antigen function may also be therapeutically useful for the treatment of autoimmune diseases.Many autoimmune disorders are the result of the inappropriate activation of T cells that are reactive against the same tissue and which promotes the production of cytokines. auto-antibodies involved in the pathology of the diseases.The prevention of the activation of autoreactive T cells can reduce or eliminate symptoms of the disease.The administration of reagents that block the co-stimulation of T cells breaking the interactions receptorpligando of the antigens of B lymphocytes , can be used to inhibit the activation of T cells and prevent the production of autoantibody pos or cytokines derived from T cells that may be involved in the disease process. Additionally, blocking reagents can induce antigen-specific tolerance of autoreactive T cells that could lead to long-term relief of the disease. The efficacy of blocking reagents in the prevention or amelioration of autoimmune disorders can be determined using a number of well-characterized animal models of human autoimmune diseases. Examples include experimental murine autoimmune encephalitis, systemic lupus erythomatosis in MRL / lpr / lpr mice or NZB hybrid mice, murine autoimmune collagen arthritis, diabetes mellitus in NOD mice and BB rats, and murine experimental myasthenia gravis (see Paul of., Fundamental Immunology, Raven Press, New York, 1989, pp. 840-856). The overregulation of an antigen function (preferably a B lymphocyte antigen function), as a means of over-regulated immune response, may also be useful in therapies. Overregulation of immune responses may be in the form of improving an existing immune response or eliciting an initial immune response. For example, improving an immune response through the stimulation of the B-cell antigen function may be useful in cases of viral infection. In addition, systemic viral diseases such as influenza, the common cold and encephalitis could be alleviated by the systemic administration of stimulant forms of B lymphocyte antigens.

Alternatively, immune anti-viral responses can be improved in an infected patient by removing T cells from the patient, by co-stimulating T cells in vitro with APCs pulsed with viral antigen either by expressing a peptide of the present invention or in conjunction with a stimulant of a soluble peptide of the present invention and reintroducing the T cells activated in vitro within the patient. Another method for improving anti-viral immune responses would be to isolate infected cells from a patient, transfecting them with a nucleic acid encoding a protein of the present invention as described herein, so that the cells express all or a portion of the protein on its surface, and reintroduce the transfected cells into the patient. The infected cells would now be able to deliver a co-stimulatory signal to, and thus activate, the T cells in vivo. In another application, upregulation or amelioration of the antigen function (preferably B lymphocyte antigen function) could be useful in the induction of tumor immunity. Tumor cells (e.g., sarcoma, melanoma, lymphoma, leukemia, neuroblastoma, carcinoma) transfected with a nucleic acid encoding at least one peptide of the present invention can be administered to a subject to overcome the specific tolerance to the tumor in the subject. If desired, the tumor cells can be transfected to express a combination of peptides. For example, tumor cells obtained from a patient can be transfected ex vivo with an expression vector that directs the expression of a peptide having similar activity to B7-2, alone or in combination with a peptide having activity similar to B7. -1 and / or activity similar to B7-3. The transfected tumor cells are returned to the patient to result in the expression of the peptides on the surface of the transfected cells. Alternatively, gene therapy techniques can be used to target a tumor cell for transfection in vivo. The presence of the peptide of the present invention, which has the activity of a B lymphocyte antigen (s) on the surface of the tumor cells, provides the necessary co-stimulation signal for the T cells to induce a immune response mediated by T cells against transfected tumor cells. In addition, tumor cells lacking MHC class I or MHC class II molecules, or that do not reexpress sufficient amounts of MHC class I or MHC class II molecules, can be transfected with nucleic acid encoding all or a portion of (e.g., a truncated portion of the cytoplasmic domain) of an MHC class I a chain protein and β2 microglobulin protein or an MHC class II a chain protein and a MHC class II β chain protein to express this forms MHC class I or MHC class II proteins on the surface of the cell. Expression of the appropriate MHC class I or classes II, in conjunction with a peptide having the activity of a B lymphocyte antigen (e.g., B7-1, B7-2, B7-3) induces a cell-mediated immune response T against the transfected tumor cell. Optionally, a gene encoding an antisense construct that blocks the expression of an associated MHC class II protein, such as the constant chain, can also be cotransfected with a DNA encoding a peptide that has the activity of B lymphocyte antigen to promote the presentation of antigens associated with tumor and induce tumor-specific immunity. Thus, the induction of an immune response mediated by T cells in a human subject may be sufficient to overcome tumor-specific tolerance in the subject. The activity of a protein of the invention can also, among other means, be measured by the following methods: Suitable assays for determining cytotoxicity of splenocytes or thymocytes include, without limitation, those described in Current Protocols in Immunology, Edited by J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro Assays for Mouse Lymphocyte Function 3.1.-3.19; Chapter 7, Immunologic studies in Humans); Herrmann et al., Proc. Nati Acad. Sci. USA 78: 2488-2492, 1981; Herrmann et al., J. Immunol. 128: 1968-1974, 1982; Handa et al., J. Immunol. 135-1564-1572, 1985; Takai et al., J. Immunol. 137: 3494-3500, 1986; Takai et al., J. Immunol. 140: 508-512. 1988; Hermann et al., Proc. Nati Acad. Sci. USA 78: 2488-2492, 1981; Herrmann et al., J. Immunol. 128: 1968-1974, 1982; Handa et al., J. Immunol. 135: 1564-1572, 1985; Takai et al., J. Immunol. 137: 3494-3500, 1986; Bowman et al., J. Virology 61: 1992-1998; Takai et al., J. Immunol. 140: 508-512, 1988; Bertagnolli et al., Cellular Immunology 133: 327-341, 1991; Brown et al., J. Immunol. 153: 3079-3092, 1994.

Assays to determine T cell-dependent immunoglobulin responses and isotype switching (which will identify, among others, proteins that modulate T cell-dependent antibody responses and that affect Thl / Th2 profiles) include, without limitation, those described in: Maliszewski, J. Immunol. 144: 3028-3033, 1990; and Assays for B cell function: In vitro antibody production, Mond, J.J. and Brunswick, M. In Current Protocols in Immunology. J.E.e.a. Coligan eds. Vol 1 pp. 3.8.1-3.8.16, John Wiley and Sons, Toronto. 1994. Mixed lymphocyte reaction (MLR) tests (which will identify, among others, proteins that predominantly generate Thl and CTL responses) include, without limitation, those described in Current Protocols in Immunology, Edited by J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro Assays for Mouse Lymphocyte Function 3.1-3.19; Chapter 7, Immunologic Studies in Humans); Takai et al., J. Immunol. 137: 3494-3500, 1986; Takai et al., J. Immunol. 140: 508-512, 1988; Bertagnolli et al., J. Immunol. 149: 3778-3783, 1992. Dendritic cell-dependent assays (which will identify, among others, proteins expressed by dendritic cells that activate natural T cells) include, without limitation, those described in: Guery et al., J. Immunol. 134: 536-544, 1995; Inaba et al., Journal of Experimental Medicine 173: 549-559, 1991; Macatonia et al., Journal of Immunology 154: 5071-5079, 1995; Porgador et al., Journal of Experimental Medicine 182: 255-260, 1995; Nair et al., Journal of Virology 67: 4062-4069, 1993; Huang et al., Science 264: 961-965, 1994; Macatonia et al., Journal of Experimental Medicine 169: 1255-1264, 1989; Bhardwaj et al., Journal of Clinical Investigation 94: 797-807, 1994; and Inaba et al., Journal of Experimental Medicine 172: 631-640, 1990. Tests to determine the survival / apoptosis of lymphocytes (which will identify, among others, the proteins that prevent apoptosis after superantigen induction and proteins). regulating lymphocyte homeostasis) include, without limitation, those described in: Darzynkiewicz et al., Cytometry 13: 795-808, 1992; Gorczyca et al., Leukemia 7: 659-670, 1993 Gorczyca et al, Cancer Research 53: 1945-1951, 1993; Itoh et al., Cell 66: 233-243, 1991; Zacharchuk, Journal of Immunology 145: 4037-4045, 1990; Zamai et al., Cytometry 14: 891-897, 1993; Gorczyca et al., International Journal of Oncology 1: 639-648, 1992. Tests for proteins that influence early stages of T cell development and confinement include, without limitation, those described in Antica et al., Blood 84; 111 -117, 1994; Fine et al., Cellular Immunology 155: 111-122, 1994; Galy et al., Blood 85: 2770-2778, 1995; Toki et al., Proc. Nat. Acad. Sci. USA 88: 7548-7551, 1991.

Hematopoiesis Regulation Activity A protein of the present invention may be useful in the regulation of hematopoiesis and, consequently, in the treatment of deficiencies of myeloid or lymphoid cells. Even a marginal biological activity in support of colony-forming cells or factor-dependent cell lines indicates involvement in the regulation of hematopoiesis, that is, in supporting the growth and proliferation of erythroid progenitor cells alone or in combination with other cytokines. , indicating utility in this way, for example, in the treatment of various anemias or to be used in conjunction with irradiation / chemotherapy to stimulate the production of erythroid precursors and / or erythroid cells; in supporting the growth and proliferation of myeloid cells such as granulocytes and monocytes / macrophages (ie, traditional CSF activity) useful, for example, in conjunction with chemotherapy to prevent or treat consequent myelosuppression; in supporting the growth and proliferation of megakaryocytes and consequently of platelets, thereby allowing the prevention or treatment of various platelet disorders such as thrombocytopenia, and in general to be used in place or in a complementary manner to platelet transfusions; and / or in sustaining the growth and proliferation of hematopoietic progenitor cells, which are capable of maturing each and every one of the aforementioned hematopoietic cells and therefore find therapeutic utility in various disorders of progenitor cells (such as those usually treated with transplants, including, without limitation, aplastic anemia and paroxysmal nocturnal hemoglobinuria) as well as in the repopulation of the division of progenitor cells that results from irradiation / chemotherapy, either in vivo or ex vivo (that is, in conjunction with transplantation of bone marrow or with the transplantation of peripheral progenitor cells (homologous or heterologous)) as normal cells or genetically engineered by gene therapy. The activity of a protein of the invention can, among other means, be measured by the following methods: Appropriate tests to determine the proliferation and differentiation of several hematopoietic lines have been cited above. Tests for the differentiation of embryonic progenitor cells (which will identify, among others, proteins that influence the hematopoiesis of embryonic differentiation) include, without limitation, those described in Johansson et al. Cellular Biology 15: 141-151, 1995; Keller et al., Molecular and Cellular Biology 13: 473-486, 1993; McClanahan et al., Blood 81: 2903-2915, 1993. Tests to determine the survival and differentiation of progenitor cells (which will identify, among others, proteins that regulate lympho-hematopoiesis) include, without limitation, those described in: Methylcellulose colony forming assays, Freshney, MG In Culture of Hematopoietic Cells, R.I. Freshney, et al. Vol pp 265-268, Wiley-Liss, Inc., New York, NY 1994; Hirayama et al., Proc Nati. Acad. Sci. USA 89: 5907-5911, 1992; Primitive hematopoietic colony forming cells with high proliferative potential, McNiece, I.K. and Briddell, R.A. In Culture of Hematopoietic Cells. R.I. Freshney, et al. eds. Vol pp. 23-39, Wiley-Liss, Inc. New York, NY 1994; Neben et al., Experimental Hematology 22: 353-359, 1994; Cobblestone area forming cell assay, Ploemacher, R.E. In Culture of Hematopoietic Cells. R.I. Freshney et al, eds. Vol pp. 1-21, Wiley-Liss, Inc. New York, NY 1994; Long term bone cultures in the presence of stromal cells, Spooncer, E., Dexter, M. and Alien, T. In Culture of Hematopoietic Cells. R.I. Freshney et al., Eds. Vol pp. 163-179, Wiley-Liss, Inc., New York, NY 1994; Long term culture initiating cell assay, Sutherland, H.J. In Culture of Hematopietic Cells, R.I. Freshney et al., Eds. Vol pp. 139-162, Wiley-Liss, Inc. New York, NY. 1994 Tissue Growth Activity A protein of the present invention may also have utility in compositions used for the growth or regeneration of bone, cartilage, tendon, ligament and / or nerve tissue, as well as for healing wounds and repair or replacement of tissue, and in the treatment of burns, incisions and ulcers. A protein of the present invention, which induces the growth of cartilage and / or bone in circumstances in which there is normally no bone formed, has application in the healing of bone fractures and damages or defects to cartilage in humans and other animals. Said preparation using a protein of the invention can have prophylactic use in the reduction of both closed and open fractures and also in the improved fixation of artificial joints. The formation of new bone induced by osteogenic agents contributes to the repair of congenital craniofacial defects, induced by trauma, or induced by oncological resection, and is also useful in cosmetic plastic surgery. A protein of this invention may also be useful in the treatment of periodental disease and other teeth repair processes. Such agents can provide an environment for attracting bone-forming cells, stimulating the growth of bone-forming cells or inducing the differentiation of progenitors of bone-forming cells. A protein of the invention may also be useful in the treatment of osteoporosis or osteoarthritis, such as through the stimulation of bone and / or cartilage repair or by blocking inflammation or tissue destruction processes (collagenase activity, osteoclastic activity, etc.) mediated by inflammatory processes. Another category of tissue regeneration activity that may be attributable to the protein of the present invention is tendon / ligament formation. A protein of the present invention, which induces tissue similar to tendon / ligament or other tissue formation in circumstances in which said tissue is not normally formed, has application in the healing of tendon or ligament tears, deformities and other defects of tendon or ligament in humans and other animals. Such preparation employing a tissue-inducing protein similar to ligament tendon may have prophylactic use in the prevention of damage to tendon or ligament tissue, as well as in the use for improved fixation of tendon or ligament to bone or other tissues, and in repair of tendon or ligament tissue defects. The formation of new tendon / ligament tissue, induced by a composition of the present invention contributes to the repair of congenital tendon or ligament defects, induced by trauma or of other origin, and is also useful in cosmetic plastic surgery for fixation or repair of tendons or ligaments. The compositions of the present invention can provide an environment for attracting tendon or ligament forming cells, stimulating the growth of tendon or ligament forming cells, inducing differentiation of progenitors of tendon or ligament forming cells, or inducing cell growth or progenitors of ex vivo ligament tendon for in vivo return to effect tissue repair. The compositions of the invention may also be useful in the treatment of tendonitis, carpal tunnel syndrome and other tendon or ligament defects. The compositions may also include an appropriate matrix and / or a sequestering agent as a carrier as is well known in the art. The protein of the present invention can also be useful for the proliferation of nerve cells and for the regeneration of nerve and brain tissue, that is, for the treatment of diseases and neuropathies of the central or peripheral nervous system, as well as of mechanical disrs and traumatic events that involve degeneration, death or injury to nerve cells or nerve tissue. More specifically, a protein can be used in the treatment of diseases of the peripheral nervous system, such as damage to the peripheral nerve, peripheral neuropathy and localized neuropathies, and diseases of the central nervous system, such as Alzheimer's disease, Parkinson's, Huntington's, amyotrophic lateral sclerosis and Shy-Drager syndrome. Additional conditions that can be treated in accordance with the present invention include mechanical and traumatic disorders, such as spinal cord disorders, head injuries and cerebrovascular diseases such as stroke. Peripheral neuropathies resulting from chemotherapy or other medical therapies can also be treatable using a protein of the present invention. The proteins of the invention may also be useful in promoting the best and fastest closure of unhealed wounds, including without limitation, pressure ulcers, ulcers associated with vascular insufficiency, trauma and surgical wounds, and the like. It is expected that a protein of the present invention may also exhibit activity for the generation or regeneration of other tissues such as tissues of organs (including, for example, pancreas, liver, intestine, kidney, skin, endothelium), muscle (soft, skeletal or cardiac) and vascular (including vascular endothelium), or to promote the growth of cells comprising said tissues. Part of the desired effects may be by inhibiting or modulating fibrotic healing to allow normal tissue to regenerate. A protein of the invention could also exhibit angiogenic activity. A protein of the present invention may also be useful for the protection or regeneration of the intestine and for the treatment of lung or liver fibrosis, reperfusion injury in various tissues and conditions resulting from systemic cytokine damage. A protein of the present invention may also be useful for promoting or inhibiting the differentiation of previously described tissues from precursor cells or tissues.; or to inhibit the growth of the tissues described above. The activity of a protein of the invention can, among other means, be measured by the following methods: Assays for determining tissue generation activity include, without limitation, those described in International Patent Publication No. WO95 / 16035 ( bone, cartilage, tendon); International Patent Publication No. WO95 / 05846 (nerve, nerve); International Patent Publication No. WO91 / 07491 (skin, endothelium). Assays for determining wound healing activity include, without limitation, those described in: Winter, Epidemial Wound Healing, pps. 71-112 (Maibach, Hl and Rovee, DT, eds.) Year Book Medical Publishers, Inc., Chicago, as modified by Eaglstein and Mertz, J. Invest. Dermatol. 71: 382-84 (1978).

Activity of Activin / Inhibin A protein of the present invention may also exhibit activities related to activin or inhibin. Inhibins are characterized by their ability to inhibit the release of follicle stimulating hormone (FSH), while activins are characterized by their ability to stimulate the release of follicle stimulating hormone (FSH). Therefore, a protein of the present invention, alone or in heterodimers with a member of the alpha family of inhibins, may be useful as a contraceptive based on the ability to inhibit or decrease fertility in female mammals and decrease spermatogenesis in mammals males The administration of sufficient amounts of other inhibins can induce infertility in these mammals. Alternatively, the protein of the invention, as a homodimer or as a heterodimer with other protein subunits of the inhibin beta group, may be useful as a fertility-inducing therapeutic, based on the ability of the activin molecules in the stimulation of the release of FSH from cells of the anterior pituitary. See, for example, U.S. Pat. No. 4,798,885. A protein of the present invention may also be useful for advancing the onset of fertility in sexually immature mammals, for the purpose of increasing the productive performance cycle of domestic animals such as cows, sheep and pigs. The activity of the protein of the invention can, among other means, be measured by the following methods: Assays for determining activin / inhibin activity include, without limitation, those described in Vale et al., Endocrinology 91: 562-572 , 1972; Ling et al., Nature 321: 779-782, 1986; Vale et al., Nature 321: 776-779, 1986; Mason et al., Nature, 318: 659-663, 1985; Forage et al., Proc. Nati Acad. Sci. USA 83: 3091-3095, 1986.

Ouimyotactic / Ouimiokinetic Activity A protein of the present invention may have chemokinetic or chemotactic activity (eg, act as a chemokine) for mammalian cells, including, for example, monocytes, fibroblasts, neutrophils, T cells, mast cells, eosinophilic, epithelial and / or endothelial. The chemokinetic and chemotactic proteins can be used to mobilize or attract a population of desired cells to a desired site of action. Chemotactic or chemokinetic proteins provide particular advantages in the treatment of wounds and other tissue injuries, as well as in the treatment of localized infections. For example, the attraction of lymphocytes, monocytes or neutrophils to tumors or sites of infection can result in improved immune responses against the tumor or infectious agent. A protein or peptide has chemotactic activity for a particular cell population if it can stimulate, directly or indirectly, the targeting or directed movement of said cell population. Preferably, the protein or peptide has the ability to directly stimulate the directed movement of cells. The fact that a particular protein has chemotactic activity for a population of cells can easily be determined by employing said protein or peptide in any known assay for cellular chemotaxis. The activity of a protein of the invention can, among other means, be measured by the following methods: Tests to determine chemotactic activity (which will identify proteins that induce or prevent chemotaxis) consist of assays that measure the ability of a protein to induce the migration of cells through a membrane as well as the ability of a protein to induce the adhesion of a population of cells to another population of cells. Appropriate assays for determining movement and adhesion include, without limitation, those described in Current Protocols in Immunology, Edited by J. E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Published by Greene Publishing Associates and Wiley-Interscience (Chapter 6.12, Measurement of alpha and Beta Chemokines 6.12.1-6.12.28; Taub et al., J. Clin. Invest. 95: 1370-1376, 1995; Lind et al., APMIS 103: 140-146, 1995; Muller et al., Eur J. Immunol., 25; 1744-1748; Gruber et al., J. Of Immunol., 152: 5860-5867, 1994; Johnson et al., J. of Immunol., 153: 1762-1768, 1994.

Hemostatic and Thrombolytic Activity A protein of the invention may also exhibit haemostatic or thrombolytic activity. As a result of this, it is expected that said protein be useful in the treatment of various coagulation disorders (including hereditary disorders, such as hemophilia) or to improve coagulation and other hemostatic events in the treatment of wounds resulting from trauma, surgeries or other causes A protein of the invention may also be useful for dissolving or inhibiting the formation of thrombosis and for the treatment and prevention of conditions resulting therefrom (such as, for example, infarction of central or cardiac nervous system vessels (eg, attack). The activity of a protein of the present invention can, among other means, be measured by the following methods: Assays for determining haemostatic and thrombolytic activity include, without limitation, those described in: Linet et al., J. Clin. Pharmacol, 26: 131-140, 1986, Burdick et al., Thrombosis Res. 45: 413-419, 1987, Humphrey et al, Fibrinolysis 5: 71-79 (1991), Schaub, Prostaglandins 35: 467-474, 1988. .

Receptor / Ligand Activity A protein of the present invention can also demonstrate activity as a receptor, ligand of receptors or inhibitors or agonists of receptor / ligand interactions. Examples of such receptors and ligands include, without limitation, cytokine receptors and their ligands, kinase receptors and their ligands, phosphatase receptors and their ligands, receptors involved in cell-cell interactions and their ligands (including, without limitation, cell adhesion molecules (such as selectins, integrins and their ligands) and receptor / ligand pairs involved in antigen presentation, antigen recognition and development of cellular and humoral immune responses). The receptors and ligands are also useful for the screening of potential peptide or small molecule inhibitors of the relevant receptor / ligand interaction. A protein of the present invention (including, without limitation, fragments of receptors and ligands) may itself be useful as an inhibitor of receptor / ligand interactions. The activity of a protein of the present invention can, among other means, be measured by the following methods: Appropriate assays for determining receptor-ligand activity include, without limitation those described in: Current Protocols in Immunology, edited by J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 7.28, Measurements of Cellular Adhesion under static conditions 7.28.1-7.28.22), Takai et al., Proc. Nati Acad. Sci. USA 84: 6864-6868, 1987; Bierer et al., J. Exp. Med. 168: 1145-1156, 1988; Rosenstein et al., J. Exp. Med 169: 149-160 1989; Stoltenborg et al., J. Immunol. Methods 175: 59-68, 1994; Stitt et al., Cell 80: 661-670, 1995.

Anti-Inflammatory Activity The proteins of the present invention may also exhibit anti-inflammatory activity. The anti-inflammatory activity can be achieved by providing a stimulus to the cells involved in the inflammatory response, inhibiting or promoting cell-cell interactions (such as, for example, cell adhesion), inhibiting or promoting the chemotaxis of cells involved in the inflammatory process, inhibiting or promoting cellular extravasation, or stimulating or suppressing the production of other factors that directly inhibit or promote an inflammatory response. Proteins exhibiting such activities can be used to treat inflammatory conditions (including chronic or acute conditions) including, without limitation, inflammation associated with infections (such as septic shock, sepsis or systemic inflammatory response syndrome (SIRS)), damage by ischemia-reperfusion, mortality by endotoxin, arthritis, hyperacute rejection mediated by complement, nephritis, lung damage induced by cytokine or chemokine, inflammatory bowel disease, Crohn's disease or resulting from overproduction of cytokines such as TNF or IL-1 The proteins of the invention may also be useful for treating anaphylaxis and hypersensitivity to a substance or antigen material.

Tumor Inhibiting Activity In addition to the activities described above for immunological treatment or tumor prevention, a protein of the present invention may exhibit other anti-tumor activities. A protein can inhibit the growth of tumors directly or indirectly (such as, for example, via ADCC). A protein may exhibit its tumor inhibitory activity by acting on tumor tissue or tumor precursor tissue, inhibiting the formation of tissues necessary to sustain tumor growth (such as, for example, inhibiting angiogenesis), causing production of other factors, agents or cell types that inhibit tumor growth, or by suppressing, eliminating or inhibiting factors, agents or cell types that promote tumor growth.

Other Activities A protein of the invention may also exhibit one or more of the following activities or effects: inhibit the growth, infection or function of, or kill, infectious agents, including, without limitation, bacteria, viruses, fungi and other parasites; affect (suppression or improvement) bodily characteristics, including, without limitation, height, weight, hair color, eye color, skin, fat / flesh or pigment ratio of other tissues, or size or partial body shape (such as, for example, example, increase or decrease of the chest, changes in the shape or configuration of bones); affect biorhythms or cycles or circadian rhythms; affect the fertility of male or female subjects, affect the metabolism, catabolism, anabolism, processing, utilization, storage or elimination of fat, lipids, proteins, carbohydrates, vitamins, minerals, cofactors or other factors or nutritional components of the diet; affect behavioral characteristics, including, without limitation, appetite, libido, stress, perception (including disorders of perception), depression (including depressive disorders) and violent behaviors; provision of analgesic effects or other pain-reducing effects; promotion of the differentiation and growth of embryonic progenitor cells in lineages other than hematopoietic lineages; hormonal or endocrine activity; in the case of enzymes, correct deficiencies of enzymes and the treatment of diseases related to deficiencies; treatment of hyperproliferative disorders (such as, for example, psoriasis); immunoglobulin-like activity (such as, for example, the ability to bind to antigens or complements); and the ability to act as an antigen in a vaccine composition to elevate the immune response against said protein or other material or entity that is reactive in some way with said protein.

LIST OF SEQUENCES (2) INFORMATION FOR SEQ ID NO: 1: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 205 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Ho or sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP00442 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 1: Met Thr Gly Leu Wing Leu Leu Tyr Ser Gly Val Phe Val Wing Phe Trp 1 5 10 15 Ala Cys Ala Leu Ala Val Gly Val Cys Tyr Thr He Phe Asp Leu Gly 20 25 30 Phe Arg Phe Asp Val Wing Trp Phe Leu Thr Glu Thr Ser Pro Phe Met 35 40 45 Trp Ser Asn Leu Gly He Gly Leu Ala He Ser Leu Ser Val Val Gly 50 55 60 Wing Wing Trp Gly He Tyr He Thr Gly Be Ser He He Gly Gly Gly 65 70 75 80 Val Lys Ala Pro Arg He Lys Thr Lys Asn Leu Val Ser He He Phe 85 90 95 Cys Glu Ala Wing Wing He Tyr Gly He He Met Wing He Val He Ser 100 105 110 Asn Met Wing Glu Pro Phe Ser Wing Thr Asp Pro Lys Wing He Gly His 115 120 125 Arg Asn Tyr His Wing Gly Tyr Ser Met Phe Gly Wing Gly Leu Thr Val 130 135 140 Gly Leu Ser Asn Leu Phe Cys Gly Val Cys Val Gly He Val Gly Ser 145 150 155 160 Gly Wing Wing Leu Wing Asp Wing Gln Asn Pro Being Leu Phe Val Lys He 165 170 175 Leu He Val Glu He Phe Gly Be Wing He Gly Leu Phe Gly Val He 180 185 190 Val Ala He Leu Gln Thr Ser Arg Val Lys Met Gly Asp 195 200 205 (2) INFORMATION FOR SEQ ID NO: 2: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 371 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Leukocyte (D) CLONE NAME: HP00804 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 2: Met Ser His Glu Lys Ser Phe Leu Val Ser Gly Asp Asn Tyr Pro Pro 1 5 10 15 Pro Asn Pro Gly Tyr Pro Gly Gly Pro Gln Pro Pro Met Pro Pro Tyr 20 25 30 Wing Gln Pro Pro Tyr Pro Gly Wing Pro Tyr Pro Gln Pro Pro Phe Gln 35 40 Pro Pro Pro Tyr Gly Gln Pro Gly Tyr Pro His Gly Pro Ser Pro Tyr 50 55 60 Pro Gln Gly Gly Tyr Pro Gln Gly Pro Tyr Pro Gln Gly Gly Tyr Pro 65 70 75 80 Gln Gly Pro Tyr Pro Gln Glu Gly Tyr Pro Gln Gly Pro Tyr Pro Gln 85 90 95 Gly Gly Tyr Pro Gln Gly Pro Tyr Pro Gln Ser Pro Phe Pro Pro Asn 100 105 110 Pro Tyr Gly Gln Pro Gln Val Phe Pro Gly Gln Asp Pro Asp Ser Pro 115 120 125 Gln His Gly Asn Tyr Gln Glu Glu Pro Pro Ser Tyr Tyr Asp Asn 130 135 140 Gln Asp Phe Pro Wing Thr Asn Trp Asp Asp Lys Ser He Arg Glu Wing 145 150 155 160 Phe He Arg Lys Val Phe Leu Val Leu Thr Leu Gln Leu Ser Val Thr 165 170 175 Leu Ser Thr Val Ser Val Phe Thr Phe Val Wing Glu Val Lys Gly Phe 180 185 190 Val Arg Glu Asn Val Trp Thr Tyr Tyr Val Ser Tyr Wing Val Phe Phe 195 200 205 He Ser Leu He Val Leu Ser Cys Cys Gly Asp Phe Arg Arg Lys His 210 210 220 Pro Trp Asn Leu Val Ala Leu Ser Val Leu Thr Ala Ser Leu Ser Tyr 225 230 235 240 Met Val Gly Met He Wing Being Phe Tyr Asn Thr Glu Wing Val He Met 245 250 255 Wing Val Gly He Thr Thr Wing Val Cys Phe Thr Val Val He Phe Ser 260 265 270 Met Gln Thr Arg Tyr Asp Phe Thr Ser Cys Met Gly Val Leu Leu Val 275 280 285 Ser Val Val Leu Phe He Phe Ala He Leu Cys He Phe He Arg 290 295 300 Asn Arg He Leu Glu He Val Tyr Ala Ser Leu Gly Ala Leu Leu Phe 305 310 315 320 Thr Cys Phe Leu Wing Val Asp Thr Gln Leu Leu Leu Gly Asn Lys Glu 325 330 335 Leu Ser Leu Ser Pro Glu Glu Tyr Val Phe Ala Ala Leu Asn Leu Tyr 340 345 350 Thr Asp He He Asn He Phe Leu Tyr He Leu Thr He He Gly Arg 355 360 365 Wing Lys Glu 370 (2) INFORMATION FOR SEQ ID NO: 3: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 179 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP01098 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 3: Met Leu Ser Leu Asp Phe Leu Asp Asp Val Arg Arg Met Asn Lys Arg 1 5 10 15 Gln Leu Tyr Tyr Gln Val Leu Asn Phe Gly Met He Val Ser Be Wing 20 25 30 Leu Met He Trp Lys Gly Leu Met Val He Thr Gly Ser Glu Ser Pro 35 40 45 He Val Val Leu Ser Gly Ser Met Glu Pro Ala Phe His Arg Gly 50 55 60 Asp Leu Leu Phe Leu Thr Asn Arg Val Glu Asp Pro He Arg Val Gly 65 70 75 80 Glu He Val Val Phe Arg He Glu Gly Arg Glu He Pro He Val His 85 90 95 Arg Val Leu Lys He His Glu Lys Gln Asn Gly His He Lys Phe Leu 100 105 110 Thr Lys Gly Asp Asn Asn Wing Val Asp Asp Arg Gly Leu Tyr Lys Gln 115 120 125 Gly Gln His Trp Leu Glu Lys Lys Asp Val Val Gly Arg Ala Arg Gly 130 135 140 Phe Val Pro Tyr He Gly He Val Thr He Leu Met Asn Asp Tyr Pro 145 150 155 160 Lys Phe Lys Tyr Ala Val Leu Phe Leu Leu Gly Leu Phe Val Leu Val 165 170 175 His Arg Glu (2) INFORMATION FOR SEQ ID NO: 4: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 347 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP01148 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 4: Met Ala Leu Leu Phe Ser Leu lie Leu Ala lie Cys Thr Arg Pro Gly 1 5 10 15 Phe Leu Wing Being Pro Gly Val Arg Leu Val Gly Gly Leu His Arg 20 25 30 Cys Glu Gly Arg Val Glu Val Glu Gln Lys Gly Gln Trp Gly Thr Val 35 40 45 Cys Asp Asp Gly Trp Asp He Lys Asp Val Wing Val Leu Cys Arg Glu 50 55 60 Leu Gly Cys Gly Wing Wing Ser Gly Thr Pro Ser Gly He Leu Tyr Glu 65 70 75 80 Pro Pro Wing Glu Lys Glu Gln Lys Val Leu He Gln Ser Val Ser Cys 85 90 95 Thr Gly Thr Glu Asp Thr Leu Wing Gln Cys Glu Gln Glu Glu Val Tyr 100 105 110 Asp Cys Ser His Glu Glu Asp Ala Gly Ala Ser Cys Glu Asn Pro Glu 115 120 125 Ser Ser Phe Ser Pro Val Pro Glu Val Val Lego Arg Wing Asp Gly Pro 130 135 140 Gly His Cys Lys Gly Arg Val Glu Val Lys His Gln Asn Gln Trp Tyr 145 150 155 160 Thr Val Cys Gln Thr Gly Trp Ser Leu Arg Ala Ala Lys Val Val Cys 165 170 175 Arg Gln Leu Gly Cys Gly Arg Wing Val Leu Thr Gln Lys Arg Cys Asn 180 185 190 Lys His Wing Tyr Gly Arg Lys Pro He Trp Leu Ser Gln Met Ser Cys 195 200 205 Ser Gly Arg Glu Wing Thr Leu Gln Asp Cys Pro Ser Gly Pro Trp Gly 210 t 215 220 Lys Asn Thr Cys Asn His Asp Glu Asp Thr Trp Val Glu Cys Glu Asp 225 230 235 240 Pro Phe Asp Leu Arg Leu Val Gly Gly Asp Asn Leu Cys Ser Gly Arg 245 250 255 Leu Glu Val Leu His Lys Gly Val Trp Gly Ser Val Cys Asp Asp Asn 260 265 270 Trp Gly Glu Lys Glu Asp Gln Val Val Cys Lys Gln Leu Gly Cys Gly 275 280 285 Lys Ser Leu Ser Pro Ser Phe Arg Asp Arg Lys Cys Tyr Gly Pro Gly 290 295 300 Val Gly Arg He Trp Leu Asp Asn Val Arg Cys Ser Gly Glu Glu Gln 305 310 315 320 Ser Leu Glu Gln Cys Gln His Arg Phe Trp Gly Phe His Asp Cys Thr 325 330 335 His Gln Glu Asp Val Wing Val He Cys Ser Gly 340 345 (2) INFORMATION FOR SEQ ID NO: 5: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 554 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP01293 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 5: Met Pro Thr Val Asp Asp He Leu Glu Gln Val Gly Glu Ser Gly Trp 1 5 10 15 Phe Gln Lys Gln Wing Phe Leu He Leu Cys Leu Leu Wing Wing Phe 20 25 30 Wing Pro He Cys Val Gly He Val Phe Leu Gly Phe Thr Pro Asp His 35 40 45 His Cys Gln Ser Pro Gly Val Ala Glu Leu Ser Gln Arg Cys Gly Trp 50 55 60 Ser Pro Wing Glu Glu Leu Asn Tyr Thr Val Pro Gly Leu Gly Pro Wing 65 70 75 80 Gly Glu Wing Phe Leu Gly Gln Cys Arg Arg Tyr Glu Val Asp Trp Asn 85 90 95 Gln Ser Ala Leu Ser Cys Val Asp Pro Leu Wing Ser Leu Wing Thr Asn LOO 105 110 Arg Ser His Leu Pro Leu Gly Pro Cys Gln Asp Gly Trp Val Tyr Asp 115 120 125 Thr Pro Gly Ser Ser He Val Thr Glu Phe Asn Leu Val Cys Wing Asp 130 135 140 Ser Trp Lys Leu Asp Leu Phe Gln Ser Cys Leu Asn Wing Gly Phe Phe 145 150 155 160 Phe Gly Ser Leu Gly Val Gly Tyr Phe Wing Asp Arg Phe Gly Arg Lys 165 170 175 Leu Cys Leu Leu Gly Thr Val Leu Val Asn Ala Val Ser Gly Val Leu 180 185 190 Met Wing Phe Ser Pro Asn Tyr Met Ser Met Leu Leu Phe Arg Leu Leu 195 200 205 Gln Gly Leu Val Ser Lys Gly Asn Trp Met Wing Gly Tyr Thr Leu He 210 215 220 Thr Glu Phe Val Gly Ser Gly Ser Arg Arg Thr Val Wing He Met Tyr 225 230 235 240 Gln Met Wing Phe Thr Val Gly Leu Val Wing Leu Thr Gly Leu Wing Tyr 245 250 255 Wing Leu Pro His Trp Arg Trp Leu Gln Leu Wing Val Ser Leu Pro Thr 260 265 270 Phe Leu Phe Leu Leu Tyr Tyr Trp Cys Val Pro Glu Ser Pro Arg Trp 275 280 285 Leu Leu Ser Gln Lys Arg Asn Thr Glu Wing He Lys He Met Asp His 290 295 300 He Wing Gln Lys Asn Gly Lys Leu Pro Pro Wing Asp Leu Lys Met Leu 305 310 315 320 Ser Leu Glu Glu Asp Val Thr Glu Lys Leu Ser Pro Ser Phe Ala Asp 325 330 335 Leu Phe Arg Thr Pro Arg Leu Arg Lys Arg Thr Phe He Leu Met Tyr 340 345 350 Leu Trp Phe Thr Asp Ser Val Leu Tyr Gln Gly Leu He Leu His Met 355 360 365 Gly Ala Thr Ser Gly Asn Leu Tyr Leu Asp Phe Leu Tyr Ser Ala Leu 370 375 380 Val Glu He Pro Gly Ala Phe He Ala Ala Leu He Thr He Asp Arg Val 385 390 395 400 Gly Arg He Tyr Pro Met Wing Val Ser Asn Leu Leu Wing Gly Wing Wing 405 410 415 Cys Leu Val Met He Phe He Ser Pro Asp Leu His Trp Leu Asn He 420 425 430 He He Met Met Cys Val Gly Arg Met Gly He Thr He Ala He Gln Met 435, 440 445 He Cys Leu Val Asn Ala Glu Leu Tyr Pro Thr Phe Val Arg Asn Leu 450 455 460 Gly Val Met Val Cys Ser Ser Leu Cys Asp He Gly Gly He He Thr 465 470 475 480 Pro Phe He Val Phe Arg Leu Arg Glu Val Trp Gln Ala Leu Pro Leu 485 490 495 He Leu Phe Wing Val Leu Gly Leu Leu Wing Wing Gly Val Thr Leu Leu 500 505 510 Leu Pro Glu Thr Lys Gly Val Wing Leu Pro Glu Thr Met Lys Asp Wing 515 520 525 Glu Asn Leu Gly Arg Lys Wing Lys Pro Lys Glu Asn Thr He Tyr Leu 530 535 540 Lys Val Gln Thr Ser Glu Pro Ser Gly Thr 545 550 (2) INFORMATION FOR SEQ ID NO: 6: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 350 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10013 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 6: Met Wing Val Phe Val Val Leu Leu Wing Leu Val Wing Gly Val Leu Gly 1 5 10 15 Asn Glu Phe Be He Leu Lys Ser Pro Gly Ser Val Val Phe Arg Asn 20 25 30 Gly Asn Trp Pro He Pro Gly Glu Arg He Pro Asp Val Ala Ala Leu 35 40 45 Ser Met Gly Phe Ser Val Lys Glu Asp Leu Ser Trp Pro Gly Leu Wing 50 55 60 16 Val Gly Asn Leu Phe His Arg Pro Arg Wing Thr Val Met Val Met Val 65 70 75 80 Lys Gly Val Asn Lys Leu Ala Leu Pro Pro Gly Ser Val He Ser Tyr 85 90 95 Pro Leu Glu Asn Wing Val Pro Phe Ser Leu Asp Ser Val Wing Asn Ser 100 105 110 He His Ser Leu Phe Ser Glu Glu Thr Pro Val Val Leu Gln Leu Ala 115, 120 Pro 125 Pro Glu Glu Arg Val Tyr Met Val Gly Lys Wing Asn Ser Val Phe 130 135 140 Glu Asp Leu Ser Val Thr Leu Arg Gln Leu Arg Asn Arg Leu Phe Gln 145 150 155 160 Glu Asn Ser Val Leu Ser Ser Leu Pro Leu Asn Ser Leu Ser Arg Asn 165 170 175 Asn Glu Val Asp Leu Leu Phe Leu Ser Glu Leu Gln Val Leu His Asp 180 185 190 He Ser Ser Leu Leu Ser Arg His Lys His Leu Ala Lys Asp His Ser 195 200 205 Pro Asp Leu Tyr Ser Leu Glu Leu Ala Gly Leu Asp Glu He Gly Lys 210 215 220 Arg Tyr Gly Glu Asp Ser Glu Gln Phe Arg Asp Wing Ser Lys He Leu 225 230 235 240 Val Asp Ala Leu Gln Lys Phe Wing Asp Asp Met Tyr Ser Leu Tyr Gly 245 250 255 Gly Asn Ala Val Val Glu Leu Val Thr Val Lys Ser Phe Asp Thr Ser 260 265 270 Leu He Arg Lys Thr Arg Thr He Leu Glu Wing Lys Gln Wing Lys Asn 275 280 285 Pro Wing Pro Pro Tyr Asn Leu Wing Tyr Lys Tyr Asn Phe Glu Tyr Ser 290 295 300 Val Val Phe Asn Met Val Leu Trp He Met He Ala Leu Ala Leu Ala 305 310 315 320 Val He He Thr Ser Tyr Asn He Trp Asn Met Asp Pro Gly Tyr Asp 325 330 335 Ser He He Tyr Arg Met Thr Asn Gln Lys He Arg Met Asp 340 345 350 (2) INFORMATION FOR SEQ ID NO: 7: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 209 (B) TYPE: Amino acid (D) TOPOLOGY: Linear (ii) SEQUENCE TYPE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10034 (xi) DESCRIPTION OF THE SEQUENCE : SEQ ID NO: 7: Met Val Ser Ser Pro Cys Thr Gln Wing Being Ser Arg Thr Cys Ser Arg 1 5 10 15 He Leu Gly Leu Ser Leu Gly Thr Ala Ala Leu Phe Ala Ala Gly Ala 20 25 30 Asn Val Ala Leu Leu Pro Asn Trp Asp Val Thr Tyr Leu Leu Arg 35 40 45 Gly Leu Leu Gly Arg His Wing Met Leu Gly Thr Gly Leu Trp Gly Gly 50 55 60 Gly Leu Met Val Leu Thr Wing Wing He Leu He Ser Leu Met Gly Trp 65 70 75 80 Arg Tyr Gly Cys Phe Ser Lys Ser Gly Leu Cys Arg Ser Val Leu Thr 85 90 95 Wing Leu Leu Be Gly Gly Leu Wing Leu Leu Gly Wing Leu He Cys Phe 100 105 110 Val Thr Ser Gly Val Wing Leu Lys Asp Gly Pro Phe Cys Met Phe Asp 115 120 125 Val Ser Ser Phe Asn Gln Thr Gln Wing Trp Lys Tyr Gly Tyr Pro Phe 130 135 140 Lys Asp Leu His Ser Arg Asn Tyr Leu Tyr Asp Arg Ser Leu Trp Asn 145 150 155 160 Ser Val Cys Leu Glu Pro Ser Ala Ala Val Val Trp His Val Ser Leu 165 170 175 Phe Ser Ala Leu Leu Cys He Ser Leu Leu Gln Leu Leu Leu Val Val 180 185 190 Val His Val He Asn Ser Leu Leu Gly Leu Phe Cys Ser Leu Cys Glu 195 200 205 Lys (2) INFORMATION FOR SEQ ID NO: 8: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 163 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10050 (xi) DESCRIPTION OF THE SEQUENCE : SEQ ID NO: 8: Met Ala Ala Gly Leu Phe Gly Leu Ser Ala Arg Arg Leu Leu Ala Ala 1 5 10 15 Wing Wing Thr Arg Gly Leu Pro Wing Wing Arg Val Arg Trp Glu Be Ser 20 25 30 Phe Ser Arg Thr Val Val Wing Pro Wing Val Wing Gly Lys Arg Pro 35 40 45 Pro Glu Pro Thr Thr Pro Trp Gln Glu Asp Pro Glu Pro Glu Asp Glu 50 55 60 Asn Leu Tyr Glu Lys Asn Pro Asp Ser His Gly Tyr Asp Lys Asp Pro 65 70 75 80 Val Leu Asp Val Trp Asn Met Arg Leu Val Phe Phe Phe Gly Val Ser 85 90 95 He He Leu Val Leu Gly Ser Thr Phe Val Wing Tyr Leu Pro Asp Tyr 100 105 110 Arg Cys Thr Gly Cys Pro Arg Wing Trp Asp Gly Met Lys Glu Trp Ser 115 120 125 Arg Arg Glu Wing Glu Arg Leu Val Lys Tyr Arg Glu Wing Asn Gly Leu 130 135 140 Pro He Met Glu Be Asn Cys Phe Asp Pro Ser Lys He Gln Leu Pro 145 150 155 160 Glu Asp Glu (2) INFORMATION FOR SEQ ID NO: 9: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 92 (B) TYPE: Amino acid (D) TOPOLOGY: Linear (ii) SEQUENCE TYPE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10071 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 9: Met Thr Lys Leu Wing Gln Trp Leu Trp Gly Leu Wing He Leu Gly Ser 1 5 10 15 Thr Trp Val Wing Leu Thr Thr Gly Wing Leu Gly Leu Glu Leu Pro Leu 20 25 30 Ser Cys Gln Glu Val Leu Trp Pro Leu Pro Wing Tyr Leu Leu Val Ser 35 40 45 Wing Gly Cys Tyr Wing Leu Gly Thr Val Gly Tyr Arg Val Ala Thr Phe 50 55 60 His Asp Cys Glu Asp Wing Wing Arg Glu Leu Gln Ser Gln He Gln Glu 65 70 75 80 Wing Arg Wing Asp Leu Wing Arg Arg Gly Leu Arg Phe 85 90 (2) INFORMATION FOR SEQ ID NO: 10: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 172 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10076 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 10: Met Glu Tyr Leu Ala His Pro Ser Thr Leu Gly Leu Ala Val Gly Val 1 5 10 15 Wing Cys Gly Met Cys Leu Gly Trp Ser Leu Arg Val Cys Phe Gly Met 20 25 30 Leu Pro Lys Ser Lys Thr Ser Lys Thr His Thr Asp Thr Glu Ser Glu 35 40 45 Wing Ser He Leu Gly Asp Ser Gly Glu Tyr Lys Met He Leu Val Val 50 55 60 Arg Asn Asp Leu Lys Met Gly Lys Gly Lys Val Wing Wing Gln Cys Ser 65 70 75 80 His Ala Ala Ala Ser Ala Tyr Lys Gln He Gln Arg Arg Asn Pro Glu 85 90 95 Met Leu Lys Gln Trp Glu Tyr Cys Gly Gln Pro Lys Val Val Val Lys 100 105 110 Wing Pro Asp Glu Glu Thr Leu He Wing Leu Leu Wing His Wing Lys Met 115 120 125 Leu Gly Leu Thr Val Ser Leu He Gln Asp Wing Gly Arg Thr Glu He 130 135 140 Wing Pro Gly Ser Gln Thr Val Leu Gly He Gly Pro Gly Pro Wing Asp 145 150 155 160 Leu He Asp Lys Val Thr Gly His Leu Lys Leu Tyr 165 170 (2) INFORMATION FOR SEQ ID NO: 11: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 149 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10085 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 11: Met Met Thr Lys His Lys Lys Cys Phe He He Val Val Val Leu He 1 5 10 15 Thr Thr Asn He He Thr Leu He Val Lys Leu Thr Arg Asp Ser Gln 20 25 30 Being Leu Cys Pro Tyr Asp Trp He Gly Phe Gln Asn Lys Cys Tyr Tyr 35 40 45 Phe Ser Lys Glu Glu Gly Asp Trp Asn Ser Ser Lys Tyr Asn Cys Ser 50 55 60 Thr Gln His Wing Asp Leu Thr He He Asp Asn He Glu Glu Met Asn 65 70 75 80 Phe Leu Arg Arg Tyr Lys Cys Ser As Asp His Trp He Gly Leu Lys 85 90 95 Met Wing Lys Asn Arg Thr Gly Gln Trp Val Asp Gly Wing Thr Phe Thr 100 105 110 Lys Ser Phe Gly Met Arg Gly Ser Glu Gly Cys Wing Tyr Leu Ser Asp 115 120 125 Asp Gly Wing Wing Thr Wing Arg Cys Tyr Thr Glu Arg Lys Trp He Cys 130 135 140 Arg Lys Arg He His 145 (2) INFORMATION FOR SEQ ID NO: 12: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 188 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10122 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 12: Met Ser Thr Met Phe Wing Asp Thr Leu Leu He Val Phe He Ser Val 1 5 10 15 Cys Thr Ala Leu Leu Ala Glu Gly He Thr Trp Val Leu Val Tyr Arg 20 25 30 Thr Asp Lys Tyr Lys Arg Leu Lys Wing Glu Val Glu Lys Gln Ser Lys 35 40 45 Lys Leu Glu Lys Lys Lys Glu Thr He Thr Glu Ser Ala Gly Arg Gln 50 55 60 Gln Lys Lys He Glu Arg Gln Glu Glu Lys Leu Lys Asn Asn Asn 65 70 75 80 Arg Asp Leu Ser Met Val Arg Met Lys Ser Met Phe Wing He Gly Phe 85 90 95 Cys Phe Thr Ala Leu Met Gly Met Phe Asn Ser He Phe Asp Gly Arg 100 105 110 Val Val Ala Lys Leu Pro Phe Thr Pro Leu Ser Tyr He Gln Gly Leu 115 120 125 Ser His Arg Asn Leu Leu Gly Asp Asp Thr Thr Asp Cys Ser Phe He 130 135 140 Phe Leu Tyr He Leu Cys Thr Met Ser He Arg Gln Asn He Gln Lys 145 150 155 160 He Leu Gly Leu Wing Pro Being Arg Wing Wing Thr Lys Gln Wing Gly Gly 165 170 175 Phe Leu Gly Pro Pro Pro Pro Ser Gly Lys Phe Ser 180 185 (2) INFORMATION FOR SEQ ID NO: 13: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 215 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10136 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 13: Met Val Leu Leu Thr Met He Wing Arg Val Wing Asp Gly Leu Pro Leu 1 5 10 15 Wing Wing Met Met Gln Glu Asp Glu Gln Ser Gly Arg Asp Leu Gln Gln 20 25 30 Tyr Gln Ser Gln Wing Lys Gln Leu Phe Arg Lys Leu Asn Glu Gln Ser 35 40 45 Pro Thr Arg Cys Thr Leu Glu Wing Gly Wing Mßt Thr Phe His Tyr He 50 55 60 He Glu Gln Gly Val Cys Tyr Leu Val Leu Cys Glu Ala Wing Phe Pro 65 70 75 80 Lys Lys Leu Wing Phe Wing Tyr Leu Glu Asp Leu His Ser Glu Phe Asp 85 90 95 Glu Gln His Gly Lys Lys Val Pro Thr Val Ser Arg Pro Tyr Ser Phe 100 105 110 He Glu Phe Asp Thr Phe He Gln Lys Thr Lys Lys Leu Tyr He Asp 115 120 125 Ser Arg Ala Arg Arg Asn Leu Gly Ser He Asn Thr Glu Leu Gln Asp 130 135 140 Val Gln Arg He Met Val Wing Asn He Glu Glu Val Leu Gln Arg Gly 145 150 155 160 Glu Ala Leu Ser Ala Leu Asp Ser Lys Ala Asn Asn Leu Ser Ser Leu 165 170 175 Be Lys Lys Tyr Arg Gln Asp Wing Lys Tyr Leu Asn Met Arg Ser Thr 180 185 190 Tyr Wing Lys Wing Wing Val Wing Val Phe Phe He Met Leu He Val 195 200 205 Tyr Val Arg Phe Trp Trp Leu 210 215 (2) INFORMATION FOR SEQ ID NO: 14: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 112 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10175 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 14: Met Gln Asp Thr Gly Ser Val Val Pro Leu His Trp Phe Gly Phe Gly 1 5 10 15 Tyr Ala Ala Leu Val Ala Ser Gly Gly He He Gly Tyr Val Lys Wing 20 25 30 Gly Ser Val Pro Ser Leu Ala Wing Gly Leu Lehe Phe Gly Ser Leu Wing 35 40 45 Gly Leu Gly Wing Tyr Gln Leu Ser Gln Asp Pro Arg Asn Val Trp Val 50 55 60 Phe Leu Wing Thr Ser Gly Thr Leu Wing Gly He Met Gly Met Arg Phe 65 70 75 80 Tyr His Ser Gly Lys Phe Met Pro Wing Gly Leu He Wing Gly Wing Ser 85 90 95 Leu Leu Met Val Ala Lys Val Gly Val Ser Met Phe Asn Arg Pro His 100 105 110 (2) INFORMATION FOR SEQ ID NO: 15: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 114 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELLULAR LINE: KB (D) CLONE NAME: HP10179 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 15: Met Glu Lys Pro Leu Phe Pro Leu Val Pro Leu His Trp Phe Gly Phe 1 5 10 15 Gly Tyr Thr Ala Leu Val Val Ser Gly Gly He Val Gly Tyr Val Lys 20 25 30 Thr Gly Ser Val Pro Ser Leu Ala Wing Gly Leu Lehe Phe Gly Ser Leu 35 40 45 Wing Gly Leu Gly Wing Tyr Gln Leu Tyr Gln Asp Pro Arg Asn Val Trp 50 55 60 Gly Phe Leu Wing Wing Thr Ser Val Thr Phe Val Gly Val Met Gly Met 65 70 75 80 Arg Ser Tyr Tyr Tyr Gly Lys Phe Met Pro Val Gly Leu He Wing Gly 85 90 95 Ala Ser Leu Leu Met Ala Ala Lys Val Gly Val Arg Met Leu Met Thr 100 105 110 Ser Asp (2) INFORMATION FOR SEQ ID NO: 16: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 327 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein. (iii) HYPOTHETICAL: No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10196 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 16: Met Ala Ala Ala Ala Ala Ala Ala Ala Ala Ala Thr Asn Gly Thr Gly Gly 1 '5 10 15 Be Ser Gly Met Glu Val Asp Ala Ala Val Val Pro Ser Val Met Wing 20 25 30 Cys Gly Val Thr Gly Ser Val Ser Val Ala Leu His Pro Leu Val He 35 40 45 Leu Asn He Ser Asp His Trp He Arg Met Arg Ser Gln Glu Gly Arg 50 55 60 Pro Val Gln Val He Gly Ala Leu He Gly Lys Gln Glu Gly Arg Asn 65 70 75 80 He Glu Val Met Asn Ser Phe Glu Leu Leu Ser His Thr Val Glu Glu 85 90 95 Lys He He He As Asp Lys Glu Tyr Tyr Tyr Thr Lys Glu Glu Gln Phe 100 105 110 Lys Gln Val Phe Lys Glu Leu Glu Phe Leu Gly Trp Tyr Thr Thr Gly 115 120 125 Gly Pro Pro Asp Pro Ser Asp He His Val His Lys Gln Val Cys Glu 130 135 140 He He Glu Ser Pro Leu Phe Leu Lys Leu Asn Pro Met Thr Lys His 145 150 155 160 Thr Asp Leu Pro Val Ser Val Phe Glu Ser Val He Asp He He Asn 165 170 175 Gly Glu Wing Thr Met Leu Phe Wing Glu Leu Thr Tyr Thr Leu Wing Thr 180 185 190 Glu Glu Wing Glu Arg He Gly Val Asp His Val Wing Arg Met Thr Wing 195 200 205 Thr Gly Ser Gly Glu Asn Ser Thr Val Wing Glu His Leu He Wing Gln 210 215 220 His Ser Wing He Lys Met Leu His Ser Arg Val Lys Leu He Leu Glu 225 230 235 240 Tyr Val Lys Wing Ser Glu Wing Gly Glu Val Pro Phe Asn His Glu He 245 250 255 Leu Arg Glu Ala Tyr Ala Leu Cys His Cys Leu Pro Val Leu Ser Thr 260 265 270 Asp Lys Phe Lys Thr Asp Phe Tyr Asp Gln Cys Asn Asp Val Gly Leu 275 280 285 Met Wing Tyr Leu Gly Thr He Thr Lys Thr Cys Asn Thr Met Asn Gln 290 295 300 Phe Val Asn Lys Phe Asn Val Leu Tyr Asp Arg Gln Gly He Gly Arg 305 310 315 320 Arg Met Arg Gly Leu Phe Phe 325 (2) INFORMATION FOR SEQ ID NO: 17: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 373 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10235 (xi) DESCRIPTION OF THE SEQUENCE : SEQ ID NO: 17: Met Thr Leu Cys Wing Met Leu Pro Leu Leu Leu Phe Thr Tyr Leu Asn 1 5 10 15 Be Phe Leu His Gln Arg He Pro Gln Ser Val Arg He Leu Gly Ser 20 25 30 Leu Val Ala He Leu Leu Val Phe Leu He Thr Ala He Leu Val Lys 35 40 45 Val Gln Leu Asp Ala Leu Pro Phe Phe Val He Thr Met He Lys He 50 55 60 Val Leu He Asn Ser Phe Gly Ala He Leu Gln Gly Ser Leu Phe Gly 65 70 75 80 Leu Wing Gly Leu Leu Pro Wing Being Tyr Thr Wing Pro He Met Being Gly 85 90 95 Gln Gly Leu Wing Gly Phe Phe Wing Ser Val Wing Met He Cys Wing 100 105 110 Wing Ser Gly Ser Glu Leu Ser Glu Ser Wing Phe Gly Tyr Phe He Thr 115 120 125 Wing Cys Wing Val He He Leu Thr He He Cys Tyr Leu Gly Leu Pro 130 135 140 Arg Leu Glu Phe Tyr Arg Tyr Tyr Gln Gln Leu Lys Leu Glu Gly Pro 145 150 155 160 Gly Glu Gln Glu Thr Lys Leu Asp Leu He Ser Lys Gly Glu Glu Pro 165 170 175 Arg Ala Gly Lys Glu Glu Ser Gly Val Ser Val Ser Asn Ser Gln Pro 180 185 190 Thr Asn Glu Ser His Ser lie Lys Ala He Leu Lys Asn He Ser Val 195 200 205 Leu Ala Phe Ser Val Cys Phe He Phe Thr He Thr He Gly Met Phe 210 215 220 Pro Wing Val Thr Val Glu Val Lys Ser Ser Wing Wing Gly Ser Ser Thr 225 230 235 240 Trp Glu Arg Tyr Phe He Pro Val Ser Cys Phe Leu Thr Phe Asn He 245 250 255 Phe Asp Trp Leu Gly Arg Ser Leu Thr Wing Val Phe Met Trp Pro Gly 260 265 270 Lys Asp Ser Arg Trp Leu Pro Ser Leu Val Leu Wing Arg Leu Val Phe 275 280 285 Val Pro Leu Leu Leu Leu Cys Asn He Lys Pro Arg Arg Tyr Leu Thr 290 295 300 Val Val Phe Glu His Asp Wing Trp Phe He Phe Phe Met Wing Wing Phe 305 310 315 320 Wing Phe Ser Asn Gly Tyr Leu Wing Ser Leu Cys Met Cys Phe Gly Pro 325 330 335 Lys Lys Val Lys Pro Wing Glu Wing Glu Thr Wing Gly Wing He Met Wing 340 345 350 Phe Phe Leu Cys Leu Gly Leu Wing Leu Gly Wing Val Phe Ser Phe Leu 355 360 365 Phe Arg Wing He Val 370 (2) INFORMATION FOR SEQ ID NO: 18: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 183 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10297 (i) DESCRIPTION OF SEQUENCE: SEQ ID NO: 18: Met Lys Leu Leu Ser Leu Val Wing Val Val Gly Cys Leu Leu Val Pro 1 5 10 15 Pro Wing Glu Wing Asn Lys Ser Ser Glu Asp He Arg Cys Lys Cys He 20 25 30 Cys Pro Pro Tyr Arg Asn He Ser Gly His He Tyr Asn Gln Asn Val 35 40 45 Ser Gln Lys Asp Cys Asn Cys Leu His Val Val Glu Pro Met Pro Val 50 55 60 Pro Gly His Asp Val Glu Ala Tyr Cys Leu Leu Cys Glu Cys Arg Tyr 65 70 75 80 Glu Glu Arg Ser Thr Thr He Lys Val He He Val He Tyr Leu 85 90 95 Val Val Gly Ala Leu Leu Leu Tyr Met Ala Phe Leu Met Leu Val 00 105 110 Asp Pro Leu He Arg Lys Pro Asp Ala Tyr Thr Glu Gln Leu His Asn 115 120 125 Glu Glu Glu Asn Glu Asp Ala Arg Ser Met Ala Ala Ala Ala Ala Ser 130 135 140 Leu Gly Gly Pro Arg Ala Asn Thr Val Leu Glu Arg Val Glu Gly Ala 145 150 155 160 Gln Gln Arg Trp Lys Leu Gln Val Gln Glu Gln Arg Lys Thr Val Phe 165 170 175 Asp Arg His Lys Met Leu Ser 180 (2) INFORMATION FOR SEQ ID NO: 19: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 116 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10299 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 19: Met Wing Being Thr Val Val Wing Val Gly Leu Thr He Wing Wing Wing Gly 1 5 10 15 Phe Wing Gly Arg Tyr Val Leu Gln Wing Met Lys His Met Glu Pro Gln 20 25 30 Val Lys Gln Val Phe Gln Ser Leu Pro Lys Ser Wing Phe Ser Gly Gly 35 40 45 Tyr Tyr Arg Gly Gly Phe Glu Pro Lys Met Thr Lys Arg Glu Wing Wing 50 55 60 Leu He Leu Gly Val Ser Pro Thr Wing Asn Lys Gly Lys He Arg Asp 65 70 75 80 Wing His Arg Arg He Met Leu Leu Asn His Pro Asp Lys Gly Gly Ser 85 90 95 Pro Tyr He Wing Wing Lys He Asn Glu Wing Lys Asp Leu Leu Glu Gly 100 105 110 Gln Wing Lys Lys 115 (2) INFORMATION FOR SEQ ID NO: 20: (i) CHARACTERISTICS OF THE SEQUENCE: ((A) LENGTH: 152 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL: No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELLULAR LINE: KB (D) CLONE NAME: HP10301 (xi) DESCRIPTION OF THE SEQUENCE : SEQ ID NO: 20: Met Wing Val Leu Ser Lys Glu Tyr Gly Phe Val Leu Leu Thr Gly Wing 1 5 10 15 Wing Being Phe He Met Val Wing His Wing Leu Wing Asn Val Being Lys Wing 20 25 30 Arg Lys Lys Tyr Lys Val Glu Tyr Pro He Mßt Tyr Ser Thr Asp Pro 35 40 45 Glu Asn Gly His He Phe Asn Cys He Gln Arg Ala His Gln Asn Thr 50 55 60 Leu Glu Val Tyr Pro Pro Phe Leu Phe Phe Leu Wing Val Gly Gly Val 65 70 75 80 Tyr His Pro Arg He Wing Ser Gly Leu Gly Leu Wing Trp He Val Gly 85 90 95 Arg Val Leu Tyr Wing Tyr Gly Tyr Tyr Thr Gly Glu Pro Ser Lys Arg 100 105 110 Be Arg Gly Wing Leu Gly Be He Wing Leu Leu Gly Leu Val Gly Thr 115 120 125 Thr Val Cys Ser Wing Phe Gln His Leu Gly Trp Val Lys Ser Gly Leu 130 135 140 Gly Ser Gly Pro Lys Cys Cys His 145 150 (2) INFORMATION FOR SEQ ID NO: 21: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 559 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP10302 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 21: Met Wing Pro Thr Leu Gln Gln Wing Tyr Arg Arg Arg Trp Trp Met Wing 1 5 10 15 Cys Thr Wing Val Leu Glu Asn Leu Phe Phe Be Wing Val Leu Leu Gly 20 25 30 Trp Gly Ser Leu Leu He He Leu Lys Asn Glu Gly Phe Tyr Ser Ser 35 40 45 Thr Cys Pro Wing Glu Be Ser Thr Asn Thr Thr Gln Asp Glu Gln Arg 50 55 60 Arg Trp Pro Gly Cys Asp Gln Gln Asp Glu Met Leu Asn Leu Gly Phe 65 70 75 80 Thr He Gly Ser Phe Val Leu Ser Wing Thr Thr Leu Pro Leu Gly He 85 90 95 Leu Met Asp Arg Phe Gly Pro Arg Pro Val Arg Leu Val Gly Ser Ala 100 105 110 Cys Phe Thr Ala Ser Cys Thr Leu Met Ala Leu Ala Ser Arg Asp Val 115 120 125 Glu Ala Leu Ser Pro Leu He Phe Leu Ala Leu Ser Leu Asn Gly Phe 130 135 140 Gly Gly He Cys Leu Thr Phe Thr Ser Leu Thr Leu Pro Asn Met Phe 145 150 155 160 Gly Asn Leu Arg Being Thr Leu Met Wing Leu Met He Gly Being Tyr Wing 165 170 175 Be Being Wing He Thr Phe Pro Gly He Lys Leu He Tyr Asp Wing Gly 180 185 190 Val Wing Phe Val Val He Met Phe Thr Trp Ser Gly Leu Wing Cys Leu 195 200 205 He Phe Leu Asn Cys Thr Leu Asn Trp Pro He Glu Wing Phe Pro Wing 210 215 220 Pro Glu Glu Val Asn Tyr Thr Lys Lys He Lys Leu Ser Gly Leu Wing 225 230 235 240 Leu Asp His Lys Val Thr Gly Asp Leu Phe Tyr Thr His Val Thr Thr 245 250 255 Met Gly Gln Arg Leu Ser Gln Lys Wing Pro Ser Leu Glu Asp Gly Ser 260 265 270 Asp Wing Phe Met Ser Pro Gln Asp Val Arg Gly Thr Ser Glu Asn Leu 275 280 285 Pro Glu Arg Ser Val Pro Leu Arg Lys Ser Leu Cys Be Pro Thr Phe 290 295 300 Leu Trp Be Leu Leu Thr Met Gly Met Thr Gln Leu Arg He He Phe 305 310 315 320 Tyr Met Ala Ala Val Asn Lys Met Leu Glu Tyr Leu Val Thr Gly Gly 325 330 335 Gln Glu His Glu Thr Asn Glu Gln Gln Gln Lys Val Wing Glu Thr Val 340 345 350 Gly Phe Tyr Ser Val Phe Gly Wing Met Gln Leu Leu Cys Leu Leu 355 360 365 Thr Cys Pro Leu He Gly Tyr He Met Asp Trp Arg He Lys Asp Cys 370 375 380 Val Asp Wing Pro Thr Gln Gly Thr Val Leu Gly Asp Wing Arg Asp Gly 385 390 395 400 Val Ala Thr Lys Ser He Arg Pro Arg Tyr Cys Lys He Gln Lys Leu 405 410 415 Thr Asn Wing Be Wing Phe Thr Leu Thr Asn Leu Leu Leu Val Gly 420 425 430 Phe Gly He Thr Cys Leu He Asn Asn Leu His Leu Gln Phe Val Thr 435 440 445 Phe Val Leu His Thr He Val Arg Gly Phe Phe His Be Ala Cys Gly 450 455 460 Ser Leu Tyr Ala Ala Val Phe Pro Ser Asn His Phe Gly Thr Leu Thr 465 470 475 480 Gly Leu Gln Ser Leu Ha Be Wing Val Phe Ala Leu Leu Gln Gln Pro 485 490 495 Leu Phe Met Wing Met Val Gly Pro Leu Lys Gly Glu Pro Phe Trp Val 500 505 510 Asn Leu Gly Leu Leu Phe Ser Leu Leu Gly Phe Leu Leu Pro Ser 515 520 525 Tyr Leu Phe Tyr Tyr Arg Ala Arg Leu Gln Gln Glu Tyr Ala Ala Asn 530 535 540 Gly Met Gly Pro Leu Lys Val Leu Ser Gly Ser Glu Val Thr Ala 545 550 555 (2) INFORMATION FOR SEQ ID NO: 22: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 330 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10304 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 22: Met Glu Gly Ala Pro Pro Gly Ser Leu Ala Leu Arg Leu Leu Leu Phe 1 5 10 15 Val Ala Leu Pro Wing Ser Gly Trp Leu Thr Thr Gly Wing Pro Glu Pro 20 25 30 Pro Pro Leu Ser Gly Wing Pro Gln Asp Gly He Arg He Asn Val Thr 35 40 45 Thr Leu Lys Asp Asp Gly Asp He Ser Lys Gln Gln Val Val Leu Asn 50 55 60 He Thr Tyr Glu Ser Gly Gln Val Tyr Val Asn Asp Leu Pro Val Asn 65 70 75 80 Ser Gly Val Thr Arg He Ser Cys Gln Thr Leu He Val Lys Asn Glu 85 90 95 Asn Leu Glu Asn Leu Glu Glu Lys Glu Tyr Phe Gly He Val Ser Val 100 105 110 Arg He Leu Val His Glu Trp Pro Met Thr Ser Gly Ser Ser Leu Gln 115 120 125 Leu He Val He Gln Glu Val Val Glu He Asp Gly Lys Gln Val 130 135 140 Gln Gln Lys Asp Val Thr Glu He Asp He Leu Val Lys Asn Arg Gly 145 150 155 160 Val Leu Arg His Ser Asn Tyr Thr Leu Pro Leu Glu Glu Ser Met Leu 165 170 175 Tyr Ser He Ser Arg Asp Ser Asp He Leu Phe Thr Leu Pro Asn Leu 180 185 190 Ser Lys Lys Glu Ser Val Ser Ser Leu Gln Thr Thr Ser Gln Tyr Leu 195 200 205 He Arg Asn Val Glu Thr Val Val Asp Glu Asp Val Leu Pro Gly Lys 210 215 220 Leu Pro Glu Thr Pro Leu Arg Ala Glu Pro Pro Ser Ser Tyr Lys Val 225 230 235 240 Met Cys Gln Trp Met Glu Lys Phe Arg Lys Asp Leu Cys Arg Phe Trp 245 250 255 Be Asn Val Phe Pro Val Phe Phe Gln Phe Leu Asn He Met Val Val 260 265 270 Gly He Thr Gly Wing Wing Val Val He Thr He Leu Val Val Phe Phe 275 '280 285 Pro Val Ser Glu Tyr Lys Gly He Leu Gln Leu Asp Lys Val Asp Val 290 295 300 He Pro Val Thr Ala He Asn Leu Tyr Pro Asp Gly Pro Glu Lys Arg 305 310 315 320 Wing Glu Asn Leu Glu Asp Lys Thr Cys He 325 330 (2) INFORMATION FOR SEQ ID NO: 23: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 108 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10305 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 23: Met Ser Leu Thr Ser Ser Ser Ser Val Val Val Glu Trp He Ala Ala 1 5 10 15 Val Thr He Wing Wing Gly Thr Wing Wing He Gly Tyr Leu Wing Tyr Lys 20 25 30 Arg Phe Tyr Val Lys Asp His Arg Asn Lys Wing Met He Asn Leu His 35 40 45 He Gln Lys Asp Asn Pro Lys He Val His Wing Phe Asp Met Glu Asp 50 55 60 Leu Gly Asp Lys Wing Val Tyr Cys Arg Cys Trp Arg Ser Lys Lys Phe 65 70 75 80 Pro Phe Cys Asp Gly Ala His Thr Lys His Asn Glu Glu Thr Gly Asp 85 90 95 Asn Val Gly Pro Leu He He Lys Lys Lys Glu Thr 100 105 (2) INFORMATION FOR SEQ ID NO: 24: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 101 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Ostaosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10306 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 24: Met Asn Leu Glu Arg Val Ser Asn Glu Glu Lys Leu Asn Leu Cys Arg 1 5 10 15 Lys Tyr Tyr Leu Gly Gly Phe Wing Phe Leu Pro Phe Leu Trp Leu Val 20 25 30 Asn He Phe Trp Phe Phe Arg Glu Wing Phe Leu Val Pro Wing Tyr Thr 35 40 45 Glu Gln Ser Gln He Lys Gly Tyr Val Trp Arg Ser Wing Val Gly Phe 50 55 60 Leu Phe Trp Val He Val Leu Thr Ser Trp He Thr He Phe Gln He 65 70 75 80 Tyr Arg Pro Arg Trp Gly Wing Leu Gly Asp Tyr Leu Ser Phe Thr He 85 90 95 Pro Leu Gly Thr Pro 100 (2) INFORMATION FOR SEQ ID NO: 25: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 372 (B) TYPE: Amino Acid (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: Protein (iii) HYPOTHETICAL : No (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELLULAR LINE: KB (D) CLONE NAME: HP10328 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 25: Met Lys Tyr Leu Arg His Arg Arg Pro Asn Wing Thr Leu He Leu Wing 1 5 10 15 He Gly Wing Phe Thr Leu Leu Leu Phe Ser Leu Leu Val Ser Pro Pro 20 25 30 Thr Cys Lys Val Gln Gllu Pro Pro Wing Pro Glu Ala Leu Wing 35 40 45 Trp Pro Thr Pro Pro Thr Arg Pro Wing Pro Pro Wing Cys His Ala Asn 50 55 60 Thr Ser Met Val Thr His Pro Asp Phe Ala Thr Gln Pro Gln His Val 65 70 75 80 Gln Asn Phe Leu Leu Tyr Arg His Cys Arg His Phe Pro Leu Leu Gln 85 90 95 Asp Val Pro Pro Ser Lys Cys Wing Gln Pro Val Phe Leu Leu Val Val 105 105 110 He Lys Ser Ser Pro Ser Asn Tyr Val Arg Arg Glu Leu Leu Arg Arg 115 120 125 Thr Trp Gly Arg Glu Arg Lys Val Arg Gly Leu Gln Leu Arg Leu Leu 130 135 140 Phe Leu Val Gly Thr Ala Ser Asn Pro His Glu Ala Arg Lys Val Asn 145 150 155 160 Arg Leu Leu Glu Leu Glu Wing Gln Thr His Gly Asp He Leu Gln Trp 165 170 175 Asp Phe His Asp Ser Phe Phe Asn Leu Thr Leu Lys Gln Val Leu Phe 180 185 190 Leu Gln Trp Gln Glu Thr Arg Cys Wing Asn Wing Being Phe Val Leu Asn 195 200 205 Gly Asp Asp Asp Val Phe Wing His Thr Asp Asn Met Val Pha Tyr Leu 210 215 220 Gln Asp His Asp Pro Gly Arg His Leu Phe Val Gly Gln Leu He Gln 225 230 235 240 Asn Val Gly Pro He Arg Ala Phe Trp Ser Lys Tyr Tyr Val Pro Glu 245 250 255 Val Val Thr Gln Asn Glu Arg Tyr Pro Pro Tyr Cys Gly Gly Gly Gly 260 265 270 Phe Leu Leu Ser Arg Phe Thr Wing Wing Wing Leu Arg Wing Ala Wing 275 280 285 Val Leu Asp He Phe Pro He Asp Asp Val Phe Leu Gly Met Cys Leu 290 295 300 Glu Leu Glu Gly Leu Lys Pro Wing His Ser Gly He Arg Thr Ser 305 310 315 320 Gly Val Arg Ala Pro Ser Gln His Leu Ser Ser Phe Asp Pro Cys Phe 325 330 335 Tyr Arg Asp Leu Leu Leu Val His Arg Phe Leu Pro Tyr Glu Met Leu 340 345 350 Leu Met Trp Asp Ala Leu Asn Gln Pro Asn Leu Thr Cys Gly Asn Gln 355 360 365 Thr Gln He Tyr 370 (2) INFORMATION FOR SEQ ID NO: 26: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 615 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP00442 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 26: ATGACGGGGC TAGCACTGCT CTACTCCGGG GTCTTCGTGG CCTTCTGGGC CTGCGCGCTG 60 GCCGTGGGAG TCTGCTACAC CATTTTTGAT TTGGGCTTCC GCTTTGATGT GGCATGGTTC 120 CTGACGGAGA CTTCGCCCTT CATGTGGTCC AACCTGGGCA TTGGCCTAGC TATCTCCCTG 180 TCTGTGGTTG GGGCAGCCTG GGGCATCTAT ATTACCGGCT CCTCCATCAT TGGTGGAGGA 240 GTGAAGGCCC CCAGGATCAA GACCAAGAAC CTGGTCAGCA TCATCTTCTG TGAGGCTGTG 300 GCCATCTACG GCATCATCAT GGCAATTGTC ATTAGCAACA TGGCTGAGCC TTTCAGTGCC 360 ACAGACCCCA AGGCCATCGG CCATCGGAAC TACCATGCAG GCTACTCCAT GTTTGGGGCT 420 GGCCTCACCG TAGGCCTGTC TAACCTCTTC TGTGGAGTCT GCGTGGGCAT CGTGGGCAGT 480 GGGGCTGCCC TGGCCGATGC TCAGAACCCC AGCCTCTTTG TAAAGATTCT CATCGTGGAG 540 ATCTTTGGCA GCGCCATTGG CCTCTTTGGG GTCATCGTCG GAATTCTTCA GACCTCCAGA 600 GTGAAGATGG GTGAC 615 (2) INFORMATION FOR SEQ ID NO: 27: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1113 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Leukocyte (D) CLONE NAME: HP00804 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 27 : ATGTCCCATG AAAAGAGTTT TTTGGTGTCT GGGGACAACT ATCCTCCCCC CAACCCTGGA 60 TATCCGGGGG GGCCCCAGCC ACCCATGCCC CCCTATGCTC AGCCTCCCTA CCCTGGGGCC 120 CCTTACCCAC AGCCCCCTTT CCAGCCCTCC CCCTACGGTC AGCCAGGGTA CCCCCATGGC 180 CCCAGCCCCT ACCCCCAAGG GGGCTACCCA CAGGGTCCCT ACCCCCAAGG GGGCTACCCA 240 CAGGGCCCCT ACCCACAAGA GGGCTACCCA CAGGGCCCCT ACCCCCAAGG GGGCTACCCC 300 CAGGGGCCAT ATCCCCAGAG CCCCTTCCCC CCCAACCCCT ATGGACAGCC ACAGGTCTTC 360 CCAGGACAAG ACCCTGACTC ACCCCAGCAT GGAAACTACC AGGAGGAGGG TCCCCCATCC 420 TACTATGACA ACCAGGACTT CCCTGCCACC AACTGGGATG ACAAGAGCAT CCGACAGGCC 480 TTCATCCGCA AGGTGTTCCT AGTGCTGACC TTGCAGCTGT CGGTGACCCT GTCCACGGTG 540 TCTGTGTTCA CTTTTGTTGC GGAGGTGAAG GGCTTTGTCC GGGAGAATGT CTGGACCTAC 600 TATGTCTCCT ATGCTGTCTT CTTCATCTCT CTCATCGTCC TCAGCTGTTG TGGGGACTTC 660 CGGCGAAAGC ACCCCTGGAA CCTTGTTGCA CTGTCGGTCC TGACCGCCAG CCTGTCGTAC 720 ATGGTGGGGA TGATCGCCAG CTTCTACAAC ACCGAGGCAG TCATCATGGC CGTGGGCATC 780 ACCACAGCCG TCTGCTTCAC CGTCGTCATC TTCTCCATGC AGACCCGCTA CGACTTCACC 840 TCATGCATGG GCGTGCTCCT GGTGAGCATG GTGGTGCTCT TCATCTTCGC CATTCTCTGC 900 ATCTTCATCC GGAACCGCAT CCTGGAGATC GTGTACGCCT CACTGGGCGC TCTGCTCTTC 960 ACCTGCTTCC TCGCAGTGGA CACCCAGCTG CTGCTGGGGA ACAAGCAGCT GTCCCTGAGC 1020 CCAGAAGAGT ATGTGTTTGC TGCGCTGAAC CTGTACACAG ACATCATCAA CATCTTCCTG 1080 TACATCCTCA CCATCATTGG CCGCGCCAAG GAG 1113 (2) INFORMATION FOR SEQ ID NO: 28: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 537 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP01098 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO : 28: ATGCTGTCTC TAGACTTTTT GGACGATGTG CGGCGGATGA ACAAGCGGCA GCTCTATTAT 60 CAAGTCCTAA ATTTTGGAAT GATTGTCTCA TCGGCACTAA TGATCTGGAA GGGGTTAATG 120 GTAATAACTG GAAGTGAAAG TCCGATTGTA GTGGTGCTCA GTGGCAGCAT GGAACCTGCA 180 TTTCATAGAG GAGATCTTCT CTTTCTAACA AATCGAGTTG AAGATCCCAT ACGAGTGGGA 240 GAAATTGTTG TTTTTAGGAT AGAAGGAAGA GAGATTCCTA TAGTTCACCG AGTCTTGAAG 300 ATTCATGAAA AGCAAAATGG GCATATCAAG TTTTTGACCA AAGGAGATAA TAATGCGGTT 360 GATGACCGAG GCCTCTATAA ACAAGGACAA CATTGGCTAG AGAAAAAAAA TGTTGTGGGG 420 AGAGCCAGGG GATTTGTTCC TTATATTGGA ATTGTGACGA TCCTCATGAA TGACTATCCT 480 AAATTTAAGT ATGCAGTTCT CTTTTTTGCTG GGTTTATTCG TGCTGGTTCA TCGTGAG 537 (2) INFORMATION FOR SEQ ID NO: 29: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1041 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP01148 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 29 : ATGGCTCTGC TATTCTCCTT GATCCTTGCC ATTTGCACCA GACCTGGATT CCTAGCGTCT 60 CCATCTGGAG TGCGGCTGGT GGGGGGCCTC CACCGCTGTG AAGGGCGGGT GGAGGTGGAA 120 CAGAAAGGCC AGTGGGGCAC CGTGTGTGAT GACGGCTGGG ACATTAAGGA CGTGGCTGTG 180 TTGTGCCGGG AGCTGGGCTG TGGAGCTGCC AGCGGAACCC CTAGTGGTAT TTTGTATGAG 240 CCACCAGCAG AAAAAGAGCA AAAGGTCCTC ATCCAATCAG TCAGTTGCAC AGGAACAGAA 300 GATACATTGG CTCAGTGTGA GCAAGAAGAA GTTTATGATT GTTCACATGA AGAAGATGCT 360 GGGGCATCGT GTGAGAACCC AGAGAGCTCT TTCTCCCCAG TCCCAGAGGG TGTCAGGCTG 420 GCTGACGGCC CTGGGCATTG CAAGGGACGC GTGGAAGTGA AGCACCAGAA CCAGTGGTAT 480 ACCGTGTGCC AGACAGGCTG GAGCCTCCGG GCCGCAAAGG TGGTGTGCCG GCAGCTGGGA 540 TGTGGGAGGG CTGTACTGAC TCAAAAACGC TGCAACAAGC ATGCCTATGG CCGAAAACCC 600 ATCTGGCTGA GCCAGATGTC ATGCTCAGGA CGAGAAGCAA CCCTTCAGGA TTGCCCTTCT 660 GGGCCTTGGG GGAAGAACAC CTGCAACCAT GATGAAGACA CGTGGGTCGA ATGTGAAGAT 720 CCCTTTGACT TGAGACTAGT AGGAGGAGAC AACCTCTGCT CTGGGCGACT GGAGGTGCTG 780 CACAAGGGCG TATGGGGCTC TGTCTGTGAT GACAACTGGG GAGAAAAGGA GGACCAGGTG 840 GTATGCAAGC AACTGGGCTG TGGGAAGTCC CTCTCTCCCT CCTTCAGAGA CCGGAAATGC 900 TATGGCCCTG GGGTTGGCCG CATCTGGCTG GATAATGTTC GTTGCTCAGG GGAGGAGCAG 960 TCCCTGGAGC AGTGCCAGCA CAGATTTTGG GGGTTTCACG ACTGCACCCA CCAGGAAGAT 1020 GTGGCTGTCA TCTGCTCAGG A 1041 (2) INFORMATION FOR SEQ ID NO: 30: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1662 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Ho or sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP01293 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 30: ATGCCCACCG TGGATGACAT TCTGGAGCAG GTTGGGGAGT CTGGCTGGTT CCAGAAGCAA 60 GCCTTCCTCA TCTTATGCCT GCTGTCGGCT GCCTTTGCGC CCATCTGTGT GGGCATCGTC 120 TTCCTGGGTT TCACACCTGA CCACCACTGC CAGAGTCCTG GGGTGGCTGA GCTGAGCCAG 180 CGCTGTGGCT GGAGCCCTGC GGAGGAGCTO AACTATACAG TGCCAGGCCT GGGGCCCGCG 240 GGCGAGGCCT TCCTTGGCCA GTGCAGGCGC TATGAAGTGG ACTGGAACCA GAGCGCCCTC 300 AGCTGTGTAG ACCCCCTGGC TAGCCTGGCC ACCAACAGGA GCCACCTGCC GCTGGGTCCC 360 TGCCAGGATG GCTGGGTGTA TGACACGCCC GGCTCTTCCA TCGTCACTGA GTTCAACCTG 420 GTGTGTGCTG ACTCCTGGAA GCTCGACCTC TTTCAGTCCT GTTTGAATGC GGGCTTCTTC 480 TTTGGCTCTC TCGGTGTTGG CTACTTTGCA GACAGGTTTG GCCGTAAGCT GTGTCTCCTG 540 GGAACTGTGC TGGTCAACGC GGTGTCGGGC GTGCTCATGG CCTTCTCGCC CAACTACATG 600 TCCATGCTGC TCTTCCGCCT GCTGCAGGGC CTGGTCAGCA AGGGCAACTG GATGGCTGGC 660 TACACCCTAA TCACAGAATT TGTTGGCTCG GGCTCCAGAA GAACGGTGGC GATCATGTAC 720 CAGATGGCCT TCACGGTGGG GCTGGTGGCG CTTACCGGGC TGGCCTACGC CCTGCCTCAC 780 TGGCGCTGGC TGCAGCTGGC AGTCTCCCTG CCCACCTTCC TCTTCCTGCT CTACTACTGG 840 TGTGTGCCGG AGTCCCCTCG GTGGCTGTTA TCACAAAAAA GAAACACTGA AGCAATAAAG 900 ATAATGGACC ACATCGCTCA AAAGAATGGG AAGTTGCCTC CTGCTGATTT AAAGATGCTT 960 TCCCTCGAAG AGGATGTCAC CGAAAAGCTG AGCCCTTCAT TTGCAGACCT GTTCCGCACG 1020 CCGCGCCTGA GGAAGCGCAC CTTCATCCTG ATGTACCTGT GGTTCACGGA CTCTGTGCTC 1080 TATCAGGGGC TCATCCTGCA CATGGGCGCC ACCAGCGGGA ACCTCTACCT GGATTTCCTT 1140 TACTCCGCTC TGGTCGAAAT CCCGGGGGCC TTCATAGCCC TCATCACCAT TGACCGCGTG 1200 GGCCGCATCT ACCCCATGGC CGTGTCAAAT TTGTTGGCGG GGGCAGCCTG CCTCGTCATG 1260 ATTTTTTATCT CACCTGACCT GCACTGGTTA AACATCATAA TCATGTGTGT TGGCCGAATG 1320 GGAATCACCA TTGCAATACA AATGATCTGC CTGGTGAATG CTGAGCTGTA CCCCACATTC 1380 GTCAGGAACC TCGGAGTGAT GGTGTGTTCC TCCCTGTGTG ACATAGGTGG GATAATCACC 1440 CCCTTCATAG TCTTCAGGCT GAGGGAGGTC TGGCAAGCCT TGCCCCTCAT TTTGTTTGCG 1500 GTGTTGGGCC TGCTTGCCGC GGGAGTGACG CTACTTCTTC CAGAGACCAA GGGGGTCGCT 1560 TTGCCAGAGA CCATGAAGGA CGCCGAGAAC CTTGGGAGAA AAGCAAAGCC CAAAGAAAAC 1620 ACGATTTACC TTAAGGTCCA AACCTCAGAA CCCTCGGGCA CC 1662 (2) INFORMATION FOR SEQ ID NO: 31: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1050 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10013 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 31: ATGGCTGTGT TTGTCGTGCT CCTGGCGTTG GTGGCGGGTG TTTTGGGGAA CGAGTTTAGT 60 ATATTAAAAT CACCAGGGTC TGTTGTTTTC CGAAATGGAA ATTGGCCTAT ACCAGGAGAG 120 CGGATCCCAG ACGTGGCTGC ATTGTCCATG GGCTTCTCTG TGAAAGAAGA CCTTTCTTGG 180 CCAGGACTCG CAGTGGGTAA CCTGTTTCAT CGTCCTCGGG CTACCGTCAT GGTGATGGTG 240 AAGGGAGTGA ACAAACTGGC TCTACCCCCA GGCAGTGTCA TTTCGTACCC TTTGGAGAAT 300 GCAGTTCCTT TTAGTCTTGA CAGTGTTGCA AATTCCATTC ACTCCTTATT TTCTGAGGAA 360 ACTCCTGTTG TTTTGCAGTT GGCTCCCAGT GAGGAAAGAG TGTATATGGT AGGGAAGGCA 420 AACTCAGTGT TTGAAGACCT TTCAGTCACC TTGCGCCAGC TCCGTAATCG CCTGTTTCAA 480 GAAAACTCTG TTCTCAGTTC ACTCCCCCTC AATTCTCTGA GTAGGAACAA TGAAGTTGAC 540 CTGCTCTTTC TTTCTGAACT GCAAGTGCTA CATGATATTT CAAGCTTGCT GTCTCGTCAT 600 AAGCATCTAG CCAAGGATCA TTCTCCTGAT TTATATTCAC TGGAGCTGGC AGGTTTGGAT 660 GAAATTGGGA AGCGTTATGG GGAAGACTCT GAACAATTCA GAGATGCTTC TAAGATCCTT 720 GTTGACGCTC TGCAAAAGTT TGCAGATGAC ATGTACAGTC TTTATGGTGG GAATGCAGTG 780 GTAGAGTTAG TCACTGTCAA GTCATTTGAC ACCTCCCTCA TTAGGAAGAC AAGGACTATC 840 CTTGAGGCAA AACAAGCGAA GAACCCAGCA AGTCCCTATA ACCTTGCATA TAAGTATAAT 900 TTTGAATATT CCGTGGTTTT CAACATGGTA CTTTGGATAA TGATCGCCTT GGCCTTGGCT 960 GTGATTATCA CCTCTTACAA TATTTGGAAC ATGGATCCTG GATATGATAG CATCATTTAT 1020 AGGATGACAA ACCAGAAGAT TCGAATGGAT 1050 (2) INFORMATION FOR SEQ ID NO: 32: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 627 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10034 (xi) DESCRIPTION SEQUENCE: SEQ ID NO: 32: ATGGTGTCCT CTCCCTGCAC GCAGGCAAGC TCACGGACTT GCTCCCGTAT CCTGGGACTG 60 AGCCTTGGGA CTGCAGCCCT GTTTGCTGCT GGGGCCAACG TGGCACTCCT CCTTCCTAAC 120 TGGGATGTCA CCTACCTGTT GAGGGGCCTC CTTGGCAGGC ATGCCATGCT GGGAACTGGG 180 CTCTGGGGAG GAGGCCTCAT GGTACTCACT GCAGCTATCC TCATCTCCTT GATGGGCTGG 240 AGATACGGCT GCTTCAGTAA GAGTGGGCTC TGTCGAAGCG TGCTTACTGC TCTGTTGTCA 300 GGTGGCCTGG CTTTACTTGG AGCCCTGATT TGCTTTGTCA CTTCTGGAGT TGCTCTGAAA 360 GATGGTCCTT TTTGCATGTT TGATGTTTCA TCCTTCAATC AGACACAAGC TTGGAAATAT 420 GGTTACCCAT TCAAAGACCT GCATAGTAGG AATTATCTGT ATGACCGTTC GCTCTGGAAC 480 TCCGTCTGCC TGGA GCCCTC TGCAGCTGTT GTCTGGCACG TGTCCCTCTT CTCCGCCCTT 540 CTGTGCATCA GCCTGCTCCA GCTTCTCCTG GTGGTCGTTC ATGTCATCAA CAGCCTCCTG 600 GGCCTTTTCT GCAGCCTCTG CGAGAAG 627 (2) INFORMATION FOR SEQ ID NO: 33: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 489 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10050 (xi) DESCRIPTION SEQUENCE: SEQ ID NO: 33: ATGGCGGCTG GGCTGTTTGG TTTGAGCGCT CGCCGTCTTT TGGCGGCAGC GGCGACGCGA 60 GGGCTCCCGG CCGCCCGCGT CCGCTGGGAA TCTAGCTTCT CCAGGACTGT GGTCGCCCCG 120 TCCGCTGTGG CGGGAAAGCG GCCCCCAGAA CCGACCACAC CGTGGCAAGA GGACCCAGAA 180 CCCGAGGACG AAAACTTGTA TGAGAAGAAC CCAGACTCCC ATGGTTATGA CAAGGACCCC 240 GTTTTGGACG TCTGGAACAT GCGACTTGTC TTCTTCTTTG GCGTCTCCAT CATCCTGGTC 300 CTTGGCAGCA CCTTTGTGGC CTATCTGCCT GACTACAGGT GCACAGGGTG TCCAAGAGCG 360 TGGGATGGGA TGAAAGAGTG GTCCCGCCGC GAAGCTGAGA GGCTTGTGAA ATACCGAGAG 420 GCCAATGGCC TTCCCATCAT GGAATCCAAC TGCTTCGACC CCAGCAAGAT CCAGCTGCCA 480 GAGGATGAG 489 (2) INFORMATION FOR SEQ ID NO: 34: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 276 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear * - í (ii) ) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10071 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 34: ATGACGAAAT TAGCGCAGTG GCTTTGGGGA CTAGCGATCC TGGGCTCCAC CTGGGTGGCC 60 CTGACCACGG GAGCCTTGGG CCTGGAGCTG CCCTTGTCCT GCCAGGAAGT CCTGTGGCCA 120 CTGCCCGCCT ACTTGCTGGT GTCCGCCGGC TGCTATGCCC TGGGCACTGT GGGCTATCGT 180 GTGGCCACTT TTCATGACTG CGAGGACGCC GCACGCGAGC TGCAGAGCCA GATACAGGAG 240 GCCCGAGCCG ACTTAGCCCG CAGGGGGCTG CGCTTC 276 (2) INFORMATION FOR SEQ ID NO: 35: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 516 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10076 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 35: ATGGAATATT TGGCTCATCC CAGTACACTC GGCTTGGCTG TTGGAGTTGC TTGTGGCATG 60 TGCCTGGGCT GGAGCCTTCG AGTATGCTTT GGGATGCTCC CCAAAAGCAA GACGAGCAAG 120 ACACACACAG ATACTGAAAG TGAAGCAAGC ATCTTGGGAG ACAGCGGGGA GTACAAGATG 180 ATTCTTGTGG TTCGAAATGA CTTAAAGATG GGAAAAGGGA AAGTGGCTGC CCAGTGCTCT 240 CATGCTGCTG TTTCAGCCTA CAAGCAGATT CAAAGAAGAA ATCCTGAAAT GCTCAAACAA 300 TGGGAATACT GTGGCCAGCC CAAGGTGGTG GTCAAAGCTC CTGATGAAGA AACCCTGATT 360 GCATTATTGG CCCATGCAAA AATGCTGGGA CTGACTGTAA GTTTAATTCA AGATGCTGGA 420 CGTACTCAGA TTGCACCAGG CTCTCAAACT GTCCTAGGGA TTGGGCCAGG ACCAGCAGAC 480 CTAATTGACA AAGTCACTGG T CACCTAAAA CTTTAC 516 (2) INFORMATION FOR SEQ ID NO: 36: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 447 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10085 '(xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 36: ATGATGACCA AACATAAAAA GTGTTTTATA ATTGTTGGTG TTTTAATAAC AACTAATATT 60 ATTACTCTGA TAGTTAAACT AACTCGAGAT TCTCAGAGTT TATGCCCCTA TGATTGGATT 120 GGTTTCCAAA ACAAATGCTA TTATTTCTCT AAAGAAGAAG GAGATTGGAA TTCAAGTAAA 180 TACAACTGTT CCACTCAACA TGCCGACCTA ACTATAATTG ACAACATAGA AGAAATGAAT 240 TTTCTTAGGC GGTATAAATG CAGTTCTGAT CACTGGATTG GACTGAAGAT GGCAAAAAAT 300 CGAAGAGGAC AATGGGTAGA TGGAGCTACA TTTACCAAAT CGTTTGGCAT GAGAGGGAGT 360 GAAGGATGTG CCTACCTCAG CGATGATGGT GCAGCAACAG CTAGATGTTA CACCGAAAGA 420 AAATGGATTT GCAGGAAAAG AATACAC 447 (2) INFORMATION FOR SEQ ID NO: 37: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 564 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10122 (i) DESCRIPTION OF SEQUENCE: SEQ ID NO : 37: ATGAGCACTA TGTTCGCGGA CACTCTCCTC ATCGTTTTTA TCTCTGTGTG CACGGCTCTG 60 CTCGCAGAGG GCATAACCTG GGTCCTGGTT TACAGGACAG ACAAGTACAA GAGACTGAAG 120 GCAGAAGTGG AAAAACAGAG TAAAAAATTG GAAAAGAAGA AGGAAACAAT AACAGAGTCA 180 GCTGGTCGAC AACAGAAAAA GAAAATAGAG AGACAAGAAG AGAAACTGAA GAATAACAAC 240 AGAGATCTAT CAATGGTTCG AATGAAATCC ATGTTTGCTA TTGGCTTTTG TTTTACTGCC 300 CTAATGGGAA TGTTCAATTC CATATTTGAT GGTAGAGTGG TGGCAAAGCT TCCTTTTACC 360 CCTCTTTCTT ACATCCAAGG ACTGTCTCAT CGAAATCTGC TGGGAGATGA CACCACAGAC 420 TGTTCCTTCA TTTTCCTGTA TATTCTCTGT ACTATGTCGA TTCGACAGAA CATTCAGAAG 480 ATTCTCGGCC TTGCCCCTTC ACGAGCCGCC ACCAAGCAGG CAGGTGGATT TCTTGGCCCA 540 CCACCTCCTT CTGGGAAGTT CTCT 564 (2) INFORMATION FOR SEQ ID NO: 38: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 645 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear '(ii) TYPE SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELL LINE: U937 (D) CLONE NAME: HP10136 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 38: ATGGTGTTGC TAACAATGAT CGCCCGAGTG GCGGACGGGC TCCCGCTGGC CGCCTCGATG 60 CAGGAGGACG AACAGTCTGG CCGGGACCTT CAACAGTATC AGAGTCAGGC TAAGCAACTC 120 TTTCGAAAGT TGAATGAACA GTCCCCTACC AGATGTACCT TGGAAGCAGG AGCCATGACT 180 TTTCACTACA TTATTGAGCA GGGGGTGTGT TATTTGGTTT TATGTGAAGC TGCCTTCCCT 240 AAGAAGTTGG CTTTTGCCTA CCTAGAAGAT TTGCACTCAG AATTTGATGA ACAGCATGGA 300 AAGAAGGTGC CCACTGTGTC CCGACCCTAT TCCTTTATTG AATTTGATAC TTTCATTCAG 360 AAAACCAAGA AGCTCTACAT TGACAGTCGT GCTCGAAGAA ATCTAGGCTC CATCAAGACT 420 GAATTGCAAG ATGTGCAGAG GATCATGGTG GCCAATATTG AAGAAGTGTT ACAACGAGGA 480 GAAGCACTCT CAGCATTGGA TTCAAAGGCT AACAATTTGT CCAGTCTGTC CAAGAAATAC 540 CGCCAGGATG CGAAGTACTT GAACATGCGT TCCACTTATG CCAAACTTGC AGCAGTAGCT 600 GTATTTTTCA TCATGTTAAT AGTGTATGTC CGATTCTGGT GGCTG 645 (2) INFORMATION FOR SEQ ID NO: 39: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 336 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10175 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO : 39: ATGCAGGACA CTGGCTCAGT AGTGCCTTTG CATTGGTTTG GCTTTGGCTA CGCAGCACTG 60 GTTGCTTCTG GTGGGATCAT TGGCTATGTA AAAGCAGGCA GCGTGCCGTC CCTGGCTGCA 120 GGGCTGCTCT TTGGCAGTCT AGCCGGCCTG GGTGCTTACC AGCTGTCTCA GGATCCAAGG 180 AACGTTTGGG TTTTCCTAGC TACATCTGGT ACCTTGGCTG GCATTATGGG AATGAGGTTC 240 TACCACTCTG GAAAATTCAT GCCTGCAGGT TTAATTGCAG GTGCCAGTTT GCTGATGGTC 300 GCCAAAGTTG GAGTTAGTAT GTTCAACAGA CCCCAT 336 (2) INFORMATION FOR SEQ ID NO: 40: '(i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 342 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Epidermoid carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10179 (xi) DESCRIPTION SEQUENCE: SEQ ID NO: 40: ATGGAGAAGC CCCTCTTCCC ATTAGTGCCT TTGCATTGGT TTGGCTTTGG CTACACAGCA 60 CTGGTTGTTT CTGGTGGGAT CGTTGGCTAT GTAAAAACAG GCAGCGTGCC GTCCCTGGCT 120 GCAGGGCTGC TCTTCGGCAG TCTAGCCGGC CTGGGTGCTT ACCAGCTGTA TCAGGATCCA 180 AGGAACGTTT GGGGTTTCCT AGCCGCTACA TCTGTTACTT TTGTTGGTGT TATGGGAATG 240 AGATCCTACT ACTATGGAAA ATTCATGCCT GTAGGTTTAA TTGCAGGTGC CAGTTTGCTG 300 ATGGCCGCCA AAGTTGGAGT TCGTATGTTG ATGACATCTG AT 342 (2) INFORMATION FOR SEQ ID NO: 41: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 981 (B) TYPE: Nualáic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10196 (xi) DESCRIPTION SEQUENCE: SEQ ID NO: 41: ATGGCGGCGG CGGCGGCGGC GGCTGCAGCT ACGAACGGGA CCGGAGGAAG CAGCGGGATG 60 GAGGTGGATG CAGCAGTAGT CCCCAGCGTG ATGGCCTGCG GAGTGACTGG GAGTGTTTCC 120 GTCGCTCTCC ATCCCCTTGT CATTCTCAAC ATCTCAGACC ACTGGATCCG CATGCGCTCC 180 CAGGAGGGGC GGCCTGTGCA GGTGATTGGG GCTCTGATTG GCAAGCAGGA GGGCCGAAAT 240 ATCGAGGTGA TGAACTCCTT TGAGCTGCTG TCCCACACCG TGGAAGAGAA GATTATCATT 300 GACAAGGAAT ATTATTACAC CAAGGAGGAG CAGTTTAAAC AGGTGTTCAA GGAGCTGGAG 360 TTTCTGGGTT GGTATACCAC AGGGGGGCCA CCTGACCCCT CGGACATCCA CGTCCATAAG 420 CAGGTGTGTG AGATCATCGA GAGCCCCCTC TTTCTGAAGT TGAACCCTAT GACCAAGCAC 480 ACAGATCTTC CT GTCAGCGT TTTTGAGTCT GTCATTGATA TAATCAATGG AGAGGCCACA 540 ATGCTGTTTG CTGAGCTGAC CTACACTCTG GCCACAGAGG AAGCGGAACG CATTGGTGTA 600 GACCACGTAG CCCGAATGAC AGCAACAGGC AGTGGAGAGA ACTCCACTGT GGCTGAACAC 660 CTGATAGCAC AGCACAGCGC CATCAAGATG CTGCACAGCC GCGTCAAGCT CATCTTGGAG 720 TACGTCAAGG CCTCTGAAGC GGGAGAGGTC CCCTTTAATC ATGAGATCCT GCGGGAGGCC 780 TATGCTCTGT GTCACTGTCT CCCGGTGCTC AGCACAGACA AGTTCAAGAC AGATTTTTAT 840 GATCAATGCA ACGACGTGGG GCTCATGGCC TACCTCGGCA CCATCACCAA AACGTGCAAC 900 ACCATGAACC AGTTTGTGAA CAAGTTCAAT GTCCTCTACG ACCGACAAGG CATCGGCAGG 960 AGAATGCGCG GGCTCTTTTT C 981 (2) INFORMATION FOR SEQ ID NO: 42: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1119 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) LINE CELL: HT-1080 (D) NAME CLONE: HP10235 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 42: ATGACCCTAT GTGCCATGCT GCCCCTGCTG TTATTCACCT ACCTCAACTC CTTCCTGCAT 60 CAGAGGATCC CCCAGTCCGT ACGGATCCTG GGCAGCCTGG TGGCCATCCT GCTGGTGTTT 120 CTGATCACTG CCATCCTGGT GAAGGTGCAG CTGGATGCTC TGCCCTTCTT TGTCATCACC 180 ATGATCAAGA TCGTGCTCAT TAATTCATTT GGTGCCATCC TGCAGGGCAG CCTGTTTGGT 240 CTGGCTGGCC TTCTGCCTGC CAGCTACACG GCCCCCATCA TGAGTGGCCA GGGCCTAGCA 300 GGCTTCTTTG CCTCCGTGGC CATGATCTGC GCTATTGCCA GTGGCTCGGA GCTATCAGAA 360 AGTGCCTTCG GCTACTTTAT CACAGCCTGT GCTGTTATCA TTTTGACCAT CATCTGTTAC 420 CTGGGCCTGC CCCGCCTGGA ATTCTACCGC TACTACCAGC AGCTCAAGCT TGAAGGACCC 480 GGGGAGCAGG AGACCAAGTT GGACCTCATT AGCAAAGGAG AGGAGCCAAG AGCAGGCAAA 540 GAGGAATCTG GAGTTTCAGT CTCCAACTCT CAGCCCACCA ATGAAAGCCA CTCTATCAAA 600%% GCCATCCTGA AAAATATCTC AGTCCTGGCT TTCTCTGTCT GCTTCATCTT CACTATCACC 660 ATTGGGATGT TTCCAGCCGT GACTGTTGAG GTCAAGTCCA GCATCGCAGG CAGCAGCACC 720 TGGGAACGTT ACTTCATTCC TGTGTCCTGT TTCTTGACTT TCAATATCTT TGACTGGTTG 780 GGCCGGAGCC TCACAGCTGT ATTCATGTGG CCTGGGAAGG ACAGCCGCTG GCTGCCAAGC 840 CTGGTGCTGG CCCGGCTGGT GTTTGTGCCA CTGCTGCTGC TGTGCAACAT TAAGCCCCGC 900 CGCTACCTGA CTGTGGTCTT CGAGCACGAT GCCTGGTTCA TCTTCTTCAT GGCTGCCTTT 960 GCCTTCTCCA ACGGCTACCT CGCCAGCCTC TGCATGTGCT TCGGGCCCAA GAAAGTGAAG 1020 CCAGCTGAGG CAGAGACCGC AGGAGCCATC ATGGCCTTCT TCCTGTGTCT GGGTCTGGCA 1080 CTGGGGGCTG TTTTCTCCTT CCTGTTCCGG GCAATTGTG 1119 (2) INFORMATION FOR SEQ ID NO: 43: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 549 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10297 (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO : 43: ATGAAGCTCT TATCTTTGGT GGCTGTGGTC GGGTGTTTGC TGGTGCCCCC AGCTGAAGCC 60 AACAAGAGTT CTGAAGATAT CCGGTGCAAA TGCATCTGTC CACCTTATAG AAACATCAGT 120 GGGCACATTT AGAACCAGAA TGTATCCCAG AAGGACTGCA ACTGCCTGCA CGTGGTGGAG 180 CCCATGCCAG TGCCTGGCCA TGACGTGGAG GCCTACTGCC TGCTGTGCGA GTGCAGGTAC 240 GAGGAGCGCA GCACCACCAC CATCAAGGTC ATCATTGTCA TCTACCTGTC CGTGGTGGGT 300 GCCCTGTTGC TCTACATGGC CTTCCTGATG CTGGTGGACC CTCTGATCCG AAAGCCGGAT 360 GCATACACTG AGCAACTGCA CAATGAGGAG GAGAATGAGG ATGCTCGCTC TATGGCAGCA 420 GCTGCTGCAT CCCTCGGGGG ACCCCGAGCA AACACAGTCC TGGAGCGTGT GGAAGGTGCC 480 CAGCAGCGGT GGAAGCTGCA GGTGCAGGAG CAGCGGAAGA CAGTCTTCGA TCGGCACAAG 540 ATGCTCAGC 549 (2) INFORMATION FOR SEQ ID NO: 44: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 348 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10299, (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 44: ATGGCCAGTA CAGTGGTAGC AGTTGGACTG ACCATTGCTG CTGCAGGATT TGCAGGCCGT 60 TACGTTTTGC AAGCCATGAA GCATATGGAG CCTCAAGTAA AACAAGTTTT TCAAAGCCTA 120 CCAAAATCTG CCTTCAGTGG TGGCTATTAT AGAGGTGGGT TTGAACCCAA AATGACAAAA 180 CGGGAAGCA GCATTAATAC TAGGTGTAAG CCCTACTGCC AATAAAGGGA AAATAAGAGA 240 GCTCATCGAC GAATTATGCT TTTAAATCAT CCTGACAAAG GAGGATCTCC TTATATAGCA 300 GCCAAAATCA ATGAAGCTAA AGATTTACTA GAAGGTCAAG CTAAAAAA 348 (2) INFORMATION FOR SEQ ID NO: 45: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 456 (B) TYPE: Nuclide Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10301 (xi) DESCRIPTION SEQUENCE: SEQ ID NO: 45: ATGGCTGTCC TCTCTAAGGA ATATGGTTTT GTGCTTCTAA CTGGTGCTGC CAGCTTTATA 60 ATGGTGGCCC ACCTAGCCAT CAATGTTTCC AAGGCCCGCA AGAAGTACAA AGTGGAGTAT 120 CCTATCATGT ACAGCACGGA CCCTGAAAAT GGGCACATCT TCAACTGCAT TCAGCGAGCC 180 CACCAGAACA CGTTGGAAGT GTATCCTCCC TTCTTATTTT TTCTAGCTGT TGGAGGTGTT 240 TACCACCCGC GTATAGCTTC TGGCCTGGGC TTGGCCTGGA TTGTTGGACG AGTTCTTTAT 300 GCTTATGGCT ATTACACGGG AGAACCCAGC AAGCGTAGTC GAGGAGCCCT GGGGTCCATC 360 GCCCTCCTGG GCTTGGTGGG CACAACTGTG TGCTCTGCTT TCCAGCATCT TGGTTGGGTT 420 AAAAGTGGCT TGGGCAGTGG ACCCAAATGC TGCCAT 456 (2) INFORMATION FOR SEQ ID NO: 46: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1677 (B) TYPE: Nucleic Acid (C) BRANCH: Do ^ le (D) TOPOLOGY ": Linear (ii) ) TYPE OF SEQUENCE: cDNA for mRNA (i) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP10302 '(xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 46: ATGGCCCCCA CGCTGCAACA GGCGTACCGG AGGCGCTGGT GGATGGCCTG CACGGCTGTG 60 CTGGAGAACC TCTTCTTCTC TGCTGTACTC CTGGGCTGGG GCTCCCTGTT GATCATTCTG 120 AAGAACGAGG GCTTCTATTC CAGCACGTGC CCAGCTGAGA GCAGCACCAA CACCACCCAG 180 GATGAGCAGC GCAGGTGGCC AGGCTGTGAC CAGCAGGACG AGATGCTCAA CCTGGGCTTC 240 ACCATTGGTT CCTTCGTGCT CAGCGCCACC ACCCTGCCAC TGGGGATCCT CATGGACCGC 300 TTTGGCCCCC GACCCGTGCG GCTGGTTGGC AGTGCCTGCT TCACTGCGTC CTGCACCCTC 360 ATGGCCCTGG CCTCCCGGGA CGTGGAAGCT CTGTCTCCGT TGATATTCCT GGCGCTGTCC 420 CTGAATGGCT TTGGTCGCAT CTGCCTAACG TTCACTTCAC TCACGCTGCC CAACATGTTT 480 GGGAACCTGC GCTCCACGTT AATGGCCCTC ATGATTGGCT CTTACGCCTC TTCTGCCATT 540 ACGTTCCCAG GAATCAAGCT GATCTACGAT GCCGGTGTGG CCTTCGTGGT CATCATGTTC 600 ACCTGGTCTG GCCTGGCCTG CCTTATCTTT CTGAACTGCA CCCTCAACTG GCCCATCGAA 660 GCCTTTCCTG CCCCTGAGGA AGTCAATTAC ACGAAGAAGA TCAAGCTGAG TGGGCTGGCC 720 CTGGACCACA AGGTGACAGG TGACCTCTTC TACACCCATG TGACCACCAT GGGCCAGAGG 780 CTCAGCCAGA AGGCCCCCAG CCTGGAGGAC GGTTCGGATG CCTTCATGTC ACCCCAGGAT 840 GTTCGGGGCA CCTCAGAAAA CCTTCCTGAG AGGTCTGTCC CCTTACGCAA GAGCCTCTGC 900 TCCCCCACTT TCCTGTGGAG CCTCCTCACC ATGGGCATGA CCCAGCTGCG GATCATCTTC 960 TACATGGCTG CTGTGAACAA GATGCTGGAG TACCTTGTGA CTGGTGGCCA GGAGCATGAG 1020 ACAAATGAAC AGCAACAAAA GGTGGCAGAG ACAGTTGGGT TCTACTCCTC CGTCTTCGGG 1080 GCCATGCAGC TGTTGTGCCT TCTCACCTGC CCCCTCATTG GCTACATCAT GGACTGGCGG 1140 ATCAAGGACT GCGTGGACGC CCCAACTCAG GGCACTGTCC TCGGAGATGC CAGGGACGGG 1200 GTTGCTACCA AATCCATCAG ACCACGCTAC TGCAAGATCC AAAAGCTCAC CAATGCCATC 1260 AGTGCCTTCA CCCTGACCAA CCTGCTGCTT GTGGGTTTTG GCATCACCTG TCTCATCAAC 1320 AACTTACACC TCCAGTTTGT GACCTTTGTC CTGCACACCA TTGTTCGAGG TTTCTTCCAC 1380 TCAGCCTGTG GGAGTCTCTA TGCTGCAGTG TTCCCATCCA ACCACTTTGG GACGCTGACA 1440 GGCCTGCAGT CCCTCATCAG TGCTGTGTTC GCCTTGCTTC AGCAGCCACT TTTCATGGCG 1500 ATGGTGGGAC CCCTGAAAGG AGAGCCCTTC TGGGTGAATC TGGGCCTCCT GCTATTCTCA 1560 CTCCTGGGAT TCCTGTTGCC TTCCTACCTC TTCTATTACC GTGCCCGGCT CCAGCAGGAG 1620 TACGCCGCCA ATGGGATGGG CCCACTGAAG GTGCTTAGCG GCTCTGAGGT GACCGCA 1677 (2) INFORMATION FOR SEQ ID NO: 47: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 990 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10304 (i) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 47: ATGGAGGGCG CTCCACCGGG GTCGCTCGCC CTCCGGCTCC TGCTGTTCGT GGCGCTACCC 60 GCCTCCGGCT GGCTGACGAC GGGCGCCCCC GAGCCGCCGC CGCTGTCCGG AGCCCCACAG 120 GACGGCATCA GAATTAATGT AACTACACTG AAAGATGATG GGGACATATC TAAACAGCAG 180 GTTGTTCTTA ACATAACCTA TGAGAGTGGA CAGGTGTATG TAAATGACTT ACCTGTAAAT 240 AGTGGTGTAA CCCGAATAAG CTGTCAGACT TTGATAGTGA AGAATGAAAA TCTTGAAAAT 300 TTGGAGGAAA AAGAATATTT TGGAATTGTC AGTGTAAGGA TTTTAGTTCA TGAGTGGCCT 360 ATGACATCTG GTTCCAGTTT GCAACTAATT GTCATTCAAG AAGAGGTAGT AGAGATTGAT 420 GGAAAACAAG TTCAGCAAAA GGATGTCACT GAAATTGATA TTTTAGTTAA GAACCGGGGA 480 GTACTCAGAC ATTCAAACTA TACCCTCCCT TTGGAAGAAA GCATGCTCTA CTCTATTTCT 540 CGAGACAGTG ACATTTTATT TACCCTTCCT AACCTCTCCA AAAAAGAAAG TGTTAGTTCA 600 CTGCAAACCA CTAGCCAGTA TCTTATCAGG AATGTGGAAA CCACTGTAGA TGAAGATGTT 660 TTACCTGGCA AGTTACCTGA AACTCCTCTC AGAGCAGAGC CGCCATCTTC ATATAAGGTA 720 ATGTGTCAGT GGATGGAAAA GTTTAGAAAA GATCTGTGTA GGTTCTGGAG CAACGTTTTC 780 CCAGTATTCT TTCAGTTTTT GAACATCATG GTGGTTGGAA TTACAGGAGC AGCTGTGGTA 840 ATAACCATCT. TAAAGGTGTT TTTCCCAGTT TCTGAATACA AAGGAATTCT TCAGTTGGAT 900 AAAGTGGACG TCATACCTGT GACAGCTATC AACTTATATC CAGATGGTCC AGAGAAAAGA 960 GCTGAAAACC TTGAAGATAA AACATGTATT 990 (2) INFORMATION FOR SEQ ID NO: 48: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 324 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10305, (xi) ) SEQUENCE DESCRIPTION: SEQ ID NO: 48: ATGAGTCTGA CTTCCAGTTC CAGCGTACGA GTTGAATGGA TCGCAGCAGT TACCATTGCT 60 GCTGGGACAG CTGCAATTGG TTATCTAGCT TACAAAAGAT TTTATGTTAA AGATCATCGA 120 AATAAAGCTA TGATAAACCT TCACATCCAG AAAGACAACC CCAAGATAGT ACATGCTTTT 180 GACATGGAGG ATTTGGGAGA TAAAGCTGTG TACTGCCGTT GTTGGAGGTC CAAAAAGTTC 240 CCATTCTGTG ATGGGGCTCA CACAAAACAT AACGAAGAGA CTGGAGACAA TGTGGGCCCT 300 CTGATCATCA AGAAAAAAGA AACT 324 (2) INFORMATION FOR SEQ ID NO: 49: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 303 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10306 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 49: ATGAACCTGG AGCGAGTGTC CAATGAGGAG AAATTGAACC TGTGCCGGAA GTACTACCTG 60 GGGGGGTTTG CTTTCCTGCC TTTTCTCTGG TTGGTCAACA TCTTCTGGTT CTTCCGAGAG 120 GCCTTCCTTG TCCCAGCCTA CACAGAACAG AGCCAAATCA AAGGCTATGT CTGGCGCTCA 180 GCTGTGGGCT TCCTCTTCTG GGTGATAGTG CTCACCTCCT GGATCACCAT CTTCCAGATC 240 TACCGGCCCC GCTGGGGTGC CCTTGGGGAC TACCTCTCCT TCACCATACC CCTGGGCACC 300 CCC 303 (2) INFORMATION FOR SEQ ID NO: 50: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1116 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: ADNo for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10328 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 50: ATGAAGTATC TCCGGCACCG GCGGCCCAAT GCCACCCTCA TTCTGGCCAT CGGCGCTTTC 60 ACCCTCCTCC TCTTCAGTCT GCTAGTGTCA CCACCCACCT GCAAGGTCCA GGAGCAGCCA 120 CCGGCGATCC CCGAGGCCCT GGCCTGGCCC ACTCCACCCA CCCGCCCAGC CCCGGCCCCG 180 TGCCATGCCA ACACCTCTAT GGTCACCCAC CCGGACTTCG CCACGCAGCC GCAGCACGTT 240 CAGAACTTCC TCCTGTACAG ACACTGCCGC CACTTTCCCC TGCTGCAGGA CGTGCCCCCC 300 TCTAAGTGCG CGCAGCCGGT CTTCCTGCTG CTGGTGATCA AGTCCTCCCC TAGCAACTAT 360 GTGCGCCGCG AGCTGCTGCG GCGCACGTGG GGCCGCGAGC GCAAGGTACG GGGTTTGCAG 420 CTGCGCCTCC TCTTCCTGGT GGGCACAGCC TCCAACCCGC ACGAGGCCCG CAAGGTCAAC 480 CGGCTGCTGG AGCTGGAGGC ACAGACTCAC GGAGACATCC TGCAGTGGGA CTTCCACGAC 540 TCCTTCTTCA ACCTCACGCT CAAGCAGGTC CTGTTCTTAC AGTGGCAGGA GACAAGGTGC 600 GCCAACGCCA GCTTCGTGCT CAACGGGGAT GATGACGTCT TTGCACACAC AGACAACATG 660 GTCTTCTACC TGCAGGACCA TGACCCTGGC CGCCACCTCT TCGTGGGGCA ACTGATCCAA 720 AACGTGGGCC CCATCCGGGC TTTTTGGAGC AAGTACTATG TGCCAGAGGT GGTGACTCAG 780 AATGAGCGGT ACCCACCCTA TTGTGGGGGT GGTGGCTTCT TGCTGTCCCG CTTCACGGCC 840 GCTGCCCTGC GCCGTGCTGC CCATGTCTTG GACATCTTCC CCATTGATGA TGTCTTCCTG 900 GGTATGTGTC TGGAGCTTGA GGGACTGAAG CCTGCCTCCC ACAGCGGCAT CCGCACGTCT 960 GGCGTGCGGG CTCCATCGCA ACACCTGTCC TCCTTTGACC CCTGCTTCTA CCGAGACCTG 1020 CTGCTGGTGC ACCGCTTCCT ACCTTATGAG ATGCTGCTCA TGTGGGATGC GCTGAACCAG 1080 CCCAACCTCA CCTGCGGCAA TCAGACACAG ATCTAC 1116 (2) INFORMATION FOR SEQ ID NO: 51: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 986 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (Vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1Q80 (D) CLONE NAME: HP10442 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 82 .. 699 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 51: AGACTGCGGG ACGGACGGTG GACGCTGGGA CGCGTTTGTA GCTCCGGCCC CGCCGTTCCG 60 ACCCCCGCCG CCGTCGCCGC C ATG ACG GGG CTA GCA CTG CTC TAC TCC GGG 111 t Met Thr Gly Leu Wing Leu Leu Tyr Ser Gly 1 5 10 GTC TTC GTG GCC TTC TGG GCC TGC GCG CTG GCC GTG GGA GTC TGC TAC 159 Val Pha Val Wing Phe Trp Ala Cys Ala Leu Ala Val Gly Val Cys Tyr 15 20 25 ACC ATT TTT GAT TTG GGC TTC CGC TTT GAT GTG GCA TGG TTC CTG ACG 207 Thr He Phe Asp Leu Gly Phe Arg Phe Asp Val Wing Trp Phe Leu Thr 30 35 40 GAG ACT TCG CCC TTC ATG TGG TCC AAC CTG GGC ATT GGC CTA GCT ATC 255 Glu Thr Ser Pro Phe Met Trp Ser Asn Leu Gly Ha Gly Leu Wing He 45 50 55 TCC CTG TCT GTG GTT GGG GCA GCC TGG GGC ATC TAT ATT ACC GGC TCC 303 Ser Leu Ser Val Val Gly Wing Wing Trp Gly He Tyr He Thr Gly Ser 60 65 70 TCC ATC ATT GGT GGA GGA GTG AAG GCC CCC AGG ATC AAG ACC AAG AAC 351 Be He He Gly Gly Gly Val Lys Pro Wing Arg He Lys Thr Lys Asn 75 80 85 90 CTG GTC AGC ATC ATC TTC TGT GAG GCT GTG GCC ATC TAC GGC ATC ATC 399 Leu Val Ser He He Phe Cys Glu Ala Val Wing He Tyr Gly He He 95 100 105 ATG GCA ATT GTC ATT AGC AAC ATG GCT GAC CCT TTC AGT GCC ACA GAC 447 Met Wing He Val He Ser Asn Met Wing Glu Pro Phe Ser Wing Thr Asp 110 115 120 CCC AAG GCC ATC GGC CAT CGG AAC TAC CAT GCA GGC TAC TCC ATG TTT 495 Pro Lys Wing He Gly His Arg Asn Tyr His Wing Gly Tyr Ser Met Phe 125 130 135 GGG GCT GGC CTC ACC GTA GGC CTG TCT AAC CTC TTC TGT GGA GTC TGC 543 Gly Wing Gly Leu Thr Val Gly Leu Ser Asn Leu Phe Cys Gly Val Cys 140 145 150 GTG GGC ATC GTG GGC AGT GGG GCT GCC CTG GCC GAT GCT CAG AAC CCC 591 Val Gly He Val Gly Ser Gly Ala Ala Leu Ala Asp Ala Gln Asn Pro 155 160 165 170 AGC CTC TTT GTA AAG ATT CTC ATC GTG GAG ATC TTT GGC AGC GCC ATT 639 Ser Leu Phe Val Lys He Leu He Val Glu He Phe Gly Ser Wing He 175 180 185 GGC CTC TTT GGG GTC ATC GTC GCA ATT CTT CAG ACC TCC AGA GTG AAG 687 Gly Leu Phe Gly Val He Val Wing He Leu Gln Thr Ser Arg V to Lys 190 195 200 GGT ATG GAC TAGATGATAT GTGTGGGTGG GGCCGTGCCT Met Gly Asp CACT 730 205 TTTATTTATT GCTGGTTTTC CTGGGACAGC TGGAGCTGTG TCCCTTAGCC TTTCAGAGGC 790 TTGGTGTTCA GGGCCCTCCC TGCACTCCCC TCTTGCTGCG TGTTGATTTG GAGGCACTGC 850 AGTCCAGGCC GAGTCCTCAG TGCGGGGAGC AGGCTGCTGC TGCTGACTCT GTGCAGCTGC 910 GCACCTGTGT CCCCCACCTC CACCCTCAAC CCATCTTCCT AGTGTTTGTG AAATAAACTT 970 986 GGTATTTGTC TGGGTC (2) INFORMATION FOR SEQ ID NO: 52: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1824 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Leukocyte (D) CLONE NAME: HP00804 (ix) SEQUENCE CHARACTERISTICS: (A) CODE OF CHARACTERIZATION: CDS (B) EXISTENCE POSITION: 133 .. 1248 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 52: GGCCCAGCTG AGCGGCCGCC GAGCGGGTGC GGGTGCGGGC GCATCGGCCA TCACCGCGCG 60 GCCGCGCAGC GGACACCGTG CGTACCGGCC TGCGGCGCCC GGCCACCGGG GCGGACCGCG 120 GAACCCGAGG CC ATG TCC CAT GAA AAG AGT TTT TTG GTG TCT GGG GAC AAC 171 Met Ser His Glu Lys Ser Phe Leu Val Ser Gly Asp Asn 1 5 10 TAT CCT CCC CCC AAC CCT GGA TAT CCG GGG GGG CCC CAG CCA CCC ATG 219 Tyr Pro Pro Pro Asn Pro Gly Tyr Pro Gly Gly Pro Gln Pro Pro Met 15 20 25 CCC CCC TAT GCT CAG CCT CCC TAC CCT GGG GCC CCT TAC CAC GAG CCC 267 Pro Pro Tyr Wing Gln Pro Pro Tyr Pro Gly Wing Pro Tyr Pro Gln Pro 30 35 40 45 CCT TTC CAG CCC TCC CCC TAC GGT CAG CCA GGG TAC CCC CAT GGC CCC 315 Pro Phe Gln Pro Ser Pro Tyr Gly Gln Pro Gly Tyr Pro His Gly Pro 50 55 60 AGC CCC TAC CCC CAA GGG GGC TAC CAC CAG GGT CCC TAC CCC CAA GGG 363 Ser Pro Tyr Pro Gln Gly Tyr Pro Gln Gly Pro Tyr Pro Gln Gly 65 70 75 GGC TAC CCA CAG GGC CCC TAC CCA CAA GAG GGC TAC CCA CAG GGC CCC 411 Gly Tyr Pro Gln Gly Pro Tyr Pro Gln Glu Gly Tyr Pro Gln Gly Pro 80 85 90 TAC CCC CAA GGG GGC TAC CCC CAG GGG CCA TAT CCC CAG AGC CCC TTC 459 Tyr Pro Glu Gly Gly Tyr Pro Gln Gly Pro Tyr Pro Gln Ser Pro Phe 95 100 105 CCC CCC AAC CCC TAT GGA CAG CCA CAG GTC TTC CCA GGA CAA GAC CCT 507 Pro Pro Asn Pro Tyr Gly Gln Pro Gln Va Phe Pro Gly Gln Asp Pro 110 115" "120 125 GAC TCA CCC CAG CAT GGA AAC TAC CAG GAG GGT CCC CCA TCC TAC 555 Asp Ser Pro Gln His Gly Asn Tyr Gln Glu Glu Gly Pro Pro Ser Tyr 130 135 140 TAT GAC AAC CAG GAC TTC CCT GCC ACC AAC TGG GAT GAC AAG AGC ATC 603 Tyr Asp Asn Gln Asp Phe Pro Wing Thr Asn Trp Asp Asp Lys Ser He .145 150 155 CGA CAG GCC TTC ATC CGC AAG GTG TTC CTA GTG CTG ACC TTG CAG CTG 651 Arg Gln Wing Phe He Arg Lys Val Phe Leu Val Leu Thr Lau Gln Leu 160 165 170 TCG GTG ACC CTG TCC ACG GTG TCT GTG TTC ACT TTT GTT GCG GTG 699 Ser Val Thr Leu Ser Thr Val Ser Val Phe Thr Phe Val Ala Glu Val 175 180 185 AAG GGC TTT GTC CGG GAG AAT GTC TGG ACC TAC TAT GTC TCC TAT GCT 747 Lys Gly Phe Val Arg Glu Asn Val Trp Thr Tyr Tyr Val Ser Tyr Wing 190 195 200 205 GTC TTC TTC ATC TCT CTC ATC GTC CTC AGC TGT TGT GGG GAC TTC CGG 795 Val Phe Phe He Ser Leu He Val Leu Ser Cys Cys Gly Asp Phe Arg 210 215 220 CGA AAG CAC CCC TGG AAC CTT GTT GCA CTG TCG GTC CTG ACC GCC AGC 843 Arg Lys His Pro Trp Asn Leu Val Ala Leu Ser Val Leu Thr Wing Ser 225 230 235 CTG TCG TAC ATG GTG GGG ATG ATC GCC AGC TTC TAC AAC ACC GAG GCA 891 Leu Ser Tyr Met Val Gly Mat Has Wing Ser Phe Tyr Asn Thr Glu Wing 240 245 250 GTC ATC ATG GCC GTG GGC ATC ACC ACA GCC GTC TGC TTC ACC GTC GTC 939 Val He Mßt Wing Val Gly He Thr Thr Wing Val Cys Phe Thr Val Val 255 260 265 ATC TTC TCC ATG CAG ACC CGC TAC GAC TTC ACC TCA TGC ATG GGC GTG 987 He Phe Ser Mat Gln Thr Arg Tyr Asp Phe Thr Ser Cys Met Gly Val 270 275 280 285 CTC CTG GTG AGC ATG GTG GTG CTC TTC ATC TTC GCC ATT CTC TGC ATC 1035 Leu Leu Val Ser Met Val Val Leu Phe He Pha Wing He Leu Cys Ha 290 295 300 TTC ATC CGG AAC CGC ATC CTG GAG ATC GTG TAC GCC TCA CTG GGC GCT 1083 Phe He Arg Asn Arg He Leu Glu He Val Tyr Ala Ser Leu Gly Wing 305 310 315 CTG CTC TTC ACC TGC TTC CTC GCA GTG GAC ACC CAG CTG CTG CTG GGG 1131 Leu Leu Phe Thr Cys Phß Leu Ala Val Asp Thr Gln Leu Leu Leu Gly 320 325 330 AAC AAG CAG CTG TCC CTG AGC CCA GAA GAG TAT GTG TTT GCT GCG CTG 1179 Asn Lys Gln Leu Ser Leu Ser Pro Glu Glu Tyr Val Phe Ala Ala Leu 335 340 345 AAC CTG TAC ACÁ GAC ATC ATC AAC ATC TTC CTG TAC ATC CTC ACC ATC 1227 Asn Leu Tyr Thr Asp He He Asn He Pha Leu Tyr He Leu Thr He 350 355 360 365 ATT GGC CGC GCC AAG GAG TAGCCGAGCT CCAGCTCGCT GTGCC 1270 He Gly Arg Wing Lys Glu 370 CGCTCAGGTG GCACGGCTGG CCTGGACCCT GCCCCTGGCA CGGCAGTGCC AGCTGTACTT 1330TTGTCCCCAG GCACAGCCTA GGGAAAAGGA TGCCTCTCTC CAACCCTCCT 1390 GTATGTACAC TGCAGATACT TCCATTTGGA CCCGCTGTGG CCACAGCATG GCCCCTTTAG_1450_TCCTCCCGCC C.CCGCCAAGG GGCACCAAGG CCACGTTTCC GTGCCACCTC CTGTCTACTC 1510 ATTGTTGCAT GAGCCCTGTC TGCCAGCCCA CCCCAGGGAC TGGGGGCAGC ACCAGGTCCC 1570 GGGGAGAGGG ATTGAGCCAA GAGGTGAGGG TGCACGTCTT CCCTCCTGTC CCAGCTCCCC 1630 AGCCTGGCGT AGAGCACCCC TCCCCTCCCC CCCACCCCCC TGGAGTGCTG CCCTCTGGGG 1690 ACATGCGGAG TGGGGGTCTT ATCCCTGTGC TGAGCCCTGA GGGCAGAGAG GATGGCATGT 1750 TTCAGGGGAG GGGGAAGCCT TCCTCTCAAT TTGTTGTCAG TGAAATTCCA ATAAATGGGA 1810 TTTGCTCTCT GCCT 1824 (2) INFORMATION FOR SEQ ID NO: 53: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1076 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP01098 (ix) SEQUENCE CHARACTERISTICS: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 62 .. 601 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 53: AGTTCCGCCC GCTGGTCATC GCGCCCTTTC CCCTGCCGGT GTCCTGCTCG CCGTCCCCGC 60 C ATG CTG TCT CTA GAC TTT TTG GAC GAT GTG CGG CGG ATG AAC AAG CGG 109 Met Leu Ser Leu Asp Phe Leu Asp Asp Val Arg Arg Met Asn Lys Arg 1 5 10 15 CAG CTC TAT TAT CAA GTC CTA AAT TTT GGA ATG ATT GTC TCA TCG GCA 157 Gln Leu Tyr Tyr Gln Val Leu Asn Phe Gly Met He Val Ser Be Ala? 20 25 30 CTA ATG ATG TGG AAG GGG TTA ATG GTA ATA ACT GGA AGT GAA AGT CCG 205 Lau Mßt He Trp Lys Gly Leu Met Val He Thr Gly Ser Glu Ser Pro 35 40 45 ATT GTA GTG GTG CTC AGT GGC AGC ATG GAA CCT GCA TTT CAT AGA GGA 253 He Val Val Leu Ser Gly Ser Met Glu Pro Wing Phe His Arg Gly 50 55 60 GAT CTT CTC TTT CTA ACA AAT CGA GTT GAA GAT CCC ATA CGA GTG GGA 301 Asp Leu Leu Phs Leu Thr Asn Arg Val Glu Asp Pro He Arg Val Gly 65 70 75 80 GAA ATT GTT GTT TTT AGG ATA GAA GGA AGA GAG ATT CCT ATA GTT CAC 349 Glu He Val Val Phe Arg He Glu Gly Arg Glu He Pro He Val His 85 90 95 CGA GTC TTG AAG ATT CAT GAA AAG CAA AAT GGG CAT ATC AAG TTT TTG 397 Arg Val Leu Lys He His Glu Lys Gln Asn Gly His Ha Lys Phe Leu, 100 105 110 ACC AAA GGA GAT AAT AAT GCG GTT GAT GAC CGA GGC CTC TAT AAA CAA 445 Thr Lys Gly Asp Asn Asn Wing Val Asp Asp Arg Gly Leu Tyr Lys Gln 115 120 125 GGA CAA CAT TGG CTA GAG AAA AAA GAT GTT GTG GGG AGA GCC AGG GGA 493 Gly Gln His Trp Leu Glu Lys Lys Asp Val Val Gly Arg Ala Arg Gly 130 135 140 TTT GTT CCT TAT ATT GGA ATT GTG ACG ATC CTC ATG AAT GAC TAT CCT 541 Phe Val Pro Tyr He Gly He Val Thr He Leu Met Asn Asp Tyr Pro 145 150 155 160 AAA TTT AAG TAT GCA GTT CTC TTT TTG CTG GGT TTA TTC GTG CTG GTT 589 Lys Phe Lys Tyr Wing Val Leu Phe Leu Leu Gly Leu Phe Val Leu Val 165 170 175 CAT CGT GAG TA AGAAGCC TGCCTTGCTG TTCCTGGGAA GAT 630 His Arg Glu GCCATAGTTT TCGTTACTGG ATGTTTGGAG TAGATACTGG TCTGTGATTG GTGGAATGGA 690 GAACACACGT GTTGGTGCTT CTGGGTAGCA CTGGTTTGCA TTAGTTTATG TTTCCATGCC 750 AGAGTTTGTG TGGGCGGGCG CATGTGCACC ACAGAGTGCA CTCGAGGGGA CTTTCAGTCA 810 CAGGATTTCA TAATTGTCAT TGTCACACTT TCAAATTTTT GTACATCAGT GAATTTTTTT 870 ATATTAAAAG GTTGAGCCAA AGCCCCCAGT GTTTGTATTT TGAAGCCAAG CTTCACTTCT 930 AAAGTGCCTA CAGAGACTTG TAAATGAAAA TGCAGCTCTG CACGAGTTTG AAACCGTCAT 990 ACCTCCTTCT ATTAGGAATG GCATATACTG AGGTGGTCGT AAGTCTTAAC TTCTAAAATT 1050 TTAAATAAAA GACTTTGCAC ATTGAG 1076 (2) INFORMATION FOR SEQ ID NO: 54: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1591 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP01148 (ix) SEQUENCE CHARACTERISTICS: (A) CODE OF CHARACTERIZATION: CDS (B) EXISTENCE POSITION: 102 .. 1145 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 54: GTCCCTCCTC TTAACATACT TGCAGCTAAA ACTAAATATT GCTGCTTGGG GACCTCCTTC 60 TAGCCTTAAA TTTCAGCTCA TCACCTTCAC CTGCCTTGGT C ATG GCT CTG CTA TTC 116 Met Ala Leu Leu Phe 1 5 TCC TTG ATC CTT GCC ATT TGC ACC AGA CCT GGA TTC CTA GCG TCT CCA 164 Ser Leu Ha Leu Ala He Cys Thr Arg Pro Gly Phe Lau Ala Ser Pro 10 15 20 TCT GGA GTG CGG CTG GTG GGG GGC CTC CAC CGC TGT GAA GGG CGG GTG 212 Ser Gly Val Arg Leu Val Gly Gly Leu His Arg Cys Glu Gly Arg Val 25 30 35 GAG GTG GAA CAG AAA GGC CAG TGG GGC ACC GTG TGT GAT GAC GGC TGG 260 Glu Val Glu Gln Lys Gly Gln Trp Gly Thr Val Cys Asp Asp Gly Trp 40 45 50 GAC ATT AAG GAC GTG GCT GTG TTG TGC CGG GAG CTG GGC TGT GGA GCT 308 Asp He Lys Asp Val Ala Val Leu Cys Arg Glu Leu Gly Cly Gly Wing 55 60 65 GCC AGC GGA ACC CCT AGT GGT ATT TTG TAT GAG CCA CCA GCA GAA AAA 356 Wing Being Gly Thr Pro Being Gly He Leu Tyr Glu Pro Pro Wing Glu Lys 70 75 80 85 GAG CAA AAG GTC CTC ATC CAA TCA GTC AGT TGC ACÁ GGA ACÁ GAA GAT 404 Glu Gln Lys Val Leu He Gln Ser Val Ser Cys Thr Gly Thr Glu Asp 90 95 100 ACÁ TTG GCT CAG TGT GAG CAA GAA GAA GTT TAT GAT TGT TCA CAT GAA 452 Thr Leu Wing Gln Cys Glu Gln Glu Glu Val Tyr Asp Cys Ser His Glu 105 110 115 GAA GAT GCT GGG GCA TCG TGT GAG AAC CCA GAG AGC TCT TTC TCC CCA 500 Glu Asp Wing Gly Wing Ser Cys Glu Asn Pro Glu Ser Ser Phe Sar Pro 120 125 130 GTC CCA GAG GGT GTC AGG CTG GCT GAC GGC CCT GGG CAT TGC AAG GGA 548 Val Pro Glu Gly Val Arg Leu Wing Asp Gly Pro Gly His Cys Lys Gly 135 140 145 CGC GTG GAA GTG AAG CAC CAG AAC CAG TGG TAT ACC GTG TGC CAG ACA 596 Arg Val Glu Val Lys His Gln Asn Gln Trp Tyr Thr Val Cys Gln Thr 150 155 160 165 GGC TGG AGC CTC CGG GCC GCA AAG GTG GTG TGC CGG CAG CTG GGA TGT 644 Gly Trp Ser Leu Arg Ala Ala Lys Val Val Cys Arg Gln Leu Gly Cys 170 175 180 GGG AGG GCT GTA CTG ACT CAA AAA CGC TGC AAC AAG CAT GCC TAT GGC 692 Gly Arg Wing Val Leu Thr Gln Lys Arg Cys Asn Lys His Wing Tyr Gly 185 190 195 CGA AAA CCC ATC TGG CTG AGC CAG ATG TCA TGC TCA GGA CGA GAA GCA 740 Arg Lys Pro He Trp Leu Ser Gln Met Ser Cys Ser Gly Arg Glu Wing 200 205 210 ACC CTT CAG GAT TGC CCT TCT GGG CCT TGG GGG AAG AAC ACC TGC AAC 788 Thr Leu Gln Asp Cys Pro Ser Gly Pro Trp Gly Lys Asn Thr Cys Asn 215 220 225 CAT GAT GAA GAC ACG TGG GTC GAA TGT GAA GAT CCC TTT GAC TTG AGA 836 His Asp Glu Asp Thr Trp Val Glu Cys Glu Asp Pro Phe Asp Leu Arg 230 235 240 245 CTA GTA GGA GAC AAC CTC TGC TCT GGG CGA CTG GAG GTG CTG CAC 884 Leu Val Gly Gly Asp Asn Leu Cys Ser Gly Arg Leu Glu Val Leu His 250 255 260 AAG GGC GTA TGG GGC TCT GTC TGT GAT GAC AAC TGG GGA GAA AAG GAG 932 Lys Gly Val Trp Gly Ser Val Cys Asp Asp Asn Trp Gly Glu Lys Glu 265 270 275 GAC CAG GTG GTA TGC AAG CAA CTG GGC TGT GGG AAG TCC CTC TCT CCC 980 Asp Gln Val Val Cys Lys Gln Leu Gly Cys Gly Lys Ser Leu Ser Pro 280 285 290 TCC TTC AGA GAC CGG AAA TGC TAT GGC CCT GGG GTT GGC CGC ATC TGG 1028 Ser Phe Arg Asp Arg Lys Cys Tyr Gly Pro Gly Val Gly Arg He Trp 295 300 305 CTG GAT AAT GTT CGT TGC TCA GGG GAG GAG CAG TCC CTG GAG CAG TGC 1076 Leu Asp Asn Val Arg Cys Ser Gly Glu Glu Gln Ser Leu Glu Gln Cys 310 315 320 325 CAG CAC AGA TTT TGG GGG TTT CAC GAC TGC ACC CAC CAG GAA GAT GTG 1124 Gln His Arg Phe Trp Gly Phe His Asp Cys Thr His Gln Glu Asp Val 330 335 340 GCT GTC ATC TGC TCA GGA TAGTATCCTG GTGTTGCTTG ACCTGGCC 1170 Wing Val He Cys Ser Gly 345 CCCCTGGCCC CGCCTGCCCT CTGCTTGTTC TCCTGAGCCC TGATTATCCT CATACTCATT 1230 CTGGGGCTCA GGCTTGAGCC ACTACTCCCT CATCCCCTCA GGAGTCTGAA CACTGGGCTT 1290 ATGCCTTACT CTCAGGGACA AGCAGCCCCC ATTGCTGCCT GTAGATGTGA GCTGTTGAGT 1350 TCCCTCTTGC TGGGGAAGAT GAGCTTCCAT GTATCCTGTG CTCAACCCTG ACCCTTTGAC 1410 ACTGGTTCTG GCCTTTCCTG CCTTTTCTCA AGCTGCCTGG AATCCTCAAA CCTGTCACTT 1470 TGGTCAGATG TGCAGACCAT TACTAAGGTC TATGTCTGCA AACATTACTA ATCTAGGTCC 1530 TATTACTAAT CTATGTCTGC AAACATTAAA GGAATGAAAC AATGAAAGGA ACATTTGAAA 1590 G 1591 (2) INFORMATION FOR SEQ ID NO: 55: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1888 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: linked (D) CLONE NAME: HP01293 (ix) SEQUENCE CHARACTERISTICS: (A) CODE CHARACTERIZATION: CDS (B) EXISTENCE POSITION: 90 .. 1754 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 55: CCTTTTTCAAA GATCTCTGAG GGAGACATTG CACCTGGCCA CTGCAGCCCA GAGCAGGTCT 60 GGCCACGGCC ATGAGCATGC TGAGCCATC ATG CCC ACC GTG GAT GAC ATT CTG 113 Met Pro Thr Val Asp Asp He Leu 1 May GAG CAG GTT GGG GAG TCT GGC TGG TTC CAG AAG CAA GCC TTC CTC ATC 161 Glu Gln Val Gly Glu Ser Gly Trp Phe Gln Lys Gln Ala Phß Leu He 10 15 20 TTA TGC CTG CTG TCG GCT GCC TTT GCG CCC ATC TGT GTG GGC ATC GTC 209 Leu Cys Leu Lau Be Ala Wing Phe Wing Pro He Cys Val Gly He Val 25 30 35 40 TTC CTG GGT TTC ACÁ CCT GAC CAC CAC TGC CAG AGT CCT GGG GTG GCT 257 Phe Leu Gly Phe Thr Pro Asp His His Cys Gln Ser Pro Gly Val Wing 45 50 55 GAG CTG AGC CAG CGC TGT GGC TGG AGC CCT GCG GAG GAG CTG AAC TAT 305 Glu Leu Ser Gln Arg Cys Gly Trp Ser Pro Ala Glu Glu Leu Asn Tyr 60 65 70 ACA GTG CCA GGC CTG GGG CCC GCG GGC GAG GCC TTC CTT GGC CAG TGC 353 Thr Val Pro Gly Leu Gly Pro Ala Gly Glu Ala Phe Leu Gly Gln Cys 75 80 85 AGG CGC TAT GAA GTG GAC TGG AAC CAG AGC GCC CTC AGC TGT GTA GAC 401 Arg Arg Tyr Glu Val Asp Trp Asn Gln Ser Wing Leu Ser Cys Val Asp 90 95 100 CCC CTG GCT AGC CTG GCC ACC AAC A GG AGC CAC CTG CCG CTG GGT CCC 449 Pro Leu Wing Ser Leu Wing Thr Asn Arg Ser His Leu Pro Leu Gly Pro 105 110 115 120 TGC CAG GAT GGC TGG GTG TAT GAC ACG CCC GGC TCT TCC ATC GTC ACT 497 Cys Gln Asp Gly Trp Val Tyr Asp Thr Pro Gly Ser Ser He Val Thr 125 130 135 GAG TTC AAC CTG GTG TGT GCT GAC TCC TGG AAG CTG GAC CTC TTT CAG 545 Glu Phe Asn Leu Val Cys Wing Asp Ser Trp Lys Leu Asp Leu Phe Gln 140 145 150 TCC TGT TTG AAT GCG GGC TTC TTC TTT GGC TCT CTC GGT GTT GGC TAC 593 Ser Cys Lau Asn Ala Gly Phe Phe Phe Gly Ser Leu Gly Val Gly Tyr 155 160 165 TTT GCA GAC AGG TTT GGC CGT AAG CTG TGT CTC CTG GGA ACT GTG CTG 641 Phe Wing Asp Arg Phe Gly Arg Lys Leu Cys Leu Leu Gly Thr Val Leu 170 175 180 GTC AAC GCG GTG TCG GGC GTG CTC ATG GCC TTC TCG CCC AAC TAC ATG 689 Val Asn Wing Val Sar Gly Val Leu Met Wing Pha Ser Pro Asn Tyr Met 185 185 195 200 TCC ATG CTG CTC TTC CGC CTG CTG CAG GGC CTG GTC AGC AAG GGC AAC 737 Ser Met Leu Leu Phe Arg Leu Leu Gln Gly Leu Val Ser Lys Gly Asn 205 210 215 TGG AT G GCT GGC TAC ACC CTA ATC ACA GAA TTT GTT CGC TCG GGC TCC 785 Trp Met Ala Gly Tyr Thr Leu He Thr Glu Phe Val Gly Ser Gly Ser 220 225 230 AGA AGA ACG GTG GCG ATC ATG TAC CAG ATG GCC TTC ACG GTG GGG CTG 833 Arg Arg Thr Val Wing He Met Tyr Gln Met Wing Ph Ph Thr Val Gly Leu 235. 240 245 GTG GCG CTT ACC GGG CTG GCC TAC GCC CTG CCT CAC TGG CGC TGG CTG 881 Val Ala Leu Thr Gly Leu Ala Tyr Ala Leu Pro His Trp Arg Trp Leu 250 255 260 CAG CTG GCA GTC TCC CTG CCC ACC TTC CTC TTC CTG CTC TAC TAC TGG 929 Gln Leu Wing Val Ser Leu Pro Thr Phe Leu Phe Leu Leu Tyr Tyr Trp 265 270 275 280 TGT GTG CCG GAG TCC CCT CGG TGG CTG TTA TCA CAA AAA AGA AAC ACT 977 Cys Val Pro Glu Ser Pro Arg Trp Leu Leu Ser Gln Lys Arg Asn Thr 285 290 295 GAA GCA ATA AAG ATA ATG GAC CAC ATC GCT CAA AAG AAT GGG AAG TTG 1025 Glu Wing He Lys He Met Asp His He Wing Gln Lys Asn Gly Lys Leu 300 305 310 CCT CCT GCT GAT TTA AAG ATG CTT TCC CTC GAA GAG GAT GTC ACC GAA 1073 Pro Pro Wing Asp Leu Lys Met Leu Ser Leu Glu Glu Asp Val Thr Glu 315 320 325 AAG CTG AGC CCT TCA TTT GCA GAC CTG TTC CGC ACG CCG CGC CTG AGG 1121 Lys Leu Ser Pro Ser Phe Wing Asp Leu Phe Arg Thr Pro Arg Leu Arg 330 335 340 AAG CGC ACC TTC ATC CTG ATG TAC CTG TGG TTC ACG GAC TCT GTG CTC 1169 Lys Arg Thr Phe He Leu Met Tyr Leu Trp Phe Thr Asp Ser Val Leu 345 350 355 360 TAT CAG GGG CTC ATC CTG CAC ATG GGC GCC ACC AGC GGG AAC CTC TAC 1217 Tyr Gln Gly Leu He Leu His Met Gly Ala Thr Ser Gly Asn Leu Tyr 365 370 375 CTG GAT TTC CTT TAC TCC GCT CTG GTC GAA ATC CCG GGG GCC TTC ATA 1265 Leu Asp Phe Leu Tyr Ser Ala Leu Val Glu He Pro Gly Ala Phe He 380 385 390 GCC CTC ATC ACC ATT GAC CGC GTG GGC GCC ATC TAC CCC ATG GCC GTG 1313 Ala Leu lia Thr He Asp Arg Val Gly Arg lia Tyr Pro MSST Ala Val 395 400 405 TCA AAT TTG TTG GCG GGG GCA GCC TGC CTC GTC ATG ATT TTT ATC TCA 1361 Ser Asn Leu Leu Wing Wing Wing Wing Cys Leu Val Met He Phe He Ser 410 415 420 CCT GAC CTG CAC TGG TTA AAC ATC ATA ATC ATG TGT GTG GGC CGA ATG 1409 Pro Asp Leu His Trp Leu Asn Ha He He Met Cys Val Gly Arg Met 425 430 435 440 GGA ATC ACC ATT GCA ATA CAA ATG ATC TGC CTG GTG AAT GCT CTG 1457 Gly He Thr He Wing He Gln Met He Cys Leu Val Asn Wing Glu Leu 445 450 455 TAC CCC ACÁ TTC GTC AGG AAC CTC GGA GTG ATG GTG TGT TCC TCC CTG 1505 Tyr Pro Thr Phe Val Arg Asn Leu Gly Val Met Val Cys Ser Ser Leu 460 465 470 TGT GAC ATA GGT GGG ATA ATC ACC CCC TTC ATA GTC TTC AGG CTG AGG 1553 Cys Asp He Gly Gly He He Thr Pro Phe He Val Phe Arg Leu Arg 475 480 485 GAG GTC TGG CAA GCC TTG CCC CTC ATT TTG TTG GCG GTG TTG GGC CTG 1601 Glu Val Trp Gln Ala Leu Pro Leu He Leu Phe Ala Val Leu Gly Leu 490, 495 500 CTT GCC GCG GGA GTG ACG CTA CTT CTT CCA GAG ACC AAG GGG GTC GCT 1649 Leu Ala Wing Gly Val Thr Leu Leu Pro Glu Thr Lys Gly Val Wing 505 510 515 520 TTG CCA GAG ACC ATG AAG GAC GCC GAG AAC CTT GGG AGA AAA GCA AAG 1697 Leu Pro Glu Thr Met Lys Asp Ala Glu Asn Leu Gly Arg Lys Ala Lys 525 530 535 CCC AAA GAA AAC ACG ATT TAC CTT AAG GTC CAA ACC TCA GAA CCC TCG 1745 Pro Lys Glu Asn Thr He Tyr Leu Lys Val Gln Thr Ser Glu Pro Ser 540 545 550 GGC ACC TGAGAGAGAT GTTTTGCGGC GATGTCGTGT TGGAGGGATG AAGATGGAG 1800 Gly Thr TTATCCTCTG CAGAAATTCC TAGACGCCTT CACTTCTCTG TATTCTTCCT CATACTTGCC 1860 TACCCCCAAA TTAATATCAG TCCTAAAG 1888 (2) INFORMATION FOR SEQ ID NO: 56: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 2033 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10013 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 97 .. 1149 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 56: GAGTCCGAGC GCGTCACCTC CTCACGCTGC GGCTGTCGCCCGTGTCCCGC CGGCCCGTTC 60 CGTGTCGCCC CGCAGTGCTG CGGCCGCCGC GGCACC ATG GCT GTG TTT GTC GTG 114 Met Wing Val Phe Val Val 1 5 CTC CTG GCG TTG GTG GCG GGT GTT TTG GGG AAC GAG TTT AGT ATA TTA 162 Leu Leu Ala Leu Val Ala Gly Val Leu Gly Asn Glu Phe Ser He Leu 10 15 20 AAA TCA CCA GGG TCT GTT GTT TTC CGA AAT GGA AAT TGG CCT ATA CCA 210 Lys Ser Pro Gly Ser Val Val Phe Arg Asn Gly Asn Trp Pro He Pro 25 30"35 GGA GAG CGG ATC CCA GAC GTG GCT GCA TTG TCC ATG GGC TTC TCT GTG 258 Gly Glu Arg He Pro Asp Val Wing Wing Leu Ser Mat Gly Phe Ser Val 40 45 50 AAA GAA GAC CTT TCT TGG CCA GGA CTC GCA GTG GGT AAC CTG TTT CAT 306 Lys Glu Asp Leu Ser Trp Pro Gly Leu Wing Val Gly Asn Leu Phe His 55. 60 65 70 CGT CCT CGG GCT ACC GTC ATG GTG ATG GTG AAG GGA GTG AAC AAA CTG 354 Arg Pro Arg Wing Thr Val Met Val Met Val Lys Gly Val Asn Lys Leu 75 80 85 GCT CTA CCC CCA GGC AGT GTC ATT TCG TAC CCT TTG GAG AAT GCA GTT 402 Wing Leu Pro Pro Gly Ser Val He Ser Tyr Pro Leu Glu Asn Wing Val 90 95 100 CCT TTT AGT CTT GAC AGT GTT GCA AAT TCC ATT CAC TCC TTT TCT 450 Pro Phe Ser Leu Asp Ser Val Wing Asn Ser He His Ser Leu Phe Ser 105 110 115 GAG GAA ACT CCT GTT GTT TTG CAG TTG GCT CCC AGT GAG GAA AGA GTG 498 Glu Glu Thr Pro Val Val Leu Gln Leu Pro Wing Glu Glu Arg Val 120 125 130 TAT ATG GTA GGG AAG GCA AAC TCA GTG TTT GAA GAC CTT TCA GTC ACC 546 Tyr Met Val Gly Lys Wing Asn Ser Val Phe Glu Asp Leu Ser Val Thr 135 140 145 150 TTG CGC CAG CTC CGT AAT CGC CTG TTT CAA GAA AAC TCT GTT CTC AGT 594 Leu Arg Gln Leu Arg Asn Arg Leu Phe Gln Glu Asn Ser Val Leu Ser 155 160 165 TCA CTC CCC CTC AAT TCT CTG AGT AGG AAC AAT GAA GTT GAC CTG CTC 642 Ser Leu Pro Leu Asn Ser Leu Ser Arg Asn Asn Glu Val Asp Leu Leu 170 175 180 TTT CTT TCT GAA CTG CAA GTG CTA CAT GAT ATT TCA AGC TTG CTG TCT 690 Pha Leu Ser Glu Leu Gln Val Leu His Asp He Ser Ser Leu Leu Ser 185 190 195 CGT CAT AAG CAT CTA GCC AAG GAT CAT TCT CCT GAT TTA TAT TCA CTG 738 Arg His Lys His Leu Wing Lys Asp His Ser Pro Asp Leu Tyr Ser Leu 200 205 210 GAG CTG GCA GGT TTG GAT GAA ATT GGG AAG CGT TAT GGG GAA GAC TCT 786 Glu Leu Wing Gly Leu Asp Glu He Gly Lys Arg Tyr Gly Glu Asp Ser 215 220 225 230 GAA CAA TTC AGA GAT GCT TCT AAG ATC CTT GTT GAC GCT CTG CAA AAG 834 Glu Gln Phß Arg Asp Ala Ser Lys He Leu Val Asp Ala Leu Gln Lys 235 240 245 TTT GCA GAT GAC ATG TAC AGT CTT TAT GGT GGG AAT GCA GTG GTA GAG 882 Phß Ala Asp Asp Mat Tyr Ser Leu Tyr Gly Gly Asn Wing Val Val Glu 250 255 260 TTA GTC ACT GTC AAG TCA TTT GAC ACC TCC CTC ATT AGG AAG ACA AGG 930 Leu Val Thr Val Lys Ser Phe Asp Thr Ser Leu He Arg Lys Thr Arg 265 270 275 ACT ATC CTT GAG GCA AAA CAA GCG AAG AAC CCA GCA AGT CCC TAT AAC 978 Thr He Leu Glu Wing Lys Gln Wing Lys Asn_ Pro Wing Pro Tyr Asn 280 285 290 CTT GCA TAT AAT TAT AAT TTT GAA TAT TCC GTG GTT TTC AAC ATG GTA 1026 Leu Wing Tyr Lys Tyr Asn Phe Glu Tyr Ser Val Val Pha Asn Met Val 295 300 305 310 CTT TGG ATA ATG ATC GCC TTG GCC TTG GCT GTG ATT ATC ACC TCT TAC 1074 Leu Trp He Met He Wing Leu Wing Lau Wing Val Ha Ha Thr Ser Tyr 315 320 325 AAT ATT TGG AAC ATG GAT CCT GGA TAT GAT AGC ATC ATT TAT AGG ATG 1122 Asn He Trp Asn Met Asp Pro Gly Tyr Asp Ser He He Tyr Arg Met 330 335 340 AC AAC CAG AAG ATT CGA ATG GAT TGAATGTTAC CTGTGCCAGA ATTA 1170 Thr Asn Gln Lys He Arg Met Asp 345 350 GAAAAGGGGG TTGGAAATTG GCTGTTTTGT TAAAATATAT CTTTTAGTGT GCTTTAAAGT 1230 AGATAGTATA CTTTACATTT ATAAAAAAAA ATCAAATTTT GTTCTTTATT TTGTGTGTGC 1290 CTGTGATGTT TTTCTAGAGT GAATTATAGT ATTGACGTGA ATCCCACTGT GGTATAGATT 1350 CCATAATATG CTTGAATATT ATGATATAGC CATTTAATAA CATTGATTTC ATTCTGTTTA 1410 ATGAATTTGG AAATATGCAC TGAAAGAAAT GTAAAACATT TAGAATAGCT CGTGTTATGG 1470 AAAAAAGTGC ACTGAATTTA TTAGACAAAC TTACGAATGC TTAACTTCTT TACACAGCAT 1530 AGGTGAAAAT CATATTTGGG CTATTGTATA CTATGAACAA TTTGTAAATG TCTTAATTTG 1590 ATGTAAATAA CTCTGAAACA AGAGAAAAGG TTTTTAACTT AGAGTAGCCC TAAAATATGG 1650 ATGTGCTTAT ATAATCGCTT AGTTTTGGAA CTGTATCTGA GTAACAGAGG ACAGCTGTTT 1710 TTTAACCCTC TTCTGCAAGT TTGTTGACCT ACATGGGCTA ATATGGATAC TAAAAATACT 1770 ACATTGATCT AAGAAGAAAC TAGCCTTGTG GAGTATATAG ATGCTTTTCA TTATACACAC 1830 AAAAATCCCT GAGGGACATT TTGAGGCATG AATATAAAAC ATTTTTATTT CAGTAACTTT 1890 TCCCCCTGTG TAAGTTACTA TGGTTTGTGG TACAACTTCA TTCTATAGAA TATTAAGTGG 1950 AAGTGGGTGA ATTCTACTTT TTATGTTGGA GTGGACCAAT GTCTATCAAG AGTGACAAAT 2010 AAAGTTAATG ATGATTCCAA AAC 2033 (2) INFORMATION FOR SEQ ID NO: 57: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 911 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10034 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 176 .. 805 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 57: ACGCCTGGGT GACCTCTACG TATATACAGA GCCTCCCTGG CCCTCCTGGA AAGAGTCCTG 60 GAAAGACAAC CTTCAGGTCC AGCCCTGGAG CTGGAGGAGT GGAGCCCCAC TCTGAAGACG 120 CAGCCTTTCT CCAGGTTCTG TCTCTCCCAT TCTGATTCTT GACACCAGAT GCAGG ATG 178 1 GTG TCC TCT CCC TGC ACG CAG GCA AGC TCA CGG ACT TGC TCC CGT ATC 226 Val Ser Ser Pro Cys Thr Gln Wing Ser Ser Arg Thr Cys Ser Arg Ha 5 10 15 CTG GGA CTG AGC CTT GGG ACT GCA GCC CTG TTT GCT GCT GGG GCC AAC 274 Leu Gly Leu Ser Leu Gly Thr Ala Ala Leu Phß Ala Ala Gly Ala Asn 20 25 30 GTG GCA CTC CTC CTT CCT AAC TGG GAT GTC ACC TAC CTG TTG AGG GGC 322 Val Ala Leu Leu Leu Pro Asn Trp Asp Val Thr Tyr Leu Leu Arg Gly 35 40 45 CTC CTT GGC AGG CAT GCC ATG CTG GGA ACT GGG CTC TGG GGA GGA GGC 370 Leu Leu Gly Arg His Wing Met Leu Gly Thr Gly Leu Trp Gly Gly Gly 50 55 60 65 CTC ATG GTA CTC ACT GCA GCT ATC CTC ATC TCC TTG ATG GGC TGG AGA 418 Leu Met Val Leu Thr Ala Wing He Leu He Ser Leu Met Gly Trp Arg 70 75 80 TAC GGC TGC TTC AGT AAG AGT GGG CTC TGT CGA AGC GTG CTT ACT GCT 466 Tyr Gly Cys Phe Ser Lys Ser Gly Leu Cys Arg Ser Val Leu Thr Wing 85 90 95 CTG TTG TCA GGT GGC CTG GCT TTA CTT GGA GCC CTG ATT TGC TTT GTC 514 Leu Leu Ser Gly Gly Leu Ala Leu Leu Gly Ala Leu lia Cys Phe Val 100 105 110 ACT TCT GGA GTT GCT CTG AAA GAT GGT CCT TTT TGC ATG TTT GAT GTT 562 Thr Ser Gly Val Ala Leu Lys Asp Gly Pro Phe Cys Met Phe Asp Val 115 120 125 TCA TCC TTC AAT CAG ACA CAA GCT TGG AAA TAT GGT TAC CCA TTC AAA 610 Ser Ser Phe Asn Gln Thr Gln Wing Trp Lys Tyr Gly Tyr Pro Phe Lys 130 135 140 145 GAC CTG CAT AGT AGG AAT TAT CTG TAT GAC CGT TCG CTC TGG AAC TCC 658 Asp Leu His Ser Arg Asn Tyr Leu Tyr Asp Arg Ser Leu Trp Asn Ser 150 155 160 GTC TGC CTG GAG CCC TCT GCA GCT GTT GTC TGG CAC G TG TCC CTC TTC 706 Val Cys Leu Glu Pro Ser Ala Ala Val Val Trp His Val Ser Leu Phe 165 170 175 TCC GCC CTT CTG TGC ATC AGC CTG CTC CAG CTT CTC CTG GTG GTC GTT 754 Ser Ala Leu Leu Cys He Ser Leu Lau Gln Leu Leu Leu Val Val Val 180 185 190 t * CAT GTC ATC AAC AGC CTC CTG GGC CTT TTC TGC AGC CTC TGC GAG AAG 802 His Val He Asn Ser Leu Leu Gly Leu Phe Cys Ser Leu Cys Glu Lys 195 200 205 TGACAGGC AGAACCTTCA CTTGCAAGCA TGGGTGTTTA TCATCATCGG CTGTCTTGAA 860 TCCTTTCTAC AAGGAGTGGG TACGAATTAT AAACAAACTT CCCCTTTAGG T 911 (2) INFORMATION FOR SEQ ID NO: 58: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 601 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10050 (ix) SEQUENCE CHARACTERISTICS: (A) CODE CHARACTERIZATION: CDS (B) EXISTENCE POSITION: 10 .. 501 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 58: CCATCTGTC ATG GCG GCT GGG CTG TTT GGT TTG AGC GCT CGC CGT CTT TTG 51 Met Wing Wing Gly Leu Phe Gly Leu Wing Wing Arg Arg Leu Leu 1 5 10 GCG GCA GCG GCG ACG CGA GGG CTC CCG GCC GCC CGC GTC CGC TGG GAA 99ing Thr Arg Gly Leu Pro Wing Wing Arg Val Arg Trp Glu 15 20 25 30 TCT AGC TTC TCC AGG ACT GTG GTC GCC CCG TCC GCT GTG GCG GGA AAG 147 Ser Ser Pha Ser Arg Thr Val Val Wing Pro Ser Wing Val Ala Gly Lys 35 40 45 CGG CCC CCA GAA CCG ACC ACA CCG TGG CAA GAG GAC CCA GAA CCC GAG 195 Arg Pro Pro Glu Pro Thr Pro Trp Gln Glu Asp Pro Glu Pro Glu 50 55 60 GAC GAA AAC TTG TAT GAG AAG AAC CCA GAC TCC CAT GGT TAT GAC AAG 243 Asp Glu Asn Leu Tyr Glu Lys Asn Pro Asp Ser His Gly Tyr Asp Lys 65 70 75 GAC CCC GTT TTG GAC GTC TGG AAC ATG CGA CTT GTC TTC TTC TTG GGC 291 Asp Pro Val Leu Asp Val Trp Asn Met Arg Leu Val Phe Phe Phe Gly 80 85 90 GTC TCC ATC ATC CTG GTC CTT GGC AGC ACC TTT GTG GCC TAT CTG CCT 339 Val Ser He Leu Val Leu Gly Ser Thr Phe Val Wing Tyr Leu Pro 95 100 105 110 GAC TAC AGG TGC ACA GGG TGT CCA AGA GCG TGG GAT GGG ATG AAA GAG 387 Asp Tyr Arg Cys Thr Gly Cys Pro Arg Wing Trp Asp Gly Met Lys Glu 115 120 125 TGG TCC CGC GAC GCT AGG CTG GTG AAA TAC CGA GAG GCC AAT 435 Trp Ser Arg Arg Glu Wing Glu Arg Leu Val Lys Tyr Arg Glu Wing Asn 130 135 140 GGC CTT CCC ATC ATG GAA TCC AAC TGC TTC GAC CCC AGC AAG ATC CAG 483 Gly Leu Pro He Met Glu Be Asn Cys Phß Asp Pro Ser Lys He Gln 145 150 155 CTG CCA GAG GAT GAG TGACCAGTTG CTAAGTGGGG CTCAAGAAGC AC 530 Leu Pro Glu Asp Glu 160 CGCCTTCCCC ACCCCCTGCC TGCCATTCTG ACCTCTTCTC AGAGCACCTA ATTAAAGGGG 590 CTGAAAGTCT G 601 (2) INFORMATION FOR SEQ ID NO: 59: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 394 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10071 (ix) SEQUENCE CHARACTERISTICS: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 47 .. 325 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 59: AACATCCGGG CCGCGCGGGG AAGGGGAGAC GTGGGGTATA GTGACC ATG ACG AAA 55 Met Thr Lys 1 TTA GCG CAG TGG CTT TGG GGA CTA GCG ATC CTG GGC TCC ACC TGG GTG 103 Leu Ala Gln Trp Leu Trp Gly Leu Ala He Leu Gly Ser Thr Trp Val 5 10 15 GCC CTG ACC GGCC ACG GGT TTG GGC CTG GAG CTG CCC TTG TCC TGC CAG 151 Wing Leu Thr Thr Gly Wing Leu Gly Leu Glu Leu Pro Leu Ser Cys Gln 20 25 30 35 GAA GTC CTG TGG CCA CTG CCC GCC TAC TTG CTG GTG TCC GCC GGC TGC 199 Glu Val Lau Trp Pro Leu Pro Wing Tyr Leu Leu Val Ser Wing Gly Cys 40 45 50 TAT GCC CTG GGC ACT GTG GGC TAT CGT GTG GCC ACT TTT CAT GAC TGC 247 Tyr Wing Leu Gly Thr Val Gly Tyr Arg Val Wing Thr Phe His Asp Cys 55 60 65 GAG GAC GCC GCA CGC GAG CTG CAG AGC CAG ATA CAG GAG GCC CGA GCC 295 Glu Asp Wing Wing Arg Glu Leu Gln Ser Gln He Gln Glu Wing Arg Wing 70 75 80 GAC TTA GCC CGC AGG GGG CTG CGC TTC TGACAGCCTA ACCCCATT 340 Asp Leu Wing Arg Arg Gly Leu Arg Phe 85 90 CCTGTGCGGA CAGCCCTTCC TCCCATTTCC CATTAAAGAG CCAGTTTATT TTCT 394 (2) INFORMATION FOR SEQ ID NO: 60: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 732 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR line: U937 (D) CLONE NAME: HP10076 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 82 .. 600 (C) CHARACTERIZATION METHOD: E (i) DESCRIPTION OF SEQUENCE: SEQ ID NO: 60: AGAAACGTGT TCGCTGCCCA GAAGAAGGGA AGGCGCGAGT GAGGAAAGGA GGTACTGTAG_60_ATGCCCTCCA AATCCTTGGT T ATG GAA TAT TTG GCT CAT CCC AGT ACA CTC 111 Met Glu Tyr Leu Ala His Pro Ser Thr Leu 1 5 10 GGC TTG GCT GTT GGA GTT GCT TGT GGC ATG TGC CTG GGC TGG AGC CTT 159 Gly Leu Ala Val Gly Val Wing Cys Gly Met Cys Leu Gly Trp Ser Leu 15 20 25 CGA GTA TGC TTT GGG ATG CTC CCC AAA AGC AAG ACG AGC AAG ACA CAC 207 Arg Val Cys Phe Gly Met Leu Pro Lys Ser Lys Thr Ser Lys Thr His 30 35 40 ACÁ GAT ACT GAA AGT GAA GCA AGC ATC TTG GGA AGC GGG GAG TAC 255 Thr Asp Thr Glu Ser Glu Wing Ser Ha Leu Gly Asp Ser Gly Glu Tyr 45 50 55 AAG ATG ATT CTT GTG GTT CGA AAT GAC TTA AAG ATG GGA AAA GGG AAA 303 Lys Met He Leu Val Val Arg Asn Asp Leu Lys Met Gly Lys Gly Lys 60 65 70 GTG GCT GCC GAG TGC TCT CAT GCT GCT GTT TCA GCC TAC AAG CAG ATT 351 Val Wing Wing Gln Cys Ser His Wing Wing Val Wing Tyr Lys Gln He 75 80 85 90 CAA AGA AGA AAT CCT GAA ATG CTC AAA CAA TGG GAA TAC TGT GGC CAG 399 Gln Arg Arg Asn Pro Glu Met Leu Lys Gln Trp Glu Tyr Cys Gly Gln 95 100 105 CCC AAG GTG GTG GTC AAA GCT CCT GAT GAA GAA ACC CTG ATT GCA TTA 447 Pro Lys Val Val Lys Ala Pro Asp Glu Glu Thr Leu Ha Ala Leu 110 115 120 TTG GCC CAT GCA AAA ATG CTG GGA CTG ACT GTA AGT TTA ATT CAA GAT 495 Leu Ala His Wing Lys Mat Leu Gly Leu Thr Val Ser Leu He Gln Asp 125 130 135 GCT GGA CGT ACT CAG ATT GCA CCA GGC TCT CAA ACT GTC CTA GGG ATT 543 Wing Gly Arg Thr Gln Ha Wing Pro Gly Ser Gln Thr Val Leu Gly He 140 145 150 GGG CCA GGA CCA GCA GAC CTA ATT GAC AAA GTC ACT GGT CAC CTA AAA 591 Gly Pro Gly Pro Wing Asp Leu He Asp Lys Val Thr Gly His Leu Lys 155, 160 165 170 CTT TAC TAGGTGGACT TTGATATGAC AACAACCCCT CCATCACAAG TGT 640 Leu Tyr TTGAAGCCTG TCAGATTCTA ACAACAAAAG CTGAATTTCT TCACCCAACT TAAATGTTCT 700 TGAGATGAAA ATAAAACCTA TTCCCATGTT CT 732 (2) INFORMATION FOR SEQ ID NO: 61: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 697 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: DNAs for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10085 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 151 .. 600 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 61: TATACCTCTA GTTTGGAGCT GTGCTGTAAA AACAAGAGTA ACATTTTTAT ATTAAAGTTA 60 AATAAAGTTA CAACTTTGAA GAGAGTTTCT GCAAGACATG ACACAAAGCT GCTAGCAGAA 120 AATCAAAACG CTGATTAAAA GAAGCACGGT ATG ACC AAA CAT AAA AAG TGT 174 Met Mat Thr Lys His Lys Lys Cys 1 5 TTT ATA ATT GTT GGT GTT TTA ATA ACA ACT AAT ATT ATT ACT CTG ATA 222 Phe He He Val Val Gly Val Leu Ha Thr Thr Asn He He Thr Leu He 10 15 20 GTT AAA CTA ACT CGA GAT TCT CAG AGT TTA TGC CCC TAT GAT TGG ATT 270 Val Lys Leu Thr Arg Asp Ser Gln Ser Leu Cys Pro Tyr Asp Trp He 25 30 35 40 GGT TTC CAA AAC AAA TGC TAT TAT TTC TCT AAA GAA GAA GGA GAT TGG 318 Gly Phe Gln Asn Lys Cys Tyr Tyr Phe Ser Lys Glu Glu Gly Asp Trp 45 50 55 AAT TCA AGT AAA TAC AAC TGT TCC ACT FAC CAT GCC GAC CTA ACT ATA 366 Asn Ser Ser Lys Tyr Asn Cys Ser Thr Gln His Wing Asp Leu Thr He 60 65 70 ATT GAC AAC ATA GAA GAA ATG AAT TTT CTT AGG CGG TAT AAA TGC AGT 414 He Asp Asn He Glu Glu Met Asn Phe Leu Arg Arg Tyr Lys Cys Ser 75 80 85 TCT GAT CAC TGG ATT GGA CTG AAG ATG GCA AAA AAT CGA ACA GGA CAA 462 Ser Asp His Trp He Gly Leu Lys Mßt Ala Lys Asn Arg Thr Gly Gln 90 95 100 TGG GTA GAT GGA GCT ACA TTT ACC AAA TCG TTT GGC ATG AGA GGG AGT 510 Trp Val Asp Gly Wing Thr Phe Thr Lys Ser Phe Gly Met Arg Gly Ser 105 110 115 120 GAA GGA TGT GCC TAC CTC AGC GAT GAT GCA GCA GCA ACA GCT AGA TGT 558 Glu Gly Cys Wing Tyr Leu Ser Asp Asp Gly Wing Wing Thr Wing Arg Cys 125 130 135 TAC ACC GAA AGA AAA TGG ATT TGC AGG AAA AGA ATA CAC TAA 600 Tyr Thr Glu Arg Lys Trp He Cys Arg Lys Arg Ha His 140 145 GTTAATGTCT AAGATAATGG GGAAAATAGA AAATAACATT ATTAAGTGTA AAACCAGCAA 660 AGTACTTTTT TAATTAAACA AAGTTCGAGT TTTGTAC 697 (2) INFORMATION FOR SEQ ID NO: 62: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1186 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10122 (ix) SEQUENCE CHARACTERISTICS: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 139 .. 705 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 62: AAGTGCGATC TTCGGGCTGT CAGAGTTGGT CTGTTACTCG GTGGTGGCGG AGTCTACGGA 60 AGCCGTTTTC GCTTCACTTT TCCTGGCTGT AGAGCGCTTT CCCCCTGGCG GGTGAGAGTG 120 CAGAGACGAA GGTGCGAG ATG AGC ACT ATG TTC GCG GAC ACT CTC CTC ATC 171 Mat Ser Thr Met Phe Wing Asp Thr Leu Leu He 1 5 10 GTT TTT ATC TCT GTG TGC ACG GCT CTG CTC GG GG GGC ATA ACC TGG 219 Val Phe He Ser Val Cys Thr Ala Leu Leu Ala Glu Gly He Thr Trp 15 20 25 GTC CTG GTT TAC AGG ACÁ GAC AAG TAC AAG AGA CTG AAG GCA GAA GTG 267 Val Leu Val Tyr Arg Thr Asp Lys Tyr Lys Arg Leu Lys Wing Glu Val 30 35 40 GAA AAA CAG AGT AAA AAA TTG GAA AAG AAG AAG GAA ATA ATA GAG 315 Glu Lys Gln Ser Lys Lys Leu Glu Lys Lys Lys Glu Thr He Thr Glu 45 50 55 TCA GCT GGT CGA CAA CAG AAA AAA AAA ATA GAG AGA CAA GAA GAG AAA 363 Ser Ala Gly Arg Gln Gln Lys Lys He Glu Arg Gln Glu Glu Lys 60 65 70 75 CTG AAG AAT .AAC AAC AGA GAT CTA TCA ATG GTT CGA ATG AAA TCC ATG 411 Leu Lys Asn Asn Asg Arg Asp Leu Ser Met Val Arg Met Lys Ser Met 80 85 90 TTT GCT ATT GGC TTT TGT TTT ACT GCC CTA ATG GGA ATG TTC AAT TCC 459 Phe Ala He Gly Phe Cys Phß Thr Ala Leu Met Gly Met Phe Asn Ser 95 100 105 ATA TTT GAT GGT AGA GTG GG AAG CTT CCT TTT ACC CCT CTT TCT 507 He Phe Asp Gly Arg Val Val Ala Lys Leu Pro Phe Thr Pro Lau Ser 110 115 1 20 TAC ATC CAA GGA CTG CTT CAT CGA AAT CTG GG GAC GAC ACC AC 555 Tyr He Gln Gly Leu Ser His Arg Asn Leu Leu Gly Asp Asp Thr Thr 125 130 135 GAC TGT TCC TTC ATT TTC CTG TAT ATT CTC TGT ACT ATG TCG ATT CGA 603 Asp Cys Ser Phe He Phe Leu Tyr He Leu Cys Thr Mßt Ser He Arg 140 145 150 155 CAG AAC ATT CAG AAG ATT CTC GGC CTT GCC CCT TCA CGA GCC GCC ACC 651 Gln Asn He Gln Lys He Leu Gly Leu Wing Pro Ser Arg Wing Wing Thr 160 165 170 AAG CAG GCA GGT GTC TTT CTT GGC CCA CCA CCT CCT TCT GGG AAG TTC 699 Lys Gln Wing Gly Gly Phe Leu Gly Pro Pro Pro Ser Gly Lys Phe 175 180 185 TCT TGAACTCAAG AACTCTTTAT TTTCTATCAT TCTTTCTAGA CACACACA 750 Be CATCAGACTG GCAACTGTTT TGTAGCAAGA GCCATAGGTA GCCTTACTAC TTGGGCCTCT 810 TTCTAGTTTT GAATTATTTC TAAGCCTTTT GGGTATGATT AGAGTGAAAA TGGCAGCCAG 870 CAAACTTGAT AGTGCTTTTG GTCCTAGATG ATTTTTATCA AATAAGTGGA TTGATTAGTT 930 AAGTTCAGGT AATGTTTATG TAATGAAAAA CAAATAGCAT CCTTCTTGTT TCATTTACAT 990 AAGTATTTTC TGTGGGACCG ACTCTCAAGG CACTGTGTAT GCCCTGCAAG TTGGCTGTCT 1050 ATGAGCATTT AGAGATTTAG AAGAAAAATT TAGTTTGTTT AACCCTTGTA ACTGTTTGTT 1110 TTGTTGTTGT TTTTTTTTTCA AGCCAAATAC ATGACATAAG ATCAATAAAG AGGCCAAATT 1170 TTTAGCTGTT TTATGT 1186 (2) INFORMATION FOR SEQ ID NO: 63: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1409 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Lymphoma (C) CELLULAR LINE: U937 (D) CLONE NAME: HP10136, (i?) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 82 .. 729 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 63: ATAACTGTTG TCGCGGCGGA GGAAGTGAGG ACGGCGCCAA GGGCCTTCCG GGCCAGTGTT 60 GGATCCCTGT AGTTTGTGAA G ATG GTG TTG CTA ATG ATC GCC CGA GTG 111 Met Val Leu Leu Thr Met lie Wing Arg Val 1 5 10 GCG GAC GGG CTC CCG CTG GCC GCC TCG ATG CAG GAG GAC GAA CAG TCT 159 Wing Asp Gly Leu Pro Leu Ala Ala Ser Met Gln Glu Asp Glu Gln Ser 15 20 25 GGC CGG GAC CTT CAA CAG TAT CAG AGT CAG GCT AAG CAA CTC TTT CGA 207 Gly Arg Asp Leu Gln Gln Tyr Gln Sar Gln Ala Lys Gln Leu Phe Arg 30 35 40 AAG TTG AAT GAA CAG TCC CCT ACC AGA TGT ACC TTG GAA GCA GGA GCC 255 Lys Leu Asn Glu Gln Ser Pro Thr Arg Cys Thr Leu Glu Ala Gly Wing 45 50 55 ATG ACT TTT CAC TAC ATT ATT GAG CAG GGG GTG TGT TAT TTG GTT TTA 303 Met Thr Pha His Tyr Ha He Glu Gln Gly Val Cys Tyr Leu Val Leu 60 65 70 TGT GAA GCT GCC TTC CCT AAG AAG TTG GCT TTT GCC TAC CTA GAA GAT 351 Cys Glu Wing Wing Phe Pro Lys Lys Leu Wing Phe Wing Tyr Leu Glu Asp 75 80 85 90 TTG CAC TCA GAA TTT GAT GAA CAG CAT GGA AAG AAG GTG CCC ACT GTG 399 Lau His Ser Glu Phe Asp Glu Gln His Gly Lys Lys Val Pro Thr Val 95 100 105 TCC CGA CCC TAT TCC TTT ATT GAA TTT GAT ACT TTC ATT CAG AAA ACC 447 Ser Arg Pro Tyr Ser Phe He Glu Phe Asp Thr Phe Ha Gln Lys Thr 110 115 120 AAG AAG CTC TAC ATT GAC AGT CGT GCT CGA AGA AAT CTA GGC TCC ATC 495 Lys Lys Tyr He Asp Ser Arg Wing Arg Arg Asn Leu Gly Ser He 125 130 135 AAC ACT GAA TTG CAA GAT GTG CAG AGG ATC ATG GTG GCC AAT ATT GAA 543 Asn Thr Glu Leu Gln Asp Val Gln Arg He Met Val Wing Asn He Glu 140 145 150 GAA GTG TTA CAA CGA GGA GAA GCA CTC TCA GCA TTG GAT TCA AAG GCT 591 Glu Val Leu Gln Arg Gly Glu Ala Leu Sar Ala Leu Asp Ser Lys Ala 155 160 165 170 AAC AAT TTG TCC AGT CTG TCC AAG AAA TAC CGC CAG GAT GCG AAG TAC 639 Asn Asn Leu Ser Ser Leu Ser Lys Lys Tyr Arg Gln Asp Wing Lys Tyr 175 180 185 TTG AAC ATG CGT TCC ACT TAT GCC AAA CTT GCA GCA G TA GCT GTA TTT 687 Leu Asn Mat Arg Ser Thr Tyr Wing Lys Leu Wing Wing Val Wing Val Phe 190 195 200 TTC ATC ATG TTA ATA GTG TAT GTC CGA TTC TGG TGG CTG TGAA 730 Phe Ha Met Leu Ha Val Tyr Val Arg Phe Trp Trp Lau 205 210 215 ATAATGAATA CAGTCACTGG TAAGGGAGAA CCTAGAACCC AGTAGGTGTA TATTTTCAGG 790 AAACTGAGCT CACAGAGATG TGTATTAGAA TCCAAGTGGA ACTTCTGCCT CTAAAGACCT 850 TGCAAGAAAA GAGATGCCCT GAAAATGAAA GGTTGCACCT CATTTAATGA AGCTTAACCC 910 TATGTAGAAA GTCTCTTTCG GGGGCAGAGG CTTTCTCTGG GTGCCAAGCC ATATATATTA 970 GGGAATAGTA GATTGTTAAT TTCGTTTTTT CCCTCCCAGT GCATTTTAAA AACAGCACTG 1030 GCTGGGGCAT TCTCATTCTC TGATGGAGCC ATCAATGAGA TTTAACTTAG TCAACCTGTG 1090 CTAGCAACAT TCTGAAATTC CTTCAAAGAA GGCAGTCCTT TGGGAAGGTG TTTTTTTTTT 1150 TTTTTTTTTT TTTGACTCTA ATCAACATTC CTTTTGTTGG TGACATTTGT GATTTTCAGT 1210 AATCTGAGTT TTTGATGGCC TTTTAAACAA GACTCCAGTA TGTGAAGGTT AATTGCTGTG 1270 CTCCACAGAT CTTGTCTATT GGCCCCTGTA GAAAGTTAAG CTTTGTTGTT TTCCTTTTAT 1330 AATTTGCTTA TTGCACAATT GCTTTAGGGT AAGTGAATTA TATTAAGATG CCTTGAAATT 1390 ATAGCACTCC TTGATTAAG 1409 (2) INFORMATION FOR SEQ ID NO: 64: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 974 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10175 (ix) SEQUENCE CHARACTERISTICS: (A) CODE OF CHARACTERIZATION: CDS (B) POSITION OF EXISTENCE: 174 .. 512 (C) METHOD OF CHARACTERIZATION: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 64: AGAGCCGCTC CCCTCTCCTC GCCCCGCCAC CGGGACGGAG AGCGCCCGCC GCTGCATTTC 60 CGGCGACACC TCGCAGTCAT TCCTGCGGCT TGCGCGCCCT TGTAGACAGC CGGGGCCTTC 120 GTGAGACCGG TGCAGGCCTG GGGTAGTCTC CTGTCTGGAC AGAGAAGAGA AAA ATG 176 Met 1 CAG GAC ACT GGC TCA GTA GTG CCT TTG CAT TGG TTT GGC TTT GGC TAC 224 G n Asp Thr Gly Ser Val Val Pro Leu Hia Trp Phe Gly Phe Gly Tyr 5 10 15 GCA GCA CTG GTT GCT TCT GGT GGG ATC ATT GGC TAT GTA AAA GCA GGC 272 Wing Wing Leu Val Wing Gly Gly He He He Gly Tyr Val Lys Wing Gly 20 25 30 AGC GTG CCG TCC CTG GCT GCA GGG CTG CTC TTT GGC AGT CTA GCC GGC 320 Ser Val Pro Ser Leu Ala Wing Gly Leu Leu Phe Gly Ser Leu Wing Gly 35 40 45 CTG GGT GCT TAC CAG CTG TCT CAG GAT CCA AGG AAC GTT TGG GTT TTC 368 Leu Gly Wing Tyr Gln Leu Ser Gln Asp Pro Arg Asn Val Trp Val Phe 50 55 60 65 CTA GCT ACT TCT GGT ACC TTG GCT GGC ATT ATG GGA ATG AGG TTC TAC 416 Leu Wing Thr Ser Gly Thr Leu Wing Gly Met Met Gly Met Arg Phe Tyr 70 75 80 CAC TCT GGA AAA TTC ATG CCT GCA GGT TTA ATT GCA GGT GCC AGT TTG 464 His Ser Gly Lys Phe Met Pro Wing Gly Leu He Wing Gly Wing Ser Leu 85 90 95 CTG ATG GTC GCC AAA GTT GGA GTT AGT ATG TTC AAC AGA CCC CAT 509 Met Val Leu Ala Gly Val Val Lys Ser Met Arg Phe Asn Pro His 100 105 110 T AGCAGAAGTC ATGTTCCAGC TTAGACTGAT GAAGAATTAA AAATCTGCAT 560 CTTCCACTAT TTTCAATATA TTAAGAGAAA TAAGTGCAGC ATTTTTGCAT CTGACATTTT 620 ACCTAAAAAA AAAGACACCA AACTTGGCAG AGAGGTGGAA AATCAGTCAT GATTACAAAC 680 CTACAGAGGT GGCGAGTATG TAACACAAGA GCTTAATAAG ACCCTCATAG AGCTTGATTC 740 TTGTATATTG ATGTTGTCTT TTCTTTCTGT ATCTGTAGGT AAATCTCAAG GGTAAAATGT 800 S. TAGGTGTCAG CTTTCAGGGC TCTGAAACCC TATTCCCTGC TCTGAGGAAC AGTGTGAAAA 860 AAAGTCTTTT AGGAGATTTA CAATATCTGT TCTTTTGCTC ATCTTAGACC ACAGACTGAC 920 TTTGAAATTA TGTTAAGTGA AATATCAATG TAAATAAAGT TTACTATAAA TAAT 974 (2) INFORMATION FOR SEQ ID NO: 65: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 925 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10179 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 122 .. 466 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 65: AATCGCGTTT CCGGAGAGAC CTGGCTGCTG TGTCCCGCGG CTTGCGCTCC GTAGTGGACT 60 CCGCGGGCCT TCGGCAGATG CAGGCCTGGG GTAGTCTCCT TTCTGGACTG AGAAGAGAAG 120 ATG GAG AAG CCC CTC TTC CCA TTA GTG CCT TTG CAT TGG TTT GGC TTT 168 Met Glu Lys Pro Leu Phe Pro Leu Val Pro Leu His Trp Pha Gly Phe 1 5 10 15 GGC TAC ACA GCA CTG GTT GTT TCT GGT GGG ATC GTT GGC TAT GTA AAA 216 Gly Tyr Thr Ala Leu Val Val Ser Gly Gly Ha Val Gly Tyr Val Lys 20 25 30 ACÁ GGC AGC GTG CCG TCC CTG GCA GCA GGG CTG CTC TTC GGC AGT CTA 264 Thr Gly Ser Val Pro Sar Lau Wing Wing Wing Gly Leu Leu Phe Gly Ser Leu 35 40 45 GCC GGC CTG GGT GCT TAC CAG CTG TAT CAG GAT CCT AGG AAC GTT TGG 312 Wing Gly Leu Gly Wing Tyr Gln Leu Tyr Gln Asp Pro Arg Asn Val Trp 50 55 60 GGT TTC CTA GCC GCT ACT TCT GTT ACT TTT GTT GGT GTT ATG GGA ATA 360 Gly Phe Leu Wing Ala Thr Ser Val Thr Phe Val Gly Val Met Gly Met 65 70 75 80 AGA TCC TAC TAC TAT TGA TGA TGA ATG CCT GTA TGA GTA TTA ATT GCA GGT 408 Arg Ser Tyr Tyr Tyr Gly Lys Phe Met Pro Val Gly Leu He Wing Gly 85 90 95 GCC AGT TTG CTG ATG GCC GCC AAA GTT GGA GTT CGT ATG TTG ATG ACÁ 456 Wing Ser Leu Lau Mat Wing Wing Val Gly Val Arg Met Leu Met Thr 100 105 110 TCT GAT TAGCAGAAGT CATGTTCGCA GCTTGGACTC ATGAAGGATT AAAAAT CT 510 Be Asp GCATCTTCCA CTATTTTCAA TGTATTAAGA GAAATAAGTG CAGCATTTTT GCATCTGACA 570 TTTTACCTAA AAAAAAAAAG ACACCAAATT TGGCGGAGGG GTGGAAAATC AGTTGTTACC 630 ATTATAACCC TACAGAGGTG GTGAGCATGT AACATGAGCT TATTGAGACC ATCATAGAGA 690 TCGATTCTTG TATATTGATT TTATCTCTTT CTGTATCTAT AGGTAAATCT CAAGGGTAAA 750 ATGTTAGGTG TTGACATTGA GAACCCTGAA ACCCCATTCC CTGCTCAGAG GAACAGTGTG 810 AAAAAAAATC TCTTGAGAGA TTTAGAATAT CTTTTCTTTT GCTCATCTTA GACCACAGAC 870 TGACTTTGAA ATTATGTTAA GTGAAATATC AATGAAAATA AACTTTACTA TAAAT 925 (2) INFORMATION FOR SEQ ID NO: 66: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1115 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: ADNa for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosaraome (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10196 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 10 .. 993 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 66: GCGGGGAAA ATG GCG GCG GCG GCG GCG GCG GCT GCA GCT ACG AAC GGG ACC 51 Met Wing Wing Wing Wing Wing Wing Wing Wing Thr Asn Gly Thr 1 5 10 GGA GGA AGC AGC GGG ATG GAG GTG GAT GCA GCA GTA GTC CCC AGC GTG 99 Gly Gly Be Ser Gly Met Glu Val Asp Ala Wing Val Val Pro Ser Val 15 20 25 30 ATG GCC TGC GGA GTG ACT GGG AGT GTT TCC GTC GCT CTC CAT CCC CTT 147 Met Wing Cys Gly Val Thr Gly Ser Val Sar Val Ala Leu His Pro Leu 35 40 45 GTC ATT CTC AAC ATC TCA GAC CAC TGG ATC CGC ATG CGC TCC CAG GAG 195 Val Ha Leu Asn He Ser Asp His Trp He Arg Mat Arg Ser Gln Glu 50 55 60 GGG CGG CCT GTG GAG GTG ATT GGG GCT CTG ATT GGC AAG CAG GAG GGC 243 Gly Arg Pro Val Gln Val He Gly Ala Leu Ha Gly Lys Gln Glu Gly 65 70 75 CGA AAT ATC GAG GTG ATG AAC TCC TTT GAG CTG CTG TCC CAC ACC GTG 291 Arg Asn He Glu Val Met Asn Ser Phe Glu Leu Leu Ser His Thr Val 80 85 90 GAA GAG AAG ATT ATC ATT GAC AAG GAA TAT TAT TAC ACC AAG GAG GAG 339 Glu Glu Lys Ha He As Asp Lys Glu Tyr Tyr Tyr Thr Lys Glu Glu 95 100 105 110 CAG TTT AAA CAG GTG TTC AAG GAG CTG GAG TTT CTG GGT TGG TAT ACC 387 Gln Phe Lys Gln Val Phe Lys Glu Leu Glu Pha Leu Gly Trp Tyr Thr 115 120 125 ACÁ GGG GGG CCA CCT GAC CCC TCG GAC ATC CAC GTC CAT AAG CAG GTG 435 Thr Gly Gly Pro Pro Asp Pro Sar Asp He His Val His Lys Gln Val 130 135 140 TGT GAG ATC ATC GAG AGC CCC CTC TTT CTG AAG TTG AAC CCT ATG ACC 483 Cys Glu He He Glu Ser Pro Leu Phe Leu Lys Leu Asn Pro Mßt Thr 145 150 155 AAG CAC ACA GAT CTT CCT GTC AGC GTT TTT GAG TCT GTC ATT GAT ATA 531 Lys His Thr Asp Leu Pro Val Ser Val Phe Glu Ser Val He Asp He 160 165 170 ATC AAT GGA GAG GCC ACA ATG CTG TTT GCT GAG CTG ACC TAC ACT CTG 579 He Asn Gly Glu Wing Thr Met Leu Phe Wing Glu Leu Thr Tyr Thr Leu 175 180 185 190 GCC ACÁ GAG GAA GCG GAA CGC ATT GGT GTA GAC CAC GTA GCC CGA ATG 627 Wing Thr Glu Glu Wing Glu Arg He Gly Val Asp His Val Wing Arg Met 195 200 205 ACÁ GCA ACÁ GGC AGT GGA GAG AAC TCC ACT GTG GCT GAA CAC CTG ATA 675 Thr Wing Thr Gly Ser Gly Glu Asn Sar Thr Val Wing Glu His Lau He 210 215 220 GCA CAG CAC AGC GCC ATC AAG ATG CTG CAC AGC CGC GTC AAG CTC ATC 723 Wing Gln His Ser Wing Ha Lys Met Leu His Ser Arg Val Lys Leu Ha 225 230 235 TTG GAG TAC GTC AAG GCC TCT GAA GCG GGA GTC GTC CCC TTT AAT CAT 771 Leu Glu Tyr Val Lys Wing Ser Glu Wing Gly Glu Val Pro Phe Asn His 240 245 250 GAG ATC CTG CGG GAG GCC TAT GCT CTG TGT CAC TGT CTC CCG GTG CTC 819 Glu He Lau Arg Glu Ala Tyr Ala Lau Cys His Cys Leu Pro Val Leu 255 260 265 270 AGC ACÁ GAC AAG TTC AAG ACÁ GAT TTT TAT GAT CAA TGC AAC GAC GTG 867 Ser Thr Asp Lys Phe Lys Thr Asp Phe Tyr Asp Gln Cys Asn Asp Val 275 280 285 GGG CTC ATG GCC TAC CTC GGC ACC ATC ACC AAA ACG TGC AAC ACC ATG 915 Gly Leu Mat Wing Tyr Leu Gly Thr He Thr Lys Thr Cys Asn Thr Met 290 295 300 AAC CAG TTT GTG AAC AAG TTC AAT GTC CTC TAC GAC CGA CAA CAG GGC ATC 963 Asn Gln Phß Val Asn Lys Phe Asn Val Leu Tyr Asp Arg Gln Gly He 305 310 315 GGC AGG AGA ATG CGC G GG CTC TTT TTC TGATGAGGGT 1000 Gly Arg Arg Met Arg Gly Leu Phe Phe 320 325 ACTTGAAGGG CTGATGGACA GGGGTCAGGC AACTATCCCA AAGGGGAGGG CACTACACTT 1060 CCTTGAGAGA AACCACTGTC ATTAATAAAA GGGGAGCAGC CCCTGAGCAC CCCTG 1115 (2) INFORMATION FOR SEQ ID NO: 67: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1721 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Fibrosarcoma (C) CELLULAR LINE: HT-1080 (D) CLONE NAME: HP10235 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CODE OF CHARACTERIZATION: CDS (B) POSITION OF EXISTENCE: 6 .. 1127 (C) METHOD OF CHARACTERIZATION: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 67: ATGTC ATG ACC CTA TGT GCC ATG CTG CCC CTG CTG TTA TTC ACC TAC CTC 50 Met Thr Leu Cys Wing Met Leu Pro Leu Leu Leu Phe Thr Tyr Leu 1 5 10 15 AAC TCC TTC CTG CAT CAG AGG ATC CCC CAG TCC GTA CGG ATC CTG GGC 98 Asn Ser Phe Leu His Gln Arg He Pro Gln Ser Val Arg He Leu Gly 20 25 30 AGC CTG GTG GCC ATC CTG CTG GTG TTT CTG ATC ACT GCC ATC CTG GTG 146 Ser Lau Val Ala He Leu Leu Val Phe Leu He Thr Ala He Leu Val 35 40 4 5 AAG GTG CAG CTG GAT GCT CTG CCC TTC TTT GTC ATC ACC ATG ATC AAG 194 Lys Val Gln Leu Asp Ala Leu Pro Phe Phe Val He Thr Met He Lys 50 55 60 ATC GTG CTC ATT AAT TCA TTT GGT GCC ATC CTG CAG GGC AGC CTG TTT 242 Ha Val Leu He Asn Ser Phe Gly Ala Ha Lau Gln Gly Ser Leu Pha 65 70 75 GGT CTG GCT GGC CTT CTG CCT GCC AGC TAC ACG GCC CCC ATC ATG AGT 290 Gly Leu Wing Gly Leu Leu Pro Wing Being Tyr Thr Wing Pro Ha Met Being 80 85 90 95 GGC CAG GGC CTA GCA GGC TTC TTT GCC TCC GTG GCC ATG ATC TGC GCT 338 Gly Gln Gly Leu Wing Gly Phe Phe Wing Ser Val Wing Mat He Cys Wing 100 105 110 ATT GCC AGT GGC TCG GAG CTA TCA GAA AGT GCC TTC GGC TAC TTT ATC 386 Ha Wing Ser Gly Ser Glu Leu Ser Glu Ser Wing Pha Gly Tyr Phß He 115 120 125 AC GCC TGT GCT GTT ATC ATT TTG ATC ATC TGT TAC CTG GGC CTG 434 Thr Ala Cys Ala Val He He Leu Thr Ha He Cys Tyr Leu Gly Leu 130 135 140 CCC CGC CTG GAA TTC TAC TAC TAC TAC CAG CAG CTC AAG CTT GAA GGA 482 Pro Arg Leu Glu Phe Tyr Arg Tyr Tyr Gln Gln Leu Lys Leu Glu Gly 145 150 155 CCC GGG GAG CAG GAG ACC AAG TTG GAC CTC ATT AGC AAA GGA GAG GAG 530 Pro Gly Glu Gln Glu Thr Lys Leu Asp Leu Ha Ser Lys Gly Glu Glu 160 165 170 175 CCA AGA GCA GGC AAA GAG GAA TCT GGA GTT TCA GTC TCC AAC TCT CAG 578 Pro Arg Wing Gly Lys Glu Glu Ser Gly Val Sar Val Ser Asn Ser Gln 180 185 190 CCC ACC AAT GAA AGC CAC TCT ATC AAA GCC ATC CTG AAA AAT ATC TCA 626 Pro Thr Asn Glu Ser His Lys Wing He Leu Lys Asn He Ser 195 200 205 GTC CTG GCT TTC TCT GTC TGC TTC ATC TTC ACT ATC ACC ATT GGG ATG 674 Val Leu Wing Phe Ser Val Cys Phe He Phe Thr He Thr He Gly Met 210 215 220 TTT CCA GCC GTG ACT GTT GAG GTC AAG TCC AGC ATC GCA GGC AGC AGC 722 Pha Pro Wing Val Thr Val Glu Val Lys Ser Ser He Wing Gly Ser Ser 225 230 235 ACC TGG GAA CGT TAC TTC ATT CCT GTG TTC TGT TTC TTG ACT TTC AAT 770 Thr Trp Glu Arg Tyr Phe He Pro Val Ser Cys Phe Leu Thr Pha Asn 240 245 250 255 ATC TTT GAC TGG TTG GGC CGG AGC CTC ACÁ GCT GTA TTC ATG TGG CCT 818 Ha Pha Asp Trp Leu Gly Arg Ser Leu Thr Wing Val Phe Met Trp Pro 260 265 270 GGG AAG GAC AGC CGC TGG CTG CCA AGC CTG GTG CTG GCC CGG CTG GTG 866 Gly Lys Asp Ser Arg Trp Leu Pro Ser Leu Val Leu Wing Arg Leu Val 275 280 285 TTT GTG CCA CTG CTG CTG CTG TGC AAC ATT AAG CCC CGC CT CT 914 Phß Val Pro Leu Leu Leu Leu Cys Asn He Lys Pro Arg Arg Tyr Leu 290 295 300 ACT GTG GTC TTC GAG CAC GAT GCC TGG TTC ATC TTC TTC ATG GCT GCC 962 Thr Val Val Pha Glu His Asp Wing Trp Phe He Phe Phe Met Wing Wing 305 310 315 TTT GCC TTC TCC AAC GGC TAC CTC GCC AGC CTC TGC TGG ATG TGC TTC GGG 1010 Pha Wing Pha Ser Asn Gly Tyr Leu Wing Lau Cys Mys Cys Pha Gly 320 325 330 335 CCC AAG AAA GTG AAG CCA GCT GAG GAC GAC ACC GCA GCC GCC ATC ATG 1058 Pro Lys Lys Val Lys Pro Ala Glu Ala Glu Thr Ala Gly Ala He Met 340 345 350 GCC TTC CTG TGT CTG GGT CTG GCA CTG GGG GCT GTT TTC TCC TTC 1106 Wing Phe Phß Leu Cys Leu Gly Leu Wing Leu Gly Wing Val Phe Ser Phe 355 360 365 CTG TTC CGG GCA ATT GTG TGACAAAGGA TGGACAGAAG GACTGC 1150 Leu Phe Arg Wing He Val 370 CTGCCTCCCT CCCTGTCTGC CTCCTGCCCC TTCCTTCTGC CAGGGGTGAT CCTGAGTGGT 1210 CTGGCGGTTT TTTCTTCTAA CTGACTTCTG CTTTCCACGG CGTGTGCTGG GCCCGGATCT 1270 CCAGGCCCTG GGGAGGGAGC CTCTGGACGG ACAGTGGGGA CATTGTGGGT TTGGGGCTCA 1330 GAGTCGAGGG ACGGGGTGTA GCCTCGGCAT TTGCTTGAGT TTCTCCACTC TTGGCTCTGA 1390 CTGATCCCTG CTTGTGCAGG CCAGTGGAGG CTCTTGGGCT TGGAGAACAC GTGTGTCTCT 1450 GTGTATGTGT CTGTGTGTCT GCGTCCGTGT CTGTCAGACT GTCTGCCTGT CCTGGGGTGG 1510 CTAGGAGCTG GGTCTGACCG TTGTATGGTT TGACCTGATA TACTCCATTC TCCCCTGCGC 1570 CTCCTCCTCT GTGTTCTCTC CATGTCCCCC TCCCAACTCC CCATGCCCAG TTCTTACCCA 1630 TCATGCACCC TGTACAGTTG CCACGTTACT GCCTTTTTTA AAAATATATT TGACAGAAAC 1690 CAGGTGCCTT CAGAGGCTCT CTGATTTAAA T 1721 (2) INFORMATION FOR SEQ ID NO: 68: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1504 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10297 (ix) SEQUENCE CHARACTERISTICS: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 63 .. 614 (C) CHARACTERIZATION METHOD: E (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 68: CTTTTGCGGC TGCAGCGGGC TTGTAGGTGT CCGGCTTTGC TGGCCCAGCA AGCCTGATAA 60 GC ATG AAG CTC TTA TCT TTG GTG GCT GTG GTC GGG TGT TTG CTG GTG 107 Mat Lys Leu Leu Ser Leu Val Wing Val Val Gly Cys Leu Leu Val 1 5 10 15 CCC CCA GCT GAA GCC AAC AAG AGT TCT GAA GAT ATC CGG TGC AAA TGC 155 Pro Pro Wing Glu Wing Asn Lys Ser Sar Glu Asp He Arg Cys Lys Cys 20 25 30 ATC TGT CCA CCT TAT AGA AAC ATC AGT GG GCAC ATT TAC AAC CAG AAT 203 Ha Cys Pro Pro Tyr Arg Asn He Ser Gly His He Tyr Asn Gln Asn 35 40 45 GTA TCC CAG AAG GAC TGC AAC TGC CTG CAC GTG GTG GAG CCC ATG CCA 251 Val Ser Gln Lys Asp Cys Asn Cys Leu His Val Val Glu Pro Met Pro 50 55 60 GTG CCT GGC CAT GAC GTG GAG GCC TAC TGC CTG CTG TGC GAG TGC AGG 299 Val Pro Gly His Asp Val Glu Ala Tyr Cys Leu Leu Cys Glu Cys Arg 65 70 75 TAC GAG GAG CGC AGC ACC ACC ACC ATC AAG GTC ATC ATT GTC ATC TAC 347 Tyr Glu Glu Arg Ser Thr Thr He Lys Val He Ha Val Ha Tyr 80 85 90 95 CTG TCC GTG GTG GGT GCC CTG TTG CTC TAC ATG GCC TTC CTG ATG CTG 395 Leu Ser Val Val Gly Ala Leu Leu Lau Tyr Met Ala Phe Leu Met Leu 100 105 110 GTG GAC CCT CTG ATC CGA AAG CCG GAT GCA TAC ACT GAG CAA CTG CAC 443 Val Asp Pro Lau He Arg Lys Pro Asp Ala Tyr Thr Glu Gln Leu His 115 120 125 AAT GAG GAG GAG AAT GAG GAT GCT CGC TCT ATG GCA GCA GCT GCT GCT GCA 491 Asn Glu Glu Glu Asn Glu Asp Wing Arg Sar Met Wing Wing Wing Wing Wing 130 135 140 TCC CTC GGG GGA CCC CGA GCC AAC GTC CTG GAG CGG CGG GTG GGT 539 Ser Leu Gly Gly Pro Arg Ala Asn Thr Val Leu Glu Arg Val Glu Gly 145 150 155 GCC CAG CAG CGG TGG AAG CTG CAG GTG CAG GAG CAG CGG AAG ACA GTC 587 Wing Gln Gln Arg Trp Lys Leu Gln Val Gln Glu Gln Arg Lys Thr Val 160 165 170 175 TTC GAT CGG CAC AAG ATG CTC AGC TAGATGGGCT GGTGTGGTTG GGTCAAGGC 640 Phe Asp Arg His Lys Met Leu Ser 180 CCCAACACCA TGGCTGCCAG CTTCCAGGCT GGACAAAGCA GGGGGCTACT TCTCCCTTCC 700 CTCGGTTCCA GTCTTCCCTT TAAAAGCCTG TGGCATTTTT CCTCCTTCTC CCTAACTTTA 760 GAAATGTTGT ACTTGGCTAT TTTGATTAGG GAAGAGGGAT GTGGTCTCTG ATCTCTGTTG 820 TCTTCTTGGG TCTTTGGGGT TGAAGGGAGG GGGAAGGCAG GCCAGAAGGG AATGGAGACA 880 TTCGAGGCGG CCTCAGGAGT GGATGCGATC TGTCTCTCCT GGCTCCACTC TTGCCGCCTT 940 CCAGCTCTGA GTCTTGGGAA TGTTGTTACC CTTGGAAGAT AAAGCTGGGT CTTCAGGAAC 1000 TCAGTGTCTG GGAGGAAAGC ATGGCCCAGC ATTCAGCATG TGTTCCTTTC TGCAGTGGTT 1060 CTTATCACCA QCTCCCTCCC AGCCCCAGCG CCTCAGCCCC AGCCCCAGCT CCAGCCCTGA 1120 GGACAGCTCT GATGGGAGAG CTGGGCCCCC TGAGCCCACT GGGTCTTCAG GGTGCACTGG 1180 AAGCTGGTGT TCGCTGTCCC CTGTGCACTT CTCGCACTGG GGCATGGAGT GCCCATGCAT 1240 ACTCTGCTGC CGGTCCCCTC ACCTGCACTT GAGGGGTCTG GGCAGTCCCT CCTCTCCCCA 1300 GTGTCCACAG TCACTGAGCC AGACGGTCGG TTGGAACATG AGACTCGAGG CTGAGCGTGG 1360 ATCTGAACAC CACAGCCCCT GTACTTGGGT TGCCTCTTGT CCCTGAACTT CGTTGTACCA 1420 GTGCATGGAG AGAAAATTTT GTCCTCTTGT CTTAGAGTTG TGTGTAAATC AAGGAAGCCA 1480 TCATTAAATT GTTTTATTTC TCTC 1504 (2) INFORMATION FOR SEQ ID NO: 69: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 532 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Stomach cancer (D) CLONE NAME: HP10299 (ix) SEQUENCE CHARACTERISTICS: (A) CODE OF CHARACTERIZATION: CDS (B) POSITION OF EXISTENCE: 93 .. 443 (C) METHOD OF CHARACTERIZATION:? (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 69: GCTCTCTGGT AAAGGCGTGC AGGTGTTGGC CGCGGCCTCT GAGCTGGGAT GAGCCGTGCT 60 CCCGGTGGAA GCAAGGGAGC CCAGCCGGAG CC ATG GCC AGT ACÁ GTG GTA 113 GTA Mat Wing Thr Val Val Wing 1 5 GTT GGA CTG ACC ATT GCT GCT GCA GGA TTT GCA GGC CGT TAC GTT TTG 161 Val Gly Leu Thr Ha Wing Wing Wing Gly Ala Gly Wing Arg Tyr Val Lau 10 15 20 CAA GCC ATG AAG CAT ATG GAG CCT CAA GTA AAA CAA GTT TTT CAA AGC 209 Gln Wing Met Lys His Met Glu Pro Gln Val Lys Gln Val Pha Gln Ser 25 30 35 CTA CCA AAA TCT GCC TTC AGT GGT GGC TAT TAT AGA GGT GGG TTT GAA 257 Leu Pro Lys Ser Wing Phe Ser Gly Gly Tyr Tyr Arg Gly Gly Phe Glu 40 45 _ 50 55 CCC AAA ATG AA AAA CGG GAA GCA GCA TTA ATA CTA GGT GTA AGC CCT 305 Pro Lys Mat Thr Lys Arg Glu Wing Wing Leu He Leu Gly Val Ser Pro 60 65 70 ACT GCC AAT AAA GGG AAA ATA AGA GAT GCT CAT CGA CGA ATT ATG CTT 353 Thr Wing Asn Lys Gly Lys He Arg Asp Wing His Arg Arg He Mßt Leu 75 80 85 TTA AAT CAT CCT GAC AAA GGA GGA TCT CCT TAT ATA GCA GCC AAA ATC 401 Leu Asn His Pro Asp Lys Gly Gly Ser Pro Tyr He Ala Wing Lys He 90 95 100 AAT GAA GCT AAA GAT TTA CTA GAA GGT CAA GCT AAA AAA TGAAGTAAAT 450 Asn Glu Ala Lys Asp Leu Leu Glu Gly Gln Ala Lys Lys 105 110 115 GTATGATGAA TTTTAAGTTC GTATTAGTTT ATGTATATGA GTACTAAGTT TTTATAATAA 510 AATGCCTCAG AGCTACAATT TT 532 (2) INFORMATION FOR SEQ ID NO: 70: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 662 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for RNAra (i) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10301 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 92 .. 550 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 70: TCTAGCCCCG CCCCAGGCGA GGGCGCCGCA CCCACACCGC GCTGCGCAGT TTTGTTCTGC 60 TCCAGCTGTT CGAAGGTGAT CCAGACGCAA G ATG GCT CTC TCT AAG GAA 112 Mat Wing Val Leu Ser Lys Glu 1 5 TAT GGT TTT GTG CTT CTA ACT GGT GCT GCC AGC TTT ATA ATG GTG GCC 160 Tyr Gly Phe Val Leu Lau Thr Gly Ala Wing Phß Ser He Mßt Val Wing 10 15 20 CAC CTA GCC ATC AAT GTT TCC AAG GCC CGC AAG AAG TAC AAA GTG GAG 208 His Leu Wing Asn Val Ser Lys Wing Arg Lys Lys Tyr Lys Val Glu 25 30 35 TAT CCT ATC ATG TAC AGC ACG GAC CCT GAA AAT GGG CAC ATC TTC AAC 256 Tyr Pro Ha Met Tyr Ser Thr Asp Pro Glu Asn Gly His He Pha Asn 40 45 50 55 TGC ATT CAG CGA GCC CAC CAG AAC_ACG TTG GAA GTG TAT CCT CCC TTC 304 Cys He Gln Arg Ala His Gln Asn ~ Thr Leu Glu Val Tyr Pro Pro Phß 60 65 70 TTA TTT TTT CTA GCT GTT GGT GTT TAC CAC CCG CGT ATA GCT TCT 352 Leu Phe Phe Lau Wing Val Gly Gly Val Tyr His Pro Arg He Wing Ser 75 80 85 GGC CTG GGC TTG GCC TGG ATT GTT GGA CGA GTT CTT TAT GCT TAT GGC 400 Gly Leu Gly Leu Wing Trp He Val Gly Arg Val Leu Tyr Wing Tyr Gly 90, 95 100 TAT TAC ACG GGA GAA CCC AGC AAG CGT AGT CGA GGA GCC CTG GGG TCC 448 Tyr Tyr Thr Gly Glu Pro Ser Lys Arg Ser Arg Gly Ala Leu Gly Ser 105 110 115 ATC GCC CTC CTG GGC TTG GTG GGC ACÁ ACT GTG TGC TCT GCT TTC CAG 496 He Ala Leu Leu Gly Leu Val Gly Thr Thr Val Cys Sar Ala Phe Gln 120 125 130 135 CAT CTT GGT TGG GTT AAA AGT GGC TTG GGC AGT GGA CCC AAA TGC TGC 544 His Leu Gly Trp Val Lys Ser Gly Leu Gly Ser Gly Pro Lys Cys Cys 140 145 150 CAT TAAAGAATTA TAGGGGTTTA AAAACTCTCA TTCATTTTAA ATG 590 His ACTTACCTTT ATTTCCAGTT ACATTTTTTT TCTAAATATA ATAAAAACTT ACCTGGCATC 650 AGCCTCATAC CT 662 (2) INFORMATION FOR SEQ ID NO: 71: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 2372 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Liver (D) CLONE NAME: HP10302 (ix) SEQUENCE CHARACTERISTICS: (A) CODE OF CHARACTERIZATION: CDS (B) EXISTENCE POSITION: 134 .. 1813 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 71: GAAGACCCCA GCGCCGGCGC GGCTCAGGGC TGGGCCCACG GGACTCCGGA CGCGCCGCGA 60 AAGCGTTGCG CTCCCGGAGG CGTCCGCAGC TGCTGGCTGC TCATTTGCCG GTGACCGGAG 120 GCTCGGGGCC AGC ATG GCC CCC ACG CTG CAA CAG GCG TAC CGG AGG CGC 169 Met Wing Pro Thr Leu Gln Gln Wing Tyr Arg Arg Arg 1 5 10 TGG TGG ATG GCC TGC ACG GCT GTG CTG GAG AAC CTC TTC TTC TCT GCT 217 Trp Trp Mss Ala Cys Thr Ala Val Leu Glu Asn Leu Phß Phe Ser Wing 15 20 25 * GTA CTC CTG GGC TGG GGC TCC CTG TTG ATC ATT CTG AAG AAC GAG GGC 265 Val Leu Leu Gly Trp Gly Ser Leu Leu lie? L Leu Lys Asn Glu Gly 30 35 40 TTC TAT TCC AGC ACG TGC CCA GCT GAG AGC AGC ACC AAC ACC ACC CAG 313 Phe Tyr Ser Ser Thr Cys Pro Wing Glu Ser Ser Thr Asn Thr Thr Gln 45 50 55 60 GAT GAG CAG CGC AGG TGG CCA GGC TGT GAC CAG CAG GAC GAG ATG CTC 361 Asp Glu Gln Arg Arg Trp Pro Gly Cys Asp Gln Gln Asp Glu Met Leu 65 70 75 AAC CTG GGC TTC ACC ATT GGT TCC TTC GTG CTC AGC GCC ACC ACC CTG 409 Asn Leu Gly Phe Thr He Gly Ser Phe Val Leu Ser Wing Thr Thr Leu 80 85 90 CCA CTG GGG ATC CTC ATG GAC CGC TTT GGC CCC CGA CCC GTG CGG CTG 457 Pro Leu Gly He Lau Mat Asp Arg Phe Gly Pro Arg Pro Val Arg Leu 95 100 105 GTT GGC AGT GCC TGC TTC ACT GCG TCC TGC ACC CTC ATG GCC CTG GCC 505 Val Gly Ser Ala Cys Phe Thr Ala Ser Cys Thr Leu Met Ala Leu Wing 110 115 120 TCC CGG GAC GTG GAA GCT CTG TCT CCG TTG ATA TTC CTG GCG CTG TCC 553 Ser Arg Asp Val Glu Ala Leu Ser Pro Leu He Pha Leu Ala Leu Ser 125 130 135 140 CTG AAT GGC TTT GGT GGC ATC TGC CTA ACG TTC ACT TCA CTC ACG CTG 601 Leu Asn Gly Phe Gly He Cys Leu Thr Phe Thr Ser Leu Thr Leu 145 150 155 CCC AAC ATG TTT GGG AAC CTG CGC TCC ACG TTA ATG GCC CT C ATG ATT 649 Pro Asn Met Phe Gly Asn Leu Arg Ser Thr Leu Mßt Ala Leu Met He 160 165 170 GGC TCT TAC GCC TCT TCT GCC ATT ACG TTC CCA GGA ATC AAG CTG ATC 697 Gly Ser Tyr Ala Ser Ser Ala Lie Thr Phe Pro Gly Ha Lys Leu He 175 180 185 TAC GAT GCC GGT GTG GCC TTC GTG GTC ATC ATG TTC ACC TGG TCT GGC 745 Tyr Asp Wing Gly Val Wing Phe Val Val He Mat Phe Thr Trp Ser Gly 190 195 200 CTG GCC TGC CTT ATC TTT CTG AAC TGC ACC CTC AAC TGG CCC ATC GAA 793 Leu Wing Cys Leu Ha Phß Leu Asn Cys Thr Leu Asn Trp Pro He Glu 205 210 215 220 GCC TTT CCT GCC CCT GAG GAA GTC AAT TAC ACG AAG AAG ATC AAG CTG 841 Wing Phe Pro Pro Glu Glu Val Asn Tyr Thr Lys Lys He Lys Leu 225 230 235 AGT GGG CTG GCC CTG GAC CAC AAG GTG ACA GGT GAC CTC TTC TAC ACC 889 Sar Gly Lau Ala Leu Asp His Lys Val Thr Gly Asp Leu Phe Tyr Thr 240 245 250 CAT GTG ACC ACC ATG GGC CAG AGG CTC AGC CAG AAG GCC CCC AGC CTG 937 His Val Thr Thr Met Gly Gln Arg Leu Ser Gln Lys Ala Pro Ser Leu 255 260 265 GAG GAC GGT TCG GAT GTC TTC ATG TCA CCC CAG GAT GTT CGG GGC ACC 985 Glu Asp Gly Ser Asp Wing Phe Mßt Ser Pro Gln Asp Val Arg Gly Thr 270 275 280 TCA GAA AAC CTT CCT GAG AGG TCT GTC CCC TTA CGC AAG AGC CTC TGC 1033 Ser Glu Asn Leu Pro Glu Arg Ser Val Pro Leu Arg Lys Ser Leu Cys 285 290 295 300 TCC CCC ACT TTC CTG TGG AGC CTC CTC ACC ATG GGC ATG ACC CAG CTG 1081 Ser Pro Thr Phe Leu Trp Ser Leu Leu Thr Met Gly Met Thr Gln Leu 305 310 315 CGG ATC ATC TTC TAC ATG GCT GCT GTG AAC AAG ATG CTG GAG TAC CTT 1129 Arg Ha Ha Pha Tyr Met Wing Wing Val Asn Lys Met Leu Glu Tyr Leu 320 325 330 GTG ACT GGT GGC CAG GAG CAT GAG ACÁ AAT GAA CAG CAA CAA AAG GTG 1177 Val Thr Gly Gly Gln Glu His Glu Thr Asn Glu Gln Gln Gln Lys Val 335 340 345 GCA GAG HERE GTT GGG TTC TAC TCC TCC GTC TTC GGG GCC ATG CAG CTG 1225 Wing Glu Thr Val Gly Phe Tyr Ser Val Pha Gly Ala Met Gln Leu 350 355 360 TTG TGC CTT CTC ACC TGC CCC CTC ATT GGC TAC ATC ATG GAC TGG CGG 1273 Leu Cys Leu Leu Thr Cys Pro Leu He Gly Tyr He Met Asp Trp Arg 365 370 375 380 ATC AAG GAC TGC GTG GAC GCC CCA ACT GAG GGC ACT GTC CTC GGA GAT 1321 He Lys Asp Cys Val Asp Ala Pro Thr Gln Gly Thr Val Leu Gly Asp 385 390 395 GCC AGG GAC GGG GTT GCT ACC AAA TCC ATC AGA CCA CGC TAC TGC AAG 1369 Ala Arg Asp Gly Val Ala Thr Lys Ser he Arg Pro Arg Tyr Cys Lys 400 405 410 ATC CAA AAG CTC ACC AAT GCC ATC AGT GCC TTC ACC CTG ACC AAC CTG 1417 Ha Gln Lys Leu Thr Asn Ala has Ser Ala Phe Thr Lau Thr Asn Leu 415 420 425 CTG CTT GTG GGT TTT GGC ATC ACC TGT CTC ATC AAC AAC TTA CAC CTC 1465 Leu Leu Val Gly PHSS Gly He Thr Cys Leu I Asn Asn Leu His Leu 430,435,440 CAG TTT GTG ACC TTT GTC CTG CAC ACC ATT GTT CGA GGT TTC TTC CAC 1513 Phe Val Gln Thr Val Leu His Thr PHSS Val Arg Gly Phe He Phe His TCA 445 450 455 460 GCC CTC TGT GGG AGT TAT GTG GCT GCA CCA TTC TCC CAC AAC TTT 1561 Ala Cys Ser Ser Gly Leu Tyr Ala Ala Val Phe Pro Sar Asn His Phe 465 470 475 GGG ACG CTG ACÁ GGC CTG CAG TCC CTC ATC AGT GCT GTG TTC GCC TTG 1609 Gly Thr Leu Thr Gly Leu Gln Ser Leu Ha Ser Ala Val Phe Ala Leu 480,485,490 CTT CAG CAG CCA CTT TTC ATG GCG ATG GTG GGA CCC CTG AAA GGA GAG 1657 Leu Gln Gln Pro Leu Phe Met Ala MSST Val Gly Pro Leu Lys Gly Glu 495 500 505 CCC TTC TGG GTG AAT CTG GGC CTC CTG CTA TTC TCA CTC CTG GGA TTC 1705 Pro PHSS Trp Val Asn Lau Gly Leu Leu Leu PHSS Ser Leu Lau Gly Phe 510 515 520 CTG TTG CCT TCC TAC CTC TTC TAT TAC CGT GCC CGG CTC CAG CAG GAG 1753 Lau Leu Pro Sar Tyr Leu PHSS Tyr Tyr Arg Ala Arg Leu Gln Gln Glu 525 530 535 540 TAC GCC GCC AAT GGG ATG GGC CCA CTG AAG GTG CTT AGC GGC TCT GAG 1801 Tyr Ala Ala Asn Gly Met Gly Pro Leu Lys Val Leu Ser Gly Ser Glu 545 550 555 GTG ACC GCA TAGACTTCTC AGACCAAGGG ACCTGGATGA 1840 Val Thr Wing CAGGCAATCA AGGCCTGAGC AACCAAAAGG AGTGCCCCAT ATGGCTTTTC TACCTGTAAC 1900 ATGCACATAG AGCCATGGCC GTAGATTTAT AAATACCAAG AGAAGTTCTA TTTTTGTAAA 1960 GACTGCAAAA AGGAGGAAAA AAAAACCTTC AAAAACGCCC CCTAAGTCAA CGCTCCATTG 2020 ACTGAAGACA GTCCCTATCC TAGAGGGGTT GAGCCTTCTT CCTCCTTGGG TTGGAGGAGA 2080 CCAGGGTGCC TCTTATCTCC TTCTAGCGGT CTGCCTCCTG GTACCTCTTG GGGGGATCGG 2140 CAAACAGGCT ACCCCTGAGG TCCCATGTGC CATGAGTGTG CACACATGCA TGTGTCTGTG 2200 TATGTGTGAA TGTGAGAGAG ACACAGCCCT CCTTTCAGAA GGAAAGGGGC CTGAGGTGCC 2260 AGCTGTGTCC TGGGTTAGGG GTTGGGGGTC GGCCCCTTCC AGGGCCAGGA GGGCAGGTTC 2320 CCTCTCTGGT GCTGCTGCTT GCAAGTCTTA GAGGAAATAA AAAGGGAAGT GAG 2373 (2) INFORMATION FOR SEQ ID NO: 72: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 1316 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10304 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CODE OF CHARACTERIZATION: CDS (B) POSITION OF EXISTENCE: 11 .. 1003 (C) METHOD OF CHARACTERIZATION: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 72: GTTGTCCAAG ATG GAG GGC GCT CCA CCG GGG TCG CTC GCC CTC CGG CTC 49 Met Glu Gly Ala Pro Pro Gly Ser Leu Ala Leu Arg Leu 1 5 10 CTG CTG TTC GTG GCG CTA CCC GCC TCC GGC TGG CTG ACG ACG GGC GCC 97 Leu Leu Phß Val Ala Lau Pro Ala Sar Gly Trp Leu Thr Thr Gly Wing 15 20 25 CCC GAG CCG CCG CCG CTG TCC GGA GCC CCA CAG GAC GGC ATC AGA ATT 145 Pro Glu Pro Pro Pro Leu Ser Gly Pro Wing Gln Asp Gly Ha Arg Ha 30 35 40 45 AAT GTA ACT AA CTG AAA GAT GAT GG GAC ATA TCT AAA CAG CAG GTT 193 Asn Val Thr Thu Leu Lys Asp Asp Gly Asp He Ser Lys Gln Gln Val 50 55 60 GTT CTT AAC ATA ACC TAT GAG AGT GGA CAG GTG TAT GTA AAT GAC TTA 241 Val Leu Asn He Thr Tyr Glu Ser Gly Gln Val Tyr Val Asn Asp Leu 65 70 75 CCT GTA AAT AGT GGT GTA ACC CGA ATA AGC TGT CAG ACT TTG ATA GTG 289 Pro Val Asn Ser Gly Val Thr Arg He Ser Cys Gln Thr Lau He Val 80 85 90 AAG AAT GAA AAT CTT GAA AAT TTG GAG GAA AAA GAA TAT TTT GGA ATT 337 Lys Asn Glu Asn Leu Glu Asn Leu Glu Glu Lys Glu Tyr Phe Gly He 95 100 105 GTC AGT GTA AGG ATT TTA GTT CAT GAG TGG CCT ATG ACT TCT GGT TCC 385 Val Ser Val Arg He Leu Val His Glu Trp Pro Mat Thr Ser Gly Ser 110 115 120 125 AGT TTG CAA CTA ATT GTC ATT CAA GAA GAG GTA GTA GTA ATT GAT GGA 433 Ser Leu Gln Leu He Val He Gln Glu Val Val Glu He Asp Gly 130 135 140 AAA CAA GTT CAG CAA AAG GAT GTC ACT GAA ATT GAT ATT TTA GTT AAG 481 Lys Gln Val Gln Gln Lys Asp Val Thr Glu He Asp He Leu Val Lys 145 150 155 AAC CGG GGA GTA CTC AGA CAT TCA AAC TAT ACC CTC CCT TTG GAA 529 Asn Arg Gly Val Leu Arg His Ser Asn Tyr Thu Leu Pro Lau Glu Glu 160 165 170 'AGC ATG CTC TAC TCT ATT TCT CGA GAC AGT GAC ATT TTA TTT ACC CTT 577 Ser Met Lau Tyr Ser Ha Be Arg Asp Ser Asp He Leu Phe Thr Leu 175 180 185 CCT AAC CTC TCC AAA AAA GAA AGT GTT AGT TCA CTG CAA ACC ACT AGC 625 Pro Asn Leu Ser Lys Lys Glu Ser Val Ser Ser Lau Gln Thr Thr Ser 190 195 200 205 CAG TAT CTT ATC AGG AAT GTG GAA ACC ACT GTA GAAT GAT GTT TTA 673 Gln Tyr Leu Ha Arg Asn Val Glu Thr Thr Val Asp Glu Asp Val Leu 210 215 220 CCT GGC AAG TTA CCT GAA ACT CCT CTC AGA GCA GAG CCG CCA TCT TCA 721 Pro Gly Lys Leu Pro Glu Thr Pro Leu Arg Wing Glu Pro Pro Ser Ser 225 230 235 TAT AAG GTA ATG TGT CAG TGG ATG GAA AAG TTT AGA AAA GAT CTG TGT 769 Tyr Lys Val Met Cys Gln Trp Mßt Glu Lys Phe Arg Lys Asp Leu Cys 240 245 250 AGG TTC TGG AGC AAC GTT TTC CCA GTA TTC TTT CAG TTT TTG AAC ATC 817 Arg Pha Trp Ser Asn Val Pha Pro Val Pha Phe Gln Pha Leu Asn He 255 260 265 ATG GTG GTT GGA ATT ACÁ GGA GCT GCT GTG GTA ATTA ACC ATC TTA AAG 865 Met Val Val Gly He Thr Gly Ala Ala Val Val He Thr He Leu Lys 270 275 280 285 GTG TTT TTC CTC GTT TCT GAA TAC AAA GGA ATT CTT CAG TTG GAT AAA 913 Val Pha Pha Pro Val Ser Glu Tyr Lys Gly He Leu Gln Lau Asp Lys 290 295 300 GTG GAC GTC ATA CCT GTG ACÁ GCT ATC AAC TTA TAT CCA GAT GGT CCA 961 Val Asp Val He Pro Val Thr Wing Ha Asn Leu Tyr Pro Asp Gly Pro 305 310 315 GAG AAA AGA GCT GAA AAC CTT GAA GAT AAA ACA TGT ATT TAAAACGCCA 1010 Glu Lys Arg Ala Glu Asn Leu Glu Asp Lys Thr Cys He 320 325 330 TCTCATATCA TGGACTCCGA AGTAGCCTGT TGCCTCCAAA TTTGCCACTT GAATATAATT 1070 TTCTTTAAAT CGTTAAGAAT CAGTTTATAC ACTAGAGAAA TTGCTAAACT CTAAGACTGC 1130 CTGAAAATTG ACCTTTACAG TGCCAAGTTA AAGTTTACCT TATTCTCGGC CGGGTGCAGT 1190 GGCTCATGCC TGTAATCCCA GGACTTTGGG AGGCCAATGC GGGCGGATCA CGAGGTCAGA 1250 TCAAGACCAT CCTGCCAACA TGGTGAAACC CTGTCTCTAC TAAAAAAAAT AAAAAAGTTA 1310 GCTGGG 1316 (2) INFORMATION FOR SEQ ID NO: 73: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 893 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: cDNA for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10305 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) POSITION OF EXISTENCE: 110 .. 436 (C) METHOD OF CHARACTERIZATION: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 73: ATCGCGGAGT CGGTGCTTTA GTACGCCGCT GGCACCTTTA CTCTCGCCGG CCGCGCGAAC 60 CCGTTTGAGC TCGGTATCCT AGTGCACACG CCTTGCAAGC GACGGCGCC ATG AGT CTG 118 Met Ser Leu 1 ACT TCC AGT TCC AGC GTA CGA GTT GAA TGG ATC GCA GCA GTT ACC ATT 166 Thr Ser Ser Ser Ser Val Arg Val Glu Trp He Ala Ala Val Thr He 5 10 15 GCT GCT GGG ACÁ GCT GCA ATT GGT TAT CTA GCT TAC AAA AGA TTT TAT 214 Wing Wing Gly Thr Wing Wing He Gly Tyr Leu Wing Tyr Lys Arg Phe Tyr 20 25 30 35 GTT AAA GAT CAT CGA AAT AAA GCT ATG ATA AAG CTT CAC ATC CAG AAA 262 Val Lys Asp His Arg Asn Lys Ala Met He Asn Leu His He Gln Lys 40 45 50 GAC AAC CCC AAG ATA GTA CAT GCT TTT GAC ATG GAG GAT TTG GGA GAT 310 Asp Asn Pro Lys He Val His Wing Phe Asp Mat Glu Asp Leu Gly Asp 55 60 65 AAA GCT GTG TAC TGC TGT TGT TGG AGG TCC AAA AAG TTC CCA TTC TGT 358 Lys Wing Val Tyr Cys Arg Cys Trp Arg Sar Lys Lys Pha Pro Phe Cys 70 75 80 GAT GGG GCT CAC AAA CAT AAC GAA GAG ACT GGA GAC AAT GTG GGC 406 Asp Gly Ala His Thr Lys His Asn Glu Glu Thr Gly Asp Asn Val Gly 85 90 95 CCT CTG ATC ATC AAG AAA AAA GAA ACT TAAATGGACA CTTTTGA 450 Pro Leu Ha He Lys Lys Lys-Glu Thr 100, 105 TGCTGCAAAT CAGCTTGTCG TGAAGTTACC TGATTGTTTA ATTAGAATGA CTACCACCTC 510 TGTCTGATTC ACCTTCGCTG GATTCTAAAT GTGGTATATT GCAAACTGCA GCTTTCACAT 570 TTATGGCATT TGTCTTGTTG AAACATCGTG GTGCACATTT GTTTAAACAA AAAAAAAAAA 630 AAAAAGGAAA AACCAACCTC ATGGCCTGTG GGTTATTTTG GTCTTGTAAG GATCCATTTC 690 TTTAAAATAC TGACATATAG AGTTGTACCT TATATAGAAT ATAGTTGTAT CTTGAAGTCA 750 ACATATTAAA TTATTCTCAA AATTATGTAT TTGCAGATTG TACTTGTAAG TTTCAAAGAA 810 AAATTACCAT CTTTTCATAT TGACCTGGAA ACTAAATAGG ATGTGATTCA GCTACATTAA 870 TTTCTTAATA CAATCTAGGA AAG 893 (2) INFORMATION FOR SEQ ID NO: 74: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 690 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: ADNa for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Osteosarcoma (C) CELLULAR LINE: U-2 OS (D) CLONE NAME: HP10306 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CHARACTERIZATION CODE: CDS (B) EXISTENCE POSITION: 230 .. 535 (C) CHARACTERIZATION METHOD: E (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 74: TAACAGCGCA TGCGTGCAGT GTTGCCTCGC CCAAAGAAGA CTACAATCTC CAGGGAAACC 60 TGGGGCGTCT CGCGCAAACG TCCATAACTG AAAGTAGCTA AGGCACCCCA GCCGGAGGAA 120 GTGAGCTCTC CTGGGGCGTG GTTGTTCGTG ATCCTTGCAT CTGTTACTTA GGGTCAAGGC 180 TTGGGTCTTG CCCCGCAGAC CCTTGGGACG ACCCGGCCCC AGCGCAGCT ATG AAC CTG 238 Met Asn Leu 1 GAG CGA GTG TCC AAT GAG GAG AAA TTG AAC CTG TGC CGG AAG TAC TAC 286 Glu Arg Val Ser Asn Glu Glu Lys Leu Asn Leu Cys Arg Lys Tyr Tyr 10 15 CTG GGG GGC TTT GCT TTC CTG CCT TTT CTC TGG TTG GTC AAC ATC TTC 334 Leu Gly Gly Phe Wing Phe Leu Pro Phe Leu Trp Leu Val Asn Ha Phe 20 25 30 35 TGG TTC TTC CGA GAG GCC TTC CTT GTC CCA GCC TAC HERE GAA CAG AGC 382 Trp Phe Phe Arg Glu Wing Phe Leu Val Pro Wing Tyr Thr Glu Gln Ser 40 45 50 CAA ATC AAA GGC TAT GTC TGG CGC TCA GCT GTG GGC TTC CTC TTC TGG 430 Gln Ha Lys Gly Tyr Val Trp Arg Ser Wing Val Gly Pha Lau Phß Trp 55 60 65 GTG ATA GTG CTC ACC TCC TGG ATC ACC ATC TTC CAG ATC TAC CGG CCC 478 Val He Val Leu Thr Ser Trp He Thr He Phe Gln He Tyr Arg Pro 70 75 80 CGC TGG GGT GCC CTT GGG GAC TAC CTC TCC TTC ACC ATA CCC CTG GGC 526 Arg Trp Gly Wing Leu Gly Asp Tyr Lau Ser Phe Thr He Pro Leu Gly 85 90 95 ACC CCC TGACAACTTC TGCACATACT GGGGCCCTGC TTATTCTCCC AGGACAGG 580 Thr Pro 100 CTCCTTAAAG CAGAGGAGCC TGTCCTGGGA GCCCCTTCTC AAACTCCTAA GACTTGTTTT 640 CATGTCCCAC GTTCTCTGCT GACATCCCCC AATAAAGGAC CCTAACTTTC 690 (2) INFORMATION FOR SEQ ID NO: 75: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 2186 (B) TYPE: Nucleic Acid (C) BRANCH: Double (D) TOPOLOGY: Linear (ii) TYPE OF SEQUENCE: ADNa for mRNA (vi) ORIGINAL SOURCE: (A) ORGANISM SPECIES: Homo sapiens (B) TYPE OF CELL: Squamous cell carcinoma (C) CELL LINE: KB (D) CLONE NAME: HP10328 (ix) CHARACTERISTICS OF THE SEQUENCE: (A) CODE OF CHARACTERIZATION: CDS (B) POSITION OF EXISTENCE: 118 .. 1236 (C) METHOD OF CHARACTERIZATION: E. { xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 75: ACTCTTTCTT CGGCTCGCGA GCTGAGAGGA GCAGGTAGAG GGGCAGAGGC GGGACTGTCG 60 TCTGGGGGAG CCGCCCAGGA GGCTCCTCAG GCCGACCCCA GACCCTGGCT GGCCAGG 117 ATG AAG TAT CTC CGG CAC CGG CCC AAT GCC ACC CTC ATT CTG GCC 165 Met Lys Tyr Leu Arg His Arg Arg Pro Asn Wing Thr Leu He Leu Wing 1 5 10 15 ATC GGC GCT TTC ACC CTC CTC CTC TTC AGT CTG CTA GTG TCA CCA CCC 213 lie Gly Ala Pha Thr Leu Leu Lau Pha Ser Lau Lau Val Ser Pro Pro 20 25 30 ACC TGC AAG GTC CAG GAG CAG CCA CCG GCG ATC CCC GAG GCC CTG GCC 261 Thr Cys Lys Val Gln Glu Gln Pro Pro Ala Has Pro Glu Ala Leu Wing 35 40 45 TGG CCC ACT CCA CCC ACC CGC CCA GCC CCG GCC CCG TGC CAT GCC AAC 309 Trp Pro Thr Pro Pro Thr Arg Pro Wing Pro Pro Wing Cys His Wing Asn 50 55 60 ACC TCT ATG GTC ACC CAC CCG GAC TTC GCC ACG CAG CCG CAG CAC GTT 357 Thr Ser Mßt Val Thr His Pro Asp Phe Ala Thr Gln Pro Gln His Val 65 70 75 80 CAG AAC TTC CTC CTG TAC AGA CAC TGC CGC CAC TTT CCC CTG CTG CAG 405 Gln Asn Phe Leu Leu Tyr Arg His Cys Arg His Pha Pro Leu Leu Gln 85 90 95 GAC GTG CCC CCC TCT AAG TGC GCG CAG CCG GTC TTC CTG CTG CTG GTG 453 Asp Val Pro Pro Ser Lys Cys Ala Gln Pro Val Phe Leu Leu Leu Val 100 105 110 ATC AAG TCC TCC CCT AGC AAC TAT GTG CGC GG CTG CTG CGG CGC 501 Ha Lys Ser Ser Pro Ser Asn Tyr Val Arg Arg Glu Leu Arg Arg 115 120 125 ACG TGG GGC CGC GAG CGC AAG GTA CGG GGT TTG CAG CTG CGC CTC CTC 549 Thr Trp Gly Arg Glu Arg Lys Val Arg Gly Lau Gln Leu Arg Leu Leu 130 135 140 TTC CTG GTG GGC ACA GCC TCC AAC CCG CAC GAG GCC CGC AAG GTC AAC 597 Phe Leu Val Gly Thr Ala Ser Asn Pro His Glu Ala Arg Lys Val Asn 145 150 155 160 CGG CTG CTG GAG CTG GAG GCA CAG ACT CAC GGA GAC ATC CTG CAG TGG 645 Arg Leu Leu Glu Leu Glu Wing Gln Thr His Gly Asp He Leu Gln Trp 165 170 175 GAC TTC CAC GAC TCC TTC TTC AAC CTC ACG CTC AA G CAG GTC CTG TTC 693 Asp Pha His Asp Sar Phe Pha Asn Leu Thr Leu Lys Gln Val Leu Phß 180 185 190 TTA CAG TGG CAG GAG HERE AGG TGC GCC AAC GCC AGC TTC GTG CTC AAC 741 Leu Gln Trp Gln Glu Thr Arg Cys Wing Asn Wing Ser Phe Val Leu Asn 195 200 205 GGG GAT GAT GTC GTC TTT GCA CAC ACA GAC AAC ATG GTC TTC TAC CTG 789 Gly Asp Asp Asp Val Phe Wing His Thr Asp Asn Met Val Ph? Tyr Leu 210 215 220 GAG GAC CAT GAC CCT GGC CGC CAC CTC TTC GTG GGG CAA CTG ATC CAA 837 Gln Asp His Asp Pro Gly Arg His Leu Phe Val Gly Gln Leu He Gln 225 230 235 240 AAC GTG GGC CCC ATC CGG GCT TTT TGG AGC AAG TAC TAT GTG CCA GAG 885 Asn Val Gly Pro He Arg Ala Pha Trp Ser Lys Tyr Tyr Val Pro Glu 245 250 255 GTG GTG ACT CAG AAT GAG CGG TAC CCA CCC TAT TGT GGG GGT GGT GGC 933 Val Val Thr Gln Asn Glu Arg Tyr Pro Pro Tyr Cys Gly Gly Gly Gly 260 265 270 TTC TTG CTG TCC CGC TTC ACG GCC GCT GCC CTG CGC CGT GCT GCC CAT 981 Pha Leu Lau Ser Arg Phe Thr Wing Wing Wing Leu Arg Arg Wing Wing His 275 280 285 GTC TTG GAC ATC TT C CCC ATT GAT GAT GTC TTC CTG GGT ATG TGT CTG 1029 Val Leu Asp He Pha Pro He Asp Asp Val Pha Lau Gly Mßt Cys Leu 290 295 300 GAG CTT GAG GG CTG AAG CCT GCC TCC CAC AGC GGC ATC CGC ACG TCT 1077 Glu Leu Glu Gly Leu Lys Pro Wing Ser Gly He Arg Thr Ser 305 310 315 320 GGC GTG CGG GCT CCA TCG CAA CAC CTG TCC TCC TTT GAC CCC TGC TTC 1125 Gly Val Arg Ala Pro Ser Gln His Leu Ser Ser Phe Asp Pro Cys Phe 325 330 335 TAC CGA GAC CTG CTG GTG CAC CGC TTC CTA CCT TAT GAG ATG CTG 1173 Tyr Arg Asp Leu Leu Leu Val His Arg Pha Leu Pro Tyr Glu Mat Leu 340 345 350 CTC ATG TGG GAT GCG CTG AAC CAG CCC AAC CTC ACC TGC GGC AAT CAG 1221 Leu Met Trp Asp Ala Leu Asn Gln Pro Asn Leu Thr Cys Gly Asn Gln 355 360 365 ACÁ CAG ATC TAC TGAGTCAGCA TCAGGGTCCC CAGCCTCTGG GCTCCTG 1270 Thr Gln He Tyr 370 TTTCCATAGG AAGGGGCGAC ACCTTCCTCC CAGGAAGCTG AGACCTTTGT GGTCTGAGCA 1330 TAAGGGAGTG CCAGGGAAGG TTTGAGGTTT GATGAGTGAA TATTCTGGCT GGCGAACTCC 1390 TACACATCCT TCAAAACCCA CCTGGTACTG TTCCAGCATC TTCCCTGGAT GGCTGGAGGA 1450 ACTCCAGAAA ATATCCATCT TCTTTTTTGTG GCTGCTAATG GCAGAAGTGC CTGTGCTAGA 1510 GTTCCAACTG TGGATGCATC CGTCCCGTTT GAGTCAAAGT CTTACTTCCC TGCTCTCACC 1570 TACTCACAGA CGGGATGCTA AGCAGTGCAC CTGCAGTGGT TTAATGGCAG ATAAGCTCCG 1630 TCTGCAGTTC CAGGCCAGCC AGAAACTCCT GTGTCCACAT AGAGCTGACG TGAGAAATAT 1690 CTTTCAGCCC AGGAGAGAGG GGTCCTGATC TTAACCCTTT CCTGGGTCTC AGACAACTCA 1750 GAAGGTTGGG GGGATACCAG AGAGGTGGTG GAATAGGACC GCCCCCTCCT TACTTGTGGG 1810 ATCAAATGCT'GTAATGGTGG AGGTGTGGGC AGAGGAGGGA GGCAAGTGTC CTTTGAAAGT 1870 TGTGAGAGCT CAGAGTTTCT GGGGTCCTCA TTAGGAGCCC CCATCCCTGT GTTCCCCAAG 1930 AATTCAGAGA ACAGCACTGG GGCTGGAATG ATCTTTAATG GGCCCAAGGC CAACAGGCAT 1990 ATGCCTCACT ACTGCCTGGA GAAGGGAGAG ATTCAGGTCC TCCAGCAGCC TCCCTCACCC 2050 AGTATGTTTT ACAGATTACG GGGGGACCGG GTGAGCCAGT GACCCCCTGC AGCCCCCAGC 2110 TTCAGGCCTC AGTGTCTGCC AGTCAAGCTT CACAGGCATT GTGATGGGGC AGCCTTGGGG 2170 AATATAAAAT TTTGTG 2186

Claims

Novelty of the Invention 1. A protein containing any of the amino acid sequences represented by Sequence No. 1 to Sequence No. 2, or Sequence No. 4 to Sequence No. 25.
A DNA encoding any of the proteins described in claim 1.
3. A cDNA containing any of the base sequences represented by Sequence No, 26 to Sequence No. 50.
4. A cDNA as described in claim 3, which comprises any of the base sequences represented by Sequence No. 51 to Sequence No. 75.
5. A transformed eukaryotic cell, capable of expressing any DNAs as described in claims 2 to 4, and which produces a protein as described in claim 1.